The crystal structure of the reduced, Zn2+-bound form of the B. subtilis Hsp33 chaperone and its implications for the activation mechanism.
about
Protein design: toward functional metalloenzymesStructure and function of Bacillus subtilis YphP, a prokaryotic disulfide isomerase with a CXC catalytic motifCrystal Structures of Archaemetzincin Reveal a Moldable Substrate-Binding SiteHydrogen-deuterium exchange mass spectrometry for determining protein structural changes in drug discovery.First- and second-shell metal binding residues in human proteins are disproportionately associated with disease-related SNPs.Minimal functional sites allow a classification of zinc sites in proteins.Application of protein engineering to enhance crystallizability and improve crystal properties.Archease from Pyrococcus abyssi improves substrate specificity and solubility of a tRNA m5C methyltransferase.Thiol-based redox switchesRedox-regulated chaperones.Unfolding of metastable linker region is at the core of Hsp33 activation as a redox-regulated chaperoneConditionally and transiently disordered proteins: awakening cryptic disorder to regulate protein function.Hypoxia-induced changes in pulmonary and systemic vascular resistance: where is the O2 sensor?Systematic replacement of lysine with glutamine and alanine in Escherichia coli malate synthase G: effect on crystallization.Beyond transcription--new mechanisms for the regulation of molecular chaperones.Oxygen sensing in hypoxic pulmonary vasoconstriction: using new tools to answer an age-old question.E. coli chaperones DnaK, Hsp33 and Spy inhibit bacterial functional amyloid assembly.The redox-switch domain of Hsp33 functions as dual stress sensorDisorder in the lifetime of a proteinClassification of the treble clef zinc finger: noteworthy lessons for structure and function evolution.On the design of zinc-finger models with cyclic peptides bearing a linear tail.A dynamic zinc redox switch.HSP33 in eukaryotes - an evolutionary tale of a chaperone adapted to photosynthetic organisms.Stress-Activated Chaperones: A First Line of Defense.An inter-subunit disulfide bond of artemin acts as a redox switch for its chaperone-like activity.Structure of Nm23-H1 under oxidative conditions.Crystal structure of constitutively monomeric E. coli Hsp33 mutant with chaperone activity.
P2860
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P2860
The crystal structure of the reduced, Zn2+-bound form of the B. subtilis Hsp33 chaperone and its implications for the activation mechanism.
description
2004 nî lūn-bûn
@nan
2004 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2004 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
2004年の論文
@ja
2004年論文
@yue
2004年論文
@zh-hant
2004年論文
@zh-hk
2004年論文
@zh-mo
2004年論文
@zh-tw
2004年论文
@wuu
name
The crystal structure of the r ...... for the activation mechanism.
@ast
The crystal structure of the r ...... for the activation mechanism.
@en
type
label
The crystal structure of the r ...... for the activation mechanism.
@ast
The crystal structure of the r ...... for the activation mechanism.
@en
prefLabel
The crystal structure of the r ...... for the activation mechanism.
@ast
The crystal structure of the r ...... for the activation mechanism.
@en
P2093
P2860
P50
P1433
P1476
The crystal structure of the r ...... for the activation mechanism.
@en
P2093
David R Cooper
Izabela Janda
Jakub Bielnicki
Paul C F Graf
Ursula Jakob
Yancho Devedjiev
Zygmunt S Derewenda
P2860
P304
P356
10.1016/J.STR.2004.08.003
P577
2004-10-01T00:00:00Z