Hochschulschrift
The adaptor protein Sti1/Hop connects the Hsp70 and Hsp90 chaperone cycle
- Location
-
Deutsche Nationalbibliothek Frankfurt am Main
- ISBN
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9783868532913
- Dimensions
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21 cm, 327 gr.
- Extent
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203 S.
- Edition
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1. Aufl.
- Language
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Deutsch
- Notes
-
graph. Darst.
Zugl.: München, Techn. Univ., Diss., 2009
- Classification
-
Biowissenschaften, Biologie
- Table of contents
- Rights
-
Bei diesem Objekt liegt nur das Inhaltsverzeichnis digital vor. Der Zugriff darauf ist unbeschränkt möglich.
- Last update
-
11.06.2025, 2:11 PM CEST
Data provider
This object is provided by:
Deutsche Nationalbibliothek. If you have any questions about the object, please contact the data provider.
Deutsche Nationalbibliothek. If you have any questions about the object, please contact the data provider.
Object type
- Hochschulschrift
Associated
- Schmid, Andreas B.
- Verl. Dr. Hut
Time of origin
- 2009
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The Hsp70-Hsp90 co-chaperone Hop/Stip1 shifts the proteostatic balance from folding towards degradation
Mechanistic Analysis of the Hsp70/ Hsp90 Co-chaperone Sti1
Exploring the human Hsp70-Hop-Hsp90 system for Tau recognition
Proteininteraktionsdomänen in Hsp70-Hsp90-Multichaperonkomplexen
Proteininteraktionsdomänen in Hsp70-Hsp90-Multichaperonkomplexen
Co-chaperone interactions in the Hsp90 chaperone cycle
Investigation of the interaction of the Hsp70 and Hsp90 chaperone machine with co-chaperones and substrates
Mechanism of the molecular chaperone Hsp90
Conformational dynamics of the Hsp70 chaperone
The chaperone system in cancer therapies: Hsp90
Phospho-regulation of the Hsp90 chaperone machinery
Targeting the Hsp90-Cdc37-client protein interaction to disrupt Hsp90 chaperone machinery
The Hsp70-Hsp90 co-chaperone Hop/Stip1 shifts the proteostatic balance from folding towards degradation
Mechanistic Analysis of the Hsp70/ Hsp90 Co-chaperone Sti1
Exploring the human Hsp70-Hop-Hsp90 system for Tau recognition
Proteininteraktionsdomänen in Hsp70-Hsp90-Multichaperonkomplexen
Proteininteraktionsdomänen in Hsp70-Hsp90-Multichaperonkomplexen
Co-chaperone interactions in the Hsp90 chaperone cycle
Investigation of the interaction of the Hsp70 and Hsp90 chaperone machine with co-chaperones and substrates
Mechanism of the molecular chaperone Hsp90
Conformational dynamics of the Hsp70 chaperone
The chaperone system in cancer therapies: Hsp90
Phospho-regulation of the Hsp90 chaperone machinery