ArticleThe Journal of biological chemistry2018
Structure-function analyses reveal the mechanism of the ARH3-dependent hydrolysis of ADP-ribosylation.
Article in The Journal of biological chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 17 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
17 citing papers in PubMed, 21 citations in OpenAlex.
- NovelNeurology. Genetics · 2026Article
- Review
- ARH Family of ADP-Ribose-Acceptor Hydrolases.Cells · 2022Review
- BiallelicLife science alliance · 2021Article
- Episodic psychosis, ataxia, motor neuropathy with pyramidal signs (PAMP syndrome) caused by a novel mutation in ADPRHL2 (AHR3).Neurological sciences : official journal of the Italian Neurological Society and of the Italian Society of Clinical Neurophysiology · 2021Article
- Mechanistic insights into the three steps of poly(ADP-ribosylation) reversal.Nature communications · 2021Article
- The Making and Breaking of Serine-ADP-Ribosylation in the DNA Damage Response.Frontiers in cell and developmental biology · 2021Review
- AI26 inhibits the ADP-ribosylhydrolase ARH3 and suppresses DNA damage repair.The Journal of biological chemistry · 2020Article
- Article
- The Controversial Roles of ADP-Ribosyl Hydrolases MACROD1, MACROD2 and TARG1 in Carcinogenesis.Cancers · 2020Review
- (ADP-ribosyl)hydrolases: structure, function, and biology.Genes & development · 2020Review
- Article
- The ARH and Macrodomain Families of α-ADP-ribose-acceptor Hydrolases Catalyze α-NADACS chemical biology · 2019Article
- ADP-ribosylation signalling and human disease.Open biology · 2019Review
- Review
- (ADP-ribosyl)hydrolases: Structural Basis for Differential Substrate Recognition and Inhibition.Cell chemical biology · 2018Article
- Structural and biochemical analysis of human ADP-ribosyl-acceptor hydrolase 3 reveals the basis of metal selectivity and different roles for the two magnesium ions.The Journal of biological chemistryArticle
Corrections and comments
- Erratum issued
Authors and funding
6 authors at 3 institutions in 2 countries.
Funding
Abstract
ADP-ribosylation of proteins plays key roles in multiple biological processes, including DNA damage repair. Recent evidence suggests that serine is an important acceptor for ADP-ribosylation, and that serine ADP-ribosylation is hydrolyzed by ADP-ribosylhydrolase 3 (ARH3 or ADPRHL2). However, the structural details in ARH3-mediated hydrolysis remain elusive. Here, we determined the structure of ARH3 in a complex with ADP-ribose (ADPR). Our analyses revealed a group of acidic residues in ARH3 that keep two Mg
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.