Please use this identifier to cite or link to this item: https://repositorio.uca.edu.ar/handle/123456789/8789
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dc.contributor.authorFantini, Jacqueses
dc.contributor.authorDi Scala, Coraliees
dc.contributor.authorBaier, Carlos J.es
dc.contributor.authorBarrantes, Francisco Josées
dc.date.accessioned2019-09-24T22:29:57Z-
dc.date.available2019-09-24T22:29:57Z-
dc.date.issued2016-
dc.identifier.citationFantini J, Di Scala C, Baier CJ, Barrantes FJ. Molecular mechanisms of protein-cholesterol interactions in plasma membranes : functional distinction between topological (tilted) and consensus (CARC/CRAC) domains [en línea]. Chemistry and Physics of Lipids. 2016;199:52-60. doi:10.1016/j.chemphyslip.2016.02.009 Disponible en: https://repositorio.uca.edu.ar/handle/123456789/8789es
dc.identifier.issn0009-3084 (impreso)-
dc.identifier.issn1873-2941 (online)-
dc.identifier.urihttps://repositorio.uca.edu.ar/handle/123456789/8789-
dc.description.abstractAbstract: The molecular mechanisms that control the multiple possible modes of protein association with membrane cholesterol are remarkably convergent. These mechanisms, which include hydrogen bonding, CH-π stacking and dispersion forces, are used by a wide variety of extracellular proteins (e.g. microbial or amyloid) and membrane receptors. Virus fusion peptides penetrate the membrane of host cells with a tilted orientation that is compatible with a transient interaction with cholesterol; this tilted orientation is also characteristic of the process of insertion of amyloid proteins that subsequently form oligomeric pores in the plasma membrane of brain cells. Membrane receptors that are associated with cholesterol generally display linear consensus binding motifs (CARC and CRAC) characterized by a triad of basic (Lys/Arg), aromatic (Tyr/phe) and aliphatic (Leu/Val) amino acid residues. In some cases, the presence of both CARC and CRAC within the same membrane-spanning domain allows the simultaneous binding of two cholesterol molecules, one in each membrane leaflet. In this review the molecular basis and the functional significance of the different modes of protein-cholesterol interactions in plasma membranes are discussed.es
dc.formatapplication/pdfes
dc.language.isoenges
dc.publisherElsevieres
dc.rightsAcceso abierto. 12 meses de embargo*
dc.rights.urihttp://creativecommons.org/licenses/by-nc-sa/4.0/*
dc.sourceChemistry and Physics of Lipids. 2016;199:52-60es
dc.subjectAMINOACIDOSes
dc.subjectCOLESTEROLes
dc.subjectLIPIDOSes
dc.subjectPROTEINASes
dc.subjectMEMBRANA CELULARes
dc.titleMolecular mechanisms of protein-cholesterol interactions in plasma membranes : functional distinction between topological (tilted) and consensus (CARC/CRAC) domainses
dc.typeArtículoes
dc.identifier.doi10.1016/j.chemphyslip.2016.02.009-
dc.identifier.pmid26987951-
uca.disciplinaMEDICINAes
uca.issnrd1es
uca.affiliationFil: Fantini, Jacques. Aix-Marseille Université. Interactions Moléculaires et Systèmes Membranaires; Franciaes
uca.affiliationFil: Di Scala, Coralie. Aix-Marseille Université. Interactions Moléculaires et Systèmes Membranaires; Franciaes
uca.affiliationFil: Baier, Carlos J. Pontificia Universidad Católica Argentina. Facultad de Ciencias Médicas. Instituto de Investigaciones Biomédicas. Laboratorio de Neurobiología Molecular; Argentinaes
uca.affiliationFil: Baier, Carlos J. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentinaes
uca.affiliationFil: Barrantes, Francisco José. Pontificia Universidad Católica Argentina. Facultad de Ciencias Médicas. Instituto de Investigaciones Biomédicas. Laboratorio de Neurobiología Molecular; Argentinaes
uca.affiliationFil: Barrantes, Francisco José. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentinaes
uca.versionacceptedVersiones
item.fulltextWith Fulltext-
item.grantfulltextopen-
item.languageiso639-1en-
crisitem.author.deptInstituto de Investigaciones Biomédicas - BIOMED-
crisitem.author.deptLaboratorio de Neurobiología Molecular-
crisitem.author.orcid0000-0002-4745-681X-
crisitem.author.parentorgFacultad de Ciencias Médicas-
crisitem.author.parentorgInstituto de Investigaciones Biomédicas - BIOMED-
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