000165615 001__ 165615
000165615 005__ 20230908114821.0
000165615 020__ $$a978-1-0716-2596-5 (print)
000165615 020__ $$a978-1-0716-2597-2 (electronic)
000165615 0247_ $$2doi$$a10.1007/978-1-0716-2597-2_15
000165615 0247_ $$2pmid$$apmid:36310206
000165615 0247_ $$2ISSN$$a1064-3745
000165615 0247_ $$2ISSN$$a1940-6029
000165615 0247_ $$2altmetric$$aaltmetric:137888235
000165615 037__ $$aDZNE-2022-01748
000165615 041__ $$aEnglish
000165615 082__ $$a570
000165615 1001_ $$0P:(DE-2719)2812812$$aHochmair, Janine$$b0$$eFirst author$$udzne
000165615 245__ $$aLight Microscopy and Dynamic Light Scattering to Study Liquid-Liquid Phase Separation of Tau Proteins In Vitro.
000165615 260__ $$aNew York, NY$$bSpringer US$$c2023
000165615 29510 $$aProtein Aggregation / Cieplak, Andrzej Stanisław (Editor) ; New York, NY : Springer US, 2023, Chapter 15 ; ISSN: 1064-3745=1940-6029 ; ISBN: 978-1-0716-2596-5=978-1-0716-2597-2 ; doi:10.1007/978-1-0716-2597-2
000165615 300__ $$a225 - 243
000165615 3367_ $$2ORCID$$aBOOK_CHAPTER
000165615 3367_ $$07$$2EndNote$$aBook Section
000165615 3367_ $$2DRIVER$$abookPart
000165615 3367_ $$2BibTeX$$aINBOOK
000165615 3367_ $$2DataCite$$aOutput Types/Book chapter
000165615 3367_ $$0PUB:(DE-HGF)7$$2PUB:(DE-HGF)$$aContribution to a book$$bcontb$$mcontb$$s1694166467_31830
000165615 4900_ $$aMethods in Molecular Biology$$v2551
000165615 520__ $$aTau is an intrinsically disordered protein that binds and stabilizes axonal microtubules (MTs) in neurons of the central nervous system. The binding of Tau to MTs is mediated by its repeat domain and flanking proline-rich domains. The positively charged (basic) C-terminal half of Tau also mediates the assembly Tau into fibrillar aggregates in Alzheimer's disease (AD) and tauopathy brains. In recent years, another assembly form of Tau has been identified: Tau can undergo liquid-liquid phase separation (LLPS), which leads to its condensation into liquid-dense phases, either by complex coacervation with polyanions like heparin or RNA or through 'self-coacervation' at high Tau concentrations. Condensation of Tau in the absence of polyanions can be enhanced by the presence of molecular crowding agents in a dilute Tau solution. In vitro experiments using recombinant purified Tau are helpful to study the physicochemical determinants of Tau LLPS, which can then be extrapolated into the cellular context. Tau condensation is a new aspect of Tau biology that may play a role for the initiation of Tau aggregation, but also for its physiological function(s), for example, the binding to microtubules. Here we describe how to study the condensation of Tau in vitro using light microscopy, including fluorescence recovery after photobleaching (FRAP), to assess the shape and molecular diffusion in the condensates, a proxy for the degree of condensate percolation. We also describe turbidity measurements of condensate-containing solutions to assess the overall amount of LLPS and time-resolved dynamic light scattering (trDLS) to study the formation and size of Tau condensates.
000165615 536__ $$0G:(DE-HGF)POF4-352$$a352 - Disease Mechanisms (POF4-352)$$cPOF4-352$$fPOF IV$$x0
000165615 588__ $$aDataset connected to CrossRef Book Series, PubMed, , Journals: pub.dzne.de
000165615 650_7 $$2Other$$aCoacervation
000165615 650_7 $$2Other$$aCondensation
000165615 650_7 $$2Other$$aCrowding agents
000165615 650_7 $$2Other$$aFRAP
000165615 650_7 $$2Other$$aLLPS
000165615 650_7 $$2Other$$aMAPT
000165615 650_7 $$2Other$$aPolyethylene glycol
000165615 650_7 $$2Other$$aRNA
000165615 650_7 $$2NLM Chemicals$$atau Proteins
000165615 650_7 $$2NLM Chemicals$$apolyanions
000165615 650_2 $$2MeSH$$aHumans
000165615 650_2 $$2MeSH$$atau Proteins: metabolism
000165615 650_2 $$2MeSH$$aMicroscopy
000165615 650_2 $$2MeSH$$aDynamic Light Scattering
000165615 650_2 $$2MeSH$$aAlzheimer Disease: metabolism
000165615 7001_ $$aExner, Christian$$b1
000165615 7001_ $$aBetzel, Christian$$b2
000165615 7001_ $$0P:(DE-2719)2541671$$aMandelkow, Eckhard$$b3$$udzne
000165615 7001_ $$0P:(DE-2719)2812695$$aWegmann, Susanne$$b4$$eLast author$$udzne
000165615 773__ $$a10.1007/978-1-0716-2597-2_15
000165615 909CO $$ooai:pub.dzne.de:165615$$pVDB
000165615 9101_ $$0I:(DE-588)1065079516$$6P:(DE-2719)2812812$$aDeutsches Zentrum für Neurodegenerative Erkrankungen$$b0$$kDZNE
000165615 9101_ $$0I:(DE-588)1065079516$$6P:(DE-2719)2541671$$aDeutsches Zentrum für Neurodegenerative Erkrankungen$$b3$$kDZNE
000165615 9101_ $$0I:(DE-588)1065079516$$6P:(DE-2719)2812695$$aDeutsches Zentrum für Neurodegenerative Erkrankungen$$b4$$kDZNE
000165615 9131_ $$0G:(DE-HGF)POF4-352$$1G:(DE-HGF)POF4-350$$2G:(DE-HGF)POF4-300$$3G:(DE-HGF)POF4$$4G:(DE-HGF)POF$$aDE-HGF$$bGesundheit$$lNeurodegenerative Diseases$$vDisease Mechanisms$$x0
000165615 9141_ $$y2023
000165615 915__ $$0StatID:(DE-HGF)0200$$2StatID$$aDBCoverage$$bSCOPUS$$d2020-09-11
000165615 915__ $$0StatID:(DE-HGF)0300$$2StatID$$aDBCoverage$$bMedline$$d2020-09-11
000165615 9201_ $$0I:(DE-2719)1810006$$kAG Wegmann$$lProtein Actions in Neurodegeneration$$x0
000165615 9201_ $$0I:(DE-2719)1013014$$kAG Mandelkow 1$$lStructural Principles of Neurodegeneration$$x1
000165615 980__ $$acontb
000165615 980__ $$aVDB
000165615 980__ $$aI:(DE-2719)1810006
000165615 980__ $$aI:(DE-2719)1013014
000165615 980__ $$aUNRESTRICTED