Monografie
Hsp70 resolves misfolded states and accelerates productive folding of multi-domain proteins
- Language
-
Englisch
- Identifier
-
1248030567
- Subject
-
Proteins
- Contributor
-
İmamoğlu, Rahmi
Hartl, Ulrich
- DOI
-
10.5282/edoc.29042
- URN
- Rights
-
Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Last update
-
26.01.2023, 1:57 PM CET
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
- Monografie
Associated
- İmamoğlu, Rahmi
- Hartl, Ulrich
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Analysis of chaperone function in multi-domain protein folding
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Transition states and loop closure principles in protein folding
Mechanisms of de novo multi-domain protein folding in bacteria and eukaryotes
Chaperonin-catalyzed rescue of kinetically trapped states in protein folding
Standard Folding
Role of the Hep1 chaperone in the de novo folding and the prevention of aggregation of the mitochondrial Hsp70 chaperone Ssc1
Role of the Hep1 chaperone in the de novo folding and the prevention of aggregation of the mitochondrial Hsp70 chaperone Ssc1
From RNA folding to inverse folding: a computational study : Folding and design of RNA molecules
The eukaryotic chaperonin TRiC domain-wise folding of multi-domain proteins
The eukaryotic chaperonin TRiC : domain-wise folding of multi-domain proteins
Structural basis for the cooperation of Hsp110 and Hsp70 molecular chaperones in protein folding
Analysis of chaperone function in multi-domain protein folding
Folding
Transition states and loop closure principles in protein folding
Mechanisms of de novo multi-domain protein folding in bacteria and eukaryotes
Chaperonin-catalyzed rescue of kinetically trapped states in protein folding
Standard Folding
Role of the Hep1 chaperone in the de novo folding and the prevention of aggregation of the mitochondrial Hsp70 chaperone Ssc1
Role of the Hep1 chaperone in the de novo folding and the prevention of aggregation of the mitochondrial Hsp70 chaperone Ssc1
From RNA folding to inverse folding: a computational study : Folding and design of RNA molecules
The eukaryotic chaperonin TRiC domain-wise folding of multi-domain proteins
The eukaryotic chaperonin TRiC : domain-wise folding of multi-domain proteins
Structural basis for the cooperation of Hsp110 and Hsp70 molecular chaperones in protein folding
Analysis of chaperone function in multi-domain protein folding
Folding
Transition states and loop closure principles in protein folding
Mechanisms of de novo multi-domain protein folding in bacteria and eukaryotes
Chaperonin-catalyzed rescue of kinetically trapped states in protein folding
Standard Folding
Role of the Hep1 chaperone in the de novo folding and the prevention of aggregation of the mitochondrial Hsp70 chaperone Ssc1
Role of the Hep1 chaperone in the de novo folding and the prevention of aggregation of the mitochondrial Hsp70 chaperone Ssc1