Manual transfer of experimentally-verified manual GO annotation data to orthologs by curator judgment of sequence similarity

Annotation inferences using phylogenetic trees

Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt

Gene Ontology annotation based on curation of immunofluorescence data

Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara

Electronic Gene Ontology annotations created by ARBA machine learning models

Combined Automated Annotation using Multiple IEA Methods

Identification and characterization of a mammalian 39-kDa poly(ADP-ribose) glycohydrolase.

The structure of human ADP-ribosylhydrolase 3 (ARH3) provides insights into the reversibility of protein ADP-ribosylation.

The 39-kDa poly(ADP-ribose) glycohydrolase ARH3 hydrolyzes O-acetyl-ADP-ribose, a product of the Sir2 family of acetyl-histone deacetylases.

Functional localization of two poly(ADP-ribose)-degrading enzymes to the mitochondrial matrix.

Hydrolysis of O-acetyl-ADP-ribose isomers by ADP-ribosylhydrolase 3.

ADP-ribosylhydrolase 3 (ARH3), not poly(ADP-ribose) glycohydrolase (PARG) isoforms, is responsible for degradation of mitochondrial matrix-associated poly(ADP-ribose).

ADP-ribosyl-acceptor hydrolase 3 regulates poly (ADP-ribose) degradation and cell death during oxidative stress.

Serine ADP-ribosylation reversal by the hydrolase ARH3.

Proteomic analyses identify ARH3 as a serine mono-ADP-ribosylhydrolase.

Structure of human ADP-ribosyl-acceptor hydrolase 3 bound to ADP-ribose reveals a conformational switch that enables specific substrate recognition.

Structure-function analyses reveal the mechanism of the ARH3-dependent hydrolysis of ADP-ribosylation.

Biallelic Mutations in ADPRHL2, Encoding ADP-Ribosylhydrolase 3, Lead to a Degenerative Pediatric Stress-Induced Epileptic Ataxia Syndrome.

Bi-allelic ADPRHL2 Mutations Cause Neurodegeneration with Developmental Delay, Ataxia, and Axonal Neuropathy.

PARP1 inhibition alleviates injury in ARH3-deficient mice and human cells.

The ARH and Macrodomain Families of α-ADP-ribose-acceptor Hydrolases Catalyze α-NAD(+) Hydrolysis.

A reference map of the human binary protein interactome.

An HPF1/PARP1-Based Chemical Biology Strategy for Exploring ADP-Ribosylation.

Molecular Tools for the Study of ADP-Ribosylation: A Unified and Versatile Method to Synthesise Native Mono-ADP-Ribosylated Peptides.

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.

Unrestrained poly-ADP-ribosylation provides insights into chromatin regulation and human disease.

Mechanistic insights into the three steps of poly(ADP-ribosylation) reversal.

Biallelic ADPRHL2 mutations in complex neuropathy affect ADP ribosylation and DNA damage response.

The regulatory landscape of the human HPF1- and ARH3-dependent ADP-ribosylome.

Quantitative high-confidence human mitochondrial proteome and its dynamics in cellular context.

Serine ADP-ribosylation in Drosophila provides insights into the evolution of reversible ADP-ribosylation signalling.

Reversal of tyrosine-linked ADP-ribosylation by ARH3 and PARG.

Resolution of AP sites via the multiple-nucleotide patch replacement pathway

ADPRHL2 hydrolyses poly(ADP-ribose)