- Weitere Titel
-
Mechanistische Analyse des Hsp70 / Hsp90 Co-Chaperons Sti1
- Standort
-
Deutsche Nationalbibliothek Frankfurt am Main
- Umfang
-
Online-Ressource
- Sprache
-
Englisch
- Anmerkungen
-
München, Technische Universität München, Dissertation, 2020
- Ereignis
-
Veröffentlichung
- (wo)
-
München
- (wer)
-
Universitätsbibliothek der TU München
- (wann)
-
2020
- Urheber
-
Hack, Gordon
- Beteiligte Personen und Organisationen
- URN
-
urn:nbn:de:bvb:91-diss-20200221-1507618-1-7
- Rechteinformation
-
Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Letzte Aktualisierung
-
15.08.2025, 07:34 MESZ
Datenpartner
Dieses Objekt wird bereitgestellt von:
Deutsche Nationalbibliothek. Bei Fragen zum Objekt wenden Sie sich bitte an den Datenpartner.
Deutsche Nationalbibliothek. Bei Fragen zum Objekt wenden Sie sich bitte an den Datenpartner.
Beteiligte
- Hack, Gordon
- Buchner, Johannes
- Rief, Matthias
- Universitätsbibliothek der TU München
Entstanden
- 2020
Ähnliche Objekte (12)
Co-chaperone interactions in the Hsp90 chaperone cycle
The adaptor protein Sti1/Hop connects the Hsp70 and Hsp90 chaperone cycle
Mechanistic Analysis of Conformational Dynamics of the Molecular Chaperone Hsp90
The Hsp70-Hsp90 co-chaperone Hop/Stip1 shifts the proteostatic balance from folding towards degradation
Investigation of the interaction of the Hsp70 and Hsp90 chaperone machine with co-chaperones and substrates
Proteininteraktionsdomänen in Hsp70-Hsp90-Multichaperonkomplexen
Proteininteraktionsdomänen in Hsp70-Hsp90-Multichaperonkomplexen
Mechanistic and conformational studies on the glucocorticoid receptor and the molecular chaperone Hsp90
Crucial HSP70 co-chaperone complex unlocks metazoan protein disaggregation
Investigation of the Hsp90 co-chaperone machinery in eukaryotes
Conformational dynamics of the Hsp70 chaperone
Mechanism of the molecular chaperone Hsp90
Co-chaperone interactions in the Hsp90 chaperone cycle
The adaptor protein Sti1/Hop connects the Hsp70 and Hsp90 chaperone cycle
Mechanistic Analysis of Conformational Dynamics of the Molecular Chaperone Hsp90
The Hsp70-Hsp90 co-chaperone Hop/Stip1 shifts the proteostatic balance from folding towards degradation
Investigation of the interaction of the Hsp70 and Hsp90 chaperone machine with co-chaperones and substrates
Proteininteraktionsdomänen in Hsp70-Hsp90-Multichaperonkomplexen
Proteininteraktionsdomänen in Hsp70-Hsp90-Multichaperonkomplexen
Mechanistic and conformational studies on the glucocorticoid receptor and the molecular chaperone Hsp90
Crucial HSP70 co-chaperone complex unlocks metazoan protein disaggregation
Investigation of the Hsp90 co-chaperone machinery in eukaryotes
Conformational dynamics of the Hsp70 chaperone
Mechanism of the molecular chaperone Hsp90
Co-chaperone interactions in the Hsp90 chaperone cycle
The adaptor protein Sti1/Hop connects the Hsp70 and Hsp90 chaperone cycle
Mechanistic Analysis of Conformational Dynamics of the Molecular Chaperone Hsp90
The Hsp70-Hsp90 co-chaperone Hop/Stip1 shifts the proteostatic balance from folding towards degradation
Investigation of the interaction of the Hsp70 and Hsp90 chaperone machine with co-chaperones and substrates
Proteininteraktionsdomänen in Hsp70-Hsp90-Multichaperonkomplexen
Proteininteraktionsdomänen in Hsp70-Hsp90-Multichaperonkomplexen
Mechanistic and conformational studies on the glucocorticoid receptor and the molecular chaperone Hsp90
Crucial HSP70 co-chaperone complex unlocks metazoan protein disaggregation
Investigation of the Hsp90 co-chaperone machinery in eukaryotes
Conformational dynamics of the Hsp70 chaperone