Poly(ADP-ribosyl)ation of acetyltransferase NAT10 by PARP1 is required for its nucleoplasmic translocation and function in response to DNA damage
- Standort
-
Deutsche Nationalbibliothek Frankfurt am Main
- ISSN
-
1478-811X
- Umfang
-
Online-Ressource
- Sprache
-
Englisch
- Anmerkungen
-
online resource.
- Erschienen in
-
Poly(ADP-ribosyl)ation of acetyltransferase NAT10 by PARP1 is required for its nucleoplasmic translocation and function in response to DNA damage ; volume:20 ; number:1 ; day:19 ; month:8 ; year:2022 ; pages:1-13 ; date:12.2022
Cell communication and signaling ; 20, Heft 1 (19.8.2022), 1-13, 12.2022
- Urheber
-
Liu, Hong-Yi
Liu, Ying-Ying
Zhang, Yin-Ling
Ning, Yan
Zhang, Fang-Lin
Li, Da-Qiang
- Beteiligte Personen und Organisationen
-
SpringerLink (Online service)
- DOI
-
10.1186/s12964-022-00932-1
- URN
-
urn:nbn:de:101:1-2022110718265470534283
- Rechteinformation
-
Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Letzte Aktualisierung
- 15.08.2025, 07:22 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
- Liu, Hong-Yi
- Liu, Ying-Ying
- Zhang, Yin-Ling
- Ning, Yan
- Zhang, Fang-Lin
- Li, Da-Qiang
- SpringerLink (Online service)
Ähnliche Objekte (12)
PARP1-produced poly-ADP-ribose causes the PARP12 translocation to stress granules and impairment of Golgi complex functions
Mitochondrial PARP1 regulates NAD+-dependent poly ADP-ribosylation of mitochondrial nucleoids
Poly-ADP ribosyl polymerase 1 (PARP1) regulates influenza A virus polymerase
At the crossroads of ADP-ribose, PARP1, and XRCC1 in the genotoxic stress response
PARP1 allows proper telomere replication through TRF1 poly (ADP-ribosyl)ation and helicase recruitment
Poly(ADP-ribose)-mediated interplay of XPA and PARP1 leads to reciprocal regulation of protein function
Preserving ester-linked modifications reveals glutamate and aspartate mono-ADP-ribosylation by PARP1 and its reversal by PARG
Therapeutic Potentials of Poly (ADP‐Ribose) Polymerase 1 (PARP1) Inhibition in Multiple Sclerosis and Animal Models: Concept Revisiting
Divalent and multivalent cations control liquid-like assembly of poly(ADP-ribosyl)ated PARP1 into multimolecular associates in vitro
The biological functions of PARP1
PARP1 catalytic variants reveal branching and chain length-specific functions of poly(ADP-ribose) in cellular physiology and stress response
ADP
PARP1-produced poly-ADP-ribose causes the PARP12 translocation to stress granules and impairment of Golgi complex functions
Mitochondrial PARP1 regulates NAD+-dependent poly ADP-ribosylation of mitochondrial nucleoids
Poly-ADP ribosyl polymerase 1 (PARP1) regulates influenza A virus polymerase
At the crossroads of ADP-ribose, PARP1, and XRCC1 in the genotoxic stress response
PARP1 allows proper telomere replication through TRF1 poly (ADP-ribosyl)ation and helicase recruitment
Poly(ADP-ribose)-mediated interplay of XPA and PARP1 leads to reciprocal regulation of protein function
Preserving ester-linked modifications reveals glutamate and aspartate mono-ADP-ribosylation by PARP1 and its reversal by PARG
Therapeutic Potentials of Poly (ADP‐Ribose) Polymerase 1 (PARP1) Inhibition in Multiple Sclerosis and Animal Models: Concept Revisiting
Divalent and multivalent cations control liquid-like assembly of poly(ADP-ribosyl)ated PARP1 into multimolecular associates in vitro
The biological functions of PARP1
PARP1 catalytic variants reveal branching and chain length-specific functions of poly(ADP-ribose) in cellular physiology and stress response
ADP
PARP1-produced poly-ADP-ribose causes the PARP12 translocation to stress granules and impairment of Golgi complex functions
Mitochondrial PARP1 regulates NAD+-dependent poly ADP-ribosylation of mitochondrial nucleoids
Poly-ADP ribosyl polymerase 1 (PARP1) regulates influenza A virus polymerase
At the crossroads of ADP-ribose, PARP1, and XRCC1 in the genotoxic stress response
PARP1 allows proper telomere replication through TRF1 poly (ADP-ribosyl)ation and helicase recruitment
Poly(ADP-ribose)-mediated interplay of XPA and PARP1 leads to reciprocal regulation of protein function
Preserving ester-linked modifications reveals glutamate and aspartate mono-ADP-ribosylation by PARP1 and its reversal by PARG
Therapeutic Potentials of Poly (ADP‐Ribose) Polymerase 1 (PARP1) Inhibition in Multiple Sclerosis and Animal Models: Concept Revisiting
Divalent and multivalent cations control liquid-like assembly of poly(ADP-ribosyl)ated PARP1 into multimolecular associates in vitro
The biological functions of PARP1
PARP1 catalytic variants reveal branching and chain length-specific functions of poly(ADP-ribose) in cellular physiology and stress response