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dc.contributor.authorRichmond, Gregory S.
dc.contributor.authorSmith, Terry K.
dc.date.accessioned2011-03-23T11:31:03Z
dc.date.available2011-03-23T11:31:03Z
dc.date.issued2011-01
dc.identifier.citationRichmond , G S & Smith , T K 2011 , ' Phospholipases A 1 ' , International Journal of Molecular Sciences , vol. 12 , no. 1 , pp. 588-612 . https://doi.org/10.3390/ijms12010588en
dc.identifier.issn1422-0067
dc.identifier.otherPURE: 6247546
dc.identifier.otherPURE UUID: 4e501b9b-7a20-42dd-97aa-189005c58753
dc.identifier.otherWOS: 000286583400031
dc.identifier.otherScopus: 79251649500
dc.identifier.urihttp://hdl.handle.net/10023/1708
dc.descriptionResearch in the author's laboratory is supported in part by a Wellcome Trust Senior Research Fellowship (067441), and Wellcome Trust project grants (086658 and 093228) and a Wellcome Trust Prize Studentship (G.S.R).en
dc.description.abstractPhospholipase A1 (PLA1) is an enzyme that hydrolyzes phospholipids and produces 2-acyl-lysophospholipids and fatty acids. This lipolytic activity is conserved in a wide range of organisms but is carried out by a diverse set of PLA1 enzymes. Where their function is known, PLA1s have been shown to act as digestive enzymes, possess central roles in membrane maintenance and remodeling, or regulate important cellular mechanisms by the production of various lysophospholipid mediators, such as lysophosphatidylserine and lysophosphatidic acid, which in turn have multiple biological functions.
dc.format.extent25
dc.language.isoeng
dc.relation.ispartofInternational Journal of Molecular Sciencesen
dc.rights© 2011 by the authors; licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/3.0/).en
dc.subjectPhospholipase A(1)en
dc.subjectPhospholipiden
dc.subjectLysophospholipiden
dc.subjectMammalian sec23p-interacting proteinen
dc.subjectPlatelet-activating-factoren
dc.subjectPig heart microsomesen
dc.subjectLipase gene familyen
dc.subjectPhosphatidic-aciden
dc.subjectArachidonic-aciden
dc.subjectTrypanosoma-bruceien
dc.subjectEscherichia-colien
dc.subjectBovine brainen
dc.subjectGuinea-pigen
dc.subjectQH426 Geneticsen
dc.subject.lccQH426en
dc.titlePhospholipases A1en
dc.typeJournal itemen
dc.description.versionPublisher PDFen
dc.contributor.institutionUniversity of St Andrews.School of Biologyen
dc.contributor.institutionUniversity of St Andrews.Biomedical Sciences Research Complexen
dc.identifier.doihttps://doi.org/10.3390/ijms12010588
dc.description.statusPeer revieweden


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