The redox-switch domain of Hsp33 functions as dual stress sensor
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Bleach activates a redox-regulated chaperone by oxidative protein unfoldingProtein plasticity underlines activation and function of ATP-independent chaperonesBacterial responses to reactive chlorine speciesThe roles of conditional disorder in redox proteinsRedox-switch modulation of human SSADH by dynamic catalytic loopStructural and Biochemical Bases for the Redox Sensitivity of Mycobacterium tuberculosis RslAThe protein targeting factor Get3 functions as ATP-independent chaperone under oxidative stress conditions.Role of cysteines in the stability and DNA-binding activity of the hypochlorite-specific transcription factor HypTSuccinic semialdehyde dehydrogenase: biochemical-molecular-clinical disease mechanisms, redox regulation, and functional significanceZinc coordination is essential for the function and activity of the type II secretion ATPase EpsEROSics: chemistry and proteomics of cysteine modifications in redox biology.Redox biology: computational approaches to the investigation of functional cysteine residuesCP12 from Chlamydomonas reinhardtii, a permanent specific "chaperone-like" protein of glyceraldehyde-3-phosphate dehydrogenase.Redox regulation of the human dual specificity phosphatase YVH1 through disulfide bond formation.Thiol-based redox switchesRedox-regulated chaperones.Interplay of cellular cAMP levels, {sigma}S activity and oxidative stress resistance in Escherichia coli.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.Thermodynamic analysis of a molecular chaperone binding to unfolded protein substrates.Conditional disorder in chaperone action.Are zinc-finger domains of protein kinase C dynamic structures that unfold by lipid or redox activation?Transcriptomic analysis of Staphylococcus xylosus in the presence of nitrate and nitrite in meat reveals its response to nitrosative stressPsychrobacter arcticus 273-4 uses resource efficiency and molecular motion adaptations for subzero temperature growth.Protein quality control under oxidative stress conditions.About the dangers, costs and benefits of living an aerobic lifestyle.An effective method for profiling the selenium-binding proteins using its reactive metabolic intermediate.Analysis and functional prediction of reactive cysteine residues.Hsp33 confers bleach resistance by protecting elongation factor Tu against oxidative degradation in Vibrio cholerae.Characterization of two Lactococcus lactis zinc membrane proteins, Llmg_0524 and Llmg_0526, and role of Llmg_0524 in cell wall integrityOrder out of disorder: working cycle of an intrinsically unfolded chaperone.Redox-switch regulatory mechanism of thiolase from Clostridium acetobutylicum.Foldon unfolding mediates the interconversion between M(pro)-C monomer and 3D domain-swapped dimerCysteine reactivity distinguishes redox sensing by the heat-inducible and constitutive forms of heat shock protein 70Protein unfolding as a switch from self-recognition to high-affinity client bindingQuantifying changes in the thiol redox proteome upon oxidative stress in vivo.Tyr130 phosphorylation triggers Syk release from antigen receptor by long-distance conformational uncoupling.Oxidant sensing by reversible disulfide bond formationFunctional diversity of cysteine residues in proteins and unique features of catalytic redox-active cysteines in thiol oxidoreductasesA new oxidative sensing and regulation pathway mediated by the MgrA homologue SarZ in Staphylococcus aureus.
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The redox-switch domain of Hsp33 functions as dual stress sensor
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on 21 May 2007
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
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vědecký článek
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name
The redox-switch domain of Hsp33 functions as dual stress sensor
@en
The redox-switch domain of Hsp33 functions as dual stress sensor.
@nl
type
label
The redox-switch domain of Hsp33 functions as dual stress sensor
@en
The redox-switch domain of Hsp33 functions as dual stress sensor.
@nl
prefLabel
The redox-switch domain of Hsp33 functions as dual stress sensor
@en
The redox-switch domain of Hsp33 functions as dual stress sensor.
@nl
P2093
P2860
P356
P1476
The redox-switch domain of Hsp33 functions as dual stress sensor
@en
P2093
Hauke Lilie
Janina Horst
Jeannette Winter
Marianne Ilbert
Paul C F Graf
Sebastian Ahrens
Ursula Jakob
P2860
P2888
P304
P356
10.1038/NSMB1244
P577
2007-05-21T00:00:00Z
P5875
P6179
1039040046