SET7/9-dependent methylation of ARTD1 at K508 stimulates poly-ADP-ribose formation after oxidative stress
- Location
-
Deutsche Nationalbibliothek Frankfurt am Main
- Extent
-
Online-Ressource
- Language
-
Englisch
- Bibliographic citation
-
In: Open Biology ; 3 (2013), 10. - S. 120173-120173. - eISSN 2046-2441
- Classification
-
Biowissenschaften, Biologie
- Event
-
Veröffentlichung
- (where)
-
Konstanz
- (who)
-
Bibliothek der Universität Konstanz
- (when)
-
2013
- Contributor
- URN
-
urn:nbn:de:bsz:352-256988
- Rights
-
Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Last update
-
18.08.2025, 4:01 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
- Kassner, Ingrid
- Andersson, Anneli
- Fey, Monika
- Tomas, Martin
- Ferrando-May, Elisa
- Hottiger, Michael
- Bibliothek der Universität Konstanz
Time of origin
- 2013
Other Objects (12)
Funktion und Regulation des Photorezeptors Sensorrhodopsin I aus Halobacterium salinarium
High-Affinity Interaction of Poly(ADP-ribose) and the Human DEK Oncoprotein Depends upon Chain Length
DEK Is a Poly(ADP-Ribose) Acceptor in Apoptosis and Mediates Resistance to Genotoxic Stress
Poly(ADP-ribose) : PARadigms and PARadoxes
Nucleocytoplasmic transport in apoptosis
Neuronal death in nigral grafts in the absence of poly (ADP-ribose) polymerase activation
PARP1 catalytic variants reveal branching and chain length-specific functions of poly(ADP-ribose) in cellular physiology and stress response
Targeting poly(ADP-ribose) polymerase activity for cancer therapy
In vitro assay for the quantitation of apoptosis-induced alterations of nuclear envelope permeability
NFDI4BIOIMAGE - An Initiative for a National Research Data Infrastructure for Microscopy Data
Physical and functional interactions of the tumor suppressor protein p53 with poly(ADP-ribose) polymerase-1 and its enzymatic product poly(ADP-ribose)
Targeting Poly(ADP)ribose polymerase in BCR/ABL1-positive cells
Funktion und Regulation des Photorezeptors Sensorrhodopsin I aus Halobacterium salinarium
High-Affinity Interaction of Poly(ADP-ribose) and the Human DEK Oncoprotein Depends upon Chain Length
DEK Is a Poly(ADP-Ribose) Acceptor in Apoptosis and Mediates Resistance to Genotoxic Stress
Poly(ADP-ribose) : PARadigms and PARadoxes
Nucleocytoplasmic transport in apoptosis
Neuronal death in nigral grafts in the absence of poly (ADP-ribose) polymerase activation
PARP1 catalytic variants reveal branching and chain length-specific functions of poly(ADP-ribose) in cellular physiology and stress response
Targeting poly(ADP-ribose) polymerase activity for cancer therapy
In vitro assay for the quantitation of apoptosis-induced alterations of nuclear envelope permeability
NFDI4BIOIMAGE - An Initiative for a National Research Data Infrastructure for Microscopy Data
Physical and functional interactions of the tumor suppressor protein p53 with poly(ADP-ribose) polymerase-1 and its enzymatic product poly(ADP-ribose)
Targeting Poly(ADP)ribose polymerase in BCR/ABL1-positive cells
Funktion und Regulation des Photorezeptors Sensorrhodopsin I aus Halobacterium salinarium
High-Affinity Interaction of Poly(ADP-ribose) and the Human DEK Oncoprotein Depends upon Chain Length
DEK Is a Poly(ADP-Ribose) Acceptor in Apoptosis and Mediates Resistance to Genotoxic Stress
Poly(ADP-ribose) : PARadigms and PARadoxes
Nucleocytoplasmic transport in apoptosis
Neuronal death in nigral grafts in the absence of poly (ADP-ribose) polymerase activation
PARP1 catalytic variants reveal branching and chain length-specific functions of poly(ADP-ribose) in cellular physiology and stress response
Targeting poly(ADP-ribose) polymerase activity for cancer therapy
In vitro assay for the quantitation of apoptosis-induced alterations of nuclear envelope permeability
NFDI4BIOIMAGE - An Initiative for a National Research Data Infrastructure for Microscopy Data
Physical and functional interactions of the tumor suppressor protein p53 with poly(ADP-ribose) polymerase-1 and its enzymatic product poly(ADP-ribose)