Dual roles of HSP70 chaperone HSPA1 in quality control of nascent and newly synthesized proteins
- Location
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Deutsche Nationalbibliothek Frankfurt am Main
- Extent
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Online-Ressource
- Language
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Englisch
- Bibliographic citation
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Dual roles of HSP70 chaperone HSPA1 in quality control of nascent and newly synthesized proteins ; day:19 ; month:05 ; year:2021 ; extent:23
The EMBO journal / European Molecular Biology Organization ; (19.05.2021) (gesamt 23)
- Creator
- DOI
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10.15252/embj.2020106183
- URN
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urn:nbn:de:101:1-2021052015040631123704
- Rights
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Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Last update
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14.08.2025, 10:49 AM CEST
Data provider
This object is provided by:
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Deutsche Nationalbibliothek. If you have any questions about the object, please contact the data provider.
Associated
- Tian, Guiyou
- Hu, Cheng
- Yun, Yun
- Yang, Wensheng
- Dubiel, Wolfgang
- Cheng, Yabin
- Wolf, Dieter A.
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Multistep mechanism of substrate binding determines chaperone activity of Hsp70
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Conformational dynamics of the Hsp70 chaperone
Crucial HSP70 co-chaperone complex unlocks metazoan protein disaggregation
Mechanistic Analysis of the Hsp70/ Hsp90 Co-chaperone Sti1
Multistep mechanism of substrate binding determines chaperone activity of Hsp70
Getting newly synthesized proteins into shape
Multitasking of Hsp70 chaperone in the biogenesis of bacterial functional amyloids
Structure and function of hip, an attenuator of the Hsp70 chaperone cycle
The adaptor protein Sti1/Hop connects the Hsp70 and Hsp90 chaperone cycle
Structure and function of hip, an attenuator of the Hsp70 chaperone cycle
Cholesterol bound Plasmodium falciparum co-chaperone ‘PFA0660w’ complexes with major virulence factor ‘PfEMP1’ via chaperone ‘PfHsp70-x’
Multiple Funktionen mitochondrialer Chaperone der Klassen Hsp70, 90 und 100 in der Proteinbiogenese
Chaperone-assisted folding of newly synthesized proteins in the cytosol
Conformational dynamics of the Hsp70 chaperone
Crucial HSP70 co-chaperone complex unlocks metazoan protein disaggregation
Mechanistic Analysis of the Hsp70/ Hsp90 Co-chaperone Sti1
Multistep mechanism of substrate binding determines chaperone activity of Hsp70
Getting newly synthesized proteins into shape
Multitasking of Hsp70 chaperone in the biogenesis of bacterial functional amyloids
Structure and function of hip, an attenuator of the Hsp70 chaperone cycle
The adaptor protein Sti1/Hop connects the Hsp70 and Hsp90 chaperone cycle
Structure and function of hip, an attenuator of the Hsp70 chaperone cycle
Cholesterol bound Plasmodium falciparum co-chaperone ‘PFA0660w’ complexes with major virulence factor ‘PfEMP1’ via chaperone ‘PfHsp70-x’