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5001
|
Fluorinated aminoglycosides and their mechanistic implication for aminoglycoside 3`-phosphotransferases from ...
|
5002
|
Fluorinated aminoglycosides and their mechanistic implication for aminoglycoside 3`-phosphotransferases from ...
|
5003
|
Active site mutants of Drosophila melanogaster multisubstrate deoxyribonucleoside kinase
|
5004
|
Active site mutants of Drosophila melanogaster multisubstrate deoxyribonucleoside kinase
|
5005
|
Active site mutants of Drosophila melanogaster multisubstrate deoxyribonucleoside kinase
|
5006
|
Active site mutants of Drosophila melanogaster multisubstrate deoxyribonucleoside kinase
|
5007
|
Active site mutants of Drosophila melanogaster multisubstrate deoxyribonucleoside kinase
|
5008
|
Active site mutants of Drosophila melanogaster multisubstrate deoxyribonucleoside kinase
|
5009
|
Active site mutants of Drosophila melanogaster multisubstrate deoxyribonucleoside kinase
|
5010
|
Active site mutants of Drosophila melanogaster multisubstrate deoxyribonucleoside kinase
|
5011
|
The metabolism of nitrosothiols in the Mycobacteria: identification and characterization of S-nitrosomycothiol ...
|
5012
|
Mechanism of the reaction catalyzed by dehydroascorbate reductase from spinach chloroplasts
|
5013
|
Mechanism of the reaction catalyzed by dehydroascorbate reductase from spinach chloroplasts
|
5014
|
Mechanism of the reaction catalyzed by dehydroascorbate reductase from spinach chloroplasts
|
5015
|
Mechanism of the reaction catalyzed by dehydroascorbate reductase from spinach chloroplasts
|
5016
|
Catalysis and function of the p38 alpha.MK2a signaling complex
|
5017
|
Catalysis and function of the p38 alpha.MK2a signaling complex
|
5018
|
Catalysis and function of the p38 alpha.MK2a signaling complex
|
5019
|
Fatty Acid Synthetase
|
5020
|
Fatty Acid Synthetase
|
5021
|
Fatty Acid Synthetase
|
5022
|
Fatty Acid Synthetase
|
5023
|
Fatty Acid Synthetase
|
5024
|
Fatty Acid Synthetase
|
5025
|
Fatty Acid Synthetase
|
5026
|
Fatty Acid Synthetase
|
5027
|
Kinetic Studies on Pig Heart Cytoplasmic Malate Dehydrogenase
|
5028
|
Kinetic Studies on Pig Heart Cytoplasmic Malate Dehydrogenase
|
5029
|
Kinetic Studies on Pig Heart Cytoplasmic Malate Dehydrogenase
|
5030
|
Origin of Cooperativity in the Activation of Fructose-1,6-bisphosphatase by Mg2
|
5031
|
Origin of Cooperativity in the Activation of Fructose-1,6-bisphosphatase by Mg2
|
5032
|
Origin of Cooperativity in the Activation of Fructose-1,6-bisphosphatase by Mg2
|
5033
|
Origin of Cooperativity in the Activation of Fructose-1,6-bisphosphatase by Mg2
|
5034
|
Origin of Cooperativity in the Activation of Fructose-1,6-bisphosphatase by Mg2
|
5035
|
Origin of Cooperativity in the Activation of Fructose-1,6-bisphosphatase by Mg2
|
5036
|
Origin of Cooperativity in the Activation of Fructose-1,6-bisphosphatase by Mg2
|
5037
|
Origin of Cooperativity in the Activation of Fructose-1,6-bisphosphatase by Mg2
|
5038
|
Structural and kinetic analysis of catalysis by a thiamin diphosphate-dependent enzyme, benzoylformate ...
|
5039
|
Structural and kinetic analysis of catalysis by a thiamin diphosphate-dependent enzyme, benzoylformate ...
|
5040
|
Structural and kinetic analysis of catalysis by a thiamin diphosphate-dependent enzyme, benzoylformate ...
|
5041
|
Structural and kinetic analysis of catalysis by a thiamin diphosphate-dependent enzyme, benzoylformate ...
|
5042
|
Structural and kinetic analysis of catalysis by a thiamin diphosphate-dependent enzyme, benzoylformate ...
|
5043
|
Structural and kinetic analysis of catalysis by a thiamin diphosphate-dependent enzyme, benzoylformate ...
|
5044
|
Structural and kinetic analysis of catalysis by a thiamin diphosphate-dependent enzyme, benzoylformate ...
|
5045
|
Structural and kinetic analysis of catalysis by a thiamin diphosphate-dependent enzyme, benzoylformate ...
|
5046
|
Kinetic properties of human thymidylate synthase, an anticancer drug target
|
5047
|
Kinetic properties of human thymidylate synthase, an anticancer drug target
|
5048
|
Kinetic properties of human thymidylate synthase, an anticancer drug target
|
5049
|
Kinetic properties of human thymidylate synthase, an anticancer drug target
|
5050
|
Kinetic properties of human thymidylate synthase, an anticancer drug target
|
5051
|
Kinetic properties of human thymidylate synthase, an anticancer drug target
|
5052
|
Kinetic properties of human thymidylate synthase, an anticancer drug target
|
5053
|
Kinetic properties of human thymidylate synthase, an anticancer drug target
|
5054
|
High-throughput screening for potent and selective inhibitors of Plasmodium falciparum dihydroorotate ...
|
5055
|
High-throughput screening for potent and selective inhibitors of Plasmodium falciparum dihydroorotate ...
|
5056
|
High-throughput screening for potent and selective inhibitors of Plasmodium falciparum dihydroorotate ...
|
5057
|
Steady-state kinetic mechanism of Escherichia coli UDP-N-acetylenolpyruvylglucosamine reductase
|
5058
|
Steady-state kinetic mechanism of Escherichia coli UDP-N-acetylenolpyruvylglucosamine reductase
|
5059
|
Steady-state kinetic mechanism of Escherichia coli UDP-N-acetylenolpyruvylglucosamine reductase
|
5060
|
Steady-state kinetic mechanism of Escherichia coli UDP-N-acetylenolpyruvylglucosamine reductase
|
5061
|
Steady-state kinetic mechanism of Escherichia coli UDP-N-acetylenolpyruvylglucosamine reductase
|
5062
|
Steady-state kinetic mechanism of Escherichia coli UDP-N-acetylenolpyruvylglucosamine reductase
|
5063
|
Steady-state kinetic mechanism of Escherichia coli UDP-N-acetylenolpyruvylglucosamine reductase
|
5064
|
Steady-state kinetic mechanism of Escherichia coli UDP-N-acetylenolpyruvylglucosamine reductase
|
5065
|
Steady-state kinetic mechanism of Escherichia coli UDP-N-acetylenolpyruvylglucosamine reductase
|
5066
|
Steady-state kinetic mechanism of Escherichia coli UDP-N-acetylenolpyruvylglucosamine reductase
|
5067
|
Steady-state kinetic mechanism of Escherichia coli UDP-N-acetylenolpyruvylglucosamine reductase
|
5068
|
Steady-state kinetic mechanism of Escherichia coli UDP-N-acetylenolpyruvylglucosamine reductase
|
5069
|
Steady-state kinetic mechanism of Escherichia coli UDP-N-acetylenolpyruvylglucosamine reductase
|
5070
|
Steady-state kinetic mechanism of Escherichia coli UDP-N-acetylenolpyruvylglucosamine reductase
|
5071
|
Steady-state kinetic mechanism of Escherichia coli UDP-N-acetylenolpyruvylglucosamine reductase
|
5072
|
Steady-state kinetic mechanism of Escherichia coli UDP-N-acetylenolpyruvylglucosamine reductase
|
5073
|
Steady-state kinetic mechanism of Escherichia coli UDP-N-acetylenolpyruvylglucosamine reductase
|
5074
|
Steady-state kinetic mechanism of Escherichia coli UDP-N-acetylenolpyruvylglucosamine reductase
|
5075
|
Steady-state kinetic mechanism of Escherichia coli UDP-N-acetylenolpyruvylglucosamine reductase
|
5076
|
Steady-state kinetic mechanism of Escherichia coli UDP-N-acetylenolpyruvylglucosamine reductase
|
5077
|
Steady-state kinetic mechanism of Escherichia coli UDP-N-acetylenolpyruvylglucosamine reductase
|
5078
|
Steady-state kinetic mechanism of Escherichia coli UDP-N-acetylenolpyruvylglucosamine reductase
|
5079
|
Steady-state kinetic mechanism of Escherichia coli UDP-N-acetylenolpyruvylglucosamine reductase
|
5080
|
Steady-state kinetic mechanism of Escherichia coli UDP-N-acetylenolpyruvylglucosamine reductase
|
5081
|
Steady-state kinetic mechanism of Escherichia coli UDP-N-acetylenolpyruvylglucosamine reductase
|
5082
|
Steady-state kinetic mechanism of Escherichia coli UDP-N-acetylenolpyruvylglucosamine reductase
|
5083
|
Steady-state kinetic mechanism of Escherichia coli UDP-N-acetylenolpyruvylglucosamine reductase
|
5084
|
Steady-state kinetic mechanism of Escherichia coli UDP-N-acetylenolpyruvylglucosamine reductase
|
5085
|
Steady-state kinetic mechanism of Escherichia coli UDP-N-acetylenolpyruvylglucosamine reductase
|
5086
|
Steady-state kinetic mechanism of Escherichia coli UDP-N-acetylenolpyruvylglucosamine reductase
|
5087
|
Steady-state kinetic mechanism of Escherichia coli UDP-N-acetylenolpyruvylglucosamine reductase
|
5088
|
Steady-state kinetic mechanism of Escherichia coli UDP-N-acetylenolpyruvylglucosamine reductase
|
5089
|
Steady-state kinetic mechanism of Escherichia coli UDP-N-acetylenolpyruvylglucosamine reductase
|
5090
|
Steady-state kinetic mechanism of Escherichia coli UDP-N-acetylenolpyruvylglucosamine reductase
|
5091
|
Steady-state kinetic mechanism of Escherichia coli UDP-N-acetylenolpyruvylglucosamine reductase
|
5092
|
Steady-state kinetic mechanism of Escherichia coli UDP-N-acetylenolpyruvylglucosamine reductase
|
5093
|
Steady-state kinetic mechanism of Escherichia coli UDP-N-acetylenolpyruvylglucosamine reductase
|
5094
|
Steady-state kinetic mechanism of Escherichia coli UDP-N-acetylenolpyruvylglucosamine reductase
|
5095
|
Steady-state kinetic mechanism of Escherichia coli UDP-N-acetylenolpyruvylglucosamine reductase
|
5096
|
Steady-state kinetic mechanism of Escherichia coli UDP-N-acetylenolpyruvylglucosamine reductase
|
5097
|
Steady-state kinetic mechanism of Escherichia coli UDP-N-acetylenolpyruvylglucosamine reductase
|
5098
|
Steady-state kinetic mechanism of Escherichia coli UDP-N-acetylenolpyruvylglucosamine reductase
|
5099
|
Steady-state kinetic mechanism of Escherichia coli UDP-N-acetylenolpyruvylglucosamine reductase
|
5100
|
Steady-state kinetic mechanism of Escherichia coli UDP-N-acetylenolpyruvylglucosamine reductase
|
5101
|
Steady-state kinetic mechanism of Escherichia coli UDP-N-acetylenolpyruvylglucosamine reductase
|
5102
|
Steady-state kinetic mechanism of Escherichia coli UDP-N-acetylenolpyruvylglucosamine reductase
|
5103
|
Steady-state kinetic mechanism of Escherichia coli UDP-N-acetylenolpyruvylglucosamine reductase
|
5104
|
Steady-state kinetic mechanism of Escherichia coli UDP-N-acetylenolpyruvylglucosamine reductase
|
5105
|
Steady-state kinetic mechanism of Escherichia coli UDP-N-acetylenolpyruvylglucosamine reductase
|
5106
|
Steady-state kinetic mechanism of Escherichia coli UDP-N-acetylenolpyruvylglucosamine reductase
|
5107
|
Steady-state kinetic mechanism of Escherichia coli UDP-N-acetylenolpyruvylglucosamine reductase
|
5108
|
Steady-state kinetic mechanism of Escherichia coli UDP-N-acetylenolpyruvylglucosamine reductase
|
5109
|
Steady-state kinetic mechanism of Escherichia coli UDP-N-acetylenolpyruvylglucosamine reductase
|
5110
|
Steady-state kinetic mechanism of Escherichia coli UDP-N-acetylenolpyruvylglucosamine reductase
|
5111
|
Kinetic Analysis of the L-Ornithine transcarbamoylase from Pseudomonas savastanoi pv. phaseolicola That Is ...
|
5112
|
Kinetic Analysis of the L-Ornithine transcarbamoylase from Pseudomonas savastanoi pv. phaseolicola That Is ...
|
5113
|
Kinetic Analysis of the L-Ornithine transcarbamoylase from Pseudomonas savastanoi pv. phaseolicola That Is ...
|
5114
|
Kinetic Analysis of the L-Ornithine transcarbamoylase from Pseudomonas savastanoi pv. phaseolicola That Is ...
|
5115
|
Kinetic Analysis of the L-Ornithine transcarbamoylase from Pseudomonas savastanoi pv. phaseolicola That Is ...
|
5116
|
Kinetic Analysis of the L-Ornithine transcarbamoylase from Pseudomonas savastanoi pv. phaseolicola That Is ...
