Molecular chaperones in cellular protein folding
- 1 September 1994
- Vol. 16 (9) , 689-692
- https://doi.org/10.1002/bies.950160916
Abstract
The discovery of “molecular chaperones” has dramatically changed our concept of cellular protein folding. Rather than folding spontaneously, most newly synthesized polypeptide chains seem to acquire their native conformation in a reaction mediated by these versatile helper proteins. Understanding the structure and function of molecular chaperones is likely to yield useful applications for medicine and biotechnology in the future.Keywords
This publication has 45 references indexed in Scilit:
- Calnexin: a membrane-bound chaperone of the endoplasmic reticulumTrends in Biochemical Sciences, 1994
- Identification of six Tcp-1-related genes encoding divergent subunits of the TCP-1-containing chaperoninCurrent Biology, 1994
- ATP induces large quaternary rearrangements in a cage-like chaperonin structureCurrent Biology, 1993
- TCP1 complex is a molecular chaperone in tubulin biogenesisNature, 1992
- Chaperonin-mediated protein folding at the surface of groEL through a 'molten globule'-like intermediateNature, 1991
- 70K heat shock related proteins stimulate protein translocation into microsomesNature, 1988
- Speculations on the functions of the major heat shock and glucose-regulated proteinsCell, 1986
- Purification and properties of groE, a host protein involved in bacteriophage assemblyJournal of Molecular Biology, 1979
- Isolation and characterization of the host protein groE involved in bacteriophage lambda assemblyJournal of Molecular Biology, 1979
- Host participation in bacteriophage lambda head assemblyJournal of Molecular Biology, 1973