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Article: Cyclic ADP-ribose and its metabolic enzymes

TitleCyclic ADP-ribose and its metabolic enzymes
Authors
KeywordsADP-ribosyl cyclase
Ca2+ signaling
Cyclic ADP-ribose
Issue Date1995
PublisherElsevier France, Editions Scientifiques et Medicales. The Journal's web site is located at http://www.elsevier.com/locate/biochi
Citation
Biochimie, 1995, v. 77 n. 5, p. 345-355 How to Cite?
AbstractCyclic 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 progress 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.
Persistent Identifierhttp://hdl.handle.net/10722/132580
ISSN
2015 Impact Factor: 2.474
2015 SCImago Journal Rankings: 1.462
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorLee, HCen_HK
dc.contributor.authorGraeff, Ren_HK
dc.contributor.authorWalseth, TFen_HK
dc.date.accessioned2011-03-28T09:26:30Z-
dc.date.available2011-03-28T09:26:30Z-
dc.date.issued1995en_HK
dc.identifier.citationBiochimie, 1995, v. 77 n. 5, p. 345-355en_HK
dc.identifier.issn0300-9084en_HK
dc.identifier.urihttp://hdl.handle.net/10722/132580-
dc.description.abstractCyclic 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 progress 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.en_HK
dc.languageengen_US
dc.publisherElsevier France, Editions Scientifiques et Medicales. The Journal's web site is located at http://www.elsevier.com/locate/biochien_HK
dc.relation.ispartofBiochimieen_HK
dc.subjectADP-ribosyl cyclaseen_HK
dc.subjectCa2+ signalingen_HK
dc.subjectCyclic ADP-riboseen_HK
dc.titleCyclic ADP-ribose and its metabolic enzymesen_HK
dc.typeArticleen_HK
dc.identifier.emailGraeff, R: graeffr@hku.hken_HK
dc.identifier.authorityGraeff, R=rp01464en_HK
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.doi10.1016/0300-9084(96)88145-4en_HK
dc.identifier.pmid8527488en_HK
dc.identifier.scopuseid_2-s2.0-0029100238en_HK
dc.identifier.volume77en_HK
dc.identifier.issue5en_HK
dc.identifier.spage345en_HK
dc.identifier.epage355en_HK
dc.identifier.isiWOS:A1995RK56300007-
dc.publisher.placeFranceen_HK
dc.identifier.scopusauthoridLee, HC=25934603600en_HK
dc.identifier.scopusauthoridGraeff, R=7003614053en_HK
dc.identifier.scopusauthoridWalseth, TF=7005424273en_HK

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