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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 ...
|