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14001 Steady-state kinetic analysis of the quinoprotein methylamine dehydrogenase from Paracoccus denitrificans
14001 Steady-state kinetic analysis of the quinoprotein methylamine dehydrogenase from Paracoccus denitrificans
14002 Steady-state kinetic analysis of the quinoprotein methylamine dehydrogenase from Paracoccus denitrificans
14002 Steady-state kinetic analysis of the quinoprotein methylamine dehydrogenase from Paracoccus denitrificans
14003 Steady-state kinetic analysis of the quinoprotein methylamine dehydrogenase from Paracoccus denitrificans
14003 Steady-state kinetic analysis of the quinoprotein methylamine dehydrogenase from Paracoccus denitrificans
14004 Steady-state kinetic analysis of the quinoprotein methylamine dehydrogenase from Paracoccus denitrificans
14004 Steady-state kinetic analysis of the quinoprotein methylamine dehydrogenase from Paracoccus denitrificans
14005 Steady-state kinetic analysis of the quinoprotein methylamine dehydrogenase from Paracoccus denitrificans
14005 Steady-state kinetic analysis of the quinoprotein methylamine dehydrogenase from Paracoccus denitrificans
14006 Steady-state kinetic analysis of the quinoprotein methylamine dehydrogenase from Paracoccus denitrificans
14006 Steady-state kinetic analysis of the quinoprotein methylamine dehydrogenase from Paracoccus denitrificans
14007 Steady-state kinetic analysis of the quinoprotein methylamine dehydrogenase from Paracoccus denitrificans
14007 Steady-state kinetic analysis of the quinoprotein methylamine dehydrogenase from Paracoccus denitrificans
14008 Steady-state kinetic analysis of the quinoprotein methylamine dehydrogenase from Paracoccus denitrificans
14008 Steady-state kinetic analysis of the quinoprotein methylamine dehydrogenase from Paracoccus denitrificans
14009 Steady-state kinetic analysis of the quinoprotein methylamine dehydrogenase from Paracoccus denitrificans
14009 Steady-state kinetic analysis of the quinoprotein methylamine dehydrogenase from Paracoccus denitrificans
14010 Steady-state kinetic analysis of the quinoprotein methylamine dehydrogenase from Paracoccus denitrificans
14010 Steady-state kinetic analysis of the quinoprotein methylamine dehydrogenase from Paracoccus denitrificans
14011 Steady-state kinetic analysis of the quinoprotein methylamine dehydrogenase from Paracoccus denitrificans
14011 Steady-state kinetic analysis of the quinoprotein methylamine dehydrogenase from Paracoccus denitrificans
14012 Steady-state kinetic analysis of the quinoprotein methylamine dehydrogenase from Paracoccus denitrificans
14012 Steady-state kinetic analysis of the quinoprotein methylamine dehydrogenase from Paracoccus denitrificans
14013 Overall Kinetic Mechanism of Saccharopine Dehydrogenase from Saccharomyces cerevisiae
14013 Overall Kinetic Mechanism of Saccharopine Dehydrogenase from Saccharomyces cerevisiae
14014 Overall Kinetic Mechanism of Saccharopine Dehydrogenase from Saccharomyces cerevisiae
14014 Overall Kinetic Mechanism of Saccharopine Dehydrogenase from Saccharomyces cerevisiae
14015 Overall Kinetic Mechanism of Saccharopine Dehydrogenase from Saccharomyces cerevisiae
14015 Overall Kinetic Mechanism of Saccharopine Dehydrogenase from Saccharomyces cerevisiae
14016 Overall Kinetic Mechanism of Saccharopine Dehydrogenase from Saccharomyces cerevisiae
14016 Overall Kinetic Mechanism of Saccharopine Dehydrogenase from Saccharomyces cerevisiae
14017 Overall Kinetic Mechanism of Saccharopine Dehydrogenase from Saccharomyces cerevisiae
14017 Overall Kinetic Mechanism of Saccharopine Dehydrogenase from Saccharomyces cerevisiae
14018 Overall Kinetic Mechanism of Saccharopine Dehydrogenase from Saccharomyces cerevisiae
14018 Overall Kinetic Mechanism of Saccharopine Dehydrogenase from Saccharomyces cerevisiae
14019 Overall Kinetic Mechanism of Saccharopine Dehydrogenase from Saccharomyces cerevisiae
14019 Overall Kinetic Mechanism of Saccharopine Dehydrogenase from Saccharomyces cerevisiae
14020 Overall Kinetic Mechanism of Saccharopine Dehydrogenase from Saccharomyces cerevisiae
14020 Overall Kinetic Mechanism of Saccharopine Dehydrogenase from Saccharomyces cerevisiae
14021 Overall Kinetic Mechanism of Saccharopine Dehydrogenase from Saccharomyces cerevisiae
14021 Overall Kinetic Mechanism of Saccharopine Dehydrogenase from Saccharomyces cerevisiae
14022 Overall Kinetic Mechanism of Saccharopine Dehydrogenase from Saccharomyces cerevisiae
14022 Overall Kinetic Mechanism of Saccharopine Dehydrogenase from Saccharomyces cerevisiae
14023 Overall Kinetic Mechanism of Saccharopine Dehydrogenase from Saccharomyces cerevisiae
14023 Overall Kinetic Mechanism of Saccharopine Dehydrogenase from Saccharomyces cerevisiae
14024 Overall Kinetic Mechanism of Saccharopine Dehydrogenase from Saccharomyces cerevisiae
14024 Overall Kinetic Mechanism of Saccharopine Dehydrogenase from Saccharomyces cerevisiae
14025 Overall Kinetic Mechanism of Saccharopine Dehydrogenase from Saccharomyces cerevisiae
14025 Overall Kinetic Mechanism of Saccharopine Dehydrogenase from Saccharomyces cerevisiae
14026 Overall Kinetic Mechanism of Saccharopine Dehydrogenase from Saccharomyces cerevisiae
14026 Overall Kinetic Mechanism of Saccharopine Dehydrogenase from Saccharomyces cerevisiae
14027 Overall Kinetic Mechanism of Saccharopine Dehydrogenase from Saccharomyces cerevisiae
14027 Overall Kinetic Mechanism of Saccharopine Dehydrogenase from Saccharomyces cerevisiae
14028 Overall Kinetic Mechanism of Saccharopine Dehydrogenase from Saccharomyces cerevisiae
14028 Overall Kinetic Mechanism of Saccharopine Dehydrogenase from Saccharomyces cerevisiae
14029 Overall Kinetic Mechanism of Saccharopine Dehydrogenase from Saccharomyces cerevisiae
14029 Overall Kinetic Mechanism of Saccharopine Dehydrogenase from Saccharomyces cerevisiae
14030 Overall Kinetic Mechanism of Saccharopine Dehydrogenase from Saccharomyces cerevisiae
14030 Overall Kinetic Mechanism of Saccharopine Dehydrogenase from Saccharomyces cerevisiae
14031 Overall Kinetic Mechanism of Saccharopine Dehydrogenase from Saccharomyces cerevisiae
14031 Overall Kinetic Mechanism of Saccharopine Dehydrogenase from Saccharomyces cerevisiae
14032 Overall Kinetic Mechanism of Saccharopine Dehydrogenase from Saccharomyces cerevisiae
14032 Overall Kinetic Mechanism of Saccharopine Dehydrogenase from Saccharomyces cerevisiae
14033 Overall Kinetic Mechanism of Saccharopine Dehydrogenase from Saccharomyces cerevisiae
14033 Overall Kinetic Mechanism of Saccharopine Dehydrogenase from Saccharomyces cerevisiae
14034 Overall Kinetic Mechanism of Saccharopine Dehydrogenase from Saccharomyces cerevisiae
14034 Overall Kinetic Mechanism of Saccharopine Dehydrogenase from Saccharomyces cerevisiae
14035 Overall Kinetic Mechanism of Saccharopine Dehydrogenase from Saccharomyces cerevisiae
14035 Overall Kinetic Mechanism of Saccharopine Dehydrogenase from Saccharomyces cerevisiae
14036 Overall Kinetic Mechanism of Saccharopine Dehydrogenase from Saccharomyces cerevisiae
14036 Overall Kinetic Mechanism of Saccharopine Dehydrogenase from Saccharomyces cerevisiae
14037 Overall Kinetic Mechanism of Saccharopine Dehydrogenase from Saccharomyces cerevisiae
14037 Overall Kinetic Mechanism of Saccharopine Dehydrogenase from Saccharomyces cerevisiae
14038 Overall Kinetic Mechanism of Saccharopine Dehydrogenase from Saccharomyces cerevisiae
14038 Overall Kinetic Mechanism of Saccharopine Dehydrogenase from Saccharomyces cerevisiae
14039 Overall Kinetic Mechanism of Saccharopine Dehydrogenase from Saccharomyces cerevisiae
14039 Overall Kinetic Mechanism of Saccharopine Dehydrogenase from Saccharomyces cerevisiae
14040 Overall Kinetic Mechanism of Saccharopine Dehydrogenase from Saccharomyces cerevisiae
14040 Overall Kinetic Mechanism of Saccharopine Dehydrogenase from Saccharomyces cerevisiae
14041 Overall Kinetic Mechanism of Saccharopine Dehydrogenase from Saccharomyces cerevisiae
14041 Overall Kinetic Mechanism of Saccharopine Dehydrogenase from Saccharomyces cerevisiae
14042 Overall Kinetic Mechanism of Saccharopine Dehydrogenase from Saccharomyces cerevisiae
14042 Overall Kinetic Mechanism of Saccharopine Dehydrogenase from Saccharomyces cerevisiae
14043 Overall Kinetic Mechanism of Saccharopine Dehydrogenase from Saccharomyces cerevisiae
14043 Overall Kinetic Mechanism of Saccharopine Dehydrogenase from Saccharomyces cerevisiae
14070 Metal ion specificity at the catalytic site of yeast enolase
14070 Metal ion specificity at the catalytic site of yeast enolase
14071 Metal ion specificity at the catalytic site of yeast enolase
14071 Metal ion specificity at the catalytic site of yeast enolase
14072 Metal ion specificity at the catalytic site of yeast enolase
14072 Metal ion specificity at the catalytic site of yeast enolase
14073 Metal ion specificity at the catalytic site of yeast enolase
14073 Metal ion specificity at the catalytic site of yeast enolase
14074 Metal ion specificity at the catalytic site of yeast enolase
14074 Metal ion specificity at the catalytic site of yeast enolase
14075 Metal ion specificity at the catalytic site of yeast enolase
14075 Metal ion specificity at the catalytic site of yeast enolase
14076 Metal ion specificity at the catalytic site of yeast enolase
14076 Metal ion specificity at the catalytic site of yeast enolase
14077 Metal ion specificity at the catalytic site of yeast enolase
14077 Metal ion specificity at the catalytic site of yeast enolase
14078 Metal ion specificity at the catalytic site of yeast enolase
14078 Metal ion specificity at the catalytic site of yeast enolase
14079 Metal ion specificity at the catalytic site of yeast enolase
14079 Metal ion specificity at the catalytic site of yeast enolase
14080 Metal ion specificity at the catalytic site of yeast enolase
14080 Metal ion specificity at the catalytic site of yeast enolase
14081 Metal ion specificity at the catalytic site of yeast enolase
14081 Metal ion specificity at the catalytic site of yeast enolase
14082 Metal ion specificity at the catalytic site of yeast enolase
14082 Metal ion specificity at the catalytic site of yeast enolase
14083 Metal ion specificity at the catalytic site of yeast enolase
14083 Metal ion specificity at the catalytic site of yeast enolase
14084 Metal ion specificity at the catalytic site of yeast enolase
14084 Metal ion specificity at the catalytic site of yeast enolase
14085 Metal ion specificity at the catalytic site of yeast enolase
14085 Metal ion specificity at the catalytic site of yeast enolase
14086 Metal ion specificity at the catalytic site of yeast enolase
14086 Metal ion specificity at the catalytic site of yeast enolase
14087 Methylthioadenosine phosphorylase from the archaeon Pyrococcus furiosus. Mechanism of the reaction and ...
14087 Methylthioadenosine phosphorylase from the archaeon Pyrococcus furiosus. Mechanism of the reaction and ...
14088 Methylthioadenosine phosphorylase from the archaeon Pyrococcus furiosus. Mechanism of the reaction and ...
14088 Methylthioadenosine phosphorylase from the archaeon Pyrococcus furiosus. Mechanism of the reaction and ...
14089 Methylthioadenosine phosphorylase from the archaeon Pyrococcus furiosus. Mechanism of the reaction and ...
14089 Methylthioadenosine phosphorylase from the archaeon Pyrococcus furiosus. Mechanism of the reaction and ...
14090 Methylthioadenosine phosphorylase from the archaeon Pyrococcus furiosus. Mechanism of the reaction and ...
14090 Methylthioadenosine phosphorylase from the archaeon Pyrococcus furiosus. Mechanism of the reaction and ...
14091 Methylthioadenosine phosphorylase from the archaeon Pyrococcus furiosus. Mechanism of the reaction and ...
14091 Methylthioadenosine phosphorylase from the archaeon Pyrococcus furiosus. Mechanism of the reaction and ...
14092 Methylthioadenosine phosphorylase from the archaeon Pyrococcus furiosus. Mechanism of the reaction and ...
14092 Methylthioadenosine phosphorylase from the archaeon Pyrococcus furiosus. Mechanism of the reaction and ...
14093 Methylthioadenosine phosphorylase from the archaeon Pyrococcus furiosus. Mechanism of the reaction and ...
14093 Methylthioadenosine phosphorylase from the archaeon Pyrococcus furiosus. Mechanism of the reaction and ...
14094 Methylthioadenosine phosphorylase from the archaeon Pyrococcus furiosus. Mechanism of the reaction and ...
14094 Methylthioadenosine phosphorylase from the archaeon Pyrococcus furiosus. Mechanism of the reaction and ...
14095 Methylthioadenosine phosphorylase from the archaeon Pyrococcus furiosus. Mechanism of the reaction and ...
14095 Methylthioadenosine phosphorylase from the archaeon Pyrococcus furiosus. Mechanism of the reaction and ...
14096 Pathway for the synthesis of mannosylglycerate in the hyperthermophilic archaeon Pyrococcus horikoshii. ...
14096 Pathway for the synthesis of mannosylglycerate in the hyperthermophilic archaeon Pyrococcus horikoshii. ...
14097 Pathway for the synthesis of mannosylglycerate in the hyperthermophilic archaeon Pyrococcus horikoshii. ...
14097 Pathway for the synthesis of mannosylglycerate in the hyperthermophilic archaeon Pyrococcus horikoshii. ...
14098 Pathway for the synthesis of mannosylglycerate in the hyperthermophilic archaeon Pyrococcus horikoshii. ...
14098 Pathway for the synthesis of mannosylglycerate in the hyperthermophilic archaeon Pyrococcus horikoshii. ...
14099 Pathway for the synthesis of mannosylglycerate in the hyperthermophilic archaeon Pyrococcus horikoshii. ...
14099 Pathway for the synthesis of mannosylglycerate in the hyperthermophilic archaeon Pyrococcus horikoshii. ...
14100 Pathway for the synthesis of mannosylglycerate in the hyperthermophilic archaeon Pyrococcus horikoshii. ...
14100 Pathway for the synthesis of mannosylglycerate in the hyperthermophilic archaeon Pyrococcus horikoshii. ...
14101 Pathway for the synthesis of mannosylglycerate in the hyperthermophilic archaeon Pyrococcus horikoshii. ...
14101 Pathway for the synthesis of mannosylglycerate in the hyperthermophilic archaeon Pyrococcus horikoshii. ...
14102 Pathway for the synthesis of mannosylglycerate in the hyperthermophilic archaeon Pyrococcus horikoshii. ...
14102 Pathway for the synthesis of mannosylglycerate in the hyperthermophilic archaeon Pyrococcus horikoshii. ...
14103 Pathway for the synthesis of mannosylglycerate in the hyperthermophilic archaeon Pyrococcus horikoshii. ...
14103 Pathway for the synthesis of mannosylglycerate in the hyperthermophilic archaeon Pyrococcus horikoshii. ...
14104 Pathway for the synthesis of mannosylglycerate in the hyperthermophilic archaeon Pyrococcus horikoshii. ...
14104 Pathway for the synthesis of mannosylglycerate in the hyperthermophilic archaeon Pyrococcus horikoshii. ...
14105 Pathway for the synthesis of mannosylglycerate in the hyperthermophilic archaeon Pyrococcus horikoshii. ...
14105 Pathway for the synthesis of mannosylglycerate in the hyperthermophilic archaeon Pyrococcus horikoshii. ...
14106 Pathway for the synthesis of mannosylglycerate in the hyperthermophilic archaeon Pyrococcus horikoshii. ...
14106 Pathway for the synthesis of mannosylglycerate in the hyperthermophilic archaeon Pyrococcus horikoshii. ...
14107 Pathway for the synthesis of mannosylglycerate in the hyperthermophilic archaeon Pyrococcus horikoshii. ...
14107 Pathway for the synthesis of mannosylglycerate in the hyperthermophilic archaeon Pyrococcus horikoshii. ...
14108 Characterization of human UDP-glucose dehydrogenase. CYS-276 is required for the second of two successive ...
14108 Characterization of human UDP-glucose dehydrogenase. CYS-276 is required for the second of two successive ...
14109 Characterization of human UDP-glucose dehydrogenase. CYS-276 is required for the second of two successive ...
14109 Characterization of human UDP-glucose dehydrogenase. CYS-276 is required for the second of two successive ...
14110 Characterization of human UDP-glucose dehydrogenase. CYS-276 is required for the second of two successive ...
14110 Characterization of human UDP-glucose dehydrogenase. CYS-276 is required for the second of two successive ...
14111 Characterization of human UDP-glucose dehydrogenase. CYS-276 is required for the second of two successive ...
14111 Characterization of human UDP-glucose dehydrogenase. CYS-276 is required for the second of two successive ...
14112 Characterization of human UDP-glucose dehydrogenase. CYS-276 is required for the second of two successive ...
14112 Characterization of human UDP-glucose dehydrogenase. CYS-276 is required for the second of two successive ...
14113 Site-directed mutagenesis of a hexapeptide segment involved in substrate recognition of phenylalanine ...
14113 Site-directed mutagenesis of a hexapeptide segment involved in substrate recognition of phenylalanine ...
14114 Site-directed mutagenesis of a hexapeptide segment involved in substrate recognition of phenylalanine ...
14114 Site-directed mutagenesis of a hexapeptide segment involved in substrate recognition of phenylalanine ...
14115 Site-directed mutagenesis of a hexapeptide segment involved in substrate recognition of phenylalanine ...
14115 Site-directed mutagenesis of a hexapeptide segment involved in substrate recognition of phenylalanine ...
14116 Site-directed mutagenesis of a hexapeptide segment involved in substrate recognition of phenylalanine ...
14116 Site-directed mutagenesis of a hexapeptide segment involved in substrate recognition of phenylalanine ...
14117 Site-directed mutagenesis of a hexapeptide segment involved in substrate recognition of phenylalanine ...
14117 Site-directed mutagenesis of a hexapeptide segment involved in substrate recognition of phenylalanine ...
14118 Site-directed mutagenesis of a hexapeptide segment involved in substrate recognition of phenylalanine ...
