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dc.contributor.authorDoñate Macián, Pau
dc.contributor.authorÁlvarez Marimon, Elena
dc.contributor.authorSepulcre Sánchez, Francesc
dc.contributor.authorVázquez Ibar, José Luis
dc.contributor.authorPeralvarez Marin, Alex
dc.contributor.otherUniversitat Politècnica de Catalunya. Departament d'Enginyeria Agroalimentària i Biotecnologia
dc.date.accessioned2020-03-19T08:11:51Z
dc.date.available2020-03-19T08:11:51Z
dc.date.issued2019-02-05
dc.identifier.citationDoñate, P. [et al.]. The Membrane proximal domain of TRPV1 and TRPV2 channels mediates protein-protein interactions and lipid binding in vitro. "International journal of molecular sciences", 5 Febrer 2019, vol. 20, p. 1-11.
dc.identifier.issn1422-0067
dc.identifier.urihttp://hdl.handle.net/2117/180468
dc.description.abstractConstitutive or regulated membrane protein trafficking is a key cell biology process.Transient receptor potential channels are somatosensory proteins in charge of detecting severalphysical and chemical stimuli, thus requiring fine vesicular trafficking. The membrane proximalor pre-S1 domain (MPD) is a highly conserved domain in transient receptor potential channels from the vanilloid (TRPV) subfamily.
dc.format.extent11 p.
dc.language.isoeng
dc.rightsAttribution-NonCommercial-NoDerivs 3.0 Spain
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/3.0/es/
dc.subjectÀrees temàtiques de la UPC::Enginyeria agroalimentària::Ciències de la terra i de la vida::Microbiologia
dc.subject.lcshMembranes (Biology)--Research.
dc.subject.otherTransient Receptor Potential (TRP) channels
dc.subject.otherExocytosis
dc.subject.otherBiophysics
dc.subject.otherProtein–proteininteractions
dc.subject.otherLipid-protein interactions
dc.subject.otherAgrotech
dc.titleThe Membrane proximal domain of TRPV1 and TRPV2 channels mediates protein-protein interactions and lipid binding in vitro
dc.typeArticle
dc.subject.lemacProteïnes -- Investigació
dc.contributor.groupUniversitat Politècnica de Catalunya. GINEMQUAL - Gestió Integrada de Nematodes Fitoparàsits i dels Efectes sobre el Rendiment i Qualitat de la Collita
dc.identifier.doi10.3390/ijms20030682
dc.rights.accessOpen Access
local.identifier.drac23950355
dc.description.versionPostprint (published version)
dc.relation.projectidinfo:eu-repo/grantAgreement/EC/FP7/237120/EU/Single Particle Cryo-Electron Microscopy and Biophysical Characterization of Transient Receptor Potential Vanilloid 2 channel: a Three-Dimensional Structure Characterization of a Membrane Nociceptor./PAIN_TRPV2
dc.relation.projectidinfo:eu-repo/grantAgreement/EC/H2020/721385/EU/European Training Network for the sustainable, zero-waste valorisation of (critical) metal containing industrial process residues/SOCRATES
dc.relation.projectidinfo:eu-repo/grantAgreement/EC/FP7/237120/EU/Single Particle Cryo-Electron Microscopy and Biophysical Characterization of Transient Receptor Potential Vanilloid 2 channel: a Three-Dimensional Structure Characterization of a Membrane Nociceptor./PAIN_TRPV2
dc.relation.projectidinfo:eu-repo/grantAgreement/MICINN//SAF2010-21385/ES/RELACION ESTRUCTURA-FUNCION DEL CANAL IONICO TRPV2 Y SUS IMPLICACIONES EN TERMOCEPCION./
dc.relation.projectidinfo:eu-repo/grantAgreement/MICINN/BFU2017-87843
dc.relation.projectidinfo:eu-repo/grantAgreement/EC/FP7/115004/EU/Pharmacoepidemiolocal Research on Outcomes of Therapeutics by a European ConsorTium/PROTECT
local.citation.authorDoñate, P.; Álvarez, E.; Sepulcre, F.; Vázquez, J.; Peralvarez, A.
local.citation.publicationNameInternational journal of molecular sciences
local.citation.volume20
local.citation.startingPage1
local.citation.endingPage11


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