|
5117
|
Kinetic Analysis of the L-Ornithine transcarbamoylase from Pseudomonas savastanoi pv. phaseolicola That Is ...
|
5118
|
Kinetic Analysis of the L-Ornithine transcarbamoylase from Pseudomonas savastanoi pv. phaseolicola That Is ...
|
5119
|
Biosynthesis reaction mechanism and kinetics of deoxynucleoside triphosphates, dATP and dGTP
|
5120
|
Biosynthesis reaction mechanism and kinetics of deoxynucleoside triphosphates, dATP and dGTP
|
5121
|
Kinetic evaluation of catalase and peroxygenase activities of tyrosinase
|
5122
|
Kinetic evaluation of catalase and peroxygenase activities of tyrosinase
|
5123
|
Kinetic evaluation of catalase and peroxygenase activities of tyrosinase
|
5124
|
Kinetic evaluation of catalase and peroxygenase activities of tyrosinase
|
5125
|
Kinetic evaluation of catalase and peroxygenase activities of tyrosinase
|
5126
|
Kinetic evaluation of catalase and peroxygenase activities of tyrosinase
|
5127
|
Kinetic evaluation of catalase and peroxygenase activities of tyrosinase
|
5128
|
RNA packaging device of double-stranded RNA bacteriophages, possibly as simple as hexamer of P4 protein
|
5129
|
RNA packaging device of double-stranded RNA bacteriophages, possibly as simple as hexamer of P4 protein
|
5130
|
RNA packaging device of double-stranded RNA bacteriophages, possibly as simple as hexamer of P4 protein
|
5131
|
RNA packaging device of double-stranded RNA bacteriophages, possibly as simple as hexamer of P4 protein
|
5132
|
RNA packaging device of double-stranded RNA bacteriophages, possibly as simple as hexamer of P4 protein
|
5133
|
RNA packaging device of double-stranded RNA bacteriophages, possibly as simple as hexamer of P4 protein
|
5134
|
Mechanistic features of lignin peroxidase-catalyzed oxidation of substituted phenols and 1,2-dimethoxyarenes
|
5135
|
Mechanistic features of lignin peroxidase-catalyzed oxidation of substituted phenols and 1,2-dimethoxyarenes
|
5136
|
Mechanistic features of lignin peroxidase-catalyzed oxidation of substituted phenols and 1,2-dimethoxyarenes
|
5137
|
Mechanistic features of lignin peroxidase-catalyzed oxidation of substituted phenols and 1,2-dimethoxyarenes
|
5138
|
Mechanistic features of lignin peroxidase-catalyzed oxidation of substituted phenols and 1,2-dimethoxyarenes
|
5139
|
Mechanistic features of lignin peroxidase-catalyzed oxidation of substituted phenols and 1,2-dimethoxyarenes
|
5140
|
Mechanistic features of lignin peroxidase-catalyzed oxidation of substituted phenols and 1,2-dimethoxyarenes
|
5141
|
Mechanistic features of lignin peroxidase-catalyzed oxidation of substituted phenols and 1,2-dimethoxyarenes
|
5142
|
Mechanistic features of lignin peroxidase-catalyzed oxidation of substituted phenols and 1,2-dimethoxyarenes
|
5143
|
Mechanistic features of lignin peroxidase-catalyzed oxidation of substituted phenols and 1,2-dimethoxyarenes
|
5144
|
Mechanistic features of lignin peroxidase-catalyzed oxidation of substituted phenols and 1,2-dimethoxyarenes
|
5145
|
Mechanistic features of lignin peroxidase-catalyzed oxidation of substituted phenols and 1,2-dimethoxyarenes
|
5146
|
Mechanistic features of lignin peroxidase-catalyzed oxidation of substituted phenols and 1,2-dimethoxyarenes
|
5147
|
Mechanistic features of lignin peroxidase-catalyzed oxidation of substituted phenols and 1,2-dimethoxyarenes
|
5148
|
Mechanistic features of lignin peroxidase-catalyzed oxidation of substituted phenols and 1,2-dimethoxyarenes
|
5149
|
Mechanistic features of lignin peroxidase-catalyzed oxidation of substituted phenols and 1,2-dimethoxyarenes
|
5150
|
Mechanistic features of lignin peroxidase-catalyzed oxidation of substituted phenols and 1,2-dimethoxyarenes
|
5151
|
Mechanistic features of lignin peroxidase-catalyzed oxidation of substituted phenols and 1,2-dimethoxyarenes
|
5152
|
Mechanistic features of lignin peroxidase-catalyzed oxidation of substituted phenols and 1,2-dimethoxyarenes
|
5153
|
Mechanistic features of lignin peroxidase-catalyzed oxidation of substituted phenols and 1,2-dimethoxyarenes
|
5154
|
Mechanistic features of lignin peroxidase-catalyzed oxidation of substituted phenols and 1,2-dimethoxyarenes
|
5155
|
Mechanistic features of lignin peroxidase-catalyzed oxidation of substituted phenols and 1,2-dimethoxyarenes
|
5156
|
Mechanistic features of lignin peroxidase-catalyzed oxidation of substituted phenols and 1,2-dimethoxyarenes
|
5157
|
Mechanistic features of lignin peroxidase-catalyzed oxidation of substituted phenols and 1,2-dimethoxyarenes
|
5158
|
Mechanistic features of lignin peroxidase-catalyzed oxidation of substituted phenols and 1,2-dimethoxyarenes
|
5159
|
Mechanistic features of lignin peroxidase-catalyzed oxidation of substituted phenols and 1,2-dimethoxyarenes
|
5160
|
Mechanistic features of lignin peroxidase-catalyzed oxidation of substituted phenols and 1,2-dimethoxyarenes
|
5161
|
Mechanistic features of lignin peroxidase-catalyzed oxidation of substituted phenols and 1,2-dimethoxyarenes
|
5162
|
Mechanistic features of lignin peroxidase-catalyzed oxidation of substituted phenols and 1,2-dimethoxyarenes
|
5163
|
Mechanistic features of lignin peroxidase-catalyzed oxidation of substituted phenols and 1,2-dimethoxyarenes
|
5164
|
Mechanistic features of lignin peroxidase-catalyzed oxidation of substituted phenols and 1,2-dimethoxyarenes
|
5165
|
Mechanistic features of lignin peroxidase-catalyzed oxidation of substituted phenols and 1,2-dimethoxyarenes
|
5166
|
Characterization of the ligandin site of maize glutathione S-transferase I
|
5167
|
Characterization of the ligandin site of maize glutathione S-transferase I
|
5168
|
Characterization of the ligandin site of maize glutathione S-transferase I
|
5169
|
Characterization of the ligandin site of maize glutathione S-transferase I
|
5170
|
Characterization of the ligandin site of maize glutathione S-transferase I
|
5171
|
Characterization of the ligandin site of maize glutathione S-transferase I
|
5172
|
Characterization of the ligandin site of maize glutathione S-transferase I
|
5173
|
Characterization of the ligandin site of maize glutathione S-transferase I
|
5174
|
Characterization of the ligandin site of maize glutathione S-transferase I
|
5175
|
Characterization of the ligandin site of maize glutathione S-transferase I
|
5176
|
Characterization of the ligandin site of maize glutathione S-transferase I
|
5177
|
Characterization of the ligandin site of maize glutathione S-transferase I
|
5178
|
Characterization of the ligandin site of maize glutathione S-transferase I
|
5179
|
Characterization of the ligandin site of maize glutathione S-transferase I
|
5180
|
Characterization of the ligandin site of maize glutathione S-transferase I
|
5181
|
Characterization of the ligandin site of maize glutathione S-transferase I
|
5182
|
Characterization of the ligandin site of maize glutathione S-transferase I
|
5183
|
Characterization of the ligandin site of maize glutathione S-transferase I
|
5184
|
Identification of a factor Xa-interactive site within residues 337-372 of the factor VIII heavy chain
|
5185
|
Identification of a factor Xa-interactive site within residues 337-372 of the factor VIII heavy chain
|
5186
|
Identification of a factor Xa-interactive site within residues 337-372 of the factor VIII heavy chain
|
5187
|
Identification of a factor Xa-interactive site within residues 337-372 of the factor VIII heavy chain
|
5188
|
Kinetic Properties of the glucose-6-phosphate and 6-phosphogluconate dehydrogenases from Corynebacterium ...
|
5189
|
Kinetic Properties of the glucose-6-phosphate and 6-phosphogluconate dehydrogenases from Corynebacterium ...
|
5190
|
Kinetic Properties of the glucose-6-phosphate and 6-phosphogluconate dehydrogenases from Corynebacterium ...
|
5191
|
Kinetic Properties of the glucose-6-phosphate and 6-phosphogluconate dehydrogenases from Corynebacterium ...
|
5192
|
Kinetic Properties of the glucose-6-phosphate and 6-phosphogluconate dehydrogenases from Corynebacterium ...
|
5193
|
Kinetic Properties of the glucose-6-phosphate and 6-phosphogluconate dehydrogenases from Corynebacterium ...
|
5194
|
Kinetic Properties of the glucose-6-phosphate and 6-phosphogluconate dehydrogenases from Corynebacterium ...
|
5195
|
Kinetic Properties of the glucose-6-phosphate and 6-phosphogluconate dehydrogenases from Corynebacterium ...
|
5196
|
Kinetic Properties of the glucose-6-phosphate and 6-phosphogluconate dehydrogenases from Corynebacterium ...
|
5197
|
Kinetic Properties of the glucose-6-phosphate and 6-phosphogluconate dehydrogenases from Corynebacterium ...
|
5198
|
Kinetic Properties of the glucose-6-phosphate and 6-phosphogluconate dehydrogenases from Corynebacterium ...
|
5199
|
Kinetic Properties of the glucose-6-phosphate and 6-phosphogluconate dehydrogenases from Corynebacterium ...
|
5200
|
Kinetic Properties of the glucose-6-phosphate and 6-phosphogluconate dehydrogenases from Corynebacterium ...
|
5201
|
Kinetic Properties of the glucose-6-phosphate and 6-phosphogluconate dehydrogenases from Corynebacterium ...
|
5202
|
Kinetic Properties of the glucose-6-phosphate and 6-phosphogluconate dehydrogenases from Corynebacterium ...
|
5203
|
Kinetic Properties of the glucose-6-phosphate and 6-phosphogluconate dehydrogenases from Corynebacterium ...
|
5204
|
Kinetic Properties of the glucose-6-phosphate and 6-phosphogluconate dehydrogenases from Corynebacterium ...
|
5205
|
Kinetic Properties of the glucose-6-phosphate and 6-phosphogluconate dehydrogenases from Corynebacterium ...
|
5227
|
Kinetic studies of rat liver hekokinase D('glucokinase') in non-co-operative conditions show an ordered ...
|
5228
|
Kinetic studies of rat liver hekokinase D('glucokinase') in non-co-operative conditions show an ordered ...
|
5229
|
Kinetic studies of rat liver hekokinase D('glucokinase') in non-co-operative conditions show an ordered ...
|
5230
|
Kinetic studies of rat liver hekokinase D('glucokinase') in non-co-operative conditions show an ordered ...
|
5231
|
Kinetic studies of rat liver hekokinase D('glucokinase') in non-co-operative conditions show an ordered ...
|
5232
|
Kinetic studies of rat liver hekokinase D('glucokinase') in non-co-operative conditions show an ordered ...
|
5233
|
Kinetic studies of rat liver hekokinase D('glucokinase') in non-co-operative conditions show an ordered ...
|
5234
|
Kinetic studies of rat liver hekokinase D('glucokinase') in non-co-operative conditions show an ordered ...
|
5235
|
Involvement of the chicken liver 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase sequence ...
|
5236
|
Involvement of the chicken liver 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase sequence ...
|
5237
|
Involvement of the chicken liver 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase sequence ...
|
5238
|
Involvement of the chicken liver 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase sequence ...
|
5239
|
Involvement of the chicken liver 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase sequence ...
|
5240
|
Involvement of the chicken liver 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase sequence ...
|
5241
|
Involvement of the chicken liver 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase sequence ...
|
5242
|
Involvement of the chicken liver 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase sequence ...
|
5243
|
Involvement of the chicken liver 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase sequence ...
|
5244
|
Involvement of the chicken liver 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase sequence ...
|
5245
|
Involvement of the chicken liver 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase sequence ...
|
5246
|
Involvement of the chicken liver 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase sequence ...
|
5247
|
Involvement of the chicken liver 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase sequence ...
|
5248
|
Involvement of the chicken liver 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase sequence ...
|
5249
|
Involvement of the chicken liver 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase sequence ...
|
5250
|
Involvement of the chicken liver 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase sequence ...
|
5251
|
Involvement of the chicken liver 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase sequence ...
|
5252
|
Involvement of the chicken liver 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase sequence ...
|
5253
|
Involvement of the chicken liver 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase sequence ...
|
5254
|
Involvement of the chicken liver 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase sequence ...
|
5255
|
Involvement of the chicken liver 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase sequence ...
|
5256
|
Involvement of the chicken liver 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase sequence ...
|
5257
|
Involvement of the chicken liver 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase sequence ...
|
5258
|
Involvement of the chicken liver 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase sequence ...
|
5259
|
Involvement of the chicken liver 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase sequence ...
|
5260
|
Involvement of the chicken liver 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase sequence ...
|
5261
|
Involvement of the chicken liver 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase sequence ...
|
5262
|
Involvement of the chicken liver 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase sequence ...
|
5263
|
Involvement of the chicken liver 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase sequence ...
|
5264
|
Involvement of the chicken liver 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase sequence ...