14118 Site-directed mutagenesis of a hexapeptide segment involved in substrate recognition of phenylalanine ...
14119 Site-directed mutagenesis of a hexapeptide segment involved in substrate recognition of phenylalanine ...
14119 Site-directed mutagenesis of a hexapeptide segment involved in substrate recognition of phenylalanine ...
14120 Site-directed mutagenesis of a hexapeptide segment involved in substrate recognition of phenylalanine ...
14120 Site-directed mutagenesis of a hexapeptide segment involved in substrate recognition of phenylalanine ...
14121 Site-directed mutagenesis of a hexapeptide segment involved in substrate recognition of phenylalanine ...
14121 Site-directed mutagenesis of a hexapeptide segment involved in substrate recognition of phenylalanine ...
14122 Site-directed mutagenesis of a hexapeptide segment involved in substrate recognition of phenylalanine ...
14122 Site-directed mutagenesis of a hexapeptide segment involved in substrate recognition of phenylalanine ...
14123 Site-directed mutagenesis of a hexapeptide segment involved in substrate recognition of phenylalanine ...
14123 Site-directed mutagenesis of a hexapeptide segment involved in substrate recognition of phenylalanine ...
14124 Site-directed mutagenesis of a hexapeptide segment involved in substrate recognition of phenylalanine ...
14124 Site-directed mutagenesis of a hexapeptide segment involved in substrate recognition of phenylalanine ...
14125 Site-directed mutagenesis of a hexapeptide segment involved in substrate recognition of phenylalanine ...
14125 Site-directed mutagenesis of a hexapeptide segment involved in substrate recognition of phenylalanine ...
14126 Site-directed mutagenesis of a hexapeptide segment involved in substrate recognition of phenylalanine ...
14126 Site-directed mutagenesis of a hexapeptide segment involved in substrate recognition of phenylalanine ...
14127 Site-directed mutagenesis of a hexapeptide segment involved in substrate recognition of phenylalanine ...
14127 Site-directed mutagenesis of a hexapeptide segment involved in substrate recognition of phenylalanine ...
14128 Site-directed mutagenesis of a hexapeptide segment involved in substrate recognition of phenylalanine ...
14128 Site-directed mutagenesis of a hexapeptide segment involved in substrate recognition of phenylalanine ...
14129 Site-directed mutagenesis of a hexapeptide segment involved in substrate recognition of phenylalanine ...
14129 Site-directed mutagenesis of a hexapeptide segment involved in substrate recognition of phenylalanine ...
14130 Site-directed mutagenesis of a hexapeptide segment involved in substrate recognition of phenylalanine ...
14130 Site-directed mutagenesis of a hexapeptide segment involved in substrate recognition of phenylalanine ...
14131 Site-directed mutagenesis of a hexapeptide segment involved in substrate recognition of phenylalanine ...
14131 Site-directed mutagenesis of a hexapeptide segment involved in substrate recognition of phenylalanine ...
14132 Site-directed mutagenesis of a hexapeptide segment involved in substrate recognition of phenylalanine ...
14132 Site-directed mutagenesis of a hexapeptide segment involved in substrate recognition of phenylalanine ...
14133 Site-directed mutagenesis of a hexapeptide segment involved in substrate recognition of phenylalanine ...
14133 Site-directed mutagenesis of a hexapeptide segment involved in substrate recognition of phenylalanine ...
14134 Site-directed mutagenesis of a hexapeptide segment involved in substrate recognition of phenylalanine ...
14134 Site-directed mutagenesis of a hexapeptide segment involved in substrate recognition of phenylalanine ...
14135 Site-directed mutagenesis of a hexapeptide segment involved in substrate recognition of phenylalanine ...
14135 Site-directed mutagenesis of a hexapeptide segment involved in substrate recognition of phenylalanine ...
14136 Site-directed mutagenesis of a hexapeptide segment involved in substrate recognition of phenylalanine ...
14136 Site-directed mutagenesis of a hexapeptide segment involved in substrate recognition of phenylalanine ...
14137 Site-directed mutagenesis of a hexapeptide segment involved in substrate recognition of phenylalanine ...
14137 Site-directed mutagenesis of a hexapeptide segment involved in substrate recognition of phenylalanine ...
14138 Site-directed mutagenesis of a hexapeptide segment involved in substrate recognition of phenylalanine ...
14138 Site-directed mutagenesis of a hexapeptide segment involved in substrate recognition of phenylalanine ...
14139 Insulin does not change the intracellular distribution of hexokinase in rat heart
14139 Insulin does not change the intracellular distribution of hexokinase in rat heart
14140 Insulin does not change the intracellular distribution of hexokinase in rat heart
14140 Insulin does not change the intracellular distribution of hexokinase in rat heart
14141 Insulin does not change the intracellular distribution of hexokinase in rat heart
14141 Insulin does not change the intracellular distribution of hexokinase in rat heart
14142 Insulin does not change the intracellular distribution of hexokinase in rat heart
14142 Insulin does not change the intracellular distribution of hexokinase in rat heart
14143 Insulin does not change the intracellular distribution of hexokinase in rat heart
14143 Insulin does not change the intracellular distribution of hexokinase in rat heart
14144 Insulin does not change the intracellular distribution of hexokinase in rat heart
14144 Insulin does not change the intracellular distribution of hexokinase in rat heart
14145 Insulin does not change the intracellular distribution of hexokinase in rat heart
14145 Insulin does not change the intracellular distribution of hexokinase in rat heart
14146 Insulin does not change the intracellular distribution of hexokinase in rat heart
14146 Insulin does not change the intracellular distribution of hexokinase in rat heart
14147 Insulin does not change the intracellular distribution of hexokinase in rat heart
14147 Insulin does not change the intracellular distribution of hexokinase in rat heart
14148 Insulin does not change the intracellular distribution of hexokinase in rat heart
14148 Insulin does not change the intracellular distribution of hexokinase in rat heart
14149 Insulin does not change the intracellular distribution of hexokinase in rat heart
14149 Insulin does not change the intracellular distribution of hexokinase in rat heart
14150 Insulin does not change the intracellular distribution of hexokinase in rat heart
14150 Insulin does not change the intracellular distribution of hexokinase in rat heart
14151 Insulin does not change the intracellular distribution of hexokinase in rat heart
14151 Insulin does not change the intracellular distribution of hexokinase in rat heart
14152 Insulin does not change the intracellular distribution of hexokinase in rat heart
14152 Insulin does not change the intracellular distribution of hexokinase in rat heart
14153 Insulin does not change the intracellular distribution of hexokinase in rat heart
14153 Insulin does not change the intracellular distribution of hexokinase in rat heart
14154 Insulin does not change the intracellular distribution of hexokinase in rat heart
14154 Insulin does not change the intracellular distribution of hexokinase in rat heart
14155 Insulin does not change the intracellular distribution of hexokinase in rat heart
14155 Insulin does not change the intracellular distribution of hexokinase in rat heart
14156 Insulin does not change the intracellular distribution of hexokinase in rat heart
14156 Insulin does not change the intracellular distribution of hexokinase in rat heart
14157 Insulin does not change the intracellular distribution of hexokinase in rat heart
14157 Insulin does not change the intracellular distribution of hexokinase in rat heart
14158 Insulin does not change the intracellular distribution of hexokinase in rat heart
14158 Insulin does not change the intracellular distribution of hexokinase in rat heart
14159 The fast-reacting sulfhydryl group of rat muscle phosphoglycerate kinase is necessary for activity and ...
14159 The fast-reacting sulfhydryl group of rat muscle phosphoglycerate kinase is necessary for activity and ...
14160 The fast-reacting sulfhydryl group of rat muscle phosphoglycerate kinase is necessary for activity and ...
14160 The fast-reacting sulfhydryl group of rat muscle phosphoglycerate kinase is necessary for activity and ...
14161 The fast-reacting sulfhydryl group of rat muscle phosphoglycerate kinase is necessary for activity and ...
14161 The fast-reacting sulfhydryl group of rat muscle phosphoglycerate kinase is necessary for activity and ...
14162 The fast-reacting sulfhydryl group of rat muscle phosphoglycerate kinase is necessary for activity and ...
14162 The fast-reacting sulfhydryl group of rat muscle phosphoglycerate kinase is necessary for activity and ...
14163 The fast-reacting sulfhydryl group of rat muscle phosphoglycerate kinase is necessary for activity and ...
14163 The fast-reacting sulfhydryl group of rat muscle phosphoglycerate kinase is necessary for activity and ...
14164 The fast-reacting sulfhydryl group of rat muscle phosphoglycerate kinase is necessary for activity and ...
14164 The fast-reacting sulfhydryl group of rat muscle phosphoglycerate kinase is necessary for activity and ...
14165 The fast-reacting sulfhydryl group of rat muscle phosphoglycerate kinase is necessary for activity and ...
14165 The fast-reacting sulfhydryl group of rat muscle phosphoglycerate kinase is necessary for activity and ...
14166 The fast-reacting sulfhydryl group of rat muscle phosphoglycerate kinase is necessary for activity and ...
14166 The fast-reacting sulfhydryl group of rat muscle phosphoglycerate kinase is necessary for activity and ...
14167 The fast-reacting sulfhydryl group of rat muscle phosphoglycerate kinase is necessary for activity and ...
14167 The fast-reacting sulfhydryl group of rat muscle phosphoglycerate kinase is necessary for activity and ...
14168 Construction of a synthetic gene for an R-plasmid-encoded dihydrofolate reductase and studies on the role of ...
14168 Construction of a synthetic gene for an R-plasmid-encoded dihydrofolate reductase and studies on the role of ...
14169 Construction of a synthetic gene for an R-plasmid-encoded dihydrofolate reductase and studies on the role of ...
14169 Construction of a synthetic gene for an R-plasmid-encoded dihydrofolate reductase and studies on the role of ...
14170 Construction of a synthetic gene for an R-plasmid-encoded dihydrofolate reductase and studies on the role of ...
14170 Construction of a synthetic gene for an R-plasmid-encoded dihydrofolate reductase and studies on the role of ...
14171 Construction of a synthetic gene for an R-plasmid-encoded dihydrofolate reductase and studies on the role of ...
14171 Construction of a synthetic gene for an R-plasmid-encoded dihydrofolate reductase and studies on the role of ...
14189 Kinetic Studies on the reaction catalyzed by Phosphoglycerate Kinase. I. The Effect of Mg2+ and Adenosine ...
14189 Kinetic Studies on the reaction catalyzed by Phosphoglycerate Kinase. I. The Effect of Mg2+ and Adenosine ...
14190 Kinetic Studies on the reaction catalyzed by Phosphoglycerate Kinase. I. The Effect of Mg2+ and Adenosine ...
14190 Kinetic Studies on the reaction catalyzed by Phosphoglycerate Kinase. I. The Effect of Mg2+ and Adenosine ...
14191 Kinetic Studies on the reaction catalyzed by Phosphoglycerate Kinase. I. The Effect of Mg2+ and Adenosine ...
14191 Kinetic Studies on the reaction catalyzed by Phosphoglycerate Kinase. I. The Effect of Mg2+ and Adenosine ...
14192 Kinetic Studies on the reaction catalyzed by Phosphoglycerate Kinase. I. The Effect of Mg2+ and Adenosine ...
14192 Kinetic Studies on the reaction catalyzed by Phosphoglycerate Kinase. I. The Effect of Mg2+ and Adenosine ...
14193 Kinetic Studies on the reaction catalyzed by Phosphoglycerate Kinase. I. The Effect of Mg2+ and Adenosine ...
14193 Kinetic Studies on the reaction catalyzed by Phosphoglycerate Kinase. I. The Effect of Mg2+ and Adenosine ...
14194 Kinetic Studies on the reaction catalyzed by Phosphoglycerate Kinase. I. The Effect of Mg2+ and Adenosine ...
14194 Kinetic Studies on the reaction catalyzed by Phosphoglycerate Kinase. I. The Effect of Mg2+ and Adenosine ...
14195 Kinetic Studies on the reaction catalyzed by Phosphoglycerate Kinase. I. The Effect of Mg2+ and Adenosine ...
14195 Kinetic Studies on the reaction catalyzed by Phosphoglycerate Kinase. I. The Effect of Mg2+ and Adenosine ...
14196 Kinetic Studies on the reaction catalyzed by Phosphoglycerate Kinase. I. The Effect of Mg2+ and Adenosine ...
14196 Kinetic Studies on the reaction catalyzed by Phosphoglycerate Kinase. I. The Effect of Mg2+ and Adenosine ...
14197 Kinetic Studies on the reaction catalyzed by Phosphoglycerate Kinase. I. The Effect of Mg2+ and Adenosine ...
14197 Kinetic Studies on the reaction catalyzed by Phosphoglycerate Kinase. I. The Effect of Mg2+ and Adenosine ...
14198 Kinetic Studies on the reaction catalyzed by Phosphoglycerate Kinase. I. The Effect of Mg2+ and Adenosine ...
14198 Kinetic Studies on the reaction catalyzed by Phosphoglycerate Kinase. I. The Effect of Mg2+ and Adenosine ...
14199 Kinetic Studies on the reaction catalyzed by Phosphoglycerate Kinase. I. The Effect of Mg2+ and Adenosine ...
14199 Kinetic Studies on the reaction catalyzed by Phosphoglycerate Kinase. I. The Effect of Mg2+ and Adenosine ...
14200 Kinetic Studies on the reaction catalyzed by Phosphoglycerate Kinase. I. The Effect of Mg2+ and Adenosine ...
14200 Kinetic Studies on the reaction catalyzed by Phosphoglycerate Kinase. I. The Effect of Mg2+ and Adenosine ...
14201 Kinetic Studies on the reaction catalyzed by Phosphoglycerate Kinase. I. The Effect of Mg2+ and Adenosine ...
14201 Kinetic Studies on the reaction catalyzed by Phosphoglycerate Kinase. I. The Effect of Mg2+ and Adenosine ...
14202 Kinetic Studies on the reaction catalyzed by Phosphoglycerate Kinase. I. The Effect of Mg2+ and Adenosine ...
14202 Kinetic Studies on the reaction catalyzed by Phosphoglycerate Kinase. I. The Effect of Mg2+ and Adenosine ...
14203 Kinetic Studies on the reaction catalyzed by Phosphoglycerate Kinase. I. The Effect of Mg2+ and Adenosine ...
14203 Kinetic Studies on the reaction catalyzed by Phosphoglycerate Kinase. I. The Effect of Mg2+ and Adenosine ...
14204 Properties of uridine diphosphate glucose pyrophosphorylase from Golgi apparatus of liver
14204 Properties of uridine diphosphate glucose pyrophosphorylase from Golgi apparatus of liver
14205 Properties of uridine diphosphate glucose pyrophosphorylase from Golgi apparatus of liver
14205 Properties of uridine diphosphate glucose pyrophosphorylase from Golgi apparatus of liver
14206 Properties of uridine diphosphate glucose pyrophosphorylase from Golgi apparatus of liver
14206 Properties of uridine diphosphate glucose pyrophosphorylase from Golgi apparatus of liver
14207 Properties of uridine diphosphate glucose pyrophosphorylase from Golgi apparatus of liver
14207 Properties of uridine diphosphate glucose pyrophosphorylase from Golgi apparatus of liver
14208 The contribution of lysine-36 to catalysis by human myo-inositol monophosphatase
14208 The contribution of lysine-36 to catalysis by human myo-inositol monophosphatase
14209 The contribution of lysine-36 to catalysis by human myo-inositol monophosphatase
14209 The contribution of lysine-36 to catalysis by human myo-inositol monophosphatase
14210 The contribution of lysine-36 to catalysis by human myo-inositol monophosphatase
14210 The contribution of lysine-36 to catalysis by human myo-inositol monophosphatase
14211 The contribution of lysine-36 to catalysis by human myo-inositol monophosphatase
14211 The contribution of lysine-36 to catalysis by human myo-inositol monophosphatase
14212 The contribution of lysine-36 to catalysis by human myo-inositol monophosphatase
14212 The contribution of lysine-36 to catalysis by human myo-inositol monophosphatase
14213 The contribution of lysine-36 to catalysis by human myo-inositol monophosphatase
14213 The contribution of lysine-36 to catalysis by human myo-inositol monophosphatase
14214 The contribution of lysine-36 to catalysis by human myo-inositol monophosphatase
14214 The contribution of lysine-36 to catalysis by human myo-inositol monophosphatase
14215 The contribution of lysine-36 to catalysis by human myo-inositol monophosphatase
14215 The contribution of lysine-36 to catalysis by human myo-inositol monophosphatase
14216 The contribution of lysine-36 to catalysis by human myo-inositol monophosphatase
14216 The contribution of lysine-36 to catalysis by human myo-inositol monophosphatase
14217 The contribution of lysine-36 to catalysis by human myo-inositol monophosphatase
14217 The contribution of lysine-36 to catalysis by human myo-inositol monophosphatase
14218 The contribution of lysine-36 to catalysis by human myo-inositol monophosphatase
14218 The contribution of lysine-36 to catalysis by human myo-inositol monophosphatase
14219 The contribution of lysine-36 to catalysis by human myo-inositol monophosphatase
14219 The contribution of lysine-36 to catalysis by human myo-inositol monophosphatase
14220 The contribution of lysine-36 to catalysis by human myo-inositol monophosphatase
14220 The contribution of lysine-36 to catalysis by human myo-inositol monophosphatase
14221 The contribution of lysine-36 to catalysis by human myo-inositol monophosphatase
14221 The contribution of lysine-36 to catalysis by human myo-inositol monophosphatase
14222 The contribution of lysine-36 to catalysis by human myo-inositol monophosphatase
14222 The contribution of lysine-36 to catalysis by human myo-inositol monophosphatase
