Beyond transcription--new mechanisms for the regulation of molecular chaperones (Q36069364)

12 August 2017

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title

Beyond transcription--new mechanisms for the regulation of molecular chaperones (English)

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12 August 2017

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Jeannette Winter

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12 August 2017

Ursula Jakob

series ordinal

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12 August 2017

publication date

1 September 2004

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Critical Reviews in Biochemistry and Molecular Biology

12 August 2017

published in

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12 August 2017

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12 August 2017

issue

5-6

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12 August 2017

page(s)

297-317

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BAG-1--a nucleotide exchange factor of Hsc70 with multiple cellular functions

12 August 2017

cites work

1 reference

https://api.crossref.org/works/10.1080%2F10409230490900658

Reactive oxygen species: metabolism, oxidative stress, and signal transduction

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490900658

Regulation of the OxyR transcription factor by hydrogen peroxide and the cellular thiol-disulfide status

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490900658

Two redox centers within Yap1 for H2O2 and thiol-reactive chemicals signaling

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490900658

Mass spectrometry unravels disulfide bond formation as the mechanism that activates a molecular chaperone.

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490900658

The small heat-shock protein Hsp26 of Saccharomyces cerevisiae assembles into a high molecular weight aggregate

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490900658

Protein Oxidation in Aging, Disease, and Oxidative Stress

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490900658

Quality control in the endoplasmic reticulum: PDI mediates the ER retention of unassembled procollagen C-propeptides

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490900658

ER protein quality control and proteasome-mediated protein degradation

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490900658

The Hsp70 and Hsp60 Chaperone Machines

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490900658

Redox regulation of heat shock protein expression in aging and neurodegenerative disorders associated with oxidative stress: a nutritional approach.

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490900658

Characterization of twenty-six new heat shock genes of Escherichia coli

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490900658

Genealogy of the alpha-crystallin--small heat-shock protein superfamily

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490900658

H2O2 sensing through oxidation of the Yap1 transcription factor

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490900658

Mutations that allow disulfide bond formation in the cytoplasm of Escherichia coli.

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490900658

Trigger factor and DnaK cooperate in folding of newly synthesized proteins.

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490900658

Temperature-controlled activity of DnaK-DnaJ-GrpE chaperones: protein-folding arrest and recovery during and after heat shock depends on the substrate protein and the GrpE concentration

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490900658

In vivo kinetics of a redox-regulated transcriptional switch

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490900658

Binding of non-native protein to Hsp25 during heat shock creates a reservoir of folding intermediates for reactivation.

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490900658

Quality control in the endoplasmic reticulum

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490900658

Protein Folding: Importance of the Anfinsen Cage

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490900658

Principles of protein folding in the cellular environment

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490900658

Pathways for protein disulphide bond formation

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490900658

The ERO1 gene of yeast is required for oxidation of protein dithiols in the endoplasmic reticulum

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490900658

Protein disulfide isomerases exploit synergy between catalytic and specific binding domains

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490900658

Protein folding in the cell

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490900658

Export of a cysteine-free misfolded secretory protein from the endoplasmic reticulum for degradation requires interaction with protein disulfide isomerase

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490900658

Virulence and the heat shock response

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490900658

Redox-regulated molecular chaperones

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490900658

Activation of the redox-regulated chaperone Hsp33 by domain unfolding.

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490900658

Reversible thermal transition in GrpE, the nucleotide exchange factor of the DnaK heat-shock system

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490900658

Thermosensor action of GrpE. The DnaK chaperone system at heat shock temperatures

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490900658

Folding properties of the nucleotide exchange factor GrpE from Thermus thermophilus: GrpE is a thermosensor that mediates heat shock response

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490900658

GrpE, a nucleotide exchange factor for DnaK.

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490900658

Crystal structure of the nucleotide exchange factor GrpE bound to the ATPase domain of the molecular chaperone DnaK

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490900658

Molecular chaperones in the cytosol: from nascent chain to folded protein

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490900658

sHsps and their role in the chaperone network

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490900658

Hsp42 is the general small heat shock protein in the cytosol of Saccharomyces cerevisiae

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490900658

Hsp26: a temperature-regulated chaperone

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490900658

Identification of a redox-regulated chaperone network

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490900658

Pathways of Oxidative Damage

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490900658

Chaperone activity with a redox switch

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490900658

The crystal structure of the reduced, Zn2+-bound form of the B. subtilis Hsp33 chaperone and its implications for the activation mechanism

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490900658

RsrA, an anti-sigma factor regulated by redox change

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490900658

Crystal structure of proteolytic fragments of the redox-sensitive Hsp33 with constitutive chaperone activity

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490900658

The b' domain provides the principal peptide-binding site of protein disulfide isomerase but all domains contribute to binding of misfolded proteins

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490900658

A small heat shock protein stably binds heat-denatured model substrates and can maintain a substrate in a folding-competent state

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490900658

A small heat shock protein cooperates with heat shock protein 70 systems to reactivate a heat-denatured protein

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490900658

Targeting of cholera toxin and Escherichia coli heat labile toxin in polarized epithelia: role of COOH-terminal KDEL

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490900658

Redox regulation of PI 3-kinase signalling via inactivation of PTEN

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490900658

Not every disulfide lasts forever: disulfide bond formation as a redox switch

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490900658

The roles of the two zinc binding sites in DnaJ.

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490900658

Is protein disulfide isomerase a redox-dependent molecular chaperone?