|
5265
|
Involvement of the chicken liver 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase sequence ...
|
5266
|
Involvement of the chicken liver 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase sequence ...
|
5267
|
Involvement of the chicken liver 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase sequence ...
|
5268
|
Involvement of the chicken liver 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase sequence ...
|
5269
|
Involvement of the chicken liver 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase sequence ...
|
5270
|
Involvement of the chicken liver 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase sequence ...
|
5271
|
Involvement of the chicken liver 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase sequence ...
|
5272
|
Involvement of the chicken liver 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase sequence ...
|
5273
|
Involvement of the chicken liver 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase sequence ...
|
5274
|
Involvement of the chicken liver 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase sequence ...
|
5275
|
Involvement of the chicken liver 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase sequence ...
|
5276
|
Involvement of the chicken liver 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase sequence ...
|
5277
|
Involvement of the chicken liver 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase sequence ...
|
5278
|
Involvement of the chicken liver 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase sequence ...
|
5279
|
Involvement of the chicken liver 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase sequence ...
|
5280
|
Involvement of the chicken liver 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase sequence ...
|
5281
|
Involvement of the chicken liver 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase sequence ...
|
5282
|
Involvement of the chicken liver 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase sequence ...
|
5283
|
Involvement of the chicken liver 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase sequence ...
|
5284
|
Involvement of the chicken liver 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase sequence ...
|
5285
|
Involvement of the chicken liver 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase sequence ...
|
5286
|
Involvement of the chicken liver 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase sequence ...
|
5287
|
Involvement of the chicken liver 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase sequence ...
|
5288
|
Involvement of the chicken liver 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase sequence ...
|
5289
|
Involvement of the chicken liver 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase sequence ...
|
5290
|
Involvement of the chicken liver 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase sequence ...
|
5291
|
Involvement of the chicken liver 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase sequence ...
|
5292
|
Involvement of the chicken liver 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase sequence ...
|
5293
|
Involvement of the chicken liver 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase sequence ...
|
5294
|
Involvement of the chicken liver 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase sequence ...
|
5295
|
Involvement of the chicken liver 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase sequence ...
|
5296
|
Involvement of the chicken liver 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase sequence ...
|
5297
|
Involvement of the chicken liver 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase sequence ...
|
5298
|
Involvement of the chicken liver 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase sequence ...
|
5299
|
Involvement of the chicken liver 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase sequence ...
|
5300
|
Involvement of the chicken liver 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase sequence ...
|
5301
|
Involvement of the chicken liver 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase sequence ...
|
5302
|
Involvement of the chicken liver 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase sequence ...
|
5303
|
Involvement of the chicken liver 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase sequence ...
|
5304
|
Involvement of the chicken liver 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase sequence ...
|
5305
|
Involvement of the chicken liver 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase sequence ...
|
5306
|
Involvement of the chicken liver 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase sequence ...
|
5307
|
Involvement of the chicken liver 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase sequence ...
|
5308
|
Involvement of the chicken liver 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase sequence ...
|
5309
|
Involvement of the chicken liver 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase sequence ...
|
5310
|
Involvement of the chicken liver 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase sequence ...
|
5311
|
Involvement of the chicken liver 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase sequence ...
|
5312
|
Involvement of the chicken liver 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase sequence ...
|
5313
|
How does Pseudomonas fluorescens avoid suicide from its antibiotic pseudomonic acid?: Evidence for two ...
|
5314
|
How does Pseudomonas fluorescens avoid suicide from its antibiotic pseudomonic acid?: Evidence for two ...
|
5315
|
How does Pseudomonas fluorescens avoid suicide from its antibiotic pseudomonic acid?: Evidence for two ...
|
5316
|
Reaction mechanism of the heterotetrameric (alpha2beta2) E1 component of 2-oxo acid dehydrogenase multienzyme ...
|
5317
|
Reaction mechanism of the heterotetrameric (alpha2beta2) E1 component of 2-oxo acid dehydrogenase multienzyme ...
|
5318
|
Purification and characterization of rat skeletal muscle ...
|
5319
|
Purification and characterization of rat skeletal muscle ...
|
5320
|
Differences in kinetic properties of phospho and dephospho forms of fructose-6-phosphate, 2-kinase and ...
|
5321
|
Differences in kinetic properties of phospho and dephospho forms of fructose-6-phosphate, 2-kinase and ...
|
5322
|
Differences in kinetic properties of phospho and dephospho forms of fructose-6-phosphate, 2-kinase and ...
|
5323
|
Differences in kinetic properties of phospho and dephospho forms of fructose-6-phosphate, 2-kinase and ...
|
5324
|
Differences in kinetic properties of phospho and dephospho forms of fructose-6-phosphate, 2-kinase and ...
|
5325
|
Differences in kinetic properties of phospho and dephospho forms of fructose-6-phosphate, 2-kinase and ...
|
5326
|
Differences in kinetic properties of phospho and dephospho forms of fructose-6-phosphate, 2-kinase and ...
|
5327
|
Differences in kinetic properties of phospho and dephospho forms of fructose-6-phosphate, 2-kinase and ...
|
5328
|
Differences in kinetic properties of phospho and dephospho forms of fructose-6-phosphate, 2-kinase and ...
|
5329
|
L-threonine dehydrogenase. Purification and properties of the homogeneous enzyme from Escherichia coli K-12
|
5330
|
L-threonine dehydrogenase. Purification and properties of the homogeneous enzyme from Escherichia coli K-12
|
5331
|
L-threonine dehydrogenase. Purification and properties of the homogeneous enzyme from Escherichia coli K-12
|
5332
|
L-threonine dehydrogenase. Purification and properties of the homogeneous enzyme from Escherichia coli K-12
|
5333
|
L-threonine dehydrogenase. Purification and properties of the homogeneous enzyme from Escherichia coli K-12
|
5334
|
L-threonine dehydrogenase. Purification and properties of the homogeneous enzyme from Escherichia coli K-12
|
5335
|
L-threonine dehydrogenase. Purification and properties of the homogeneous enzyme from Escherichia coli K-12
|
5336
|
L-threonine dehydrogenase. Purification and properties of the homogeneous enzyme from Escherichia coli K-12
|
5337
|
Structural, kinetic and calorimetric charecterization of the cold-active phosphoglycerate kinase from the ...
|
5338
|
Structural, kinetic and calorimetric charecterization of the cold-active phosphoglycerate kinase from the ...
|
5339
|
Structural, kinetic and calorimetric charecterization of the cold-active phosphoglycerate kinase from the ...
|
5340
|
Structural, kinetic and calorimetric charecterization of the cold-active phosphoglycerate kinase from the ...
|
5341
|
General base catalysis in the urate oxidase reaction: evidence for a novel Thr-Lys catalytic diad
|
5342
|
General base catalysis in the urate oxidase reaction: evidence for a novel Thr-Lys catalytic diad
|
5343
|
General base catalysis in the urate oxidase reaction: evidence for a novel Thr-Lys catalytic diad
|
5344
|
General base catalysis in the urate oxidase reaction: evidence for a novel Thr-Lys catalytic diad
|
5345
|
General base catalysis in the urate oxidase reaction: evidence for a novel Thr-Lys catalytic diad
|
5346
|
General base catalysis in the urate oxidase reaction: evidence for a novel Thr-Lys catalytic diad
|
5347
|
The catalytic role of the distal site asparagine-histidine couple in catalase-peroxidases
|
5348
|
The catalytic role of the distal site asparagine-histidine couple in catalase-peroxidases
|
5349
|
The catalytic role of the distal site asparagine-histidine couple in catalase-peroxidases
|
5350
|
Mutational analysis of the conserved cationic residues of Bacillus stearothermophilus 6-phosphoglucose ...
|
5351
|
Mutational analysis of the conserved cationic residues of Bacillus stearothermophilus 6-phosphoglucose ...
|
5352
|
Mutational analysis of the conserved cationic residues of Bacillus stearothermophilus 6-phosphoglucose ...
|
5353
|
Mutational analysis of the conserved cationic residues of Bacillus stearothermophilus 6-phosphoglucose ...
|
5354
|
Mutational analysis of the conserved cationic residues of Bacillus stearothermophilus 6-phosphoglucose ...
|
5355
|
Mutational analysis of the conserved cationic residues of Bacillus stearothermophilus 6-phosphoglucose ...
|
5356
|
Mutational analysis of the conserved cationic residues of Bacillus stearothermophilus 6-phosphoglucose ...
|
5357
|
Mutational analysis of the conserved cationic residues of Bacillus stearothermophilus 6-phosphoglucose ...
|
5358
|
Mutational analysis of the conserved cationic residues of Bacillus stearothermophilus 6-phosphoglucose ...
|
5359
|
Mutational analysis of the conserved cationic residues of Bacillus stearothermophilus 6-phosphoglucose ...
|
5360
|
Mutational analysis of the conserved cationic residues of Bacillus stearothermophilus 6-phosphoglucose ...
|
5361
|
Vibrationally enhanced hydrogen tunneling in the Escherichia coli thymidylate synthase catalyzed reaction
|
5362
|
Sulfaphenazole derivatives as tools for comparing cytochrome P450 2C5 and human cytochromes P450 2Cs: ...
|
5363
|
Sulfaphenazole derivatives as tools for comparing cytochrome P450 2C5 and human cytochromes P450 2Cs: ...
|
5364
|
Sulfaphenazole derivatives as tools for comparing cytochrome P450 2C5 and human cytochromes P450 2Cs: ...
|
5365
|
Sulfaphenazole derivatives as tools for comparing cytochrome P450 2C5 and human cytochromes P450 2Cs: ...
|
5366
|
Sulfaphenazole derivatives as tools for comparing cytochrome P450 2C5 and human cytochromes P450 2Cs: ...
|
5367
|
Sulfaphenazole derivatives as tools for comparing cytochrome P450 2C5 and human cytochromes P450 2Cs: ...
|
5368
|
Sulfaphenazole derivatives as tools for comparing cytochrome P450 2C5 and human cytochromes P450 2Cs: ...
|
5369
|
Sulfaphenazole derivatives as tools for comparing cytochrome P450 2C5 and human cytochromes P450 2Cs: ...
|
5370
|
Sulfaphenazole derivatives as tools for comparing cytochrome P450 2C5 and human cytochromes P450 2Cs: ...
|
5371
|
Sulfaphenazole derivatives as tools for comparing cytochrome P450 2C5 and human cytochromes P450 2Cs: ...
|
5372
|
Sulfaphenazole derivatives as tools for comparing cytochrome P450 2C5 and human cytochromes P450 2Cs: ...
|
5373
|
Sulfaphenazole derivatives as tools for comparing cytochrome P450 2C5 and human cytochromes P450 2Cs: ...
