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21001
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Separation and properties of NAD+- and NADP+-dependent glyceraldehyde-3-phosphate dehydrogenases from ...
|
21002
|
Separation and properties of NAD+- and NADP+-dependent glyceraldehyde-3-phosphate dehydrogenases from ...
|
21003
|
Separation and properties of NAD+- and NADP+-dependent glyceraldehyde-3-phosphate dehydrogenases from ...
|
21004
|
Separation and properties of NAD+- and NADP+-dependent glyceraldehyde-3-phosphate dehydrogenases from ...
|
21005
|
Separation and properties of NAD+- and NADP+-dependent glyceraldehyde-3-phosphate dehydrogenases from ...
|
21006
|
Separation and properties of NAD+- and NADP+-dependent glyceraldehyde-3-phosphate dehydrogenases from ...
|
21007
|
Separation and properties of NAD+- and NADP+-dependent glyceraldehyde-3-phosphate dehydrogenases from ...
|
21008
|
Separation and properties of NAD+- and NADP+-dependent glyceraldehyde-3-phosphate dehydrogenases from ...
|
21009
|
Separation and properties of NAD+- and NADP+-dependent glyceraldehyde-3-phosphate dehydrogenases from ...
|
21010
|
Separation and properties of NAD+- and NADP+-dependent glyceraldehyde-3-phosphate dehydrogenases from ...
|
21011
|
Separation and properties of NAD+- and NADP+-dependent glyceraldehyde-3-phosphate dehydrogenases from ...
|
21012
|
Separation and properties of NAD+- and NADP+-dependent glyceraldehyde-3-phosphate dehydrogenases from ...
|
21013
|
Separation and properties of NAD+- and NADP+-dependent glyceraldehyde-3-phosphate dehydrogenases from ...
|
21014
|
Arginine 165/arginine 277 pair in (S)-mandelate dehydrogenase from Pseudomonas putida: role in catalysis and ...
|
21015
|
Arginine 165/arginine 277 pair in (S)-mandelate dehydrogenase from Pseudomonas putida: role in catalysis and ...
|
21016
|
Arginine 165/arginine 277 pair in (S)-mandelate dehydrogenase from Pseudomonas putida: role in catalysis and ...
|
21017
|
Arginine 165/arginine 277 pair in (S)-mandelate dehydrogenase from Pseudomonas putida: role in catalysis and ...
|
21018
|
Arginine 165/arginine 277 pair in (S)-mandelate dehydrogenase from Pseudomonas putida: role in catalysis and ...
|
21019
|
Arginine 165/arginine 277 pair in (S)-mandelate dehydrogenase from Pseudomonas putida: role in catalysis and ...
|
21020
|
Arginine 165/arginine 277 pair in (S)-mandelate dehydrogenase from Pseudomonas putida: role in catalysis and ...
|
21021
|
Arginine 165/arginine 277 pair in (S)-mandelate dehydrogenase from Pseudomonas putida: role in catalysis and ...
|
21022
|
Arginine 165/arginine 277 pair in (S)-mandelate dehydrogenase from Pseudomonas putida: role in catalysis and ...
|
21023
|
Arginine 165/arginine 277 pair in (S)-mandelate dehydrogenase from Pseudomonas putida: role in catalysis and ...
|
21024
|
Arginine 165/arginine 277 pair in (S)-mandelate dehydrogenase from Pseudomonas putida: role in catalysis and ...
|
21025
|
Arginine 165/arginine 277 pair in (S)-mandelate dehydrogenase from Pseudomonas putida: role in catalysis and ...
|
21026
|
Arginine 165/arginine 277 pair in (S)-mandelate dehydrogenase from Pseudomonas putida: role in catalysis and ...
|
21027
|
Arginine 165/arginine 277 pair in (S)-mandelate dehydrogenase from Pseudomonas putida: role in catalysis and ...
|
21028
|
Arginine 165/arginine 277 pair in (S)-mandelate dehydrogenase from Pseudomonas putida: role in catalysis and ...
|
21029
|
Arginine 165/arginine 277 pair in (S)-mandelate dehydrogenase from Pseudomonas putida: role in catalysis and ...
|
21030
|
Arginine 165/arginine 277 pair in (S)-mandelate dehydrogenase from Pseudomonas putida: role in catalysis and ...
|
21031
|
Arginine 165/arginine 277 pair in (S)-mandelate dehydrogenase from Pseudomonas putida: role in catalysis and ...
|
21032
|
Isozymic nature of spore coat-associated alanine racemase of Bacillus subtilis
|
21033
|
Isozymic nature of spore coat-associated alanine racemase of Bacillus subtilis
|
21034
|
Isozymic nature of spore coat-associated alanine racemase of Bacillus subtilis
|
21035
|
Isozymic nature of spore coat-associated alanine racemase of Bacillus subtilis
|
21036
|
Isozymic nature of spore coat-associated alanine racemase of Bacillus subtilis
|
21037
|
Isozymic nature of spore coat-associated alanine racemase of Bacillus subtilis
|
21038
|
Isozymic nature of spore coat-associated alanine racemase of Bacillus subtilis
|
21039
|
Isozymic nature of spore coat-associated alanine racemase of Bacillus subtilis
|
21040
|
Isozymic nature of spore coat-associated alanine racemase of Bacillus subtilis
|
21041
|
Isozymic nature of spore coat-associated alanine racemase of Bacillus subtilis
|
21042
|
Isozymic nature of spore coat-associated alanine racemase of Bacillus subtilis
|
21043
|
Isozymic nature of spore coat-associated alanine racemase of Bacillus subtilis
|
21044
|
Isozymic nature of spore coat-associated alanine racemase of Bacillus subtilis
|
21045
|
Isozymic nature of spore coat-associated alanine racemase of Bacillus subtilis
|
21046
|
Isozymic nature of spore coat-associated alanine racemase of Bacillus subtilis
|
21047
|
Isozymic nature of spore coat-associated alanine racemase of Bacillus subtilis
|
21048
|
Isozymic nature of spore coat-associated alanine racemase of Bacillus subtilis
|
21049
|
Isozymic nature of spore coat-associated alanine racemase of Bacillus subtilis
|
21050
|
Isozymic nature of spore coat-associated alanine racemase of Bacillus subtilis
|
21051
|
Role of residues 104, 164, 166, 238 and 240 in the substrate profile of PER-1 beta-lactamase hydrolysing ...
|
21052
|
Role of residues 104, 164, 166, 238 and 240 in the substrate profile of PER-1 beta-lactamase hydrolysing ...
|
21053
|
Role of residues 104, 164, 166, 238 and 240 in the substrate profile of PER-1 beta-lactamase hydrolysing ...
|
21054
|
Role of residues 104, 164, 166, 238 and 240 in the substrate profile of PER-1 beta-lactamase hydrolysing ...
|
21055
|
Role of residues 104, 164, 166, 238 and 240 in the substrate profile of PER-1 beta-lactamase hydrolysing ...
|
21056
|
Role of residues 104, 164, 166, 238 and 240 in the substrate profile of PER-1 beta-lactamase hydrolysing ...
|
21057
|
Role of residues 104, 164, 166, 238 and 240 in the substrate profile of PER-1 beta-lactamase hydrolysing ...
|
21058
|
Role of residues 104, 164, 166, 238 and 240 in the substrate profile of PER-1 beta-lactamase hydrolysing ...
|
21059
|
Role of residues 104, 164, 166, 238 and 240 in the substrate profile of PER-1 beta-lactamase hydrolysing ...
|
21060
|
Role of residues 104, 164, 166, 238 and 240 in the substrate profile of PER-1 beta-lactamase hydrolysing ...
|
21061
|
Role of residues 104, 164, 166, 238 and 240 in the substrate profile of PER-1 beta-lactamase hydrolysing ...
|
21062
|
Role of residues 104, 164, 166, 238 and 240 in the substrate profile of PER-1 beta-lactamase hydrolysing ...
|
21063
|
Role of residues 104, 164, 166, 238 and 240 in the substrate profile of PER-1 beta-lactamase hydrolysing ...
|
21064
|
Role of residues 104, 164, 166, 238 and 240 in the substrate profile of PER-1 beta-lactamase hydrolysing ...
|
21065
|
Role of residues 104, 164, 166, 238 and 240 in the substrate profile of PER-1 beta-lactamase hydrolysing ...
|
21066
|
Role of residues 104, 164, 166, 238 and 240 in the substrate profile of PER-1 beta-lactamase hydrolysing ...
|
21067
|
Role of residues 104, 164, 166, 238 and 240 in the substrate profile of PER-1 beta-lactamase hydrolysing ...
|
21068
|
Role of residues 104, 164, 166, 238 and 240 in the substrate profile of PER-1 beta-lactamase hydrolysing ...
|
21069
|
Role of residues 104, 164, 166, 238 and 240 in the substrate profile of PER-1 beta-lactamase hydrolysing ...
|
21070
|
Role of residues 104, 164, 166, 238 and 240 in the substrate profile of PER-1 beta-lactamase hydrolysing ...
|
21071
|
Role of residues 104, 164, 166, 238 and 240 in the substrate profile of PER-1 beta-lactamase hydrolysing ...
|
21072
|
Role of residues 104, 164, 166, 238 and 240 in the substrate profile of PER-1 beta-lactamase hydrolysing ...
|
21073
|
Role of residues 104, 164, 166, 238 and 240 in the substrate profile of PER-1 beta-lactamase hydrolysing ...
|
21074
|
Role of residues 104, 164, 166, 238 and 240 in the substrate profile of PER-1 beta-lactamase hydrolysing ...
|
21075
|
Role of residues 104, 164, 166, 238 and 240 in the substrate profile of PER-1 beta-lactamase hydrolysing ...
|
21076
|
Role of residues 104, 164, 166, 238 and 240 in the substrate profile of PER-1 beta-lactamase hydrolysing ...
|
21077
|
Role of residues 104, 164, 166, 238 and 240 in the substrate profile of PER-1 beta-lactamase hydrolysing ...
|
21078
|
Role of residues 104, 164, 166, 238 and 240 in the substrate profile of PER-1 beta-lactamase hydrolysing ...
|
21079
|
Role of residues 104, 164, 166, 238 and 240 in the substrate profile of PER-1 beta-lactamase hydrolysing ...
|
21080
|
Role of residues 104, 164, 166, 238 and 240 in the substrate profile of PER-1 beta-lactamase hydrolysing ...
|
21081
|
Role of residues 104, 164, 166, 238 and 240 in the substrate profile of PER-1 beta-lactamase hydrolysing ...
|
21082
|
Role of residues 104, 164, 166, 238 and 240 in the substrate profile of PER-1 beta-lactamase hydrolysing ...
|
21083
|
Role of residues 104, 164, 166, 238 and 240 in the substrate profile of PER-1 beta-lactamase hydrolysing ...
|
21084
|
Role of residues 104, 164, 166, 238 and 240 in the substrate profile of PER-1 beta-lactamase hydrolysing ...
|
21085
|
Role of residues 104, 164, 166, 238 and 240 in the substrate profile of PER-1 beta-lactamase hydrolysing ...
|
21086
|
Role of residues 104, 164, 166, 238 and 240 in the substrate profile of PER-1 beta-lactamase hydrolysing ...
|
21087
|
Role of residues 104, 164, 166, 238 and 240 in the substrate profile of PER-1 beta-lactamase hydrolysing ...
|
21088
|
Role of residues 104, 164, 166, 238 and 240 in the substrate profile of PER-1 beta-lactamase hydrolysing ...
|
21089
|
Role of residues 104, 164, 166, 238 and 240 in the substrate profile of PER-1 beta-lactamase hydrolysing ...
|
21090
|
Role of residues 104, 164, 166, 238 and 240 in the substrate profile of PER-1 beta-lactamase hydrolysing ...
|
21091
|
Role of residues 104, 164, 166, 238 and 240 in the substrate profile of PER-1 beta-lactamase hydrolysing ...
|
21092
|
Role of residues 104, 164, 166, 238 and 240 in the substrate profile of PER-1 beta-lactamase hydrolysing ...
|
21093
|
Role of residues 104, 164, 166, 238 and 240 in the substrate profile of PER-1 beta-lactamase hydrolysing ...
|
21094
|
Role of residues 104, 164, 166, 238 and 240 in the substrate profile of PER-1 beta-lactamase hydrolysing ...
|
21095
|
Hibernation impact on the catalytic activities of the mitochondrial D-3-hydroxybutyrate dehydrogenase in liver ...
|
21096
|
Hibernation impact on the catalytic activities of the mitochondrial D-3-hydroxybutyrate dehydrogenase in liver ...
|
21097
|
Hibernation impact on the catalytic activities of the mitochondrial D-3-hydroxybutyrate dehydrogenase in liver ...
|
21098
|
Hibernation impact on the catalytic activities of the mitochondrial D-3-hydroxybutyrate dehydrogenase in liver ...
|
21099
|
Hibernation impact on the catalytic activities of the mitochondrial D-3-hydroxybutyrate dehydrogenase in liver ...
|
21100
|
Hibernation impact on the catalytic activities of the mitochondrial D-3-hydroxybutyrate dehydrogenase in liver ...
|
21101
|
Hibernation impact on the catalytic activities of the mitochondrial D-3-hydroxybutyrate dehydrogenase in liver ...
|
21102
|
Hibernation impact on the catalytic activities of the mitochondrial D-3-hydroxybutyrate dehydrogenase in liver ...
|
21103
|
Hibernation impact on the catalytic activities of the mitochondrial D-3-hydroxybutyrate dehydrogenase in liver ...
|
21104
|
Hibernation impact on the catalytic activities of the mitochondrial D-3-hydroxybutyrate dehydrogenase in liver ...
|
21105
|
Hibernation impact on the catalytic activities of the mitochondrial D-3-hydroxybutyrate dehydrogenase in liver ...
|
21106
|
Hibernation impact on the catalytic activities of the mitochondrial D-3-hydroxybutyrate dehydrogenase in liver ...
|
21107
|
Hibernation impact on the catalytic activities of the mitochondrial D-3-hydroxybutyrate dehydrogenase in liver ...
