- Standort
-
Deutsche Nationalbibliothek Frankfurt am Main
- ISSN
-
2041-1723
- Umfang
-
Online-Ressource
- Sprache
-
Englisch
- Anmerkungen
-
online resource.
- Erschienen in
-
LONP1 and mtHSP70 cooperate to promote mitochondrial protein folding ; volume:12 ; number:1 ; day:11 ; month:1 ; year:2021 ; pages:1-10 ; date:12.2021
Nature Communications ; 12, Heft 1 (11.1.2021), 1-10, 12.2021
- Urheber
-
Shin, Chun-Shik
Meng, Shuxia
Garbis, Spiros D.
Moradian, Annie
Taylor, Robert W.
Sweredoski, Michael J.
Lomenick, Brett
Chan, David C.
- Beteiligte Personen und Organisationen
-
SpringerLink (Online service)
- DOI
-
10.1038/s41467-020-20597-z
- URN
-
urn:nbn:de:101:1-2021020612073267197839
- Rechteinformation
-
Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Letzte Aktualisierung
-
27.12.20252032, 08:53 MEZ
Datenpartner
Dieses Objekt wird bereitgestellt von:
Deutsche Nationalbibliothek. Bei Fragen zum Objekt wenden Sie sich bitte an den Datenpartner.
Deutsche Nationalbibliothek. Bei Fragen zum Objekt wenden Sie sich bitte an den Datenpartner.
Beteiligte
- Shin, Chun-Shik
- Meng, Shuxia
- Garbis, Spiros D.
- Moradian, Annie
- Taylor, Robert W.
- Sweredoski, Michael J.
- Lomenick, Brett
- Chan, David C.
- SpringerLink (Online service)
Ähnliche Objekte (12)
The molecular chaperones DNAJB6 and Hsp70 cooperate to suppress α-synuclein aggregation
Trigger factor and DnaK cooperate in folding of newly synthesized proteins
Trigger factor and DnaK cooperate in folding of newly synthesized proteins
Author Correction: The molecular chaperones DNAJB6 and Hsp70 cooperate to suppress α-synuclein aggregation
Hsp70 resolves misfolded states and accelerates productive folding of multi-domain proteins
Structural remodeling of ribosome associated Hsp40-Hsp70 chaperones during co-translational folding
Intronic motif pairs cooperate across exons to promote pre-mRNA splicing
Structural basis for the cooperation of Hsp110 and Hsp70 molecular chaperones in protein folding
Cytotoxin- and chemotaxis-genes cooperate to promote adhesion of photobacterium damselae subsp. damselae
The Hsp70-Hsp90 co-chaperone Hop/Stip1 shifts the proteostatic balance from folding towards degradation
Communicate to cooperate
Cochaperones enable Hsp70 to use ATP energy to stabilize native proteins out of the folding equilibrium
The molecular chaperones DNAJB6 and Hsp70 cooperate to suppress α-synuclein aggregation
Trigger factor and DnaK cooperate in folding of newly synthesized proteins
Trigger factor and DnaK cooperate in folding of newly synthesized proteins
Author Correction: The molecular chaperones DNAJB6 and Hsp70 cooperate to suppress α-synuclein aggregation
Hsp70 resolves misfolded states and accelerates productive folding of multi-domain proteins
Structural remodeling of ribosome associated Hsp40-Hsp70 chaperones during co-translational folding
Intronic motif pairs cooperate across exons to promote pre-mRNA splicing
Structural basis for the cooperation of Hsp110 and Hsp70 molecular chaperones in protein folding
Cytotoxin- and chemotaxis-genes cooperate to promote adhesion of photobacterium damselae subsp. damselae
The Hsp70-Hsp90 co-chaperone Hop/Stip1 shifts the proteostatic balance from folding towards degradation
Communicate to cooperate
Cochaperones enable Hsp70 to use ATP energy to stabilize native proteins out of the folding equilibrium
The molecular chaperones DNAJB6 and Hsp70 cooperate to suppress α-synuclein aggregation
Trigger factor and DnaK cooperate in folding of newly synthesized proteins
Trigger factor and DnaK cooperate in folding of newly synthesized proteins
Author Correction: The molecular chaperones DNAJB6 and Hsp70 cooperate to suppress α-synuclein aggregation
Hsp70 resolves misfolded states and accelerates productive folding of multi-domain proteins
Structural remodeling of ribosome associated Hsp40-Hsp70 chaperones during co-translational folding
Intronic motif pairs cooperate across exons to promote pre-mRNA splicing
Structural basis for the cooperation of Hsp110 and Hsp70 molecular chaperones in protein folding
Cytotoxin- and chemotaxis-genes cooperate to promote adhesion of photobacterium damselae subsp. damselae
The Hsp70-Hsp90 co-chaperone Hop/Stip1 shifts the proteostatic balance from folding towards degradation
Communicate to cooperate