|
5374
|
Structural basis for the altered activity of Gly794 variants of Escherichia coli beta-galactosidase
|
5375
|
Structural basis for the altered activity of Gly794 variants of Escherichia coli beta-galactosidase
|
5376
|
Structural basis for the altered activity of Gly794 variants of Escherichia coli beta-galactosidase
|
5377
|
Structural basis for the altered activity of Gly794 variants of Escherichia coli beta-galactosidase
|
5378
|
Structural basis for the altered activity of Gly794 variants of Escherichia coli beta-galactosidase
|
5379
|
Structural basis for the altered activity of Gly794 variants of Escherichia coli beta-galactosidase
|
5380
|
Structural basis for the altered activity of Gly794 variants of Escherichia coli beta-galactosidase
|
5381
|
Structural basis for the altered activity of Gly794 variants of Escherichia coli beta-galactosidase
|
5382
|
Structural basis for the altered activity of Gly794 variants of Escherichia coli beta-galactosidase
|
5383
|
Structural basis for the altered activity of Gly794 variants of Escherichia coli beta-galactosidase
|
5384
|
Structural basis for the altered activity of Gly794 variants of Escherichia coli beta-galactosidase
|
5385
|
Structural basis for the altered activity of Gly794 variants of Escherichia coli beta-galactosidase
|
5386
|
Structural basis for the altered activity of Gly794 variants of Escherichia coli beta-galactosidase
|
5387
|
Structural basis for the altered activity of Gly794 variants of Escherichia coli beta-galactosidase
|
5388
|
Structural basis for the altered activity of Gly794 variants of Escherichia coli beta-galactosidase
|
5389
|
Structural basis for the altered activity of Gly794 variants of Escherichia coli beta-galactosidase
|
5390
|
Structural basis for the altered activity of Gly794 variants of Escherichia coli beta-galactosidase
|
5391
|
Structural basis for the altered activity of Gly794 variants of Escherichia coli beta-galactosidase
|
5392
|
Structural basis for the altered activity of Gly794 variants of Escherichia coli beta-galactosidase
|
5393
|
Structural basis for the altered activity of Gly794 variants of Escherichia coli beta-galactosidase
|
5394
|
Structural basis for the altered activity of Gly794 variants of Escherichia coli beta-galactosidase
|
5395
|
Structural basis for the altered activity of Gly794 variants of Escherichia coli beta-galactosidase
|
5396
|
Structural basis for the altered activity of Gly794 variants of Escherichia coli beta-galactosidase
|
5397
|
Structural basis for the altered activity of Gly794 variants of Escherichia coli beta-galactosidase
|
5398
|
Structural basis for the altered activity of Gly794 variants of Escherichia coli beta-galactosidase
|
5399
|
Structural basis for the altered activity of Gly794 variants of Escherichia coli beta-galactosidase
|
5400
|
Structural basis for the altered activity of Gly794 variants of Escherichia coli beta-galactosidase
|
5401
|
Structural basis for the altered activity of Gly794 variants of Escherichia coli beta-galactosidase
|
5402
|
Structural basis for the altered activity of Gly794 variants of Escherichia coli beta-galactosidase
|
5403
|
Structural basis for the altered activity of Gly794 variants of Escherichia coli beta-galactosidase
|
5404
|
Structural basis for the altered activity of Gly794 variants of Escherichia coli beta-galactosidase
|
5405
|
Structural basis for the altered activity of Gly794 variants of Escherichia coli beta-galactosidase
|
5406
|
Structural basis for the altered activity of Gly794 variants of Escherichia coli beta-galactosidase
|
5407
|
Structural basis for the altered activity of Gly794 variants of Escherichia coli beta-galactosidase
|
5408
|
Structural basis for the altered activity of Gly794 variants of Escherichia coli beta-galactosidase
|
5409
|
Structural basis for the altered activity of Gly794 variants of Escherichia coli beta-galactosidase
|
5410
|
Structural basis for the altered activity of Gly794 variants of Escherichia coli beta-galactosidase
|
5411
|
Structural basis for the altered activity of Gly794 variants of Escherichia coli beta-galactosidase
|
5412
|
Structural basis for the altered activity of Gly794 variants of Escherichia coli beta-galactosidase
|
5413
|
Structural basis for the altered activity of Gly794 variants of Escherichia coli beta-galactosidase
|
5414
|
Structural basis for the altered activity of Gly794 variants of Escherichia coli beta-galactosidase
|
5415
|
Structural basis for the altered activity of Gly794 variants of Escherichia coli beta-galactosidase
|
5416
|
Positional isotope exchange analysis of the pantothenate synthetase reaction
|
5417
|
Mutation and evolution of the magnesium-binding site of a class II aminoacyl-tRNA synthetase
|
5418
|
Mutation and evolution of the magnesium-binding site of a class II aminoacyl-tRNA synthetase
|
5419
|
Mutation and evolution of the magnesium-binding site of a class II aminoacyl-tRNA synthetase
|
5420
|
Mutation and evolution of the magnesium-binding site of a class II aminoacyl-tRNA synthetase
|
5421
|
Mutation and evolution of the magnesium-binding site of a class II aminoacyl-tRNA synthetase
|
5422
|
Mutation and evolution of the magnesium-binding site of a class II aminoacyl-tRNA synthetase
|
5423
|
Mutation and evolution of the magnesium-binding site of a class II aminoacyl-tRNA synthetase
|
5424
|
Mutation and evolution of the magnesium-binding site of a class II aminoacyl-tRNA synthetase
|
5425
|
Mutation and evolution of the magnesium-binding site of a class II aminoacyl-tRNA synthetase
|
5426
|
Mutation and evolution of the magnesium-binding site of a class II aminoacyl-tRNA synthetase
|
5427
|
Mutation and evolution of the magnesium-binding site of a class II aminoacyl-tRNA synthetase
|
5428
|
Mutation and evolution of the magnesium-binding site of a class II aminoacyl-tRNA synthetase
|
5429
|
Kinetic characterization of thiolate anion formation and chemical catalysis of activated microsomal ...
|
5430
|
Kinetic characterization of thiolate anion formation and chemical catalysis of activated microsomal ...
|
5431
|
Kinetic characterization of thiolate anion formation and chemical catalysis of activated microsomal ...
|
5432
|
Kinetic characterization of thiolate anion formation and chemical catalysis of activated microsomal ...
|
5433
|
Kinetic characterization of thiolate anion formation and chemical catalysis of activated microsomal ...
|
5434
|
Kinetic characterization of thiolate anion formation and chemical catalysis of activated microsomal ...
|
5435
|
Kinetic characterization of thiolate anion formation and chemical catalysis of activated microsomal ...
|
5436
|
Kinetic characterization of thiolate anion formation and chemical catalysis of activated microsomal ...
|
5437
|
S-methylmethionine is both a substrate and an inactivator of 1-aminocyclopropane-1-carboxylate synthase
|
5438
|
S-methylmethionine is both a substrate and an inactivator of 1-aminocyclopropane-1-carboxylate synthase
|
5439
|
Expression and regulation of 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase isoenzymes white adipose ...
|
5440
|
Expression and regulation of 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase isoenzymes white adipose ...
|
5441
|
Expression and regulation of 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase isoenzymes white adipose ...
|
5442
|
Expression and regulation of 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase isoenzymes white adipose ...
|
5443
|
Allosteric inhibition of PTP1B activity by selective modification of a non-active site cysteine residue
|
5444
|
Allosteric inhibition of PTP1B activity by selective modification of a non-active site cysteine residue
|
5445
|
Kinetic inactivation study of mushroom tyrosinase: intermediate detection by denaturants
|
5446
|
Kinetic inactivation study of mushroom tyrosinase: intermediate detection by denaturants
|
5447
|
Kinetic inactivation study of mushroom tyrosinase: intermediate detection by denaturants
|
5448
|
The deoxyfluoro-D-glucopyranose 6-phosphates and their effect on yeast glucose phosphate isomerase
|
5449
|
The deoxyfluoro-D-glucopyranose 6-phosphates and their effect on yeast glucose phosphate isomerase
|
5450
|
The deoxyfluoro-D-glucopyranose 6-phosphates and their effect on yeast glucose phosphate isomerase
|
5451
|
The deoxyfluoro-D-glucopyranose 6-phosphates and their effect on yeast glucose phosphate isomerase
|
5452
|
The deoxyfluoro-D-glucopyranose 6-phosphates and their effect on yeast glucose phosphate isomerase
|
5453
|
The deoxyfluoro-D-glucopyranose 6-phosphates and their effect on yeast glucose phosphate isomerase
|
5454
|
The deoxyfluoro-D-glucopyranose 6-phosphates and their effect on yeast glucose phosphate isomerase
|
5455
|
The severe acute respiratory syndrome (SARS) coronavirus NTPase/helicase belongs to a distinct class of 5` to ...
|
5456
|
The severe acute respiratory syndrome (SARS) coronavirus NTPase/helicase belongs to a distinct class of 5` to ...
|
5457
|
The severe acute respiratory syndrome (SARS) coronavirus NTPase/helicase belongs to a distinct class of 5` to ...
|
5458
|
The severe acute respiratory syndrome (SARS) coronavirus NTPase/helicase belongs to a distinct class of 5` to ...
|
5459
|
The severe acute respiratory syndrome (SARS) coronavirus NTPase/helicase belongs to a distinct class of 5` to ...
|
5460
|
The severe acute respiratory syndrome (SARS) coronavirus NTPase/helicase belongs to a distinct class of 5` to ...
|
5461
|
The severe acute respiratory syndrome (SARS) coronavirus NTPase/helicase belongs to a distinct class of 5` to ...
|
5462
|
The severe acute respiratory syndrome (SARS) coronavirus NTPase/helicase belongs to a distinct class of 5` to ...
|
5463
|
Reactivity study on microperoxidase-8
|
5464
|
Reactivity study on microperoxidase-8
|
5465
|
Oxidation of 2,4-dichlorophenol catalyzed by horseradish peroxidase: characterization of the reaction ...
|
5466
|
Oxidation of 2,4-dichlorophenol catalyzed by horseradish peroxidase: characterization of the reaction ...
|
5467
|
A variant of rabbit phosphoglucose isomerase
|
5468
|
A variant of rabbit phosphoglucose isomerase
|
5469
|
A variant of rabbit phosphoglucose isomerase
|
5470
|
A variant of rabbit phosphoglucose isomerase
|
5471
|
Astrocytic glucose-6-phosphatase and the permeability of brain microsomes to glucose 6-phosphate
|
5472
|
Astrocytic glucose-6-phosphatase and the permeability of brain microsomes to glucose 6-phosphate
|
5473
|
Astrocytic glucose-6-phosphatase and the permeability of brain microsomes to glucose 6-phosphate
|
5474
|
Astrocytic glucose-6-phosphatase and the permeability of brain microsomes to glucose 6-phosphate
|
5475
|
Crystal structure of extended-spectrum beta-lactamase Toho-1: insights into the molecular mechanism for ...
|
5476
|
Crystal structure of extended-spectrum beta-lactamase Toho-1: insights into the molecular mechanism for ...
|
5477
|
Crystal structure of extended-spectrum beta-lactamase Toho-1: insights into the molecular mechanism for ...
|
5478
|
Crystal structure of extended-spectrum beta-lactamase Toho-1: insights into the molecular mechanism for ...
|
5479
|
Crystal structure of extended-spectrum beta-lactamase Toho-1: insights into the molecular mechanism for ...
|
5480
|
Crystal structure of extended-spectrum beta-lactamase Toho-1: insights into the molecular mechanism for ...
|
5481
|
Crystal structure of extended-spectrum beta-lactamase Toho-1: insights into the molecular mechanism for ...
|
5482
|
Crystal structure of extended-spectrum beta-lactamase Toho-1: insights into the molecular mechanism for ...
|
5483
|
Crystal structure of extended-spectrum beta-lactamase Toho-1: insights into the molecular mechanism for ...
|
5484
|
Crystal structure of extended-spectrum beta-lactamase Toho-1: insights into the molecular mechanism for ...
|
5485
|
Crystal structure of extended-spectrum beta-lactamase Toho-1: insights into the molecular mechanism for ...
|
5486
|
Functions of the conserved anionic amino acids and those interacting with the substrate phosphate group of ...
|
5487
|
Functions of the conserved anionic amino acids and those interacting with the substrate phosphate group of ...
|
5488
|
Functions of the conserved anionic amino acids and those interacting with the substrate phosphate group of ...
|
5489
|
Functions of the conserved anionic amino acids and those interacting with the substrate phosphate group of ...
|
5490
|
Functions of the conserved anionic amino acids and those interacting with the substrate phosphate group of ...
|
5491
|
Functions of the conserved anionic amino acids and those interacting with the substrate phosphate group of ...
|
5492
|
Functions of the conserved anionic amino acids and those interacting with the substrate phosphate group of ...
|
5493
|
Functions of the conserved anionic amino acids and those interacting with the substrate phosphate group of ...
|
5494
|
Functions of the conserved anionic amino acids and those interacting with the substrate phosphate group of ...
|
5495
|
Functions of the conserved anionic amino acids and those interacting with the substrate phosphate group of ...
|
5496
|
Functions of the conserved anionic amino acids and those interacting with the substrate phosphate group of ...
|
5497
|
Functions of the conserved anionic amino acids and those interacting with the substrate phosphate group of ...
|
5498
|
Functions of the conserved anionic amino acids and those interacting with the substrate phosphate group of ...
|
5499
|
Functions of the conserved anionic amino acids and those interacting with the substrate phosphate group of ...
|
5500
|
Functions of the conserved anionic amino acids and those interacting with the substrate phosphate group of ...
|
5501
|
Phenol hydroxylase from Bacillus thermoglucosidasius A7, a two-protein component monooxygenase with a dual ...
|
5502
|
Phenol hydroxylase from Bacillus thermoglucosidasius A7, a two-protein component monooxygenase with a dual ...
|
5503
|
Phenol hydroxylase from Bacillus thermoglucosidasius A7, a two-protein component monooxygenase with a dual ...
|
5504
|
Phenol hydroxylase from Bacillus thermoglucosidasius A7, a two-protein component monooxygenase with a dual ...
|
5505
|
Phenol hydroxylase from Bacillus thermoglucosidasius A7, a two-protein component monooxygenase with a dual ...
|
5506
|
Phenol hydroxylase from Bacillus thermoglucosidasius A7, a two-protein component monooxygenase with a dual ...
|
5507
|
Phenol hydroxylase from Bacillus thermoglucosidasius A7, a two-protein component monooxygenase with a dual ...
|
5508
|
Phenol hydroxylase from Bacillus thermoglucosidasius A7, a two-protein component monooxygenase with a dual ...
|
5509
|
Phenol hydroxylase from Bacillus thermoglucosidasius A7, a two-protein component monooxygenase with a dual ...
|
5510
|
Phenol hydroxylase from Bacillus thermoglucosidasius A7, a two-protein component monooxygenase with a dual ...
|
5511
|
Phenol hydroxylase from Bacillus thermoglucosidasius A7, a two-protein component monooxygenase with a dual ...
|
5512
|
pH and kinetic isotope effects on sarcosine oxidation by N-methyltryptophan oxidase
|
5513
|
pH and kinetic isotope effects on sarcosine oxidation by N-methyltryptophan oxidase
|
5514
|
pH and kinetic isotope effects on sarcosine oxidation by N-methyltryptophan oxidase
|
5515
|
pH and kinetic isotope effects on sarcosine oxidation by N-methyltryptophan oxidase
|
5516
|
pH and kinetic isotope effects on sarcosine oxidation by N-methyltryptophan oxidase
|
5517
|
Autocatalytic formation of green heme: evidence for H2O2-dependent formation of a covalent methionine-heme ...
|
5518
|
Autocatalytic formation of green heme: evidence for H2O2-dependent formation of a covalent methionine-heme ...
|
5519
|
Determination of the Affinity of Each Component of a Composite Quaternary Transition-State Analogue Complex of ...
|
5520
|
Determination of the Affinity of Each Component of a Composite Quaternary Transition-State Analogue Complex of ...
|
5521
|
Determination of the Affinity of Each Component of a Composite Quaternary Transition-State Analogue Complex of ...
