- Location
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Deutsche Nationalbibliothek Frankfurt am Main
- Extent
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1 Online-Ressource.
- Language
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Englisch
- Bibliographic citation
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Single-molecule evidence of Entropic Pulling by Hsp70 chaperones ; volume:15 ; number:1 ; day:8 ; month:10 ; year:2024 ; pages:1-8 ; date:12.2024
Nature Communications ; 15, Heft 1 (8.10.2024), 1-8, 12.2024
- Creator
- Contributor
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SpringerLink (Online service)
- DOI
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10.1038/s41467-024-52674-y
- URN
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urn:nbn:de:101:1-2412202118115.653240043641
- Rights
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Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Last update
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15.08.2025, 7:21 AM 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.
Associated
- Rukes, Verena
- Rebeaud, Mathieu E.
- Perrin, Louis W.
- De Los Rios, Paolo
- Cao, Chan
- SpringerLink (Online service)
Other Objects (12)
Analysis of the conformational dynamics of Hsp70 and Hsp90 chaperones
Insights into the molecular mechanisms of interdomain communication in Hsp70 chaperones
Single-molecule fluorescence studies of protein folding and molecular chaperones
Single-molecule fluorescence studies of Protein Folding and Molecular Chaperones
The molecular chaperones DNAJB6 and Hsp70 cooperate to suppress α-synuclein aggregation
Structural remodeling of ribosome associated Hsp40-Hsp70 chaperones during co-translational folding
DNAJB6 mutants display toxic gain of function through unregulated interaction with Hsp70 chaperones
Structural basis for the cooperation of Hsp110 and Hsp70 molecular chaperones in protein folding
Author Correction: The molecular chaperones DNAJB6 and Hsp70 cooperate to suppress α-synuclein aggregation
Pulling
Entropic herding
Investigation of the interaction of the Hsp70 and Hsp90 chaperone machine with co-chaperones and substrates
Analysis of the conformational dynamics of Hsp70 and Hsp90 chaperones
Insights into the molecular mechanisms of interdomain communication in Hsp70 chaperones
Single-molecule fluorescence studies of protein folding and molecular chaperones
Single-molecule fluorescence studies of Protein Folding and Molecular Chaperones
The molecular chaperones DNAJB6 and Hsp70 cooperate to suppress α-synuclein aggregation
Structural remodeling of ribosome associated Hsp40-Hsp70 chaperones during co-translational folding
DNAJB6 mutants display toxic gain of function through unregulated interaction with Hsp70 chaperones
Structural basis for the cooperation of Hsp110 and Hsp70 molecular chaperones in protein folding
Author Correction: The molecular chaperones DNAJB6 and Hsp70 cooperate to suppress α-synuclein aggregation
Pulling
Entropic herding
Investigation of the interaction of the Hsp70 and Hsp90 chaperone machine with co-chaperones and substrates
Analysis of the conformational dynamics of Hsp70 and Hsp90 chaperones
Insights into the molecular mechanisms of interdomain communication in Hsp70 chaperones
Single-molecule fluorescence studies of protein folding and molecular chaperones
Single-molecule fluorescence studies of Protein Folding and Molecular Chaperones
The molecular chaperones DNAJB6 and Hsp70 cooperate to suppress α-synuclein aggregation
Structural remodeling of ribosome associated Hsp40-Hsp70 chaperones during co-translational folding
DNAJB6 mutants display toxic gain of function through unregulated interaction with Hsp70 chaperones
Structural basis for the cooperation of Hsp110 and Hsp70 molecular chaperones in protein folding
Author Correction: The molecular chaperones DNAJB6 and Hsp70 cooperate to suppress α-synuclein aggregation
Pulling
Entropic herding