|
21108
|
Hibernation impact on the catalytic activities of the mitochondrial D-3-hydroxybutyrate dehydrogenase in liver ...
|
21109
|
Hibernation impact on the catalytic activities of the mitochondrial D-3-hydroxybutyrate dehydrogenase in liver ...
|
21110
|
Hibernation impact on the catalytic activities of the mitochondrial D-3-hydroxybutyrate dehydrogenase in liver ...
|
21111
|
Hibernation impact on the catalytic activities of the mitochondrial D-3-hydroxybutyrate dehydrogenase in liver ...
|
21112
|
Hibernation impact on the catalytic activities of the mitochondrial D-3-hydroxybutyrate dehydrogenase in liver ...
|
21113
|
Hibernation impact on the catalytic activities of the mitochondrial D-3-hydroxybutyrate dehydrogenase in liver ...
|
21114
|
Hibernation impact on the catalytic activities of the mitochondrial D-3-hydroxybutyrate dehydrogenase in liver ...
|
21115
|
Hibernation impact on the catalytic activities of the mitochondrial D-3-hydroxybutyrate dehydrogenase in liver ...
|
21116
|
Hibernation impact on the catalytic activities of the mitochondrial D-3-hydroxybutyrate dehydrogenase in liver ...
|
21117
|
Hibernation impact on the catalytic activities of the mitochondrial D-3-hydroxybutyrate dehydrogenase in liver ...
|
21118
|
Hibernation impact on the catalytic activities of the mitochondrial D-3-hydroxybutyrate dehydrogenase in liver ...
|
21119
|
Purification and properties of thyroidal UDP-glucose-4-epimerase
|
21120
|
Purification and properties of thyroidal UDP-glucose-4-epimerase
|
21121
|
Purification and properties of thyroidal UDP-glucose-4-epimerase
|
21122
|
Purification and characterization of the 4-aminobutyrate--2,ketoglutarate transaminase from mouse brain
|
21123
|
Purification and characterization of the 4-aminobutyrate--2,ketoglutarate transaminase from mouse brain
|
21124
|
Studies of phospholipid-requiring bacterial enzymes. 3. Purification and properties of uridine diphosphate ...
|
21125
|
Studies of phospholipid-requiring bacterial enzymes. 3. Purification and properties of uridine diphosphate ...
|
21126
|
Essential role of histidine 20 in the catalytic mechanism of Escherichia coli peptidyl-tRNA hydrolase
|
21127
|
Essential role of histidine 20 in the catalytic mechanism of Escherichia coli peptidyl-tRNA hydrolase
|
21128
|
Essential role of histidine 20 in the catalytic mechanism of Escherichia coli peptidyl-tRNA hydrolase
|
21129
|
Essential role of histidine 20 in the catalytic mechanism of Escherichia coli peptidyl-tRNA hydrolase
|
21130
|
Essential role of histidine 20 in the catalytic mechanism of Escherichia coli peptidyl-tRNA hydrolase
|
21131
|
Essential role of histidine 20 in the catalytic mechanism of Escherichia coli peptidyl-tRNA hydrolase
|
21132
|
Essential role of histidine 20 in the catalytic mechanism of Escherichia coli peptidyl-tRNA hydrolase
|
21133
|
Essential role of histidine 20 in the catalytic mechanism of Escherichia coli peptidyl-tRNA hydrolase
|
21134
|
Essential role of histidine 20 in the catalytic mechanism of Escherichia coli peptidyl-tRNA hydrolase
|
21135
|
Essential role of histidine 20 in the catalytic mechanism of Escherichia coli peptidyl-tRNA hydrolase
|
21136
|
Essential role of histidine 20 in the catalytic mechanism of Escherichia coli peptidyl-tRNA hydrolase
|
21137
|
The contribution of adjacent subunits to the active sites of 3-D-Phosphoglycerate Dehydrogenase
|
21138
|
The contribution of adjacent subunits to the active sites of 3-D-Phosphoglycerate Dehydrogenase
|
21139
|
The contribution of adjacent subunits to the active sites of 3-D-Phosphoglycerate Dehydrogenase
|
21140
|
The contribution of adjacent subunits to the active sites of 3-D-Phosphoglycerate Dehydrogenase
|
21141
|
The contribution of adjacent subunits to the active sites of 3-D-Phosphoglycerate Dehydrogenase
|
21142
|
The contribution of adjacent subunits to the active sites of 3-D-Phosphoglycerate Dehydrogenase
|
21143
|
The contribution of adjacent subunits to the active sites of 3-D-Phosphoglycerate Dehydrogenase
|
21144
|
The contribution of adjacent subunits to the active sites of 3-D-Phosphoglycerate Dehydrogenase
|
21145
|
The contribution of adjacent subunits to the active sites of 3-D-Phosphoglycerate Dehydrogenase
|
21146
|
The contribution of adjacent subunits to the active sites of 3-D-Phosphoglycerate Dehydrogenase
|
21147
|
The contribution of adjacent subunits to the active sites of 3-D-Phosphoglycerate Dehydrogenase
|
21148
|
The contribution of adjacent subunits to the active sites of 3-D-Phosphoglycerate Dehydrogenase
|
21149
|
The contribution of adjacent subunits to the active sites of 3-D-Phosphoglycerate Dehydrogenase
|
21150
|
The contribution of adjacent subunits to the active sites of 3-D-Phosphoglycerate Dehydrogenase
|
21151
|
The contribution of adjacent subunits to the active sites of 3-D-Phosphoglycerate Dehydrogenase
|
21152
|
The contribution of adjacent subunits to the active sites of 3-D-Phosphoglycerate Dehydrogenase
|
21153
|
The contribution of adjacent subunits to the active sites of 3-D-Phosphoglycerate Dehydrogenase
|
21154
|
The contribution of adjacent subunits to the active sites of 3-D-Phosphoglycerate Dehydrogenase
|
21155
|
The contribution of adjacent subunits to the active sites of 3-D-Phosphoglycerate Dehydrogenase
|
21156
|
The contribution of adjacent subunits to the active sites of 3-D-Phosphoglycerate Dehydrogenase
|
21157
|
The contribution of adjacent subunits to the active sites of 3-D-Phosphoglycerate Dehydrogenase
|
21158
|
The contribution of adjacent subunits to the active sites of 3-D-Phosphoglycerate Dehydrogenase
|
21159
|
The contribution of adjacent subunits to the active sites of 3-D-Phosphoglycerate Dehydrogenase
|
21160
|
The contribution of adjacent subunits to the active sites of 3-D-Phosphoglycerate Dehydrogenase
|
21161
|
The contribution of adjacent subunits to the active sites of 3-D-Phosphoglycerate Dehydrogenase
|
21162
|
The contribution of adjacent subunits to the active sites of 3-D-Phosphoglycerate Dehydrogenase
|
21163
|
The contribution of adjacent subunits to the active sites of 3-D-Phosphoglycerate Dehydrogenase
|
21164
|
The contribution of adjacent subunits to the active sites of 3-D-Phosphoglycerate Dehydrogenase
|
21165
|
The contribution of adjacent subunits to the active sites of 3-D-Phosphoglycerate Dehydrogenase
|
21166
|
The contribution of adjacent subunits to the active sites of 3-D-Phosphoglycerate Dehydrogenase
|
21167
|
Site-directed mutagenesis of beta-lactamase I: role of Glu-166
|
21168
|
Site-directed mutagenesis of beta-lactamase I: role of Glu-166
|
21169
|
Site-directed mutagenesis of beta-lactamase I: role of Glu-166
|
21170
|
Site-directed mutagenesis of beta-lactamase I: role of Glu-166
|
21171
|
Site-directed mutagenesis of beta-lactamase I: role of Glu-166
|
21172
|
Site-directed mutagenesis of beta-lactamase I: role of Glu-166
|
21173
|
Site-directed mutagenesis of beta-lactamase I: role of Glu-166
|
21174
|
Site-directed mutagenesis of beta-lactamase I: role of Glu-166
|
21175
|
Site-directed mutagenesis of beta-lactamase I: role of Glu-166
|
21176
|
Site-directed mutagenesis of beta-lactamase I: role of Glu-166
|
21177
|
Site-directed mutagenesis of beta-lactamase I: role of Glu-166
|
21178
|
Site-directed mutagenesis of beta-lactamase I: role of Glu-166
|
21179
|
Site-directed mutagenesis of beta-lactamase I: role of Glu-166
|
21180
|
Site-directed mutagenesis of beta-lactamase I: role of Glu-166
|
21181
|
Site-directed mutagenesis of beta-lactamase I: role of Glu-166
|
21182
|
Site-directed mutagenesis of beta-lactamase I: role of Glu-166
|
21183
|
Site-directed mutagenesis of beta-lactamase I: role of Glu-166
|
21184
|
Site-directed mutagenesis of beta-lactamase I: role of Glu-166
|
21185
|
Site-directed mutagenesis of beta-lactamase I: role of Glu-166
|
21186
|
Site-directed mutagenesis of beta-lactamase I: role of Glu-166
|
21187
|
Properties of mutant SHV-5 beta-lactamases constructed by substitution of isoleucine or valine for methionine ...
|
21188
|
Properties of mutant SHV-5 beta-lactamases constructed by substitution of isoleucine or valine for methionine ...
|
21189
|
Properties of mutant SHV-5 beta-lactamases constructed by substitution of isoleucine or valine for methionine ...
|
21190
|
Properties of mutant SHV-5 beta-lactamases constructed by substitution of isoleucine or valine for methionine ...
|
21191
|
Properties of mutant SHV-5 beta-lactamases constructed by substitution of isoleucine or valine for methionine ...
|
21192
|
Properties of mutant SHV-5 beta-lactamases constructed by substitution of isoleucine or valine for methionine ...
|
21193
|
Properties of mutant SHV-5 beta-lactamases constructed by substitution of isoleucine or valine for methionine ...
|
21194
|
Properties of mutant SHV-5 beta-lactamases constructed by substitution of isoleucine or valine for methionine ...
|
21195
|
Properties of mutant SHV-5 beta-lactamases constructed by substitution of isoleucine or valine for methionine ...
|
21196
|
Properties of mutant SHV-5 beta-lactamases constructed by substitution of isoleucine or valine for methionine ...
|
21197
|
Properties of mutant SHV-5 beta-lactamases constructed by substitution of isoleucine or valine for methionine ...
|
21198
|
Properties of mutant SHV-5 beta-lactamases constructed by substitution of isoleucine or valine for methionine ...
|
21199
|
Properties of mutant SHV-5 beta-lactamases constructed by substitution of isoleucine or valine for methionine ...
|
21200
|
Properties of mutant SHV-5 beta-lactamases constructed by substitution of isoleucine or valine for methionine ...
|
21201
|
Properties of mutant SHV-5 beta-lactamases constructed by substitution of isoleucine or valine for methionine ...
|
21202
|
Properties of mutant SHV-5 beta-lactamases constructed by substitution of isoleucine or valine for methionine ...
|
21203
|
Properties of mutant SHV-5 beta-lactamases constructed by substitution of isoleucine or valine for methionine ...
|
21204
|
Properties of mutant SHV-5 beta-lactamases constructed by substitution of isoleucine or valine for methionine ...
|
21205
|
Properties of mutant SHV-5 beta-lactamases constructed by substitution of isoleucine or valine for methionine ...
|
21206
|
Properties of mutant SHV-5 beta-lactamases constructed by substitution of isoleucine or valine for methionine ...
|
21207
|
Properties of mutant SHV-5 beta-lactamases constructed by substitution of isoleucine or valine for methionine ...
|
21215
|
Use of site-directed mutagenesis to identify residues specific for each reaction catalyzed by Chorismate ...
|
21216
|
Use of site-directed mutagenesis to identify residues specific for each reaction catalyzed by Chorismate ...
|
21217
|
Use of site-directed mutagenesis to identify residues specific for each reaction catalyzed by Chorismate ...
|
21218
|
Use of site-directed mutagenesis to identify residues specific for each reaction catalyzed by Chorismate ...
|
21219
|
Use of site-directed mutagenesis to identify residues specific for each reaction catalyzed by Chorismate ...
|
21220
|
Use of site-directed mutagenesis to identify residues specific for each reaction catalyzed by Chorismate ...
|
21221
|
Use of site-directed mutagenesis to identify residues specific for each reaction catalyzed by Chorismate ...
|
21222
|
Use of site-directed mutagenesis to identify residues specific for each reaction catalyzed by Chorismate ...
|
21223
|
Use of site-directed mutagenesis to identify residues specific for each reaction catalyzed by Chorismate ...
|
21224
|
Use of site-directed mutagenesis to identify residues specific for each reaction catalyzed by Chorismate ...
|
21225
|
Use of site-directed mutagenesis to identify residues specific for each reaction catalyzed by Chorismate ...
|
21226
|
Use of site-directed mutagenesis to identify residues specific for each reaction catalyzed by Chorismate ...
|
21227
|
Use of site-directed mutagenesis to identify residues specific for each reaction catalyzed by Chorismate ...
|
21228
|
Use of site-directed mutagenesis to identify residues specific for each reaction catalyzed by Chorismate ...
|
21229
|
Use of site-directed mutagenesis to identify residues specific for each reaction catalyzed by Chorismate ...
|
21230
|
Use of site-directed mutagenesis to identify residues specific for each reaction catalyzed by Chorismate ...
|
21231
|
Use of site-directed mutagenesis to identify residues specific for each reaction catalyzed by Chorismate ...
|
21232
|
Use of site-directed mutagenesis to identify residues specific for each reaction catalyzed by Chorismate ...
|
21233
|
Use of site-directed mutagenesis to identify residues specific for each reaction catalyzed by Chorismate ...
|
21234
|
Use of site-directed mutagenesis to identify residues specific for each reaction catalyzed by Chorismate ...
|
21235
|
Use of site-directed mutagenesis to identify residues specific for each reaction catalyzed by Chorismate ...
|
21236
|
Use of site-directed mutagenesis to identify residues specific for each reaction catalyzed by Chorismate ...