|
5522
|
Determination of the Affinity of Each Component of a Composite Quaternary Transition-State Analogue Complex of ...
|
5523
|
Determination of the Affinity of Each Component of a Composite Quaternary Transition-State Analogue Complex of ...
|
5524
|
Determination of the Affinity of Each Component of a Composite Quaternary Transition-State Analogue Complex of ...
|
5525
|
Determination of the Affinity of Each Component of a Composite Quaternary Transition-State Analogue Complex of ...
|
5526
|
Determination of the Affinity of Each Component of a Composite Quaternary Transition-State Analogue Complex of ...
|
5527
|
Determination of the Affinity of Each Component of a Composite Quaternary Transition-State Analogue Complex of ...
|
5528
|
Determination of the Affinity of Each Component of a Composite Quaternary Transition-State Analogue Complex of ...
|
5529
|
Determination of the Affinity of Each Component of a Composite Quaternary Transition-State Analogue Complex of ...
|
5530
|
Determination of the Affinity of Each Component of a Composite Quaternary Transition-State Analogue Complex of ...
|
5531
|
Purification and characterization of Go alpha and three types of Gi alpha after expression in Escherichia coli
|
5532
|
Purification and characterization of Go alpha and three types of Gi alpha after expression in Escherichia coli
|
5533
|
Purification and characterization of Go alpha and three types of Gi alpha after expression in Escherichia coli
|
5534
|
Purification and characterization of Go alpha and three types of Gi alpha after expression in Escherichia coli
|
5535
|
Production of the Neuromodulator H2S by Cystathionine beta-Synthase via the Condensation of Cysteine and ...
|
5536
|
Production of the Neuromodulator H2S by Cystathionine beta-Synthase via the Condensation of Cysteine and ...
|
5537
|
Acetylation of the chemotaxis response regulator CheY by acetyl-CoA synthetase purified from Escherichia coli
|
5538
|
The effect of pH and temperature on the kinetic parameters of phosphoglucose isomerase. Participation of ...
|
5539
|
The effect of pH and temperature on the kinetic parameters of phosphoglucose isomerase. Participation of ...
|
5540
|
The effect of pH and temperature on the kinetic parameters of phosphoglucose isomerase. Participation of ...
|
5541
|
Disruption of the aldolase A tetramer into catalytically active monomers
|
5542
|
Disruption of the aldolase A tetramer into catalytically active monomers
|
5543
|
Disruption of the aldolase A tetramer into catalytically active monomers
|
5544
|
Disruption of the aldolase A tetramer into catalytically active monomers
|
5545
|
Disruption of the aldolase A tetramer into catalytically active monomers
|
5546
|
Disruption of the aldolase A tetramer into catalytically active monomers
|
5547
|
Disruption of the aldolase A tetramer into catalytically active monomers
|
5548
|
Disruption of the aldolase A tetramer into catalytically active monomers
|
5549
|
Disruption of the aldolase A tetramer into catalytically active monomers
|
5550
|
Disruption of the aldolase A tetramer into catalytically active monomers
|
5551
|
Disruption of the aldolase A tetramer into catalytically active monomers
|
5552
|
The isozymes of glucose-phosphate isomerase (GPI-A2 and GPI-B2) from the teleost fish Fundulus heteroclitus ...
|
5553
|
The isozymes of glucose-phosphate isomerase (GPI-A2 and GPI-B2) from the teleost fish Fundulus heteroclitus ...
|
5554
|
The isozymes of glucose-phosphate isomerase (GPI-A2 and GPI-B2) from the teleost fish Fundulus heteroclitus ...
|
5555
|
The isozymes of glucose-phosphate isomerase (GPI-A2 and GPI-B2) from the teleost fish Fundulus heteroclitus ...
|
5556
|
The isozymes of glucose-phosphate isomerase (GPI-A2 and GPI-B2) from the teleost fish Fundulus heteroclitus ...
|
5557
|
The isozymes of glucose-phosphate isomerase (GPI-A2 and GPI-B2) from the teleost fish Fundulus heteroclitus ...
|
5558
|
The isozymes of glucose-phosphate isomerase (GPI-A2 and GPI-B2) from the teleost fish Fundulus heteroclitus ...
|
5559
|
The isozymes of glucose-phosphate isomerase (GPI-A2 and GPI-B2) from the teleost fish Fundulus heteroclitus ...
|
5560
|
The isozymes of glucose-phosphate isomerase (GPI-A2 and GPI-B2) from the teleost fish Fundulus heteroclitus ...
|
5561
|
The isozymes of glucose-phosphate isomerase (GPI-A2 and GPI-B2) from the teleost fish Fundulus heteroclitus ...
|
5562
|
The isozymes of glucose-phosphate isomerase (GPI-A2 and GPI-B2) from the teleost fish Fundulus heteroclitus ...
|
5563
|
The isozymes of glucose-phosphate isomerase (GPI-A2 and GPI-B2) from the teleost fish Fundulus heteroclitus ...
|
5564
|
The isozymes of glucose-phosphate isomerase (GPI-A2 and GPI-B2) from the teleost fish Fundulus heteroclitus ...
|
5565
|
The isozymes of glucose-phosphate isomerase (GPI-A2 and GPI-B2) from the teleost fish Fundulus heteroclitus ...
|
5566
|
The isozymes of glucose-phosphate isomerase (GPI-A2 and GPI-B2) from the teleost fish Fundulus heteroclitus ...
|
5567
|
The isozymes of glucose-phosphate isomerase (GPI-A2 and GPI-B2) from the teleost fish Fundulus heteroclitus ...
|
5568
|
The isozymes of glucose-phosphate isomerase (GPI-A2 and GPI-B2) from the teleost fish Fundulus heteroclitus ...
|
5569
|
The isozymes of glucose-phosphate isomerase (GPI-A2 and GPI-B2) from the teleost fish Fundulus heteroclitus ...
|
5570
|
The isozymes of glucose-phosphate isomerase (GPI-A2 and GPI-B2) from the teleost fish Fundulus heteroclitus ...
|
5571
|
The isozymes of glucose-phosphate isomerase (GPI-A2 and GPI-B2) from the teleost fish Fundulus heteroclitus ...
|
5572
|
The isozymes of glucose-phosphate isomerase (GPI-A2 and GPI-B2) from the teleost fish Fundulus heteroclitus ...
|
5573
|
The isozymes of glucose-phosphate isomerase (GPI-A2 and GPI-B2) from the teleost fish Fundulus heteroclitus ...
|
5574
|
The isozymes of glucose-phosphate isomerase (GPI-A2 and GPI-B2) from the teleost fish Fundulus heteroclitus ...
|
5575
|
The isozymes of glucose-phosphate isomerase (GPI-A2 and GPI-B2) from the teleost fish Fundulus heteroclitus ...
|
5576
|
Human ocular aldehyde dehydrogenase isozymes: distribution and properties as major soluble proteins in cornea ...
|
5577
|
Human ocular aldehyde dehydrogenase isozymes: distribution and properties as major soluble proteins in cornea ...
|
5578
|
Human ocular aldehyde dehydrogenase isozymes: distribution and properties as major soluble proteins in cornea ...
|
5579
|
Human ocular aldehyde dehydrogenase isozymes: distribution and properties as major soluble proteins in cornea ...
|
5580
|
Human ocular aldehyde dehydrogenase isozymes: distribution and properties as major soluble proteins in cornea ...
|
5581
|
Methadone metabolism by human placenta
|
5582
|
Methadone metabolism by human placenta
|
5583
|
Kinetic and stability properties of Penicillium chrysogenum ATP sulfurylase missing the C-terminal regulatory ...
|
5584
|
Kinetic and stability properties of Penicillium chrysogenum ATP sulfurylase missing the C-terminal regulatory ...
|
5585
|
Kinetic and stability properties of Penicillium chrysogenum ATP sulfurylase missing the C-terminal regulatory ...
|
5586
|
Kinetic and stability properties of Penicillium chrysogenum ATP sulfurylase missing the C-terminal regulatory ...
|
5587
|
Kinetic and stability properties of Penicillium chrysogenum ATP sulfurylase missing the C-terminal regulatory ...
|
5588
|
Kinetic and stability properties of Penicillium chrysogenum ATP sulfurylase missing the C-terminal regulatory ...
|
5589
|
A novel O-phospho-L-serine sulfhydrylation reaction catalyzed by O-acetylserine sulfhydrylase from Aeropyrum ...
|
5590
|
A novel O-phospho-L-serine sulfhydrylation reaction catalyzed by O-acetylserine sulfhydrylase from Aeropyrum ...
|
5591
|
A novel O-phospho-L-serine sulfhydrylation reaction catalyzed by O-acetylserine sulfhydrylase from Aeropyrum ...
|
5592
|
Kinetic mechanism of choline oxidase from Arthrobacter globiformis
|
5593
|
Kinetic mechanism of choline oxidase from Arthrobacter globiformis
|
5594
|
Kinetic mechanism of choline oxidase from Arthrobacter globiformis
|
5595
|
Kinetic mechanism of choline oxidase from Arthrobacter globiformis
|
5596
|
Phosphorylation of human erythrocyte pyruvate kinase by soluble cyclic-AMP-dependent protein kinases
|
5597
|
Phosphorylation of human erythrocyte pyruvate kinase by soluble cyclic-AMP-dependent protein kinases
|
5598
|
Phosphorylation of human erythrocyte pyruvate kinase by soluble cyclic-AMP-dependent protein kinases
|
5599
|
Phosphorylation of human erythrocyte pyruvate kinase by soluble cyclic-AMP-dependent protein kinases
|
5600
|
Phosphorylation of human erythrocyte pyruvate kinase by soluble cyclic-AMP-dependent protein kinases
|
5601
|
Phosphorylation of human erythrocyte pyruvate kinase by soluble cyclic-AMP-dependent protein kinases
|
5602
|
Phosphorylation of human erythrocyte pyruvate kinase by soluble cyclic-AMP-dependent protein kinases
|
5603
|
Phosphorylation of human erythrocyte pyruvate kinase by soluble cyclic-AMP-dependent protein kinases
|
5604
|
Phosphorylation of human erythrocyte pyruvate kinase by soluble cyclic-AMP-dependent protein kinases
|
5605
|
Phosphorylation of human erythrocyte pyruvate kinase by soluble cyclic-AMP-dependent protein kinases
|
5606
|
Phosphorylation of human erythrocyte pyruvate kinase by soluble cyclic-AMP-dependent protein kinases
|
5607
|
Phosphorylation of human erythrocyte pyruvate kinase by soluble cyclic-AMP-dependent protein kinases
|
5608
|
Phosphorylation of human erythrocyte pyruvate kinase by soluble cyclic-AMP-dependent protein kinases
|
5609
|
Phosphorylation of human erythrocyte pyruvate kinase by soluble cyclic-AMP-dependent protein kinases
|
5610
|
Phosphorylation of human erythrocyte pyruvate kinase by soluble cyclic-AMP-dependent protein kinases
|
5611
|
Phosphorylation of human erythrocyte pyruvate kinase by soluble cyclic-AMP-dependent protein kinases
|
5612
|
Insights into the mechanism of Drosophila melanogaster Golgi alpha-mannosidase II through the structural ...
|
5613
|
Insights into the mechanism of Drosophila melanogaster Golgi alpha-mannosidase II through the structural ...
|
5614
|
Insights into the mechanism of Drosophila melanogaster Golgi alpha-mannosidase II through the structural ...
|
5615
|
Insights into the mechanism of Drosophila melanogaster Golgi alpha-mannosidase II through the structural ...
|
5616
|
Insights into the mechanism of Drosophila melanogaster Golgi alpha-mannosidase II through the structural ...
|
5617
|
Insights into the mechanism of Drosophila melanogaster Golgi alpha-mannosidase II through the structural ...
|
5618
|
Kinetic modeling of beta-chloroprene metabolism: I. In vitro rates in liver and lung tissue fractions from ...
|
5619
|
Kinetic modeling of beta-chloroprene metabolism: I. In vitro rates in liver and lung tissue fractions from ...
|
5620
|
Kinetic modeling of beta-chloroprene metabolism: I. In vitro rates in liver and lung tissue fractions from ...
|
5621
|
Kinetic modeling of beta-chloroprene metabolism: I. In vitro rates in liver and lung tissue fractions from ...
|
5622
|
Kinetic modeling of beta-chloroprene metabolism: I. In vitro rates in liver and lung tissue fractions from ...
|
5623
|
Kinetic modeling of beta-chloroprene metabolism: I. In vitro rates in liver and lung tissue fractions from ...
|
5624
|
Kinetic modeling of beta-chloroprene metabolism: I. In vitro rates in liver and lung tissue fractions from ...
|
5625
|
Kinetic modeling of beta-chloroprene metabolism: I. In vitro rates in liver and lung tissue fractions from ...
|
5626
|
Kinetic modeling of beta-chloroprene metabolism: I. In vitro rates in liver and lung tissue fractions from ...
|
5627
|
Kinetic modeling of beta-chloroprene metabolism: I. In vitro rates in liver and lung tissue fractions from ...
|
5628
|
Kinetic modeling of beta-chloroprene metabolism: I. In vitro rates in liver and lung tissue fractions from ...
|
5629
|
Kinetic modeling of beta-chloroprene metabolism: I. In vitro rates in liver and lung tissue fractions from ...
|
5630
|
Kinetic modeling of beta-chloroprene metabolism: I. In vitro rates in liver and lung tissue fractions from ...
|
5631
|
Kinetic modeling of beta-chloroprene metabolism: I. In vitro rates in liver and lung tissue fractions from ...
