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3001
|
Cysteine and keto acids modulate mosquito kynurenine aminotransferase catalyzed kynurenic acid production
|
3002
|
Cysteine and keto acids modulate mosquito kynurenine aminotransferase catalyzed kynurenic acid production
|
3003
|
Cysteine and keto acids modulate mosquito kynurenine aminotransferase catalyzed kynurenic acid production
|
3004
|
Cysteine and keto acids modulate mosquito kynurenine aminotransferase catalyzed kynurenic acid production
|
3005
|
Cysteine and keto acids modulate mosquito kynurenine aminotransferase catalyzed kynurenic acid production
|
3006
|
Cysteine and keto acids modulate mosquito kynurenine aminotransferase catalyzed kynurenic acid production
|
3007
|
Cysteine and keto acids modulate mosquito kynurenine aminotransferase catalyzed kynurenic acid production
|
3008
|
Cysteine and keto acids modulate mosquito kynurenine aminotransferase catalyzed kynurenic acid production
|
3009
|
Cysteine and keto acids modulate mosquito kynurenine aminotransferase catalyzed kynurenic acid production
|
3010
|
Rat Liver gamma-Butyrobetaine Hydroxylase Catalyzed Reaction: Influence of Potassium, Substrates, and ...
|
3011
|
Rat Liver gamma-Butyrobetaine Hydroxylase Catalyzed Reaction: Influence of Potassium, Substrates, and ...
|
3012
|
Rat Liver gamma-Butyrobetaine Hydroxylase Catalyzed Reaction: Influence of Potassium, Substrates, and ...
|
3013
|
Rat Liver gamma-Butyrobetaine Hydroxylase Catalyzed Reaction: Influence of Potassium, Substrates, and ...
|
3014
|
Rat Liver gamma-Butyrobetaine Hydroxylase Catalyzed Reaction: Influence of Potassium, Substrates, and ...
|
3015
|
Rat Liver gamma-Butyrobetaine Hydroxylase Catalyzed Reaction: Influence of Potassium, Substrates, and ...
|
3016
|
Rat Liver gamma-Butyrobetaine Hydroxylase Catalyzed Reaction: Influence of Potassium, Substrates, and ...
|
3017
|
Rat Liver gamma-Butyrobetaine Hydroxylase Catalyzed Reaction: Influence of Potassium, Substrates, and ...
|
3018
|
Kinetics of the activation of rat liver pyruvate kinase by fructose 1,6-diphosphate and methods for ...
|
3019
|
Kinetics of the activation of rat liver pyruvate kinase by fructose 1,6-diphosphate and methods for ...
|
3020
|
Kinetics of the activation of rat liver pyruvate kinase by fructose 1,6-diphosphate and methods for ...
|
3021
|
Kinetics of the activation of rat liver pyruvate kinase by fructose 1,6-diphosphate and methods for ...
|
3022
|
Kinetics of the activation of rat liver pyruvate kinase by fructose 1,6-diphosphate and methods for ...
|
3023
|
Kinetics of the activation of rat liver pyruvate kinase by fructose 1,6-diphosphate and methods for ...
|
3024
|
Separation, Properties, and regulation of Acyl Coenzyme A dehydrogenase from Bovine Heart and Liver
|
3025
|
Separation, Properties, and regulation of Acyl Coenzyme A dehydrogenase from Bovine Heart and Liver
|
3026
|
Separation, Properties, and regulation of Acyl Coenzyme A dehydrogenase from Bovine Heart and Liver
|
3027
|
Separation, Properties, and regulation of Acyl Coenzyme A dehydrogenase from Bovine Heart and Liver
|
3028
|
Separation, Properties, and regulation of Acyl Coenzyme A dehydrogenase from Bovine Heart and Liver
|
3029
|
Separation, Properties, and regulation of Acyl Coenzyme A dehydrogenase from Bovine Heart and Liver
|
3030
|
Separation, Properties, and regulation of Acyl Coenzyme A dehydrogenase from Bovine Heart and Liver
|
3031
|
Separation, Properties, and regulation of Acyl Coenzyme A dehydrogenase from Bovine Heart and Liver
|
3032
|
Separation, Properties, and regulation of Acyl Coenzyme A dehydrogenase from Bovine Heart and Liver
|
3033
|
Separation, Properties, and regulation of Acyl Coenzyme A dehydrogenase from Bovine Heart and Liver
|
3034
|
Separation, Properties, and regulation of Acyl Coenzyme A dehydrogenase from Bovine Heart and Liver
|
3035
|
Separation, Properties, and regulation of Acyl Coenzyme A dehydrogenase from Bovine Heart and Liver
|
3036
|
Tyrosinase inhibitory activity of cucumber compounds: enzymes responsible for browning in cucumber
|
3037
|
Tyrosinase inhibitory activity of cucumber compounds: enzymes responsible for browning in cucumber
|
3038
|
Tyrosinase inhibitory activity of cucumber compounds: enzymes responsible for browning in cucumber
|
3039
|
Alpha-glucan, water dikinase (GWD): a plastidic enzyme with redox-regulated and coordinated catalytic activity ...
|
3040
|
Alpha-glucan, water dikinase (GWD): a plastidic enzyme with redox-regulated and coordinated catalytic activity ...
|
3041
|
Alpha-glucan, water dikinase (GWD): a plastidic enzyme with redox-regulated and coordinated catalytic activity ...
|
3042
|
Acetylcholinesterase active centre and gorge conformations analysed by combinatorial mutations and ...
|
3043
|
Acetylcholinesterase active centre and gorge conformations analysed by combinatorial mutations and ...
|
3044
|
Acetylcholinesterase active centre and gorge conformations analysed by combinatorial mutations and ...
|
3045
|
Acetylcholinesterase active centre and gorge conformations analysed by combinatorial mutations and ...
|
3046
|
Acetylcholinesterase active centre and gorge conformations analysed by combinatorial mutations and ...
|
3047
|
Acetylcholinesterase active centre and gorge conformations analysed by combinatorial mutations and ...
|
3048
|
Acetylcholinesterase active centre and gorge conformations analysed by combinatorial mutations and ...
|
3049
|
Acetylcholinesterase active centre and gorge conformations analysed by combinatorial mutations and ...
|
3050
|
Acetylcholinesterase active centre and gorge conformations analysed by combinatorial mutations and ...
|
3051
|
Acetylcholinesterase active centre and gorge conformations analysed by combinatorial mutations and ...
|
3052
|
Acetylcholinesterase active centre and gorge conformations analysed by combinatorial mutations and ...
|
3053
|
Acetylcholinesterase active centre and gorge conformations analysed by combinatorial mutations and ...
|
3054
|
Acetylcholinesterase active centre and gorge conformations analysed by combinatorial mutations and ...
|
3055
|
Acetylcholinesterase active centre and gorge conformations analysed by combinatorial mutations and ...
|
3056
|
Chemical mechanism and substrate specificity of RhlI, an acylhomoserine lactone synthase from Pseudomonas ...
|
3057
|
Chemical mechanism and substrate specificity of RhlI, an acylhomoserine lactone synthase from Pseudomonas ...
|
3058
|
Chemical mechanism and substrate specificity of RhlI, an acylhomoserine lactone synthase from Pseudomonas ...
|
3059
|
Chemical mechanism and substrate specificity of RhlI, an acylhomoserine lactone synthase from Pseudomonas ...
|
3060
|
MtmMII-mediated C-methylation during biosynthesis of the antitumor drug mithramycin is essential for ...
|
3061
|
Glucuronidation of catechol estrogens by expressed human UDP-glucuronosyltransferases (UGTs) 1A1, 1A3, and 2B7
|
3062
|
Glucuronidation of catechol estrogens by expressed human UDP-glucuronosyltransferases (UGTs) 1A1, 1A3, and 2B7
|
3063
|
Glucuronidation of catechol estrogens by expressed human UDP-glucuronosyltransferases (UGTs) 1A1, 1A3, and 2B7
|
3064
|
Glucuronidation of catechol estrogens by expressed human UDP-glucuronosyltransferases (UGTs) 1A1, 1A3, and 2B7
|
3065
|
Glucuronidation of catechol estrogens by expressed human UDP-glucuronosyltransferases (UGTs) 1A1, 1A3, and 2B7
|
3066
|
Glucuronidation of catechol estrogens by expressed human UDP-glucuronosyltransferases (UGTs) 1A1, 1A3, and 2B7
|
3067
|
Glucuronidation of catechol estrogens by expressed human UDP-glucuronosyltransferases (UGTs) 1A1, 1A3, and 2B7
|
3068
|
Glucuronidation of catechol estrogens by expressed human UDP-glucuronosyltransferases (UGTs) 1A1, 1A3, and 2B7
|
3069
|
Glucuronidation of catechol estrogens by expressed human UDP-glucuronosyltransferases (UGTs) 1A1, 1A3, and 2B7
|
3070
|
Glucuronidation of catechol estrogens by expressed human UDP-glucuronosyltransferases (UGTs) 1A1, 1A3, and 2B7
|
3071
|
Glucuronidation of catechol estrogens by expressed human UDP-glucuronosyltransferases (UGTs) 1A1, 1A3, and 2B7
|
3072
|
Glucuronidation of catechol estrogens by expressed human UDP-glucuronosyltransferases (UGTs) 1A1, 1A3, and 2B7
|
3073
|
Glucuronidation of catechol estrogens by expressed human UDP-glucuronosyltransferases (UGTs) 1A1, 1A3, and 2B7
|
3074
|
Glucuronidation of catechol estrogens by expressed human UDP-glucuronosyltransferases (UGTs) 1A1, 1A3, and 2B7
|
3075
|
Glucuronidation of catechol estrogens by expressed human UDP-glucuronosyltransferases (UGTs) 1A1, 1A3, and 2B7
|
3076
|
Glucuronidation of catechol estrogens by expressed human UDP-glucuronosyltransferases (UGTs) 1A1, 1A3, and 2B7
|
3077
|
Glucuronidation of catechol estrogens by expressed human UDP-glucuronosyltransferases (UGTs) 1A1, 1A3, and 2B7
|
3078
|
Glucuronidation of catechol estrogens by expressed human UDP-glucuronosyltransferases (UGTs) 1A1, 1A3, and 2B7
|
3079
|
Glucuronidation of catechol estrogens by expressed human UDP-glucuronosyltransferases (UGTs) 1A1, 1A3, and 2B7
|
3080
|
Glucuronidation of catechol estrogens by expressed human UDP-glucuronosyltransferases (UGTs) 1A1, 1A3, and 2B7
|
3081
|
Glucuronidation of catechol estrogens by expressed human UDP-glucuronosyltransferases (UGTs) 1A1, 1A3, and 2B7
|
3082
|
Glucuronidation of catechol estrogens by expressed human UDP-glucuronosyltransferases (UGTs) 1A1, 1A3, and 2B7
|
3083
|
Glucuronidation of catechol estrogens by expressed human UDP-glucuronosyltransferases (UGTs) 1A1, 1A3, and 2B7
|
3084
|
Glucuronidation of catechol estrogens by expressed human UDP-glucuronosyltransferases (UGTs) 1A1, 1A3, and 2B7
|
3085
|
Glucuronidation of catechol estrogens by expressed human UDP-glucuronosyltransferases (UGTs) 1A1, 1A3, and 2B7
|
3086
|
Glucuronidation of catechol estrogens by expressed human UDP-glucuronosyltransferases (UGTs) 1A1, 1A3, and 2B7
|
3087
|
Glucuronidation of catechol estrogens by expressed human UDP-glucuronosyltransferases (UGTs) 1A1, 1A3, and 2B7
|
3088
|
Glucuronidation of catechol estrogens by expressed human UDP-glucuronosyltransferases (UGTs) 1A1, 1A3, and 2B7
|
3089
|
Glucuronidation of catechol estrogens by expressed human UDP-glucuronosyltransferases (UGTs) 1A1, 1A3, and 2B7
|
3090
|
Glucuronidation of catechol estrogens by expressed human UDP-glucuronosyltransferases (UGTs) 1A1, 1A3, and 2B7
|
3091
|
Glucuronidation of catechol estrogens by expressed human UDP-glucuronosyltransferases (UGTs) 1A1, 1A3, and 2B7
|
3092
|
Glucuronidation of catechol estrogens by expressed human UDP-glucuronosyltransferases (UGTs) 1A1, 1A3, and 2B7
|
3093
|
Glucuronidation of catechol estrogens by expressed human UDP-glucuronosyltransferases (UGTs) 1A1, 1A3, and 2B7
|
3094
|
Mechanism of chorismate synthase. Role of the two invariant histidine residues in the active site
|
3095
|
Mechanism of chorismate synthase. Role of the two invariant histidine residues in the active site
|
3096
|
Mechanism of chorismate synthase. Role of the two invariant histidine residues in the active site
|
3097
|
Mechanism of chorismate synthase. Role of the two invariant histidine residues in the active site
|
3098
|
Mechanism of chorismate synthase. Role of the two invariant histidine residues in the active site
|
3099
|
Mechanism of chorismate synthase. Role of the two invariant histidine residues in the active site
|
3100
|
Mechanism of chorismate synthase. Role of the two invariant histidine residues in the active site
|
3101
|
Redox regulation and reaction mechanism of human cystathionine-beta-synthase: a PLP-dependent hemesensor ...