14223 The contribution of lysine-36 to catalysis by human myo-inositol monophosphatase
14223 The contribution of lysine-36 to catalysis by human myo-inositol monophosphatase
14224 Electrostatic stabilization in a pre-organized polar active site: the catalytic role of Lys-80 in Candida ...
14224 Electrostatic stabilization in a pre-organized polar active site: the catalytic role of Lys-80 in Candida ...
14225 Electrostatic stabilization in a pre-organized polar active site: the catalytic role of Lys-80 in Candida ...
14225 Electrostatic stabilization in a pre-organized polar active site: the catalytic role of Lys-80 in Candida ...
14226 Electrostatic stabilization in a pre-organized polar active site: the catalytic role of Lys-80 in Candida ...
14226 Electrostatic stabilization in a pre-organized polar active site: the catalytic role of Lys-80 in Candida ...
14227 Electrostatic stabilization in a pre-organized polar active site: the catalytic role of Lys-80 in Candida ...
14227 Electrostatic stabilization in a pre-organized polar active site: the catalytic role of Lys-80 in Candida ...
14228 Electrostatic stabilization in a pre-organized polar active site: the catalytic role of Lys-80 in Candida ...
14228 Electrostatic stabilization in a pre-organized polar active site: the catalytic role of Lys-80 in Candida ...
14229 Electrostatic stabilization in a pre-organized polar active site: the catalytic role of Lys-80 in Candida ...
14229 Electrostatic stabilization in a pre-organized polar active site: the catalytic role of Lys-80 in Candida ...
14230 Electrostatic stabilization in a pre-organized polar active site: the catalytic role of Lys-80 in Candida ...
14230 Electrostatic stabilization in a pre-organized polar active site: the catalytic role of Lys-80 in Candida ...
14231 Electrostatic stabilization in a pre-organized polar active site: the catalytic role of Lys-80 in Candida ...
14231 Electrostatic stabilization in a pre-organized polar active site: the catalytic role of Lys-80 in Candida ...
14232 Electrostatic stabilization in a pre-organized polar active site: the catalytic role of Lys-80 in Candida ...
14232 Electrostatic stabilization in a pre-organized polar active site: the catalytic role of Lys-80 in Candida ...
14233 Electrostatic stabilization in a pre-organized polar active site: the catalytic role of Lys-80 in Candida ...
14233 Electrostatic stabilization in a pre-organized polar active site: the catalytic role of Lys-80 in Candida ...
14234 Electrostatic stabilization in a pre-organized polar active site: the catalytic role of Lys-80 in Candida ...
14234 Electrostatic stabilization in a pre-organized polar active site: the catalytic role of Lys-80 in Candida ...
14235 Electrostatic stabilization in a pre-organized polar active site: the catalytic role of Lys-80 in Candida ...
14235 Electrostatic stabilization in a pre-organized polar active site: the catalytic role of Lys-80 in Candida ...
14236 Electrostatic stabilization in a pre-organized polar active site: the catalytic role of Lys-80 in Candida ...
14236 Electrostatic stabilization in a pre-organized polar active site: the catalytic role of Lys-80 in Candida ...
14237 Electrostatic stabilization in a pre-organized polar active site: the catalytic role of Lys-80 in Candida ...
14237 Electrostatic stabilization in a pre-organized polar active site: the catalytic role of Lys-80 in Candida ...
14238 Electrostatic stabilization in a pre-organized polar active site: the catalytic role of Lys-80 in Candida ...
14238 Electrostatic stabilization in a pre-organized polar active site: the catalytic role of Lys-80 in Candida ...
14239 Electrostatic stabilization in a pre-organized polar active site: the catalytic role of Lys-80 in Candida ...
14239 Electrostatic stabilization in a pre-organized polar active site: the catalytic role of Lys-80 in Candida ...
14240 Electrostatic stabilization in a pre-organized polar active site: the catalytic role of Lys-80 in Candida ...
14240 Electrostatic stabilization in a pre-organized polar active site: the catalytic role of Lys-80 in Candida ...
14241 Electrostatic stabilization in a pre-organized polar active site: the catalytic role of Lys-80 in Candida ...
14241 Electrostatic stabilization in a pre-organized polar active site: the catalytic role of Lys-80 in Candida ...
14242 Electrostatic stabilization in a pre-organized polar active site: the catalytic role of Lys-80 in Candida ...
14242 Electrostatic stabilization in a pre-organized polar active site: the catalytic role of Lys-80 in Candida ...
14243 Electrostatic stabilization in a pre-organized polar active site: the catalytic role of Lys-80 in Candida ...
14243 Electrostatic stabilization in a pre-organized polar active site: the catalytic role of Lys-80 in Candida ...
14244 Electrostatic stabilization in a pre-organized polar active site: the catalytic role of Lys-80 in Candida ...
14244 Electrostatic stabilization in a pre-organized polar active site: the catalytic role of Lys-80 in Candida ...
14245 Electrostatic stabilization in a pre-organized polar active site: the catalytic role of Lys-80 in Candida ...
14245 Electrostatic stabilization in a pre-organized polar active site: the catalytic role of Lys-80 in Candida ...
14246 Phosphofructokinase from Lactobacteriaceae II. Purification and Properties of Phosphofructokinase from ...
14246 Phosphofructokinase from Lactobacteriaceae II. Purification and Properties of Phosphofructokinase from ...
14247 Phosphofructokinase from Lactobacteriaceae II. Purification and Properties of Phosphofructokinase from ...
14247 Phosphofructokinase from Lactobacteriaceae II. Purification and Properties of Phosphofructokinase from ...
14248 Phosphofructokinase from Lactobacteriaceae II. Purification and Properties of Phosphofructokinase from ...
14248 Phosphofructokinase from Lactobacteriaceae II. Purification and Properties of Phosphofructokinase from ...
14249 Phosphofructokinase from Lactobacteriaceae II. Purification and Properties of Phosphofructokinase from ...
14249 Phosphofructokinase from Lactobacteriaceae II. Purification and Properties of Phosphofructokinase from ...
14250 Phosphofructokinase from Lactobacteriaceae II. Purification and Properties of Phosphofructokinase from ...
14250 Phosphofructokinase from Lactobacteriaceae II. Purification and Properties of Phosphofructokinase from ...
14251 Phosphofructokinase from Lactobacteriaceae II. Purification and Properties of Phosphofructokinase from ...
14251 Phosphofructokinase from Lactobacteriaceae II. Purification and Properties of Phosphofructokinase from ...
14252 Catalytic properties of the archaeal S-adenosylmethionine decarboxylase from Methanococcus jannaschii
14252 Catalytic properties of the archaeal S-adenosylmethionine decarboxylase from Methanococcus jannaschii
14253 Catalytic properties of the archaeal S-adenosylmethionine decarboxylase from Methanococcus jannaschii
14253 Catalytic properties of the archaeal S-adenosylmethionine decarboxylase from Methanococcus jannaschii
14254 Catalytic properties of the archaeal S-adenosylmethionine decarboxylase from Methanococcus jannaschii
14254 Catalytic properties of the archaeal S-adenosylmethionine decarboxylase from Methanococcus jannaschii
14255 Isolation and biochemical characterization of two soluble iron(III) reductases from Paracoccus denitrificans
14255 Isolation and biochemical characterization of two soluble iron(III) reductases from Paracoccus denitrificans
14256 Isolation and biochemical characterization of two soluble iron(III) reductases from Paracoccus denitrificans
14256 Isolation and biochemical characterization of two soluble iron(III) reductases from Paracoccus denitrificans
14257 Isolation and biochemical characterization of two soluble iron(III) reductases from Paracoccus denitrificans
14257 Isolation and biochemical characterization of two soluble iron(III) reductases from Paracoccus denitrificans
14258 Isolation and biochemical characterization of two soluble iron(III) reductases from Paracoccus denitrificans
14258 Isolation and biochemical characterization of two soluble iron(III) reductases from Paracoccus denitrificans
14259 Isolation and biochemical characterization of two soluble iron(III) reductases from Paracoccus denitrificans
14259 Isolation and biochemical characterization of two soluble iron(III) reductases from Paracoccus denitrificans
14260 Isolation and biochemical characterization of two soluble iron(III) reductases from Paracoccus denitrificans
14260 Isolation and biochemical characterization of two soluble iron(III) reductases from Paracoccus denitrificans
14261 Isolation and biochemical characterization of two soluble iron(III) reductases from Paracoccus denitrificans
14261 Isolation and biochemical characterization of two soluble iron(III) reductases from Paracoccus denitrificans
14262 Isolation and biochemical characterization of two soluble iron(III) reductases from Paracoccus denitrificans
14262 Isolation and biochemical characterization of two soluble iron(III) reductases from Paracoccus denitrificans
14263 Isolation and biochemical characterization of two soluble iron(III) reductases from Paracoccus denitrificans
14263 Isolation and biochemical characterization of two soluble iron(III) reductases from Paracoccus denitrificans
14264 Isolation and biochemical characterization of two soluble iron(III) reductases from Paracoccus denitrificans
14264 Isolation and biochemical characterization of two soluble iron(III) reductases from Paracoccus denitrificans
14265 Purification and properties of fructokinase I from Lactococcus lactis. Localization of scrK on the ...
14265 Purification and properties of fructokinase I from Lactococcus lactis. Localization of scrK on the ...
14266 Purification and properties of fructokinase I from Lactococcus lactis. Localization of scrK on the ...
14266 Purification and properties of fructokinase I from Lactococcus lactis. Localization of scrK on the ...
14267 Purification and properties of fructokinase I from Lactococcus lactis. Localization of scrK on the ...
14267 Purification and properties of fructokinase I from Lactococcus lactis. Localization of scrK on the ...
14268 Characterization of aromatic aminotransferases from the hyperthermophilic archaeon Thermococcus litoralis
14268 Characterization of aromatic aminotransferases from the hyperthermophilic archaeon Thermococcus litoralis
14269 Characterization of aromatic aminotransferases from the hyperthermophilic archaeon Thermococcus litoralis
14269 Characterization of aromatic aminotransferases from the hyperthermophilic archaeon Thermococcus litoralis
14270 Characterization of aromatic aminotransferases from the hyperthermophilic archaeon Thermococcus litoralis
14270 Characterization of aromatic aminotransferases from the hyperthermophilic archaeon Thermococcus litoralis
14271 Characterization of aromatic aminotransferases from the hyperthermophilic archaeon Thermococcus litoralis
14271 Characterization of aromatic aminotransferases from the hyperthermophilic archaeon Thermococcus litoralis
14272 Characterization of aromatic aminotransferases from the hyperthermophilic archaeon Thermococcus litoralis
14272 Characterization of aromatic aminotransferases from the hyperthermophilic archaeon Thermococcus litoralis
14273 Characterization of aromatic aminotransferases from the hyperthermophilic archaeon Thermococcus litoralis
14273 Characterization of aromatic aminotransferases from the hyperthermophilic archaeon Thermococcus litoralis
14274 Structure and mechanism of glutamate racemase from Aquifex pyrophilus
14274 Structure and mechanism of glutamate racemase from Aquifex pyrophilus
14275 Structure and mechanism of glutamate racemase from Aquifex pyrophilus
14275 Structure and mechanism of glutamate racemase from Aquifex pyrophilus
14276 Structure and mechanism of glutamate racemase from Aquifex pyrophilus
14276 Structure and mechanism of glutamate racemase from Aquifex pyrophilus
14277 Structure and mechanism of glutamate racemase from Aquifex pyrophilus
14277 Structure and mechanism of glutamate racemase from Aquifex pyrophilus
14278 Structure and mechanism of glutamate racemase from Aquifex pyrophilus
14278 Structure and mechanism of glutamate racemase from Aquifex pyrophilus
14279 Structure and mechanism of glutamate racemase from Aquifex pyrophilus
14279 Structure and mechanism of glutamate racemase from Aquifex pyrophilus
14280 A transient intermediate in the reaction catalyzed by (S)-mandelate dehydrogenase from Pseudomonas putida
14280 A transient intermediate in the reaction catalyzed by (S)-mandelate dehydrogenase from Pseudomonas putida
14281 A transient intermediate in the reaction catalyzed by (S)-mandelate dehydrogenase from Pseudomonas putida
14281 A transient intermediate in the reaction catalyzed by (S)-mandelate dehydrogenase from Pseudomonas putida
14282 Enzymatic proof for the identity of the S-sulfocysteine synthase and cysteine synthase B of Salmonella ...
14282 Enzymatic proof for the identity of the S-sulfocysteine synthase and cysteine synthase B of Salmonella ...
14283 Enzymatic proof for the identity of the S-sulfocysteine synthase and cysteine synthase B of Salmonella ...
14283 Enzymatic proof for the identity of the S-sulfocysteine synthase and cysteine synthase B of Salmonella ...
14284 Single-turnover kinetics of homoprotocatechuate 2,3-dioxygenase
14284 Single-turnover kinetics of homoprotocatechuate 2,3-dioxygenase
14285 Single-turnover kinetics of homoprotocatechuate 2,3-dioxygenase
14285 Single-turnover kinetics of homoprotocatechuate 2,3-dioxygenase
14286 Single-turnover kinetics of homoprotocatechuate 2,3-dioxygenase
14286 Single-turnover kinetics of homoprotocatechuate 2,3-dioxygenase
14287 Single-turnover kinetics of homoprotocatechuate 2,3-dioxygenase
14287 Single-turnover kinetics of homoprotocatechuate 2,3-dioxygenase
14288 Magnesium ion requirements for yeast enolase activity
14288 Magnesium ion requirements for yeast enolase activity
14289 Magnesium ion requirements for yeast enolase activity
14289 Magnesium ion requirements for yeast enolase activity
14290 Mutational analysis of the catalytic domain of O-linked N-acetylglucosaminyl transferase
14290 Mutational analysis of the catalytic domain of O-linked N-acetylglucosaminyl transferase
14291 Mutational analysis of the catalytic domain of O-linked N-acetylglucosaminyl transferase
14291 Mutational analysis of the catalytic domain of O-linked N-acetylglucosaminyl transferase
14292 Mutational analysis of the catalytic domain of O-linked N-acetylglucosaminyl transferase
14292 Mutational analysis of the catalytic domain of O-linked N-acetylglucosaminyl transferase
14293 Mutational analysis of the catalytic domain of O-linked N-acetylglucosaminyl transferase
14293 Mutational analysis of the catalytic domain of O-linked N-acetylglucosaminyl transferase
14294 Mutational analysis of the catalytic domain of O-linked N-acetylglucosaminyl transferase
14294 Mutational analysis of the catalytic domain of O-linked N-acetylglucosaminyl transferase
14295 Tyrosine residues near the FAD binding site are critical for FAD binding and for the maintenance of the stable ...
14295 Tyrosine residues near the FAD binding site are critical for FAD binding and for the maintenance of the stable ...
14296 Tyrosine residues near the FAD binding site are critical for FAD binding and for the maintenance of the stable ...
14296 Tyrosine residues near the FAD binding site are critical for FAD binding and for the maintenance of the stable ...
14297 Tyrosine residues near the FAD binding site are critical for FAD binding and for the maintenance of the stable ...
14297 Tyrosine residues near the FAD binding site are critical for FAD binding and for the maintenance of the stable ...
14298 Tyrosine residues near the FAD binding site are critical for FAD binding and for the maintenance of the stable ...
14298 Tyrosine residues near the FAD binding site are critical for FAD binding and for the maintenance of the stable ...
14299 Tyrosine residues near the FAD binding site are critical for FAD binding and for the maintenance of the stable ...
14299 Tyrosine residues near the FAD binding site are critical for FAD binding and for the maintenance of the stable ...
14300 Tyrosine residues near the FAD binding site are critical for FAD binding and for the maintenance of the stable ...
14300 Tyrosine residues near the FAD binding site are critical for FAD binding and for the maintenance of the stable ...
14301 Tyrosine residues near the FAD binding site are critical for FAD binding and for the maintenance of the stable ...
14301 Tyrosine residues near the FAD binding site are critical for FAD binding and for the maintenance of the stable ...
14302 Tyrosine residues near the FAD binding site are critical for FAD binding and for the maintenance of the stable ...
14302 Tyrosine residues near the FAD binding site are critical for FAD binding and for the maintenance of the stable ...
14303 Tyrosine residues near the FAD binding site are critical for FAD binding and for the maintenance of the stable ...
14303 Tyrosine residues near the FAD binding site are critical for FAD binding and for the maintenance of the stable ...
14304 Tyrosine residues near the FAD binding site are critical for FAD binding and for the maintenance of the stable ...
14304 Tyrosine residues near the FAD binding site are critical for FAD binding and for the maintenance of the stable ...
14305 Tyrosine residues near the FAD binding site are critical for FAD binding and for the maintenance of the stable ...
14305 Tyrosine residues near the FAD binding site are critical for FAD binding and for the maintenance of the stable ...
14306 Tyrosine residues near the FAD binding site are critical for FAD binding and for the maintenance of the stable ...
