Multitasking of Hsp70 chaperone in the biogenesis of bacterial functional amyloids
- Standort
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Deutsche Nationalbibliothek Frankfurt am Main
- ISSN
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2399-3642
- Umfang
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Online-Ressource
- Sprache
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Englisch
- Anmerkungen
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online resource.
- Erschienen in
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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
- Klassifikation
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Biowissenschaften, Biologie
- Urheber
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Sugimoto, Shinya
- Beteiligte Personen und Organisationen
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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
- Rechteinformation
-
Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Letzte Aktualisierung
-
15.08.2025, 07:28 MESZ
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Beteiligte
- Sugimoto, Shinya
- Arita-Morioka, Ken-ichi
- Terao, Akari
- Yamanaka, Kunitoshi
- Ogura, Teru
- Mizunoe, Yoshimitsu
- SpringerLink (Online service)
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Crucial HSP70 co-chaperone complex unlocks metazoan protein disaggregation
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The adaptor protein Sti1/Hop connects the Hsp70 and Hsp90 chaperone cycle
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Cholesterol bound Plasmodium falciparum co-chaperone ‘PFA0660w’ complexes with major virulence factor ‘PfEMP1’ via chaperone ‘PfHsp70-x’
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Conformational dynamics of the Hsp70 chaperone
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Multistep mechanism of substrate binding determines chaperone activity of Hsp70
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The adaptor protein Sti1/Hop connects the Hsp70 and Hsp90 chaperone cycle
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Multiple Funktionen mitochondrialer Chaperone der Klassen Hsp70, 90 und 100 in der Proteinbiogenese
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