Functional role of ADP-ribosyl-acceptor hydrolase 3 in poly(ADPribose) polymerase-1 response to oxidative stress

Current Protein and Peptide Science

Volumn 17, Issue 7, 2016, Pages 633-640

  Mashimo, Masato ^a   Moss, Joel ^b  

^a DOSHISHA WOMEN'S COLLEGE OF LIBERAL ARTS   (Japan)

^b NATIONAL HEART LUNG AND BLOOD INSTITUTE   (United States)

Author keywords

ADP ribose acceptor hydrolase 3; Apoptosis inducing factor; Parthanatos; Poly(ADP ribose); Poly(ADP ribose) polymerase 1; Poly(ADPribose) glycohydrolase

Indexed keywords

ADENOSINE DIPHOSPHATE RIBOSE; APOPTOSIS INDUCING FACTOR; GLYCOSIDASE; HYDROLASE; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE 1; ADP RIBOSYL ACCEPTOR HYDROLASE 3; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE 2; NICOTINAMIDE ADENINE DINUCLEOTIDE NUCLEOSIDASE; UNCLASSIFIED DRUG; ADPRHL2 PROTEIN, HUMAN; POLY(ADENOSINE DIPHOSPHATE RIBOSE); PROTEIN BINDING;

CELL FUNCTION; CELLULAR DISTRIBUTION; CHROMATIN ASSEMBLY AND DISASSEMBLY; DNA ALKYLATION; DNA END JOINING REPAIR; DNA REPAIR; ENERGY METABOLISM; ENZYME ACTIVITY; EXCISION REPAIR; GENE SILENCING; GENETIC STABILITY; HOMOLOGOUS RECOMBINATION; NONHUMAN; NUCLEAR LOCALIZATION SIGNAL; OXIDATIVE STRESS; PROTEIN FUNCTION; PROTEIN MODIFICATION; REVIEW; ADENOSINE DIPHOSPHATE RIBOSYLATION; ARTICLE; CELL DEATH; DNA DAMAGE; GENE; HUMAN; PARG GENE; PROTEIN DEGRADATION; PROTEIN EXPRESSION; PROTEIN HYDROLYSIS; PROTEIN LOCALIZATION; PROTEIN STRUCTURE; ANIMAL; CHEMISTRY; ENZYME ACTIVATION; GENE EXPRESSION REGULATION; GENETICS; HYDROLYSIS; METABOLISM; MITOCHONDRION; MULTIGENE FAMILY; PROTEIN DOMAIN; PROTEIN PROCESSING; PROTEIN TRANSPORT;

ANIMALS; CELL DEATH; DNA DAMAGE; ENZYME ACTIVATION; GENE EXPRESSION REGULATION, ENZYMOLOGIC; GLYCOSIDE HYDROLASES; HUMANS; HYDROLYSIS; MITOCHONDRIA; MULTIGENE FAMILY; OXIDATIVE STRESS; POLY (ADP-RIBOSE) POLYMERASE-1; POLY ADENOSINE DIPHOSPHATE RIBOSE; PROTEIN BINDING; PROTEIN INTERACTION DOMAINS AND MOTIFS; PROTEIN PROCESSING, POST-TRANSLATIONAL; PROTEIN TRANSPORT; PROTEOLYSIS;

EID: 84989219415     PISSN: 13892037     EISSN: 18755550     Source Type: Journal    
DOI: 10.2174/1389203717666160419144603     Document Type: Review

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