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Title: Structural and biochemical analysis of human ADP-ribosyl-acceptor hydrolase 3 reveals the basis of m

Journal Article · · J. Biol. Chem.

Research Organization:
Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
Sponsoring Organization:
DOE - Office Of Science; National Institutes of Health (NIH)
OSTI ID:
1784972
Journal Information:
J. Biol. Chem., Vol. 296
Country of Publication:
United States
Language:
ENGLISH

References (44)

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(ADP-ribosyl)hydrolases: Structural Basis for Differential Substrate Recognition and Inhibition journal December 2018
Structure of human ADP-ribosyl-acceptor hydrolase 3 bound to ADP-ribose reveals a conformational switch that enables specific substrate recognition journal August 2018
Structure–function analyses reveal the mechanism of the ARH3-dependent hydrolysis of ADP-ribosylation journal September 2018
Proteomic analyses identify ARH3 as a serine mono-ADP-ribosylhydrolase journal December 2017
The ARH and Macrodomain Families of α-ADP-ribose-acceptor Hydrolases Catalyze α-NAD + Hydrolysis journal October 2019
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Serine is the major residue for ADP-ribosylation upon DNA damage journal February 2018
Serine ADP-Ribosylation Depends on HPF1 journal March 2017
HPF1 completes the PARP active site for DNA damage-induced ADP-ribosylation journal February 2020
ADP-ribosyl-acceptor hydrolase 3 regulates poly (ADP-ribose) degradation and cell death during oxidative stress journal November 2013
Bi-allelic ADPRHL2 Mutations Cause Neurodegeneration with Developmental Delay, Ataxia, and Axonal Neuropathy journal November 2018
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