|
5632
|
Kinetic modeling of beta-chloroprene metabolism: I. In vitro rates in liver and lung tissue fractions from ...
|
5633
|
Kinetic modeling of beta-chloroprene metabolism: I. In vitro rates in liver and lung tissue fractions from ...
|
5634
|
Kinetic modeling of beta-chloroprene metabolism: I. In vitro rates in liver and lung tissue fractions from ...
|
5635
|
Kinetic modeling of beta-chloroprene metabolism: I. In vitro rates in liver and lung tissue fractions from ...
|
5636
|
Kinetic modeling of beta-chloroprene metabolism: I. In vitro rates in liver and lung tissue fractions from ...
|
5637
|
Kinetic modeling of beta-chloroprene metabolism: I. In vitro rates in liver and lung tissue fractions from ...
|
5638
|
Kinetic modeling of beta-chloroprene metabolism: I. In vitro rates in liver and lung tissue fractions from ...
|
5639
|
Kinetic modeling of beta-chloroprene metabolism: I. In vitro rates in liver and lung tissue fractions from ...
|
5640
|
Kinetic modeling of beta-chloroprene metabolism: I. In vitro rates in liver and lung tissue fractions from ...
|
5641
|
Kinetic modeling of beta-chloroprene metabolism: I. In vitro rates in liver and lung tissue fractions from ...
|
5642
|
Kinetic modeling of beta-chloroprene metabolism: I. In vitro rates in liver and lung tissue fractions from ...
|
5643
|
Kinetic modeling of beta-chloroprene metabolism: I. In vitro rates in liver and lung tissue fractions from ...
|
5644
|
Direct interaction between substrates and endogenous steroids in the active site may change the activity of ...
|
5645
|
Direct interaction between substrates and endogenous steroids in the active site may change the activity of ...
|
5646
|
Direct interaction between substrates and endogenous steroids in the active site may change the activity of ...
|
5647
|
Direct interaction between substrates and endogenous steroids in the active site may change the activity of ...
|
5648
|
Direct interaction between substrates and endogenous steroids in the active site may change the activity of ...
|
5649
|
Direct interaction between substrates and endogenous steroids in the active site may change the activity of ...
|
5650
|
Direct interaction between substrates and endogenous steroids in the active site may change the activity of ...
|
5651
|
Direct interaction between substrates and endogenous steroids in the active site may change the activity of ...
|
5652
|
D-Fucose metabolism in a pseudomonad. I. Oxidation of D-fucose to D-fucono- -lactone by a D-aldohexose ...
|
5653
|
D-Fucose metabolism in a pseudomonad. I. Oxidation of D-fucose to D-fucono- -lactone by a D-aldohexose ...
|
5654
|
D-Fucose metabolism in a pseudomonad. I. Oxidation of D-fucose to D-fucono- -lactone by a D-aldohexose ...
|
5655
|
D-Fucose metabolism in a pseudomonad. I. Oxidation of D-fucose to D-fucono- -lactone by a D-aldohexose ...
|
5656
|
D-Fucose metabolism in a pseudomonad. I. Oxidation of D-fucose to D-fucono- -lactone by a D-aldohexose ...
|
5657
|
D-Fucose metabolism in a pseudomonad. I. Oxidation of D-fucose to D-fucono- -lactone by a D-aldohexose ...
|
5658
|
D-Fucose metabolism in a pseudomonad. I. Oxidation of D-fucose to D-fucono- -lactone by a D-aldohexose ...
|
5659
|
D-Fucose metabolism in a pseudomonad. I. Oxidation of D-fucose to D-fucono- -lactone by a D-aldohexose ...
|
5660
|
D-Fucose metabolism in a pseudomonad. I. Oxidation of D-fucose to D-fucono- -lactone by a D-aldohexose ...
|
5661
|
Molecular dissection of human methionine synthase reductase: determination of the flavin redox potentials in ...
|
5662
|
Structural and regulatory properties of pyruvate kinase from the Cyanobacterium synechococcus PCC 6301
|
5663
|
Structural and regulatory properties of pyruvate kinase from the Cyanobacterium synechococcus PCC 6301
|
5664
|
Structural and regulatory properties of pyruvate kinase from the Cyanobacterium synechococcus PCC 6301
|
5665
|
Structural and regulatory properties of pyruvate kinase from the Cyanobacterium synechococcus PCC 6301
|
5666
|
Structural and regulatory properties of pyruvate kinase from the Cyanobacterium synechococcus PCC 6301
|
5667
|
Structural and regulatory properties of pyruvate kinase from the Cyanobacterium synechococcus PCC 6301
|
5668
|
Structural and regulatory properties of pyruvate kinase from the Cyanobacterium synechococcus PCC 6301
|
5669
|
Structural and regulatory properties of pyruvate kinase from the Cyanobacterium synechococcus PCC 6301
|
5670
|
Structural and regulatory properties of pyruvate kinase from the Cyanobacterium synechococcus PCC 6301
|
5671
|
Structural and regulatory properties of pyruvate kinase from the Cyanobacterium synechococcus PCC 6301
|
5672
|
Structural and regulatory properties of pyruvate kinase from the Cyanobacterium synechococcus PCC 6301
|
5673
|
Structural and regulatory properties of pyruvate kinase from the Cyanobacterium synechococcus PCC 6301
|
5674
|
Structural and regulatory properties of pyruvate kinase from the Cyanobacterium synechococcus PCC 6301
|
5675
|
Structural and regulatory properties of pyruvate kinase from the Cyanobacterium synechococcus PCC 6301
|
5676
|
Structural and regulatory properties of pyruvate kinase from the Cyanobacterium synechococcus PCC 6301
|
5677
|
Structural and regulatory properties of pyruvate kinase from the Cyanobacterium synechococcus PCC 6301
|
5678
|
Structural and regulatory properties of pyruvate kinase from the Cyanobacterium synechococcus PCC 6301
|
5679
|
Structural and regulatory properties of pyruvate kinase from the Cyanobacterium synechococcus PCC 6301
|
5680
|
Structural and regulatory properties of pyruvate kinase from the Cyanobacterium synechococcus PCC 6301
|
5681
|
Site-directed mutagenesis of active site residues of phosphite dehydrogenase
|
5682
|
Site-directed mutagenesis of active site residues of phosphite dehydrogenase
|
5683
|
Site-directed mutagenesis of active site residues of phosphite dehydrogenase
|
5684
|
Site-directed mutagenesis of active site residues of phosphite dehydrogenase
|
5685
|
Site-directed mutagenesis of active site residues of phosphite dehydrogenase
|
5686
|
Site-directed mutagenesis of active site residues of phosphite dehydrogenase
|
5687
|
Site-directed mutagenesis of active site residues of phosphite dehydrogenase
|
5688
|
Active Site Mutations of Pseudomonas aeruginosa Exotoxin A
|
5689
|
Active Site Mutations of Pseudomonas aeruginosa Exotoxin A
|
5690
|
Active Site Mutations of Pseudomonas aeruginosa Exotoxin A
|
5691
|
Active Site Mutations of Pseudomonas aeruginosa Exotoxin A
|
5692
|
Overexpression, purification, and characterization of VanX, a D-, D-dipeptidase which is essential for ...
|
5693
|
Overexpression, purification, and characterization of VanX, a D-, D-dipeptidase which is essential for ...
|
5694
|
Overexpression, purification, and characterization of VanX, a D-, D-dipeptidase which is essential for ...
|
5695
|
Overexpression, purification, and characterization of VanX, a D-, D-dipeptidase which is essential for ...
|
5696
|
Overexpression, purification, and characterization of VanX, a D-, D-dipeptidase which is essential for ...
|
5697
|
Overexpression, purification, and characterization of VanX, a D-, D-dipeptidase which is essential for ...
|
5698
|
Overexpression, purification, and characterization of VanX, a D-, D-dipeptidase which is essential for ...
|
5699
|
Overexpression, purification, and characterization of VanX, a D-, D-dipeptidase which is essential for ...
|
5700
|
Overexpression, purification, and characterization of VanX, a D-, D-dipeptidase which is essential for ...
|
5701
|
Overexpression, purification, and characterization of VanX, a D-, D-dipeptidase which is essential for ...
|
5702
|
Identification of an archaeal alpha-L-fucosidase encoded by an interrupted gene. Production of a functional ...
|
5703
|
Kinetic analysis of phenylalanine dehydrogenase mutants designed for aliphatic amino acid dehydrogenase ...
|
5704
|
Kinetic analysis of phenylalanine dehydrogenase mutants designed for aliphatic amino acid dehydrogenase ...
|
5705
|
Kinetic analysis of phenylalanine dehydrogenase mutants designed for aliphatic amino acid dehydrogenase ...
|
5706
|
Kinetic analysis of phenylalanine dehydrogenase mutants designed for aliphatic amino acid dehydrogenase ...
|
5707
|
Kinetic analysis of phenylalanine dehydrogenase mutants designed for aliphatic amino acid dehydrogenase ...
|
5708
|
Kinetic analysis of phenylalanine dehydrogenase mutants designed for aliphatic amino acid dehydrogenase ...
|
5709
|
Kinetic analysis of phenylalanine dehydrogenase mutants designed for aliphatic amino acid dehydrogenase ...
|
5710
|
Kinetic analysis of phenylalanine dehydrogenase mutants designed for aliphatic amino acid dehydrogenase ...
|
5711
|
Kinetic analysis of phenylalanine dehydrogenase mutants designed for aliphatic amino acid dehydrogenase ...
|
5712
|
Kinetic analysis of phenylalanine dehydrogenase mutants designed for aliphatic amino acid dehydrogenase ...
|
5713
|
Kinetic analysis of phenylalanine dehydrogenase mutants designed for aliphatic amino acid dehydrogenase ...
|
5714
|
Kinetic analysis of phenylalanine dehydrogenase mutants designed for aliphatic amino acid dehydrogenase ...
|
5715
|
Kinetic analysis of phenylalanine dehydrogenase mutants designed for aliphatic amino acid dehydrogenase ...
|
5716
|
Kinetic analysis of phenylalanine dehydrogenase mutants designed for aliphatic amino acid dehydrogenase ...
|
5717
|
Kinetic analysis of phenylalanine dehydrogenase mutants designed for aliphatic amino acid dehydrogenase ...
|
5718
|
Kinetic analysis of phenylalanine dehydrogenase mutants designed for aliphatic amino acid dehydrogenase ...
|
5719
|
Kinetic analysis of phenylalanine dehydrogenase mutants designed for aliphatic amino acid dehydrogenase ...
|
5720
|
Kinetic analysis of phenylalanine dehydrogenase mutants designed for aliphatic amino acid dehydrogenase ...
|
5721
|
Kinetic analysis of phenylalanine dehydrogenase mutants designed for aliphatic amino acid dehydrogenase ...
|
5722
|
Kinetic analysis of phenylalanine dehydrogenase mutants designed for aliphatic amino acid dehydrogenase ...
|
5723
|
Kinetic analysis of phenylalanine dehydrogenase mutants designed for aliphatic amino acid dehydrogenase ...
|
5724
|
Kinetic analysis of phenylalanine dehydrogenase mutants designed for aliphatic amino acid dehydrogenase ...
|
5725
|
Kinetic analysis of phenylalanine dehydrogenase mutants designed for aliphatic amino acid dehydrogenase ...
|
5726
|
Kinetic analysis of phenylalanine dehydrogenase mutants designed for aliphatic amino acid dehydrogenase ...
|
5727
|
Kinetic analysis of phenylalanine dehydrogenase mutants designed for aliphatic amino acid dehydrogenase ...
|
5728
|
Kinetic analysis of phenylalanine dehydrogenase mutants designed for aliphatic amino acid dehydrogenase ...
|
5729
|
Kinetic analysis of phenylalanine dehydrogenase mutants designed for aliphatic amino acid dehydrogenase ...
|
5730
|
Kinetic analysis of phenylalanine dehydrogenase mutants designed for aliphatic amino acid dehydrogenase ...
|
5731
|
Kinetic analysis of phenylalanine dehydrogenase mutants designed for aliphatic amino acid dehydrogenase ...
|
5732
|
Kinetic analysis of phenylalanine dehydrogenase mutants designed for aliphatic amino acid dehydrogenase ...
|
5733
|
Kinetic analysis of phenylalanine dehydrogenase mutants designed for aliphatic amino acid dehydrogenase ...
|
5734
|
Kinetic analysis of phenylalanine dehydrogenase mutants designed for aliphatic amino acid dehydrogenase ...
|
5735
|
Kinetic analysis of phenylalanine dehydrogenase mutants designed for aliphatic amino acid dehydrogenase ...
|
5736
|
Kinetic analysis of phenylalanine dehydrogenase mutants designed for aliphatic amino acid dehydrogenase ...
|
5737
|
Kinetic analysis of phenylalanine dehydrogenase mutants designed for aliphatic amino acid dehydrogenase ...
|
5738
|
Kinetic analysis of phenylalanine dehydrogenase mutants designed for aliphatic amino acid dehydrogenase ...
|
5739
|
Kinetic analysis of phenylalanine dehydrogenase mutants designed for aliphatic amino acid dehydrogenase ...
|
5740
|
Kinetic analysis of phenylalanine dehydrogenase mutants designed for aliphatic amino acid dehydrogenase ...
|
5741
|
Kinetic analysis of phenylalanine dehydrogenase mutants designed for aliphatic amino acid dehydrogenase ...
|
5742
|
Kinetic analysis of phenylalanine dehydrogenase mutants designed for aliphatic amino acid dehydrogenase ...
