Crystal structure of proteolytic fragments of the redox-sensitive Hsp33 with constitutive chaperone activity
about
An NMR approach to structural proteomics.Crystal structures of human DJ-1 and Escherichia coli Hsp31, which share an evolutionarily conserved domainThe crystal structure of the reduced, Zn2+-bound form of the B. subtilis Hsp33 chaperone and its implications for the activation mechanism.The conserved lid tryptophan, W211, potentiates thermostability and thermoactivity in bacterial thermoalkalophilic lipasesArchease from Pyrococcus abyssi improves substrate specificity and solubility of a tRNA m5C methyltransferase.Unfolding of metastable linker region is at the core of Hsp33 activation as a redox-regulated chaperoneAlpha-crystallin-type heat shock proteins: socializing minichaperones in the context of a multichaperone network.Thermodynamic analysis of a molecular chaperone binding to unfolded protein substrates.Beyond transcription--new mechanisms for the regulation of molecular chaperones.Hsp33 controls elongation factor-Tu stability and allows Escherichia coli growth in the absence of the major DnaK and trigger factor chaperonesThe redox-switch domain of Hsp33 functions as dual stress sensorRoles of the N- and C-terminal sequences in Hsp27 self-association and chaperone activity.Home Alone: Elimination of All but One Alternative Sigma Factor in Listeria monocytogenes Allows Prediction of New Roles for σB.PrrC from Rhodobacter sphaeroides, a homologue of eukaryotic Sco proteins, is a copper-binding protein and may have a thiol-disulfide oxidoreductase activity.Activation of the redox-regulated chaperone Hsp33 by domain unfolding.Oligomeric Hsp33 with enhanced chaperone activity: gel filtration, cross-linking, and small angle x-ray scattering (SAXS) analysis.Crystal structure of constitutively monomeric E. coli Hsp33 mutant with chaperone activity.Verification of the interdomain contact site in the inactive monomer, and the domain-swapped fold in the active dimer of Hsp33 in solution.
P2860
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P2860
Crystal structure of proteolytic fragments of the redox-sensitive Hsp33 with constitutive chaperone activity
description
2001 nî lūn-bûn
@nan
2001 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի մայիսին հրատարակված գիտական հոդված
@hy
2001年の論文
@ja
2001年論文
@yue
2001年論文
@zh-hant
2001年論文
@zh-hk
2001年論文
@zh-mo
2001年論文
@zh-tw
2001年论文
@wuu
name
Crystal structure of proteolyt ...... onstitutive chaperone activity
@ast
Crystal structure of proteolyt ...... onstitutive chaperone activity
@en
Crystal structure of proteolyt ...... onstitutive chaperone activity
@nl
type
label
Crystal structure of proteolyt ...... onstitutive chaperone activity
@ast
Crystal structure of proteolyt ...... onstitutive chaperone activity
@en
Crystal structure of proteolyt ...... onstitutive chaperone activity
@nl
prefLabel
Crystal structure of proteolyt ...... onstitutive chaperone activity
@ast
Crystal structure of proteolyt ...... onstitutive chaperone activity
@en
Crystal structure of proteolyt ...... onstitutive chaperone activity
@nl
P2093
P921
P356
P1476
Crystal structure of proteolyt ...... onstitutive chaperone activity
@en
P2093
P304
P356
10.1038/87639
P577
2001-05-01T00:00:00Z