14306 Tyrosine residues near the FAD binding site are critical for FAD binding and for the maintenance of the stable ...
14307 Tyrosine residues near the FAD binding site are critical for FAD binding and for the maintenance of the stable ...
14307 Tyrosine residues near the FAD binding site are critical for FAD binding and for the maintenance of the stable ...
14308 Tyrosine residues near the FAD binding site are critical for FAD binding and for the maintenance of the stable ...
14308 Tyrosine residues near the FAD binding site are critical for FAD binding and for the maintenance of the stable ...
14309 Tyrosine residues near the FAD binding site are critical for FAD binding and for the maintenance of the stable ...
14309 Tyrosine residues near the FAD binding site are critical for FAD binding and for the maintenance of the stable ...
14310 Tyrosine residues near the FAD binding site are critical for FAD binding and for the maintenance of the stable ...
14310 Tyrosine residues near the FAD binding site are critical for FAD binding and for the maintenance of the stable ...
14311 Tyrosine residues near the FAD binding site are critical for FAD binding and for the maintenance of the stable ...
14311 Tyrosine residues near the FAD binding site are critical for FAD binding and for the maintenance of the stable ...
14312 Tyrosine residues near the FAD binding site are critical for FAD binding and for the maintenance of the stable ...
14312 Tyrosine residues near the FAD binding site are critical for FAD binding and for the maintenance of the stable ...
14313 Tyrosine residues near the FAD binding site are critical for FAD binding and for the maintenance of the stable ...
14313 Tyrosine residues near the FAD binding site are critical for FAD binding and for the maintenance of the stable ...
14314 Tyrosine residues near the FAD binding site are critical for FAD binding and for the maintenance of the stable ...
14315 Tyrosine residues near the FAD binding site are critical for FAD binding and for the maintenance of the stable ...
14316 Site-directed mutagenesis of catalytic residues of influenza virus neuraminidase as an aid to drug design
14317 Site-directed mutagenesis of catalytic residues of influenza virus neuraminidase as an aid to drug design
14318 Site-directed mutagenesis of catalytic residues of influenza virus neuraminidase as an aid to drug design
14319 Site-directed mutagenesis of catalytic residues of influenza virus neuraminidase as an aid to drug design
14320 Site-directed mutagenesis of catalytic residues of influenza virus neuraminidase as an aid to drug design
14321 Site-directed mutagenesis of catalytic residues of influenza virus neuraminidase as an aid to drug design
14322 Site-directed mutagenesis of catalytic residues of influenza virus neuraminidase as an aid to drug design
14323 Site-directed mutagenesis of catalytic residues of influenza virus neuraminidase as an aid to drug design
14324 Site-directed mutagenesis of catalytic residues of influenza virus neuraminidase as an aid to drug design
14325 Site-directed mutagenesis of catalytic residues of influenza virus neuraminidase as an aid to drug design
14326 Site-directed mutagenesis of catalytic residues of influenza virus neuraminidase as an aid to drug design
14327 Site-directed mutagenesis of catalytic residues of influenza virus neuraminidase as an aid to drug design
14328 Site-directed mutagenesis of catalytic residues of influenza virus neuraminidase as an aid to drug design
14329 Site-directed mutagenesis of catalytic residues of influenza virus neuraminidase as an aid to drug design
14330 Site-directed mutagenesis of catalytic residues of influenza virus neuraminidase as an aid to drug design
14331 Site-directed mutagenesis of catalytic residues of influenza virus neuraminidase as an aid to drug design
14332 Site-directed mutagenesis of catalytic residues of influenza virus neuraminidase as an aid to drug design
14333 Catalytic and structural characteristics of carp hepatopancreas D-amino acid oxidase expressed in Escherichia ...
14334 Catalytic and structural characteristics of carp hepatopancreas D-amino acid oxidase expressed in Escherichia ...
14335 Catalytic and structural characteristics of carp hepatopancreas D-amino acid oxidase expressed in Escherichia ...
14336 Catalytic and structural characteristics of carp hepatopancreas D-amino acid oxidase expressed in Escherichia ...
14337 Catalytic and structural characteristics of carp hepatopancreas D-amino acid oxidase expressed in Escherichia ...
14338 Catalytic and structural characteristics of carp hepatopancreas D-amino acid oxidase expressed in Escherichia ...
14339 Catalytic and structural characteristics of carp hepatopancreas D-amino acid oxidase expressed in Escherichia ...
14340 Catalytic and structural characteristics of carp hepatopancreas D-amino acid oxidase expressed in Escherichia ...
14341 Catalytic and structural characteristics of carp hepatopancreas D-amino acid oxidase expressed in Escherichia ...
14342 Catalytic and structural characteristics of carp hepatopancreas D-amino acid oxidase expressed in Escherichia ...
14343 Catalytic and structural characteristics of carp hepatopancreas D-amino acid oxidase expressed in Escherichia ...
14344 Catalytic and structural characteristics of carp hepatopancreas D-amino acid oxidase expressed in Escherichia ...
14345 Characterization of recombinant diaminopropionate ammonia-lyase from Escherichia coli and Salmonella ...
14346 Characterization of recombinant diaminopropionate ammonia-lyase from Escherichia coli and Salmonella ...
14347 Characterization of recombinant diaminopropionate ammonia-lyase from Escherichia coli and Salmonella ...
14348 Characterization of recombinant diaminopropionate ammonia-lyase from Escherichia coli and Salmonella ...
14349 Characterization of recombinant diaminopropionate ammonia-lyase from Escherichia coli and Salmonella ...
14350 Characterization of recombinant diaminopropionate ammonia-lyase from Escherichia coli and Salmonella ...
14351 The tRNA-dependent activation of arginine by arginyl-tRNA synthetase requires inter-domain communication
14352 The tRNA-dependent activation of arginine by arginyl-tRNA synthetase requires inter-domain communication
14353 The tRNA-dependent activation of arginine by arginyl-tRNA synthetase requires inter-domain communication
14354 The tRNA-dependent activation of arginine by arginyl-tRNA synthetase requires inter-domain communication
14355 The tRNA-dependent activation of arginine by arginyl-tRNA synthetase requires inter-domain communication
14356 The tRNA-dependent activation of arginine by arginyl-tRNA synthetase requires inter-domain communication
14357 The tRNA-dependent activation of arginine by arginyl-tRNA synthetase requires inter-domain communication
14358 The tRNA-dependent activation of arginine by arginyl-tRNA synthetase requires inter-domain communication
14359 The tRNA-dependent activation of arginine by arginyl-tRNA synthetase requires inter-domain communication
14360 The tRNA-dependent activation of arginine by arginyl-tRNA synthetase requires inter-domain communication
14361 The tRNA-dependent activation of arginine by arginyl-tRNA synthetase requires inter-domain communication
14362 The tRNA-dependent activation of arginine by arginyl-tRNA synthetase requires inter-domain communication
14363 The tRNA-dependent activation of arginine by arginyl-tRNA synthetase requires inter-domain communication
14364 The tRNA-dependent activation of arginine by arginyl-tRNA synthetase requires inter-domain communication
14365 The tRNA-dependent activation of arginine by arginyl-tRNA synthetase requires inter-domain communication
14366 The tRNA-dependent activation of arginine by arginyl-tRNA synthetase requires inter-domain communication
14367 The tRNA-dependent activation of arginine by arginyl-tRNA synthetase requires inter-domain communication
14368 The tRNA-dependent activation of arginine by arginyl-tRNA synthetase requires inter-domain communication
14369 The tRNA-dependent activation of arginine by arginyl-tRNA synthetase requires inter-domain communication
14370 The tRNA-dependent activation of arginine by arginyl-tRNA synthetase requires inter-domain communication
14371 The tRNA-dependent activation of arginine by arginyl-tRNA synthetase requires inter-domain communication
14372 The tRNA-dependent activation of arginine by arginyl-tRNA synthetase requires inter-domain communication
14373 The tRNA-dependent activation of arginine by arginyl-tRNA synthetase requires inter-domain communication
14374 The tRNA-dependent activation of arginine by arginyl-tRNA synthetase requires inter-domain communication
14375 The tRNA-dependent activation of arginine by arginyl-tRNA synthetase requires inter-domain communication
14376 The tRNA-dependent activation of arginine by arginyl-tRNA synthetase requires inter-domain communication
14377 The tRNA-dependent activation of arginine by arginyl-tRNA synthetase requires inter-domain communication
14378 The tRNA-dependent activation of arginine by arginyl-tRNA synthetase requires inter-domain communication
14379 The tRNA-dependent activation of arginine by arginyl-tRNA synthetase requires inter-domain communication
14380 The tRNA-dependent activation of arginine by arginyl-tRNA synthetase requires inter-domain communication
14381 The tRNA-dependent activation of arginine by arginyl-tRNA synthetase requires inter-domain communication
14382 The tRNA-dependent activation of arginine by arginyl-tRNA synthetase requires inter-domain communication
14383 The tRNA-dependent activation of arginine by arginyl-tRNA synthetase requires inter-domain communication
14384 The tRNA-dependent activation of arginine by arginyl-tRNA synthetase requires inter-domain communication
14385 The tRNA-dependent activation of arginine by arginyl-tRNA synthetase requires inter-domain communication
14386 The tRNA-dependent activation of arginine by arginyl-tRNA synthetase requires inter-domain communication
14387 The tRNA-dependent activation of arginine by arginyl-tRNA synthetase requires inter-domain communication
14388 The tRNA-dependent activation of arginine by arginyl-tRNA synthetase requires inter-domain communication
14389 The tRNA-dependent activation of arginine by arginyl-tRNA synthetase requires inter-domain communication
14390 The tRNA-dependent activation of arginine by arginyl-tRNA synthetase requires inter-domain communication
14391 The tRNA-dependent activation of arginine by arginyl-tRNA synthetase requires inter-domain communication
14392 The tRNA-dependent activation of arginine by arginyl-tRNA synthetase requires inter-domain communication
14393 The tRNA-dependent activation of arginine by arginyl-tRNA synthetase requires inter-domain communication
14394 The tRNA-dependent activation of arginine by arginyl-tRNA synthetase requires inter-domain communication
14395 The tRNA-dependent activation of arginine by arginyl-tRNA synthetase requires inter-domain communication
14396 The tRNA-dependent activation of arginine by arginyl-tRNA synthetase requires inter-domain communication
14397 The tRNA-dependent activation of arginine by arginyl-tRNA synthetase requires inter-domain communication
14398 The tRNA-dependent activation of arginine by arginyl-tRNA synthetase requires inter-domain communication
14399 The tRNA-dependent activation of arginine by arginyl-tRNA synthetase requires inter-domain communication
14400 The tRNA-dependent activation of arginine by arginyl-tRNA synthetase requires inter-domain communication
14401 The tRNA-dependent activation of arginine by arginyl-tRNA synthetase requires inter-domain communication
14402 The tRNA-dependent activation of arginine by arginyl-tRNA synthetase requires inter-domain communication
14403 The tRNA-dependent activation of arginine by arginyl-tRNA synthetase requires inter-domain communication
14404 The tRNA-dependent activation of arginine by arginyl-tRNA synthetase requires inter-domain communication
14405 The tRNA-dependent activation of arginine by arginyl-tRNA synthetase requires inter-domain communication
14406 The tRNA-dependent activation of arginine by arginyl-tRNA synthetase requires inter-domain communication
14407 Ornithine transcarbamylase from Streptococcus faecalis and bovine liver. II. Multiple binding sites for ...
14408 Ornithine transcarbamylase from Streptococcus faecalis and bovine liver. II. Multiple binding sites for ...
14409 Ornithine transcarbamylase from Streptococcus faecalis and bovine liver. II. Multiple binding sites for ...
14410 Ornithine transcarbamylase from Streptococcus faecalis and bovine liver. II. Multiple binding sites for ...
14411 Ornithine transcarbamylase from Streptococcus faecalis and bovine liver. II. Multiple binding sites for ...
14412 Ornithine transcarbamylase from Streptococcus faecalis and bovine liver. II. Multiple binding sites for ...
14413 Ornithine transcarbamylase from Streptococcus faecalis and bovine liver. II. Multiple binding sites for ...
14414 Ornithine transcarbamylase from Streptococcus faecalis and bovine liver. II. Multiple binding sites for ...
14415 Ornithine transcarbamylase from Streptococcus faecalis and bovine liver. II. Multiple binding sites for ...
14416 Ornithine transcarbamylase from Streptococcus faecalis and bovine liver. II. Multiple binding sites for ...
14417 Ornithine transcarbamylase from Streptococcus faecalis and bovine liver. II. Multiple binding sites for ...
14418 Ornithine transcarbamylase from Streptococcus faecalis and bovine liver. II. Multiple binding sites for ...
14419 Ornithine transcarbamylase from Streptococcus faecalis and bovine liver. II. Multiple binding sites for ...
14420 Ornithine transcarbamylase from Streptococcus faecalis and bovine liver. II. Multiple binding sites for ...
14421 Ornithine transcarbamylase from Streptococcus faecalis and bovine liver. II. Multiple binding sites for ...
14422 Ornithine transcarbamylase from Streptococcus faecalis and bovine liver. II. Multiple binding sites for ...
14423 Ornithine transcarbamylase from Streptococcus faecalis and bovine liver. II. Multiple binding sites for ...
14424 Ornithine transcarbamylase from Streptococcus faecalis and bovine liver. II. Multiple binding sites for ...
14425 Ornithine transcarbamylase from Streptococcus faecalis and bovine liver. II. Multiple binding sites for ...
14426 Ornithine transcarbamylase from Streptococcus faecalis and bovine liver. II. Multiple binding sites for ...
14427 Ornithine transcarbamylase from Streptococcus faecalis and bovine liver. II. Multiple binding sites for ...
14428 Ornithine transcarbamylase from Streptococcus faecalis and bovine liver. II. Multiple binding sites for ...
14429 Ornithine transcarbamylase from Streptococcus faecalis and bovine liver. II. Multiple binding sites for ...
14430 Ornithine transcarbamylase from Streptococcus faecalis and bovine liver. II. Multiple binding sites for ...
14431 Ornithine transcarbamylase from Streptococcus faecalis and bovine liver. II. Multiple binding sites for ...
14432 Ornithine transcarbamylase from Streptococcus faecalis and bovine liver. II. Multiple binding sites for ...
14433 Ornithine transcarbamylase from Streptococcus faecalis and bovine liver. II. Multiple binding sites for ...
14434 Ornithine transcarbamylase from Streptococcus faecalis and bovine liver. II. Multiple binding sites for ...
14435 Ornithine transcarbamylase from Streptococcus faecalis and bovine liver. II. Multiple binding sites for ...
14436 Ornithine transcarbamylase from Streptococcus faecalis and bovine liver. II. Multiple binding sites for ...
14437 Ornithine transcarbamylase from Streptococcus faecalis and bovine liver. II. Multiple binding sites for ...
14438 Ornithine transcarbamylase from Streptococcus faecalis and bovine liver. II. Multiple binding sites for ...
14439 Ornithine transcarbamylase from Streptococcus faecalis and bovine liver. II. Multiple binding sites for ...
14440 Ornithine transcarbamylase from Streptococcus faecalis and bovine liver. II. Multiple binding sites for ...
14441 Ornithine transcarbamylase from Streptococcus faecalis and bovine liver. II. Multiple binding sites for ...
14442 Ornithine transcarbamylase from Streptococcus faecalis and bovine liver. II. Multiple binding sites for ...
14443 Ornithine transcarbamylase from Streptococcus faecalis and bovine liver. II. Multiple binding sites for ...
14444 Ornithine transcarbamylase from Streptococcus faecalis and bovine liver. II. Multiple binding sites for ...
14445 Ornithine transcarbamylase from Streptococcus faecalis and bovine liver. II. Multiple binding sites for ...
14446 Ornithine transcarbamylase from Streptococcus faecalis and bovine liver. II. Multiple binding sites for ...
14447 Ornithine transcarbamylase from Streptococcus faecalis and bovine liver. II. Multiple binding sites for ...
14448 Ornithine transcarbamylase from Streptococcus faecalis and bovine liver. II. Multiple binding sites for ...
14449 Ornithine transcarbamylase from Streptococcus faecalis and bovine liver. II. Multiple binding sites for ...
14450 Ornithine transcarbamylase from Streptococcus faecalis and bovine liver. II. Multiple binding sites for ...
14451 Ornithine transcarbamylase from Streptococcus faecalis and bovine liver. II. Multiple binding sites for ...
14452 Ornithine transcarbamylase from Streptococcus faecalis and bovine liver. II. Multiple binding sites for ...
14453 Ornithine transcarbamylase from Streptococcus faecalis and bovine liver. II. Multiple binding sites for ...
14454 Ornithine transcarbamylase from Streptococcus faecalis and bovine liver. II. Multiple binding sites for ...
14455 Ornithine transcarbamylase from Streptococcus faecalis and bovine liver. II. Multiple binding sites for ...
