000075425 001__ 75425
000075425 005__ 20200221144305.0
000075425 0247_ $$2doi$$a10.1021/acschemneuro.5b00324
000075425 0248_ $$2sideral$$a107780
000075425 037__ $$aART-2016-107780
000075425 041__ $$aeng
000075425 100__ $$aHorrocks, M.H.
000075425 245__ $$aSingle-molecule imaging of individual amyloid protein aggregates in human biofluids
000075425 260__ $$c2016
000075425 5060_ $$aAccess copy available to the general public$$fUnrestricted
000075425 5203_ $$aThe misfolding and aggregation of proteins into amyloid fibrils characterizes many neurodegenerative disorders such as Parkinson’s and Alzheimer’s diseases. We report here a method, termed SAVE (single aggregate visualization by enhancement) imaging, for the ultrasensitive detection of individual amyloid fibrils and oligomers using single-molecule fluorescence microscopy. We demonstrate that this method is able to detect the presence of amyloid aggregates of a-synuclein, tau, and amyloid-ß. In addition, we show that aggregates can also be identified in human cerebrospinal fluid (CSF). Significantly, we see a twofold increase in the average aggregate concentration in CSF from Parkinson’s disease patients compared to age-matched controls. Taken together, we conclude that this method provides an opportunity to characterize the structural nature of amyloid aggregates in a key biofluid, and therefore has the potential to study disease progression in both animal models and humans to enhance our understanding of neurodegenerative disorders.
000075425 540__ $$9info:eu-repo/semantics/openAccess$$aby$$uhttp://creativecommons.org/licenses/by/3.0/es/
000075425 590__ $$a3.883$$b2016
000075425 591__ $$aCHEMISTRY, MEDICINAL$$b7 / 60 = 0.117$$c2016$$dQ1$$eT1
000075425 591__ $$aNEUROSCIENCES$$b72 / 258 = 0.279$$c2016$$dQ2$$eT1
000075425 591__ $$aBIOCHEMISTRY & MOLECULAR BIOLOGY$$b85 / 287 = 0.296$$c2016$$dQ2$$eT1
000075425 592__ $$a1.538$$b2016
000075425 593__ $$aMedicine (miscellaneous)$$c2016$$dQ1
000075425 593__ $$aBiochemistry$$c2016$$dQ1
000075425 593__ $$aPhysiology$$c2016$$dQ1
000075425 593__ $$aCell Biology$$c2016$$dQ2
000075425 593__ $$aCognitive Neuroscience$$c2016$$dQ2
000075425 655_4 $$ainfo:eu-repo/semantics/article$$vinfo:eu-repo/semantics/publishedVersion
000075425 700__ $$aLee, S.F.
000075425 700__ $$aGandhi, S.
000075425 700__ $$aMagdalinou, N.K.
000075425 700__ $$aChen, S.W.
000075425 700__ $$aDevine, M.J.
000075425 700__ $$aTosatto, L.
000075425 700__ $$aKjaergaard, M.
000075425 700__ $$aBeckwith, J.S.
000075425 700__ $$aZetterberg, H.
000075425 700__ $$aIljina, M.
000075425 700__ $$0(orcid)0000-0002-9138-6687$$aCremades, N.$$uUniversidad de Zaragoza
000075425 700__ $$aDobson, C.M.
000075425 700__ $$aWood, N.W.
000075425 700__ $$aKlenerman, D.
000075425 7102_ $$11002$$2060$$aUniversidad de Zaragoza$$bDpto. Bioq.Biolog.Mol. Celular$$cÁrea Bioquímica y Biolog.Mole.
000075425 773__ $$g7, 3 (2016), 399-406$$pACS CHEMICAL NEUROSCIENCE$$tACS CHEMICAL NEUROSCIENCE$$x1948-7193
000075425 8564_ $$s3247542$$uhttps://zaguan.unizar.es/record/75425/files/texto_completo.pdf$$yVersión publicada
000075425 8564_ $$s111073$$uhttps://zaguan.unizar.es/record/75425/files/texto_completo.jpg?subformat=icon$$xicon$$yVersión publicada
000075425 909CO $$ooai:zaguan.unizar.es:75425$$particulos$$pdriver
000075425 951__ $$a2020-02-21-13:34:35
000075425 980__ $$aARTICLE