|
21237
|
Use of site-directed mutagenesis to identify residues specific for each reaction catalyzed by Chorismate ...
|
21238
|
Use of site-directed mutagenesis to identify residues specific for each reaction catalyzed by Chorismate ...
|
21239
|
Use of site-directed mutagenesis to identify residues specific for each reaction catalyzed by Chorismate ...
|
21240
|
Use of site-directed mutagenesis to identify residues specific for each reaction catalyzed by Chorismate ...
|
21241
|
Use of site-directed mutagenesis to identify residues specific for each reaction catalyzed by Chorismate ...
|
21242
|
Use of site-directed mutagenesis to identify residues specific for each reaction catalyzed by Chorismate ...
|
21243
|
Use of site-directed mutagenesis to identify residues specific for each reaction catalyzed by Chorismate ...
|
21244
|
Use of site-directed mutagenesis to identify residues specific for each reaction catalyzed by Chorismate ...
|
21245
|
Human milk bile salt-activated lipase. Further characterization and kinetic studies
|
21246
|
Human milk bile salt-activated lipase. Further characterization and kinetic studies
|
21247
|
Human milk bile salt-activated lipase. Further characterization and kinetic studies
|
21248
|
Human milk bile salt-activated lipase. Further characterization and kinetic studies
|
21249
|
Human milk bile salt-activated lipase. Further characterization and kinetic studies
|
21250
|
Human milk bile salt-activated lipase. Further characterization and kinetic studies
|
21251
|
Human milk bile salt-activated lipase. Further characterization and kinetic studies
|
21252
|
Human milk bile salt-activated lipase. Further characterization and kinetic studies
|
21253
|
Human milk bile salt-activated lipase. Further characterization and kinetic studies
|
21254
|
Human milk bile salt-activated lipase. Further characterization and kinetic studies
|
21255
|
3-phosphoglycerate kinase from rabbit sceletal muscle and yeast
|
21256
|
3-phosphoglycerate kinase from rabbit sceletal muscle and yeast
|
21257
|
3-phosphoglycerate kinase from rabbit sceletal muscle and yeast
|
21258
|
3-phosphoglycerate kinase from rabbit sceletal muscle and yeast
|
21259
|
3-phosphoglycerate kinase from rabbit sceletal muscle and yeast
|
21260
|
3-phosphoglycerate kinase from rabbit sceletal muscle and yeast
|
21261
|
3-phosphoglycerate kinase from rabbit sceletal muscle and yeast
|
21262
|
3-phosphoglycerate kinase from rabbit sceletal muscle and yeast
|
21263
|
Mitochondrial aldehyde reductase: identification and characterization in rat liver and kidney cortex
|
21264
|
Mitochondrial aldehyde reductase: identification and characterization in rat liver and kidney cortex
|
21265
|
Mitochondrial aldehyde reductase: identification and characterization in rat liver and kidney cortex
|
21266
|
Mitochondrial aldehyde reductase: identification and characterization in rat liver and kidney cortex
|
21267
|
Mitochondrial aldehyde reductase: identification and characterization in rat liver and kidney cortex
|
21268
|
Mitochondrial aldehyde reductase: identification and characterization in rat liver and kidney cortex
|
21269
|
Mitochondrial aldehyde reductase: identification and characterization in rat liver and kidney cortex
|
21270
|
Mitochondrial aldehyde reductase: identification and characterization in rat liver and kidney cortex
|
21271
|
Mitochondrial aldehyde reductase: identification and characterization in rat liver and kidney cortex
|
21272
|
Mitochondrial aldehyde reductase: identification and characterization in rat liver and kidney cortex
|
21273
|
Mitochondrial aldehyde reductase: identification and characterization in rat liver and kidney cortex
|
21274
|
Mitochondrial aldehyde reductase: identification and characterization in rat liver and kidney cortex
|
21275
|
Location of the coenzyme binding site in the porcine mitochondrial NADP-dependent isocitrate dehydrogenase
|
21276
|
Location of the coenzyme binding site in the porcine mitochondrial NADP-dependent isocitrate dehydrogenase
|
21277
|
Location of the coenzyme binding site in the porcine mitochondrial NADP-dependent isocitrate dehydrogenase
|
21278
|
Location of the coenzyme binding site in the porcine mitochondrial NADP-dependent isocitrate dehydrogenase
|
21279
|
Location of the coenzyme binding site in the porcine mitochondrial NADP-dependent isocitrate dehydrogenase
|
21280
|
Location of the coenzyme binding site in the porcine mitochondrial NADP-dependent isocitrate dehydrogenase
|
21281
|
Location of the coenzyme binding site in the porcine mitochondrial NADP-dependent isocitrate dehydrogenase
|
21282
|
Location of the coenzyme binding site in the porcine mitochondrial NADP-dependent isocitrate dehydrogenase
|
21283
|
Location of the coenzyme binding site in the porcine mitochondrial NADP-dependent isocitrate dehydrogenase
|
21284
|
Location of the coenzyme binding site in the porcine mitochondrial NADP-dependent isocitrate dehydrogenase
|
21285
|
Location of the coenzyme binding site in the porcine mitochondrial NADP-dependent isocitrate dehydrogenase
|
21286
|
Location of the coenzyme binding site in the porcine mitochondrial NADP-dependent isocitrate dehydrogenase
|
21287
|
Location of the coenzyme binding site in the porcine mitochondrial NADP-dependent isocitrate dehydrogenase
|
21288
|
Location of the coenzyme binding site in the porcine mitochondrial NADP-dependent isocitrate dehydrogenase
|
21289
|
Location of the coenzyme binding site in the porcine mitochondrial NADP-dependent isocitrate dehydrogenase
|
21290
|
Location of the coenzyme binding site in the porcine mitochondrial NADP-dependent isocitrate dehydrogenase
|
21291
|
Location of the coenzyme binding site in the porcine mitochondrial NADP-dependent isocitrate dehydrogenase
|
21292
|
Location of the coenzyme binding site in the porcine mitochondrial NADP-dependent isocitrate dehydrogenase
|
21293
|
Location of the coenzyme binding site in the porcine mitochondrial NADP-dependent isocitrate dehydrogenase
|
21294
|
Location of the coenzyme binding site in the porcine mitochondrial NADP-dependent isocitrate dehydrogenase
|
21295
|
Location of the coenzyme binding site in the porcine mitochondrial NADP-dependent isocitrate dehydrogenase
|
21296
|
Location of the coenzyme binding site in the porcine mitochondrial NADP-dependent isocitrate dehydrogenase
|
21297
|
Location of the coenzyme binding site in the porcine mitochondrial NADP-dependent isocitrate dehydrogenase
|
21298
|
Location of the coenzyme binding site in the porcine mitochondrial NADP-dependent isocitrate dehydrogenase
|
21299
|
The presence of 2-keto-3-deoxygluconic acid and oxoaldehyde dehydrogenase activity in human erythrocytes
|
21300
|
The presence of 2-keto-3-deoxygluconic acid and oxoaldehyde dehydrogenase activity in human erythrocytes
|
21301
|
The presence of 2-keto-3-deoxygluconic acid and oxoaldehyde dehydrogenase activity in human erythrocytes
|
21302
|
Stereo-specific substrate recognition by phosphatidylinositol phosphate kinases is swapped by changing a ...
|
21303
|
Stereo-specific substrate recognition by phosphatidylinositol phosphate kinases is swapped by changing a ...
|
21304
|
Stereo-specific substrate recognition by phosphatidylinositol phosphate kinases is swapped by changing a ...
|
21305
|
Stereo-specific substrate recognition by phosphatidylinositol phosphate kinases is swapped by changing a ...
|
21306
|
Stereo-specific substrate recognition by phosphatidylinositol phosphate kinases is swapped by changing a ...
|
21307
|
Stereo-specific substrate recognition by phosphatidylinositol phosphate kinases is swapped by changing a ...
|
21308
|
Stereo-specific substrate recognition by phosphatidylinositol phosphate kinases is swapped by changing a ...
|
21309
|
Stereo-specific substrate recognition by phosphatidylinositol phosphate kinases is swapped by changing a ...
|
21310
|
Stereo-specific substrate recognition by phosphatidylinositol phosphate kinases is swapped by changing a ...
|
21311
|
Stereo-specific substrate recognition by phosphatidylinositol phosphate kinases is swapped by changing a ...
|
21312
|
Stereo-specific substrate recognition by phosphatidylinositol phosphate kinases is swapped by changing a ...
|
21313
|
Purification, characterization, and biosynthesis of human acid ceramidase
|
21314
|
Purification, characterization, and biosynthesis of human acid ceramidase
|
21315
|
Purification, characterization, and biosynthesis of human acid ceramidase
|
21316
|
Purification, characterization, and biosynthesis of human acid ceramidase
|
21317
|
Purification, characterization, and biosynthesis of human acid ceramidase
|
21318
|
Purification, characterization, and biosynthesis of human acid ceramidase
|
21319
|
Purification, characterization, and biosynthesis of human acid ceramidase
|
21320
|
Purification, characterization, and biosynthesis of human acid ceramidase
|
21321
|
Purification, characterization, and biosynthesis of human acid ceramidase
|
21322
|
Short-chain 3-hydroxy-2-methylacyl-CoA dehydrogenase from rat liver: purification and characterization of a ...
|
21323
|
Short-chain 3-hydroxy-2-methylacyl-CoA dehydrogenase from rat liver: purification and characterization of a ...
|
21324
|
Short-chain 3-hydroxy-2-methylacyl-CoA dehydrogenase from rat liver: purification and characterization of a ...
|
21325
|
Fructose metabolizing enzymes in the rat liver and metabolic parameters: Interactions between dietary copper, ...
|
21326
|
Fructose metabolizing enzymes in the rat liver and metabolic parameters: Interactions between dietary copper, ...
|
21327
|
Fructose metabolizing enzymes in the rat liver and metabolic parameters: Interactions between dietary copper, ...
|
21328
|
Fructose metabolizing enzymes in the rat liver and metabolic parameters: Interactions between dietary copper, ...
|
21329
|
Fructose metabolizing enzymes in the rat liver and metabolic parameters: Interactions between dietary copper, ...
|
21330
|
Fructose metabolizing enzymes in the rat liver and metabolic parameters: Interactions between dietary copper, ...
|
21331
|
Fructose metabolizing enzymes in the rat liver and metabolic parameters: Interactions between dietary copper, ...
|
21332
|
Fructose metabolizing enzymes in the rat liver and metabolic parameters: Interactions between dietary copper, ...
|
21333
|
Fructose metabolizing enzymes in the rat liver and metabolic parameters: Interactions between dietary copper, ...
|
21334
|
Fructose metabolizing enzymes in the rat liver and metabolic parameters: Interactions between dietary copper, ...
|
21335
|
Fructose metabolizing enzymes in the rat liver and metabolic parameters: Interactions between dietary copper, ...
|
21336
|
Fructose metabolizing enzymes in the rat liver and metabolic parameters: Interactions between dietary copper, ...
|
21337
|
Fructose metabolizing enzymes in the rat liver and metabolic parameters: Interactions between dietary copper, ...
|
21338
|
Fructose metabolizing enzymes in the rat liver and metabolic parameters: Interactions between dietary copper, ...
|
21339
|
Fructose metabolizing enzymes in the rat liver and metabolic parameters: Interactions between dietary copper, ...
|
21340
|
Fructose metabolizing enzymes in the rat liver and metabolic parameters: Interactions between dietary copper, ...
|
21341
|
Fructose metabolizing enzymes in the rat liver and metabolic parameters: Interactions between dietary copper, ...
|
21342
|
Fructose metabolizing enzymes in the rat liver and metabolic parameters: Interactions between dietary copper, ...
|
21343
|
Fructose metabolizing enzymes in the rat liver and metabolic parameters: Interactions between dietary copper, ...
|
21344
|
Fructose metabolizing enzymes in the rat liver and metabolic parameters: Interactions between dietary copper, ...
|
21345
|
Fructose metabolizing enzymes in the rat liver and metabolic parameters: Interactions between dietary copper, ...
|
21346
|
Fructose metabolizing enzymes in the rat liver and metabolic parameters: Interactions between dietary copper, ...
|
21347
|
Fructose metabolizing enzymes in the rat liver and metabolic parameters: Interactions between dietary copper, ...
|
21348
|
Fructose metabolizing enzymes in the rat liver and metabolic parameters: Interactions between dietary copper, ...
|
21349
|
Fructose metabolizing enzymes in the rat liver and metabolic parameters: Interactions between dietary copper, ...
|
21350
|
Fructose metabolizing enzymes in the rat liver and metabolic parameters: Interactions between dietary copper, ...
|
21351
|
Fructose metabolizing enzymes in the rat liver and metabolic parameters: Interactions between dietary copper, ...
|
21352
|
Fructose metabolizing enzymes in the rat liver and metabolic parameters: Interactions between dietary copper, ...
|
21353
|
Fructose metabolizing enzymes in the rat liver and metabolic parameters: Interactions between dietary copper, ...
|
21354
|
Fructose metabolizing enzymes in the rat liver and metabolic parameters: Interactions between dietary copper, ...
|
21355
|
Fructose metabolizing enzymes in the rat liver and metabolic parameters: Interactions between dietary copper, ...
|
21356
|
Fructose metabolizing enzymes in the rat liver and metabolic parameters: Interactions between dietary copper, ...
|
21357
|
Fructose metabolizing enzymes in the rat liver and metabolic parameters: Interactions between dietary copper, ...
|
21358
|
Fructose metabolizing enzymes in the rat liver and metabolic parameters: Interactions between dietary copper, ...
|
21359
|
Fructose metabolizing enzymes in the rat liver and metabolic parameters: Interactions between dietary copper, ...
|
21360
|
Fructose metabolizing enzymes in the rat liver and metabolic parameters: Interactions between dietary copper, ...
|
21361
|
Fructose metabolizing enzymes in the rat liver and metabolic parameters: Interactions between dietary copper, ...
|
21362
|
Fructose metabolizing enzymes in the rat liver and metabolic parameters: Interactions between dietary copper, ...
