File Download

There are no files associated with this item.

  Links for fulltext
     (May Require Subscription)
Supplementary

Article: Structures and activities of cyclic ADP-ribose, NAADP and their metabolic enzymes

TitleStructures and activities of cyclic ADP-ribose, NAADP and their metabolic enzymes
Authors
KeywordsCa2+
Cyclic ADP-ribose (cADPR)
Nicotinic acid adenine dinucleotide phosphate (NAADP)
Issue Date1999
PublisherSpringer New York LLC. The Journal's web site is located at http://springerlink.metapress.com/openurl.asp?genre=journal&issn=0300-8177
Citation
Molecular And Cellular Biochemistry, 1999, v. 193 n. 1-2, p. 89-98 How to Cite?
AbstractADP-ribosyl cyclase and CD38 are multi-functional enzymes involved in calcium signaling. Both can cyclize NAD and its guanine analog, NGD, at two different sites of the purine ring, N1 and N7, respectively, to produce cyclic ADP-ribose (cADPR) and cyclic GDP-ribose, a fluorescent but inactive analog. Both enzymes can also catalyze the exchange of the nicotinamide group of NADP with nicotinic acid, producing yet another potent activator of Ca2+ mobilization, nicotinic acid adenine dinucleotide phosphate (NAADP). The Ca2+ release mechanism activated by NAADP is totally independent of cADPR and inositol trisphosphate indicating it is a novel and hitherto unknown Ca2+ signaling pathway. This article summarizes the current results on the structures and activities of cADPR, NAADP and the enzymes that catalyze their syntheses. A comprehensive model accounting for the novel multi-functionality of ADP-ribosyl cyclase and CD38 is presented.
Persistent Identifierhttp://hdl.handle.net/10722/132569
ISSN
2015 Impact Factor: 2.613
2015 SCImago Journal Rankings: 1.019
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorLee, HCen_HK
dc.contributor.authorMunshi, Cen_HK
dc.contributor.authorGraeff, Ren_HK
dc.date.accessioned2011-03-28T09:26:23Z-
dc.date.available2011-03-28T09:26:23Z-
dc.date.issued1999en_HK
dc.identifier.citationMolecular And Cellular Biochemistry, 1999, v. 193 n. 1-2, p. 89-98en_HK
dc.identifier.issn0300-8177en_HK
dc.identifier.urihttp://hdl.handle.net/10722/132569-
dc.description.abstractADP-ribosyl cyclase and CD38 are multi-functional enzymes involved in calcium signaling. Both can cyclize NAD and its guanine analog, NGD, at two different sites of the purine ring, N1 and N7, respectively, to produce cyclic ADP-ribose (cADPR) and cyclic GDP-ribose, a fluorescent but inactive analog. Both enzymes can also catalyze the exchange of the nicotinamide group of NADP with nicotinic acid, producing yet another potent activator of Ca2+ mobilization, nicotinic acid adenine dinucleotide phosphate (NAADP). The Ca2+ release mechanism activated by NAADP is totally independent of cADPR and inositol trisphosphate indicating it is a novel and hitherto unknown Ca2+ signaling pathway. This article summarizes the current results on the structures and activities of cADPR, NAADP and the enzymes that catalyze their syntheses. A comprehensive model accounting for the novel multi-functionality of ADP-ribosyl cyclase and CD38 is presented.en_HK
dc.languageengen_US
dc.publisherSpringer New York LLC. The Journal's web site is located at http://springerlink.metapress.com/openurl.asp?genre=journal&issn=0300-8177en_HK
dc.relation.ispartofMolecular and Cellular Biochemistryen_HK
dc.subjectCa2+en_HK
dc.subjectCyclic ADP-ribose (cADPR)en_HK
dc.subjectNicotinic acid adenine dinucleotide phosphate (NAADP)en_HK
dc.titleStructures and activities of cyclic ADP-ribose, NAADP and their metabolic enzymesen_HK
dc.typeArticleen_HK
dc.identifier.emailLee, HC: leehc@hku.hken_HK
dc.identifier.emailGraeff, R: graeffr@hku.hken_HK
dc.identifier.authorityLee, HC=rp00545en_HK
dc.identifier.authorityGraeff, R=rp01464en_HK
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.pmid10331643-
dc.identifier.scopuseid_2-s2.0-0032945168en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0032945168&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume193en_HK
dc.identifier.issue1-2en_HK
dc.identifier.spage89en_HK
dc.identifier.epage98en_HK
dc.identifier.isiWOS:000079986300014-
dc.publisher.placeUnited Statesen_HK
dc.identifier.scopusauthoridLee, HC=26642959100en_HK
dc.identifier.scopusauthoridMunshi, C=7003972383en_HK
dc.identifier.scopusauthoridGraeff, R=7003614053en_HK

Export via OAI-PMH Interface in XML Formats


OR


Export to Other Non-XML Formats