|
3102
|
Redox regulation and reaction mechanism of human cystathionine-beta-synthase: a PLP-dependent hemesensor ...
|
3103
|
Redox regulation and reaction mechanism of human cystathionine-beta-synthase: a PLP-dependent hemesensor ...
|
3104
|
Probing hydrogen-bonding interactions in the active site of medium-chain acyl-CoA dehydrogenase using Raman ...
|
3105
|
Probing hydrogen-bonding interactions in the active site of medium-chain acyl-CoA dehydrogenase using Raman ...
|
3106
|
Probing hydrogen-bonding interactions in the active site of medium-chain acyl-CoA dehydrogenase using Raman ...
|
3107
|
Probing hydrogen-bonding interactions in the active site of medium-chain acyl-CoA dehydrogenase using Raman ...
|
3108
|
Probing hydrogen-bonding interactions in the active site of medium-chain acyl-CoA dehydrogenase using Raman ...
|
3141
|
Studies on Bovine Hepatic Fructose 1,6-Diphosphatase
|
3142
|
Studies on Bovine Hepatic Fructose 1,6-Diphosphatase
|
3143
|
Characterization of the peroxidase system at low H2O2
|
3144
|
Characterization of the peroxidase system at low H2O2
|
3145
|
Characterization of the peroxidase system at low H2O2
|
3146
|
Characterization of the peroxidase system at low H2O2
|
3147
|
Characterization of the peroxidase system at low H2O2
|
3148
|
Modifying the stereochemistry of an enzyme-catalyzed reaction by directed evolution
|
3149
|
Modifying the stereochemistry of an enzyme-catalyzed reaction by directed evolution
|
3150
|
Modifying the stereochemistry of an enzyme-catalyzed reaction by directed evolution
|
3151
|
Modifying the stereochemistry of an enzyme-catalyzed reaction by directed evolution
|
3152
|
Modifying the stereochemistry of an enzyme-catalyzed reaction by directed evolution
|
3153
|
Modifying the stereochemistry of an enzyme-catalyzed reaction by directed evolution
|
3154
|
Modifying the stereochemistry of an enzyme-catalyzed reaction by directed evolution
|
3155
|
Modifying the stereochemistry of an enzyme-catalyzed reaction by directed evolution
|
3156
|
Modifying the stereochemistry of an enzyme-catalyzed reaction by directed evolution
|
3157
|
Modifying the stereochemistry of an enzyme-catalyzed reaction by directed evolution
|
3158
|
Modifying the stereochemistry of an enzyme-catalyzed reaction by directed evolution
|
3159
|
Modifying the stereochemistry of an enzyme-catalyzed reaction by directed evolution
|
3160
|
Modifying the stereochemistry of an enzyme-catalyzed reaction by directed evolution
|
3161
|
Modifying the stereochemistry of an enzyme-catalyzed reaction by directed evolution
|
3187
|
Inhibition of lentil copper/TPQ amine oxidase by the mechanism-based inhibitor derived from tyramine
|
3188
|
Inhibition of lentil copper/TPQ amine oxidase by the mechanism-based inhibitor derived from tyramine
|
3189
|
Inhibition of lentil copper/TPQ amine oxidase by the mechanism-based inhibitor derived from tyramine
|
3190
|
Inhibition of lentil copper/TPQ amine oxidase by the mechanism-based inhibitor derived from tyramine
|
3191
|
Inhibition of lentil copper/TPQ amine oxidase by the mechanism-based inhibitor derived from tyramine
|
3192
|
Inhibition of lentil copper/TPQ amine oxidase by the mechanism-based inhibitor derived from tyramine
|
3193
|
Kinetic studies of oxygen reactivity in soybean lipoxygenase-1
|
3194
|
Kinetic studies of oxygen reactivity in soybean lipoxygenase-1
|
3195
|
Kinetic studies of oxygen reactivity in soybean lipoxygenase-1
|
3196
|
Kinetic studies of oxygen reactivity in soybean lipoxygenase-1
|
3197
|
Kinetic studies of oxygen reactivity in soybean lipoxygenase-1
|
3198
|
Catalytic properties of mutant 23 S ribosomes resistant to oxazolidinones
|
3199
|
Catalytic properties of mutant 23 S ribosomes resistant to oxazolidinones
|
3200
|
Catalytic properties of mutant 23 S ribosomes resistant to oxazolidinones
|
3201
|
Catalytic properties of mutant 23 S ribosomes resistant to oxazolidinones
|
3202
|
Catalytic properties of mutant 23 S ribosomes resistant to oxazolidinones
|
3203
|
Catalytic properties of mutant 23 S ribosomes resistant to oxazolidinones
|
3204
|
Catalytic properties of mutant 23 S ribosomes resistant to oxazolidinones
|
3205
|
Catalytic properties of mutant 23 S ribosomes resistant to oxazolidinones
|
3206
|
Catalytic properties of mutant 23 S ribosomes resistant to oxazolidinones
|
3207
|
Catalytic properties of mutant 23 S ribosomes resistant to oxazolidinones
|
3208
|
Catalytic properties of mutant 23 S ribosomes resistant to oxazolidinones
|
3209
|
Catalytic properties of mutant 23 S ribosomes resistant to oxazolidinones
|
3210
|
Catalytic properties of mutant 23 S ribosomes resistant to oxazolidinones
|
3211
|
Catalytic properties of mutant 23 S ribosomes resistant to oxazolidinones
|
3212
|
Catalytic properties of mutant 23 S ribosomes resistant to oxazolidinones
|
3213
|
Catalytic properties of mutant 23 S ribosomes resistant to oxazolidinones
|
3214
|
Catalytic properties of mutant 23 S ribosomes resistant to oxazolidinones
|
3215
|
Catalytic properties of mutant 23 S ribosomes resistant to oxazolidinones
|
3216
|
Catalytic properties of mutant 23 S ribosomes resistant to oxazolidinones
|
3217
|
Allosteric and catalytic functions of the PPi-binding motif in the ATP sulfurylase-GTPase system
|
3218
|
Allosteric and catalytic functions of the PPi-binding motif in the ATP sulfurylase-GTPase system
|
3219
|
Allosteric and catalytic functions of the PPi-binding motif in the ATP sulfurylase-GTPase system
|
3220
|
Allosteric and catalytic functions of the PPi-binding motif in the ATP sulfurylase-GTPase system
|
3221
|
Allosteric and catalytic functions of the PPi-binding motif in the ATP sulfurylase-GTPase system
|
3222
|
Allosteric and catalytic functions of the PPi-binding motif in the ATP sulfurylase-GTPase system
|
3223
|
Allosteric and catalytic functions of the PPi-binding motif in the ATP sulfurylase-GTPase system
|
3224
|
Allosteric and catalytic functions of the PPi-binding motif in the ATP sulfurylase-GTPase system
|
3225
|
Allosteric and catalytic functions of the PPi-binding motif in the ATP sulfurylase-GTPase system
|
3226
|
Allosteric and catalytic functions of the PPi-binding motif in the ATP sulfurylase-GTPase system
|
3227
|
Allosteric and catalytic functions of the PPi-binding motif in the ATP sulfurylase-GTPase system
|
3228
|
Allosteric and catalytic functions of the PPi-binding motif in the ATP sulfurylase-GTPase system
|
3229
|
Allosteric and catalytic functions of the PPi-binding motif in the ATP sulfurylase-GTPase system
|
3230
|
Allosteric and catalytic functions of the PPi-binding motif in the ATP sulfurylase-GTPase system
|
3231
|
Relaxing the nicotinamide cofactor specificity of phosphite dehydrogenase by rational design
|
3232
|
Relaxing the nicotinamide cofactor specificity of phosphite dehydrogenase by rational design
|
3233
|
Relaxing the nicotinamide cofactor specificity of phosphite dehydrogenase by rational design
|
3234
|
Relaxing the nicotinamide cofactor specificity of phosphite dehydrogenase by rational design
|
3235
|
Relaxing the nicotinamide cofactor specificity of phosphite dehydrogenase by rational design
|
3236
|
Relaxing the nicotinamide cofactor specificity of phosphite dehydrogenase by rational design
|
3237
|
Relaxing the nicotinamide cofactor specificity of phosphite dehydrogenase by rational design
|
3238
|
Relaxing the nicotinamide cofactor specificity of phosphite dehydrogenase by rational design
|
3239
|
Characterization and kinetics of 45 kDa chitosanase from Bacillus sp. P16
|
3240
|
Escherichia coli cystathionine gamma-synthase does not obey ping-pong kinetics. Novel continuous assays for ...
|
3241
|
Escherichia coli cystathionine gamma-synthase does not obey ping-pong kinetics. Novel continuous assays for ...
|
3242
|
Escherichia coli cystathionine gamma-synthase does not obey ping-pong kinetics. Novel continuous assays for ...
|
3243
|
Escherichia coli cystathionine gamma-synthase does not obey ping-pong kinetics. Novel continuous assays for ...
|
3244
|
Escherichia coli cystathionine gamma-synthase does not obey ping-pong kinetics. Novel continuous assays for ...
|
3245
|
Escherichia coli cystathionine gamma-synthase does not obey ping-pong kinetics. Novel continuous assays for ...
|
3246
|
Escherichia coli cystathionine gamma-synthase does not obey ping-pong kinetics. Novel continuous assays for ...
|
3247
|
Escherichia coli cystathionine gamma-synthase does not obey ping-pong kinetics. Novel continuous assays for ...
|
3248
|
Escherichia coli cystathionine gamma-synthase does not obey ping-pong kinetics. Novel continuous assays for ...
|
3249
|
Escherichia coli cystathionine gamma-synthase does not obey ping-pong kinetics. Novel continuous assays for ...
|
3250
|
Potassium transport in a halophilic member of the bacteria domain: identification and characterization of the ...
|
3251
|
Potassium transport in a halophilic member of the bacteria domain: identification and characterization of the ...
|
3252
|
Potassium transport in a halophilic member of the bacteria domain: identification and characterization of the ...
|
3253
|
Treponema denticola cystalysin catalyzes beta-desulfination of L-cysteine sulfinic acid and ...
|
3254
|
Treponema denticola cystalysin catalyzes beta-desulfination of L-cysteine sulfinic acid and ...
|
3255
|
Treponema denticola cystalysin catalyzes beta-desulfination of L-cysteine sulfinic acid and ...
|
3256
|
Analysis of the role of the active site residue Arg98 in the flavoprotein tryptophan 2-monooxygenase, a member ...
|
3257
|
Analysis of the role of the active site residue Arg98 in the flavoprotein tryptophan 2-monooxygenase, a member ...
|
3258
|
Analysis of the role of the active site residue Arg98 in the flavoprotein tryptophan 2-monooxygenase, a member ...
|
3259
|
Analysis of the role of the active site residue Arg98 in the flavoprotein tryptophan 2-monooxygenase, a member ...
|
3260
|
Analysis of the role of the active site residue Arg98 in the flavoprotein tryptophan 2-monooxygenase, a member ...
|
3261
|
Analysis of the role of the active site residue Arg98 in the flavoprotein tryptophan 2-monooxygenase, a member ...
