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Article

Ubiquitin Modification by the E3 Ligase/ADP-Ribosyltransferase Dtx3L/Parp9.

Molecular cell - 18 May 2017

Yang Chun-Song, Jividen Kasey, Spencer Adam, Dworak Natalia, Ni Li, Oostdyk Luke T, Chatterjee Mandovi, Kuśmider Beata, Reon Brian, Parlak Mahmut, Gorbunova Vera, Abbas Tarek, Jeffery Erin, Sherman Nicholas E, Paschal Bryce M

Abstract excerpt

ADP-ribosylation of proteins is emerging as an important regulatory mechanism. Depending on the family member, ADP-ribosyltransferases either conjugate a single ADP-ribose to a target or generate ADP-ribose chains. Here we characterize Parp9, a mono-ADP-ribosyltransferase reported to be enzymatically inactive. Parp9 undergoes heterodimerization with Dtx3L, a histone E3 ligase involved in DNA damage repair. We...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 28525742
DOI: 10.1016/j.molcel.2017.04.028
PMCID: PMC5556935

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026. Manifest publication-graph-cohort-2026-09-05.1.

Source receipt: pubmed, retrieved 5 Sept 2026.

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