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Titolo:
pADPRT-2: a novel mammalian polymerizing(ADP-ribosyl)transferase gene related to truncated pADPRT homologues in plants and Caenorhabditis elegans
Autore:
Berghammer, H; Ebner, M; Marksteiner, R; Auer, B;
Indirizzi:
Innsbruck Univ, Inst Biochem, A-6020 Innsbruck, Austria Innsbruck Univ Innsbruck Austria A-6020 ochem, A-6020 Innsbruck, Austria
Titolo Testata:
FEBS LETTERS
fascicolo: 2-3, volume: 449, anno: 1999,
pagine: 259 - 263
SICI:
0014-5793(19990423)449:2-3<259:PANMPG>2.0.ZU;2-I
Fonte:
ISI
Lingua:
ENG
Soggetto:
POLY(ADP-RIBOSE) POLYMERASE; DICTYOSTELIUM-DISCOIDEUM; TRANSFERASE; GENERATION; ADPRT; MOUSE; CELLS; MICE;
Keywords:
poly(ADP-ribosyl)ation; polymerizing(ADP-ribosyl)transferase negative mouse; genomic organization; activity gel analysis; sequence comparison;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
24
Recensione:
Indirizzi per estratti:
Indirizzo: Auer, B Innsbruck Univ, Inst Biochem, Peter Mayrstr 1A, A-6020 Innsbruck, Austria Innsbruck Univ Peter Mayrstr 1A Innsbruck Austria A-6020 Austria
Citazione:
H. Berghammer et al., "pADPRT-2: a novel mammalian polymerizing(ADP-ribosyl)transferase gene related to truncated pADPRT homologues in plants and Caenorhabditis elegans", FEBS LETTER, 449(2-3), 1999, pp. 259-263

Abstract

Until recently, poly(ADP-ribosyl)ation was supposed to he confined only topolymerizing(ADP-ribosyl)transferase/(ADP-ribose)polymerase (E.C. 2.4.2.30), Here, we present novel polymerizing(ADP-ribosyl)transferase homologues from mouse and man that lack all of the N-terminal DSA binding and BRCA1 C-terminus domains and will be designated polymerizing(ADP-ribosyl)transferase-2 as distinguished from the classical polymerizing(ADP-ribosyl)transferase(polymerizing(ADP-ribosyl)transferase-1). The murine polymerizing(ADP-ribosyl)transferase-2 gene shares three identical intron positions with its Caenorhabditis elegans (EMBL nucleotide sequence database Z47075) and one withthe Arabidopsis thaliana homologue ('APP', GenBank database AF069298), Expression of the murine polymerizing(ADP-ribosyl)transferase-2 gene was elevated in spleen, thymus and testis and the corresponding poly(ADP-ribosyl)ation activity might account for most of the residual poly(ADP-ribosyl)ation observed in polymerizing(ADP-ribosyl)transferase-1(-/-) mice. (C) 1999 Federation of European Biochemical Societies.

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Documento generato il 27/05/20 alle ore 09:06:17