Multitasking of Hsp70 chaperone in the biogenesis of bacterial functional amyloids
- Location
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Deutsche Nationalbibliothek Frankfurt am Main
- ISSN
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2399-3642
- Extent
-
Online-Ressource
- Language
-
Englisch
- Notes
-
online resource.
- Bibliographic citation
-
Multitasking of Hsp70 chaperone in the biogenesis of bacterial functional amyloids ; volume:1 ; number:1 ; day:31 ; month:5 ; year:2018 ; pages:1-14 ; date:12.2018
Communications biology ; 1, Heft 1 (31.5.2018), 1-14, 12.2018
- Classification
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Biowissenschaften, Biologie
- Creator
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Sugimoto, Shinya
- Contributor
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Arita-Morioka, Ken-ichi
Terao, Akari
Yamanaka, Kunitoshi
Ogura, Teru
Mizunoe, Yoshimitsu
SpringerLink (Online service)
- DOI
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10.1038/s42003-018-0056-0
- URN
-
urn:nbn:de:101:1-2018072217400466044860
- Rights
-
Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Last update
-
15.08.2025, 7:28 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
- Sugimoto, Shinya
- Arita-Morioka, Ken-ichi
- Terao, Akari
- Yamanaka, Kunitoshi
- Ogura, Teru
- Mizunoe, Yoshimitsu
- SpringerLink (Online service)
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The adaptor protein Sti1/Hop connects the Hsp70 and Hsp90 chaperone cycle
Structure and function of hip, an attenuator of the Hsp70 chaperone cycle
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Snapshots of proteasomal precursor complexes reveal chaperone involvement in 20S proteasome biogenesis
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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
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
Snapshots of proteasomal precursor complexes reveal chaperone involvement in 20S proteasome biogenesis
Multitasking
Multitasking
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
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
Snapshots of proteasomal precursor complexes reveal chaperone involvement in 20S proteasome biogenesis
Multitasking