14456 Ornithine transcarbamylase from Streptococcus faecalis and bovine liver. II. Multiple binding sites for ...
14457 Ornithine transcarbamylase from Streptococcus faecalis and bovine liver. II. Multiple binding sites for ...
14458 Ornithine transcarbamylase from Streptococcus faecalis and bovine liver. II. Multiple binding sites for ...
14459 Ornithine transcarbamylase from Streptococcus faecalis and bovine liver. II. Multiple binding sites for ...
14460 Ornithine transcarbamylase from Streptococcus faecalis and bovine liver. II. Multiple binding sites for ...
14461 Ornithine transcarbamylase from Streptococcus faecalis and bovine liver. II. Multiple binding sites for ...
14462 Interaction of D-fructose and fructose 1-phosphate with yeast phosphofructokinase and its influence on ...
14463 Interaction of D-fructose and fructose 1-phosphate with yeast phosphofructokinase and its influence on ...
14464 Interaction of D-fructose and fructose 1-phosphate with yeast phosphofructokinase and its influence on ...
14465 Interaction of D-fructose and fructose 1-phosphate with yeast phosphofructokinase and its influence on ...
14466 Interaction of D-fructose and fructose 1-phosphate with yeast phosphofructokinase and its influence on ...
14467 Interaction of D-fructose and fructose 1-phosphate with yeast phosphofructokinase and its influence on ...
14468 Interaction of D-fructose and fructose 1-phosphate with yeast phosphofructokinase and its influence on ...
14469 Interaction of D-fructose and fructose 1-phosphate with yeast phosphofructokinase and its influence on ...
14470 Interaction of D-fructose and fructose 1-phosphate with yeast phosphofructokinase and its influence on ...
14471 Interaction of D-fructose and fructose 1-phosphate with yeast phosphofructokinase and its influence on ...
14472 Functional characterization of Delta3,Delta2-enoyl-CoA isomerases from rat liver
14473 Functional characterization of Delta3,Delta2-enoyl-CoA isomerases from rat liver
14474 Functional characterization of Delta3,Delta2-enoyl-CoA isomerases from rat liver
14475 Functional characterization of Delta3,Delta2-enoyl-CoA isomerases from rat liver
14476 Functional characterization of Delta3,Delta2-enoyl-CoA isomerases from rat liver
14477 Functional characterization of Delta3,Delta2-enoyl-CoA isomerases from rat liver
14478 Functional characterization of Delta3,Delta2-enoyl-CoA isomerases from rat liver
14479 Functional characterization of Delta3,Delta2-enoyl-CoA isomerases from rat liver
14480 Functional characterization of Delta3,Delta2-enoyl-CoA isomerases from rat liver
14481 Functional characterization of Delta3,Delta2-enoyl-CoA isomerases from rat liver
14482 Functional characterization of Delta3,Delta2-enoyl-CoA isomerases from rat liver
14483 Functional characterization of Delta3,Delta2-enoyl-CoA isomerases from rat liver
14484 Functional characterization of Delta3,Delta2-enoyl-CoA isomerases from rat liver
14485 Functional characterization of Delta3,Delta2-enoyl-CoA isomerases from rat liver
14486 Functional characterization of Delta3,Delta2-enoyl-CoA isomerases from rat liver
14487 Functional characterization of Delta3,Delta2-enoyl-CoA isomerases from rat liver
14488 Functional characterization of Delta3,Delta2-enoyl-CoA isomerases from rat liver
14489 Functional characterization of Delta3,Delta2-enoyl-CoA isomerases from rat liver
14490 Functional characterization of Delta3,Delta2-enoyl-CoA isomerases from rat liver
14491 Functional characterization of Delta3,Delta2-enoyl-CoA isomerases from rat liver
14492 Functional characterization of Delta3,Delta2-enoyl-CoA isomerases from rat liver
14493 Functional characterization of Delta3,Delta2-enoyl-CoA isomerases from rat liver
14494 Functional characterization of Delta3,Delta2-enoyl-CoA isomerases from rat liver
14495 Functional characterization of Delta3,Delta2-enoyl-CoA isomerases from rat liver
14496 Human platelet 6-phosphofructokinase. Relation between inhibition by Mg-ATP2-and cooperativity towards ...
14497 Human platelet 6-phosphofructokinase. Relation between inhibition by Mg-ATP2-and cooperativity towards ...
14498 Human platelet 6-phosphofructokinase. Relation between inhibition by Mg-ATP2-and cooperativity towards ...
14499 Human platelet 6-phosphofructokinase. Relation between inhibition by Mg-ATP2-and cooperativity towards ...
14500 Human platelet 6-phosphofructokinase. Relation between inhibition by Mg-ATP2-and cooperativity towards ...
14501 Human platelet 6-phosphofructokinase. Relation between inhibition by Mg-ATP2-and cooperativity towards ...
14502 Human platelet 6-phosphofructokinase. Relation between inhibition by Mg-ATP2-and cooperativity towards ...
14503 Human platelet 6-phosphofructokinase. Relation between inhibition by Mg-ATP2-and cooperativity towards ...
14504 Human platelet 6-phosphofructokinase. Relation between inhibition by Mg-ATP2-and cooperativity towards ...
14505 Human platelet 6-phosphofructokinase. Relation between inhibition by Mg-ATP2-and cooperativity towards ...
14506 A purification of microsomal glucose-6-phosphatase from human tissue
14507 A purification of microsomal glucose-6-phosphatase from human tissue
14508 Cytosolic and mitochondrial deoxyribonucleotidases: activity with substrate analogs, inhibitors and ...
14509 Cytosolic and mitochondrial deoxyribonucleotidases: activity with substrate analogs, inhibitors and ...
14510 Cytosolic and mitochondrial deoxyribonucleotidases: activity with substrate analogs, inhibitors and ...
14511 Cytosolic and mitochondrial deoxyribonucleotidases: activity with substrate analogs, inhibitors and ...
14512 Cytosolic and mitochondrial deoxyribonucleotidases: activity with substrate analogs, inhibitors and ...
14513 Cytosolic and mitochondrial deoxyribonucleotidases: activity with substrate analogs, inhibitors and ...
14514 Cytosolic and mitochondrial deoxyribonucleotidases: activity with substrate analogs, inhibitors and ...
14515 Cytosolic and mitochondrial deoxyribonucleotidases: activity with substrate analogs, inhibitors and ...
14516 Cytosolic and mitochondrial deoxyribonucleotidases: activity with substrate analogs, inhibitors and ...
14517 Cytosolic and mitochondrial deoxyribonucleotidases: activity with substrate analogs, inhibitors and ...
14518 Cytosolic and mitochondrial deoxyribonucleotidases: activity with substrate analogs, inhibitors and ...
14519 Cytosolic and mitochondrial deoxyribonucleotidases: activity with substrate analogs, inhibitors and ...
14520 Cytosolic and mitochondrial deoxyribonucleotidases: activity with substrate analogs, inhibitors and ...
14521 Cytosolic and mitochondrial deoxyribonucleotidases: activity with substrate analogs, inhibitors and ...
14522 Cytosolic and mitochondrial deoxyribonucleotidases: activity with substrate analogs, inhibitors and ...
14523 Cytosolic and mitochondrial deoxyribonucleotidases: activity with substrate analogs, inhibitors and ...
14524 Cytosolic and mitochondrial deoxyribonucleotidases: activity with substrate analogs, inhibitors and ...
14525 Cytosolic and mitochondrial deoxyribonucleotidases: activity with substrate analogs, inhibitors and ...
14526 Cytosolic and mitochondrial deoxyribonucleotidases: activity with substrate analogs, inhibitors and ...
14527 Reactivity and metal-dependent stereospecificity of the phosphorothioate analogs of ADP and ATP and reactivity ...
14528 Reactivity and metal-dependent stereospecificity of the phosphorothioate analogs of ADP and ATP and reactivity ...
14529 Reactivity and metal-dependent stereospecificity of the phosphorothioate analogs of ADP and ATP and reactivity ...
14530 Reactivity and metal-dependent stereospecificity of the phosphorothioate analogs of ADP and ATP and reactivity ...
14531 Reactivity and metal-dependent stereospecificity of the phosphorothioate analogs of ADP and ATP and reactivity ...
14532 Reactivity and metal-dependent stereospecificity of the phosphorothioate analogs of ADP and ATP and reactivity ...
14533 Reactivity and metal-dependent stereospecificity of the phosphorothioate analogs of ADP and ATP and reactivity ...
14534 Reactivity and metal-dependent stereospecificity of the phosphorothioate analogs of ADP and ATP and reactivity ...
14535 Reactivity and metal-dependent stereospecificity of the phosphorothioate analogs of ADP and ATP and reactivity ...
14536 Reactivity and metal-dependent stereospecificity of the phosphorothioate analogs of ADP and ATP and reactivity ...
14537 Reactivity and metal-dependent stereospecificity of the phosphorothioate analogs of ADP and ATP and reactivity ...
14538 Reactivity and metal-dependent stereospecificity of the phosphorothioate analogs of ADP and ATP and reactivity ...
14539 Reactivity and metal-dependent stereospecificity of the phosphorothioate analogs of ADP and ATP and reactivity ...
14540 Reactivity and metal-dependent stereospecificity of the phosphorothioate analogs of ADP and ATP and reactivity ...
14541 Reactivity and metal-dependent stereospecificity of the phosphorothioate analogs of ADP and ATP and reactivity ...
14542 Reactivity and metal-dependent stereospecificity of the phosphorothioate analogs of ADP and ATP and reactivity ...
14543 Reactivity and metal-dependent stereospecificity of the phosphorothioate analogs of ADP and ATP and reactivity ...
14544 Comparison of the stability and substrate specificity of purified peroxisomal 3-oxoacyl-CoA thiolases A and B ...
14545 Comparison of the stability and substrate specificity of purified peroxisomal 3-oxoacyl-CoA thiolases A and B ...
14546 Comparison of the stability and substrate specificity of purified peroxisomal 3-oxoacyl-CoA thiolases A and B ...
14547 Comparison of the stability and substrate specificity of purified peroxisomal 3-oxoacyl-CoA thiolases A and B ...
14548 Comparison of the stability and substrate specificity of purified peroxisomal 3-oxoacyl-CoA thiolases A and B ...
14549 Comparison of the stability and substrate specificity of purified peroxisomal 3-oxoacyl-CoA thiolases A and B ...
14550 Comparison of the stability and substrate specificity of purified peroxisomal 3-oxoacyl-CoA thiolases A and B ...
14551 Comparison of the stability and substrate specificity of purified peroxisomal 3-oxoacyl-CoA thiolases A and B ...
14552 Mutational study on alphaGln90 of Fe-type nitrile hydratase from Rhodococcus sp. N771
14553 Mutational study on alphaGln90 of Fe-type nitrile hydratase from Rhodococcus sp. N771
14554 Mutational study on alphaGln90 of Fe-type nitrile hydratase from Rhodococcus sp. N771
14555 Mutational study on alphaGln90 of Fe-type nitrile hydratase from Rhodococcus sp. N771
14556 Mutational study on alphaGln90 of Fe-type nitrile hydratase from Rhodococcus sp. N771
14557 Mutational study on alphaGln90 of Fe-type nitrile hydratase from Rhodococcus sp. N771
14558 Mutational study on alphaGln90 of Fe-type nitrile hydratase from Rhodococcus sp. N771
14559 Mutational study on alphaGln90 of Fe-type nitrile hydratase from Rhodococcus sp. N771
14560 Substrate specificities of 3-oxoacyl-CoA thiolase A and sterol carrier protein 2/3-oxoacyl-CoA thiolase ...
14561 Substrate specificities of 3-oxoacyl-CoA thiolase A and sterol carrier protein 2/3-oxoacyl-CoA thiolase ...
14562 Substrate specificities of 3-oxoacyl-CoA thiolase A and sterol carrier protein 2/3-oxoacyl-CoA thiolase ...
14563 Substrate specificities of 3-oxoacyl-CoA thiolase A and sterol carrier protein 2/3-oxoacyl-CoA thiolase ...
14564 Substrate specificities of 3-oxoacyl-CoA thiolase A and sterol carrier protein 2/3-oxoacyl-CoA thiolase ...
14565 Substrate specificities of 3-oxoacyl-CoA thiolase A and sterol carrier protein 2/3-oxoacyl-CoA thiolase ...
14566 Substrate specificities of 3-oxoacyl-CoA thiolase A and sterol carrier protein 2/3-oxoacyl-CoA thiolase ...
14567 Substrate specificities of 3-oxoacyl-CoA thiolase A and sterol carrier protein 2/3-oxoacyl-CoA thiolase ...
14568 Substrate specificities of 3-oxoacyl-CoA thiolase A and sterol carrier protein 2/3-oxoacyl-CoA thiolase ...
14569 Substrate specificities of 3-oxoacyl-CoA thiolase A and sterol carrier protein 2/3-oxoacyl-CoA thiolase ...
14570 Substrate specificities of 3-oxoacyl-CoA thiolase A and sterol carrier protein 2/3-oxoacyl-CoA thiolase ...
14571 Substrate specificities of 3-oxoacyl-CoA thiolase A and sterol carrier protein 2/3-oxoacyl-CoA thiolase ...
14572 Substrate specificities of 3-oxoacyl-CoA thiolase A and sterol carrier protein 2/3-oxoacyl-CoA thiolase ...
14573 Substrate specificities of 3-oxoacyl-CoA thiolase A and sterol carrier protein 2/3-oxoacyl-CoA thiolase ...
14574 Substrate specificities of 3-oxoacyl-CoA thiolase A and sterol carrier protein 2/3-oxoacyl-CoA thiolase ...
14575 Substrate specificities of 3-oxoacyl-CoA thiolase A and sterol carrier protein 2/3-oxoacyl-CoA thiolase ...
14576 Substrate specificities of 3-oxoacyl-CoA thiolase A and sterol carrier protein 2/3-oxoacyl-CoA thiolase ...
14577 Substrate specificities of 3-oxoacyl-CoA thiolase A and sterol carrier protein 2/3-oxoacyl-CoA thiolase ...
14578 Substrate specificities of 3-oxoacyl-CoA thiolase A and sterol carrier protein 2/3-oxoacyl-CoA thiolase ...
14579 Characterization of human UMP/CMP kinase and its phosphorylation of D- and L-form deoxycytidine analogue ...
14580 Characterization of human UMP/CMP kinase and its phosphorylation of D- and L-form deoxycytidine analogue ...
14581 Characterization of human UMP/CMP kinase and its phosphorylation of D- and L-form deoxycytidine analogue ...
14582 Characterization of human UMP/CMP kinase and its phosphorylation of D- and L-form deoxycytidine analogue ...
14583 Characterization of human UMP/CMP kinase and its phosphorylation of D- and L-form deoxycytidine analogue ...
14584 Characterization of human UMP/CMP kinase and its phosphorylation of D- and L-form deoxycytidine analogue ...
14585 Characterization of human UMP/CMP kinase and its phosphorylation of D- and L-form deoxycytidine analogue ...
14586 Characterization of human UMP/CMP kinase and its phosphorylation of D- and L-form deoxycytidine analogue ...
14587 Characterization of human UMP/CMP kinase and its phosphorylation of D- and L-form deoxycytidine analogue ...
14588 Characterization of human UMP/CMP kinase and its phosphorylation of D- and L-form deoxycytidine analogue ...
14589 Characterization of human UMP/CMP kinase and its phosphorylation of D- and L-form deoxycytidine analogue ...
14590 Characterization of human UMP/CMP kinase and its phosphorylation of D- and L-form deoxycytidine analogue ...
14591 Characterization of human UMP/CMP kinase and its phosphorylation of D- and L-form deoxycytidine analogue ...
14592 Characterization of human UMP/CMP kinase and its phosphorylation of D- and L-form deoxycytidine analogue ...
14593 Characterization of human UMP/CMP kinase and its phosphorylation of D- and L-form deoxycytidine analogue ...
14594 Characterization of human UMP/CMP kinase and its phosphorylation of D- and L-form deoxycytidine analogue ...
14595 Characterization of human UMP/CMP kinase and its phosphorylation of D- and L-form deoxycytidine analogue ...
14596 Characterization of human UMP/CMP kinase and its phosphorylation of D- and L-form deoxycytidine analogue ...
14597 Properties of an affinity-column-purified human deoxycytidylate deaminase
14598 Properties of an affinity-column-purified human deoxycytidylate deaminase
14599 Properties of an affinity-column-purified human deoxycytidylate deaminase
14600 Properties of an affinity-column-purified human deoxycytidylate deaminase
14601 Rat dihydroorotate dehydrogenase: isolation of the recombinant enzyme from mitochondria of insect cells
14602 Rat dihydroorotate dehydrogenase: isolation of the recombinant enzyme from mitochondria of insect cells
14603 Rat dihydroorotate dehydrogenase: isolation of the recombinant enzyme from mitochondria of insect cells
14604 Rat dihydroorotate dehydrogenase: isolation of the recombinant enzyme from mitochondria of insect cells
14605 Rat dihydroorotate dehydrogenase: isolation of the recombinant enzyme from mitochondria of insect cells
14606 Rat dihydroorotate dehydrogenase: isolation of the recombinant enzyme from mitochondria of insect cells
14607 Rat dihydroorotate dehydrogenase: isolation of the recombinant enzyme from mitochondria of insect cells
14608 Rat dihydroorotate dehydrogenase: isolation of the recombinant enzyme from mitochondria of insect cells
14609 Identification and characterisation of human aldose 1-epimerase
14610 Identification and characterisation of human aldose 1-epimerase
14611 Identification and characterisation of human aldose 1-epimerase
14612 Identification and characterisation of human aldose 1-epimerase
14613 Identification and characterisation of human aldose 1-epimerase
14614 Identification and characterisation of human aldose 1-epimerase
14615 Identification and characterisation of human aldose 1-epimerase
14637 Assay method for Escherichia coli photolyase activity using single-strand cis-syn cyclobutane pyrimidine dimer ...
14638 Engineering the active center of the 6-phospho-beta-galactosidase from Lactococcus lactis
14639 Engineering the active center of the 6-phospho-beta-galactosidase from Lactococcus lactis
14640 Engineering the active center of the 6-phospho-beta-galactosidase from Lactococcus lactis
14641 Engineering the active center of the 6-phospho-beta-galactosidase from Lactococcus lactis
14642 Engineering the active center of the 6-phospho-beta-galactosidase from Lactococcus lactis
14643 Engineering the active center of the 6-phospho-beta-galactosidase from Lactococcus lactis
14644 Engineering the active center of the 6-phospho-beta-galactosidase from Lactococcus lactis
14645 Engineering the active center of the 6-phospho-beta-galactosidase from Lactococcus lactis
