Biological roles of mono- and poly(ADP-ribosyl)ation. 1992

K Ueda, and M Banasik, and I Saito, and T Kido, and B R Das, and N A Abed, and H Komura
Department of Clinical Science and Laboratory Medicine, Kyoto University Faculty of Medicine, Japan.

UI MeSH Term Description Entries
D011065 Poly(ADP-ribose) Polymerases Enzymes that catalyze the transfer of multiple ADP-RIBOSE groups from nicotinamide-adenine dinucleotide (NAD) onto protein targets, thus building up a linear or branched homopolymer of repeating ADP-ribose units i.e., POLY ADENOSINE DIPHOSPHATE RIBOSE. ADP-Ribosyltransferase (Polymerizing),Poly ADP Ribose Polymerase,Poly(ADP-Ribose) Synthase,Poly(ADP-ribose) Polymerase,PARP Polymerase,Poly ADP Ribose Transferase,Poly ADP-Ribose Synthase,Poly(ADP-Ribose) Transferase,Poly(ADPR) Polymerase,Poly(ADPribose) Polymerase,Poly ADP Ribose Synthase,Polymerase, PARP,Synthase, Poly ADP-Ribose
D011499 Protein Processing, Post-Translational Any of various enzymatically catalyzed post-translational modifications of PEPTIDES or PROTEINS in the cell of origin. These modifications include carboxylation; HYDROXYLATION; ACETYLATION; PHOSPHORYLATION; METHYLATION; GLYCOSYLATION; ubiquitination; oxidation; proteolysis; and crosslinking and result in changes in molecular weight and electrophoretic motility. Amino Acid Modification, Post-Translational,Post-Translational Modification,Post-Translational Protein Modification,Posttranslational Modification,Protein Modification, Post-Translational,Amino Acid Modification, Posttranslational,Post-Translational Amino Acid Modification,Post-Translational Modifications,Post-Translational Protein Processing,Posttranslational Amino Acid Modification,Posttranslational Modifications,Posttranslational Protein Processing,Protein Processing, Post Translational,Protein Processing, Posttranslational,Amino Acid Modification, Post Translational,Modification, Post-Translational,Modification, Post-Translational Protein,Modification, Posttranslational,Modifications, Post-Translational,Modifications, Post-Translational Protein,Modifications, Posttranslational,Post Translational Amino Acid Modification,Post Translational Modification,Post Translational Modifications,Post Translational Protein Modification,Post Translational Protein Processing,Post-Translational Protein Modifications,Processing, Post-Translational Protein,Processing, Posttranslational Protein,Protein Modification, Post Translational,Protein Modifications, Post-Translational
D006801 Humans Members of the species Homo sapiens. Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D000067856 Poly(ADP-ribose) Polymerase Inhibitors Chemicals and drugs that inhibit the action of POLY(ADP-RIBOSE)POLYMERASES. Inhibitors of Poly(ADP-ribose) Polymerase,PARP Inhibitor,Poly(ADP-Ribose) Polymerase Inhibitor,Poly(ADP-ribosylation) Inhibitor,Inhibitors of Poly(ADP-ribose) Polymerases,PARP Inhibitors,Poly(ADP-ribosylation) Inhibitors,Inhibitor, PARP,Inhibitors, PARP
D000246 Adenosine Diphosphate Ribose An ester formed between the aldehydic carbon of RIBOSE and the terminal phosphate of ADENOSINE DIPHOSPHATE. It is produced by the hydrolysis of nicotinamide-adenine dinucleotide (NAD) by a variety of enzymes, some of which transfer an ADP-ribosyl group to target proteins. ADP Ribose,Adenosine Diphosphoribose,ADP-Ribose,ADPribose,Adenosine 5'-Diphosphoribose,5'-Diphosphoribose, Adenosine,Adenosine 5' Diphosphoribose,Diphosphate Ribose, Adenosine,Diphosphoribose, Adenosine,Ribose, ADP,Ribose, Adenosine Diphosphate
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia
D001704 Biopolymers Polymers synthesized by living organisms. They play a role in the formation of macromolecular structures and are synthesized via the covalent linkage of biological molecules, especially AMINO ACIDS; NUCLEOTIDES; and CARBOHYDRATES. Bioplastics,Bioplastic,Biopolymer
D036002 ADP Ribose Transferases Enzymes that transfer the ADP-RIBOSE group of NAD or NADP to proteins or other small molecules. Transfer of ADP-ribose to water (i.e., hydrolysis) is catalyzed by the NADASES. The mono(ADP-ribose)transferases transfer a single ADP-ribose. POLY(ADP-RIBOSE) POLYMERASES transfer multiple units of ADP-ribose to protein targets, building POLY ADENOSINE DIPHOSPHATE RIBOSE in linear or branched chains. ADP-Ribosyltransferase,Mono(ADP-Ribose) Transferases,NAD(P)(+)-Arginine ADP-Ribosyltransferase,NAD+ ADP-Ribosyltransferase,ADP Ribose Transferase,ADPRT,ADPRTs,ART Transferase,ART Transferases,ARTase,ARTases,Mono ADP-ribose Transferases,Mono ADPribose Transferase,Mono ADPribose Transferases,Mono(ADP-Ribose) Transferase,Mono(ADP-Ribosyl)transferase,Mono(ADPribosyl)transferase,Mono-ADP-Ribosyltransferase,MonoADPribosyltransferase,NAD ADP-Ribosyltransferase,NAD(+)-L-arginine ADP-D-ribosyltransferase,NAD-Agmatine ADP-Ribosyltransferase,NAD-Arginine ADP-Ribosyltransferase,NADP-ADPRTase,NADP-Arginine ADP-Ribosyltransferase,ADP Ribosyltransferase,ADP-Ribosyltransferase, NAD,ADP-Ribosyltransferase, NAD+,ADP-Ribosyltransferase, NAD-Agmatine,ADP-Ribosyltransferase, NAD-Arginine,ADP-Ribosyltransferase, NADP-Arginine,ADP-ribose Transferases, Mono,ADPribose Transferase, Mono,ADPribose Transferases, Mono,Mono ADP Ribosyltransferase,Mono ADP ribose Transferases,NAD ADP Ribosyltransferase,NAD Agmatine ADP Ribosyltransferase,NAD Arginine ADP Ribosyltransferase,NAD+ ADP Ribosyltransferase,NADP ADPRTase,NADP Arginine ADP Ribosyltransferase,Ribose Transferase, ADP,Ribose Transferases, ADP,Transferase, ADP Ribose,Transferase, ART,Transferase, Mono ADPribose,Transferases, ADP Ribose,Transferases, ART,Transferases, Mono ADP-ribose,Transferases, Mono ADPribose

