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Curr Biol. 2000 Apr 6;10(7):R260-4.

Protein folding: versatility of the cytosolic chaperonin TRiC/CCT.

Author information

1
Department of Cellular Biochemistry, Max-Planck-Institut für Biochemie, Martinsried, D-82152, Germany.

Abstract

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.

PMID:
10753735
DOI:
10.1016/s0960-9822(00)00432-2
[Indexed for MEDLINE]
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