Display Settings:

Format

Send to:

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

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

    Source

    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
    [PubMed - indexed for MEDLINE]

      Supplemental Content

      Icon for Elsevier Science

      Save items

      loading

      Recent activity

      Your browsing activity is empty.

      Activity recording is turned off.

      Turn recording back on

      See more...
      Write to the Help Desk