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Paper Details

Ubiquitin Modification by the E3 Ligase/ADP-Ribosyltransferase Dtx3L/Parp9.
Mol Cell
132
2017
ADP, ADP-, ADP-Ribosyltransferase, ADP-ribosyltransferases, Dtx3L, E1, E2 enzymes, E3, E3 Ligase, Gly76, NAD+, Parp9, Parp9 macrodomains, Ub, Ub Gly76, Ub carboxyl terminus, Ubiquitin, carboxyl, histone E3 ligase, mono-ADP-ribosyltransferase, poly(ADP-ribose), ribose, ribosyltransferases, ubiquitin
Adenosine Diphosphate Ribose, Cell Line, Tumor, DNA Repair, HEK293 Cells, Humans, Mutation, NAD, Neoplasm Proteins, Neoplasms, Poly(ADP-ribose) Polymerases, Protein Binding, Protein Interaction Domains and Motifs, RNA Interference, Time Factors, Transfection, Ubiquitin, Ubiquitin-Protein Ligases, Ubiquitination
Author NameAffiliation
Chunsong YangCenter for Cell Signaling, University of Virginia
Kasey JividenCenter for Cell Signaling, University of Virginia
Adam SpencerCenter for Cell Signaling, University of Virginia
Natalia DworakCenter for Cell Signaling, University of Virginia
Li NiCenter for Cell Signaling, University of Virginia
Luke T OostdykCenter for Cell Signaling, University of Virginia
Mandovi ChatterjeeCenter for Cell Signaling, University of Virginia
Beata KusmiderCenter for Cell Signaling, University of Virginia
Brian J ReonUniversity of Virginia
Mahmut ParlakUniversity of Virginia
Vera GorbunovaUniversity of Rochester
Tarek AbbasCenter for Cell Signaling, University of Virginia
Erin D JefferyUniversity of Virginia
Nicholas E ShermanUniversity of Virginia
Bryce M PaschalCenter for Cell Signaling, University of Virginia
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