|
3262
|
Analysis of the role of the active site residue Arg98 in the flavoprotein tryptophan 2-monooxygenase, a member ...
|
3263
|
Analysis of the role of the active site residue Arg98 in the flavoprotein tryptophan 2-monooxygenase, a member ...
|
3264
|
Analysis of the role of the active site residue Arg98 in the flavoprotein tryptophan 2-monooxygenase, a member ...
|
3265
|
Analysis of the role of the active site residue Arg98 in the flavoprotein tryptophan 2-monooxygenase, a member ...
|
3266
|
Analysis of the role of the active site residue Arg98 in the flavoprotein tryptophan 2-monooxygenase, a member ...
|
3267
|
Analysis of the role of the active site residue Arg98 in the flavoprotein tryptophan 2-monooxygenase, a member ...
|
3283
|
Fluorescence study of ligand binding to potato tuber pyrophosphate-dependent phosphofructokinase: evidence for ...
|
3284
|
Fluorescence study of ligand binding to potato tuber pyrophosphate-dependent phosphofructokinase: evidence for ...
|
3285
|
Fluorescence study of ligand binding to potato tuber pyrophosphate-dependent phosphofructokinase: evidence for ...
|
3286
|
Fluorescence study of ligand binding to potato tuber pyrophosphate-dependent phosphofructokinase: evidence for ...
|
3287
|
Fluorescence study of ligand binding to potato tuber pyrophosphate-dependent phosphofructokinase: evidence for ...
|
3288
|
Fluorescence study of ligand binding to potato tuber pyrophosphate-dependent phosphofructokinase: evidence for ...
|
3289
|
Fluorescence study of ligand binding to potato tuber pyrophosphate-dependent phosphofructokinase: evidence for ...
|
3290
|
Fluorescence study of ligand binding to potato tuber pyrophosphate-dependent phosphofructokinase: evidence for ...
|
3291
|
Fluorescence study of ligand binding to potato tuber pyrophosphate-dependent phosphofructokinase: evidence for ...
|
3292
|
Fluorescence study of ligand binding to potato tuber pyrophosphate-dependent phosphofructokinase: evidence for ...
|
3293
|
Fluorescence study of ligand binding to potato tuber pyrophosphate-dependent phosphofructokinase: evidence for ...
|
3294
|
Fluorescence study of ligand binding to potato tuber pyrophosphate-dependent phosphofructokinase: evidence for ...
|
3295
|
Fluorescence study of ligand binding to potato tuber pyrophosphate-dependent phosphofructokinase: evidence for ...
|
3296
|
Fluorescence study of ligand binding to potato tuber pyrophosphate-dependent phosphofructokinase: evidence for ...
|
3297
|
Fluorescence study of ligand binding to potato tuber pyrophosphate-dependent phosphofructokinase: evidence for ...
|
3298
|
Fluorescence study of ligand binding to potato tuber pyrophosphate-dependent phosphofructokinase: evidence for ...
|
3299
|
Roles of low specificity and cofactor interaction sites on thrombin during factor XIII activation. Competition ...
|
3300
|
Roles of low specificity and cofactor interaction sites on thrombin during factor XIII activation. Competition ...
|
3301
|
Roles of low specificity and cofactor interaction sites on thrombin during factor XIII activation. Competition ...
|
3302
|
Roles of low specificity and cofactor interaction sites on thrombin during factor XIII activation. Competition ...
|
3303
|
Roles of low specificity and cofactor interaction sites on thrombin during factor XIII activation. Competition ...
|
3304
|
Roles of low specificity and cofactor interaction sites on thrombin during factor XIII activation. Competition ...
|
3305
|
Roles of low specificity and cofactor interaction sites on thrombin during factor XIII activation. Competition ...
|
3306
|
Roles of low specificity and cofactor interaction sites on thrombin during factor XIII activation. Competition ...
|
3307
|
Roles of low specificity and cofactor interaction sites on thrombin during factor XIII activation. Competition ...
|
3308
|
Roles of low specificity and cofactor interaction sites on thrombin during factor XIII activation. Competition ...
|
3309
|
Roles of low specificity and cofactor interaction sites on thrombin during factor XIII activation. Competition ...
|
3310
|
Roles of low specificity and cofactor interaction sites on thrombin during factor XIII activation. Competition ...
|
3311
|
Roles of low specificity and cofactor interaction sites on thrombin during factor XIII activation. Competition ...
|
3312
|
Roles of low specificity and cofactor interaction sites on thrombin during factor XIII activation. Competition ...
|
3313
|
Roles of low specificity and cofactor interaction sites on thrombin during factor XIII activation. Competition ...
|
3314
|
Roles of low specificity and cofactor interaction sites on thrombin during factor XIII activation. Competition ...
|
3315
|
Roles of low specificity and cofactor interaction sites on thrombin during factor XIII activation. Competition ...
|
3316
|
Roles of low specificity and cofactor interaction sites on thrombin during factor XIII activation. Competition ...
|
3317
|
Roles of low specificity and cofactor interaction sites on thrombin during factor XIII activation. Competition ...
|
3318
|
Roles of low specificity and cofactor interaction sites on thrombin during factor XIII activation. Competition ...
|
3319
|
Roles of low specificity and cofactor interaction sites on thrombin during factor XIII activation. Competition ...
|
3320
|
Roles of low specificity and cofactor interaction sites on thrombin during factor XIII activation. Competition ...
|
3321
|
Roles of low specificity and cofactor interaction sites on thrombin during factor XIII activation. Competition ...
|
3322
|
Roles of low specificity and cofactor interaction sites on thrombin during factor XIII activation. Competition ...
|
3323
|
Roles of low specificity and cofactor interaction sites on thrombin during factor XIII activation. Competition ...
|
3324
|
Roles of low specificity and cofactor interaction sites on thrombin during factor XIII activation. Competition ...
|
3325
|
Roles of low specificity and cofactor interaction sites on thrombin during factor XIII activation. Competition ...
|
3326
|
Roles of low specificity and cofactor interaction sites on thrombin during factor XIII activation. Competition ...
|
3327
|
Roles of low specificity and cofactor interaction sites on thrombin during factor XIII activation. Competition ...
|
3328
|
Roles of low specificity and cofactor interaction sites on thrombin during factor XIII activation. Competition ...
|
3329
|
Aspartate 345 of the dopamine transporter is critical for conformational changes in substrate translocation ...
|
3330
|
Aspartate 345 of the dopamine transporter is critical for conformational changes in substrate translocation ...
|
3331
|
Aspartate 345 of the dopamine transporter is critical for conformational changes in substrate translocation ...
|
3332
|
Aspartate 345 of the dopamine transporter is critical for conformational changes in substrate translocation ...
|
3333
|
Aspartate 345 of the dopamine transporter is critical for conformational changes in substrate translocation ...
|
3334
|
Aspartate 345 of the dopamine transporter is critical for conformational changes in substrate translocation ...
|
3335
|
Aspartate 345 of the dopamine transporter is critical for conformational changes in substrate translocation ...
|
3336
|
Aspartate 345 of the dopamine transporter is critical for conformational changes in substrate translocation ...
|
3337
|
Aspartate 345 of the dopamine transporter is critical for conformational changes in substrate translocation ...
|
3338
|
Aspartate 345 of the dopamine transporter is critical for conformational changes in substrate translocation ...
|
3339
|
Aspartate 345 of the dopamine transporter is critical for conformational changes in substrate translocation ...
|
3340
|
Aspartate 345 of the dopamine transporter is critical for conformational changes in substrate translocation ...
|
3341
|
Aspartate 345 of the dopamine transporter is critical for conformational changes in substrate translocation ...
|
3342
|
Aspartate 345 of the dopamine transporter is critical for conformational changes in substrate translocation ...
|
3343
|
Aspartate 345 of the dopamine transporter is critical for conformational changes in substrate translocation ...
|
3344
|
Aspartate 345 of the dopamine transporter is critical for conformational changes in substrate translocation ...
|
3345
|
Aspartate 345 of the dopamine transporter is critical for conformational changes in substrate translocation ...
|
3346
|
Aspartate 345 of the dopamine transporter is critical for conformational changes in substrate translocation ...
|
3347
|
Aspartate 345 of the dopamine transporter is critical for conformational changes in substrate translocation ...
|
3348
|
Aspartate 345 of the dopamine transporter is critical for conformational changes in substrate translocation ...
|
3349
|
Aspartate 345 of the dopamine transporter is critical for conformational changes in substrate translocation ...
|
3350
|
Aspartate 345 of the dopamine transporter is critical for conformational changes in substrate translocation ...
|
3351
|
Aspartate 345 of the dopamine transporter is critical for conformational changes in substrate translocation ...
|
3352
|
Aspartate 345 of the dopamine transporter is critical for conformational changes in substrate translocation ...
|
3353
|
Aspartate 345 of the dopamine transporter is critical for conformational changes in substrate translocation ...
|
3354
|
Aspartate 345 of the dopamine transporter is critical for conformational changes in substrate translocation ...
|
3355
|
Aspartate 345 of the dopamine transporter is critical for conformational changes in substrate translocation ...
|
3356
|
Aspartate 345 of the dopamine transporter is critical for conformational changes in substrate translocation ...
|
3357
|
Aspartate 345 of the dopamine transporter is critical for conformational changes in substrate translocation ...
|
3358
|
Aspartate 345 of the dopamine transporter is critical for conformational changes in substrate translocation ...
|
3359
|
Aspartate 345 of the dopamine transporter is critical for conformational changes in substrate translocation ...
|
3360
|
Aspartate 345 of the dopamine transporter is critical for conformational changes in substrate translocation ...
|
3361
|
Aspartate 345 of the dopamine transporter is critical for conformational changes in substrate translocation ...
|
3362
|
Aspartate 345 of the dopamine transporter is critical for conformational changes in substrate translocation ...
|
3363
|
Aspartate 345 of the dopamine transporter is critical for conformational changes in substrate translocation ...
|
3364
|
Aspartate 345 of the dopamine transporter is critical for conformational changes in substrate translocation ...
|
3365
|
Aspartate 345 of the dopamine transporter is critical for conformational changes in substrate translocation ...
|
3366
|
Aspartate 345 of the dopamine transporter is critical for conformational changes in substrate translocation ...
|
3367
|
Aspartate 345 of the dopamine transporter is critical for conformational changes in substrate translocation ...
|
3368
|
Aspartate 345 of the dopamine transporter is critical for conformational changes in substrate translocation ...
|
3369
|
Aspartate 345 of the dopamine transporter is critical for conformational changes in substrate translocation ...
|
3370
|
Aspartate 345 of the dopamine transporter is critical for conformational changes in substrate translocation ...
|
3371
|
Aspartate 345 of the dopamine transporter is critical for conformational changes in substrate translocation ...
|
3372
|
Aspartate 345 of the dopamine transporter is critical for conformational changes in substrate translocation ...
|
3373
|
Aspartate 345 of the dopamine transporter is critical for conformational changes in substrate translocation ...
|
3374
|
Aspartate 345 of the dopamine transporter is critical for conformational changes in substrate translocation ...
|
3375
|
Aspartate 345 of the dopamine transporter is critical for conformational changes in substrate translocation ...
|
3376
|
Aspartate 345 of the dopamine transporter is critical for conformational changes in substrate translocation ...
|
3377
|
Aspartate 345 of the dopamine transporter is critical for conformational changes in substrate translocation ...
|
3378
|
Aspartate 345 of the dopamine transporter is critical for conformational changes in substrate translocation ...
|
3379
|
Aspartate 345 of the dopamine transporter is critical for conformational changes in substrate translocation ...
|
3380
|
Aspartate 345 of the dopamine transporter is critical for conformational changes in substrate translocation ...
|
3381
|
Aspartate 345 of the dopamine transporter is critical for conformational changes in substrate translocation ...
|
3382
|
Aspartate 345 of the dopamine transporter is critical for conformational changes in substrate translocation ...
|
3383
|
Aspartate 345 of the dopamine transporter is critical for conformational changes in substrate translocation ...
|
3384
|
Aspartate 345 of the dopamine transporter is critical for conformational changes in substrate translocation ...