|
21363
|
Fructose metabolizing enzymes in the rat liver and metabolic parameters: Interactions between dietary copper, ...
|
21364
|
Fructose metabolizing enzymes in the rat liver and metabolic parameters: Interactions between dietary copper, ...
|
21365
|
Characterization of an in vivo hormonally regulated phosphodiesterase 3 (PDE3) associated with a liver ...
|
21366
|
Characterization of an in vivo hormonally regulated phosphodiesterase 3 (PDE3) associated with a liver ...
|
21367
|
Characterization of an in vivo hormonally regulated phosphodiesterase 3 (PDE3) associated with a liver ...
|
21368
|
Characterization of an in vivo hormonally regulated phosphodiesterase 3 (PDE3) associated with a liver ...
|
21369
|
Characterization of an in vivo hormonally regulated phosphodiesterase 3 (PDE3) associated with a liver ...
|
21370
|
Characterization of an in vivo hormonally regulated phosphodiesterase 3 (PDE3) associated with a liver ...
|
21371
|
Characterization of an in vivo hormonally regulated phosphodiesterase 3 (PDE3) associated with a liver ...
|
21372
|
Characterization of an in vivo hormonally regulated phosphodiesterase 3 (PDE3) associated with a liver ...
|
21373
|
Characterization of an in vivo hormonally regulated phosphodiesterase 3 (PDE3) associated with a liver ...
|
21374
|
Characterization of an in vivo hormonally regulated phosphodiesterase 3 (PDE3) associated with a liver ...
|
21375
|
Characterization of an in vivo hormonally regulated phosphodiesterase 3 (PDE3) associated with a liver ...
|
21376
|
Characterization of an in vivo hormonally regulated phosphodiesterase 3 (PDE3) associated with a liver ...
|
21377
|
Calcium sensitive isocitrate and 2-oxoglutarate dehydrogenase activities in rat liver and AS-30D hepatoma ...
|
21378
|
Calcium sensitive isocitrate and 2-oxoglutarate dehydrogenase activities in rat liver and AS-30D hepatoma ...
|
21379
|
Calcium sensitive isocitrate and 2-oxoglutarate dehydrogenase activities in rat liver and AS-30D hepatoma ...
|
21380
|
Calcium sensitive isocitrate and 2-oxoglutarate dehydrogenase activities in rat liver and AS-30D hepatoma ...
|
21381
|
Calcium sensitive isocitrate and 2-oxoglutarate dehydrogenase activities in rat liver and AS-30D hepatoma ...
|
21382
|
Calcium sensitive isocitrate and 2-oxoglutarate dehydrogenase activities in rat liver and AS-30D hepatoma ...
|
21383
|
Calcium sensitive isocitrate and 2-oxoglutarate dehydrogenase activities in rat liver and AS-30D hepatoma ...
|
21384
|
Calcium sensitive isocitrate and 2-oxoglutarate dehydrogenase activities in rat liver and AS-30D hepatoma ...
|
21385
|
Calcium sensitive isocitrate and 2-oxoglutarate dehydrogenase activities in rat liver and AS-30D hepatoma ...
|
21386
|
Calcium sensitive isocitrate and 2-oxoglutarate dehydrogenase activities in rat liver and AS-30D hepatoma ...
|
21387
|
Calcium sensitive isocitrate and 2-oxoglutarate dehydrogenase activities in rat liver and AS-30D hepatoma ...
|
21388
|
Calcium sensitive isocitrate and 2-oxoglutarate dehydrogenase activities in rat liver and AS-30D hepatoma ...
|
21389
|
D-glycerate kinase deficiency as a cause of D-glyceric aciduria
|
21390
|
D-glycerate kinase deficiency as a cause of D-glyceric aciduria
|
21391
|
D-glycerate kinase deficiency as a cause of D-glyceric aciduria
|
21392
|
D-glycerate kinase deficiency as a cause of D-glyceric aciduria
|
21393
|
D-glycerate kinase deficiency as a cause of D-glyceric aciduria
|
21394
|
D-glycerate kinase deficiency as a cause of D-glyceric aciduria
|
21395
|
D-glycerate kinase deficiency as a cause of D-glyceric aciduria
|
21396
|
D-glycerate kinase deficiency as a cause of D-glyceric aciduria
|
21397
|
D-glycerate kinase deficiency as a cause of D-glyceric aciduria
|
21398
|
D-glycerate kinase deficiency as a cause of D-glyceric aciduria
|
21399
|
Characterization of cytosolic malic enzyme in human tumor cells
|
21400
|
Characterization of cytosolic malic enzyme in human tumor cells
|
21401
|
Characterization of cytosolic malic enzyme in human tumor cells
|
21402
|
Characterization of cytosolic malic enzyme in human tumor cells
|
21403
|
Characterization of cytosolic malic enzyme in human tumor cells
|
21404
|
Characterization of cytosolic malic enzyme in human tumor cells
|
21405
|
Human NAD(+)-dependent mitochondrial malic enzyme. cDNA cloning, primary structure, and expression in ...
|
21406
|
Human NAD(+)-dependent mitochondrial malic enzyme. cDNA cloning, primary structure, and expression in ...
|
21407
|
Human NAD(+)-dependent mitochondrial malic enzyme. cDNA cloning, primary structure, and expression in ...
|
21408
|
Biosynthesis of cyclic 2,3-diphosphoglycerate. Isolation and characterization of 2-phosphoglycerate kinase and ...
|
21409
|
Biosynthesis of cyclic 2,3-diphosphoglycerate. Isolation and characterization of 2-phosphoglycerate kinase and ...
|
21410
|
Biosynthesis of cyclic 2,3-diphosphoglycerate. Isolation and characterization of 2-phosphoglycerate kinase and ...
|
21411
|
Biosynthesis of cyclic 2,3-diphosphoglycerate. Isolation and characterization of 2-phosphoglycerate kinase and ...
|
21412
|
Site-directed mutagenesis of histidine 62 in the `basic patch` region of yeast phosphoglycerate kinase
|
21413
|
Site-directed mutagenesis of histidine 62 in the `basic patch` region of yeast phosphoglycerate kinase
|
21414
|
The role of the C-terminal lysine in the hinge bending mechanism of yeast phosphoglycerate kinase
|
21415
|
The role of the C-terminal lysine in the hinge bending mechanism of yeast phosphoglycerate kinase
|
21416
|
The role of the C-terminal lysine in the hinge bending mechanism of yeast phosphoglycerate kinase
|
21417
|
The role of the C-terminal lysine in the hinge bending mechanism of yeast phosphoglycerate kinase
|
21418
|
Enzyme kinetic parameters of the fluorescent ATP analogue, 2-aminopurine triphosphate
|
21419
|
Enzyme kinetic parameters of the fluorescent ATP analogue, 2-aminopurine triphosphate
|
21420
|
Enzyme kinetic parameters of the fluorescent ATP analogue, 2-aminopurine triphosphate
|
21421
|
Enzyme kinetic parameters of the fluorescent ATP analogue, 2-aminopurine triphosphate
|
21422
|
Enzyme kinetic parameters of the fluorescent ATP analogue, 2-aminopurine triphosphate
|
21423
|
Enzyme kinetic parameters of the fluorescent ATP analogue, 2-aminopurine triphosphate
|
21424
|
Enzyme kinetic parameters of the fluorescent ATP analogue, 2-aminopurine triphosphate
|
21425
|
Enzyme kinetic parameters of the fluorescent ATP analogue, 2-aminopurine triphosphate
|
21426
|
Enzyme kinetic parameters of the fluorescent ATP analogue, 2-aminopurine triphosphate
|
21427
|
Enzyme kinetic parameters of the fluorescent ATP analogue, 2-aminopurine triphosphate
|
21428
|
Enzyme kinetic parameters of the fluorescent ATP analogue, 2-aminopurine triphosphate
|
21429
|
Enzyme kinetic parameters of the fluorescent ATP analogue, 2-aminopurine triphosphate
|
21430
|
Enzyme kinetic parameters of the fluorescent ATP analogue, 2-aminopurine triphosphate
|
21431
|
Enzyme kinetic parameters of the fluorescent ATP analogue, 2-aminopurine triphosphate
|
21432
|
Enzyme kinetic parameters of the fluorescent ATP analogue, 2-aminopurine triphosphate
|
21433
|
Enzyme kinetic parameters of the fluorescent ATP analogue, 2-aminopurine triphosphate
|
21434
|
Enzyme kinetic parameters of the fluorescent ATP analogue, 2-aminopurine triphosphate
|
21435
|
Equilibrium and kinetic studies of the pyruvic kinase reaction
|
21436
|
Equilibrium and kinetic studies of the pyruvic kinase reaction
|
21437
|
Equilibrium and kinetic studies of the pyruvic kinase reaction
|
21438
|
Equilibrium and kinetic studies of the pyruvic kinase reaction
|
21439
|
Equilibrium and kinetic studies of the pyruvic kinase reaction
|
21440
|
Equilibrium and kinetic studies of the pyruvic kinase reaction
|
21441
|
Equilibrium and kinetic studies of the pyruvic kinase reaction
|
21442
|
Equilibrium and kinetic studies of the pyruvic kinase reaction
|
21443
|
Equilibrium and kinetic studies of the pyruvic kinase reaction
|
21444
|
Equilibrium and kinetic studies of the pyruvic kinase reaction
|
21445
|
Equilibrium and kinetic studies of the pyruvic kinase reaction
|
21446
|
Equilibrium and kinetic studies of the pyruvic kinase reaction
|
21447
|
Equilibrium and kinetic studies of the pyruvic kinase reaction
|
21448
|
Equilibrium and kinetic studies of the pyruvic kinase reaction
|
21449
|
Equilibrium and kinetic studies of the pyruvic kinase reaction
|
21450
|
Equilibrium and kinetic studies of the pyruvic kinase reaction
|
21451
|
A soluble dihydrofolate reductase from human placenta: purification and properties
|
21452
|
A soluble dihydrofolate reductase from human placenta: purification and properties
|
21453
|
A soluble dihydrofolate reductase from human placenta: purification and properties
|
21454
|
A soluble dihydrofolate reductase from human placenta: purification and properties
|
21455
|
A soluble dihydrofolate reductase from human placenta: purification and properties
|
21456
|
A soluble dihydrofolate reductase from human placenta: purification and properties
|
21457
|
A soluble dihydrofolate reductase from human placenta: purification and properties
|
21458
|
A soluble dihydrofolate reductase from human placenta: purification and properties
|
21459
|
A soluble dihydrofolate reductase from human placenta: purification and properties
|
21460
|
A soluble dihydrofolate reductase from human placenta: purification and properties
|
21461
|
A soluble dihydrofolate reductase from human placenta: purification and properties
|
21462
|
A soluble dihydrofolate reductase from human placenta: purification and properties
|
21463
|
A soluble dihydrofolate reductase from human placenta: purification and properties
|
21464
|
A soluble dihydrofolate reductase from human placenta: purification and properties
|
21465
|
A soluble dihydrofolate reductase from human placenta: purification and properties
|
21466
|
A soluble dihydrofolate reductase from human placenta: purification and properties
|
21467
|
A soluble dihydrofolate reductase from human placenta: purification and properties
|
21468
|
A soluble dihydrofolate reductase from human placenta: purification and properties
|
21469
|
A soluble dihydrofolate reductase from human placenta: purification and properties
|
21470
|
A soluble dihydrofolate reductase from human placenta: purification and properties
|
21471
|
A soluble dihydrofolate reductase from human placenta: purification and properties
|
21472
|
A soluble dihydrofolate reductase from human placenta: purification and properties
|
21473
|
A soluble dihydrofolate reductase from human placenta: purification and properties
|
21474
|
A soluble dihydrofolate reductase from human placenta: purification and properties
|
21475
|
A soluble dihydrofolate reductase from human placenta: purification and properties
|
21476
|
A soluble dihydrofolate reductase from human placenta: purification and properties
|
21477
|
A soluble dihydrofolate reductase from human placenta: purification and properties
|
21478
|
A soluble dihydrofolate reductase from human placenta: purification and properties
|
21479
|
Comparative studies of the rat and pigeon liver fatty acid synthetases
|
21480
|
Modulation of the interaction between aldolase and glycerol-phosphate dehydrogenase by fructose phosphates
|
21481
|
Modulation of the interaction between aldolase and glycerol-phosphate dehydrogenase by fructose phosphates
|
21482
|
Modulation of the interaction between aldolase and glycerol-phosphate dehydrogenase by fructose phosphates
|
21483
|
Modulation of the interaction between aldolase and glycerol-phosphate dehydrogenase by fructose phosphates
|
21484
|
Modulation of the interaction between aldolase and glycerol-phosphate dehydrogenase by fructose phosphates
|
21485
|
Structural basis for the alteration of coenzyme specificity in a malate dehydrogenase mutant
|
21486
|
Structural basis for the alteration of coenzyme specificity in a malate dehydrogenase mutant
|
21487
|
Structural basis for the alteration of coenzyme specificity in a malate dehydrogenase mutant
|
21488
|
Structural basis for the alteration of coenzyme specificity in a malate dehydrogenase mutant
|
21489
|
Structural basis for the alteration of coenzyme specificity in a malate dehydrogenase mutant
|
21490
|
Structural basis for the alteration of coenzyme specificity in a malate dehydrogenase mutant
|
21491
|
Structural basis for the alteration of coenzyme specificity in a malate dehydrogenase mutant
|
21492
|
Structural basis for the alteration of coenzyme specificity in a malate dehydrogenase mutant
|
21493
|
Structural basis for the alteration of coenzyme specificity in a malate dehydrogenase mutant
|
21494
|
Structural basis for the alteration of coenzyme specificity in a malate dehydrogenase mutant
|
21495
|
Structural basis for the alteration of coenzyme specificity in a malate dehydrogenase mutant
|
21496
|
Structural basis for the alteration of coenzyme specificity in a malate dehydrogenase mutant
|
21497
|
Structural basis for the alteration of coenzyme specificity in a malate dehydrogenase mutant
|
21498
|
Structural basis for the alteration of coenzyme specificity in a malate dehydrogenase mutant
|
21499
|
Structural basis for the alteration of coenzyme specificity in a malate dehydrogenase mutant
|
21500
|
Structural basis for the alteration of coenzyme specificity in a malate dehydrogenase mutant
|
21501
|
Structural basis for the alteration of coenzyme specificity in a malate dehydrogenase mutant
|
21502
|
Structural basis for the alteration of coenzyme specificity in a malate dehydrogenase mutant
|
21503
|
Structural basis for the alteration of coenzyme specificity in a malate dehydrogenase mutant
|
21504
|
Structural basis for the alteration of coenzyme specificity in a malate dehydrogenase mutant
|
21505
|
Structural basis for the alteration of coenzyme specificity in a malate dehydrogenase mutant
|
21506
|
Structural basis for the alteration of coenzyme specificity in a malate dehydrogenase mutant
|
21507
|
Purification, characterization and molecular cloning of human hepatic lysosomal acid lipase
|
21508
|
Purification, characterization and molecular cloning of human hepatic lysosomal acid lipase
|
21509
|
Purification and properties of an NADP + -dependent glycerol dehydrogenase from rabbit skeletal muscle
|
21510
|
Purification and properties of an NADP + -dependent glycerol dehydrogenase from rabbit skeletal muscle
|
21511
|
Spectral and catalytic properties of aryl-alcohol oxidase, a fungal flavoenzyme acting on polyunsaturated ...
