Role of the heat-shock response in the life and death of proteins. (Q47824004)

5 February 2018

review article

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title

Role of the heat-shock response in the life and death of proteins. (English)

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5 February 2018

author name string

Mathew A

series ordinal

1

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5 February 2018

Morimoto RI

series ordinal

2

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5 February 2018

language of work or name

English

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publication date

1 June 1998

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5 February 2018

Annals of the New York Academy of Sciences

published in

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5 February 2018

volume

851

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5 February 2018

page(s)

99-111

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5 February 2018

Proteasome inhibition leads to a heat-shock response, induction of endoplasmic reticulum chaperones, and thermotolerance

cites work

1 reference

https://api.crossref.org/works/10.1111%2FJ.1749-6632.1998.TB08982.X

Proteasome inhibitors cause induction of heat shock proteins and trehalose, which together confer thermotolerance in Saccharomyces cerevisiae

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FJ.1749-6632.1998.TB08982.X

Evidence that a rapidly turning over protein, normally degraded by proteasomes, regulates hsp72 gene transcription in HepG2 cells

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FJ.1749-6632.1998.TB08982.X

Roles of molecular chaperones in protein degradation

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FJ.1749-6632.1998.TB08982.X

Protein folding in the cell

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FJ.1749-6632.1998.TB08982.X

Chaperone functions of the heat shock proteins associated with steroid receptors

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FJ.1749-6632.1998.TB08982.X

The heat shock protein 83 (Hsp83) is required for Raf-mediated signalling in Drosophila

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FJ.1749-6632.1998.TB08982.X

Eukaryotic homologues of Escherichia coli dnaJ: a diverse protein family that functions with hsp70 stress proteins

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FJ.1749-6632.1998.TB08982.X

Hip, a novel cochaperone involved in the eukaryotic Hsc70/Hsp40 reaction cycle

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FJ.1749-6632.1998.TB08982.X

BAG-1 modulates the chaperone activity of Hsp70/Hsc70.

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FJ.1749-6632.1998.TB08982.X

Polypeptide chain binding proteins: catalysts of protein folding and related processes in cells

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FJ.1749-6632.1998.TB08982.X

Assisting spontaneity: the role of Hsp90 and small Hsps as molecular chaperones

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FJ.1749-6632.1998.TB08982.X

Molecular chaperones in cellular protein folding

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FJ.1749-6632.1998.TB08982.X

The E. coli dnaK gene product, the hsp70 homolog, can reactivate heat-inactivated RNA polymerase in an ATP hydrolysis-dependent manner

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FJ.1749-6632.1998.TB08982.X

The ubiquitin-proteasome proteolytic pathway

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FJ.1749-6632.1998.TB08982.X

Functions of the proteasome in antigen presentation

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FJ.1749-6632.1998.TB08982.X

Proteasomes: destruction as a programme

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FJ.1749-6632.1998.TB08982.X

Ubiquitin, proteasomes, and the regulation of intracellular protein degradation

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FJ.1749-6632.1998.TB08982.X

Ornithine decarboxylase is degraded by the 26S proteasome without ubiquitination

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FJ.1749-6632.1998.TB08982.X

Proteasome-dependent endoplasmic reticulum-associated protein degradation: an unconventional route to a familiar fate

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FJ.1749-6632.1998.TB08982.X

Ubiquitination of a yeast plasma membrane receptor signals its ligand-stimulated endocytosis

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FJ.1749-6632.1998.TB08982.X

Heterologous transmembrane and cytoplasmic domains direct functional chimeric influenza virus hemagglutinins into the endocytic pathway

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FJ.1749-6632.1998.TB08982.X

Resistance to cadmium mediated by ubiquitin-dependent proteolysis.

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FJ.1749-6632.1998.TB08982.X

Role of a ubiquitin-conjugating enzyme in degradation of S- and M-phase cyclins

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FJ.1749-6632.1998.TB08982.X

Involvement of the molecular chaperone Ydj1 in the ubiquitin-dependent degradation of short-lived and abnormal proteins in Saccharomyces cerevisiae

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FJ.1749-6632.1998.TB08982.X

Pharmacologic shifting of a balance between protein refolding and degradation mediated by Hsp90

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FJ.1749-6632.1998.TB08982.X

Herbimycin A induces the 20 S proteasome- and ubiquitin-dependent degradation of receptor tyrosine kinases

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FJ.1749-6632.1998.TB08982.X

Degradation of CFTR by the ubiquitin-proteasome pathway

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FJ.1749-6632.1998.TB08982.X

The molecular chaperone Ydj1 is required for the p34CDC28-dependent phosphorylation of the cyclin Cln3 that signals its degradation

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FJ.1749-6632.1998.TB08982.X

Mitochondrial molecular chaperones: their role in protein translocation

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FJ.1749-6632.1998.TB08982.X

A population of rat liver lysosomes responsible for the selective uptake and degradation of cytosolic proteins

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FJ.1749-6632.1998.TB08982.X

Activation of heat shock transcription factor 3 by c-Myb in the absence of cellular stress

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FJ.1749-6632.1998.TB08982.X

Disruption of the HSF3 gene results in the severe reduction of heat shock gene expression and loss of thermotolerance.

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FJ.1749-6632.1998.TB08982.X

The ubiquitin-proteasome pathway is required for processing the NF-kappa B1 precursor protein and the activation of NF-kappa B

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FJ.1749-6632.1998.TB08982.X

Inhibitors of the proteasome block the degradation of most cell proteins and the generation of peptides presented on MHC class I molecules

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FJ.1749-6632.1998.TB08982.X

Thermolability of ubiquitin-activating enzyme from the mammalian cell cycle mutant ts85

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FJ.1749-6632.1998.TB08982.X

Expression of heat shock factor 2 in mouse testis: potential role as a regulator of heat-shock protein gene expression during spermatogenesis.

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FJ.1749-6632.1998.TB08982.X

A novel rat homolog of the Saccharomyces cerevisiae ubiquitin-conjugating enzymes UBC4 and UBC5 with distinct biochemical features is induced during spermatogenesis

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FJ.1749-6632.1998.TB08982.X

UbiA, the major polyubiquitin locus in Caenorhabditis elegans, has unusual structural features and is constitutively expressed

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FJ.1749-6632.1998.TB08982.X

Editing of ubiquitin conjugates by an isopeptidase in the 26S proteasome

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FJ.1749-6632.1998.TB08982.X

10.1111/J.1749-6632.1998.TB08982.X

21 January 2018

Identifiers

DOI

1 reference

5 February 2018

PubMed ID

9668611

1 reference

5 February 2018