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000909074 1001_ $$0P:(DE-Juel1)177730$$aBlömeke, Lara$$b0
000909074 245__ $$aQuantitative detection of α-Synuclein and Tau oligomers and other aggregates by digital single particle counting
000909074 260__ $$aLondon [u.a.]$$bNature Publ. Group$$c2022
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000909074 520__ $$aThe pathological hallmark of neurodegenerative diseases is the formation of toxic oligomers by proteins such as alpha-synuclein (aSyn) or microtubule-associated protein tau (Tau). Consequently, such oligomers are promising biomarker candidates for diagnostics as well as drug development. However, measuring oligomers and other aggregates in human biofluids is still challenging as extreme sensitivity and specificity are required. We previously developed surface-based fluorescence intensity distribution analysis (sFIDA) featuring single-particle sensitivity and absolute specificity for aggregates. In this work, we measured aSyn and Tau aggregate concentrations of 237 cerebrospinal fluid (CSF) samples from five cohorts: Parkinson's disease (PD), dementia with Lewy bodies (DLB), Alzheimer's disease (AD), progressive supranuclear palsy (PSP), and a neurologically-normal control group. aSyn aggregate concentration discriminates PD and DLB patients from normal controls (sensitivity 73%, specificity 65%, area under the receiver operating curve (AUC) 0.68). Tau aggregates were significantly elevated in PSP patients compared to all other groups (sensitivity 87%, specificity 70%, AUC 0.76). Further, we found a tight correlation between aSyn and Tau aggregate titers among all patient cohorts (Pearson coefficient of correlation r = 0.81). Our results demonstrate that aSyn and Tau aggregate concentrations measured by sFIDA differentiate neurodegenerative disease diagnostic groups. Moreover, sFIDA-based Tau aggregate measurements might be particularly useful in distinguishing PSP from other parkinsonisms. Finally, our findings suggest that sFIDA can improve pre-clinical and clinical studies by identifying those individuals that will most likely respond to compounds designed to eliminate specific oligomers or to prevent their formation.
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000909074 7001_ $$0P:(DE-Juel1)171619$$aPils, Marlene$$b1
000909074 7001_ $$0P:(DE-Juel1)172001$$aKraemer-Schulien, Victoria$$b2
000909074 7001_ $$0P:(DE-HGF)0$$aDybala, Alexandra$$b3
000909074 7001_ $$0P:(DE-Juel1)176527$$aSchaffrath, Anja$$b4
000909074 7001_ $$0P:(DE-Juel1)162310$$aKulawik, Andreas$$b5
000909074 7001_ $$0P:(DE-Juel1)190725$$aRehn, Fabian$$b6
000909074 7001_ $$0P:(DE-Juel1)139572$$aCousin, Anneliese$$b7
000909074 7001_ $$0P:(DE-Juel1)157638$$aNischwitz, Volker$$b8
000909074 7001_ $$0P:(DE-Juel1)159192$$aWillbold, Johannes$$b9
000909074 7001_ $$0P:(DE-HGF)0$$aZack, Rebecca$$b10
000909074 7001_ $$0P:(DE-HGF)0$$aTropea, Thomas F.$$b11
000909074 7001_ $$0P:(DE-Juel1)162212$$aBujnicki, Tuyen$$b12
000909074 7001_ $$0P:(DE-Juel1)177986$$aTamgüney, Gültekin$$b13
000909074 7001_ $$0P:(DE-HGF)0$$aWeintraub, Daniel$$b14
000909074 7001_ $$0P:(DE-HGF)0$$aIrwin, David$$b15
000909074 7001_ $$0P:(DE-HGF)0$$aGrossman, Murray$$b16
000909074 7001_ $$0P:(DE-HGF)0$$aWolk, David A.$$b17
000909074 7001_ $$0P:(DE-HGF)0$$aTrojanowski, John Q.$$b18
000909074 7001_ $$0P:(DE-Juel1)157832$$aBannach, Oliver$$b19
000909074 7001_ $$0P:(DE-HGF)0$$aChen-Plotkin, Alice$$b20
000909074 7001_ $$0P:(DE-Juel1)132029$$aWillbold, Dieter$$b21$$eCorresponding author
000909074 773__ $$0PERI:(DE-600)2819218-7$$a10.1038/s41531-022-00330-x$$gVol. 8, no. 1, p. 68$$n1$$p68$$tnpj Parkinson's Disease$$v8$$x2373-8057$$y2022
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