(Q38346011)

English

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

scientific article published on 13 January 2004

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scholarly article

1 reference

Europe PubMed Central

2 September 2017

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 (English)

1 reference

Europe PubMed Central

2 September 2017

molecular chaperones

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object named as

Klaus Richter

3

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author name string

Thusnelda Stromer

1

1 reference

Europe PubMed Central

2 September 2017

Elke Fischer

2

1 reference

Europe PubMed Central

2 September 2017

Martin Haslbeck

4

1 reference

Europe PubMed Central

2 September 2017

Johannes Buchner

5

1 reference

Europe PubMed Central

2 September 2017

language of work or name

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publication date

13 January 2004

1 reference

Europe PubMed Central

2 September 2017

Journal of Biological Chemistry

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Europe PubMed Central

2 September 2017

279

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Europe PubMed Central

2 September 2017

12

1 reference

Europe PubMed Central

2 September 2017

11222-11228

1 reference

Europe PubMed Central

2 September 2017

Molecular chaperones--cellular machines for protein folding

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M310149200

21 January 2018

sHsps and their role in the chaperone network

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M310149200

21 January 2018

Alpha-crystallin

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M310149200

21 January 2018

Structure and function of the small heat shock protein/alpha-crystallin family of molecular chaperones

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M310149200

21 January 2018

Chloroplast small heat shock proteins: evidence for atypical evolution of an organelle-localized protein

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M310149200

21 January 2018

Protein folding: junior chaperones.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M310149200

21 January 2018

Alpha-crystallin-type heat shock proteins: socializing minichaperones in the context of a multichaperone network.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M310149200

21 January 2018

The major low-molecular-weight heat shock protein in chloroplasts shows antigenic conservation among diverse higher plant species

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M310149200

21 January 2018

Crystal structure of a small heat-shock protein

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M310149200

21 January 2018

Hsp26: a temperature-regulated chaperone

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M310149200

21 January 2018

Crystal structure and assembly of a eukaryotic small heat shock protein

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M310149200

21 January 2018

Caenorhabditis elegans small heat-shock proteins Hsp12.2 and Hsp12.3 form tetramers and have no chaperone-like activity

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M310149200

21 January 2018

The mammalian small heat-shock protein Hsp20 forms dimers and is a poor chaperone.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M310149200

21 January 2018

Small heat-shock protein structures reveal a continuum from symmetric to variable assemblies

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M310149200

21 January 2018

Subunit exchange, conformational stability, and chaperone-like function of the small heat shock protein 16.5 from Methanococcus jannaschii

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M310149200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M310149200

21 January 2018

GroE-dependent expression and purification of pig heart mitochondrial citrate synthase in Escherichia coli

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M310149200

21 January 2018

Expression and aggregation of recombinant alpha A-crystallin and its two domains

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M310149200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M310149200

21 January 2018

The dynamics of Hsp25 quaternary structure. Structure and function of different oligomeric species

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M310149200

21 January 2018

A novel quaternary structure of the dimeric alpha-crystallin domain with chaperone-like activity

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M310149200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M310149200

21 January 2018

Dimer structure as a minimum cooperative subunit of small heat-shock proteins

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M310149200

21 January 2018

Structure-function studies on small heat shock protein oligomeric assembly and interaction with unfolded polypeptides

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M310149200

21 January 2018

Biochemical methods for analysis of histone deacetylases

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M310149200

21 January 2018

Chaperone activity and homo- and hetero-oligomer formation of bacterial small heat shock proteins

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M310149200

21 January 2018

Identifiers

10.1074/JBC.M310149200

1 reference

Europe PubMed Central

2 September 2017

1 reference

Europe PubMed Central

2 September 2017

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