|
21512
|
Spectral and catalytic properties of aryl-alcohol oxidase, a fungal flavoenzyme acting on polyunsaturated ...
|
21513
|
Spectral and catalytic properties of aryl-alcohol oxidase, a fungal flavoenzyme acting on polyunsaturated ...
|
21514
|
Spectral and catalytic properties of aryl-alcohol oxidase, a fungal flavoenzyme acting on polyunsaturated ...
|
21515
|
Spectral and catalytic properties of aryl-alcohol oxidase, a fungal flavoenzyme acting on polyunsaturated ...
|
21516
|
Spectral and catalytic properties of aryl-alcohol oxidase, a fungal flavoenzyme acting on polyunsaturated ...
|
21517
|
Spectral and catalytic properties of aryl-alcohol oxidase, a fungal flavoenzyme acting on polyunsaturated ...
|
21518
|
Spectral and catalytic properties of aryl-alcohol oxidase, a fungal flavoenzyme acting on polyunsaturated ...
|
21519
|
Spectral and catalytic properties of aryl-alcohol oxidase, a fungal flavoenzyme acting on polyunsaturated ...
|
21520
|
Spectral and catalytic properties of aryl-alcohol oxidase, a fungal flavoenzyme acting on polyunsaturated ...
|
21521
|
Spectral and catalytic properties of aryl-alcohol oxidase, a fungal flavoenzyme acting on polyunsaturated ...
|
21522
|
Spectral and catalytic properties of aryl-alcohol oxidase, a fungal flavoenzyme acting on polyunsaturated ...
|
21523
|
Spectral and catalytic properties of aryl-alcohol oxidase, a fungal flavoenzyme acting on polyunsaturated ...
|
21524
|
Spectral and catalytic properties of aryl-alcohol oxidase, a fungal flavoenzyme acting on polyunsaturated ...
|
21525
|
Spectral and catalytic properties of aryl-alcohol oxidase, a fungal flavoenzyme acting on polyunsaturated ...
|
21526
|
Spectral and catalytic properties of aryl-alcohol oxidase, a fungal flavoenzyme acting on polyunsaturated ...
|
21527
|
Spectral and catalytic properties of aryl-alcohol oxidase, a fungal flavoenzyme acting on polyunsaturated ...
|
21528
|
Spectral and catalytic properties of aryl-alcohol oxidase, a fungal flavoenzyme acting on polyunsaturated ...
|
21529
|
Structure-activity relationships of 3-deoxy androgens as aromatase inhibitors. Synthesis and biochemical ...
|
21530
|
Structure-activity relationships of 3-deoxy androgens as aromatase inhibitors. Synthesis and biochemical ...
|
21531
|
Structure-activity relationships of 3-deoxy androgens as aromatase inhibitors. Synthesis and biochemical ...
|
21532
|
Structure-activity relationships of 3-deoxy androgens as aromatase inhibitors. Synthesis and biochemical ...
|
21533
|
Structure-activity relationships of 3-deoxy androgens as aromatase inhibitors. Synthesis and biochemical ...
|
21534
|
Structure-activity relationships of 3-deoxy androgens as aromatase inhibitors. Synthesis and biochemical ...
|
21535
|
Structure-activity relationships of 3-deoxy androgens as aromatase inhibitors. Synthesis and biochemical ...
|
21536
|
Structure-activity relationships of 3-deoxy androgens as aromatase inhibitors. Synthesis and biochemical ...
|
21537
|
Structure-activity relationships of 3-deoxy androgens as aromatase inhibitors. Synthesis and biochemical ...
|
21538
|
Structure-activity relationships of 3-deoxy androgens as aromatase inhibitors. Synthesis and biochemical ...
|
21539
|
Structure-activity relationships of 3-deoxy androgens as aromatase inhibitors. Synthesis and biochemical ...
|
21540
|
Structure-activity relationships of 3-deoxy androgens as aromatase inhibitors. Synthesis and biochemical ...
|
21541
|
Structure-activity relationships of 3-deoxy androgens as aromatase inhibitors. Synthesis and biochemical ...
|
21542
|
Farnesyl-diphosphate synthase is localized in peroxisomes
|
21543
|
Farnesyl-diphosphate synthase is localized in peroxisomes
|
21544
|
Farnesyl-diphosphate synthase is localized in peroxisomes
|
21545
|
Farnesyl-diphosphate synthase is localized in peroxisomes
|
21546
|
Farnesyl-diphosphate synthase is localized in peroxisomes
|
21547
|
Farnesyl-diphosphate synthase is localized in peroxisomes
|
21548
|
Farnesyl-diphosphate synthase is localized in peroxisomes
|
21549
|
Farnesyl-diphosphate synthase is localized in peroxisomes
|
21550
|
Farnesyl-diphosphate synthase is localized in peroxisomes
|
21551
|
Farnesyl-diphosphate synthase is localized in peroxisomes
|
21552
|
Farnesyl-diphosphate synthase is localized in peroxisomes
|
21553
|
Farnesyl-diphosphate synthase is localized in peroxisomes
|
21554
|
Farnesyl-diphosphate synthase is localized in peroxisomes
|
21555
|
Farnesyl-diphosphate synthase is localized in peroxisomes
|
21556
|
Farnesyl-diphosphate synthase is localized in peroxisomes
|
21557
|
Farnesyl-diphosphate synthase is localized in peroxisomes
|
21558
|
Farnesyl-diphosphate synthase is localized in peroxisomes
|
21559
|
Farnesyl-diphosphate synthase is localized in peroxisomes
|
21560
|
Purification and regulatory properties of pigeon erythrocyte pyruvate kinase.
|
21561
|
Purification and regulatory properties of pigeon erythrocyte pyruvate kinase.
|
21562
|
Purification and regulatory properties of pigeon erythrocyte pyruvate kinase.
|
21563
|
Purification and regulatory properties of pigeon erythrocyte pyruvate kinase.
|
21564
|
Two additional glutaredoxins exist in Escherichia coli: glutaredoxin 3 is a hydrogen donor for ribonucleotide ...
|
21565
|
Two additional glutaredoxins exist in Escherichia coli: glutaredoxin 3 is a hydrogen donor for ribonucleotide ...
|
21566
|
THE ENZYMES OF THE GALACTOSE OPERON IN ESCHERICHIA COLI. I. PURIFICATION AND CHARACTERIZATION OF URIDINE ...
|
21567
|
Purification and properties of the manganese-dependent phosphoglycerate mutase of Bacillus subtilis
|
21568
|
Purification and properties of the manganese-dependent phosphoglycerate mutase of Bacillus subtilis
|
21569
|
Purification and properties of the manganese-dependent phosphoglycerate mutase of Bacillus subtilis
|
21570
|
Purification and properties of the manganese-dependent phosphoglycerate mutase of Bacillus subtilis
|
21571
|
Modulation of the conformation of a membrane glycosyltransferase by specific lipids
|
21572
|
Modulation of the conformation of a membrane glycosyltransferase by specific lipids
|
21573
|
Cloning, overexpression, and characterization of glutaredoxin 2, an atypical glutaredoxin from Escherichia ...
|
21574
|
Cloning, overexpression, and characterization of glutaredoxin 2, an atypical glutaredoxin from Escherichia ...
|
21575
|
Cloning, overexpression, and characterization of glutaredoxin 2, an atypical glutaredoxin from Escherichia ...
|
21576
|
Cloning, overexpression, and characterization of glutaredoxin 2, an atypical glutaredoxin from Escherichia ...
|
21577
|
Alteration of the quaternary structure of human UDP-glucose dehydrogenase by a double mutation
|
21578
|
Alteration of the quaternary structure of human UDP-glucose dehydrogenase by a double mutation
|
21579
|
Alteration of the quaternary structure of human UDP-glucose dehydrogenase by a double mutation
|
21580
|
Alteration of the quaternary structure of human UDP-glucose dehydrogenase by a double mutation
|
21581
|
Conversion of a glutamate dehydrogenase into methionine/norleucine dehydrogenase by site-directed mutagenesis
|
21582
|
Conversion of a glutamate dehydrogenase into methionine/norleucine dehydrogenase by site-directed mutagenesis
|
21583
|
Conversion of a glutamate dehydrogenase into methionine/norleucine dehydrogenase by site-directed mutagenesis
|
21584
|
Conversion of a glutamate dehydrogenase into methionine/norleucine dehydrogenase by site-directed mutagenesis
|
21585
|
Conversion of a glutamate dehydrogenase into methionine/norleucine dehydrogenase by site-directed mutagenesis
|
21586
|
Conversion of a glutamate dehydrogenase into methionine/norleucine dehydrogenase by site-directed mutagenesis
|
21587
|
Conversion of a glutamate dehydrogenase into methionine/norleucine dehydrogenase by site-directed mutagenesis
|
21588
|
Conversion of a glutamate dehydrogenase into methionine/norleucine dehydrogenase by site-directed mutagenesis
|
21589
|
Conversion of a glutamate dehydrogenase into methionine/norleucine dehydrogenase by site-directed mutagenesis
|
21590
|
Conversion of a glutamate dehydrogenase into methionine/norleucine dehydrogenase by site-directed mutagenesis
|
21591
|
Conversion of a glutamate dehydrogenase into methionine/norleucine dehydrogenase by site-directed mutagenesis
|
21592
|
Conversion of a glutamate dehydrogenase into methionine/norleucine dehydrogenase by site-directed mutagenesis
|
21593
|
Conversion of a glutamate dehydrogenase into methionine/norleucine dehydrogenase by site-directed mutagenesis
|
21594
|
Conversion of a glutamate dehydrogenase into methionine/norleucine dehydrogenase by site-directed mutagenesis
|
21595
|
Conversion of a glutamate dehydrogenase into methionine/norleucine dehydrogenase by site-directed mutagenesis
|
21596
|
Conversion of a glutamate dehydrogenase into methionine/norleucine dehydrogenase by site-directed mutagenesis
|
21597
|
Conversion of a glutamate dehydrogenase into methionine/norleucine dehydrogenase by site-directed mutagenesis
|
21598
|
Conversion of a glutamate dehydrogenase into methionine/norleucine dehydrogenase by site-directed mutagenesis
|
21599
|
Conversion of a glutamate dehydrogenase into methionine/norleucine dehydrogenase by site-directed mutagenesis
|
21600
|
Conversion of a glutamate dehydrogenase into methionine/norleucine dehydrogenase by site-directed mutagenesis
|
21601
|
Conversion of a glutamate dehydrogenase into methionine/norleucine dehydrogenase by site-directed mutagenesis
|
21602
|
Conversion of a glutamate dehydrogenase into methionine/norleucine dehydrogenase by site-directed mutagenesis
|
21603
|
Conversion of a glutamate dehydrogenase into methionine/norleucine dehydrogenase by site-directed mutagenesis
|
21604
|
Conversion of a glutamate dehydrogenase into methionine/norleucine dehydrogenase by site-directed mutagenesis
|
21605
|
Conversion of a glutamate dehydrogenase into methionine/norleucine dehydrogenase by site-directed mutagenesis
|
21606
|
Conversion of a glutamate dehydrogenase into methionine/norleucine dehydrogenase by site-directed mutagenesis
|
21607
|
Conversion of a glutamate dehydrogenase into methionine/norleucine dehydrogenase by site-directed mutagenesis
|
21608
|
Conversion of a glutamate dehydrogenase into methionine/norleucine dehydrogenase by site-directed mutagenesis
|
21609
|
Conversion of a glutamate dehydrogenase into methionine/norleucine dehydrogenase by site-directed mutagenesis
|
21610
|
Conversion of a glutamate dehydrogenase into methionine/norleucine dehydrogenase by site-directed mutagenesis
|
21611
|
Conversion of a glutamate dehydrogenase into methionine/norleucine dehydrogenase by site-directed mutagenesis
|
21612
|
Conversion of a glutamate dehydrogenase into methionine/norleucine dehydrogenase by site-directed mutagenesis
|
21613
|
Conversion of a glutamate dehydrogenase into methionine/norleucine dehydrogenase by site-directed mutagenesis
|
21614
|
Conversion of a glutamate dehydrogenase into methionine/norleucine dehydrogenase by site-directed mutagenesis
|
21615
|
Conversion of a glutamate dehydrogenase into methionine/norleucine dehydrogenase by site-directed mutagenesis
|
21616
|
Conversion of a glutamate dehydrogenase into methionine/norleucine dehydrogenase by site-directed mutagenesis
|
21617
|
Conversion of a glutamate dehydrogenase into methionine/norleucine dehydrogenase by site-directed mutagenesis
|
21618
|
Conversion of a glutamate dehydrogenase into methionine/norleucine dehydrogenase by site-directed mutagenesis
|
21619
|
Conversion of a glutamate dehydrogenase into methionine/norleucine dehydrogenase by site-directed mutagenesis
|
21620
|
Characteristics and crystal structure of bacterial inosine-5`-monophosphate dehydrogenase
|
21621
|
Characteristics and crystal structure of bacterial inosine-5`-monophosphate dehydrogenase
|
21622
|
Characteristics and crystal structure of bacterial inosine-5`-monophosphate dehydrogenase
|
21623
|
Characteristics and crystal structure of bacterial inosine-5`-monophosphate dehydrogenase
|
21624
|
Characteristics and crystal structure of bacterial inosine-5`-monophosphate dehydrogenase
|
21625
|
A bifunctional enzyme catalyzes the first two steps in N-acetylneuraminic acid biosynthesis of rat liver. ...
