Protein folding: versatility of the cytosolic chaperonin TRiC/CCT.
- Published Article
- Publication Date
Apr 06, 2000
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.
Report this publication
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
This record was last updated on 07/03/2016 and may not reflect the most current and accurate biomedical/scientific data available from NLM.
The corresponding record at NLM can be accessed at https://www.ncbi.nlm.nih.gov/pubmed/10753735