Structural Changes Common to Catalysis in the Tpx Peroxiredoxin Subfamily
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Utilizing Natural and Engineered Peroxiredoxins As Intracellular Peroxide ReportersA primer on peroxiredoxin biochemistryMapping the Active Site Helix-to-Strand Conversion of CxxxxC Peroxiredoxin Q EnzymesStructural Characterisation of Tpx from Yersinia pseudotuberculosis Reveals Insights into the Binding of Salicylidene Acylhydrazide CompoundsCysteine Dioxygenase Structures from pH4 to 9: Consistent Cys-Persulfenate Formation at Intermediate pH and a Cys-Bound Enzyme at Higher pHThe Sensitive Balance between the Fully Folded and Locally Unfolded Conformations of a Model PeroxiredoxinThe structure of an orthorhombic crystal form of a `forced reduced' thiol peroxidase reveals lattice formation aided by the presence of the affinity tagObserved octameric assembly of a Plasmodium yoelii peroxiredoxin can be explained by the replacement of native "ball-and-socket" interacting residues by an affinity tag.Hydrogen-deuterium exchange mass spectrometry for determining protein structural changes in drug discovery.Tuning of peroxiredoxin catalysis for various physiological rolesStructure-based insights into the catalytic power and conformational dexterity of peroxiredoxins.A novel 1-Cys thioredoxin peroxidase gene in Apis cerana cerana: characterization of AccTpx4 and its role in oxidative stresses.Human umbilical cord blood cells protect oligodendrocytes from brain ischemia through Akt signal transduction.Peroxiredoxins in parasites.Why do bacteria use so many enzymes to scavenge hydrogen peroxide?An anaerobic bacterium, Bacteroides thetaiotaomicron, uses a consortium of enzymes to scavenge hydrogen peroxide.Identification of bacterial target proteins for the salicylidene acylhydrazide class of virulence-blocking compounds.Evolution and function of the Mycoplasma hyopneumoniae peroxiredoxin, a 2-Cys-like enzyme with a single Cys residue.Crystal and solution structural studies of mouse phospholipid hydroperoxide glutathione peroxidase 4.Expression, purification, crystallization and initial X-ray diffraction analysis of thiol peroxidase from Yersinia pseudotuberculosisHydroperoxide and peroxynitrite reductase activity of poplar thioredoxin-dependent glutathione peroxidase 5: kinetics, catalytic mechanism and oxidative inactivation
P2860
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P2860
Structural Changes Common to Catalysis in the Tpx Peroxiredoxin Subfamily
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2009 nî lūn-bûn
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2009 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
2009 թվականի նոյեմբերին հրատարակված գիտական հոդված
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2009年の論文
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2009年論文
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2009年論文
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2009年論文
@zh-hk
2009年論文
@zh-mo
2009年論文
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2009年论文
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name
Structural Changes Common to Catalysis in the Tpx Peroxiredoxin Subfamily
@ast
Structural Changes Common to Catalysis in the Tpx Peroxiredoxin Subfamily
@en
Structural Changes Common to Catalysis in the Tpx Peroxiredoxin Subfamily
@nl
type
label
Structural Changes Common to Catalysis in the Tpx Peroxiredoxin Subfamily
@ast
Structural Changes Common to Catalysis in the Tpx Peroxiredoxin Subfamily
@en
Structural Changes Common to Catalysis in the Tpx Peroxiredoxin Subfamily
@nl
prefLabel
Structural Changes Common to Catalysis in the Tpx Peroxiredoxin Subfamily
@ast
Structural Changes Common to Catalysis in the Tpx Peroxiredoxin Subfamily
@en
Structural Changes Common to Catalysis in the Tpx Peroxiredoxin Subfamily
@nl
P2860
P1476
Structural changes common to catalysis in the Tpx peroxiredoxin subfamily
@en
P2093
Andrea Hall
Banumathi Sankaran
P2860
P304
P356
10.1016/J.JMB.2009.08.040
P407
P577
2009-08-21T00:00:00Z