|
21626
|
A bifunctional enzyme catalyzes the first two steps in N-acetylneuraminic acid biosynthesis of rat liver. ...
|
21627
|
A bifunctional enzyme catalyzes the first two steps in N-acetylneuraminic acid biosynthesis of rat liver. ...
|
21628
|
A bifunctional enzyme catalyzes the first two steps in N-acetylneuraminic acid biosynthesis of rat liver. ...
|
21629
|
A bifunctional enzyme catalyzes the first two steps in N-acetylneuraminic acid biosynthesis of rat liver. ...
|
21630
|
A bifunctional enzyme catalyzes the first two steps in N-acetylneuraminic acid biosynthesis of rat liver. ...
|
21631
|
Dramatic broadening of the substrate profile of the Aeromonas hydrophila CphA metallo-beta-lactamase by ...
|
21632
|
Dramatic broadening of the substrate profile of the Aeromonas hydrophila CphA metallo-beta-lactamase by ...
|
21633
|
Dramatic broadening of the substrate profile of the Aeromonas hydrophila CphA metallo-beta-lactamase by ...
|
21634
|
Dramatic broadening of the substrate profile of the Aeromonas hydrophila CphA metallo-beta-lactamase by ...
|
21635
|
Dramatic broadening of the substrate profile of the Aeromonas hydrophila CphA metallo-beta-lactamase by ...
|
21636
|
Dramatic broadening of the substrate profile of the Aeromonas hydrophila CphA metallo-beta-lactamase by ...
|
21637
|
Dramatic broadening of the substrate profile of the Aeromonas hydrophila CphA metallo-beta-lactamase by ...
|
21638
|
Dramatic broadening of the substrate profile of the Aeromonas hydrophila CphA metallo-beta-lactamase by ...
|
21639
|
Dramatic broadening of the substrate profile of the Aeromonas hydrophila CphA metallo-beta-lactamase by ...
|
21640
|
Dramatic broadening of the substrate profile of the Aeromonas hydrophila CphA metallo-beta-lactamase by ...
|
21641
|
Dramatic broadening of the substrate profile of the Aeromonas hydrophila CphA metallo-beta-lactamase by ...
|
21642
|
Dramatic broadening of the substrate profile of the Aeromonas hydrophila CphA metallo-beta-lactamase by ...
|
21643
|
Dramatic broadening of the substrate profile of the Aeromonas hydrophila CphA metallo-beta-lactamase by ...
|
21644
|
Dramatic broadening of the substrate profile of the Aeromonas hydrophila CphA metallo-beta-lactamase by ...
|
21645
|
Dramatic broadening of the substrate profile of the Aeromonas hydrophila CphA metallo-beta-lactamase by ...
|
21646
|
Dramatic broadening of the substrate profile of the Aeromonas hydrophila CphA metallo-beta-lactamase by ...
|
21647
|
Dramatic broadening of the substrate profile of the Aeromonas hydrophila CphA metallo-beta-lactamase by ...
|
21648
|
Dramatic broadening of the substrate profile of the Aeromonas hydrophila CphA metallo-beta-lactamase by ...
|
21649
|
Dramatic broadening of the substrate profile of the Aeromonas hydrophila CphA metallo-beta-lactamase by ...
|
21650
|
Dramatic broadening of the substrate profile of the Aeromonas hydrophila CphA metallo-beta-lactamase by ...
|
21651
|
Dramatic broadening of the substrate profile of the Aeromonas hydrophila CphA metallo-beta-lactamase by ...
|
21652
|
Dramatic broadening of the substrate profile of the Aeromonas hydrophila CphA metallo-beta-lactamase by ...
|
21653
|
Dramatic broadening of the substrate profile of the Aeromonas hydrophila CphA metallo-beta-lactamase by ...
|
21654
|
Dramatic broadening of the substrate profile of the Aeromonas hydrophila CphA metallo-beta-lactamase by ...
|
21655
|
Dramatic broadening of the substrate profile of the Aeromonas hydrophila CphA metallo-beta-lactamase by ...
|
21656
|
Dramatic broadening of the substrate profile of the Aeromonas hydrophila CphA metallo-beta-lactamase by ...
|
21657
|
Dramatic broadening of the substrate profile of the Aeromonas hydrophila CphA metallo-beta-lactamase by ...
|
21658
|
Dramatic broadening of the substrate profile of the Aeromonas hydrophila CphA metallo-beta-lactamase by ...
|
21659
|
Dramatic broadening of the substrate profile of the Aeromonas hydrophila CphA metallo-beta-lactamase by ...
|
21660
|
Dramatic broadening of the substrate profile of the Aeromonas hydrophila CphA metallo-beta-lactamase by ...
|
21661
|
Dramatic broadening of the substrate profile of the Aeromonas hydrophila CphA metallo-beta-lactamase by ...
|
21662
|
Dramatic broadening of the substrate profile of the Aeromonas hydrophila CphA metallo-beta-lactamase by ...
|
21663
|
Dramatic broadening of the substrate profile of the Aeromonas hydrophila CphA metallo-beta-lactamase by ...
|
21664
|
Dramatic broadening of the substrate profile of the Aeromonas hydrophila CphA metallo-beta-lactamase by ...
|
21665
|
Dramatic broadening of the substrate profile of the Aeromonas hydrophila CphA metallo-beta-lactamase by ...
|
21666
|
Dramatic broadening of the substrate profile of the Aeromonas hydrophila CphA metallo-beta-lactamase by ...
|
21667
|
Dramatic broadening of the substrate profile of the Aeromonas hydrophila CphA metallo-beta-lactamase by ...
|
21668
|
Membrane-bound DD-carboxypeptidase and LD-transpeptidase of Streptococcus faecalis ATCC 9790
|
21669
|
Membrane-bound DD-carboxypeptidase and LD-transpeptidase of Streptococcus faecalis ATCC 9790
|
21670
|
Membrane-bound DD-carboxypeptidase and LD-transpeptidase of Streptococcus faecalis ATCC 9790
|
21671
|
Comparison of skin esterase activities from different species
|
21672
|
Comparison of skin esterase activities from different species
|
21673
|
Comparison of skin esterase activities from different species
|
21674
|
Comparison of skin esterase activities from different species
|
21675
|
Comparison of skin esterase activities from different species
|
21676
|
Comparison of skin esterase activities from different species
|
21677
|
Comparison of skin esterase activities from different species
|
21678
|
Comparison of skin esterase activities from different species
|
21679
|
Comparison of skin esterase activities from different species
|
21680
|
Comparison of skin esterase activities from different species
|
21681
|
Comparison of skin esterase activities from different species
|
21682
|
Comparison of skin esterase activities from different species
|
21683
|
Comparison of skin esterase activities from different species
|
21684
|
Comparison of skin esterase activities from different species
|
21685
|
Comparison of skin esterase activities from different species
|
21686
|
Comparison of skin esterase activities from different species
|
21687
|
Comparison of skin esterase activities from different species
|
21688
|
Comparison of skin esterase activities from different species
|
21689
|
Comparison of skin esterase activities from different species
|
21690
|
Comparison of skin esterase activities from different species
|
21691
|
Comparison of skin esterase activities from different species
|
21692
|
Comparison of skin esterase activities from different species
|
21693
|
Comparison of skin esterase activities from different species
|
21694
|
Comparison of skin esterase activities from different species
|
21695
|
Comparison of skin esterase activities from different species
|
21696
|
Comparison of skin esterase activities from different species
|
21697
|
Comparison of skin esterase activities from different species
|
21698
|
Comparison of skin esterase activities from different species
|
21699
|
Comparison of skin esterase activities from different species
|
21700
|
Comparison of skin esterase activities from different species
|
21701
|
Comparison of skin esterase activities from different species
|
21702
|
Comparison of skin esterase activities from different species
|
21703
|
Comparison of skin esterase activities from different species
|
21704
|
Comparison of skin esterase activities from different species
|
21705
|
Comparison of skin esterase activities from different species
|
21706
|
Comparison of skin esterase activities from different species
|
21707
|
Comparison of skin esterase activities from different species
|
21708
|
Comparison of skin esterase activities from different species
|
21709
|
Comparison of skin esterase activities from different species
|
21710
|
Comparison of skin esterase activities from different species
|
21711
|
Structural basis for glutamate racemase inhibition
|
21712
|
Structural basis for glutamate racemase inhibition
|
21713
|
Importance of Gly-13 for the Coenzyme Binding of Human UDP-glucose Dehydrogenase
|
21714
|
Importance of Gly-13 for the Coenzyme Binding of Human UDP-glucose Dehydrogenase
|
21715
|
Crystallization and reaction mechanism of yeast phosphoglucomutase
|
21716
|
Molecular cloning and characterization of one member of 3beta-hydroxy sterol glucosyltransferase gene family ...
|
21717
|
Molecular cloning and characterization of one member of 3beta-hydroxy sterol glucosyltransferase gene family ...
|
21718
|
Molecular cloning and characterization of one member of 3beta-hydroxy sterol glucosyltransferase gene family ...
|
21719
|
Molecular cloning and characterization of one member of 3beta-hydroxy sterol glucosyltransferase gene family ...
|
21720
|
Molecular cloning and characterization of one member of 3beta-hydroxy sterol glucosyltransferase gene family ...
|
21721
|
Molecular cloning and characterization of one member of 3beta-hydroxy sterol glucosyltransferase gene family ...
|
21722
|
Molecular cloning and characterization of one member of 3beta-hydroxy sterol glucosyltransferase gene family ...
|
21723
|
Molecular cloning and characterization of one member of 3beta-hydroxy sterol glucosyltransferase gene family ...
|
21724
|
Molecular cloning and characterization of one member of 3beta-hydroxy sterol glucosyltransferase gene family ...
|
21725
|
Molecular cloning and characterization of one member of 3beta-hydroxy sterol glucosyltransferase gene family ...
|
21726
|
Molecular cloning and characterization of one member of 3beta-hydroxy sterol glucosyltransferase gene family ...
|
21727
|
Molecular cloning and characterization of one member of 3beta-hydroxy sterol glucosyltransferase gene family ...
|
21728
|
Molecular cloning and characterization of one member of 3beta-hydroxy sterol glucosyltransferase gene family ...
|
21729
|
Molecular cloning and characterization of one member of 3beta-hydroxy sterol glucosyltransferase gene family ...
|
21730
|
Molecular cloning and characterization of one member of 3beta-hydroxy sterol glucosyltransferase gene family ...
|
21731
|
Molecular cloning and characterization of one member of 3beta-hydroxy sterol glucosyltransferase gene family ...
|
21732
|
Molecular cloning and characterization of one member of 3beta-hydroxy sterol glucosyltransferase gene family ...
|
21733
|
Molecular cloning and characterization of one member of 3beta-hydroxy sterol glucosyltransferase gene family ...
|
21734
|
Molecular cloning and characterization of one member of 3beta-hydroxy sterol glucosyltransferase gene family ...
|
21735
|
Molecular cloning and characterization of one member of 3beta-hydroxy sterol glucosyltransferase gene family ...
|
21736
|
Molecular cloning and characterization of one member of 3beta-hydroxy sterol glucosyltransferase gene family ...
|
21737
|
Molecular cloning and characterization of one member of 3beta-hydroxy sterol glucosyltransferase gene family ...
|
21738
|
Molecular cloning and characterization of one member of 3beta-hydroxy sterol glucosyltransferase gene family ...
|
21739
|
Molecular cloning and characterization of one member of 3beta-hydroxy sterol glucosyltransferase gene family ...
