Details
| Original language | English |
|---|---|
| Title of host publication | Heat Shock Protein 90 in Human Diseases and Disorders |
| Editors | Alexzander A. A. Asea, Punit Kaur |
| Pages | 387-410 |
| Edition | 1. |
| ISBN (electronic) | 978-3-030-23158-3 |
| Publication status | Published - 5 Nov 2019 |
Publication series
| Name | Heat Shock Proteins (HESP) |
|---|---|
| Volume | 19 |
| ISSN (Print) | 1877-1246 |
| ISSN (electronic) | 1877-1254 |
Abstract
Cite this
- Standard
- Harvard
- Apa
- Vancouver
- BibTeX
- RIS
Heat Shock Protein 90 in Human Diseases and Disorders. ed. / Alexzander A. A. Asea; Punit Kaur. 1. ed. 2019. p. 387-410 (Heat Shock Proteins (HESP); Vol. 19).
Research output: Chapter in book/report/conference proceeding › Contribution to book/anthology › Research
}
TY - CHAP
T1 - Hsp90
T2 - A target for susceptibilities and substitutions in biotechnological and medicinal application
AU - Warnecke, Athanasia
AU - Kirschning, Andreas
AU - Zeilinger, Carsten
AU - Landsberg, Daniel
PY - 2019/11/5
Y1 - 2019/11/5
N2 - A main influencer of the chaperome is the environmental stress eliciting continuously degraded proteins. To avoid proteotoxic stress, which hinders the protein homeostasis and cell survival, most proteins are accompanied from the early existence on by heat shock proteins (HSP) and sequestrated into different routes of renaturation, de novo folding or denaturation. Therefore, the regulation of Hsp90 presence and activity is relevant for most cells and their function. In this position, Hsp90 can decide the fate between health and disease by selective refolding of denatured proteins and is a player in the evolution. From the last century on, Hsp90 was validated as a target due to its susceptibility for natural products and to make them perfect with the aim to hinder refolding and enhance the proteotoxic stress. In this review, the links between natural producer, chemical synthesis with Hsp90 as a target as well as alternative chaperoning routes by chemical compounds are illuminated.
AB - A main influencer of the chaperome is the environmental stress eliciting continuously degraded proteins. To avoid proteotoxic stress, which hinders the protein homeostasis and cell survival, most proteins are accompanied from the early existence on by heat shock proteins (HSP) and sequestrated into different routes of renaturation, de novo folding or denaturation. Therefore, the regulation of Hsp90 presence and activity is relevant for most cells and their function. In this position, Hsp90 can decide the fate between health and disease by selective refolding of denatured proteins and is a player in the evolution. From the last century on, Hsp90 was validated as a target due to its susceptibility for natural products and to make them perfect with the aim to hinder refolding and enhance the proteotoxic stress. In this review, the links between natural producer, chemical synthesis with Hsp90 as a target as well as alternative chaperoning routes by chemical compounds are illuminated.
U2 - 10.1007/978-3-030-23158-3_18
DO - 10.1007/978-3-030-23158-3_18
M3 - Contribution to book/anthology
SN - 978-3-030-23157-6
SN - 978-3-030-23160-6
T3 - Heat Shock Proteins (HESP)
SP - 387
EP - 410
BT - Heat Shock Protein 90 in Human Diseases and Disorders
A2 - Asea, Alexzander A. A.
A2 - Kaur, Punit
ER -