Protein folding (TriC-mediated)

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Functional Subunits of Eukaryotic Chaperonin CCT/TRiC in Protein Folding

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Protein folding: Versatility of the cytosolic chaperonin TRiC/CCT

Efficient de novo folding of actins and tubulins requires two molecular chaperones, the chaperonin TRiC (or CCT) and its novel cofactor GimC (or prefoldin). Recent studies indicate that TRiC is exquisitely adapted for this task, yet has the ability to interact with and assist the folding of numerous other cellular proteins.

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Chaperone-mediated protein folding.

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Chaperonin-mediated protein folding.

Molecular chaperones are required to assist folding of a subset of proteins in Escherichia coli. We describe a conceptual framework for understanding how the GroEL-GroES system assists misfolded proteins to reach their native states. The architecture of GroEL consists of double toroids stacked back-to-back. However, most of the fundamentals of the GroEL action can be described in terms of the s...

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Chaperonin-mediated protein folding.

We have been studying chaperonins these past twenty years through an initial discovery of an action in protein folding, analysis of structure, and elucidation of mechanism. Some of the highlights of these studies were presented recently upon sharing the honor of the 2013 Herbert Tabor Award with my early collaborator, Ulrich Hartl, at the annual meeting of the American Society for Biochemistry ...

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ژورنال

عنوان ژورنال: Reactome - a curated knowledgebase of biological pathways

سال: 2009

ISSN: 1934-1792

DOI: 10.3180/react_17004.1