|
5743
|
Kinetic analysis of phenylalanine dehydrogenase mutants designed for aliphatic amino acid dehydrogenase ...
|
5744
|
Kinetic analysis of phenylalanine dehydrogenase mutants designed for aliphatic amino acid dehydrogenase ...
|
5745
|
Kinetic analysis of phenylalanine dehydrogenase mutants designed for aliphatic amino acid dehydrogenase ...
|
5746
|
Kinetic analysis of phenylalanine dehydrogenase mutants designed for aliphatic amino acid dehydrogenase ...
|
5747
|
Kinetic analysis of phenylalanine dehydrogenase mutants designed for aliphatic amino acid dehydrogenase ...
|
5748
|
Kinetic analysis of phenylalanine dehydrogenase mutants designed for aliphatic amino acid dehydrogenase ...
|
5749
|
Kinetic analysis of phenylalanine dehydrogenase mutants designed for aliphatic amino acid dehydrogenase ...
|
5750
|
Kinetic analysis of phenylalanine dehydrogenase mutants designed for aliphatic amino acid dehydrogenase ...
|
5751
|
Kinetic analysis of phenylalanine dehydrogenase mutants designed for aliphatic amino acid dehydrogenase ...
|
5752
|
Kinetic analysis of phenylalanine dehydrogenase mutants designed for aliphatic amino acid dehydrogenase ...
|
5753
|
Kinetic analysis of phenylalanine dehydrogenase mutants designed for aliphatic amino acid dehydrogenase ...
|
5754
|
Kinetic analysis of phenylalanine dehydrogenase mutants designed for aliphatic amino acid dehydrogenase ...
|
5755
|
Kinetic analysis of phenylalanine dehydrogenase mutants designed for aliphatic amino acid dehydrogenase ...
|
5756
|
Kinetic analysis of phenylalanine dehydrogenase mutants designed for aliphatic amino acid dehydrogenase ...
|
5757
|
Kinetic analysis of phenylalanine dehydrogenase mutants designed for aliphatic amino acid dehydrogenase ...
|
5758
|
Kinetic analysis of phenylalanine dehydrogenase mutants designed for aliphatic amino acid dehydrogenase ...
|
5759
|
Kinetic analysis of phenylalanine dehydrogenase mutants designed for aliphatic amino acid dehydrogenase ...
|
5760
|
Kinetic analysis of phenylalanine dehydrogenase mutants designed for aliphatic amino acid dehydrogenase ...
|
5761
|
Kinetic analysis of phenylalanine dehydrogenase mutants designed for aliphatic amino acid dehydrogenase ...
|
5762
|
Kinetic analysis of phenylalanine dehydrogenase mutants designed for aliphatic amino acid dehydrogenase ...
|
5763
|
Kinetic analysis of phenylalanine dehydrogenase mutants designed for aliphatic amino acid dehydrogenase ...
|
5764
|
Kinetic analysis of phenylalanine dehydrogenase mutants designed for aliphatic amino acid dehydrogenase ...
|
5765
|
Kinetic analysis of phenylalanine dehydrogenase mutants designed for aliphatic amino acid dehydrogenase ...
|
5766
|
Kinetic analysis of phenylalanine dehydrogenase mutants designed for aliphatic amino acid dehydrogenase ...
|
5767
|
ATP binding modulates the nucleic acid affinity of hepatitis C virus helicase
|
5768
|
ATP binding modulates the nucleic acid affinity of hepatitis C virus helicase
|
5769
|
Human Acyl-CoA dehydrogenase-9 plays a novel role in the mitochondrial beta-oxidation of unsaturated fatty ...
|
5770
|
Human Acyl-CoA dehydrogenase-9 plays a novel role in the mitochondrial beta-oxidation of unsaturated fatty ...
|
5771
|
Human Acyl-CoA dehydrogenase-9 plays a novel role in the mitochondrial beta-oxidation of unsaturated fatty ...
|
5772
|
Kinetic mechanisms of glycine oxidase from Bacillus subtilis
|
5773
|
Kinetic mechanisms of glycine oxidase from Bacillus subtilis
|
5774
|
Kinetic mechanisms of glycine oxidase from Bacillus subtilis
|
5775
|
Steady-state and pre-steady-state kinetic analysis of halopropane conversion by a rhodococcus haloalkane ...
|
5776
|
Steady-state and pre-steady-state kinetic analysis of halopropane conversion by a rhodococcus haloalkane ...
|
5777
|
Steady-state and pre-steady-state kinetic analysis of halopropane conversion by a rhodococcus haloalkane ...
|
5778
|
Steady-state and pre-steady-state kinetic analysis of halopropane conversion by a rhodococcus haloalkane ...
|
5779
|
Steady-state and pre-steady-state kinetic analysis of halopropane conversion by a rhodococcus haloalkane ...
|
5780
|
Steady-state and pre-steady-state kinetic analysis of halopropane conversion by a rhodococcus haloalkane ...
|
5781
|
Steady-state and pre-steady-state kinetic analysis of halopropane conversion by a rhodococcus haloalkane ...
|
5782
|
Steady-state and pre-steady-state kinetic analysis of halopropane conversion by a rhodococcus haloalkane ...
|
5783
|
Steady-state and pre-steady-state kinetic analysis of halopropane conversion by a rhodococcus haloalkane ...
|
5784
|
Conformational flexibility of the C terminus with implications for substrate binding and catalysis revealed in ...
|
5785
|
Conformational flexibility of the C terminus with implications for substrate binding and catalysis revealed in ...
|
5786
|
Mechanistic insights into the isochorismate pyruvate lyase activity of the catalytically promiscuous PchB from ...
|
5787
|
Mechanistic insights into the isochorismate pyruvate lyase activity of the catalytically promiscuous PchB from ...
|
5788
|
Mechanistic insights into the isochorismate pyruvate lyase activity of the catalytically promiscuous PchB from ...
|
5789
|
Mechanistic insights into the isochorismate pyruvate lyase activity of the catalytically promiscuous PchB from ...
|
5790
|
Mechanistic insights into the isochorismate pyruvate lyase activity of the catalytically promiscuous PchB from ...
|
5791
|
Mechanistic insights into the isochorismate pyruvate lyase activity of the catalytically promiscuous PchB from ...
|
5792
|
Mechanistic insights into the isochorismate pyruvate lyase activity of the catalytically promiscuous PchB from ...
|
5793
|
Mechanistic insights into the isochorismate pyruvate lyase activity of the catalytically promiscuous PchB from ...
|
5794
|
Mechanistic insights into the isochorismate pyruvate lyase activity of the catalytically promiscuous PchB from ...
|
5795
|
Mechanistic insights into the isochorismate pyruvate lyase activity of the catalytically promiscuous PchB from ...
|
5796
|
Mechanistic insights into the isochorismate pyruvate lyase activity of the catalytically promiscuous PchB from ...
|
5797
|
Mechanistic insights into the isochorismate pyruvate lyase activity of the catalytically promiscuous PchB from ...
|
5798
|
Mechanistic insights into the isochorismate pyruvate lyase activity of the catalytically promiscuous PchB from ...
|
5799
|
Mechanistic insights into the isochorismate pyruvate lyase activity of the catalytically promiscuous PchB from ...
|
5800
|
Mechanistic insights into the isochorismate pyruvate lyase activity of the catalytically promiscuous PchB from ...
|
5801
|
Mechanistic insights into the isochorismate pyruvate lyase activity of the catalytically promiscuous PchB from ...
|
5802
|
Mechanistic insights into the isochorismate pyruvate lyase activity of the catalytically promiscuous PchB from ...
|
5803
|
Mechanistic insights into the isochorismate pyruvate lyase activity of the catalytically promiscuous PchB from ...
|
5804
|
Mechanistic insights into the isochorismate pyruvate lyase activity of the catalytically promiscuous PchB from ...
|
5805
|
Mechanistic insights into the isochorismate pyruvate lyase activity of the catalytically promiscuous PchB from ...
|
5806
|
Mechanistic insights into the isochorismate pyruvate lyase activity of the catalytically promiscuous PchB from ...
|
5807
|
Mechanistic insights into the isochorismate pyruvate lyase activity of the catalytically promiscuous PchB from ...
|
5808
|
Mechanistic insights into the isochorismate pyruvate lyase activity of the catalytically promiscuous PchB from ...
|
5809
|
Mechanistic insights into the isochorismate pyruvate lyase activity of the catalytically promiscuous PchB from ...
|
5810
|
Mechanistic insights into the isochorismate pyruvate lyase activity of the catalytically promiscuous PchB from ...
|
5811
|
Characterization of recombinant xylitol dehydrogenase from Galactocandida mastotermitis expressed in ...
|
5812
|
Characterization of recombinant xylitol dehydrogenase from Galactocandida mastotermitis expressed in ...
|
5813
|
Characterization of recombinant xylitol dehydrogenase from Galactocandida mastotermitis expressed in ...
|
5814
|
Characterization of recombinant xylitol dehydrogenase from Galactocandida mastotermitis expressed in ...
|
5815
|
Characterization of recombinant xylitol dehydrogenase from Galactocandida mastotermitis expressed in ...
|
5816
|
Characterization of recombinant xylitol dehydrogenase from Galactocandida mastotermitis expressed in ...
|
5828
|
Agonist occupation of an alpha2A-adrenoreceptor-Gi1alpha fusion protein results in activation of both ...
|
5829
|
Agonist occupation of an alpha2A-adrenoreceptor-Gi1alpha fusion protein results in activation of both ...
|
5830
|
Characterization of a cytosolic malate dehydrogenase cDNA which encodes an isozyme toward oxaloacetate ...
|
5831
|
Characterization of a cytosolic malate dehydrogenase cDNA which encodes an isozyme toward oxaloacetate ...
|
5832
|
Characterization of a cytosolic malate dehydrogenase cDNA which encodes an isozyme toward oxaloacetate ...
|
5833
|
Characterization of a cytosolic malate dehydrogenase cDNA which encodes an isozyme toward oxaloacetate ...
|
5834
|
Isolation and characterization of tissue-specific isozymes of glucosephosphate isomerase from catfish and ...
|
5835
|
Isolation and characterization of tissue-specific isozymes of glucosephosphate isomerase from catfish and ...
|
5836
|
Isolation and characterization of tissue-specific isozymes of glucosephosphate isomerase from catfish and ...
|
5837
|
Isolation and characterization of tissue-specific isozymes of glucosephosphate isomerase from catfish and ...
|
5843
|
Evidence for heme-mediated redox regulation of human cystathionine beta-synthase activity
|
5844
|
Evidence for heme-mediated redox regulation of human cystathionine beta-synthase activity
|
5845
|
Glutathione Synthesis in Streptococcus agalactiae
|
5846
|
Glutathione Synthesis in Streptococcus agalactiae
|
5847
|
Glutathione Synthesis in Streptococcus agalactiae
|
5848
|
Glutathione Synthesis in Streptococcus agalactiae
|
5849
|
Glutathione Synthesis in Streptococcus agalactiae
|
5850
|
A single amino acid substitution (157 Gly----Val) in a phosphoglycerate kinase variant (PGK Shizuoka) ...
|
5851
|
A single amino acid substitution (157 Gly----Val) in a phosphoglycerate kinase variant (PGK Shizuoka) ...
|
5852
|
Kinetic mechanism and metabolic role of pyruvate phosphate dikinase from Entamoeba histolytica
|
5853
|
Kinetic mechanism and metabolic role of pyruvate phosphate dikinase from Entamoeba histolytica
|
5854
|
Kinetic mechanism and metabolic role of pyruvate phosphate dikinase from Entamoeba histolytica
|
5855
|
Kinetic mechanism and metabolic role of pyruvate phosphate dikinase from Entamoeba histolytica
|
5856
|
Kinetic mechanism and metabolic role of pyruvate phosphate dikinase from Entamoeba histolytica
|
5857
|
Kinetic mechanism and metabolic role of pyruvate phosphate dikinase from Entamoeba histolytica
|
5858
|
Kinetic mechanism and metabolic role of pyruvate phosphate dikinase from Entamoeba histolytica
|
5859
|
Kinetic mechanism and metabolic role of pyruvate phosphate dikinase from Entamoeba histolytica
|
5860
|
Kinetic mechanism and metabolic role of pyruvate phosphate dikinase from Entamoeba histolytica
|
5861
|
Kinetic mechanism and metabolic role of pyruvate phosphate dikinase from Entamoeba histolytica
|
5862
|
Kinetic mechanism and metabolic role of pyruvate phosphate dikinase from Entamoeba histolytica
|
5863
|
Kinetic mechanism and metabolic role of pyruvate phosphate dikinase from Entamoeba histolytica
|
5864
|
Kinetic properties and metabolic contributions of yeast mitochondrial and cytosolic NADP+ -specific isocitrate ...
|
5865
|
Kinetic properties and metabolic contributions of yeast mitochondrial and cytosolic NADP+ -specific isocitrate ...
|
5866
|
Kinetic properties and metabolic contributions of yeast mitochondrial and cytosolic NADP+ -specific isocitrate ...
|
5867
|
Kinetic properties and metabolic contributions of yeast mitochondrial and cytosolic NADP+ -specific isocitrate ...
|
5868
|
Kinetic properties and metabolic contributions of yeast mitochondrial and cytosolic NADP+ -specific isocitrate ...
|
5869
|
Kinetic properties and metabolic contributions of yeast mitochondrial and cytosolic NADP+ -specific isocitrate ...
|
5870
|
Kinetic properties and metabolic contributions of yeast mitochondrial and cytosolic NADP+ -specific isocitrate ...