14646 Engineering the active center of the 6-phospho-beta-galactosidase from Lactococcus lactis
14647 Engineering the active center of the 6-phospho-beta-galactosidase from Lactococcus lactis
14648 Engineering the active center of the 6-phospho-beta-galactosidase from Lactococcus lactis
14649 Cloning and characterization of dipeptidyl peptidase 10, a new member of an emerging subgroup of serine ...
14650 Cloning and characterization of dipeptidyl peptidase 10, a new member of an emerging subgroup of serine ...
14662 Activation of Thermus phosphofructokinase by monovalent cations
14663 Activation of Thermus phosphofructokinase by monovalent cations
14664 Site-directed mutagenesis of mouse dihydrofolate reductase. Mutants with increased resistance to methotrexate ...
14665 Site-directed mutagenesis of mouse dihydrofolate reductase. Mutants with increased resistance to methotrexate ...
14666 Site-directed mutagenesis of mouse dihydrofolate reductase. Mutants with increased resistance to methotrexate ...
14667 Site-directed mutagenesis of mouse dihydrofolate reductase. Mutants with increased resistance to methotrexate ...
14668 Site-directed mutagenesis of mouse dihydrofolate reductase. Mutants with increased resistance to methotrexate ...
14669 Site-directed mutagenesis of mouse dihydrofolate reductase. Mutants with increased resistance to methotrexate ...
14670 Site-directed mutagenesis of mouse dihydrofolate reductase. Mutants with increased resistance to methotrexate ...
14671 Site-directed mutagenesis of mouse dihydrofolate reductase. Mutants with increased resistance to methotrexate ...
14672 Site-directed mutagenesis of mouse dihydrofolate reductase. Mutants with increased resistance to methotrexate ...
14673 Site-directed mutagenesis of mouse dihydrofolate reductase. Mutants with increased resistance to methotrexate ...
14674 Site-directed mutagenesis of mouse dihydrofolate reductase. Mutants with increased resistance to methotrexate ...
14675 Site-directed mutagenesis of mouse dihydrofolate reductase. Mutants with increased resistance to methotrexate ...
14676 Site-directed mutagenesis of mouse dihydrofolate reductase. Mutants with increased resistance to methotrexate ...
14677 Site-directed mutagenesis of mouse dihydrofolate reductase. Mutants with increased resistance to methotrexate ...
14678 Site-directed mutagenesis of mouse dihydrofolate reductase. Mutants with increased resistance to methotrexate ...
14679 Site-directed mutagenesis of mouse dihydrofolate reductase. Mutants with increased resistance to methotrexate ...
14680 Site-directed mutagenesis of mouse dihydrofolate reductase. Mutants with increased resistance to methotrexate ...
14681 Site-directed mutagenesis of mouse dihydrofolate reductase. Mutants with increased resistance to methotrexate ...
14682 Site-directed mutagenesis of mouse dihydrofolate reductase. Mutants with increased resistance to methotrexate ...
14683 Site-directed mutagenesis of mouse dihydrofolate reductase. Mutants with increased resistance to methotrexate ...
14684 Site-directed mutagenesis of mouse dihydrofolate reductase. Mutants with increased resistance to methotrexate ...
14685 Site-directed mutagenesis of mouse dihydrofolate reductase. Mutants with increased resistance to methotrexate ...
14686 Site-directed mutagenesis of mouse dihydrofolate reductase. Mutants with increased resistance to methotrexate ...
14687 Site-directed mutagenesis of mouse dihydrofolate reductase. Mutants with increased resistance to methotrexate ...
14688 Site-directed mutagenesis of mouse dihydrofolate reductase. Mutants with increased resistance to methotrexate ...
14689 Site-directed mutagenesis of mouse dihydrofolate reductase. Mutants with increased resistance to methotrexate ...
14690 Site-directed mutagenesis of mouse dihydrofolate reductase. Mutants with increased resistance to methotrexate ...
14691 Site-directed mutagenesis of mouse dihydrofolate reductase. Mutants with increased resistance to methotrexate ...
14692 Site-directed mutagenesis of mouse dihydrofolate reductase. Mutants with increased resistance to methotrexate ...
14693 Site-directed mutagenesis of mouse dihydrofolate reductase. Mutants with increased resistance to methotrexate ...
14694 Site-directed mutagenesis of mouse dihydrofolate reductase. Mutants with increased resistance to methotrexate ...
14695 Site-directed mutagenesis of mouse dihydrofolate reductase. Mutants with increased resistance to methotrexate ...
14696 Site-directed mutagenesis of mouse dihydrofolate reductase. Mutants with increased resistance to methotrexate ...
14697 Site-directed mutagenesis of mouse dihydrofolate reductase. Mutants with increased resistance to methotrexate ...
14698 Human hereditary glutathione synthetase deficiency: kinetic properties of mutant enzymes
14699 Human hereditary glutathione synthetase deficiency: kinetic properties of mutant enzymes
14700 Human hereditary glutathione synthetase deficiency: kinetic properties of mutant enzymes
14701 Human hereditary glutathione synthetase deficiency: kinetic properties of mutant enzymes
14702 Human hereditary glutathione synthetase deficiency: kinetic properties of mutant enzymes
14703 Human hereditary glutathione synthetase deficiency: kinetic properties of mutant enzymes
14704 Human hereditary glutathione synthetase deficiency: kinetic properties of mutant enzymes
14705 Human hereditary glutathione synthetase deficiency: kinetic properties of mutant enzymes
14706 Human hereditary glutathione synthetase deficiency: kinetic properties of mutant enzymes
14707 Human hereditary glutathione synthetase deficiency: kinetic properties of mutant enzymes
14708 Human hereditary glutathione synthetase deficiency: kinetic properties of mutant enzymes
14709 Human hereditary glutathione synthetase deficiency: kinetic properties of mutant enzymes
14710 Human hereditary glutathione synthetase deficiency: kinetic properties of mutant enzymes
14711 Human hereditary glutathione synthetase deficiency: kinetic properties of mutant enzymes
14712 Human hereditary glutathione synthetase deficiency: kinetic properties of mutant enzymes
14713 Human hereditary glutathione synthetase deficiency: kinetic properties of mutant enzymes
14714 Human hereditary glutathione synthetase deficiency: kinetic properties of mutant enzymes
14715 Human hereditary glutathione synthetase deficiency: kinetic properties of mutant enzymes
14716 Human hereditary glutathione synthetase deficiency: kinetic properties of mutant enzymes
14717 Human hereditary glutathione synthetase deficiency: kinetic properties of mutant enzymes
14718 Human hereditary glutathione synthetase deficiency: kinetic properties of mutant enzymes
14719 Human hereditary glutathione synthetase deficiency: kinetic properties of mutant enzymes
14720 Human hereditary glutathione synthetase deficiency: kinetic properties of mutant enzymes
14721 Human hereditary glutathione synthetase deficiency: kinetic properties of mutant enzymes
14724 A defined subset of adenylyl cyclases is regulated by bicarbonate ion
14725 A defined subset of adenylyl cyclases is regulated by bicarbonate ion
14726 Broad substrate stereospecificity of the Mycobacterium tuberculosis 7-keto-8-aminopelargonic acid synthase: ...
14727 Broad substrate stereospecificity of the Mycobacterium tuberculosis 7-keto-8-aminopelargonic acid synthase: ...
14728 Broad substrate stereospecificity of the Mycobacterium tuberculosis 7-keto-8-aminopelargonic acid synthase: ...
14729 Broad substrate stereospecificity of the Mycobacterium tuberculosis 7-keto-8-aminopelargonic acid synthase: ...
14730 Broad substrate stereospecificity of the Mycobacterium tuberculosis 7-keto-8-aminopelargonic acid synthase: ...
14731 Nucleotide specificity of pyruvate kinase and phosphoenolpyruvate carboxykinase
14732 Nucleotide specificity of pyruvate kinase and phosphoenolpyruvate carboxykinase
14733 Nucleotide specificity of pyruvate kinase and phosphoenolpyruvate carboxykinase
14734 Nucleotide specificity of pyruvate kinase and phosphoenolpyruvate carboxykinase
14735 Nucleotide specificity of pyruvate kinase and phosphoenolpyruvate carboxykinase
14736 Nucleotide specificity of pyruvate kinase and phosphoenolpyruvate carboxykinase
14737 Nucleotide specificity of pyruvate kinase and phosphoenolpyruvate carboxykinase
14738 Nucleotide specificity of pyruvate kinase and phosphoenolpyruvate carboxykinase
14739 Nucleotide specificity of pyruvate kinase and phosphoenolpyruvate carboxykinase
14740 Nucleotide specificity of pyruvate kinase and phosphoenolpyruvate carboxykinase
14741 Nucleotide specificity of pyruvate kinase and phosphoenolpyruvate carboxykinase
14742 Nucleotide specificity of pyruvate kinase and phosphoenolpyruvate carboxykinase
14743 Nucleotide specificity of pyruvate kinase and phosphoenolpyruvate carboxykinase
14744 Nucleotide specificity of pyruvate kinase and phosphoenolpyruvate carboxykinase
14745 Nucleotide specificity of pyruvate kinase and phosphoenolpyruvate carboxykinase
14746 Nucleotide specificity of pyruvate kinase and phosphoenolpyruvate carboxykinase
14747 Nucleotide specificity of pyruvate kinase and phosphoenolpyruvate carboxykinase
14748 Nucleotide specificity of pyruvate kinase and phosphoenolpyruvate carboxykinase
14749 Nucleotide specificity of pyruvate kinase and phosphoenolpyruvate carboxykinase
14750 Nucleotide specificity of pyruvate kinase and phosphoenolpyruvate carboxykinase
14751 Nucleotide specificity of pyruvate kinase and phosphoenolpyruvate carboxykinase
14752 The effect of monovalent and divalent cations on the activity of Streptococcus lactis C10 pyruvate kinase
14753 The effect of monovalent and divalent cations on the activity of Streptococcus lactis C10 pyruvate kinase
14754 The effect of monovalent and divalent cations on the activity of Streptococcus lactis C10 pyruvate kinase
14755 The effect of monovalent and divalent cations on the activity of Streptococcus lactis C10 pyruvate kinase
14756 The effect of monovalent and divalent cations on the activity of Streptococcus lactis C10 pyruvate kinase
14757 The effect of monovalent and divalent cations on the activity of Streptococcus lactis C10 pyruvate kinase
14758 The effect of monovalent and divalent cations on the activity of Streptococcus lactis C10 pyruvate kinase
14759 The effect of monovalent and divalent cations on the activity of Streptococcus lactis C10 pyruvate kinase
14760 The effect of monovalent and divalent cations on the activity of Streptococcus lactis C10 pyruvate kinase
14761 The effect of monovalent and divalent cations on the activity of Streptococcus lactis C10 pyruvate kinase
14762 The effect of monovalent and divalent cations on the activity of Streptococcus lactis C10 pyruvate kinase
14763 The effect of monovalent and divalent cations on the activity of Streptococcus lactis C10 pyruvate kinase
14764 The effect of monovalent and divalent cations on the activity of Streptococcus lactis C10 pyruvate kinase
14765 The effect of monovalent and divalent cations on the activity of Streptococcus lactis C10 pyruvate kinase
14766 The effect of monovalent and divalent cations on the activity of Streptococcus lactis C10 pyruvate kinase
14767 The effect of monovalent and divalent cations on the activity of Streptococcus lactis C10 pyruvate kinase
14768 The effect of monovalent and divalent cations on the activity of Streptococcus lactis C10 pyruvate kinase
14769 The effect of monovalent and divalent cations on the activity of Streptococcus lactis C10 pyruvate kinase
14770 The effect of monovalent and divalent cations on the activity of Streptococcus lactis C10 pyruvate kinase
14771 The effect of monovalent and divalent cations on the activity of Streptococcus lactis C10 pyruvate kinase
14772 The effect of monovalent and divalent cations on the activity of Streptococcus lactis C10 pyruvate kinase
14773 The effect of monovalent and divalent cations on the activity of Streptococcus lactis C10 pyruvate kinase
14774 The effect of monovalent and divalent cations on the activity of Streptococcus lactis C10 pyruvate kinase
14775 The effect of monovalent and divalent cations on the activity of Streptococcus lactis C10 pyruvate kinase
14776 The effect of monovalent and divalent cations on the activity of Streptococcus lactis C10 pyruvate kinase
14777 The effect of monovalent and divalent cations on the activity of Streptococcus lactis C10 pyruvate kinase
14778 The effect of monovalent and divalent cations on the activity of Streptococcus lactis C10 pyruvate kinase
14779 The effect of monovalent and divalent cations on the activity of Streptococcus lactis C10 pyruvate kinase
14780 The effect of monovalent and divalent cations on the activity of Streptococcus lactis C10 pyruvate kinase
14781 Enzymatic characterization of a prokaryotic urea carboxylase
14782 Enzymatic characterization of a prokaryotic urea carboxylase
14783 Enzymatic characterization of a prokaryotic urea carboxylase
14784 Enzymatic characterization of a prokaryotic urea carboxylase
14785 Functional analysis of disease-causing mutations in human galactokinase
14786 Functional analysis of disease-causing mutations in human galactokinase
14787 Functional analysis of disease-causing mutations in human galactokinase
14788 Functional analysis of disease-causing mutations in human galactokinase
14789 Functional analysis of disease-causing mutations in human galactokinase
14790 Functional analysis of disease-causing mutations in human galactokinase
14791 Functional analysis of disease-causing mutations in human galactokinase
14792 Functional analysis of disease-causing mutations in human galactokinase
14793 Mutants of Escherichia coli defective in membrane phospholipid synthesis. Properties of wild type and Km ...
14794 Mutants of Escherichia coli defective in membrane phospholipid synthesis. Properties of wild type and Km ...
14795 Mutants of Escherichia coli defective in membrane phospholipid synthesis. Properties of wild type and Km ...
14796 Mutants of Escherichia coli defective in membrane phospholipid synthesis. Properties of wild type and Km ...
14797 Mutants of Escherichia coli defective in membrane phospholipid synthesis. Properties of wild type and Km ...
14798 Mutants of Escherichia coli defective in membrane phospholipid synthesis. Properties of wild type and Km ...
14799 Mutants of Escherichia coli defective in membrane phospholipid synthesis. Properties of wild type and Km ...
14800 Mutants of Escherichia coli defective in membrane phospholipid synthesis. Properties of wild type and Km ...
14801 Mutants of Escherichia coli defective in membrane phospholipid synthesis. Properties of wild type and Km ...
14802 Mutants of Escherichia coli defective in membrane phospholipid synthesis. Properties of wild type and Km ...
14803 Mutants of Escherichia coli defective in membrane phospholipid synthesis. Properties of wild type and Km ...
14804 Mutants of Escherichia coli defective in membrane phospholipid synthesis. Properties of wild type and Km ...
14805 Mutants of Escherichia coli defective in membrane phospholipid synthesis. Properties of wild type and Km ...
14806 Mutants of Escherichia coli defective in membrane phospholipid synthesis. Properties of wild type and Km ...
14807 Mutants of Escherichia coli defective in membrane phospholipid synthesis. Properties of wild type and Km ...
14808 Conserved cysteine residues of histidinol dehydrogenase are not involved in catalysis. Novel chemistry ...
14809 Conserved cysteine residues of histidinol dehydrogenase are not involved in catalysis. Novel chemistry ...
14810 Conserved cysteine residues of histidinol dehydrogenase are not involved in catalysis. Novel chemistry ...
14811 Conserved cysteine residues of histidinol dehydrogenase are not involved in catalysis. Novel chemistry ...
14812 Conserved cysteine residues of histidinol dehydrogenase are not involved in catalysis. Novel chemistry ...
14813 Conserved cysteine residues of histidinol dehydrogenase are not involved in catalysis. Novel chemistry ...
14814 Dominant Negative Role of the Glutamic Acid Residue Conserved in the Pyruvate Kinase M1 Isozyme in the ...
14815 Dominant Negative Role of the Glutamic Acid Residue Conserved in the Pyruvate Kinase M1 Isozyme in the ...
14816 Dominant Negative Role of the Glutamic Acid Residue Conserved in the Pyruvate Kinase M1 Isozyme in the ...
14817 Dominant Negative Role of the Glutamic Acid Residue Conserved in the Pyruvate Kinase M1 Isozyme in the ...
14818 Dominant Negative Role of the Glutamic Acid Residue Conserved in the Pyruvate Kinase M1 Isozyme in the ...
14819 Dominant Negative Role of the Glutamic Acid Residue Conserved in the Pyruvate Kinase M1 Isozyme in the ...
14820 Dominant Negative Role of the Glutamic Acid Residue Conserved in the Pyruvate Kinase M1 Isozyme in the ...
14821 Dominant Negative Role of the Glutamic Acid Residue Conserved in the Pyruvate Kinase M1 Isozyme in the ...
14822 Dominant Negative Role of the Glutamic Acid Residue Conserved in the Pyruvate Kinase M1 Isozyme in the ...
14823 Dominant Negative Role of the Glutamic Acid Residue Conserved in the Pyruvate Kinase M1 Isozyme in the ...
14824 Dominant Negative Role of the Glutamic Acid Residue Conserved in the Pyruvate Kinase M1 Isozyme in the ...
14825 Dominant Negative Role of the Glutamic Acid Residue Conserved in the Pyruvate Kinase M1 Isozyme in the ...
14826 Dominant Negative Role of the Glutamic Acid Residue Conserved in the Pyruvate Kinase M1 Isozyme in the ...
14827 Dominant Negative Role of the Glutamic Acid Residue Conserved in the Pyruvate Kinase M1 Isozyme in the ...
14828 Dominant Negative Role of the Glutamic Acid Residue Conserved in the Pyruvate Kinase M1 Isozyme in the ...
14829 Dominant Negative Role of the Glutamic Acid Residue Conserved in the Pyruvate Kinase M1 Isozyme in the ...
