N-terminal control of small heat shock protein oligomerization: changes in aggregate size and chaperone-like function-Reference-Cited by-同舟云学术

N-terminal control of small heat shock protein oligomerization: changes in aggregate size and chaperone-like function

Published:2005-05 Issue:2 Volume:1748 Page:146-156
ISSN:1570-9639
Container-title:Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics
language:en
Short-container-title:Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics

Author:

Eifert Cheryl,Burgio Michael R.,Bennett Pauline M.,Salerno John C.,Koretz Jane F.

Publisher

Elsevier BV

Subject

Molecular Biology,Biochemistry,Biophysics,Analytical Chemistry

Reference47 articles.

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3. 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;Basha;J. Biol. Chem.,2004

4. Reinduced expression of developmental proteins (nestin, small heat shock protein) in and around cerebral arteriovenous malformations;Ha;Clin. Neuropathol.,2003

5. Regulation of Hsp27 oligomerization, chaperone function, and protective activity against oxidative stress/tumor necrosis factor alpha by phosphorylation;Rogalla;J. Biol. Chem.,1999

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