|
5871
|
Kinetic properties and metabolic contributions of yeast mitochondrial and cytosolic NADP+ -specific isocitrate ...
|
5872
|
A mechanism of sulfite neurotoxicity direct inhibition of glutamate dehydrogenase
|
5873
|
A mechanism of sulfite neurotoxicity direct inhibition of glutamate dehydrogenase
|
5874
|
A mechanism of sulfite neurotoxicity direct inhibition of glutamate dehydrogenase
|
5875
|
A mechanism of sulfite neurotoxicity direct inhibition of glutamate dehydrogenase
|
5876
|
A mechanism of sulfite neurotoxicity direct inhibition of glutamate dehydrogenase
|
5877
|
A mechanism of sulfite neurotoxicity direct inhibition of glutamate dehydrogenase
|
5878
|
A mechanism of sulfite neurotoxicity direct inhibition of glutamate dehydrogenase
|
5879
|
A mechanism of sulfite neurotoxicity direct inhibition of glutamate dehydrogenase
|
5880
|
Importance of product/reactant equilibration in the kinetics of the phosphoglucose isomerization reaction by ...
|
5881
|
Importance of product/reactant equilibration in the kinetics of the phosphoglucose isomerization reaction by ...
|
5882
|
Importance of product/reactant equilibration in the kinetics of the phosphoglucose isomerization reaction by ...
|
5883
|
Importance of product/reactant equilibration in the kinetics of the phosphoglucose isomerization reaction by ...
|
5884
|
Importance of product/reactant equilibration in the kinetics of the phosphoglucose isomerization reaction by ...
|
5885
|
Importance of product/reactant equilibration in the kinetics of the phosphoglucose isomerization reaction by ...
|
5886
|
Functional and molecular modelling studies of two hereditary fructose intolerance-causing mutations at ...
|
5887
|
Functional and molecular modelling studies of two hereditary fructose intolerance-causing mutations at ...
|
5888
|
Functional and molecular modelling studies of two hereditary fructose intolerance-causing mutations at ...
|
5889
|
Functional and molecular modelling studies of two hereditary fructose intolerance-causing mutations at ...
|
5890
|
Functional and molecular modelling studies of two hereditary fructose intolerance-causing mutations at ...
|
5891
|
The inhibition of acetate, pyruvate, and 3-phosphogylcerate kinases by chromium adenosine triphosphate
|
5892
|
The inhibition of acetate, pyruvate, and 3-phosphogylcerate kinases by chromium adenosine triphosphate
|
5893
|
The inhibition of acetate, pyruvate, and 3-phosphogylcerate kinases by chromium adenosine triphosphate
|
5894
|
The inhibition of acetate, pyruvate, and 3-phosphogylcerate kinases by chromium adenosine triphosphate
|
5895
|
The inhibition of acetate, pyruvate, and 3-phosphogylcerate kinases by chromium adenosine triphosphate
|
5896
|
The inhibition of acetate, pyruvate, and 3-phosphogylcerate kinases by chromium adenosine triphosphate
|
5897
|
The inhibition of acetate, pyruvate, and 3-phosphogylcerate kinases by chromium adenosine triphosphate
|
5898
|
The inhibition of acetate, pyruvate, and 3-phosphogylcerate kinases by chromium adenosine triphosphate
|
5899
|
The inhibition of acetate, pyruvate, and 3-phosphogylcerate kinases by chromium adenosine triphosphate
|
5900
|
The inhibition of acetate, pyruvate, and 3-phosphogylcerate kinases by chromium adenosine triphosphate
|
5901
|
The inhibition of acetate, pyruvate, and 3-phosphogylcerate kinases by chromium adenosine triphosphate
|
5902
|
The inhibition of acetate, pyruvate, and 3-phosphogylcerate kinases by chromium adenosine triphosphate
|
5903
|
Molecular cloning and baculovirus expression of the rabbit corneal aldehyde dehydrogenase (ALDH1A1) cDNA
|
5904
|
Molecular cloning and baculovirus expression of the rabbit corneal aldehyde dehydrogenase (ALDH1A1) cDNA
|
5905
|
Molecular cloning and baculovirus expression of the rabbit corneal aldehyde dehydrogenase (ALDH1A1) cDNA
|
5906
|
Molecular cloning and baculovirus expression of the rabbit corneal aldehyde dehydrogenase (ALDH1A1) cDNA
|
5907
|
Molecular cloning and baculovirus expression of the rabbit corneal aldehyde dehydrogenase (ALDH1A1) cDNA
|
5908
|
Molecular cloning and baculovirus expression of the rabbit corneal aldehyde dehydrogenase (ALDH1A1) cDNA
|
5909
|
Molecular cloning and baculovirus expression of the rabbit corneal aldehyde dehydrogenase (ALDH1A1) cDNA
|
5910
|
Molecular cloning and baculovirus expression of the rabbit corneal aldehyde dehydrogenase (ALDH1A1) cDNA
|
5911
|
Properties and mechanism of human erythrocyte phosphoglycerate kinase
|
5912
|
Properties and mechanism of human erythrocyte phosphoglycerate kinase
|
5913
|
Properties and mechanism of human erythrocyte phosphoglycerate kinase
|
5914
|
Properties and mechanism of human erythrocyte phosphoglycerate kinase
|
5915
|
Properties and mechanism of human erythrocyte phosphoglycerate kinase
|
5916
|
Properties and mechanism of human erythrocyte phosphoglycerate kinase
|
5917
|
Properties and mechanism of human erythrocyte phosphoglycerate kinase
|
5918
|
Properties and mechanism of human erythrocyte phosphoglycerate kinase
|
5919
|
Properties and mechanism of human erythrocyte phosphoglycerate kinase
|
5920
|
Properties and mechanism of human erythrocyte phosphoglycerate kinase
|
5921
|
Properties and mechanism of human erythrocyte phosphoglycerate kinase
|
5922
|
Properties and mechanism of human erythrocyte phosphoglycerate kinase
|
5923
|
Crystal structure of bacterial morphinone reductase and properties of the C191A mutant enzyme
|
5924
|
Crystal structure of bacterial morphinone reductase and properties of the C191A mutant enzyme
|
5925
|
Crystal structure of bacterial morphinone reductase and properties of the C191A mutant enzyme
|
5926
|
Crystal structure of bacterial morphinone reductase and properties of the C191A mutant enzyme
|
5927
|
Reaction of morphinone reductase with 2-cyclohexen-1-one and 1-nitrocyclohexene: proton donation, ligand ...
|
5928
|
Reaction of morphinone reductase with 2-cyclohexen-1-one and 1-nitrocyclohexene: proton donation, ligand ...
|
5929
|
Aldehyde dismutase activity of human liver alcohol dehydrogenase
|
5930
|
Aldehyde dismutase activity of human liver alcohol dehydrogenase
|
5931
|
Aldehyde dismutase activity of human liver alcohol dehydrogenase
|
5932
|
Correlated changes of some enzyme activities and cofactor and substrate contents of pea cotyledon tissue ...
|
5933
|
Correlated changes of some enzyme activities and cofactor and substrate contents of pea cotyledon tissue ...
|
5934
|
Correlated changes of some enzyme activities and cofactor and substrate contents of pea cotyledon tissue ...
|
5935
|
Catecholase activity associated with copper-S100B
|
5936
|
Catecholase activity associated with copper-S100B
|
5937
|
Catecholase activity associated with copper-S100B
|
5938
|
Catecholase activity associated with copper-S100B
|
5939
|
Catecholase activity associated with copper-S100B
|
5940
|
Catecholase activity associated with copper-S100B
|
5941
|
Catecholase activity associated with copper-S100B
|
5942
|
Catecholase activity associated with copper-S100B
|
5943
|
4-hydroxyretinoic acid, a novel substrate for human liver microsomal UDP-glucuronosyltransferase(s) and ...
|
5944
|
4-hydroxyretinoic acid, a novel substrate for human liver microsomal UDP-glucuronosyltransferase(s) and ...
|
5945
|
4-hydroxyretinoic acid, a novel substrate for human liver microsomal UDP-glucuronosyltransferase(s) and ...
|
5946
|
4-hydroxyretinoic acid, a novel substrate for human liver microsomal UDP-glucuronosyltransferase(s) and ...
|
5947
|
Influence of lipophilicity on the interactions of hydroxy stilbenes with cytochrome P450 3A4
|
5948
|
Influence of lipophilicity on the interactions of hydroxy stilbenes with cytochrome P450 3A4
|
5949
|
Influence of lipophilicity on the interactions of hydroxy stilbenes with cytochrome P450 3A4
|
5950
|
Influence of lipophilicity on the interactions of hydroxy stilbenes with cytochrome P450 3A4
|
5951
|
Influence of lipophilicity on the interactions of hydroxy stilbenes with cytochrome P450 3A4
|
5952
|
Influence of lipophilicity on the interactions of hydroxy stilbenes with cytochrome P450 3A4
|
5953
|
Influence of lipophilicity on the interactions of hydroxy stilbenes with cytochrome P450 3A4
|
5954
|
Influence of lipophilicity on the interactions of hydroxy stilbenes with cytochrome P450 3A4
|
5955
|
Influence of lipophilicity on the interactions of hydroxy stilbenes with cytochrome P450 3A4
|
5956
|
Identification and characterization of two isoenzymes of methionine gamma-lyase from Entamoeba histolytica: a ...
|
5957
|
Identification and characterization of two isoenzymes of methionine gamma-lyase from Entamoeba histolytica: a ...
|
5958
|
Identification and characterization of two isoenzymes of methionine gamma-lyase from Entamoeba histolytica: a ...
|
5959
|
Identification and characterization of two isoenzymes of methionine gamma-lyase from Entamoeba histolytica: a ...
|
5960
|
Identification and characterization of two isoenzymes of methionine gamma-lyase from Entamoeba histolytica: a ...
|
5961
|
Identification and characterization of two isoenzymes of methionine gamma-lyase from Entamoeba histolytica: a ...
|
5962
|
Alteration of substrate specificity by a naturally-occurring aldolase B mutation (Ala337-->Val) in fructose ...
|
5963
|
Alteration of substrate specificity by a naturally-occurring aldolase B mutation (Ala337-->Val) in fructose ...
|
5964
|
Alteration of substrate specificity by a naturally-occurring aldolase B mutation (Ala337-->Val) in fructose ...
|
5965
|
Alteration of substrate specificity by a naturally-occurring aldolase B mutation (Ala337-->Val) in fructose ...
|
5966
|
Partial purification, kinetic analysis, and amino acid sequence information of a flavonol ...
|
5967
|
Partial purification, kinetic analysis, and amino acid sequence information of a flavonol ...
|
5968
|
Partial purification, kinetic analysis, and amino acid sequence information of a flavonol ...
|
5969
|
Identification of the enzymatic active site of CD38 by site-directed mutagenesis
|
5970
|
Identification of the enzymatic active site of CD38 by site-directed mutagenesis
|
5971
|
Identification of the enzymatic active site of CD38 by site-directed mutagenesis
|
5972
|
Identification of the enzymatic active site of CD38 by site-directed mutagenesis
|
5973
|
Identification of the enzymatic active site of CD38 by site-directed mutagenesis
|
5974
|
Identification of the enzymatic active site of CD38 by site-directed mutagenesis
|
5975
|
Identification of the enzymatic active site of CD38 by site-directed mutagenesis
|
5976
|
Identification of the enzymatic active site of CD38 by site-directed mutagenesis
|
5977
|
Identification of the enzymatic active site of CD38 by site-directed mutagenesis
|
5978
|
Identification of the enzymatic active site of CD38 by site-directed mutagenesis
|
5979
|
Identification of the enzymatic active site of CD38 by site-directed mutagenesis
|
5980
|
Identification of the enzymatic active site of CD38 by site-directed mutagenesis
|
5981
|
Identification of the enzymatic active site of CD38 by site-directed mutagenesis
|
5982
|
Identification of the enzymatic active site of CD38 by site-directed mutagenesis
|
5983
|
Identification of the enzymatic active site of CD38 by site-directed mutagenesis
|
5984
|
Identification of the enzymatic active site of CD38 by site-directed mutagenesis
|
5985
|
Identification of the enzymatic active site of CD38 by site-directed mutagenesis
|
5986
|
Identification of the enzymatic active site of CD38 by site-directed mutagenesis
|
5987
|
Identification of the enzymatic active site of CD38 by site-directed mutagenesis
|
5988
|
Identification of the enzymatic active site of CD38 by site-directed mutagenesis
|
5989
|
Identification of the enzymatic active site of CD38 by site-directed mutagenesis
|
5990
|
Identification of the enzymatic active site of CD38 by site-directed mutagenesis
|
5991
|
Identification of the enzymatic active site of CD38 by site-directed mutagenesis
|
5992
|
Identification of the enzymatic active site of CD38 by site-directed mutagenesis
|
5993
|
Identification of the enzymatic active site of CD38 by site-directed mutagenesis
|
5994
|
Identification of the enzymatic active site of CD38 by site-directed mutagenesis
|
5995
|
Identification of the enzymatic active site of CD38 by site-directed mutagenesis
|
5996
|
Identification of the enzymatic active site of CD38 by site-directed mutagenesis
|
5997
|
Identification of the enzymatic active site of CD38 by site-directed mutagenesis
|
5998
|
Identification of the enzymatic active site of CD38 by site-directed mutagenesis
|
5999
|
Identification of the enzymatic active site of CD38 by site-directed mutagenesis
|
6000
|
Identification of the enzymatic active site of CD38 by site-directed mutagenesis
|