The emergence of the chaperone machines
- 31 August 1992
- journal article
- review article
- Published by Elsevier BV in Trends in Biochemical Sciences
- Vol. 17 (8), 295-299
- https://doi.org/10.1016/0968-0004(92)90439-g
Abstract
No abstract availableKeywords
This publication has 18 references indexed in Scilit:
- Heat shock in Escherichia coli alters the protein-binding properties of the chaperonin groEL by inducing its phosphorylationNature, 1992
- Successive action of DnaK, DnaJ and GroEL along the pathway of chaperone-mediated protein foldingNature, 1992
- Sec61p and BiP directly facilitate polypeptide translocation into the ERCell, 1992
- Yeast Sec proteins interact with polypeptides traversing the endoplasmic reticulum membraneCell, 1992
- Different conformations for the same polypeptide bound to chaperones DnaK and GroELNature, 1992
- Recognition of nascent polypeptides for targeting and foldingTrends in Biochemical Sciences, 1991
- Cooperativity in ATP hydrolysis by GroEL is increased by GroESFEBS Letters, 1991
- Peptide-binding specificity of the molecular chaperone BiPNature, 1991
- Protein folding: local structures, domains, subunits, and assembliesBiochemistry, 1991
- Is hsp70 the cellular thermometer?Trends in Biochemical Sciences, 1991