14830 Dominant Negative Role of the Glutamic Acid Residue Conserved in the Pyruvate Kinase M1 Isozyme in the ...
14831 Dominant Negative Role of the Glutamic Acid Residue Conserved in the Pyruvate Kinase M1 Isozyme in the ...
14832 Dominant Negative Role of the Glutamic Acid Residue Conserved in the Pyruvate Kinase M1 Isozyme in the ...
14833 Dominant Negative Role of the Glutamic Acid Residue Conserved in the Pyruvate Kinase M1 Isozyme in the ...
14834 Dominant Negative Role of the Glutamic Acid Residue Conserved in the Pyruvate Kinase M1 Isozyme in the ...
14835 Dominant Negative Role of the Glutamic Acid Residue Conserved in the Pyruvate Kinase M1 Isozyme in the ...
14836 Dominant Negative Role of the Glutamic Acid Residue Conserved in the Pyruvate Kinase M1 Isozyme in the ...
14837 Dominant Negative Role of the Glutamic Acid Residue Conserved in the Pyruvate Kinase M1 Isozyme in the ...
14838 IS981-mediated adaptive evolution recovers lactate production by ldhB transcription activation in a lactate ...
14839 IS981-mediated adaptive evolution recovers lactate production by ldhB transcription activation in a lactate ...
14840 IS981-mediated adaptive evolution recovers lactate production by ldhB transcription activation in a lactate ...
14841 IS981-mediated adaptive evolution recovers lactate production by ldhB transcription activation in a lactate ...
14842 IS981-mediated adaptive evolution recovers lactate production by ldhB transcription activation in a lactate ...
14843 IS981-mediated adaptive evolution recovers lactate production by ldhB transcription activation in a lactate ...
14844 Human cytosolic adenylate kinase allelozymes; purification and characterization
14845 Human cytosolic adenylate kinase allelozymes; purification and characterization
14846 Human cytosolic adenylate kinase allelozymes; purification and characterization
14847 Human cytosolic adenylate kinase allelozymes; purification and characterization
14848 Activation of yeast enolase by Cd(II)
14849 Activation of yeast enolase by Cd(II)
14850 Activation of yeast enolase by Cd(II)
14851 Activation of yeast enolase by Cd(II)
14852 Activation of yeast enolase by Cd(II)
14853 Activation of yeast enolase by Cd(II)
14854 Activation of yeast enolase by Cd(II)
14855 Activation of yeast enolase by Cd(II)
14862 Structural function of residue-209 in coumarin 7-hydroxylase (P450coh). Enzyme-kinetic studies and ...
14863 Structural function of residue-209 in coumarin 7-hydroxylase (P450coh). Enzyme-kinetic studies and ...
14864 Structural function of residue-209 in coumarin 7-hydroxylase (P450coh). Enzyme-kinetic studies and ...
14865 Structural function of residue-209 in coumarin 7-hydroxylase (P450coh). Enzyme-kinetic studies and ...
14866 Structural function of residue-209 in coumarin 7-hydroxylase (P450coh). Enzyme-kinetic studies and ...
14867 Structural function of residue-209 in coumarin 7-hydroxylase (P450coh). Enzyme-kinetic studies and ...
14868 Structural function of residue-209 in coumarin 7-hydroxylase (P450coh). Enzyme-kinetic studies and ...
14869 Structural function of residue-209 in coumarin 7-hydroxylase (P450coh). Enzyme-kinetic studies and ...
14870 Structural function of residue-209 in coumarin 7-hydroxylase (P450coh). Enzyme-kinetic studies and ...
14871 Structural function of residue-209 in coumarin 7-hydroxylase (P450coh). Enzyme-kinetic studies and ...
14872 Structural function of residue-209 in coumarin 7-hydroxylase (P450coh). Enzyme-kinetic studies and ...
14873 Structural function of residue-209 in coumarin 7-hydroxylase (P450coh). Enzyme-kinetic studies and ...
14874 Structural function of residue-209 in coumarin 7-hydroxylase (P450coh). Enzyme-kinetic studies and ...
14875 Structural function of residue-209 in coumarin 7-hydroxylase (P450coh). Enzyme-kinetic studies and ...
14876 Structural function of residue-209 in coumarin 7-hydroxylase (P450coh). Enzyme-kinetic studies and ...
14877 Structural function of residue-209 in coumarin 7-hydroxylase (P450coh). Enzyme-kinetic studies and ...
14878 Structural function of residue-209 in coumarin 7-hydroxylase (P450coh). Enzyme-kinetic studies and ...
14879 Structural function of residue-209 in coumarin 7-hydroxylase (P450coh). Enzyme-kinetic studies and ...
14880 Structural function of residue-209 in coumarin 7-hydroxylase (P450coh). Enzyme-kinetic studies and ...
14881 Functional characterization of an aminotransferase required for pyoverdine siderophore biosynthesis in ...
14882 Functional characterization of an aminotransferase required for pyoverdine siderophore biosynthesis in ...
14883 Structural and functional properties of aldose xylose reductase from the D-xylose-metabolizing yeast Candida ...
14884 Structural and functional properties of aldose xylose reductase from the D-xylose-metabolizing yeast Candida ...
14885 Structural and functional properties of aldose xylose reductase from the D-xylose-metabolizing yeast Candida ...
14886 Structural and functional properties of aldose xylose reductase from the D-xylose-metabolizing yeast Candida ...
14887 Identification of an Archaeal 2-Hydroxy Acid Dehydrogenase Catalyzing Reactions Involved in Coenzyme ...
14888 Identification of an Archaeal 2-Hydroxy Acid Dehydrogenase Catalyzing Reactions Involved in Coenzyme ...
14889 Identification of an Archaeal 2-Hydroxy Acid Dehydrogenase Catalyzing Reactions Involved in Coenzyme ...
14890 Identification of an Archaeal 2-Hydroxy Acid Dehydrogenase Catalyzing Reactions Involved in Coenzyme ...
14891 Identification of an Archaeal 2-Hydroxy Acid Dehydrogenase Catalyzing Reactions Involved in Coenzyme ...
14892 Identification of an Archaeal 2-Hydroxy Acid Dehydrogenase Catalyzing Reactions Involved in Coenzyme ...
14893 Identification of an Archaeal 2-Hydroxy Acid Dehydrogenase Catalyzing Reactions Involved in Coenzyme ...
14894 Identification of an Archaeal 2-Hydroxy Acid Dehydrogenase Catalyzing Reactions Involved in Coenzyme ...
14895 Identification of an Archaeal 2-Hydroxy Acid Dehydrogenase Catalyzing Reactions Involved in Coenzyme ...
14896 Identification of an Archaeal 2-Hydroxy Acid Dehydrogenase Catalyzing Reactions Involved in Coenzyme ...
14897 Identification of an Archaeal 2-Hydroxy Acid Dehydrogenase Catalyzing Reactions Involved in Coenzyme ...
14898 Identification of an Archaeal 2-Hydroxy Acid Dehydrogenase Catalyzing Reactions Involved in Coenzyme ...
14899 Identification of an Archaeal 2-Hydroxy Acid Dehydrogenase Catalyzing Reactions Involved in Coenzyme ...
14900 Identification of an Archaeal 2-Hydroxy Acid Dehydrogenase Catalyzing Reactions Involved in Coenzyme ...
14901 Identification of an Archaeal 2-Hydroxy Acid Dehydrogenase Catalyzing Reactions Involved in Coenzyme ...
14902 Identification of an Archaeal 2-Hydroxy Acid Dehydrogenase Catalyzing Reactions Involved in Coenzyme ...
14903 Identification of an Archaeal 2-Hydroxy Acid Dehydrogenase Catalyzing Reactions Involved in Coenzyme ...
14904 Identification of an Archaeal 2-Hydroxy Acid Dehydrogenase Catalyzing Reactions Involved in Coenzyme ...
14905 Identification of an Archaeal 2-Hydroxy Acid Dehydrogenase Catalyzing Reactions Involved in Coenzyme ...
14906 Identification of an Archaeal 2-Hydroxy Acid Dehydrogenase Catalyzing Reactions Involved in Coenzyme ...
14907 Identification of an Archaeal 2-Hydroxy Acid Dehydrogenase Catalyzing Reactions Involved in Coenzyme ...
14908 Identification of an Archaeal 2-Hydroxy Acid Dehydrogenase Catalyzing Reactions Involved in Coenzyme ...
14909 Identification of an Archaeal 2-Hydroxy Acid Dehydrogenase Catalyzing Reactions Involved in Coenzyme ...
14910 Identification of an Archaeal 2-Hydroxy Acid Dehydrogenase Catalyzing Reactions Involved in Coenzyme ...
14911 Identification of an Archaeal 2-Hydroxy Acid Dehydrogenase Catalyzing Reactions Involved in Coenzyme ...
14912 Identification of an Archaeal 2-Hydroxy Acid Dehydrogenase Catalyzing Reactions Involved in Coenzyme ...
14913 Identification of an Archaeal 2-Hydroxy Acid Dehydrogenase Catalyzing Reactions Involved in Coenzyme ...
14914 Competition of several enzymes for a common substrate: a possible model of cellular events
14915 Competition of several enzymes for a common substrate: a possible model of cellular events
14916 Competition of several enzymes for a common substrate: a possible model of cellular events
14917 Competition of several enzymes for a common substrate: a possible model of cellular events
14918 Competition of several enzymes for a common substrate: a possible model of cellular events
14919 Competition of several enzymes for a common substrate: a possible model of cellular events
14920 Competition of several enzymes for a common substrate: a possible model of cellular events
14921 Competition of several enzymes for a common substrate: a possible model of cellular events
14922 Competition of several enzymes for a common substrate: a possible model of cellular events
14923 Competition of several enzymes for a common substrate: a possible model of cellular events
14924 Competition of several enzymes for a common substrate: a possible model of cellular events
14925 Competition of several enzymes for a common substrate: a possible model of cellular events
14926 Competition of several enzymes for a common substrate: a possible model of cellular events
14927 Competition of several enzymes for a common substrate: a possible model of cellular events
14928 Competition of several enzymes for a common substrate: a possible model of cellular events
14929 Competition of several enzymes for a common substrate: a possible model of cellular events
14930 Competition of several enzymes for a common substrate: a possible model of cellular events
14931 Competition of several enzymes for a common substrate: a possible model of cellular events
14932 Competition of several enzymes for a common substrate: a possible model of cellular events
14933 Competition of several enzymes for a common substrate: a possible model of cellular events
14934 Competition of several enzymes for a common substrate: a possible model of cellular events
14935 Competition of several enzymes for a common substrate: a possible model of cellular events
14936 Competition of several enzymes for a common substrate: a possible model of cellular events
14937 Competition of several enzymes for a common substrate: a possible model of cellular events
14938 Competition of several enzymes for a common substrate: a possible model of cellular events
14939 Characterization of the beta-lactam binding site of penicillin acylase of Escherichia coli by structural and ...
14940 Characterization of the beta-lactam binding site of penicillin acylase of Escherichia coli by structural and ...
14941 Characterization of the beta-lactam binding site of penicillin acylase of Escherichia coli by structural and ...
14942 Characterization of the beta-lactam binding site of penicillin acylase of Escherichia coli by structural and ...
14943 Characterization of the beta-lactam binding site of penicillin acylase of Escherichia coli by structural and ...
14944 Characterization of the beta-lactam binding site of penicillin acylase of Escherichia coli by structural and ...
14945 Characterization of the beta-lactam binding site of penicillin acylase of Escherichia coli by structural and ...
14946 Characterization of the beta-lactam binding site of penicillin acylase of Escherichia coli by structural and ...
14947 Characterization of the beta-lactam binding site of penicillin acylase of Escherichia coli by structural and ...
14948 Characterization of the beta-lactam binding site of penicillin acylase of Escherichia coli by structural and ...
14949 Characterization of the beta-lactam binding site of penicillin acylase of Escherichia coli by structural and ...
14950 Characterization of the beta-lactam binding site of penicillin acylase of Escherichia coli by structural and ...
14951 Characterization of the beta-lactam binding site of penicillin acylase of Escherichia coli by structural and ...
14952 Characterization of the beta-lactam binding site of penicillin acylase of Escherichia coli by structural and ...
14953 Characterization of the beta-lactam binding site of penicillin acylase of Escherichia coli by structural and ...
14954 Characterization of the beta-lactam binding site of penicillin acylase of Escherichia coli by structural and ...
14955 Evolution of enzymatic activities in the enolase superfamily: N-succinylamino acid racemase and a new pathway ...
14956 Evolution of enzymatic activities in the enolase superfamily: N-succinylamino acid racemase and a new pathway ...
14957 Evolution of enzymatic activities in the enolase superfamily: N-succinylamino acid racemase and a new pathway ...
14958 Evolution of enzymatic activities in the enolase superfamily: N-succinylamino acid racemase and a new pathway ...
14959 Evolution of enzymatic activities in the enolase superfamily: N-succinylamino acid racemase and a new pathway ...
14960 Evolution of enzymatic activities in the enolase superfamily: N-succinylamino acid racemase and a new pathway ...
14961 Evolution of enzymatic activities in the enolase superfamily: N-succinylamino acid racemase and a new pathway ...
14962 Evolution of enzymatic activities in the enolase superfamily: N-succinylamino acid racemase and a new pathway ...
14963 Evolution of enzymatic activities in the enolase superfamily: N-succinylamino acid racemase and a new pathway ...
14964 Evolution of enzymatic activities in the enolase superfamily: N-succinylamino acid racemase and a new pathway ...
14965 Evolution of enzymatic activities in the enolase superfamily: N-succinylamino acid racemase and a new pathway ...
14966 Evolution of enzymatic activities in the enolase superfamily: N-succinylamino acid racemase and a new pathway ...
14967 Evolution of enzymatic activities in the enolase superfamily: N-succinylamino acid racemase and a new pathway ...
14968 Evolution of enzymatic activities in the enolase superfamily: N-succinylamino acid racemase and a new pathway ...
14969 Evolution of enzymatic activities in the enolase superfamily: N-succinylamino acid racemase and a new pathway ...
14970 Evolution of enzymatic activities in the enolase superfamily: N-succinylamino acid racemase and a new pathway ...
14971 Evolution of enzymatic activities in the enolase superfamily: N-succinylamino acid racemase and a new pathway ...
14972 Evolution of enzymatic activities in the enolase superfamily: N-succinylamino acid racemase and a new pathway ...
14973 Evolution of enzymatic activities in the enolase superfamily: N-succinylamino acid racemase and a new pathway ...
14974 Evolution of enzymatic activities in the enolase superfamily: N-succinylamino acid racemase and a new pathway ...
14975 Evolution of enzymatic activities in the enolase superfamily: N-succinylamino acid racemase and a new pathway ...
14976 Evolution of enzymatic activities in the enolase superfamily: N-succinylamino acid racemase and a new pathway ...
14977 Evolution of enzymatic activities in the enolase superfamily: N-succinylamino acid racemase and a new pathway ...
14978 Evolution of enzymatic activities in the enolase superfamily: N-succinylamino acid racemase and a new pathway ...
14979 Evolution of enzymatic activities in the enolase superfamily: N-succinylamino acid racemase and a new pathway ...
14980 Evolution of enzymatic activities in the enolase superfamily: N-succinylamino acid racemase and a new pathway ...
14981 Evolution of enzymatic activities in the enolase superfamily: N-succinylamino acid racemase and a new pathway ...
14982 Evolution of enzymatic activities in the enolase superfamily: N-succinylamino acid racemase and a new pathway ...
14983 Evolution of enzymatic activities in the enolase superfamily: N-succinylamino acid racemase and a new pathway ...
14984 Evolution of enzymatic activities in the enolase superfamily: N-succinylamino acid racemase and a new pathway ...
14985 Evolution of enzymatic activities in the enolase superfamily: N-succinylamino acid racemase and a new pathway ...
14986 Evolution of enzymatic activities in the enolase superfamily: N-succinylamino acid racemase and a new pathway ...
14987 Evolution of enzymatic activities in the enolase superfamily: N-succinylamino acid racemase and a new pathway ...
14988 Evolution of enzymatic activities in the enolase superfamily: N-succinylamino acid racemase and a new pathway ...
14989 Evolution of enzymatic activities in the enolase superfamily: N-succinylamino acid racemase and a new pathway ...
14990 Evolution of enzymatic activities in the enolase superfamily: N-succinylamino acid racemase and a new pathway ...
14991 Evolution of enzymatic activities in the enolase superfamily: N-succinylamino acid racemase and a new pathway ...
14992 Evolution of enzymatic activities in the enolase superfamily: N-succinylamino acid racemase and a new pathway ...
14993 Evolution of enzymatic activities in the enolase superfamily: N-succinylamino acid racemase and a new pathway ...
14994 Evolution of enzymatic activities in the enolase superfamily: N-succinylamino acid racemase and a new pathway ...
14995 Evolution of enzymatic activities in the enolase superfamily: N-succinylamino acid racemase and a new pathway ...
14996 Evolution of enzymatic activities in the enolase superfamily: N-succinylamino acid racemase and a new pathway ...
14997 Evolution of enzymatic activities in the enolase superfamily: N-succinylamino acid racemase and a new pathway ...
14998 Evolution of enzymatic activities in the enolase superfamily: N-succinylamino acid racemase and a new pathway ...
14999 Evolution of enzymatic activities in the enolase superfamily: N-succinylamino acid racemase and a new pathway ...
15000 Evolution of enzymatic activities in the enolase superfamily: N-succinylamino acid racemase and a new pathway ...



