Crystal structure of triosephosphate isomerase complexed with 2-phosphoglycolate at 0.83-A resolution
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Predicting functional sites with an automated algorithm suitable for heterogeneous datasetsStructure of Plasmodium falciparum triose-phosphate isomerase-2-phosphoglycerate complex at 1.1-A resolutionProbing the role of the fully conserved Cys126 in triosephosphate isomerase by site-specific mutagenesis--distal effects on dimer stabilityHigh resolution crystal structures of triosephosphate isomerase complexed with its suicide inhibitors: The conformational flexibility of the catalytic glutamate in its closed, liganded active siteStructural and functional perturbation of Giardia lamblia triosephosphate isomerase by modification of a non-catalytic, non-conserved regionThe Potential of Secondary Metabolites from Plants as Drugs or Leads against Protozoan Neglected Diseases-Part III: In-Silico Molecular Docking InvestigationsReflections on the catalytic power of a TIM-barrel.Nonplanar peptide bonds in proteins are common and conserved but not biased toward active sites.Enzymatic catalysis of proton transfer at carbon: activation of triosephosphate isomerase by phosphite dianion.Wildtype and engineered monomeric triosephosphate isomerase from Trypanosoma brucei: partitioning of reaction intermediates in D2O and activation by phosphite dianion.Role of Lys-12 in catalysis by triosephosphate isomerase: a two-part substrate approach.Rescue of K12G triosephosphate isomerase by ammonium cations: the reaction of an enzyme in pieces.Triosephosphate isomerase I170V alters catalytic site, enhances stability and induces pathology in a Drosophila model of TPI deficiency.The activating oxydianion binding domain for enzyme-catalyzed proton transfer, hydride transfer, and decarboxylation: specificity and enzyme architecture.Mechanism for activation of triosephosphate isomerase by phosphite dianion: the role of a ligand-driven conformational change.An empirical test of the concomitantly variable codon hypothesis.Mechanism for activation of triosephosphate isomerase by phosphite dianion: the role of a hydrophobic clampDynamic requirements for a functional protein hingeRole of Loop-Clamping Side Chains in Catalysis by Triosephosphate Isomerase.Magnitude and origin of the enhanced basicity of the catalytic glutamate of triosephosphate isomeraseEffects of cell volume regulating osmolytes on glycerol 3-phosphate binding to triosephosphate isomeraseStructure-Function Studies of Hydrophobic Residues That Clamp a Basic Glutamate Side Chain during Catalysis by Triosephosphate IsomeraseStructural mutations that probe the interactions between the catalytic and dianion activation sites of triosephosphate isomerase.Role of a guanidinium cation-phosphodianion pair in stabilizing the vinyl carbanion intermediate of orotidine 5'-phosphate decarboxylase-catalyzed reactions.Mechanistic Imperatives for Deprotonation of Carbon Catalyzed by Triosephosphate Isomerase: Enzyme-Activation by Phosphite Dianion.Enzyme architecture: remarkably similar transition states for triosephosphate isomerase-catalyzed reactions of the whole substrate and the substrate in piecesA role for flexible loops in enzyme catalysis.A paradigm for enzyme-catalyzed proton transfer at carbon: triosephosphate isomerase.Enzyme architecture: on the importance of being in a protein cage.Crystal structures of two monomeric triosephosphate isomerase variants identified via a directed-evolution protocol selecting for L-arabinose isomerase activity.Enzyme Architecture: Modeling the Operation of a Hydrophobic Clamp in Catalysis by Triosephosphate Isomerase.Expression, purification, crystallization and preliminary X-ray diffraction studies of triosephosphate isomerase from methicillin-resistant Staphylococcus aureus (MRSA252).The folding pathway of glycosomal triosephosphate isomerase: structural insights into equilibrium intermediates.Detection of alternative conformations by unrestrained refinement.Stereoelectronic requirements for optimal hydrogen-bond-catalyzed enolization.Enzyme Architecture: Amino Acid Side-Chains That Function To Optimize the Basicity of the Active Site Glutamate of Triosephosphate IsomeraseCytolethal Distending Toxin: A Unique Variation on the AB Toxin Paradigm
P2860
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P2860
Crystal structure of triosephosphate isomerase complexed with 2-phosphoglycolate at 0.83-A resolution
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2003 nî lūn-bûn
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2003 թուականի Մարտին հրատարակուած գիտական յօդուած
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2003年の論文
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2003年論文
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2003年論文
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2003年論文
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2003年論文
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2003年論文
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2003年论文
@wuu
name
Crystal structure of triosepho ...... glycolate at 0.83-A resolution
@ast
Crystal structure of triosepho ...... glycolate at 0.83-A resolution
@en
Crystal structure of triosepho ...... glycolate at 0.83-A resolution
@nl
type
label
Crystal structure of triosepho ...... glycolate at 0.83-A resolution
@ast
Crystal structure of triosepho ...... glycolate at 0.83-A resolution
@en
Crystal structure of triosepho ...... glycolate at 0.83-A resolution
@nl
prefLabel
Crystal structure of triosepho ...... glycolate at 0.83-A resolution
@ast
Crystal structure of triosepho ...... glycolate at 0.83-A resolution
@en
Crystal structure of triosepho ...... glycolate at 0.83-A resolution
@nl
P2860
P356
P1476
Crystal structure of triosepho ...... glycolate at 0.83-A resolution
@en
P2093
Inari Kursula
Rik K Wierenga
P2860
P304
P356
10.1074/JBC.M211389200
P407
P577
2003-03-14T00:00:00Z