|
3385
|
Aspartate 345 of the dopamine transporter is critical for conformational changes in substrate translocation ...
|
3386
|
Aspartate 345 of the dopamine transporter is critical for conformational changes in substrate translocation ...
|
3387
|
Aspartate 345 of the dopamine transporter is critical for conformational changes in substrate translocation ...
|
3388
|
Aspartate 345 of the dopamine transporter is critical for conformational changes in substrate translocation ...
|
3389
|
Aspartate 345 of the dopamine transporter is critical for conformational changes in substrate translocation ...
|
3390
|
Aspartate 345 of the dopamine transporter is critical for conformational changes in substrate translocation ...
|
3391
|
Aspartate 345 of the dopamine transporter is critical for conformational changes in substrate translocation ...
|
3392
|
Aspartate 345 of the dopamine transporter is critical for conformational changes in substrate translocation ...
|
3393
|
Purification and properties of a new S-adenosyl-L-methionine:flavonoid 4`-O-methyltransferase from carnation ...
|
3394
|
Purification and properties of a new S-adenosyl-L-methionine:flavonoid 4`-O-methyltransferase from carnation ...
|
3395
|
Purification and properties of a new S-adenosyl-L-methionine:flavonoid 4`-O-methyltransferase from carnation ...
|
3396
|
Purification and properties of a new S-adenosyl-L-methionine:flavonoid 4`-O-methyltransferase from carnation ...
|
3397
|
The reverse activity of human acid ceramidase
|
3398
|
The reverse activity of human acid ceramidase
|
3399
|
Cuprous oxidase activity of yeast Fet3p and human ceruloplasmin: implication for function
|
3400
|
Cuprous oxidase activity of yeast Fet3p and human ceruloplasmin: implication for function
|
3401
|
Cuprous oxidase activity of yeast Fet3p and human ceruloplasmin: implication for function
|
3402
|
Cuprous oxidase activity of yeast Fet3p and human ceruloplasmin: implication for function
|
3403
|
Structural basis for catalytic differences between alpha class human glutathione transferases hGSTA1-1 and ...
|
3404
|
Structural basis for catalytic differences between alpha class human glutathione transferases hGSTA1-1 and ...
|
3405
|
Structural basis for catalytic differences between alpha class human glutathione transferases hGSTA1-1 and ...
|
3406
|
Structural basis for catalytic differences between alpha class human glutathione transferases hGSTA1-1 and ...
|
3407
|
Structural basis for catalytic differences between alpha class human glutathione transferases hGSTA1-1 and ...
|
3408
|
Structural basis for catalytic differences between alpha class human glutathione transferases hGSTA1-1 and ...
|
3409
|
Structural basis for catalytic differences between alpha class human glutathione transferases hGSTA1-1 and ...
|
3410
|
Structural basis for catalytic differences between alpha class human glutathione transferases hGSTA1-1 and ...
|
3411
|
Structural basis for catalytic differences between alpha class human glutathione transferases hGSTA1-1 and ...
|
3412
|
Structural basis for catalytic differences between alpha class human glutathione transferases hGSTA1-1 and ...
|
3413
|
Structural basis for catalytic differences between alpha class human glutathione transferases hGSTA1-1 and ...
|
3414
|
Structural basis for catalytic differences between alpha class human glutathione transferases hGSTA1-1 and ...
|
3415
|
Structural basis for catalytic differences between alpha class human glutathione transferases hGSTA1-1 and ...
|
3416
|
Structural basis for catalytic differences between alpha class human glutathione transferases hGSTA1-1 and ...
|
3417
|
Structural basis for catalytic differences between alpha class human glutathione transferases hGSTA1-1 and ...
|
3418
|
Structural basis for catalytic differences between alpha class human glutathione transferases hGSTA1-1 and ...
|
3419
|
Structural basis for catalytic differences between alpha class human glutathione transferases hGSTA1-1 and ...
|
3420
|
Structural basis for catalytic differences between alpha class human glutathione transferases hGSTA1-1 and ...
|
3421
|
Structural basis for catalytic differences between alpha class human glutathione transferases hGSTA1-1 and ...
|
3422
|
Structural basis for catalytic differences between alpha class human glutathione transferases hGSTA1-1 and ...
|
3423
|
Structural basis for catalytic differences between alpha class human glutathione transferases hGSTA1-1 and ...
|
3424
|
The cytosolic and glycosomal glyceraldehyde-3-phosphate dehydrogenase from Trypanosoma brucei. Kinetic ...
|
3425
|
The cytosolic and glycosomal glyceraldehyde-3-phosphate dehydrogenase from Trypanosoma brucei. Kinetic ...
|
3426
|
The cytosolic and glycosomal glyceraldehyde-3-phosphate dehydrogenase from Trypanosoma brucei. Kinetic ...
|
3427
|
The cytosolic and glycosomal glyceraldehyde-3-phosphate dehydrogenase from Trypanosoma brucei. Kinetic ...
|
3428
|
The cytosolic and glycosomal glyceraldehyde-3-phosphate dehydrogenase from Trypanosoma brucei. Kinetic ...
|
3429
|
The cytosolic and glycosomal glyceraldehyde-3-phosphate dehydrogenase from Trypanosoma brucei. Kinetic ...
|
3430
|
The cytosolic and glycosomal glyceraldehyde-3-phosphate dehydrogenase from Trypanosoma brucei. Kinetic ...
|
3431
|
The cytosolic and glycosomal glyceraldehyde-3-phosphate dehydrogenase from Trypanosoma brucei. Kinetic ...
|
3432
|
The cytosolic and glycosomal glyceraldehyde-3-phosphate dehydrogenase from Trypanosoma brucei. Kinetic ...
|
3433
|
The cytosolic and glycosomal glyceraldehyde-3-phosphate dehydrogenase from Trypanosoma brucei. Kinetic ...
|
3434
|
The cytosolic and glycosomal glyceraldehyde-3-phosphate dehydrogenase from Trypanosoma brucei. Kinetic ...
|
3435
|
The cytosolic and glycosomal glyceraldehyde-3-phosphate dehydrogenase from Trypanosoma brucei. Kinetic ...
|
3436
|
The cytosolic and glycosomal glyceraldehyde-3-phosphate dehydrogenase from Trypanosoma brucei. Kinetic ...
|
3437
|
The cytosolic and glycosomal glyceraldehyde-3-phosphate dehydrogenase from Trypanosoma brucei. Kinetic ...
|
3438
|
The cytosolic and glycosomal glyceraldehyde-3-phosphate dehydrogenase from Trypanosoma brucei. Kinetic ...
|
3439
|
The cytosolic and glycosomal glyceraldehyde-3-phosphate dehydrogenase from Trypanosoma brucei. Kinetic ...
|
3440
|
Human cytosolic 3alpha-hydroxysteroid dehydrogenases of the aldo-keto reductase superfamily display ...
|
3441
|
Human cytosolic 3alpha-hydroxysteroid dehydrogenases of the aldo-keto reductase superfamily display ...
|
3442
|
Human cytosolic 3alpha-hydroxysteroid dehydrogenases of the aldo-keto reductase superfamily display ...
|
3443
|
Human cytosolic 3alpha-hydroxysteroid dehydrogenases of the aldo-keto reductase superfamily display ...
|
3444
|
Human cytosolic 3alpha-hydroxysteroid dehydrogenases of the aldo-keto reductase superfamily display ...
|
3445
|
Human cytosolic 3alpha-hydroxysteroid dehydrogenases of the aldo-keto reductase superfamily display ...
|
3446
|
Human cytosolic 3alpha-hydroxysteroid dehydrogenases of the aldo-keto reductase superfamily display ...
|
3447
|
Human cytosolic 3alpha-hydroxysteroid dehydrogenases of the aldo-keto reductase superfamily display ...
|
3448
|
Human cytosolic 3alpha-hydroxysteroid dehydrogenases of the aldo-keto reductase superfamily display ...
|
3449
|
Human cytosolic 3alpha-hydroxysteroid dehydrogenases of the aldo-keto reductase superfamily display ...
|
3450
|
Human cytosolic 3alpha-hydroxysteroid dehydrogenases of the aldo-keto reductase superfamily display ...
|
3451
|
Human cytosolic 3alpha-hydroxysteroid dehydrogenases of the aldo-keto reductase superfamily display ...
|
3452
|
Human cytosolic 3alpha-hydroxysteroid dehydrogenases of the aldo-keto reductase superfamily display ...
|
3453
|
Human cytosolic 3alpha-hydroxysteroid dehydrogenases of the aldo-keto reductase superfamily display ...
|
3454
|
Human cytosolic 3alpha-hydroxysteroid dehydrogenases of the aldo-keto reductase superfamily display ...
|
3455
|
Human cytosolic 3alpha-hydroxysteroid dehydrogenases of the aldo-keto reductase superfamily display ...
|
3456
|
Control of glucose utilization in working perfused rat heart
|
3457
|
Control of glucose utilization in working perfused rat heart
|
3458
|
Control of glucose utilization in working perfused rat heart
|
3459
|
Control of glucose utilization in working perfused rat heart
|
3460
|
Control of glucose utilization in working perfused rat heart
|
3461
|
Control of glucose utilization in working perfused rat heart
|
3462
|
Control of glucose utilization in working perfused rat heart
|
3463
|
Control of glucose utilization in working perfused rat heart
|
3464
|
Control of glucose utilization in working perfused rat heart
|
3465
|
Control of glucose utilization in working perfused rat heart
|
3466
|
Control of glucose utilization in working perfused rat heart
|
3467
|
Control of glucose utilization in working perfused rat heart
|
3468
|
Control of glucose utilization in working perfused rat heart
|
3469
|
Control of glucose utilization in working perfused rat heart
|
3470
|
Control of glucose utilization in working perfused rat heart
|
3471
|
Control of glucose utilization in working perfused rat heart
|
3472
|
Control of glucose utilization in working perfused rat heart
|
3473
|
Control of glucose utilization in working perfused rat heart
|
3474
|
Control of glucose utilization in working perfused rat heart
|
3475
|
Control of glucose utilization in working perfused rat heart
|
3476
|
Control of glucose utilization in working perfused rat heart
|
3477
|
Control of glucose utilization in working perfused rat heart
|
3478
|
Control of glucose utilization in working perfused rat heart
|
3479
|
Control of glucose utilization in working perfused rat heart
|
3480
|
Control of glucose utilization in working perfused rat heart
|
3481
|
Control of glucose utilization in working perfused rat heart
|
3482
|
Control of glucose utilization in working perfused rat heart
|
3483
|
Control of glucose utilization in working perfused rat heart
|
3484
|
Control of glucose utilization in working perfused rat heart
|
3485
|
Control of glucose utilization in working perfused rat heart
|
3486
|
Control of glucose utilization in working perfused rat heart
|
3487
|
Control of glucose utilization in working perfused rat heart
|
3488
|
Control of glucose utilization in working perfused rat heart
|
3489
|
Control of glucose utilization in working perfused rat heart
|
3490
|
Control of glucose utilization in working perfused rat heart
|
3491
|
Control of glucose utilization in working perfused rat heart
|
3492
|
Control of glucose utilization in working perfused rat heart
|
3493
|
Control of glucose utilization in working perfused rat heart
|
3494
|
Control of glucose utilization in working perfused rat heart
|
3495
|
Control of glucose utilization in working perfused rat heart
|
3496
|
Snapshots of catalysis: the structure of fructose-1,6-(bis)phosphate aldolase covalently bound to the ...
|
3497
|
Control of the reactivation kinetics of homodimeric triosephosphate isomerase from unfolded monomers
|
3498
|
Control of the reactivation kinetics of homodimeric triosephosphate isomerase from unfolded monomers
|
3499
|
Control of the reactivation kinetics of homodimeric triosephosphate isomerase from unfolded monomers
|
3500
|
Control of the reactivation kinetics of homodimeric triosephosphate isomerase from unfolded monomers
|
3501
|
Purification of the Type II and Type III isozymes of rat hexokinase, expressed in yeast.
|
3502
|
Purification of the Type II and Type III isozymes of rat hexokinase, expressed in yeast.
|
3510
|
Control of dolichyl phosphoglucose formation in human liver microsomes. Kinetic and inhibition studies of ...
