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- Publisher Website: 10.1515/BC.1999.098
- Scopus: eid_2-s2.0-0032830476
- PMID: 10494827
- WOS: WOS:000082438200008
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Article: A unified mechanism of enzymatic synthesis of two calcium messengers: Cyclic ADP-ribose and NAADP
Title | A unified mechanism of enzymatic synthesis of two calcium messengers: Cyclic ADP-ribose and NAADP |
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Authors | |
Keywords | ADP-ribosyl cyclase Calcium signaling CD38 Cyclic ADP-ribose NAADP X-ray crystallography |
Issue Date | 1999 |
Publisher | Walter de Gruyter GmbH & Co KG. The Journal's web site is located at http://www.degruyter.de/journals/bc |
Citation | Biological Chemistry, 1999, v. 380 n. 7-8, p. 785-793 How to Cite? |
Abstract | Cyclic ADP-ribose (cADPR) and nicotinic acid adenine dinucleotide phosphate (NAADP) mobilize Ca2+ from two different types of intracellular stores and through completely independent mechanisms. The two Ca2+ messengers are also structurally distinct. cADPR is a cyclic nucleotide derived from NAD, while NAADP is a linear metabolite of NADP. Systems responsive to these two novel signaling molecules are widespread among eukaryotes and include protozoan, plant, invertebrate, mammalian as well as human cells. Despite their functional and structural differences, cADPR and NAADP are sibling messengers synthesized by a single enzyme, ADP-ribosyl cyclase. In this article the recent progress in understanding the physiological roles of cADPR and NAADP is briefly reviewed. A unified mechanism of catalysis is also proposed, which takes into consideration the crystallographic structure of ADP-ribosyl cyclase and accounts for its novel multi-functionality. |
Persistent Identifier | http://hdl.handle.net/10722/171665 |
ISSN | 2023 Impact Factor: 2.9 2023 SCImago Journal Rankings: 1.172 |
ISI Accession Number ID | |
References |
DC Field | Value | Language |
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dc.contributor.author | Lee, HC | en_US |
dc.date.accessioned | 2012-10-30T06:16:14Z | - |
dc.date.available | 2012-10-30T06:16:14Z | - |
dc.date.issued | 1999 | en_US |
dc.identifier.citation | Biological Chemistry, 1999, v. 380 n. 7-8, p. 785-793 | en_US |
dc.identifier.issn | 1431-6730 | en_US |
dc.identifier.uri | http://hdl.handle.net/10722/171665 | - |
dc.description.abstract | Cyclic ADP-ribose (cADPR) and nicotinic acid adenine dinucleotide phosphate (NAADP) mobilize Ca2+ from two different types of intracellular stores and through completely independent mechanisms. The two Ca2+ messengers are also structurally distinct. cADPR is a cyclic nucleotide derived from NAD, while NAADP is a linear metabolite of NADP. Systems responsive to these two novel signaling molecules are widespread among eukaryotes and include protozoan, plant, invertebrate, mammalian as well as human cells. Despite their functional and structural differences, cADPR and NAADP are sibling messengers synthesized by a single enzyme, ADP-ribosyl cyclase. In this article the recent progress in understanding the physiological roles of cADPR and NAADP is briefly reviewed. A unified mechanism of catalysis is also proposed, which takes into consideration the crystallographic structure of ADP-ribosyl cyclase and accounts for its novel multi-functionality. | en_US |
dc.language | eng | en_US |
dc.publisher | Walter de Gruyter GmbH & Co KG. The Journal's web site is located at http://www.degruyter.de/journals/bc | en_US |
dc.relation.ispartof | Biological Chemistry | en_US |
dc.subject | ADP-ribosyl cyclase | - |
dc.subject | Calcium signaling | - |
dc.subject | CD38 | - |
dc.subject | Cyclic ADP-ribose | - |
dc.subject | NAADP | - |
dc.subject | X-ray crystallography | - |
dc.subject.mesh | Adp-Ribosyl Cyclase | en_US |
dc.subject.mesh | Adenosine Diphosphate Ribose - Analogs & Derivatives - Biosynthesis - Chemistry - Physiology | en_US |
dc.subject.mesh | Animals | en_US |
dc.subject.mesh | Antigens, Cd | en_US |
dc.subject.mesh | Antigens, Cd38 | en_US |
dc.subject.mesh | Antigens, Differentiation - Metabolism | en_US |
dc.subject.mesh | Calcium - Metabolism | en_US |
dc.subject.mesh | Catalysis | en_US |
dc.subject.mesh | Cyclic Adp-Ribose | en_US |
dc.subject.mesh | Humans | en_US |
dc.subject.mesh | Membrane Glycoproteins | en_US |
dc.subject.mesh | Molecular Structure | en_US |
dc.subject.mesh | Nad+ Nucleosidase - Metabolism | en_US |
dc.subject.mesh | Nadp - Analogs & Derivatives - Biosynthesis - Chemistry - Physiology | en_US |
dc.title | A unified mechanism of enzymatic synthesis of two calcium messengers: Cyclic ADP-ribose and NAADP | en_US |
dc.type | Article | en_US |
dc.identifier.email | Lee, HC:leehc@hku.hk | en_US |
dc.identifier.authority | Lee, HC=rp00545 | en_US |
dc.description.nature | link_to_subscribed_fulltext | en_US |
dc.identifier.doi | 10.1515/BC.1999.098 | en_US |
dc.identifier.pmid | 10494827 | - |
dc.identifier.scopus | eid_2-s2.0-0032830476 | en_US |
dc.relation.references | http://www.scopus.com/mlt/select.url?eid=2-s2.0-0032830476&selection=ref&src=s&origin=recordpage | en_US |
dc.identifier.volume | 380 | en_US |
dc.identifier.issue | 7-8 | en_US |
dc.identifier.spage | 785 | en_US |
dc.identifier.epage | 793 | en_US |
dc.identifier.isi | WOS:000082438200008 | - |
dc.publisher.place | Germany | en_US |
dc.identifier.scopusauthorid | Lee, HC=26642959100 | en_US |
dc.identifier.issnl | 1431-6730 | - |