|
21740
|
Properties of extracellular neuraminidase produced by group A streptococcus
|
21741
|
Purification and properties of streptococcal hyaluronate lyase
|
21742
|
Partial Reversal of the Substrate Stereospecificity of an L-Lactate Dehydrogenase by Site-Directed Mutagenesis
|
21743
|
Partial Reversal of the Substrate Stereospecificity of an L-Lactate Dehydrogenase by Site-Directed Mutagenesis
|
21744
|
Partial Reversal of the Substrate Stereospecificity of an L-Lactate Dehydrogenase by Site-Directed Mutagenesis
|
21745
|
Partial Reversal of the Substrate Stereospecificity of an L-Lactate Dehydrogenase by Site-Directed Mutagenesis
|
21746
|
Partial Reversal of the Substrate Stereospecificity of an L-Lactate Dehydrogenase by Site-Directed Mutagenesis
|
21747
|
Partial Reversal of the Substrate Stereospecificity of an L-Lactate Dehydrogenase by Site-Directed Mutagenesis
|
21748
|
Partial Reversal of the Substrate Stereospecificity of an L-Lactate Dehydrogenase by Site-Directed Mutagenesis
|
21749
|
Partial Reversal of the Substrate Stereospecificity of an L-Lactate Dehydrogenase by Site-Directed Mutagenesis
|
21750
|
Partial Reversal of the Substrate Stereospecificity of an L-Lactate Dehydrogenase by Site-Directed Mutagenesis
|
21751
|
Partial Reversal of the Substrate Stereospecificity of an L-Lactate Dehydrogenase by Site-Directed Mutagenesis
|
21752
|
Partial Reversal of the Substrate Stereospecificity of an L-Lactate Dehydrogenase by Site-Directed Mutagenesis
|
21753
|
Partial Reversal of the Substrate Stereospecificity of an L-Lactate Dehydrogenase by Site-Directed Mutagenesis
|
21754
|
Partial Reversal of the Substrate Stereospecificity of an L-Lactate Dehydrogenase by Site-Directed Mutagenesis
|
21755
|
Partial Reversal of the Substrate Stereospecificity of an L-Lactate Dehydrogenase by Site-Directed Mutagenesis
|
21756
|
Partial Reversal of the Substrate Stereospecificity of an L-Lactate Dehydrogenase by Site-Directed Mutagenesis
|
21757
|
Partial Reversal of the Substrate Stereospecificity of an L-Lactate Dehydrogenase by Site-Directed Mutagenesis
|
21758
|
Partial Reversal of the Substrate Stereospecificity of an L-Lactate Dehydrogenase by Site-Directed Mutagenesis
|
21759
|
Partial Reversal of the Substrate Stereospecificity of an L-Lactate Dehydrogenase by Site-Directed Mutagenesis
|
21760
|
Partial Reversal of the Substrate Stereospecificity of an L-Lactate Dehydrogenase by Site-Directed Mutagenesis
|
21761
|
Partial Reversal of the Substrate Stereospecificity of an L-Lactate Dehydrogenase by Site-Directed Mutagenesis
|
21762
|
Partial Reversal of the Substrate Stereospecificity of an L-Lactate Dehydrogenase by Site-Directed Mutagenesis
|
21763
|
Partial Reversal of the Substrate Stereospecificity of an L-Lactate Dehydrogenase by Site-Directed Mutagenesis
|
21764
|
Partial Reversal of the Substrate Stereospecificity of an L-Lactate Dehydrogenase by Site-Directed Mutagenesis
|
21765
|
Partial Reversal of the Substrate Stereospecificity of an L-Lactate Dehydrogenase by Site-Directed Mutagenesis
|
21766
|
Partial Reversal of the Substrate Stereospecificity of an L-Lactate Dehydrogenase by Site-Directed Mutagenesis
|
21767
|
Partial Reversal of the Substrate Stereospecificity of an L-Lactate Dehydrogenase by Site-Directed Mutagenesis
|
21768
|
Partial Reversal of the Substrate Stereospecificity of an L-Lactate Dehydrogenase by Site-Directed Mutagenesis
|
21769
|
Partial Reversal of the Substrate Stereospecificity of an L-Lactate Dehydrogenase by Site-Directed Mutagenesis
|
21770
|
Partial Reversal of the Substrate Stereospecificity of an L-Lactate Dehydrogenase by Site-Directed Mutagenesis
|
21771
|
Partial Reversal of the Substrate Stereospecificity of an L-Lactate Dehydrogenase by Site-Directed Mutagenesis
|
21772
|
Partial Reversal of the Substrate Stereospecificity of an L-Lactate Dehydrogenase by Site-Directed Mutagenesis
|
21773
|
Partial Reversal of the Substrate Stereospecificity of an L-Lactate Dehydrogenase by Site-Directed Mutagenesis
|
21774
|
Partial Reversal of the Substrate Stereospecificity of an L-Lactate Dehydrogenase by Site-Directed Mutagenesis
|
21775
|
Partial Reversal of the Substrate Stereospecificity of an L-Lactate Dehydrogenase by Site-Directed Mutagenesis
|
21776
|
Partial Reversal of the Substrate Stereospecificity of an L-Lactate Dehydrogenase by Site-Directed Mutagenesis
|
21777
|
Partial Reversal of the Substrate Stereospecificity of an L-Lactate Dehydrogenase by Site-Directed Mutagenesis
|
21778
|
Partial Reversal of the Substrate Stereospecificity of an L-Lactate Dehydrogenase by Site-Directed Mutagenesis
|
21779
|
Partial Reversal of the Substrate Stereospecificity of an L-Lactate Dehydrogenase by Site-Directed Mutagenesis
|
21780
|
Partial Reversal of the Substrate Stereospecificity of an L-Lactate Dehydrogenase by Site-Directed Mutagenesis
|
21781
|
Partial Reversal of the Substrate Stereospecificity of an L-Lactate Dehydrogenase by Site-Directed Mutagenesis
|
21782
|
Partial Reversal of the Substrate Stereospecificity of an L-Lactate Dehydrogenase by Site-Directed Mutagenesis
|
21783
|
Partial Reversal of the Substrate Stereospecificity of an L-Lactate Dehydrogenase by Site-Directed Mutagenesis
|
21784
|
The biosynthesis of cell wall lipopolysaccharide in Escherichia coli. VI. Enzymatic transfer of galactose, ...
|
21785
|
The biosynthesis of cell wall lipopolysaccharide in Escherichia coli. VI. Enzymatic transfer of galactose, ...
|
21786
|
The biosynthesis of cell wall lipopolysaccharide in Escherichia coli. VI. Enzymatic transfer of galactose, ...
|
21787
|
Studies of a phospholipid-requiring bacterial enzyme. I. Purification and properties of uridine diphosphate ...
|
21788
|
Hydrolysis of flavin-adenine dinucleotide by rat liver lysosomes
|
21789
|
Purification and partial characterization of 3-hydroxyisobutyryl-coenzyme A hydrolase of rat liver
|
21790
|
Purification and partial characterization of 3-hydroxyisobutyryl-coenzyme A hydrolase of rat liver
|
21791
|
Purification and partial characterization of 3-hydroxyisobutyryl-coenzyme A hydrolase of rat liver
|
21792
|
Purification and partial characterization of 3-hydroxyisobutyryl-coenzyme A hydrolase of rat liver
|
21793
|
Purification and partial characterization of 3-hydroxyisobutyryl-coenzyme A hydrolase of rat liver
|
21794
|
Purification and partial characterization of 3-hydroxyisobutyryl-coenzyme A hydrolase of rat liver
|
21795
|
Purification and partial characterization of 3-hydroxyisobutyryl-coenzyme A hydrolase of rat liver
|
21796
|
Purification and partial characterization of 3-hydroxyisobutyryl-coenzyme A hydrolase of rat liver
|
21797
|
Purification and partial characterization of 3-hydroxyisobutyryl-coenzyme A hydrolase of rat liver
|
21798
|
Purification and partial characterization of 3-hydroxyisobutyryl-coenzyme A hydrolase of rat liver
|
21799
|
Purification and substrate specificity of a strongly hydrophobic extracellular metalloendopeptidase ...
|
21800
|
Purification and substrate specificity of a strongly hydrophobic extracellular metalloendopeptidase ...
|
21801
|
Purification and substrate specificity of a strongly hydrophobic extracellular metalloendopeptidase ...
|
21802
|
Purification and substrate specificity of a strongly hydrophobic extracellular metalloendopeptidase ...
|
21803
|
Citrobacter diversus ULA-27 beta-lactamases. Improved purification and general properties
|
21804
|
Citrobacter diversus ULA-27 beta-lactamases. Improved purification and general properties
|
21805
|
Citrobacter diversus ULA-27 beta-lactamases. Improved purification and general properties
|
21806
|
Citrobacter diversus ULA-27 beta-lactamases. Improved purification and general properties
|
21807
|
Citrobacter diversus ULA-27 beta-lactamases. Improved purification and general properties
|
21808
|
Citrobacter diversus ULA-27 beta-lactamases. Improved purification and general properties
|
21809
|
Citrobacter diversus ULA-27 beta-lactamases. Improved purification and general properties
|
21810
|
Citrobacter diversus ULA-27 beta-lactamases. Improved purification and general properties
|
21811
|
Citrobacter diversus ULA-27 beta-lactamases. Improved purification and general properties
|
21812
|
Citrobacter diversus ULA-27 beta-lactamases. Improved purification and general properties
|
21813
|
Citrobacter diversus ULA-27 beta-lactamases. Improved purification and general properties
|
21814
|
Citrobacter diversus ULA-27 beta-lactamases. Improved purification and general properties
|
21815
|
Citrobacter diversus ULA-27 beta-lactamases. Improved purification and general properties
|
21816
|
Citrobacter diversus ULA-27 beta-lactamases. Improved purification and general properties
|
21817
|
Citrobacter diversus ULA-27 beta-lactamases. Improved purification and general properties
|
21818
|
Citrobacter diversus ULA-27 beta-lactamases. Improved purification and general properties
|
21819
|
Citrobacter diversus ULA-27 beta-lactamases. Improved purification and general properties
|
21820
|
Citrobacter diversus ULA-27 beta-lactamases. Improved purification and general properties
|
21821
|
Citrobacter diversus ULA-27 beta-lactamases. Improved purification and general properties
|
21822
|
Citrobacter diversus ULA-27 beta-lactamases. Improved purification and general properties
|
21823
|
Citrobacter diversus ULA-27 beta-lactamases. Improved purification and general properties
|
21824
|
Citrobacter diversus ULA-27 beta-lactamases. Improved purification and general properties
|
21825
|
Citrobacter diversus ULA-27 beta-lactamases. Improved purification and general properties
|
21826
|
Citrobacter diversus ULA-27 beta-lactamases. Improved purification and general properties
|
21827
|
Citrobacter diversus ULA-27 beta-lactamases. Improved purification and general properties
|
21828
|
Citrobacter diversus ULA-27 beta-lactamases. Improved purification and general properties
|
21829
|
Citrobacter diversus ULA-27 beta-lactamases. Improved purification and general properties
|
21830
|
Citrobacter diversus ULA-27 beta-lactamases. Improved purification and general properties
|
21831
|
Overexpression, purification, and characterization of the cloned metallo-beta-lactamase L1 from ...
|
21832
|
Overexpression, purification, and characterization of the cloned metallo-beta-lactamase L1 from ...
|
21833
|
Overexpression, purification, and characterization of the cloned metallo-beta-lactamase L1 from ...
|
21834
|
Overexpression, purification, and characterization of the cloned metallo-beta-lactamase L1 from ...
|
21835
|
Overexpression, purification, and characterization of the cloned metallo-beta-lactamase L1 from ...
|
21836
|
Overexpression, purification, and characterization of the cloned metallo-beta-lactamase L1 from ...
|
21837
|
Overexpression, purification, and characterization of the cloned metallo-beta-lactamase L1 from ...
|
21838
|
Overexpression, purification, and characterization of the cloned metallo-beta-lactamase L1 from ...
|
21839
|
Overexpression, purification, and characterization of the cloned metallo-beta-lactamase L1 from ...
|
21840
|
Overexpression, purification, and characterization of the cloned metallo-beta-lactamase L1 from ...
|
21841
|
Overexpression, purification, and characterization of the cloned metallo-beta-lactamase L1 from ...
|
21842
|
Overexpression, purification, and characterization of the cloned metallo-beta-lactamase L1 from ...
|
21843
|
Overexpression, purification, and characterization of the cloned metallo-beta-lactamase L1 from ...
|
21844
|
Overexpression, purification, and characterization of the cloned metallo-beta-lactamase L1 from ...
|
21845
|
Overexpression, purification, and characterization of the cloned metallo-beta-lactamase L1 from ...
|
21846
|
Overexpression, purification, and characterization of the cloned metallo-beta-lactamase L1 from ...
|
21847
|
Overexpression, purification, and characterization of the cloned metallo-beta-lactamase L1 from ...
|
21848
|
Overexpression, purification, and characterization of the cloned metallo-beta-lactamase L1 from ...
|
21849
|
Overexpression, purification, and characterization of the cloned metallo-beta-lactamase L1 from ...
|
21850
|
Overexpression, purification, and characterization of the cloned metallo-beta-lactamase L1 from ...
|
21851
|
Overexpression, purification, and characterization of the cloned metallo-beta-lactamase L1 from ...
|
21852
|
Overexpression, purification, and characterization of the cloned metallo-beta-lactamase L1 from ...
|
21853
|
Overexpression, purification, and characterization of the cloned metallo-beta-lactamase L1 from ...
|
21854
|
Overexpression, purification, and characterization of the cloned metallo-beta-lactamase L1 from ...
|
21855
|
Overexpression, purification, and characterization of the cloned metallo-beta-lactamase L1 from ...
|
21856
|
Overexpression, purification, and characterization of the cloned metallo-beta-lactamase L1 from ...
|
21857
|
Overexpression, purification, and characterization of the cloned metallo-beta-lactamase L1 from ...
|
21858
|
Overexpression, purification, and characterization of the cloned metallo-beta-lactamase L1 from ...
|
21859
|
Overexpression, purification, and characterization of the cloned metallo-beta-lactamase L1 from ...
|
21860
|
Overexpression, purification, and characterization of the cloned metallo-beta-lactamase L1 from ...
|
21861
|
Isolation and properties of highly purified glutamine transaminase
|
21862
|
Isolation and properties of highly purified glutamine transaminase
|
21863
|
Isolation and properties of highly purified glutamine transaminase
|
21864
|
Isolation and properties of highly purified glutamine transaminase
|
21865
|
Isolation and properties of highly purified glutamine transaminase
|
21866
|
Isolation and properties of highly purified glutamine transaminase
|
21867
|
Isolation and properties of highly purified glutamine transaminase
|
21868
|
Isolation and properties of highly purified glutamine transaminase
|
21869
|
Isolation and properties of highly purified glutamine transaminase
|
21870
|
Isolation and properties of highly purified glutamine transaminase
|
21871
|
ATP-sensitive and ATP-insensitive phosphofructokinase in Escherichia coli K-12
|
21872
|
ATP-sensitive and ATP-insensitive phosphofructokinase in Escherichia coli K-12
|
21873
|
ATP-sensitive and ATP-insensitive phosphofructokinase in Escherichia coli K-12
|
21874
|
ATP-sensitive and ATP-insensitive phosphofructokinase in Escherichia coli K-12
|
21875
|
ATP-sensitive and ATP-insensitive phosphofructokinase in Escherichia coli K-12
|
21876
|
Properties of malonyl-CoA decarboxylase and its relation with malonyl-CoA incorporation into fatty acids by ...
|
21877
|
Properties of malonyl-CoA decarboxylase and its relation with malonyl-CoA incorporation into fatty acids by ...
