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The Hsp90 Complex : A Super-Chaperone Machine as a Novel Drug Target

Titelangaben

Scheibel, Thomas ; Buchner, Johannes:
The Hsp90 Complex : A Super-Chaperone Machine as a Novel Drug Target.
In: Biochemical Pharmacology. Bd. 56 (September 1998) Heft 6 . - S. 675-682.
ISSN 0006-2952
DOI: https://doi.org/10.1016/S0006-2952(98)00120-8

Abstract

Cells respond to sudden changes in the environmental temperature with increased synthesis of a distinct number of heat shock proteins (Hsps). Analysis of the function of these proteins in recent years has shown that all the major classes of conserved Hsps are molecular chaperones involved in assisting cellular protein folding and preventing irreversible side-reactions, such as unspecific aggregation. In addition to their function under stress conditions, molecular chaperones also play a critical role under physiological conditions. Hsp90 is one of the most abundant chaperones in the cytosol of eukaryotic cells. It is part of the cell’s powerful network of chaperones to fight the deleterious consequences of protein unfolding caused by nonphysiological conditions. In the absence of stress, however, Hsp90 is an obligate component of fundamental cellular processes such as hormone signaling and cell cycle control. In this context, several key regulatory proteins, such as steroid receptors, cell cycle kinases, and p53, have been identified as substrates of Hsp90. Recently, Hsp90 was shown to be the unique target for geldanamycin, a potent new anti-tumor drug that blocks cell proliferation. Interestingly, under physiological conditions, Hsp90 seems to perform its chaperone function in a complex with a set of partner proteins, suggesting that the Hsp90 complex is a multi-chaperone machine specialized in guiding the maturation of conformationally labile proteins. The regulation of key signaling molecules of the cell by the Hsp90 machinery is a stimulating new concept emerging from these studies, and Hsp90 has become a promising new drug target

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Publikationsform: Artikel in einer Zeitschrift
Begutachteter Beitrag: Ja
Keywords: stress proteins; geldanamycin; src kinases; steroid receptors; cancer; p53
Institutionen der Universität: Fakultäten
Fakultäten > Fakultät für Ingenieurwissenschaften
Fakultäten > Fakultät für Ingenieurwissenschaften > Lehrstuhl Biomaterialien
Fakultäten > Fakultät für Ingenieurwissenschaften > Lehrstuhl Biomaterialien > Lehrstuhl Biomaterialien - Univ.-Prof. Dr. Thomas Scheibel
Profilfelder > Advanced Fields > Neue Materialien
Profilfelder > Advanced Fields > Molekulare Biowissenschaften
Profilfelder > Advanced Fields > Polymer- und Kolloidforschung
Profilfelder > Emerging Fields > Lebensmittel- und Gesundheitswissenschaften
Profilfelder
Profilfelder > Advanced Fields
Profilfelder > Emerging Fields
Titel an der UBT entstanden: Nein
Themengebiete aus DDC: 600 Technik, Medizin, angewandte Wissenschaften
600 Technik, Medizin, angewandte Wissenschaften > 620 Ingenieurwissenschaften
Eingestellt am: 01 Okt 2015 12:01
Letzte Änderung: 26 Nov 2015 10:51
URI: https://eref.uni-bayreuth.de/id/eprint/20054