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Titolo:
CYCLIC ADP-RIBOSE AND ITS METABOLIC ENZYMES
Autore:
LEE HC; GRAEFF R; WALSETH TF;
Indirizzi:
UNIV MINNESOTA,LYON LAB 6 186,DEPT PHYSIOL MINNEAPOLIS MN 55455 UNIV MINNESOTA,DEPT PHARMACOL MINNEAPOLIS MN 55455
Titolo Testata:
Biochimie
fascicolo: 5, volume: 77, anno: 1995,
pagine: 345 - 355
SICI:
0300-9084(1995)77:5<345:CAAIME>2.0.ZU;2-M
Fonte:
ISI
Lingua:
ENG
Soggetto:
EGG-SPECIFIC NADASE; SEA-URCHIN EGGS; INOSITOL TRISPHOSPHATE; ANTIGEN CD38; 2ND-MESSENGER ENZYME; CRYSTAL-STRUCTURE; CALCIUM RELEASE; CA2+ RELEASE; HYDROLYSIS; CYCLASE;
Keywords:
CYCLIC ADP-RIBOSE; CA2+ SIGNALING; ADP-RIBOSYL CYCLASE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
42
Recensione:
Indirizzi per estratti:
Citazione:
H.C. Lee et al., "CYCLIC ADP-RIBOSE AND ITS METABOLIC ENZYMES", Biochimie, 77(5), 1995, pp. 345-355

Abstract

Cyclic ADP-ribose (cADPR) is a recently discovered cyclic nucleotide with Ca2+ signaling functions. There is a growing recognition that it is an endogenous modulator of the Ca2+-induced Ca2+ release mechanism in cells. The cyclic structure of cADPR has now been confirmed by X-ray crystallography. A series of analogs of cADPR has been synthesized, including antagonists and a novel analog, cyclic GDP-ribose. Considerable prepress has been made in characterizing ADP-ribosyl cyclase, the synthetic enzyme, and cADPR hydrolase, the hydrolytic enzyme. A new class of bifunctional enzymes has been identified which catalyses both the synthesis and hydrolysis of cADPR. CD38, a lymphocyte differentiation antigen, is a member of this class. The understanding of the mechanisms of regulation of the metabolic enzymes and signaling by cADPR is likely to have important implications and several possibilities are discussed in this article.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 29/09/20 alle ore 12:53:55