|
3511
|
Control of dolichyl phosphoglucose formation in human liver microsomes. Kinetic and inhibition studies of ...
|
3512
|
Characterization of a glucose-repressed pyruvate kinase (Pyk2p) in Saccharomyces cerevisiae that is ...
|
3513
|
Characterization of a glucose-repressed pyruvate kinase (Pyk2p) in Saccharomyces cerevisiae that is ...
|
3514
|
Characterization of a glucose-repressed pyruvate kinase (Pyk2p) in Saccharomyces cerevisiae that is ...
|
3515
|
Characterization of a glucose-repressed pyruvate kinase (Pyk2p) in Saccharomyces cerevisiae that is ...
|
3516
|
Characterization of a glucose-repressed pyruvate kinase (Pyk2p) in Saccharomyces cerevisiae that is ...
|
3517
|
Characterization of a glucose-repressed pyruvate kinase (Pyk2p) in Saccharomyces cerevisiae that is ...
|
3518
|
Kinetic studies of sheep kidney gamma-glutamyl transpeptidase
|
3519
|
Kinetic studies of sheep kidney gamma-glutamyl transpeptidase
|
3520
|
Kinetic studies of sheep kidney gamma-glutamyl transpeptidase
|
3521
|
YMXM motifs of IRS-1 define substrate specificity of the insulin receptor kinase
|
3522
|
YMXM motifs of IRS-1 define substrate specificity of the insulin receptor kinase
|
3523
|
YMXM motifs of IRS-1 define substrate specificity of the insulin receptor kinase
|
3524
|
YMXM motifs of IRS-1 define substrate specificity of the insulin receptor kinase
|
3525
|
YMXM motifs of IRS-1 define substrate specificity of the insulin receptor kinase
|
3526
|
YMXM motifs of IRS-1 define substrate specificity of the insulin receptor kinase
|
3527
|
YMXM motifs of IRS-1 define substrate specificity of the insulin receptor kinase
|
3528
|
YMXM motifs of IRS-1 define substrate specificity of the insulin receptor kinase
|
3529
|
YMXM motifs of IRS-1 define substrate specificity of the insulin receptor kinase
|
3530
|
YMXM motifs of IRS-1 define substrate specificity of the insulin receptor kinase
|
3531
|
YMXM motifs of IRS-1 define substrate specificity of the insulin receptor kinase
|
3532
|
YMXM motifs of IRS-1 define substrate specificity of the insulin receptor kinase
|
3533
|
YMXM motifs of IRS-1 define substrate specificity of the insulin receptor kinase
|
3534
|
YMXM motifs of IRS-1 define substrate specificity of the insulin receptor kinase
|
3535
|
YMXM motifs of IRS-1 define substrate specificity of the insulin receptor kinase
|
3536
|
Mechanistic insight into 3-deoxy-D-manno-octulosonate-8-phosphate synthase and ...
|
3537
|
Mechanistic insight into 3-deoxy-D-manno-octulosonate-8-phosphate synthase and ...
|
3538
|
Mechanistic insight into 3-deoxy-D-manno-octulosonate-8-phosphate synthase and ...
|
3539
|
Mechanistic insight into 3-deoxy-D-manno-octulosonate-8-phosphate synthase and ...
|
3544
|
Purification and Characterization of Phenylalanine 4-Monooxygenase from Rat Liver
|
3545
|
Purification and Characterization of Phenylalanine 4-Monooxygenase from Rat Liver
|
3546
|
Purification and Characterization of Phenylalanine 4-Monooxygenase from Rat Liver
|
3547
|
Purification and Characterization of Phenylalanine 4-Monooxygenase from Rat Liver
|
3548
|
Purification and Characterization of Phenylalanine 4-Monooxygenase from Rat Liver
|
3549
|
Purification and Characterization of Phenylalanine 4-Monooxygenase from Rat Liver
|
3550
|
Purification and Characterization of Phenylalanine 4-Monooxygenase from Rat Liver
|
3551
|
Purification and Characterization of Phenylalanine 4-Monooxygenase from Rat Liver
|
3552
|
Purification and Characterization of Phenylalanine 4-Monooxygenase from Rat Liver
|
3553
|
Purification and Characterization of Phenylalanine 4-Monooxygenase from Rat Liver
|
3554
|
Purification and Characterization of Phenylalanine 4-Monooxygenase from Rat Liver
|
3555
|
Purification and Characterization of Phenylalanine 4-Monooxygenase from Rat Liver
|
3556
|
Isolation and Characterization of a Novel Eukaryotic Monofunctional NAD+-Dependent ...
|
3557
|
Regulation of liver metabolism by enzyme phosphorylation during mammalian hibernation
|
3558
|
Regulation of liver metabolism by enzyme phosphorylation during mammalian hibernation
|
3559
|
Regulation of liver metabolism by enzyme phosphorylation during mammalian hibernation
|
3560
|
Regulation of liver metabolism by enzyme phosphorylation during mammalian hibernation
|
3561
|
Regulation of liver metabolism by enzyme phosphorylation during mammalian hibernation
|
3562
|
Regulation of liver metabolism by enzyme phosphorylation during mammalian hibernation
|
3563
|
Regulation of liver metabolism by enzyme phosphorylation during mammalian hibernation
|
3564
|
Regulation of liver metabolism by enzyme phosphorylation during mammalian hibernation
|
3565
|
Regulation of liver metabolism by enzyme phosphorylation during mammalian hibernation
|
3566
|
Regulation of liver metabolism by enzyme phosphorylation during mammalian hibernation
|
3567
|
Regulation of liver metabolism by enzyme phosphorylation during mammalian hibernation
|
3568
|
Regulation of liver metabolism by enzyme phosphorylation during mammalian hibernation
|
3569
|
Regulation of liver metabolism by enzyme phosphorylation during mammalian hibernation
|
3570
|
Regulation of liver metabolism by enzyme phosphorylation during mammalian hibernation
|
3571
|
Regulation of liver metabolism by enzyme phosphorylation during mammalian hibernation
|
3572
|
Regulation of liver metabolism by enzyme phosphorylation during mammalian hibernation
|
3573
|
Regulation of liver metabolism by enzyme phosphorylation during mammalian hibernation
|
3574
|
Regulation of liver metabolism by enzyme phosphorylation during mammalian hibernation
|
3575
|
Regulation of liver metabolism by enzyme phosphorylation during mammalian hibernation
|
3576
|
Regulation of liver metabolism by enzyme phosphorylation during mammalian hibernation
|
3577
|
The inhibitory effect of halides and carboxylates an hepatic NADH:cytochrome b5 oxidoreductase
|
3578
|
The inhibitory effect of halides and carboxylates an hepatic NADH:cytochrome b5 oxidoreductase
|
3579
|
The inhibitory effect of halides and carboxylates an hepatic NADH:cytochrome b5 oxidoreductase
|
3580
|
The inhibitory effect of halides and carboxylates an hepatic NADH:cytochrome b5 oxidoreductase
|
3581
|
The inhibitory effect of halides and carboxylates an hepatic NADH:cytochrome b5 oxidoreductase
|
3582
|
The inhibitory effect of halides and carboxylates an hepatic NADH:cytochrome b5 oxidoreductase
|
3583
|
The inhibitory effect of halides and carboxylates an hepatic NADH:cytochrome b5 oxidoreductase
|
3584
|
The inhibitory effect of halides and carboxylates an hepatic NADH:cytochrome b5 oxidoreductase
|
3585
|
The inhibitory effect of halides and carboxylates an hepatic NADH:cytochrome b5 oxidoreductase
|
3586
|
The inhibitory effect of halides and carboxylates an hepatic NADH:cytochrome b5 oxidoreductase
|
3587
|
The inhibitory effect of halides and carboxylates an hepatic NADH:cytochrome b5 oxidoreductase
|
3588
|
The inhibitory effect of halides and carboxylates an hepatic NADH:cytochrome b5 oxidoreductase
|
3589
|
The inhibitory effect of halides and carboxylates an hepatic NADH:cytochrome b5 oxidoreductase
|
3590
|
The inhibitory effect of halides and carboxylates an hepatic NADH:cytochrome b5 oxidoreductase
|
3591
|
The inhibitory effect of halides and carboxylates an hepatic NADH:cytochrome b5 oxidoreductase
|
3592
|
The inhibitory effect of halides and carboxylates an hepatic NADH:cytochrome b5 oxidoreductase
|
3593
|
The inhibitory effect of halides and carboxylates an hepatic NADH:cytochrome b5 oxidoreductase
|
3594
|
The inhibitory effect of halides and carboxylates an hepatic NADH:cytochrome b5 oxidoreductase
|
3595
|
The inhibitory effect of halides and carboxylates an hepatic NADH:cytochrome b5 oxidoreductase
|
3596
|
The inhibitory effect of halides and carboxylates an hepatic NADH:cytochrome b5 oxidoreductase
|
3597
|
The inhibitory effect of halides and carboxylates an hepatic NADH:cytochrome b5 oxidoreductase
|
3598
|
The inhibitory effect of halides and carboxylates an hepatic NADH:cytochrome b5 oxidoreductase
|
3599
|
The inhibitory effect of halides and carboxylates an hepatic NADH:cytochrome b5 oxidoreductase
|
3600
|
The inhibitory effect of halides and carboxylates an hepatic NADH:cytochrome b5 oxidoreductase
|
3601
|
The inhibitory effect of halides and carboxylates an hepatic NADH:cytochrome b5 oxidoreductase
|
3602
|
The inhibitory effect of halides and carboxylates an hepatic NADH:cytochrome b5 oxidoreductase
|
3603
|
The inhibitory effect of halides and carboxylates an hepatic NADH:cytochrome b5 oxidoreductase
|
3604
|
The inhibitory effect of halides and carboxylates an hepatic NADH:cytochrome b5 oxidoreductase
|
3605
|
The inhibitory effect of halides and carboxylates an hepatic NADH:cytochrome b5 oxidoreductase
|
3606
|
The inhibitory effect of halides and carboxylates an hepatic NADH:cytochrome b5 oxidoreductase
|
3607
|
The inhibitory effect of halides and carboxylates an hepatic NADH:cytochrome b5 oxidoreductase
|
3608
|
The inhibitory effect of halides and carboxylates an hepatic NADH:cytochrome b5 oxidoreductase
|
3609
|
The inhibitory effect of halides and carboxylates an hepatic NADH:cytochrome b5 oxidoreductase
|
3610
|
The inhibitory effect of halides and carboxylates an hepatic NADH:cytochrome b5 oxidoreductase
|
3611
|
The inhibitory effect of halides and carboxylates an hepatic NADH:cytochrome b5 oxidoreductase
|
3612
|
The inhibitory effect of halides and carboxylates an hepatic NADH:cytochrome b5 oxidoreductase
|
3613
|
The inhibitory effect of halides and carboxylates an hepatic NADH:cytochrome b5 oxidoreductase
|
3614
|
The inhibitory effect of halides and carboxylates an hepatic NADH:cytochrome b5 oxidoreductase
|
3615
|
The inhibitory effect of halides and carboxylates an hepatic NADH:cytochrome b5 oxidoreductase
|
3616
|
The inhibitory effect of halides and carboxylates an hepatic NADH:cytochrome b5 oxidoreductase
|
3617
|
The inhibitory effect of halides and carboxylates an hepatic NADH:cytochrome b5 oxidoreductase
|
3618
|
The inhibitory effect of halides and carboxylates an hepatic NADH:cytochrome b5 oxidoreductase
|
3619
|
The inhibitory effect of halides and carboxylates an hepatic NADH:cytochrome b5 oxidoreductase
|
3620
|
The inhibitory effect of halides and carboxylates an hepatic NADH:cytochrome b5 oxidoreductase
|
3621
|
The inhibitory effect of halides and carboxylates an hepatic NADH:cytochrome b5 oxidoreductase
|
3622
|
The inhibitory effect of halides and carboxylates an hepatic NADH:cytochrome b5 oxidoreductase
|
3623
|
The inhibitory effect of halides and carboxylates an hepatic NADH:cytochrome b5 oxidoreductase
|
3624
|
The inhibitory effect of halides and carboxylates an hepatic NADH:cytochrome b5 oxidoreductase
|
3625
|
The inhibitory effect of halides and carboxylates an hepatic NADH:cytochrome b5 oxidoreductase
|
3626
|
The inhibitory effect of halides and carboxylates an hepatic NADH:cytochrome b5 oxidoreductase
|
3627
|
The inhibitory effect of halides and carboxylates an hepatic NADH:cytochrome b5 oxidoreductase
|
3628
|
The inhibitory effect of halides and carboxylates an hepatic NADH:cytochrome b5 oxidoreductase
|
3629
|
The inhibitory effect of halides and carboxylates an hepatic NADH:cytochrome b5 oxidoreductase
