Structure-function analysis indicates that sumoylation modulates DNA-binding activity of STAT1
- Location
-
Deutsche Nationalbibliothek Frankfurt am Main
- ISSN
-
1471-2091
- Extent
-
Online-Ressource
- Language
-
Englisch
- Notes
-
online resource.
- Bibliographic citation
-
Structure-function analysis indicates that sumoylation modulates DNA-binding activity of STAT1 ; volume:13 ; number:1 ; day:8 ; month:10 ; year:2012 ; pages:1-12 ; date:12.2012
BMC biochemistry ; 13, Heft 1 (8.10.2012), 1-12, 12.2012
- Creator
-
Grönholm, Juha
- Contributor
-
Vanhatupa, Sari
Ungureanu, Daniela
Väliaho, Jouni
Laitinen, Tuomo
Valjakka, Jarkko
Silvennoinen, Olli
SpringerLink (Online service)
- DOI
-
10.1186/1471-2091-13-20
- URN
-
urn:nbn:de:1111-2016030211323
- Rights
-
Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Last update
-
15.08.2025, 7:36 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
- Grönholm, Juha
- Vanhatupa, Sari
- Ungureanu, Daniela
- Väliaho, Jouni
- Laitinen, Tuomo
- Valjakka, Jarkko
- Silvennoinen, Olli
- SpringerLink (Online service)
Other Objects (12)
Structure-function analysis of the STAT1 N-domain
Two glutamic acid residues in the DNA-binding domain are engaged in the release of STAT1 dimers from DNA
Circular RNA-encoded oncogenic PIAS1 variant blocks immunogenic ferroptosis by modulating the balance between SUMOylation and phosphorylation of STAT1
Correction: Circular RNA-encoded oncogenic PIAS1 variant blocks immunogenic ferroptosis by modulating the balance between SUMOylation and phosphorylation of STAT1
HIV-1 and SUMOylation
Stat1 Signalweg bei Atherosklerose
Hes-1 SUMOylation by protein inhibitor of activated STAT1 enhances the suppressing effect of Hes-1 on GADD45α expression to increase cell survival
Intrazelluläre Dynamik des Transkriptionsfaktors STAT1
PIAS3 modulate HIV-1 integrase SUMOylation
Inhibition of sumoylation prevents experimental fibrosis
Structure-function relationships of metalloenzymes
ERK is a negative feedback regulator for IFN-γ/STAT1 signaling by promoting STAT1 ubiquitination
Structure-function analysis of the STAT1 N-domain
Two glutamic acid residues in the DNA-binding domain are engaged in the release of STAT1 dimers from DNA
Circular RNA-encoded oncogenic PIAS1 variant blocks immunogenic ferroptosis by modulating the balance between SUMOylation and phosphorylation of STAT1
Correction: Circular RNA-encoded oncogenic PIAS1 variant blocks immunogenic ferroptosis by modulating the balance between SUMOylation and phosphorylation of STAT1
HIV-1 and SUMOylation
Stat1 Signalweg bei Atherosklerose
Hes-1 SUMOylation by protein inhibitor of activated STAT1 enhances the suppressing effect of Hes-1 on GADD45α expression to increase cell survival
Intrazelluläre Dynamik des Transkriptionsfaktors STAT1
PIAS3 modulate HIV-1 integrase SUMOylation
Inhibition of sumoylation prevents experimental fibrosis
Structure-function relationships of metalloenzymes
ERK is a negative feedback regulator for IFN-γ/STAT1 signaling by promoting STAT1 ubiquitination
Structure-function analysis of the STAT1 N-domain
Two glutamic acid residues in the DNA-binding domain are engaged in the release of STAT1 dimers from DNA
Circular RNA-encoded oncogenic PIAS1 variant blocks immunogenic ferroptosis by modulating the balance between SUMOylation and phosphorylation of STAT1
Correction: Circular RNA-encoded oncogenic PIAS1 variant blocks immunogenic ferroptosis by modulating the balance between SUMOylation and phosphorylation of STAT1
HIV-1 and SUMOylation
Stat1 Signalweg bei Atherosklerose
Hes-1 SUMOylation by protein inhibitor of activated STAT1 enhances the suppressing effect of Hes-1 on GADD45α expression to increase cell survival
Intrazelluläre Dynamik des Transkriptionsfaktors STAT1
PIAS3 modulate HIV-1 integrase SUMOylation
Inhibition of sumoylation prevents experimental fibrosis
Structure-function relationships of metalloenzymes