|
21878
|
Properties of malonyl-CoA decarboxylase and its relation with malonyl-CoA incorporation into fatty acids by ...
|
21879
|
Properties of malonyl-CoA decarboxylase and its relation with malonyl-CoA incorporation into fatty acids by ...
|
21880
|
Properties of malonyl-CoA decarboxylase and its relation with malonyl-CoA incorporation into fatty acids by ...
|
21881
|
Properties of malonyl-CoA decarboxylase and its relation with malonyl-CoA incorporation into fatty acids by ...
|
21882
|
Properties of malonyl-CoA decarboxylase and its relation with malonyl-CoA incorporation into fatty acids by ...
|
21883
|
Properties of malonyl-CoA decarboxylase and its relation with malonyl-CoA incorporation into fatty acids by ...
|
21884
|
Properties of malonyl-CoA decarboxylase and its relation with malonyl-CoA incorporation into fatty acids by ...
|
21885
|
Properties of malonyl-CoA decarboxylase and its relation with malonyl-CoA incorporation into fatty acids by ...
|
21886
|
Properties of malonyl-CoA decarboxylase and its relation with malonyl-CoA incorporation into fatty acids by ...
|
21887
|
Properties of malonyl-CoA decarboxylase and its relation with malonyl-CoA incorporation into fatty acids by ...
|
21888
|
Properties of malonyl-CoA decarboxylase and its relation with malonyl-CoA incorporation into fatty acids by ...
|
21889
|
Properties of malonyl-CoA decarboxylase and its relation with malonyl-CoA incorporation into fatty acids by ...
|
21890
|
Properties of malonyl-CoA decarboxylase and its relation with malonyl-CoA incorporation into fatty acids by ...
|
21891
|
Properties of malonyl-CoA decarboxylase and its relation with malonyl-CoA incorporation into fatty acids by ...
|
21892
|
Properties of malonyl-CoA decarboxylase and its relation with malonyl-CoA incorporation into fatty acids by ...
|
21893
|
Properties of malonyl-CoA decarboxylase and its relation with malonyl-CoA incorporation into fatty acids by ...
|
21894
|
Expression and enzymatic characterization of human glucose phosphate isomerase (GPI) variants accounting for ...
|
21895
|
Expression and enzymatic characterization of human glucose phosphate isomerase (GPI) variants accounting for ...
|
21896
|
Expression and enzymatic characterization of human glucose phosphate isomerase (GPI) variants accounting for ...
|
21897
|
Expression and enzymatic characterization of human glucose phosphate isomerase (GPI) variants accounting for ...
|
21898
|
Expression and enzymatic characterization of human glucose phosphate isomerase (GPI) variants accounting for ...
|
21899
|
Expression and enzymatic characterization of human glucose phosphate isomerase (GPI) variants accounting for ...
|
21900
|
Expression and enzymatic characterization of human glucose phosphate isomerase (GPI) variants accounting for ...
|
21901
|
Expression and enzymatic characterization of human glucose phosphate isomerase (GPI) variants accounting for ...
|
21902
|
Expression and enzymatic characterization of human glucose phosphate isomerase (GPI) variants accounting for ...
|
21903
|
Expression and enzymatic characterization of human glucose phosphate isomerase (GPI) variants accounting for ...
|
21904
|
Human liver aldehyde dehydrogenases: new method of purification of the major mitochondrial and cytosolic ...
|
21905
|
Human liver aldehyde dehydrogenases: new method of purification of the major mitochondrial and cytosolic ...
|
21906
|
Human liver aldehyde dehydrogenases: new method of purification of the major mitochondrial and cytosolic ...
|
21907
|
Human liver aldehyde dehydrogenases: new method of purification of the major mitochondrial and cytosolic ...
|
21908
|
Human liver aldehyde dehydrogenases: new method of purification of the major mitochondrial and cytosolic ...
|
21909
|
Human liver aldehyde dehydrogenases: new method of purification of the major mitochondrial and cytosolic ...
|
21910
|
Human liver aldehyde dehydrogenases: new method of purification of the major mitochondrial and cytosolic ...
|
21911
|
Human liver aldehyde dehydrogenases: new method of purification of the major mitochondrial and cytosolic ...
|
21912
|
Human liver aldehyde dehydrogenases: new method of purification of the major mitochondrial and cytosolic ...
|
21913
|
Human liver aldehyde dehydrogenases: new method of purification of the major mitochondrial and cytosolic ...
|
21914
|
Kinetic analysis of an inhibitor-resistant variant of the OHIO-1 beta-lactamase, an SHV-family class A enzyme
|
21915
|
Kinetic analysis of an inhibitor-resistant variant of the OHIO-1 beta-lactamase, an SHV-family class A enzyme
|
21916
|
Kinetic analysis of an inhibitor-resistant variant of the OHIO-1 beta-lactamase, an SHV-family class A enzyme
|
21917
|
Kinetic analysis of an inhibitor-resistant variant of the OHIO-1 beta-lactamase, an SHV-family class A enzyme
|
21918
|
Kinetic analysis of an inhibitor-resistant variant of the OHIO-1 beta-lactamase, an SHV-family class A enzyme
|
21919
|
Kinetic analysis of an inhibitor-resistant variant of the OHIO-1 beta-lactamase, an SHV-family class A enzyme
|
21920
|
Kinetic analysis of an inhibitor-resistant variant of the OHIO-1 beta-lactamase, an SHV-family class A enzyme
|
21921
|
Kinetic analysis of an inhibitor-resistant variant of the OHIO-1 beta-lactamase, an SHV-family class A enzyme
|
21922
|
Kinetic analysis of an inhibitor-resistant variant of the OHIO-1 beta-lactamase, an SHV-family class A enzyme
|
21923
|
Kinetic analysis of an inhibitor-resistant variant of the OHIO-1 beta-lactamase, an SHV-family class A enzyme
|
21924
|
Kinetic analysis of an inhibitor-resistant variant of the OHIO-1 beta-lactamase, an SHV-family class A enzyme
|
21925
|
Kinetic analysis of an inhibitor-resistant variant of the OHIO-1 beta-lactamase, an SHV-family class A enzyme
|
21926
|
Kinetic analysis of an inhibitor-resistant variant of the OHIO-1 beta-lactamase, an SHV-family class A enzyme
|
21927
|
Kinetic analysis of an inhibitor-resistant variant of the OHIO-1 beta-lactamase, an SHV-family class A enzyme
|
21928
|
Kinetic analysis of an inhibitor-resistant variant of the OHIO-1 beta-lactamase, an SHV-family class A enzyme
|
21929
|
Kinetic analysis of an inhibitor-resistant variant of the OHIO-1 beta-lactamase, an SHV-family class A enzyme
|
21930
|
Disequilibrium in the triose phosphate isomerase system in rat liver
|
21931
|
Disequilibrium in the triose phosphate isomerase system in rat liver
|
21932
|
Disequilibrium in the triose phosphate isomerase system in rat liver
|
21933
|
Disequilibrium in the triose phosphate isomerase system in rat liver
|
21934
|
Disequilibrium in the triose phosphate isomerase system in rat liver
|
21935
|
Disequilibrium in the triose phosphate isomerase system in rat liver
|
21936
|
Identification, purification and characterization of an acetoacetyl-CoA thiolase from rat liver peroxisomes
|
21937
|
Identification, purification and characterization of an acetoacetyl-CoA thiolase from rat liver peroxisomes
|
21938
|
Identification, purification and characterization of an acetoacetyl-CoA thiolase from rat liver peroxisomes
|
21939
|
Identification, purification and characterization of an acetoacetyl-CoA thiolase from rat liver peroxisomes
|
21940
|
Identification, purification and characterization of an acetoacetyl-CoA thiolase from rat liver peroxisomes
|
21941
|
Identification, purification and characterization of an acetoacetyl-CoA thiolase from rat liver peroxisomes
|
21942
|
The use of fluoro- and deoxy-substrate analogs to examine binding specificity and catalysis in the enzymes of ...
|
21943
|
The use of fluoro- and deoxy-substrate analogs to examine binding specificity and catalysis in the enzymes of ...
|
21944
|
The use of fluoro- and deoxy-substrate analogs to examine binding specificity and catalysis in the enzymes of ...
|
21945
|
The use of fluoro- and deoxy-substrate analogs to examine binding specificity and catalysis in the enzymes of ...
|
21946
|
The use of fluoro- and deoxy-substrate analogs to examine binding specificity and catalysis in the enzymes of ...
|
21947
|
The use of fluoro- and deoxy-substrate analogs to examine binding specificity and catalysis in the enzymes of ...
|
21948
|
The use of fluoro- and deoxy-substrate analogs to examine binding specificity and catalysis in the enzymes of ...
|
21949
|
The use of fluoro- and deoxy-substrate analogs to examine binding specificity and catalysis in the enzymes of ...
|
21950
|
The use of fluoro- and deoxy-substrate analogs to examine binding specificity and catalysis in the enzymes of ...
|
21951
|
The use of fluoro- and deoxy-substrate analogs to examine binding specificity and catalysis in the enzymes of ...
|
21952
|
The use of fluoro- and deoxy-substrate analogs to examine binding specificity and catalysis in the enzymes of ...
|
21953
|
The use of fluoro- and deoxy-substrate analogs to examine binding specificity and catalysis in the enzymes of ...
|
21954
|
The use of fluoro- and deoxy-substrate analogs to examine binding specificity and catalysis in the enzymes of ...
|
21955
|
The use of fluoro- and deoxy-substrate analogs to examine binding specificity and catalysis in the enzymes of ...
|
21956
|
The use of fluoro- and deoxy-substrate analogs to examine binding specificity and catalysis in the enzymes of ...
|
21957
|
The use of fluoro- and deoxy-substrate analogs to examine binding specificity and catalysis in the enzymes of ...
|
21958
|
The use of fluoro- and deoxy-substrate analogs to examine binding specificity and catalysis in the enzymes of ...
|
21959
|
PURIFICATION AND PROPERTIES OF N-ACETYL-D-GLUCOSAMINE KINASE FROM STREPTOCOCCUS PYOGENES
|
21960
|
PURIFICATION AND PROPERTIES OF N-ACETYL-D-GLUCOSAMINE KINASE FROM STREPTOCOCCUS PYOGENES
|
21961
|
PURIFICATION AND PROPERTIES OF N-ACETYL-D-GLUCOSAMINE KINASE FROM STREPTOCOCCUS PYOGENES
|
21962
|
PURIFICATION AND PROPERTIES OF N-ACETYL-D-GLUCOSAMINE KINASE FROM STREPTOCOCCUS PYOGENES
|
21963
|
Inducible aldehyde dehydrogenases from rat liver cytosol
|
21964
|
Inducible aldehyde dehydrogenases from rat liver cytosol
|
21965
|
Inducible aldehyde dehydrogenases from rat liver cytosol
|
21966
|
Inducible aldehyde dehydrogenases from rat liver cytosol
|
21967
|
Inducible aldehyde dehydrogenases from rat liver cytosol
|
21968
|
Inducible aldehyde dehydrogenases from rat liver cytosol
|
21969
|
Inducible aldehyde dehydrogenases from rat liver cytosol
|
21970
|
Inducible aldehyde dehydrogenases from rat liver cytosol
|
21971
|
Inducible aldehyde dehydrogenases from rat liver cytosol
|
21972
|
Inducible aldehyde dehydrogenases from rat liver cytosol
|
21973
|
Inducible aldehyde dehydrogenases from rat liver cytosol
|
21974
|
Inducible aldehyde dehydrogenases from rat liver cytosol
|
21975
|
Inducible aldehyde dehydrogenases from rat liver cytosol
|
21976
|
Inducible aldehyde dehydrogenases from rat liver cytosol
|
21977
|
Inducible aldehyde dehydrogenases from rat liver cytosol
|
21978
|
Inducible aldehyde dehydrogenases from rat liver cytosol
|
21979
|
Inducible aldehyde dehydrogenases from rat liver cytosol
|
21980
|
Inducible aldehyde dehydrogenases from rat liver cytosol
|
21981
|
Inducible aldehyde dehydrogenases from rat liver cytosol
|
21982
|
Inducible aldehyde dehydrogenases from rat liver cytosol
|
21983
|
Inducible aldehyde dehydrogenases from rat liver cytosol
|
21984
|
Inducible aldehyde dehydrogenases from rat liver cytosol
|
21985
|
Inducible aldehyde dehydrogenases from rat liver cytosol
|
21986
|
Inducible aldehyde dehydrogenases from rat liver cytosol
|
21987
|
Inducible aldehyde dehydrogenases from rat liver cytosol
|
21988
|
Inducible aldehyde dehydrogenases from rat liver cytosol
|
21989
|
Inducible aldehyde dehydrogenases from rat liver cytosol
|
21990
|
Inducible aldehyde dehydrogenases from rat liver cytosol
|
21991
|
Carbamate kinase from Enterococcus faecalis and Enterococcus faecium--cloning of the genes, studies on the ...
|
21992
|
Analysis of the kinetic mechanism of the bovine liver mitochondrial dihydroorotate dehydrogenase
|
21993
|
Analysis of the kinetic mechanism of the bovine liver mitochondrial dihydroorotate dehydrogenase
|
21994
|
Analysis of the kinetic mechanism of the bovine liver mitochondrial dihydroorotate dehydrogenase
|
21995
|
Analysis of the kinetic mechanism of the bovine liver mitochondrial dihydroorotate dehydrogenase
|
21996
|
Analysis of the kinetic mechanism of the bovine liver mitochondrial dihydroorotate dehydrogenase
|
21997
|
Analysis of the kinetic mechanism of the bovine liver mitochondrial dihydroorotate dehydrogenase
|
21998
|
Analysis of the kinetic mechanism of the bovine liver mitochondrial dihydroorotate dehydrogenase
|
21999
|
Analysis of the kinetic mechanism of the bovine liver mitochondrial dihydroorotate dehydrogenase
|
22000
|
Analysis of the kinetic mechanism of the bovine liver mitochondrial dihydroorotate dehydrogenase
|