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000136780 0247_ $$2doi$$a10.1073/pnas.1212100110
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000136780 0247_ $$2ISSN$$a1091-6490
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000136780 037__ $$aDZNE-2020-03102
000136780 041__ $$aEnglish
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000136780 1001_ $$0P:(DE-2719)2812695$$aWegmann, Susanne$$b0$$eCorresponding author$$udzne
000136780 245__ $$aThe fuzzy coat of pathological human Tau fibrils is a two-layered polyelectrolyte brush.
000136780 260__ $$aWashington, DC$$bNational Acad. of Sciences$$c2013
000136780 264_1 $$2Crossref$$3online$$bProceedings of the National Academy of Sciences$$c2012-12-26
000136780 264_1 $$2Crossref$$3print$$bProceedings of the National Academy of Sciences$$c2013-01-22
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000136780 520__ $$aThe structure and properties of amyloid-like Tau fibrils accumulating in neurodegenerative diseases have been debated for decades. Although the core of Tau fibrils assembles from short β-strands, the properties of the much longer unstructured Tau domains protruding from the fibril core remain largely obscure. Applying immunogold transmission EM, and force-volume atomic force microscopy (AFM), we imaged human Tau fibrils at high resolution and simultaneously mapped their mechanical and adhesive properties. Tau fibrils showed a ≈ 16-nm-thick fuzzy coat that resembles a two-layered polyelectrolyte brush, which is formed by the unstructured short C-terminal and long N-terminal Tau domains. The mechanical and adhesive properties of the fuzzy coat are modulated by electrolytes and pH, and thus by the cellular environment. These unique properties of the fuzzy coat help in understanding how Tau fibrils disturb cellular interactions and accumulate in neurofibrillary tangles.
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000136780 650_7 $$2NLM Chemicals$$aElectrolytes
000136780 650_7 $$2NLM Chemicals$$aMAPT protein, human
000136780 650_7 $$2NLM Chemicals$$aRecombinant Proteins
000136780 650_7 $$2NLM Chemicals$$atau Proteins
000136780 650_2 $$2MeSH$$aAdhesiveness
000136780 650_2 $$2MeSH$$aBiomechanical Phenomena
000136780 650_2 $$2MeSH$$aElectrolytes: chemistry
000136780 650_2 $$2MeSH$$aHumans
000136780 650_2 $$2MeSH$$aHydrogen-Ion Concentration
000136780 650_2 $$2MeSH$$aMicroscopy, Atomic Force
000136780 650_2 $$2MeSH$$aMicroscopy, Immunoelectron
000136780 650_2 $$2MeSH$$aModels, Molecular
000136780 650_2 $$2MeSH$$aProtein Interaction Domains and Motifs
000136780 650_2 $$2MeSH$$aProtein Multimerization
000136780 650_2 $$2MeSH$$aRecombinant Proteins: chemistry
000136780 650_2 $$2MeSH$$aRecombinant Proteins: genetics
000136780 650_2 $$2MeSH$$aRecombinant Proteins: ultrastructure
000136780 650_2 $$2MeSH$$atau Proteins: chemistry
000136780 650_2 $$2MeSH$$atau Proteins: genetics
000136780 650_2 $$2MeSH$$atau Proteins: physiology
000136780 650_2 $$2MeSH$$atau Proteins: ultrastructure
000136780 7001_ $$0P:(DE-HGF)0$$aMedalsy, Izhar D$$b1
000136780 7001_ $$0P:(DE-2719)2541671$$aMandelkow, Eckhard$$b2
000136780 7001_ $$0P:(DE-HGF)0$$aMüller, Daniel J$$b3
000136780 77318 $$2Crossref$$3journal-article$$a10.1073/pnas.1212100110$$b : Proceedings of the National Academy of Sciences, 2012-12-26$$n4$$pE313-E321$$tProceedings of the National Academy of Sciences$$v110$$x0027-8424$$y2012
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000136780 8567_ $$2Pubmed Central$$uhttp://www.ncbi.nlm.nih.gov/pmc/articles/PMC3557036
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000136780 9101_ $$0I:(DE-588)1065079516$$6P:(DE-2719)2541671$$aDeutsches Zentrum für Neurodegenerative Erkrankungen$$b2$$kDZNE
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