Dynamic Complexes in the Chaperonin-Mediated Protein Folding Cycle-Reference-Cited by-同舟云学术

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Dynamic Complexes in the Chaperonin-Mediated Protein Folding Cycle

Published:2016-12-08 Issue: Volume:3 Page:
ISSN:2296-889X
Container-title:Frontiers in Molecular Biosciences
language:
Short-container-title:Front. Mol. Biosci.

Author:

Weiss Celeste,Jebara Fady,Nisemblat Shahar,Azem Abdussalam

Funder

Israel Science Foundation

United States - Israel Binational Science Foundation

Publisher

Frontiers Media SA

Subject

Biochemistry, Genetics and Molecular Biology (miscellaneous),Molecular Biology,Biochemistry

Reference95 articles.

1. Effect of divalent cations on the molecular structure of the GroEL oligomer;Azem;Biochemistry,1994a

2. The protein-folding activity of chaperonins correlates with the symmetric GroEL14(GroES7)2 heterooligomer;Azem;Proc. Natl. Acad. Sci. U.S.A.,1995

3. Characterization of a functional GroEL14(GroES7)2 chaperonin hetero-oligomer;Azem;Science,1994b

4. Crystal structure of wild-type chaperonin GroEL;Bartolucci;J. Mol. Biol.,2005

5. Catalysis, commitment and encapsulation during GroE-mediated folding;Beissinger;J. Mol. Biol.,1999

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