|
3630
|
The inhibitory effect of halides and carboxylates an hepatic NADH:cytochrome b5 oxidoreductase
|
3685
|
Functionally important amino acids in Saccharomyces cerevisiae aspartate kinase
|
3686
|
Functionally important amino acids in Saccharomyces cerevisiae aspartate kinase
|
3687
|
Functionally important amino acids in Saccharomyces cerevisiae aspartate kinase
|
3688
|
Functionally important amino acids in Saccharomyces cerevisiae aspartate kinase
|
3689
|
Functionally important amino acids in Saccharomyces cerevisiae aspartate kinase
|
3690
|
Functionally important amino acids in Saccharomyces cerevisiae aspartate kinase
|
3691
|
Functionally important amino acids in Saccharomyces cerevisiae aspartate kinase
|
3692
|
Functionally important amino acids in Saccharomyces cerevisiae aspartate kinase
|
3693
|
Functionally important amino acids in Saccharomyces cerevisiae aspartate kinase
|
3694
|
Functionally important amino acids in Saccharomyces cerevisiae aspartate kinase
|
3695
|
Functionally important amino acids in Saccharomyces cerevisiae aspartate kinase
|
3696
|
Functionally important amino acids in Saccharomyces cerevisiae aspartate kinase
|
3697
|
Functionally important amino acids in Saccharomyces cerevisiae aspartate kinase
|
3698
|
Functionally important amino acids in Saccharomyces cerevisiae aspartate kinase
|
3699
|
Functionally important amino acids in Saccharomyces cerevisiae aspartate kinase
|
3700
|
Functionally important amino acids in Saccharomyces cerevisiae aspartate kinase
|
3701
|
Functionally important amino acids in Saccharomyces cerevisiae aspartate kinase
|
3702
|
Functionally important amino acids in Saccharomyces cerevisiae aspartate kinase
|
3703
|
Functionally important amino acids in Saccharomyces cerevisiae aspartate kinase
|
3704
|
Functionally important amino acids in Saccharomyces cerevisiae aspartate kinase
|
3705
|
Functionally important amino acids in Saccharomyces cerevisiae aspartate kinase
|
3706
|
Functionally important amino acids in Saccharomyces cerevisiae aspartate kinase
|
3707
|
Functionally important amino acids in Saccharomyces cerevisiae aspartate kinase
|
3708
|
Functionally important amino acids in Saccharomyces cerevisiae aspartate kinase
|
3709
|
Functionally important amino acids in Saccharomyces cerevisiae aspartate kinase
|
3710
|
Functionally important amino acids in Saccharomyces cerevisiae aspartate kinase
|
3711
|
Functionally important amino acids in Saccharomyces cerevisiae aspartate kinase
|
3712
|
Functionally important amino acids in Saccharomyces cerevisiae aspartate kinase
|
3713
|
Functionally important amino acids in Saccharomyces cerevisiae aspartate kinase
|
3714
|
Functionally important amino acids in Saccharomyces cerevisiae aspartate kinase
|
3715
|
Functionally important amino acids in Saccharomyces cerevisiae aspartate kinase
|
3716
|
Functionally important amino acids in Saccharomyces cerevisiae aspartate kinase
|
3717
|
Functionally important amino acids in Saccharomyces cerevisiae aspartate kinase
|
3718
|
Functionally important amino acids in Saccharomyces cerevisiae aspartate kinase
|
3719
|
Functionally important amino acids in Saccharomyces cerevisiae aspartate kinase
|
3720
|
Functionally important amino acids in Saccharomyces cerevisiae aspartate kinase
|
3721
|
Functionally important amino acids in Saccharomyces cerevisiae aspartate kinase
|
3722
|
Functionally important amino acids in Saccharomyces cerevisiae aspartate kinase
|
3723
|
Functionally important amino acids in Saccharomyces cerevisiae aspartate kinase
|
3724
|
Functionally important amino acids in Saccharomyces cerevisiae aspartate kinase
|
3725
|
Functionally important amino acids in Saccharomyces cerevisiae aspartate kinase
|
3726
|
Functionally important amino acids in Saccharomyces cerevisiae aspartate kinase
|
3727
|
Functionally important amino acids in Saccharomyces cerevisiae aspartate kinase
|
3728
|
Cathepsin V, a novel and potent elastolytic activity expressed in activated macrophages
|
3729
|
Cathepsin V, a novel and potent elastolytic activity expressed in activated macrophages
|
3730
|
Cathepsin V, a novel and potent elastolytic activity expressed in activated macrophages
|
3731
|
Cathepsin V, a novel and potent elastolytic activity expressed in activated macrophages
|
3732
|
Kinetic characterization of phenol and aniline derivates as substrates of peroxidase
|
3733
|
Kinetic characterization of phenol and aniline derivates as substrates of peroxidase
|
3734
|
Kinetic characterization of phenol and aniline derivates as substrates of peroxidase
|
3735
|
Kinetic characterization of phenol and aniline derivates as substrates of peroxidase
|
3736
|
Kinetic characterization of phenol and aniline derivates as substrates of peroxidase
|
3737
|
Kinetic characterization of phenol and aniline derivates as substrates of peroxidase
|
3738
|
Kinetic characterization of phenol and aniline derivates as substrates of peroxidase
|
3739
|
Kinetic characterization of phenol and aniline derivates as substrates of peroxidase
|
3740
|
Kinetic characterization of phenol and aniline derivates as substrates of peroxidase
|
3741
|
Kinetic behavior of Desulfovibrio gigas aldehyde oxidoreductase encapsulated in reverse micelles
|
3742
|
Kinetic behavior of Desulfovibrio gigas aldehyde oxidoreductase encapsulated in reverse micelles
|
3743
|
Kinetic behavior of Desulfovibrio gigas aldehyde oxidoreductase encapsulated in reverse micelles
|
3744
|
Kinetic behavior of Desulfovibrio gigas aldehyde oxidoreductase encapsulated in reverse micelles
|
3745
|
Kinetic behavior of Desulfovibrio gigas aldehyde oxidoreductase encapsulated in reverse micelles
|
3746
|
Kinetic behavior of Desulfovibrio gigas aldehyde oxidoreductase encapsulated in reverse micelles
|
3747
|
Kinetic behavior of Desulfovibrio gigas aldehyde oxidoreductase encapsulated in reverse micelles
|
3748
|
A large hinge bending domain rotation is necessary for the catalytic function of Escherichia coli ...
|
3749
|
A large hinge bending domain rotation is necessary for the catalytic function of Escherichia coli ...
|
3750
|
A large hinge bending domain rotation is necessary for the catalytic function of Escherichia coli ...
|
3751
|
A large hinge bending domain rotation is necessary for the catalytic function of Escherichia coli ...
|
3752
|
Lactococcus lactis dihydroorotate dehydrogenase A mutants reveal important facets of the enzymatic function
|
3753
|
Lactococcus lactis dihydroorotate dehydrogenase A mutants reveal important facets of the enzymatic function
|
3754
|
Lactococcus lactis dihydroorotate dehydrogenase A mutants reveal important facets of the enzymatic function
|
3755
|
Lactococcus lactis dihydroorotate dehydrogenase A mutants reveal important facets of the enzymatic function
|
3756
|
Lactococcus lactis dihydroorotate dehydrogenase A mutants reveal important facets of the enzymatic function
|
3757
|
Lactococcus lactis dihydroorotate dehydrogenase A mutants reveal important facets of the enzymatic function
|
3758
|
Lactococcus lactis dihydroorotate dehydrogenase A mutants reveal important facets of the enzymatic function
|
3759
|
Lactococcus lactis dihydroorotate dehydrogenase A mutants reveal important facets of the enzymatic function
|
3760
|
Lactococcus lactis dihydroorotate dehydrogenase A mutants reveal important facets of the enzymatic function
|
3761
|
Lactococcus lactis dihydroorotate dehydrogenase A mutants reveal important facets of the enzymatic function
|
3762
|
Lactococcus lactis dihydroorotate dehydrogenase A mutants reveal important facets of the enzymatic function
|
3763
|
Lactococcus lactis dihydroorotate dehydrogenase A mutants reveal important facets of the enzymatic function
|
3764
|
Lactococcus lactis dihydroorotate dehydrogenase A mutants reveal important facets of the enzymatic function
|
3765
|
Lactococcus lactis dihydroorotate dehydrogenase A mutants reveal important facets of the enzymatic function
|
3766
|
Lactococcus lactis dihydroorotate dehydrogenase A mutants reveal important facets of the enzymatic function
|
3767
|
Lactococcus lactis dihydroorotate dehydrogenase A mutants reveal important facets of the enzymatic function
|
3768
|
Lactococcus lactis dihydroorotate dehydrogenase A mutants reveal important facets of the enzymatic function
|
3769
|
Lactococcus lactis dihydroorotate dehydrogenase A mutants reveal important facets of the enzymatic function
|
3770
|
Lactococcus lactis dihydroorotate dehydrogenase A mutants reveal important facets of the enzymatic function
|
3771
|
Lactococcus lactis dihydroorotate dehydrogenase A mutants reveal important facets of the enzymatic function
|
3772
|
Lactococcus lactis dihydroorotate dehydrogenase A mutants reveal important facets of the enzymatic function
|
3773
|
Lactococcus lactis dihydroorotate dehydrogenase A mutants reveal important facets of the enzymatic function
|
3774
|
Lactococcus lactis dihydroorotate dehydrogenase A mutants reveal important facets of the enzymatic function
|
3775
|
Lactococcus lactis dihydroorotate dehydrogenase A mutants reveal important facets of the enzymatic function
|
3776
|
Lactococcus lactis dihydroorotate dehydrogenase A mutants reveal important facets of the enzymatic function
|
3777
|
Lactococcus lactis dihydroorotate dehydrogenase A mutants reveal important facets of the enzymatic function
|
3778
|
Lactococcus lactis dihydroorotate dehydrogenase A mutants reveal important facets of the enzymatic function
|
3779
|
Lactococcus lactis dihydroorotate dehydrogenase A mutants reveal important facets of the enzymatic function
|
3780
|
Lactococcus lactis dihydroorotate dehydrogenase A mutants reveal important facets of the enzymatic function
|
3781
|
Lactococcus lactis dihydroorotate dehydrogenase A mutants reveal important facets of the enzymatic function
|
3782
|
Lactococcus lactis dihydroorotate dehydrogenase A mutants reveal important facets of the enzymatic function
|
3783
|
Novel psychrophilic and thermolabile L-threonine dehydrogenase from psychrophilic Cytophaga sp. strain KUC-1
|
3784
|
Novel psychrophilic and thermolabile L-threonine dehydrogenase from psychrophilic Cytophaga sp. strain KUC-1
|
3785
|
Novel psychrophilic and thermolabile L-threonine dehydrogenase from psychrophilic Cytophaga sp. strain KUC-1
|
3786
|
Novel psychrophilic and thermolabile L-threonine dehydrogenase from psychrophilic Cytophaga sp. strain KUC-1
|
3787
|
Novel psychrophilic and thermolabile L-threonine dehydrogenase from psychrophilic Cytophaga sp. strain KUC-1
|
3788
|
Novel psychrophilic and thermolabile L-threonine dehydrogenase from psychrophilic Cytophaga sp. strain KUC-1
|
3789
|
Novel psychrophilic and thermolabile L-threonine dehydrogenase from psychrophilic Cytophaga sp. strain KUC-1
|
3790
|
Novel psychrophilic and thermolabile L-threonine dehydrogenase from psychrophilic Cytophaga sp. strain KUC-1
|
3791
|
Novel psychrophilic and thermolabile L-threonine dehydrogenase from psychrophilic Cytophaga sp. strain KUC-1
|
3792
|
L-Threonine dehydrogenase of chicken liver. Purification, characterization, and physiological significance
|
3793
|
Multiple hydrogen kinetic isotope effects for enzymes catalyzing exchange with solvent: application to alanine ...
