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dc.contributor.authorRuiz-Arias, Álvaro
dc.contributor.authorJurado Palomares, Rocío 
dc.contributor.authorFueyo González, Francisco
dc.contributor.authorHerranz, Rosario
dc.contributor.authorGálvez Rodríguez, Natividad 
dc.contributor.authorGonzález Vera, Juan Antonio 
dc.contributor.authorOrte Gutiérrez, Ángel 
dc.date.accessioned2021-11-24T11:59:22Z
dc.date.available2021-11-24T11:59:22Z
dc.date.issued2022-01-01
dc.identifier.citationRuiz-Arias, Á., Jurado, R., Fueyo-González, F., Herranz, R., Gálvez, N., González-Vera, J. A., & Orte, A. (2022). A FRET pair for quantitative and superresolution imaging of amyloid fibril formation. Sensors and Actuators B: Chemical, 350, 130882. [https://doi.org/10.1016/j.snb.2021.130882]es_ES
dc.identifier.urihttp://hdl.handle.net/10481/71723
dc.descriptionThis work was supported by grant CTQ2017–85658-R funded by MCIN/AEI/10.13039/501100011033/ FEDER “Una manera de hacer Europa”, and grants PID2019–104366RB-C22 and PID2020–114256RB-I00 funded by MCIN/AEI/10.13039/501100011033 . Funding for open access charge: Universidad de Granada / CBUA. We acknowledge the Centro de Instrumentación Científica (CIC) of Universidad de Granada for use of the TEM facilities. Á.R.-A. thanks the Spanish Ministerio de Educación y Formación Profesional for a FPU Ph.D. studentship.es_ES
dc.description.abstractThe presence of neuritic plaques and amyloid fibrils arising from the misfolding of certain proteins is the principal molecular indicator of neurodegenerative diseases such as Alzheimer's and Parkinson's disease. Methodologies for studying the early stages of amyloid aggregation are rapidly arising to provide a better understanding of the mechanism of fibrillization and cytotoxicity and to identify potential targets for diagnosis and therapy. The method presented here involves the simultaneous use of two different fluorophores, a quinolimide derivative and Nile Blue A. These are capable of interacting with and reporting on the formation of preamyloid aggregates and fibrils of apoferritin through fluorescence resonance energy transfer (FRET), which occurs between them, thus maximizing the contrast in detection and quantitative information of such amyloid species by using multidimensional fluorescence lifetime imaging microscopy (FLIM).es_ES
dc.description.sponsorshipCBUAes_ES
dc.description.sponsorshipSpanish Ministerio de Educación y Formaciónes_ES
dc.description.sponsorshipUniversidad de Granadaes_ES
dc.description.sponsorshipEuropean Regional Development Fund 104366RB-C22, 114256RB-I00, MCIN/AEI/10.13039/501100011033, PID2019, PID2019–104366RB-C22, PID2020, PID2020–114256RB-I00es_ES
dc.language.isoenges_ES
dc.publisherElsevieres_ES
dc.rightsAtribución-NoComercial-SinDerivadas 3.0 España*
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/3.0/es/*
dc.subjectAmyloid fibrilses_ES
dc.subjectProtein aggregationes_ES
dc.subjectSolvatochromic dyeses_ES
dc.subjectBiomarkerses_ES
dc.subjectFLIMes_ES
dc.subjectSTED microscopyes_ES
dc.titleA FRET pair for quantitative and superresolution imaging of amyloid fibril formationes_ES
dc.typeinfo:eu-repo/semantics/articlees_ES
dc.rights.accessRightsinfo:eu-repo/semantics/openAccesses_ES
dc.identifier.doi10.1016/j.snb.2021.130882
dc.type.hasVersioninfo:eu-repo/semantics/publishedVersiones_ES


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