HSP100 CLP PROTEINS - A COMMON MECHANISM EXPLAINS DIVERSE FUNCTIONS/

Citation
Ec. Schirmer et al., HSP100 CLP PROTEINS - A COMMON MECHANISM EXPLAINS DIVERSE FUNCTIONS/, Trends in biochemical sciences, 21(8), 1996, pp. 289-296
Citations number
50
Categorie Soggetti
Biology
ISSN journal
09680004
Volume
21
Issue
8
Year of publication
1996
Pages
289 - 296
Database
ISI
SICI code
0968-0004(1996)21:8<289:HCP-AC>2.0.ZU;2-0
Abstract
The HSP100/Clp proteins are a newly discovered family with a great div ersity of functions, such as increased tolerance to high temperatures, promotion of proteolysis of specific cellular substrates and regulati on of transcription. HSP100/Clp proteins are also synthesized in a var iety of specific patterns and, in eukaryotes, are localized to differe nt subcellular compartments. Recent data suggest that a common ability to disassemble higher-order protein structures and aggregates unifies the molecular functions of this diverse family.