|
3794
|
Multiple hydrogen kinetic isotope effects for enzymes catalyzing exchange with solvent: application to alanine ...
|
3795
|
Multiple hydrogen kinetic isotope effects for enzymes catalyzing exchange with solvent: application to alanine ...
|
3796
|
Multiple hydrogen kinetic isotope effects for enzymes catalyzing exchange with solvent: application to alanine ...
|
3797
|
Crystal structure of human glutathione S-transferase A3-3 and mechanistic implications for its high steroid ...
|
3798
|
Crystal structure of human glutathione S-transferase A3-3 and mechanistic implications for its high steroid ...
|
3799
|
Crystal structure of human glutathione S-transferase A3-3 and mechanistic implications for its high steroid ...
|
3800
|
Crystal structure of human glutathione S-transferase A3-3 and mechanistic implications for its high steroid ...
|
3801
|
Effects of cryostabilizers, low temperature, and freezing on the kinetics of the pectin ...
|
3802
|
Effects of cryostabilizers, low temperature, and freezing on the kinetics of the pectin ...
|
3803
|
Effects of cryostabilizers, low temperature, and freezing on the kinetics of the pectin ...
|
3804
|
Organ-specific human alcohol dehydrogenase: Isolation and characterization of isozymes from testis
|
3805
|
Organ-specific human alcohol dehydrogenase: Isolation and characterization of isozymes from testis
|
3806
|
Organ-specific human alcohol dehydrogenase: Isolation and characterization of isozymes from testis
|
3807
|
Carboxymethylproline synthase from Pectobacterium carotorova: a multifaceted member of the crotonase ...
|
3808
|
Carboxymethylproline synthase from Pectobacterium carotorova: a multifaceted member of the crotonase ...
|
3809
|
Carboxymethylproline synthase from Pectobacterium carotorova: a multifaceted member of the crotonase ...
|
3810
|
Carboxymethylproline synthase from Pectobacterium carotorova: a multifaceted member of the crotonase ...
|
3811
|
Carboxymethylproline synthase from Pectobacterium carotorova: a multifaceted member of the crotonase ...
|
3812
|
Carboxymethylproline synthase from Pectobacterium carotorova: a multifaceted member of the crotonase ...
|
3813
|
Carboxymethylproline synthase from Pectobacterium carotorova: a multifaceted member of the crotonase ...
|
3814
|
Ornithine decarboxylase promotes catalysis by binding the carboxylate in a buried pocket containing ...
|
3815
|
The active site and mechanism of action of recombinant acetohydroxy acid synthase from tobacco
|
3816
|
The active site and mechanism of action of recombinant acetohydroxy acid synthase from tobacco
|
3817
|
Coenzyme site-directed mutants of photosynthetic A4-GAPDH show selectively reduced NADPH-dependent catalysis, ...
|
3818
|
Coenzyme site-directed mutants of photosynthetic A4-GAPDH show selectively reduced NADPH-dependent catalysis, ...
|
3819
|
Coenzyme site-directed mutants of photosynthetic A4-GAPDH show selectively reduced NADPH-dependent catalysis, ...
|
3820
|
Coenzyme site-directed mutants of photosynthetic A4-GAPDH show selectively reduced NADPH-dependent catalysis, ...
|
3821
|
Coenzyme site-directed mutants of photosynthetic A4-GAPDH show selectively reduced NADPH-dependent catalysis, ...
|
3822
|
Coenzyme site-directed mutants of photosynthetic A4-GAPDH show selectively reduced NADPH-dependent catalysis, ...
|
3823
|
Coenzyme site-directed mutants of photosynthetic A4-GAPDH show selectively reduced NADPH-dependent catalysis, ...
|
3824
|
Coenzyme site-directed mutants of photosynthetic A4-GAPDH show selectively reduced NADPH-dependent catalysis, ...
|
3825
|
Coenzyme site-directed mutants of photosynthetic A4-GAPDH show selectively reduced NADPH-dependent catalysis, ...
|
3826
|
Coenzyme site-directed mutants of photosynthetic A4-GAPDH show selectively reduced NADPH-dependent catalysis, ...
|
3827
|
Mouse liver CYP2C39 is a novel retinoic acid 4-hydroxylase. Its down-regulation offers a molecular basis for ...
|
3828
|
Production and characterization of the Talaromyces stipitatus feruloyl esterase FAEC in Pichia pastoris: ...
|
3829
|
Production and characterization of the Talaromyces stipitatus feruloyl esterase FAEC in Pichia pastoris: ...
|
3830
|
Production and characterization of the Talaromyces stipitatus feruloyl esterase FAEC in Pichia pastoris: ...
|
3831
|
Production and characterization of the Talaromyces stipitatus feruloyl esterase FAEC in Pichia pastoris: ...
|
3832
|
NAD-dependent methylenetetrahydrofolate dehydrogenase-methenyltetrahydrofolate cyclohydrolase is the mammalian ...
|
3833
|
NAD-dependent methylenetetrahydrofolate dehydrogenase-methenyltetrahydrofolate cyclohydrolase is the mammalian ...
|
3834
|
NAD-dependent methylenetetrahydrofolate dehydrogenase-methenyltetrahydrofolate cyclohydrolase is the mammalian ...
|
3835
|
NAD-dependent methylenetetrahydrofolate dehydrogenase-methenyltetrahydrofolate cyclohydrolase is the mammalian ...
|
3836
|
Perforation of the tunnel wall in carbamoyl phosphate synthetase derails the passage of ammonia between ...
|
3837
|
Perforation of the tunnel wall in carbamoyl phosphate synthetase derails the passage of ammonia between ...
|
3838
|
Perforation of the tunnel wall in carbamoyl phosphate synthetase derails the passage of ammonia between ...
|
3839
|
Perforation of the tunnel wall in carbamoyl phosphate synthetase derails the passage of ammonia between ...
|
3840
|
Perforation of the tunnel wall in carbamoyl phosphate synthetase derails the passage of ammonia between ...
|
3841
|
Perforation of the tunnel wall in carbamoyl phosphate synthetase derails the passage of ammonia between ...
|
3842
|
Perforation of the tunnel wall in carbamoyl phosphate synthetase derails the passage of ammonia between ...
|
3843
|
Perforation of the tunnel wall in carbamoyl phosphate synthetase derails the passage of ammonia between ...
|
3844
|
Perforation of the tunnel wall in carbamoyl phosphate synthetase derails the passage of ammonia between ...
|
3845
|
Perforation of the tunnel wall in carbamoyl phosphate synthetase derails the passage of ammonia between ...
|
3846
|
Perforation of the tunnel wall in carbamoyl phosphate synthetase derails the passage of ammonia between ...
|
3847
|
Perforation of the tunnel wall in carbamoyl phosphate synthetase derails the passage of ammonia between ...
|
3848
|
Perforation of the tunnel wall in carbamoyl phosphate synthetase derails the passage of ammonia between ...
|
3849
|
Perforation of the tunnel wall in carbamoyl phosphate synthetase derails the passage of ammonia between ...
|
3850
|
Perforation of the tunnel wall in carbamoyl phosphate synthetase derails the passage of ammonia between ...
|
3851
|
Perforation of the tunnel wall in carbamoyl phosphate synthetase derails the passage of ammonia between ...
|
3852
|
Perforation of the tunnel wall in carbamoyl phosphate synthetase derails the passage of ammonia between ...
|
3853
|
Perforation of the tunnel wall in carbamoyl phosphate synthetase derails the passage of ammonia between ...
|
3854
|
Perforation of the tunnel wall in carbamoyl phosphate synthetase derails the passage of ammonia between ...
|
3855
|
Perforation of the tunnel wall in carbamoyl phosphate synthetase derails the passage of ammonia between ...
|
3856
|
Perforation of the tunnel wall in carbamoyl phosphate synthetase derails the passage of ammonia between ...
|
3857
|
Perforation of the tunnel wall in carbamoyl phosphate synthetase derails the passage of ammonia between ...
|
3858
|
Perforation of the tunnel wall in carbamoyl phosphate synthetase derails the passage of ammonia between ...
|
3859
|
Perforation of the tunnel wall in carbamoyl phosphate synthetase derails the passage of ammonia between ...
|
3860
|
Perforation of the tunnel wall in carbamoyl phosphate synthetase derails the passage of ammonia between ...
|
3861
|
Perforation of the tunnel wall in carbamoyl phosphate synthetase derails the passage of ammonia between ...
|
3862
|
Perforation of the tunnel wall in carbamoyl phosphate synthetase derails the passage of ammonia between ...
|
3863
|
Perforation of the tunnel wall in carbamoyl phosphate synthetase derails the passage of ammonia between ...
|
3864
|
Perforation of the tunnel wall in carbamoyl phosphate synthetase derails the passage of ammonia between ...
|
3865
|
Perforation of the tunnel wall in carbamoyl phosphate synthetase derails the passage of ammonia between ...
|
3866
|
Perforation of the tunnel wall in carbamoyl phosphate synthetase derails the passage of ammonia between ...
|
3867
|
Perforation of the tunnel wall in carbamoyl phosphate synthetase derails the passage of ammonia between ...
|
3868
|
Perforation of the tunnel wall in carbamoyl phosphate synthetase derails the passage of ammonia between ...
|
3869
|
Perforation of the tunnel wall in carbamoyl phosphate synthetase derails the passage of ammonia between ...
|
3870
|
Perforation of the tunnel wall in carbamoyl phosphate synthetase derails the passage of ammonia between ...
|
3871
|
Perforation of the tunnel wall in carbamoyl phosphate synthetase derails the passage of ammonia between ...
|
3872
|
Perforation of the tunnel wall in carbamoyl phosphate synthetase derails the passage of ammonia between ...
|
3873
|
Perforation of the tunnel wall in carbamoyl phosphate synthetase derails the passage of ammonia between ...
|
3874
|
Perforation of the tunnel wall in carbamoyl phosphate synthetase derails the passage of ammonia between ...
