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Human erythrocyte acetylcholinesterase in health and disease

dc.contributor.authorSaldanha, Carlota
dc.date.accessioned2018-07-30T11:33:46Z
dc.date.available2018-07-30T11:33:46Z
dc.date.issued2017
dc.description© 2017 by the author. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).pt_PT
dc.description.abstractThe biochemical properties of erythrocyte or human red blood cell (RBC) membrane acetylcholinesterase (AChE) and its applications on laboratory class and on research are reviewed. Evidence of the biochemical and the pathophysiological properties like the association between the RBC AChE enzyme activity and the clinical and biophysical parameters implicated in several diseases are overviewed, and the achievement of RBC AChE as a biomarker and as a prognostic factor are presented. Beyond its function as an enzyme, a special focus is highlighted in this review for a new function of the RBC AChE, namely a component of the signal transduction pathway of nitric oxide.pt_PT
dc.description.sponsorshipThis work was funded by Fundação para a Ciência e Tecnologia: LISBOA-01-0145-FEDER-007391, project cofunded by FEDER, through POR Lisboa 2020—Programa Operacional Regional de Lisboa, PORTUGAL 2020.pt_PT
dc.description.versioninfo:eu-repo/semantics/publishedVersionpt_PT
dc.identifier.citation2017; pii: E1499pt_PT
dc.identifier.doi10.3390/molecules22091499pt_PT
dc.identifier.issn1420-3049
dc.identifier.urihttp://hdl.handle.net/10451/34383
dc.language.isoengpt_PT
dc.peerreviewedyespt_PT
dc.publisherMDPIpt_PT
dc.relationLISBOA-01-0145-FEDER-007391pt_PT
dc.relation.publisherversionhttp://www.mdpi.com/journal/moleculespt_PT
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/pt_PT
dc.subjectAcetylcholinesterasept_PT
dc.subjectRred blood cellspt_PT
dc.subjectNitric oxidept_PT
dc.titleHuman erythrocyte acetylcholinesterase in health and diseasept_PT
dc.typejournal article
dspace.entity.typePublication
oaire.citation.endPage2017 Sep 8;22(9). pii: E1499pt_PT
oaire.citation.issue9pt_PT
oaire.citation.startPageE1499pt_PT
oaire.citation.titleMoleculespt_PT
oaire.citation.volume22pt_PT
rcaap.rightsopenAccesspt_PT
rcaap.typearticlept_PT

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