Title |
Heat-shock protein 90, a chaperone for folding and regulation
|
---|---|
Published in |
Cellular and Molecular Life Sciences, October 2002
|
DOI | 10.1007/pl00012491 |
Pubmed ID | |
Authors |
D. Picard |
Abstract |
Heat-shock protein 90 (Hsp90) is an abundant and highly conserved molecular chaperone that is essential for viability in eukaryotes. Hsp90 fulfills a housekeeping function in contributing to the folding, maintenance of structural integrity and proper regulation of a subset of cytosolic proteins. A remarkable proportion of its substrates are proteins involved in cell cycle control and signal transduction. Hsp90 acts with a cohort of Hsp90 co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function. The large conformational flexibility of Hsp90 and a multitude of dynamic co-chaperone complexes contribute to generating functional diversity, and allow Hsp90 to assist a wide range of substrates. |
Mendeley readers
Geographical breakdown
Country | Count | As % |
---|---|---|
United Kingdom | 4 | 2% |
United States | 3 | 1% |
Australia | 1 | <1% |
Brazil | 1 | <1% |
Canada | 1 | <1% |
Portugal | 1 | <1% |
Belgium | 1 | <1% |
Mexico | 1 | <1% |
Unknown | 243 | 95% |
Demographic breakdown
Readers by professional status | Count | As % |
---|---|---|
Student > Ph. D. Student | 53 | 21% |
Researcher | 37 | 14% |
Student > Master | 34 | 13% |
Student > Bachelor | 31 | 12% |
Student > Doctoral Student | 17 | 7% |
Other | 32 | 13% |
Unknown | 52 | 20% |
Readers by discipline | Count | As % |
---|---|---|
Agricultural and Biological Sciences | 80 | 31% |
Biochemistry, Genetics and Molecular Biology | 63 | 25% |
Medicine and Dentistry | 15 | 6% |
Neuroscience | 12 | 5% |
Chemistry | 10 | 4% |
Other | 22 | 9% |
Unknown | 54 | 21% |