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dc.contributor.authorHaney, C. M.en_US
dc.contributor.authorCleveland, C. L.en_US
dc.contributor.authorWissner, R. F.en_US
dc.contributor.authorOwei, L.en_US
dc.contributor.authorRobustelli, J.en_US
dc.contributor.authorDaniels, M. J.en_US
dc.contributor.authorCanyurt, M.en_US
dc.contributor.authorRodriguez, P.en_US
dc.contributor.authorIschiropoulos, H.en_US
dc.contributor.authorBaumgart, T.en_US
dc.contributor.authorPetersson, E. J.en_US
dc.date.accessioned2018-04-12T11:09:44Z
dc.date.available2018-04-12T11:09:44Z
dc.date.issued2017en_US
dc.identifier.issn0006-2960
dc.identifier.urihttp://hdl.handle.net/11693/37311
dc.description.abstractFibrillar aggregates of the protein α-synuclein (αS) are one of the hallmarks of Parkinson’s disease. Here, we show that measuring the fluorescence polarization (FP) of labels at several sites on αS allows one to monitor changes in the local dynamics of the protein after binding to micelles or vesicles, and during fibril formation. Most significantly, these site-specific FP measurements provide insight into structural remodeling of αS fibrils by small molecules and have the potential for use in moderate-throughput screens to identify small molecules that could be used to treat Parkinson’s disease. © 2016 American Chemical Society.en_US
dc.language.isoEnglishen_US
dc.source.titleBiochemistryen_US
dc.relation.isversionofhttp://dx.doi.org/10.1021/acs.biochem.6b01060en_US
dc.subjectBinding sitesen_US
dc.subjectFluorescenceen_US
dc.subjectPolarizationen_US
dc.subjectProteinsen_US
dc.subjectDisaggregationen_US
dc.subjectFibril formationen_US
dc.subjectFibrillar aggregatesen_US
dc.subjectFluorescence polarizationen_US
dc.subjectLocal dynamicsen_US
dc.subjectSite-specificen_US
dc.subjectSmall moleculesen_US
dc.subjectStructural remodelingen_US
dc.subjectMoleculesen_US
dc.subjectPolyphenol derivativeen_US
dc.subjectDodecyl sulfate sodiumen_US
dc.subjectEpigallocatechin gallateen_US
dc.subjectFluorescent dyeen_US
dc.subjectLiposomeen_US
dc.subjectNordihydroguaiaretic aciden_US
dc.subjectTexas reden_US
dc.subjectXanthene derivativeen_US
dc.subjectConformational transitionen_US
dc.subjectMicelleen_US
dc.subjectMolecular interactionen_US
dc.subjectPriority journalen_US
dc.subjectProtein bindingen_US
dc.subjectAnalogs and derivativesen_US
dc.subjectChemistryen_US
dc.subjectDdrug effectsen_US
dc.subjectHumanen_US
dc.subjectMetabolismen_US
dc.subjectMolecular libraryen_US
dc.subjectPharmacologyen_US
dc.subjectCatechinen_US
dc.subjectDopamineen_US
dc.subjectMasoprocolen_US
dc.subjectPhosphatidylcholinesen_US
dc.subjectProtein aggregatesen_US
dc.subjectRecombinant proteinsen_US
dc.subjectSodium dodecyl sulfateen_US
dc.subjectUnilamellar liposomesen_US
dc.subjectXanthenesen_US
dc.titleSite-specific fluorescence polarization for studying the disaggregation of α-synuclein fibrils by small moleculesen_US
dc.typeArticleen_US
dc.departmentDepartment of Chemistry
dc.citation.spage683en_US
dc.citation.epage691en_US
dc.citation.volumeNumber56en_US
dc.citation.issueNumber5en_US
dc.identifier.doi10.1021/acs.biochem.6b01060en_US
dc.publisherAmerican Chemical Societyen_US


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