- Location
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Deutsche Nationalbibliothek Frankfurt am Main
- Extent
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1 Online-Ressource.
- Language
-
Englisch
- Bibliographic citation
-
Cochaperones convey the energy of ATP hydrolysis for directional action of Hsp90 ; volume:15 ; number:1 ; day:17 ; month:1 ; year:2024 ; pages:1-11 ; date:12.2024
Nature Communications ; 15, Heft 1 (17.1.2024), 1-11, 12.2024
- Creator
- Contributor
-
SpringerLink (Online service)
- DOI
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10.1038/s41467-024-44847-6
- URN
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urn:nbn:de:101:1-2024032916362007856179
- Rights
-
Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Last update
- 14.08.2025, 8:59 AM UTC
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
- Vollmar, Leonie
- Schimpf, Julia
- Hermann, Bianca
- Hugel, Thorsten
- SpringerLink (Online service)
Other Objects (12)
Cochaperones convey the energy of ATP hydrolysis for directional action of Hsp90
Monitoring enzymatic ATP hydrolysis by EPR spectroscopy
ATP-binding and hydrolysis of human NLRP3
Thermodynamic aspects of ATP hydrolysis of actomyosin complex
The Metal Coordination of sCD39 during ATP Hydrolysis
A Tetrahymena Hsp90 co‐chaperone promotes si RNA loading by ATP ‐dependent and ATP ‐independent mechanisms
Mechanistic insights into ATP hydrolysis by the ABC transporter TAP
Visualizing the transiently populated closed-state of human HSP90 ATP binding domain
ATP impedes the inhibitory effect of Hsp90 on A[beta]40 fibrillation
Understanding the ATP hydrolysis mechanism in myosin using computer simulation techniques
The ATP hydrolysis cycle of the nucleotide-binding domain of the mitochondrial ATP-binding cassette transporter Mdl1p
Die ATP-Hydrolyse des molekularen Chaperons Hsp90 und ihre Regulation durch Co-Chaperone
Cochaperones convey the energy of ATP hydrolysis for directional action of Hsp90
Monitoring enzymatic ATP hydrolysis by EPR spectroscopy
ATP-binding and hydrolysis of human NLRP3
Thermodynamic aspects of ATP hydrolysis of actomyosin complex
The Metal Coordination of sCD39 during ATP Hydrolysis
A Tetrahymena Hsp90 co‐chaperone promotes si RNA loading by ATP ‐dependent and ATP ‐independent mechanisms
Mechanistic insights into ATP hydrolysis by the ABC transporter TAP
Visualizing the transiently populated closed-state of human HSP90 ATP binding domain
ATP impedes the inhibitory effect of Hsp90 on A[beta]40 fibrillation
Understanding the ATP hydrolysis mechanism in myosin using computer simulation techniques
The ATP hydrolysis cycle of the nucleotide-binding domain of the mitochondrial ATP-binding cassette transporter Mdl1p
Die ATP-Hydrolyse des molekularen Chaperons Hsp90 und ihre Regulation durch Co-Chaperone
Cochaperones convey the energy of ATP hydrolysis for directional action of Hsp90
Monitoring enzymatic ATP hydrolysis by EPR spectroscopy
ATP-binding and hydrolysis of human NLRP3
Thermodynamic aspects of ATP hydrolysis of actomyosin complex
The Metal Coordination of sCD39 during ATP Hydrolysis
A Tetrahymena Hsp90 co‐chaperone promotes si RNA loading by ATP ‐dependent and ATP ‐independent mechanisms
Mechanistic insights into ATP hydrolysis by the ABC transporter TAP
Visualizing the transiently populated closed-state of human HSP90 ATP binding domain
ATP impedes the inhibitory effect of Hsp90 on A[beta]40 fibrillation
Understanding the ATP hydrolysis mechanism in myosin using computer simulation techniques
The ATP hydrolysis cycle of the nucleotide-binding domain of the mitochondrial ATP-binding cassette transporter Mdl1p