Evidence for an essential function of the N terminus of a small heat shock protein in vivo, independent of in vitro chaperone activity (Q34244942)

31 July 2017

Evidence for an essential function of the N terminus of a small heat shock protein in vivo, independent of in vitro chaperone activity (English)

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31 July 2017

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Elizabeth Vierling

4

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author name string

Kim C Giese

series ordinal

1

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31 July 2017

Eman Basha

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2

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31 July 2017

Belmund Y Catague

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3

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31 July 2017

language of work or name

English

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publication date

19 December 2005

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Proceedings of the National Academy of Sciences of the United States of America

31 July 2017

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31 July 2017

102

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31 July 2017

52

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31 July 2017

18896-18901

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

31 July 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1323161

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

28 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1323161

Crystal structure and assembly of a eukaryotic small heat shock protein

28 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1323161

Synechocystis HSP17 is an amphitropic protein that stabilizes heat-stressed membranes and binds denatured proteins for subsequent chaperone-mediated refolding

28 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1323161

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

28 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1323161

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

28 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1323161

Mutation R120G in alphaB-crystallin, which is linked to a desmin-related myopathy, results in an irregular structure and defective chaperone-like function

28 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1323161

HSP27 multimerization mediated by phosphorylation-sensitive intermolecular interactions at the amino terminus

28 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1323161

A missense mutation in the alphaB-crystallin chaperone gene causes a desmin-related myopathy

28 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1323161

Crystal structure of a small heat-shock protein

28 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1323161

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

28 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1323161

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

28 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1323161

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

28 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1323161

Small heat shock proteins are molecular chaperones.

28 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1323161

Alpha-crystallin can function as a molecular chaperone

28 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1323161

A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding

28 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1323161

Structure and in vitro molecular chaperone activity of cytosolic small heat shock proteins from pea.

28 July 2018

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.0506169103

Sequential mechanism of solubilization and refolding of stable protein aggregates by a bichaperone network

21 January 2018

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.0506169103

The identity of proteins associated with a small heat shock protein during heat stress in vivo indicates that these chaperones protect a wide range of cellular functions

21 January 2018

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.0506169103

A chaperone pathway in protein disaggregation. Hsp26 alters the nature of protein aggregates to facilitate reactivation by Hsp104.

21 January 2018

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.0506169103

Disassembling protein aggregates in the yeast cytosol. The cooperation of Hsp26 with Ssa1 and Hsp104.

21 January 2018

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.0506169103

A 16.6-kilodalton protein in the Cyanobacterium synechocystis sp. PCC 6803 plays a role in the heat shock response

21 January 2018

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.0506169103

Mutants in a small heat shock protein that affect the oligomeric state. Analysis and allele-specific suppression

21 January 2018

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.0506169103

Generic Assignments, Strain Histories and Properties of Pure Cultures of Cyanobacteria

21 January 2018

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.0506169103

A critical motif for oligomerization and chaperone activity of bacterial alpha-heat shock proteins

21 January 2018

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.0506169103

Structural and Functional Defects Caused by Point Mutations in the α-Crystallin Domain of a Bacterial α-Heat Shock Protein

21 January 2018

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.0506169103

Thermally induced disintegration of the oligomeric structure of alphaB-crystallin mutant F28S is associated with diminished chaperone activity

21 January 2018

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.0506169103

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

21 January 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1323161

Changes in oligomerization are essential for the chaperone activity of a small heat shock protein in vivo and in vitro

28 October 2018

1 reference

12 December 2020

Small heat shock proteins, ClpB and the DnaK system form a functional triade in reversing protein aggregation

1 reference

12 December 2020

Structural and functional consequences of the mutation of a conserved arginine residue in alphaA and alphaB crystallins

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12 December 2020

Genetic analysis reveals domain interactions of Arabidopsis Hsp100/ClpB and cooperation with the small heat shock protein chaperone system

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12 December 2020

Identifiers

DOI

10.1073/PNAS.0506169103

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31 July 2017

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31 July 2017

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