Related Publications

K Ueda, and M Banasik, and I Saito, and T Kido, and B R Das, and N A Abed, and H Komura
December 1991, Biochemical and biophysical research communications,
K Ueda, and M Banasik, and I Saito, and T Kido, and B R Das, and N A Abed, and H Komura
January 2004, Experimental gerontology,
K Ueda, and M Banasik, and I Saito, and T Kido, and B R Das, and N A Abed, and H Komura
July 2005, Pharmacological research,
K Ueda, and M Banasik, and I Saito, and T Kido, and B R Das, and N A Abed, and H Komura
December 2013, Molecular aspects of medicine,
K Ueda, and M Banasik, and I Saito, and T Kido, and B R Das, and N A Abed, and H Komura
January 1984, Methods in enzymology,
K Ueda, and M Banasik, and I Saito, and T Kido, and B R Das, and N A Abed, and H Komura
December 2013, Molecular aspects of medicine,
K Ueda, and M Banasik, and I Saito, and T Kido, and B R Das, and N A Abed, and H Komura
July 2011, Trends in plant science,
K Ueda, and M Banasik, and I Saito, and T Kido, and B R Das, and N A Abed, and H Komura
December 2004, Science of aging knowledge environment : SAGE KE,
K Ueda, and M Banasik, and I Saito, and T Kido, and B R Das, and N A Abed, and H Komura
January 1997, Reviews of physiology, biochemistry and pharmacology,
K Ueda, and M Banasik, and I Saito, and T Kido, and B R Das, and N A Abed, and H Komura
January 2007, Nucleic acids research,
Copied contents to your clipboard!