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Article: Cyclic ADP-ribose: A new member of a super family of signalling cyclic nucleotides

TitleCyclic ADP-ribose: A new member of a super family of signalling cyclic nucleotides
Authors
Issue Date1994
PublisherElsevier Inc. The Journal's web site is located at http://www.elsevier.com/locate/cellsig
Citation
Cellular Signalling, 1994, v. 6 n. 6, p. 591-600 How to Cite?
AbstractCyclic nucleotides are second messengers exerting their cellular effects mainly through protein phosphorylation, A new member of this family, cyclic ADP-ribose, is involved, instead, in mediating mobilization of Ca2+ from internal stores. The structure of this nucleotide has now been determined by X-ray crystallography and accumulating evidence indicates it may be an endogenous modulator of the Ca2+ induced Ca+2 release mechanism. This article summarizes the current knowledge of the structure, the mechanism of action and the metabolic enzymes of this novel nucleotide. With this new addition, the signalling functions of the cyclic nucleotide family are now extended from protein phosphorylation to Ca2+ signalling.
Persistent Identifierhttp://hdl.handle.net/10722/171602
ISSN
2015 Impact Factor: 4.191
2015 SCImago Journal Rankings: 2.289
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorLee, HCen_US
dc.date.accessioned2012-10-30T06:15:55Z-
dc.date.available2012-10-30T06:15:55Z-
dc.date.issued1994en_US
dc.identifier.citationCellular Signalling, 1994, v. 6 n. 6, p. 591-600en_US
dc.identifier.issn0898-6568en_US
dc.identifier.urihttp://hdl.handle.net/10722/171602-
dc.description.abstractCyclic nucleotides are second messengers exerting their cellular effects mainly through protein phosphorylation, A new member of this family, cyclic ADP-ribose, is involved, instead, in mediating mobilization of Ca2+ from internal stores. The structure of this nucleotide has now been determined by X-ray crystallography and accumulating evidence indicates it may be an endogenous modulator of the Ca2+ induced Ca+2 release mechanism. This article summarizes the current knowledge of the structure, the mechanism of action and the metabolic enzymes of this novel nucleotide. With this new addition, the signalling functions of the cyclic nucleotide family are now extended from protein phosphorylation to Ca2+ signalling.en_US
dc.languageengen_US
dc.publisherElsevier Inc. The Journal's web site is located at http://www.elsevier.com/locate/cellsigen_US
dc.relation.ispartofCellular Signallingen_US
dc.subject.meshAdenosine Diphosphate Ribose - Analogs & Derivatives - Chemistry - Physiologyen_US
dc.subject.meshAnimalsen_US
dc.subject.meshCalcium - Metabolismen_US
dc.subject.meshCyclic Adp-Riboseen_US
dc.subject.meshHumansen_US
dc.subject.meshNucleotides, Cyclic - Physiologyen_US
dc.subject.meshPhosphorylationen_US
dc.subject.meshSecond Messenger Systemsen_US
dc.subject.meshSignal Transduction - Physiologyen_US
dc.subject.meshStructure-Activity Relationshipen_US
dc.titleCyclic ADP-ribose: A new member of a super family of signalling cyclic nucleotidesen_US
dc.typeArticleen_US
dc.identifier.emailLee, HC:leehc@hku.hken_US
dc.identifier.authorityLee, HC=rp00545en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.doi10.1016/0898-6568(94)90042-6en_US
dc.identifier.pmid7857763-
dc.identifier.scopuseid_2-s2.0-0028080275en_US
dc.identifier.volume6en_US
dc.identifier.issue6en_US
dc.identifier.spage591en_US
dc.identifier.epage600en_US
dc.identifier.isiWOS:A1994PQ56500002-
dc.publisher.placeUnited Statesen_US
dc.identifier.scopusauthoridLee, HC=26642959100en_US

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