Phosphorylation induced cochaperone unfolding promotes kinase recruitment and client class-specific Hsp90 phosphorylation
- Standort
-
Deutsche Nationalbibliothek Frankfurt am Main
- ISSN
-
2041-1723
- Umfang
-
Online-Ressource
- Sprache
-
Englisch
- Anmerkungen
-
online resource.
- Erschienen in
-
Phosphorylation induced cochaperone unfolding promotes kinase recruitment and client class-specific Hsp90 phosphorylation ; volume:9 ; number:1 ; day:17 ; month:1 ; year:2018 ; pages:1-14 ; date:12.2018
Nature Communications ; 9, Heft 1 (17.1.2018), 1-14, 12.2018
- Klassifikation
-
Naturwissenschaften
- Urheber
-
Bachman, Ashleigh B.
- Beteiligte Personen und Organisationen
-
Keramisanou, Dimitra
Xu, Wanping
Beebe, Kristin
Moses, Michael A.
Vasantha Kumar, M. V.
Gray, Geoffrey
Noor, Radwan Ebna
van der Vaart, Arjan
Neckers, Len
Gelis, Ioannis
SpringerLink (Online service)
- DOI
-
10.1038/s41467-017-02711-w
- URN
-
urn:nbn:de:1111-2018041122691
- Rechteinformation
-
Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Letzte Aktualisierung
-
14.08.2025, 11:01 MESZ
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
- Bachman, Ashleigh B.
- Keramisanou, Dimitra
- Xu, Wanping
- Beebe, Kristin
- Moses, Michael A.
- Vasantha Kumar, M. V.
- Gray, Geoffrey
- Noor, Radwan Ebna
- van der Vaart, Arjan
- Neckers, Len
- Gelis, Ioannis
- SpringerLink (Online service)
Ähnliche Objekte (12)
Hsp90 chaperone action: the impact of phosphorylation on cellular proteostasis
Phosphorylation of SARS-CoV-2 Orf9b regulates its targeting to two binding sites in TOM70 and recruitment of Hsp90
Targeting the Hsp90-Cdc37-client protein interaction to disrupt Hsp90 chaperone machinery
Effects of Inhibition of IKK Kinase Phosphorylation On the Cellular Defence System and HSP90 Activity
Phosphorylation-induced conformation of β2-adrenoceptor related to arrestin recruitment revealed by NMR
Hsp90 middle domain phosphorylation initiates a complex conformational program to recruit the ATPase-stimulating cochaperone Aha1
Large‐scale phosphorylation mapping reveals the extent of tyrosine phosphorylation in Arabidopsis
Analysis of the Hsp90 client system in Caenorhabditis elegans
Characterization of different Hsp90-client and chaperone-substrate interactions
Phosphorylation of the β1-adrenoceptor
Electrochemical Phosphorylation of Organic Molecules
Deafness‐Associated ADGRV1 Mutation Impairs USH2A Stability through Improper Phosphorylation of WHRN and WDSUB1 Recruitment
Hsp90 chaperone action: the impact of phosphorylation on cellular proteostasis
Phosphorylation of SARS-CoV-2 Orf9b regulates its targeting to two binding sites in TOM70 and recruitment of Hsp90
Targeting the Hsp90-Cdc37-client protein interaction to disrupt Hsp90 chaperone machinery
Effects of Inhibition of IKK Kinase Phosphorylation On the Cellular Defence System and HSP90 Activity
Phosphorylation-induced conformation of β2-adrenoceptor related to arrestin recruitment revealed by NMR
Hsp90 middle domain phosphorylation initiates a complex conformational program to recruit the ATPase-stimulating cochaperone Aha1
Large‐scale phosphorylation mapping reveals the extent of tyrosine phosphorylation in Arabidopsis
Analysis of the Hsp90 client system in Caenorhabditis elegans
Characterization of different Hsp90-client and chaperone-substrate interactions
Phosphorylation of the β1-adrenoceptor
Electrochemical Phosphorylation of Organic Molecules
Deafness‐Associated ADGRV1 Mutation Impairs USH2A Stability through Improper Phosphorylation of WHRN and WDSUB1 Recruitment
Hsp90 chaperone action: the impact of phosphorylation on cellular proteostasis
Phosphorylation of SARS-CoV-2 Orf9b regulates its targeting to two binding sites in TOM70 and recruitment of Hsp90
Targeting the Hsp90-Cdc37-client protein interaction to disrupt Hsp90 chaperone machinery
Effects of Inhibition of IKK Kinase Phosphorylation On the Cellular Defence System and HSP90 Activity
Phosphorylation-induced conformation of β2-adrenoceptor related to arrestin recruitment revealed by NMR
Hsp90 middle domain phosphorylation initiates a complex conformational program to recruit the ATPase-stimulating cochaperone Aha1
Large‐scale phosphorylation mapping reveals the extent of tyrosine phosphorylation in Arabidopsis
Analysis of the Hsp90 client system in Caenorhabditis elegans
Characterization of different Hsp90-client and chaperone-substrate interactions
Phosphorylation of the β1-adrenoceptor
Electrochemical Phosphorylation of Organic Molecules