The folding of most newly synthesized proteins in the cell requires the interaction of a variety of protein cofactors known as molecular chaperones. These molecules recognize and bind to nascent polypeptide chains and partially folded intermediates of proteins, preventing their aggregation and misfolding.
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Oct 1, 2004 · Successive action of DnaK, DnaJ and GroEL along the pathway of chaperone-mediated protein folding. Nature 356, 683–689 (1992). This early paper ...
Fig. 1. ... Fig. 1.General outline of chaperone-mediated protein folding in a cell. U represents nascent polypeptide or newly synthesized protein. Chaperones ...
... chaperone-mediated protein folding. Nature 356: 683–689 [PubMed] [Google Scholar]; Leroux MR, Fandrich M, Klunker D, Siegers K, Lupas AN, Brown JR, Schiebel ...
GO:0061077. chaperone-mediated protein folding. 1,078.01, 100.00 ; GO:0003755. peptidyl-prolyl cis-trans isomerase activity. 186.01, 14.05 ; GO:0044183. protein ...
Dec 8, 2022 · News and Events · All News · Search News · Bardwell and Frydman on visualization of chaperone-mediated protein folding.
chaperone-mediated protein folding · The process of inhibiting aggregation and assisting in the covalent and noncovalent assembly of single chain polypeptides or ...
Mechanisms and Pathways of Chaperone-mediated Protein Folding ... This extract was created in the absence of an abstract. Excerpt. The folding of newly ...
Chaperone-Mediated Protein Folding. Anthony L. Fink. Anthony L. Fink. Department of Chemistry and Biochemistry, The University of California, Santa Cruz ...