Evidence for an induced-fit mechanism operating in pi class glutathione transferases
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The crystal structures of glutathione S-transferases isozymes 1-3 and 1-4 from Anopheles dirus species BThermodynamic description of the effect of the mutation Y49F on human glutathione transferase P1-1 in binding with glutathione and the inhibitor S-hexylglutathioneDiuretic drug binding to human glutathione transferase P1-1: potential role of Cys-101 revealed in the double mutant C47S/Y108VCrystal structures and kinetic studies of human Kappa class glutathione transferase provide insights into the catalytic mechanismMice lacking three Loci encoding 14 glutathione transferase genes: a novel tool for assigning function to the GSTP, GSTM, and GSTT families.Detecting the native ligand orientation by interfacial rigidity: SiteInterlock.Calorimetric and structural studies of the nitric oxide carrier S-nitrosoglutathione bound to human glutathione transferase P1-1S-nitrosation of glutathione transferase p1-1 is controlled by the conformation of a dynamic active site helix.Nested Arg-specific bifunctional crosslinkers for MS-based structural analysis of proteins and protein assembliesBuffer interference with protein dynamics: a case study on human liver fatty acid binding protein.Monobromobimane occupies a distinct xenobiotic substrate site in glutathione S-transferase pi.Arabidopsis thaliana dehydroascorbate reductase 2: Conformational flexibility during catalysis.The structural roles of a conserved small hydrophobic core in the active site and an ionic bridge in domain I of Delta class glutathione S-transferase.Modeling analysis of GST (glutathione-S-transferases) from Wuchereria bancrofti and Brugia malayi.Side-chain flexibility in protein-ligand binding: the minimal rotation hypothesis.Electrostatic interactions affecting the active site of class sigma glutathione S-transferase.Solution structure of polyglutamine tracts in GST-polyglutamine fusion proteins.Functional role of the lock and key motif at the subunit interface of glutathione transferase p1-1.Glutathione S-transferase Pi has at least three distinguishable xenobiotic substrate sites close to its glutathione-binding site.Structure of the major cytosolic glutathione S-transferase from the parasitic nematode Onchocerca volvulus.Temperature adaptation of glutathione S-transferase P1-1. A case for homotropic regulation of substrate binding.
P2860
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P2860
Evidence for an induced-fit mechanism operating in pi class glutathione transferases
description
1998 nî lūn-bûn
@nan
1998 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
1998 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
1998年の論文
@ja
1998年論文
@yue
1998年論文
@zh-hant
1998年論文
@zh-hk
1998年論文
@zh-mo
1998年論文
@zh-tw
1998年论文
@wuu
name
Evidence for an induced-fit mechanism operating in pi class glutathione transferases
@ast
Evidence for an induced-fit mechanism operating in pi class glutathione transferases
@en
Evidence for an induced-fit mechanism operating in pi class glutathione transferases
@nl
type
label
Evidence for an induced-fit mechanism operating in pi class glutathione transferases
@ast
Evidence for an induced-fit mechanism operating in pi class glutathione transferases
@en
Evidence for an induced-fit mechanism operating in pi class glutathione transferases
@nl
prefLabel
Evidence for an induced-fit mechanism operating in pi class glutathione transferases
@ast
Evidence for an induced-fit mechanism operating in pi class glutathione transferases
@en
Evidence for an induced-fit mechanism operating in pi class glutathione transferases
@nl
P2093
P356
P1433
P1476
Evidence for an induced-fit mechanism operating in pi class glutathione transferases
@en
P2093
A J Oakley
G Federici
M Lo Bello
M W Parker
P304
P356
10.1021/BI980323W
P407
P577
1998-07-14T00:00:00Z