Details
| Original language | English |
|---|---|
| Pages (from-to) | 1299-1323 |
| Number of pages | 25 |
| Journal | Natural Product Reports |
| Volume | 30 |
| Issue number | 10 |
| Publication status | Published - Oct 2013 |
Abstract
Covering: 2005 to 2013 In this review recent progress in the development of heat shock proteins (Hsp90) in oncogenesis is illuminated. Particular emphasis is put on inhibitors such as geldanamycin and analogues that serve as a natural product show case. Hsp90 has emerged as an important target in cancer therapy and/or against pathogenic cells which elicit abnormal Hsp patterns. Competition for ATP by geldanamycin and related compounds abrogate the chaperone function of Hsp90. In this context, this account pursues three topics in detail: a) Hsp90 and its biochemistry, b) Hsp90 and its role in oncogenesis and c) strategies to create compound libraries of structurally complex inhibitors like geldanamycin on which SAR studies and the development of drugs that are currently in different stages of clinical testing rely.
ASJC Scopus subject areas
- Biochemistry, Genetics and Molecular Biology(all)
- Biochemistry
- Pharmacology, Toxicology and Pharmaceutics(all)
- Drug Discovery
- Chemistry(all)
- Organic Chemistry
Sustainable Development Goals
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In: Natural Product Reports, Vol. 30, No. 10, 10.2013, p. 1299-1323.
Research output: Contribution to journal › Review article › Research › peer review
}
TY - JOUR
T1 - Targeting heat-shock-protein 90 (Hsp90) by natural products
T2 - Geldanamycin, a show case in cancer therapy
AU - Franke, Jana
AU - Eichner, Simone
AU - Zeilinger, Carsten
AU - Kirschning, Andreas
PY - 2013/10
Y1 - 2013/10
N2 - Covering: 2005 to 2013 In this review recent progress in the development of heat shock proteins (Hsp90) in oncogenesis is illuminated. Particular emphasis is put on inhibitors such as geldanamycin and analogues that serve as a natural product show case. Hsp90 has emerged as an important target in cancer therapy and/or against pathogenic cells which elicit abnormal Hsp patterns. Competition for ATP by geldanamycin and related compounds abrogate the chaperone function of Hsp90. In this context, this account pursues three topics in detail: a) Hsp90 and its biochemistry, b) Hsp90 and its role in oncogenesis and c) strategies to create compound libraries of structurally complex inhibitors like geldanamycin on which SAR studies and the development of drugs that are currently in different stages of clinical testing rely.
AB - Covering: 2005 to 2013 In this review recent progress in the development of heat shock proteins (Hsp90) in oncogenesis is illuminated. Particular emphasis is put on inhibitors such as geldanamycin and analogues that serve as a natural product show case. Hsp90 has emerged as an important target in cancer therapy and/or against pathogenic cells which elicit abnormal Hsp patterns. Competition for ATP by geldanamycin and related compounds abrogate the chaperone function of Hsp90. In this context, this account pursues three topics in detail: a) Hsp90 and its biochemistry, b) Hsp90 and its role in oncogenesis and c) strategies to create compound libraries of structurally complex inhibitors like geldanamycin on which SAR studies and the development of drugs that are currently in different stages of clinical testing rely.
UR - http://www.scopus.com/inward/record.url?scp=84883855117&partnerID=8YFLogxK
U2 - 10.1039/c3np70012g
DO - 10.1039/c3np70012g
M3 - Review article
C2 - 23934201
AN - SCOPUS:84883855117
VL - 30
SP - 1299
EP - 1323
JO - Natural Product Reports
JF - Natural Product Reports
SN - 0265-0568
IS - 10
ER -