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Hsp90 isoforms: functions, expression and clinical importance
Author(s) -
Subbarao Sreedhar Amere,
Kalmár Éva,
Csermely Péter,
Shen Yu-Fei
Publication year - 2004
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(04)00229-7
Subject(s) - hsp90 , gene isoform , heat shock protein , biology , microbiology and biotechnology , chaperone (clinical) , hsp70 , computational biology , identification (biology) , cytoplasm , biochemistry , gene , medicine , pathology , botany
The 90 kDa heat shock protein, Hsp90, is a main functional component of an important cytoplasmic chaperone complex, and it is involved in various cellular processes, such as cell proliferation, differentiation and apoptosis. Identification of Hsp90 as a molecular target of various anticancer drugs highlighted its importance from the clinical point of view. Here we summarize the current knowledge on various Hsp90 isoforms regarding their genomic location, molecular evolution, functional differences, differential induction after various environmental stresses and in pathological conditions as well as the growing importance of discriminating between Hsp90 isoforms in clinical practice.