Protein folding in the cell: molecular chaperones pave the way
- 15 November 1993
- Vol. 1 (3) , 161-164
- https://doi.org/10.1016/0969-2126(93)90017-b
Abstract
No abstract availableKeywords
This publication has 13 references indexed in Scilit:
- Affinity panning of a library of peptides displayed on bacteriophages reveals the binding specificity of BiPCell, 1993
- Control of folding and membrane translocation by binding of the chaperone DnaJ to nascent polypeptides.Proceedings of the National Academy of Sciences, 1993
- MOLECULAR CHAPERONE FUNCTIONS OF HEAT-SHOCK PROTEINSAnnual Review of Biochemistry, 1993
- Successive action of DnaK, DnaJ and GroEL along the pathway of chaperone-mediated protein foldingNature, 1992
- Different conformations for the same polypeptide bound to chaperones DnaK and GroELNature, 1992
- Peptide-binding specificity of the molecular chaperone BiPNature, 1991
- Chaperonin-mediated protein folding at the surface of groEL through a 'molten globule'-like intermediateNature, 1991
- Interaction of Hsp 70 with Newly Synthesized Proteins: Implications for Protein Folding and AssemblyScience, 1990
- Reconstitution of active dimeric ribulose bisphosphate carboxylase from an unfolded state depends on two chaperonin proteins and Mg-ATPNature, 1989
- Principles that Govern the Folding of Protein ChainsScience, 1973