The 1.6-A crystal structure of the class of chaperones represented by Escherichia coli Hsp31 reveals a putative catalytic triad
about
Parkinsonism-associated protein DJ-1/Park7 is a major protein deglycase that repairs methylglyoxal- and glyoxal-glycated cysteine, arginine, and lysine residuesEvolutionary and functional relationships within the DJ1 superfamilyKeeping up with protein foldingCrystal structure of human DJ-1, a protein associated with early onset Parkinson's diseaseThe crystal structure of DJ-1, a protein related to male fertility and Parkinson's diseaseThe 1.1-A resolution crystal structure of DJ-1, the protein mutated in autosomal recessive early onset Parkinson's diseaseCrystal structure of DJ-1/RS and implication on familial Parkinson's diseaseCrystal structures of human DJ-1 and Escherichia coli Hsp31, which share an evolutionarily conserved domainThe crystal structure of Leishmania major 3-mercaptopyruvate sulfurtransferase. A three-domain architecture with a serine protease-like triad at the active siteThe crystal structure of Escherichia coli heat shock protein YedU reveals three potential catalytic active sitesA new native EcHsp31 structure suggests a key role of structural flexibility for chaperone functionThe 1.8-A resolution crystal structure of YDR533Cp from Saccharomyces cerevisiae: A member of the DJ-1/ThiJ/PfpI superfamilyCysteine p K a Depression by a Protonated Glutamic Acid in Human DJ-1 † ‡Evolution of New Enzymatic Function by Structural Modulation of Cysteine Reactivity in Pseudomonas fluorescens Isocyanide HydrataseStructure of Hsp33/YOR391Cp from the yeastSaccharomyces cerevisiaeConservation of oxidative protein stabilization in an insect homologue of parkinsonism-associated protein DJ-1A Glutathione-independent Glyoxalase of the DJ-1 Superfamily Plays an Important Role in Managing Metabolically Generated Methylglyoxal in Candida albicansStereospecific mechanism of DJ-1 glyoxalases inferred from their hemithioacetal-containing crystal structuresL166P mutant DJ-1, causative for recessive Parkinson's disease, is degraded through the ubiquitin-proteasome systemIdentification of functional subclasses in the DJ-1 superfamily proteins.Identification of glutathione (GSH)-independent glyoxalase III from Schizosaccharomyces pombe.Metabolic role for yeast DJ-1 superfamily proteins.Protein aggregation in a mutant deficient in yajL, the bacterial homolog of the Parkinsonism-associated protein DJ-1Biofabrication of ZnS:Mn luminescent nanocrystals using histidine, hexahistidine, and His-tagged proteins: a comparison study.Hsp31 of Escherichia coli K-12 is glyoxalase III.Translational defects in a mutant deficient in YajL, the bacterial homolog of the parkinsonism-associated protein DJ-1.The linker-loop region of Escherichia coli chaperone Hsp31 functions as a gate that modulates high-affinity substrate binding at elevated temperaturesIn silico engineering of aggregation-prone recombinant proteins for substrate recognition by the chaperonin GroELA role for the Parkinson's disease protein DJ-1 as a chaperone and antioxidant in the anhydrobiotic nematode Panagrolaimus superbus.The role of cysteine oxidation in DJ-1 function and dysfunction.Characterization of the PH1704 protease from Pyrococcus horikoshii OT3 and the critical functions of Tyr120.Protein misfolding in neurodegenerative diseases.Structural and biochemical studies on Vibrio cholerae Hsp31 reveals a novel dimeric form and Glutathione-independent Glyoxalase activity.Purification, crystallization and preliminary X-ray analysis of Hsp33 from Saccharomyces cerevisiae.Dissection of the dimerization modes in the DJ-1 superfamily.Gene expression profiling in human neurodegenerative disease.Glyoxalase biochemistry.Cloning, expression, purification, crystallization and preliminary X-ray analysis of the 31 kDa Vibrio cholerae heat-shock protein VcHsp31.ROS-dependent regulation of Parkin and DJ-1 localization during oxidative stress in neurons.Regulation of Escherichia coli hchA, a stress-inducible gene encoding molecular chaperone Hsp31.
P2860
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P2860
The 1.6-A crystal structure of the class of chaperones represented by Escherichia coli Hsp31 reveals a putative catalytic triad
description
2003 nî lūn-bûn
@nan
2003 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
2003 թվականի մարտին հրատարակված գիտական հոդված
@hy
2003年の論文
@ja
2003年論文
@yue
2003年論文
@zh-hant
2003年論文
@zh-hk
2003年論文
@zh-mo
2003年論文
@zh-tw
2003年论文
@wuu
name
The 1.6-A crystal structure of ...... als a putative catalytic triad
@ast
The 1.6-A crystal structure of ...... als a putative catalytic triad
@en
The 1.6-A crystal structure of ...... als a putative catalytic triad
@nl
type
label
The 1.6-A crystal structure of ...... als a putative catalytic triad
@ast
The 1.6-A crystal structure of ...... als a putative catalytic triad
@en
The 1.6-A crystal structure of ...... als a putative catalytic triad
@nl
prefLabel
The 1.6-A crystal structure of ...... als a putative catalytic triad
@ast
The 1.6-A crystal structure of ...... als a putative catalytic triad
@en
The 1.6-A crystal structure of ...... als a putative catalytic triad
@nl
P2093
P2860
P921
P356
P1476
The 1.6-A crystal structure of ...... als a putative catalytic triad
@en
P2093
Francois Baneyx
Paulene M Quigley
Wim G J Hol
P2860
P304
P356
10.1073/PNAS.0530312100
P407
P577
2003-03-05T00:00:00Z