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490900658

Microbial molecular chaperones.

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490900658

Chaperonin-mediated protein folding at the surface of groEL through a 'molten globule'-like intermediate

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490900658

BiP and PDI cooperate in the oxidative folding of antibodies in vitro

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490900658

Molecular basis for interactions of the DnaK chaperone with substrates.

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490900658

Evolving questions and paradigm shifts in endoplasmic-reticulum-associated degradation (ERAD).

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490900658

A subset of chaperones and folding enzymes form multiprotein complexes in endoplasmic reticulum to bind nascent proteins

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490900658

Refolding of substrates bound to small Hsps relies on a disaggregation reaction mediated most efficiently by ClpB/DnaK.

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490900658

Identification of thermolabile Escherichia coli proteins: prevention and reversion of aggregation by DnaK and ClpB.

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490900658

Sequential assistance of molecular chaperones and transient formation of covalent complexes during protein degradation from the ER.

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490900658

Heat shock regulation of sigmaS turnover: a role for DnaK and relationship between stress responses mediated by sigmaS and sigma32 in Escherichia coli

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490900658

Protein disulfide isomerase: the multifunctional redox chaperone of the endoplasmic reticulum

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490900658

Induction of a heat shock-like response by unfolded protein in Escherichia coli: dependence on protein level not protein degradation

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490900658

Collagens: molecular biology, diseases, and potentials for therapy

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490900658

Structural perturbation of alpha-crystallin and its chaperone-like activity

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490900658

Genome-wide expression profiling in Escherichia coli K-12

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490900658

Hsp90: chaperoning signal transduction

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490900658

Regulation of Hsp27 oligomerization, chaperone function, and protective activity against oxidative stress/tumor necrosis factor alpha by phosphorylation

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490900658

Proteome analysis in the study of the bacterial heat-shock response

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490900658

Its substrate specificity characterizes the DnaJ co-chaperone as a scanning factor for the DnaK chaperone.

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490900658

Redox regulation of protein tyrosine phosphatase 1B involves a sulphenyl-amide intermediate

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490900658

Kinetics of molecular chaperone action

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490900658

Effect of protein disulfide isomerase on the rate-determining steps of the folding of bovine pancreatic ribonuclease A.

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490900658

Immediate response of the DnaK molecular chaperone system to heat shock

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490900658

Quality control in the endoplasmic reticulum protein factory

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490900658

Oxidation of Methionine Residues of Proteins: Biological Consequences

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490900658

Analysis of the regulation of the molecular chaperone Hsp26 by temperature-induced dissociation: the N-terminal domail is important for oligomer assembly and the binding of unfolding proteins

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490900658

Different mechanisms of thioredoxin in its reduced and oxidized forms in defense against hydrogen peroxide in Escherichia coli.

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490900658

Levels of DnaK and DnaJ provide tight control of heat shock gene expression and protein repair in Escherichia coli.

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490900658

Unfolded cholera toxin is transferred to the ER membrane and released from protein disulfide isomerase upon oxidation by Ero1

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490900658

Biochemical basis of oxidative protein folding in the endoplasmic reticulum

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490900658

Oxidative protein folding in eukaryotes: mechanisms and consequences

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490900658

Redox control of cell death

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490900658

Crystal structure and assembly of a eukaryotic small heat shock protein

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490900658

Oxidation state of the active-site cysteine in protein tyrosine phosphatase 1B

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490900658

Molecular chaperones--cellular machines for protein folding

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490900658

Catalytic activity and chaperone function of human protein-disulfide isomerase are required for the efficient refolding of proinsulin

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490900658

Solution structure and dynamics of a heat shock protein assembly probed by hydrogen exchange and mass spectrometry.

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490900658

The zinc-dependent redox switch domain of the chaperone Hsp33 has a novel fold

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490900658

Reversing the Inactivation of Peroxiredoxins Caused by Cysteine Sulfinic Acid Formation

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490900658

Structure of the native cysteine-sulfenic acid redox center of enterococcal NADH peroxidase refined at 2.8 A resolution

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490900658

More than folding: localized functions of cytosolic chaperones

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490900658

The Three-dimensional Crystal Structure of Cholera Toxin

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490900658

Activation of the OxyR Transcription Factor by Reversible Disulfide Bond Formation

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490900658

Analysis of the Interaction of Small Heat Shock Proteins with Unfolding Proteins

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490900658

Protein Disulfide Isomerase Acts as a Redox-Dependent Chaperone to Unfold Cholera Toxin

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490900658

Activation of the Redox-Regulated Molecular Chaperone Hsp33—A Two-Step Mechanism

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490900658

The 2.2 Å Crystal Structure of Hsp33

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490900658

Differential Temperature-dependent Chaperone-like Activity of αA- and αB-crystallin Homoaggregates

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490900658

21 January 2018

GroEL under Heat-Shock

1 reference

https://api.crossref.org/works/10.1080%2F10409230490900658

Identification of in vivo substrates of the chaperonin GroEL

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490900658

10.1080/10409230490900658

21 January 2018

Identifiers

DOI

1 reference

release_fkgjjrptyrhdndvo2w77hskkfi

12 August 2017

Fatcat ID

1 reference

Fatcat

https://api.fatcat.wiki/v0/release/fkgjjrptyrhdndvo2w77hskkfi

mapped directly with Wikidata item

24 November 2022

based on heuristic

1 reference