Article
The physical association of multiple molecular chaperone proteins with mutant p53 is altered by geldanamycin, an hsp90-binding agent.
Molecular and cellular biology - 1 Mar 1998
Whitesell L, Sutphin P D, Pulcini E J, Martinez J D, Cook P H
Abstract excerpt
Wild-type p53 is a short-lived protein which turns over very rapidly via selective proteolysis in the ubiquitin-proteasome pathway. Most p53 mutations, however, encode for protein products which display markedly increased intracellular levels and are associated with positive tumor-promoting activ...
Topics
- Animals
- Benzoquinones
- Carrier Proteins
- Cell Line
- Peptidyl-Prolyl Isomerase F
- Cyclophilins
- Enzyme Inhibitors
- HSP70 Heat-Shock Proteins
- HSP90 Heat-Shock Proteins
- Humans
- Intramolecular Oxidoreductases
- Lactams, Macrocyclic
- Mice
- Molecular Chaperones
- Mutation