|
3875
|
Serine acetyltransferase of Escherichia coli: substrate specificity and feedback control by cysteine
|
3876
|
Serine acetyltransferase of Escherichia coli: substrate specificity and feedback control by cysteine
|
3877
|
Serine acetyltransferase of Escherichia coli: substrate specificity and feedback control by cysteine
|
3878
|
Serine acetyltransferase of Escherichia coli: substrate specificity and feedback control by cysteine
|
3879
|
Serine acetyltransferase of Escherichia coli: substrate specificity and feedback control by cysteine
|
3880
|
Key amino acid residues in the regulation of soluble methane monooxygenase catalysis by component B
|
3881
|
Key amino acid residues in the regulation of soluble methane monooxygenase catalysis by component B
|
3882
|
Key amino acid residues in the regulation of soluble methane monooxygenase catalysis by component B
|
3883
|
Key amino acid residues in the regulation of soluble methane monooxygenase catalysis by component B
|
3884
|
Key amino acid residues in the regulation of soluble methane monooxygenase catalysis by component B
|
3885
|
Key amino acid residues in the regulation of soluble methane monooxygenase catalysis by component B
|
3886
|
Key amino acid residues in the regulation of soluble methane monooxygenase catalysis by component B
|
3887
|
Key amino acid residues in the regulation of soluble methane monooxygenase catalysis by component B
|
3888
|
Key amino acid residues in the regulation of soluble methane monooxygenase catalysis by component B
|
3889
|
Key amino acid residues in the regulation of soluble methane monooxygenase catalysis by component B
|
3890
|
Key amino acid residues in the regulation of soluble methane monooxygenase catalysis by component B
|
3891
|
Key amino acid residues in the regulation of soluble methane monooxygenase catalysis by component B
|
3892
|
Key amino acid residues in the regulation of soluble methane monooxygenase catalysis by component B
|
3893
|
Key amino acid residues in the regulation of soluble methane monooxygenase catalysis by component B
|
3894
|
Key amino acid residues in the regulation of soluble methane monooxygenase catalysis by component B
|
3895
|
Key amino acid residues in the regulation of soluble methane monooxygenase catalysis by component B
|
3896
|
Key amino acid residues in the regulation of soluble methane monooxygenase catalysis by component B
|
3897
|
Key amino acid residues in the regulation of soluble methane monooxygenase catalysis by component B
|
3898
|
Key amino acid residues in the regulation of soluble methane monooxygenase catalysis by component B
|
3899
|
Key amino acid residues in the regulation of soluble methane monooxygenase catalysis by component B
|
3900
|
Key amino acid residues in the regulation of soluble methane monooxygenase catalysis by component B
|
3901
|
Key amino acid residues in the regulation of soluble methane monooxygenase catalysis by component B
|
3902
|
Key amino acid residues in the regulation of soluble methane monooxygenase catalysis by component B
|
3903
|
Key amino acid residues in the regulation of soluble methane monooxygenase catalysis by component B
|
3904
|
Key amino acid residues in the regulation of soluble methane monooxygenase catalysis by component B
|
3905
|
Key amino acid residues in the regulation of soluble methane monooxygenase catalysis by component B
|
3906
|
Key amino acid residues in the regulation of soluble methane monooxygenase catalysis by component B
|
3907
|
Key amino acid residues in the regulation of soluble methane monooxygenase catalysis by component B
|
3908
|
Key amino acid residues in the regulation of soluble methane monooxygenase catalysis by component B
|
3909
|
Key amino acid residues in the regulation of soluble methane monooxygenase catalysis by component B
|
3910
|
Key amino acid residues in the regulation of soluble methane monooxygenase catalysis by component B
|
3911
|
Key amino acid residues in the regulation of soluble methane monooxygenase catalysis by component B
|
3912
|
Key amino acid residues in the regulation of soluble methane monooxygenase catalysis by component B
|
3913
|
Key amino acid residues in the regulation of soluble methane monooxygenase catalysis by component B
|
3914
|
Key amino acid residues in the regulation of soluble methane monooxygenase catalysis by component B
|
3915
|
Key amino acid residues in the regulation of soluble methane monooxygenase catalysis by component B
|
3916
|
Key amino acid residues in the regulation of soluble methane monooxygenase catalysis by component B
|
3917
|
Key amino acid residues in the regulation of soluble methane monooxygenase catalysis by component B
|
3918
|
Key amino acid residues in the regulation of soluble methane monooxygenase catalysis by component B
|
3919
|
Key amino acid residues in the regulation of soluble methane monooxygenase catalysis by component B
|
3920
|
Key amino acid residues in the regulation of soluble methane monooxygenase catalysis by component B
|
3921
|
Key amino acid residues in the regulation of soluble methane monooxygenase catalysis by component B
|
3922
|
Key amino acid residues in the regulation of soluble methane monooxygenase catalysis by component B
|
3923
|
Key amino acid residues in the regulation of soluble methane monooxygenase catalysis by component B
|
3924
|
Key amino acid residues in the regulation of soluble methane monooxygenase catalysis by component B
|
3925
|
Key amino acid residues in the regulation of soluble methane monooxygenase catalysis by component B
|
3926
|
Key amino acid residues in the regulation of soluble methane monooxygenase catalysis by component B
|
3927
|
Key amino acid residues in the regulation of soluble methane monooxygenase catalysis by component B
|
3928
|
Key amino acid residues in the regulation of soluble methane monooxygenase catalysis by component B
|
3929
|
Key amino acid residues in the regulation of soluble methane monooxygenase catalysis by component B
|
3930
|
Key amino acid residues in the regulation of soluble methane monooxygenase catalysis by component B
|
3931
|
Maize C4 NADP-malic enzyme. Expression in Escherichia coli and characterization of site-directed mutants at ...
|
3932
|
Maize C4 NADP-malic enzyme. Expression in Escherichia coli and characterization of site-directed mutants at ...
|
3933
|
Maize C4 NADP-malic enzyme. Expression in Escherichia coli and characterization of site-directed mutants at ...
|
3934
|
Maize C4 NADP-malic enzyme. Expression in Escherichia coli and characterization of site-directed mutants at ...
|
3935
|
Maize C4 NADP-malic enzyme. Expression in Escherichia coli and characterization of site-directed mutants at ...
|
3936
|
Maize C4 NADP-malic enzyme. Expression in Escherichia coli and characterization of site-directed mutants at ...
|
3937
|
Maize C4 NADP-malic enzyme. Expression in Escherichia coli and characterization of site-directed mutants at ...
|
3938
|
Structural and functional impairment of an Old Yellow Enzyme homologue upon affinity tag incorporation
|
3939
|
Structural and functional impairment of an Old Yellow Enzyme homologue upon affinity tag incorporation
|
3940
|
Structural and functional impairment of an Old Yellow Enzyme homologue upon affinity tag incorporation
|
3941
|
Structural and functional impairment of an Old Yellow Enzyme homologue upon affinity tag incorporation
|
3942
|
Structural and functional impairment of an Old Yellow Enzyme homologue upon affinity tag incorporation
|
3943
|
Chromogenic assay for the activity of sphingomyelinase from Bacillus cereus and its application to the ...
|
3944
|
Chromogenic assay for the activity of sphingomyelinase from Bacillus cereus and its application to the ...
|
3945
|
Chromogenic assay for the activity of sphingomyelinase from Bacillus cereus and its application to the ...
|
3946
|
Chromogenic assay for the activity of sphingomyelinase from Bacillus cereus and its application to the ...
|
3947
|
Chromogenic assay for the activity of sphingomyelinase from Bacillus cereus and its application to the ...
|
3948
|
Chromogenic assay for the activity of sphingomyelinase from Bacillus cereus and its application to the ...
|
3949
|
Chromogenic assay for the activity of sphingomyelinase from Bacillus cereus and its application to the ...
|
3950
|
Chromogenic assay for the activity of sphingomyelinase from Bacillus cereus and its application to the ...
|
3951
|
Chromogenic assay for the activity of sphingomyelinase from Bacillus cereus and its application to the ...
|
3952
|
Reactions of trans-3-chloroacrylic acid dehalogenase with acetylene substrates: consequences of and evidence ...
|
3953
|
Reactions of trans-3-chloroacrylic acid dehalogenase with acetylene substrates: consequences of and evidence ...
|
3954
|
Reactions of trans-3-chloroacrylic acid dehalogenase with acetylene substrates: consequences of and evidence ...
|
3955
|
Spatial activities and induction of glutamate-cysteine ligase (GCL) in the postimplantation rat embryo and ...
|
3956
|
Spatial activities and induction of glutamate-cysteine ligase (GCL) in the postimplantation rat embryo and ...
|
3957
|
Spatial activities and induction of glutamate-cysteine ligase (GCL) in the postimplantation rat embryo and ...
|
3958
|
Spatial activities and induction of glutamate-cysteine ligase (GCL) in the postimplantation rat embryo and ...
|
3959
|
Kinetic analysis of Escherichia coli 2-C-methyl-D-erythritol-4-phosphate cytidyltransferase, wild type and ...
|
3960
|
Kinetic analysis of Escherichia coli 2-C-methyl-D-erythritol-4-phosphate cytidyltransferase, wild type and ...
|
3961
|
Kinetic analysis of Escherichia coli 2-C-methyl-D-erythritol-4-phosphate cytidyltransferase, wild type and ...
|
3962
|
Kinetic analysis of Escherichia coli 2-C-methyl-D-erythritol-4-phosphate cytidyltransferase, wild type and ...
|
3963
|
Kinetic analysis of Escherichia coli 2-C-methyl-D-erythritol-4-phosphate cytidyltransferase, wild type and ...
|
3964
|
Kinetic analysis of Escherichia coli 2-C-methyl-D-erythritol-4-phosphate cytidyltransferase, wild type and ...
|
3965
|
Kinetic analysis of Escherichia coli 2-C-methyl-D-erythritol-4-phosphate cytidyltransferase, wild type and ...
|
3966
|
Kinetic analysis of Escherichia coli 2-C-methyl-D-erythritol-4-phosphate cytidyltransferase, wild type and ...
|
3967
|
Kinetic analysis of Escherichia coli 2-C-methyl-D-erythritol-4-phosphate cytidyltransferase, wild type and ...
|
3968
|
Kinetic analysis of Escherichia coli 2-C-methyl-D-erythritol-4-phosphate cytidyltransferase, wild type and ...
|
3969
|
Kinetic analysis of Escherichia coli 2-C-methyl-D-erythritol-4-phosphate cytidyltransferase, wild type and ...
|
3970
|
Kinetic analysis of Escherichia coli 2-C-methyl-D-erythritol-4-phosphate cytidyltransferase, wild type and ...
|
3971
|
Kinetic analysis of Escherichia coli 2-C-methyl-D-erythritol-4-phosphate cytidyltransferase, wild type and ...
|
3972
|
Kinetic analysis of Escherichia coli 2-C-methyl-D-erythritol-4-phosphate cytidyltransferase, wild type and ...
|
3973
|
Kinetic analysis of Escherichia coli 2-C-methyl-D-erythritol-4-phosphate cytidyltransferase, wild type and ...
|
3974
|
Kinetic analysis of Escherichia coli 2-C-methyl-D-erythritol-4-phosphate cytidyltransferase, wild type and ...
|
3975
|
Kinetic analysis of Escherichia coli 2-C-methyl-D-erythritol-4-phosphate cytidyltransferase, wild type and ...
|
3976
|
Kinetic analysis of Escherichia coli 2-C-methyl-D-erythritol-4-phosphate cytidyltransferase, wild type and ...
|
3977
|
A kinetic analysis of the nucleotide-induced allosteric transitions in a single-ring mutant of GroEL
|
3978
|
A kinetic analysis of the nucleotide-induced allosteric transitions in a single-ring mutant of GroEL
|
3979
|
A kinetic analysis of the nucleotide-induced allosteric transitions in a single-ring mutant of GroEL
|
3980
|
Asparagine 285 plays a key role in transition state stabilization in rabbit muscle creatine kinase
|
3981
|
Asparagine 285 plays a key role in transition state stabilization in rabbit muscle creatine kinase
|
3982
|
Asparagine 285 plays a key role in transition state stabilization in rabbit muscle creatine kinase
|
3983
|
Asparagine 285 plays a key role in transition state stabilization in rabbit muscle creatine kinase
|
3984
|
Asparagine 285 plays a key role in transition state stabilization in rabbit muscle creatine kinase
|
3985
|
Asparagine 285 plays a key role in transition state stabilization in rabbit muscle creatine kinase
|
3986
|
Asparagine 285 plays a key role in transition state stabilization in rabbit muscle creatine kinase
|
3987
|
Asparagine 285 plays a key role in transition state stabilization in rabbit muscle creatine kinase
|
3988
|
Asparagine 285 plays a key role in transition state stabilization in rabbit muscle creatine kinase
|
3989
|
Asparagine 285 plays a key role in transition state stabilization in rabbit muscle creatine kinase
|
3990
|
Asparagine 285 plays a key role in transition state stabilization in rabbit muscle creatine kinase
|
3991
|
Asparagine 285 plays a key role in transition state stabilization in rabbit muscle creatine kinase
|
3992
|
Asparagine 285 plays a key role in transition state stabilization in rabbit muscle creatine kinase
|
3993
|
Asparagine 285 plays a key role in transition state stabilization in rabbit muscle creatine kinase
|
3994
|
Asparagine 285 plays a key role in transition state stabilization in rabbit muscle creatine kinase
|
3995
|
Asparagine 285 plays a key role in transition state stabilization in rabbit muscle creatine kinase
|
3996
|
Asparagine 285 plays a key role in transition state stabilization in rabbit muscle creatine kinase
|
3997
|
Asparagine 285 plays a key role in transition state stabilization in rabbit muscle creatine kinase
|
3998
|
Asparagine 285 plays a key role in transition state stabilization in rabbit muscle creatine kinase
|
3999
|
Effects of multiple ligand binding on kinetic isotope effects in PQQ-dependent methanol dehydrogenase
|
4000
|
Effects of multiple ligand binding on kinetic isotope effects in PQQ-dependent methanol dehydrogenase
|