(Q51580906)

English

A dual role for the N-terminal region of Mycobacterium tuberculosis Hsp16.3 in self-oligomerization and binding denaturing substrate proteins.

scientific article published on 15 November 2004

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scholarly article

1 reference

Europe PubMed Central

PubMed publication ID

7 April 2018

http://europepmc.org/abstract/MED/15545279

A dual role for the N-terminal region of Mycobacterium tuberculosis Hsp16.3 in self-oligomerization and binding denaturing substrate proteins. (English)

1 reference

Europe PubMed Central

PubMed publication ID

7 April 2018

http://europepmc.org/abstract/MED/15545279

Mycobacterium tuberculosis

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author name string

Xinmiao Fu

1

1 reference

Europe PubMed Central

PubMed publication ID

7 April 2018

http://europepmc.org/abstract/MED/15545279

Hui Zhang

2

1 reference

Europe PubMed Central

PubMed publication ID

7 April 2018

http://europepmc.org/abstract/MED/15545279

Xuefeng Zhang

3

1 reference

Europe PubMed Central

PubMed publication ID

7 April 2018

http://europepmc.org/abstract/MED/15545279

Yang Cao

4

1 reference

Europe PubMed Central

PubMed publication ID

7 April 2018

http://europepmc.org/abstract/MED/15545279

Wangwang Jiao

5

1 reference

Europe PubMed Central

PubMed publication ID

7 April 2018

http://europepmc.org/abstract/MED/15545279

Chong Liu

6

1 reference

Europe PubMed Central

PubMed publication ID

7 April 2018

http://europepmc.org/abstract/MED/15545279

Yang Song

7

1 reference

Europe PubMed Central

PubMed publication ID

7 April 2018

http://europepmc.org/abstract/MED/15545279

Abuduaini Abulimiti

8

1 reference

Europe PubMed Central

PubMed publication ID

7 April 2018

http://europepmc.org/abstract/MED/15545279

Zengyi Chang

9

1 reference

Europe PubMed Central

PubMed publication ID

7 April 2018

http://europepmc.org/abstract/MED/15545279

language of work or name

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publication date

15 November 2004

1 reference

Europe PubMed Central

PubMed publication ID

7 April 2018

http://europepmc.org/abstract/MED/15545279

Journal of Biological Chemistry

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Europe PubMed Central

PubMed publication ID

7 April 2018

http://europepmc.org/abstract/MED/15545279

280

1 reference

Europe PubMed Central

PubMed publication ID

7 April 2018

http://europepmc.org/abstract/MED/15545279

8

1 reference

Europe PubMed Central

PubMed publication ID

7 April 2018

http://europepmc.org/abstract/MED/15545279

6337-6348

1 reference

Europe PubMed Central

PubMed publication ID

7 April 2018

http://europepmc.org/abstract/MED/15545279

Alpha-crystallin can function as a molecular chaperone

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M406319200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M406319200

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.M406319200

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.M406319200

21 January 2018

Subunit exchange of alphaA-crystallin

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M406319200

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.M406319200

21 January 2018

Crystal structure and assembly of a eukaryotic small heat shock protein

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M406319200

21 January 2018

Small heat shock protein Hsp16.3 modulates its chaperone activity by adjusting the rate of oligomeric dissociation.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M406319200

21 January 2018

Temperature-dependent subunit exchange and chaperone-like activities of Hsp16.3, a small heat shock protein from Mycobacterium tuberculosis.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M406319200

21 January 2018

Phylogeny of the alpha-crystallin-related heat-shock proteins

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M406319200

21 January 2018

Crystal structure of a small heat-shock protein

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M406319200

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.M406319200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M406319200

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.M406319200

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.M406319200

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.M406319200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M406319200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M406319200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M406319200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M406319200

21 January 2018

Disulfide bonds convert small heat shock protein Hsp16.3 from a chaperone to a non-chaperone: implications for the evolution of cysteine in molecular chaperones.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M406319200

21 January 2018

A simple method for displaying the hydropathic character of a protein

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M406319200

21 January 2018

Blue native electrophoresis for isolation of membrane protein complexes in enzymatically active form

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M406319200

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.M406319200

21 January 2018

Identification of 1,1'-bi(4-anilino)naphthalene-5,5'-disulfonic acid binding sequences in alpha-crystallin

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M406319200

21 January 2018

Analysis of molecular masses and oligomeric states of protein complexes by blue native electrophoresis and isolation of membrane protein complexes by two-dimensional native electrophoresis

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M406319200

21 January 2018

Mutations and modifications support a 'pitted-flexiball' model for alpha-crystallin

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M406319200

21 January 2018

On the mechanism of chaperone activity of the small heat-shock protein of Methanococcus jannaschii

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M406319200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M406319200

21 January 2018

Hsp26: a temperature-regulated chaperone

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M406319200

21 January 2018

The small heat-shock protein, alphaB-crystallin, has a variable quaternary structure

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M406319200

21 January 2018

Crystal structure of riboflavin synthase

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M406319200

21 January 2018

[28] Purification and characterization of small heat shock proteins

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M406319200

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.M406319200

21 January 2018

Identifiers

10.1074/JBC.M406319200

1 reference

Europe PubMed Central

PubMed publication ID

7 April 2018

http://europepmc.org/abstract/MED/15545279

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

7 April 2018

http://europepmc.org/abstract/MED/15545279

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