Crystal structure of a small heat-shock protein (Q27765131)

Europe PubMed Central

PubMed publication ID

9707123

https://www.ebi.ac.uk/europepmc/webservices/rest/search?resulttype=core&format=json&query=SRC%3AMED%20AND%20EXT_ID%3A9707123

5 January 2025

R. Kim

series ordinal

2

1 reference

Europe PubMed Central

PubMed publication ID

9707123

https://www.ebi.ac.uk/europepmc/webservices/rest/search?resulttype=core&format=json&query=SRC%3AMED%20AND%20EXT_ID%3A9707123

5 January 2025

S. H. Kim

series ordinal

3

1 reference

Europe PubMed Central

PubMed publication ID

9707123

https://www.ebi.ac.uk/europepmc/webservices/rest/search?resulttype=core&format=json&query=SRC%3AMED%20AND%20EXT_ID%3A9707123

http://www.nature.com/articles/29106.pdf

5 January 2025

publication date

6 August 1998

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language of work or name

English

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work available at URL

1 reference

https://api.crossref.org/works/10.1038/29106

http://www.nature.com/articles/29106

5 January 2025

1 reference

https://api.crossref.org/works/10.1038/29106

5 January 2025

0 references

394

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issue

6693

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page(s)

595-9

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cites work

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Alpha A-crystallin confers cellular thermoresistance

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Alpha-crystallin can function as a molecular chaperone

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

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Mycobacterium tuberculosis 16-kDa antigen (Hsp16.3) functions as an oligomeric structure in vitro to suppress thermal aggregation

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Protein folding: junior chaperones

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

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

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Purification, Crystallization, and Preliminary X-Ray Crystallographic Data Analysis of Small Heat Shock Protein Homolog fromMethanococcus jannaschii,a Hyperthermophile

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Two rice (Oryza sativa) full-length cDNA clones encoding low-molecular-weight heat-shock proteins

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Small heat shock protein of Methanococcus jannaschii , a hyperthermophile

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The crystal structure of the bacterial chaperonin GroEL at 2.8 A

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The expanding small heat-shock protein family, and structure predictions of the conserved "alpha-crystallin domain".

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Expression of a gene encoding a 16.9-kDa heat-shock protein, Oshsp16.9, in Escherichia coli enhances thermotolerance

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Effects of site-directed mutations on the chaperone-like activity of alphaB-crystallin

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Comparison of the homologous carboxy-terminal domain and tail of alpha-crystallin and small heat shock protein

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Unique structural features of a novel class of small heat shock proteins

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Improvement of macromolecular electron-density maps by the simultaneous application of real and reciprocal space constraints

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Improved methods for building protein models in electron density maps and the location of errors in these models

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The crystal structure of the GroES co-chaperonin at 2.8 Å resolution

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Structure-Function Studies on Small Heat Shock Protein Oligomeric Assembly and Interaction with Unfolded Polypeptides

21 January 2018

1 reference