Overview of the Entry Data   (go to Help / Information)
 One line in Overview represents one entry in the database.
 Click on the key/axis name to sort by that key. Hover over the heatmap to see the data values.
 Select values by clicking on the heatmap area. Multiple categories or ranges are selected by brushing.
 Overview visible axis/keys can be set in 'Visible Overview Axes' (click to open/close)
 Selection on all graphs can be reset by using 'Reset Highlighting'.
 Selected color scheme (set in 'Color Scheme (PC, SPM, KPPC, KPSP)'): Plasma (Warm, Dark)
  

    * Keys/axis take the appropriate selection from the whole color scheme (color legend can be seen when sorting by that key) e.g.
    two valued keys (e.g. Rate Equation) use the end colors of the color scheme while unique numerical keys (e.g. EntryID) use the whole color scheme.
    * Overview shows the coloring by every key/axis (best seen when sorted by that axis/key).
    All other graphs (PC, SPM, KPPC, KPSP) use one single axis/key for coloring (chosen in 'PC, SPM: color by axis', 'KPPC, KPSP: color by axis').
    * Non-existent values of a chosen key can be made more prominent by separately selecting their color in 'NULL ("-") value color (for all graphs)':     Default (color scale minimum) selected
Highlighted Data:

0






Axes:


Allowing only eight (seven plus Index) visible PC axis to prevent clutter.

SPM full matrix


Height of the PC and KPPC graphs is limited to 1200px. If the graph is larger some tick clutter might appear on the axes.


Kinetic Parameter Data:



Appearance:

Color Scheme
(PC, SPM, KPPC, KPSP)


NULL ("-") value color
(for all graphs)
The "null" color is visible if the data is sorted by the key that contains the null values.

PC, SPM: color by axis

KPPC, KPSP: color by axis


Various:


Parallel Coordinates (PC) of the Entry Data
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 Brush the axis to select the data (supports multiple selections).
 Detailed numerical data values can be seen on Overview or SPM (or in the Entry View tab).
 PC visible axis/keys can be set in 'Visible PC Axes (max 8)'
 PC colored by the key (set in 'PC, SPM: color by axis'):
Scatter Plot Matrix (SPM) of the Entry Data (numerical values only -> pH, Temperature, Year; kinetic data separately)
Loading graph, please wait...

 Brush any of the scatter plots to select the data.
 SPM visible axis/keys can be set in 'Visible SPM Axes'
 SPM colored by the key (set in 'PC, SPM: color by axis'):
Kinetic Parameters
Parallel Coordinates (KPPC) of the Kinetic Parameters (plus temperature, pH) (each entry can have many parameters)
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 Each entry can have multiple kinetic parameters that can be explored in the two graphs (KPPC, KPSP).
 Brush the axis to select the data.
 Detailed numerical data values can be seen on scatter plot KPSP (or in the Entry View tab).
 KPPC visible axis/keys can be set in 'Visible KPPC Axes'
 Currently showing types (set in 'Used Data Types'):
 KPPC colored by the key (set in 'KPPC, KPSP: color by axis'):
 KPPC, KPSP using the color scheme (set in 'Color Scheme (PC, SPM, KPPC, KPSP)'):
 Use KPSP to see the parameter details.
 KPPC local zoom status (allows detailed parameter space exploration not possible through the search):
    Parameter data types have to be reselected on zoom out (set in 'Used Data Types'). Not all types are available when zoomed.


Search button will give you the entries with all of thier parameters.
Limit the search locally first, by zooming and then selecting for the search.
Not selecting anything before the search will give you the initial result.





Scatter Plot (KPSP) of the Kinetic Parameter Values (plus temperature, pH) (each entry can have many parameters)
Loading graph, please wait...


  Points currently colored by:
 KPSP currently showing: Start Value vs
 KPSP serves as a addition of KPPC to see the parameter details (hover over point to see the values).
 Data can be zoomed and panned, but should be selected on KPPC.
Show/hide
First three graphs represent the general information for the database entries (Overview, PC, SPM).
Since each entry can contain several kinetic parameters, data space of the kinetic parameters can be separately explored (using KPPC and KPSP).
Last two graphs offer more details about the kinetic parameters (KPPC, KPSP) belonging to the entries and an option to explore through their data space.
A number of entries is obtained as a result of a search.

Select/highlight the subset of the data on one of the graphs. Number of highlighted data and the used attributes are visible on the top right side of the visualization tab (as is the number of the selected kinetic parameters).
By clicking on "Add Selection to Search" search is performed applying the selected criteria (highlighting) on the resulting data, thus refining the search. E.g.
If the current search query is a refinement of the previous query "Use Previous Query (Go Back)" button can be used to perform the previous query again. Only one automatic step back is possible, but the query can be manually manipulated if desired.


The graphs can be manipulated and the data highlighted in the following ways:

Overview of the resulting data entries is given in the heat map:
* Sort per column (upwards, downwards) by clicking on the attribute's title, hold the "shift" key and drag the column to rearrange columns.
* Show/hide columns using Visible Overview Axes.
* Highlight individual values by clicking.
* Highlight ranges by brushing (range of the sorted column, marked with a green line).
* While brushing, the thin green line (extending from the thick one) shows the full range of the selected categories.

Parallel Coordinates (PC):
* Sort axis by double clicking on the axis title, rearrange axes by dragging.
* Show/hide axes using Visible PC Axes (maximum 7 in addition to the Index axis).
* Highlight ranges by brushing on different axes (more ranges on a single axis are possible).
* Height of the PC graph is determined by the data, but limited (has minimum and maximum height). If the graph should be larger than the maximum height some tick clutter might appear on the axes.
* Numerical axes (e.g. pH and Temperature) have their null values shown below the line unlike categorical axes (like UniprotID) that have the null value or "-" as a category on the axis.

Scatter Plot Matrix (SPM):
* Show/hide attributes (numerical ones) using Visible SPM Axes.
* Highlight range by brushing on one of the scatter plots.
* Histograms show the attribute value frequency (divided into 10 bins/columns).
* Full SPM matrix can be shown.
* Details about the point values can be seen on a tooltip when hovering above the point.
* Points with no value ("-") are shown on the left side or under the axis.
* If only points with no value ("-") are present, they are shown under or left of the zero line on the bottom/left of the respective image.
* Lower tick values are valid for the histogram graphs while ticks on the left (plus the lower ones) are only valid for the scatter plots in the matrix.

Kinetic Parameter Parallel Coordinates (KPPC):
* EntryID axis on KPPC connects the kinetic parameters with the other graphs: each parameter belongs to an entry. One entry can have more parameters.
* Sort axis by double clicking on the axis title, rearrange axes by dragging.
* Show/hide axes using Visible KPPC Axes (Type and EntryID are always visible).
* Highlight ranges by brushing on different axes (single range possible on a single axis).
* Select shown kinetic parameter data type by selecting Used Data Types (must be at least one).
     * Types are preselected on search giving types: Km, Vmax, kcat as default (if present). The user can view any other type by selecting it in the GUI.
     * Currently selected types are stated below the graph.
* Start Value Original axis shows the original values of the parameter.
* Start Value Log axis is a logarithmic axis (since the original range of the shown values can be huge). The original range can be seen in Brush Info Kinetic Parameters PC.
* Graph can be searched locally by using the Zoom in / Zoom out buttons.
* Once the desired values are narrowed down (and selected on the KPPC) they can be searched by using the "Add Selection to Search" button.
     * the kinetic parameter search query uses the selected keywords (where available) e.g. ParameterType, AssociatedSpecies.
     * where no keywords are available the kinetic parameter search query uses entryIDs.
     * the result of the search gives full entries (meaning resulting parameter data is bigger than the selection).
* Height of the KPPC graph is determined by the data, but limited (has minimum and maximum height). If the graph should be larger than the maximum height some tick clutter might appear on the axes.
* For convenience, KPPC can also show temperature and pH values and the axis can also be colored by those values.
* Numerical axes (e.g. pH and Temperature) have their null values shown below the line unlike categorical axes that have the null value or "-" as a category on the axis.

Scatter Plot of the Kinetic Parameter Values (KPSP):
* Scatter plot is showing the values of the "Start Value Original" vs "Temperature", "pH" or "EntryID" values.
* The user can choose values on the y axis using the dropdown menu ("Temperature", "pH" or "EntryID") above the graph.
* The user can choose the axis used for the point size using the dropdown menu ("Uniform", "Temperature", "pH" or "EntryID") above the graph. Point size is interpolated between a set range (size 5 to 10). Larger range [1,30] can be set by using the range slider. Uniform size is size 5 (no range slider).
* The user can choose the kinetic parameter types of the shown values in the GUI using "Used data types" (the graph updates accordingly).
* Graph can be zoomed and panned by using the computer mouse or touchpad.
* Viewed data points can again be centered by pressing the Reset position button (zoom value is seen above the button).
* Details about the point values can be seen in a tooltip when hovering above the point.
* Points with no value ("-") are shown under the axis.
* If only points with no value ("-") are present, they are shown under the zero line.
* Used data types, their units and associated species are visible on the Start Value axis label (all can be seen in a tooltip when hovering above with the mouse pointer).
* Corresponding data is highlighted when selecting data on any of the other graphs.
* Data cannot be selected on this graph. The graph responds to the selection on the KPPC.
* Details about selection (made on KPPC) can be viewed below in the Brush Info section.

Additional Information:
* Highlighting data entries on one of the graphs (Overview, PC, SPM) highlights the same data on all other graphs (and their parameters on KPPC, KPSP).
* Highlighting kinetic parameter data on KPPC graph highlights the matching entries on other graphs (Overview, PC, SPM, KPSP). Each parameter belongs to an entry. One entry can have more parameters.
* Details about selection can be viewed below in the Brush Info section.
* Reset highlighted values by using "Reset Highlighting".
* Index attribute is only the sequential numbering of the result and cannot be used for further searching.
* Color:
     * Different color schemes for the graphs can be selected (see image).
     * Overview uses the full range of the color scheme for each of the attributes.
     * Which attribute is used for coloring PC and SPM axes can be manually selected, otherwise it changes upon sorting columns in Overview.
     * Which attribute is used for coloring KPPC axes (and KPSP) can also be manually selected (and does not change upon sorting columns in Overview).
     * Color of the null values can be selected by using the "NULL ("-") value color" in the GUI. Default color is the faded minimum color of the chosen color scheme. Users can select another color that offers more contrast and visibility in combination with the chosen color scheme (red, green, blue, cyan, magenta, yellow, black). When changing the used color scheme the null color is reset to the default color for that scheme (faded minimum color). Note that coloring ("PC, SPM: color by axis") or sorting the Overview (and hence coloring PC and SPM) by a certain key/axis (containing the null values), makes the null values nicely visible on the PC and SPM graphs. For the null value color to be visible on the KPPC and KPSP graphs, they need to be colored by that key/axis ("KPPC, KPSP: color by axis").
* Screenshots of the produced graphs can be downloaded together with the solr search expression.
* Hovering with a pointer over a shortened tick name (three dots) shows the full name.
* Temperature is given in degrees Celsius (°C).
* Overview currently shows maximum 10000 data, PC and SPM maximum 400 (to not over clutter). The data limit for PC and SPM can be turned off by ticking "Allow More Data" in the GUI. This option only appears if the number of data entries is between 400 and 10000.
Brush Info