Site-directed mutations within the core “α-crystallin” domain of the small heat-shock protein, human αB-crystallin, decrease molecular chaperone functions-Reference-Cited by-同舟云学术

Site-directed mutations within the core “α-crystallin” domain of the small heat-shock protein, human αB-crystallin, decrease molecular chaperone functions

Published:1999-06 Issue:2 Volume:289 Page:397-411
ISSN:0022-2836
Container-title:Journal of Molecular Biology
language:en
Short-container-title:Journal of Molecular Biology

Author:

Muchowski Paul J,Wu Gabrielle J.S,Liang Jack J.N,Adman Elinor T,Clark John I

Publisher

Elsevier BV

Subject

Molecular Biology,Structural Biology

Reference52 articles.

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3. X-PLOR, A System for Crystallography and NMR;Brunger,1992

4. Identification by 1H NMR spectroscopy of flexible C-terminal extensions in bovine lens alpha-crystallin;Carver;FEBS Letters,1992

5. 1H NMR spectroscopy reveals that mouse Hsp25 has a flexible C-terminal extension of 18 amino acids;Carver;FEBS Letters,1995

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