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000057095 0247_ $$2DOI$$a10.1016/j.jsb.2006.11.010
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000057095 084__ $$2WoS$$aBiochemistry & Molecular Biology
000057095 084__ $$2WoS$$aBiophysics
000057095 084__ $$2WoS$$aCell Biology
000057095 1001_ $$0P:(DE-HGF)0$$aSchaap, I.A.T.$$b0
000057095 245__ $$aTau protein binding forms a 1 nm thick layer along protofilaments without affecting the radial elasticity of microtubules
000057095 260__ $$aSan Diego, Calif.$$bElsevier$$c2007
000057095 300__ $$a282 - 292
000057095 3367_ $$0PUB:(DE-HGF)16$$2PUB:(DE-HGF)$$aJournal Article
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000057095 440_0 $$03814$$aJournal of Structural Biology$$v158$$x1047-8477
000057095 500__ $$aRecord converted from VDB: 12.11.2012
000057095 520__ $$aTau is one of the most abundant microtubule-associated proteins involved in kinetic stabilization and bundling of axonal microtubules. Although intense research has revealed much about tau function and its involvement in Alzheimer's disease during the past years, it still remains unclear how exactly tau binds on microtubules and if the kinetic stabilization of microtubules by tau is accompanied, at least in part, by a mechanical reinforcement of microtubules. In this paper, we have used atomic force microscopy to address both aspects by visualizing and mechanically analyzing microtubules in the presence of native tau isoforms. We could show that tau at saturating concentrations forms a 1 nm thick layer around the microtubule, but leaves the protofilament structure well visible. The latter observation argues for tau binding mainly along and not across the protofilaments. The radial elasticity of microtubules was almost unaffected by tau, consistent with tau binding along the tops of the protofilaments. Tau did increase the resistance of microtubules against rupture. Finite-element calculations confirmed our findings.
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000057095 650_2 $$2MeSH$$aAnimals
000057095 650_2 $$2MeSH$$aElasticity
000057095 650_2 $$2MeSH$$aKinetics
000057095 650_2 $$2MeSH$$aMicroscopy, Atomic Force
000057095 650_2 $$2MeSH$$aMicrotubule-Associated Proteins: chemistry
000057095 650_2 $$2MeSH$$aMicrotubules: chemistry
000057095 650_2 $$2MeSH$$aProtein Binding
000057095 650_2 $$2MeSH$$aProtein Isoforms
000057095 650_2 $$2MeSH$$aSwine: metabolism
000057095 650_2 $$2MeSH$$atau Proteins: chemistry
000057095 650_7 $$00$$2NLM Chemicals$$aMicrotubule-Associated Proteins
000057095 650_7 $$00$$2NLM Chemicals$$aProtein Isoforms
000057095 650_7 $$00$$2NLM Chemicals$$atau Proteins
000057095 650_7 $$2WoSType$$aJ
000057095 65320 $$2Author$$amicrotubule
000057095 65320 $$2Author$$atau protein
000057095 65320 $$2Author$$akinesin
000057095 65320 $$2Author$$aatomic force microscopy
000057095 65320 $$2Author$$aAFM
000057095 65320 $$2Author$$afinite element modeling
000057095 65320 $$2Author$$aFEM
000057095 7001_ $$0P:(DE-Juel1)VDB27696$$aHoffmann, B.$$b1$$uFZJ
000057095 7001_ $$0P:(DE-HGF)0$$aCarrasco, C.$$b2
000057095 7001_ $$0P:(DE-Juel1)128833$$aMerkel, R.$$b3$$uFZJ
000057095 7001_ $$0P:(DE-HGF)0$$aSchmidt, C. F.$$b4
000057095 773__ $$0PERI:(DE-600)1469822-5$$a10.1016/j.jsb.2006.11.010$$gVol. 158, p. 282 - 292$$p282 - 292$$q158<282 - 292$$tJournal of structural biology$$v158$$x1047-8477$$y2007
000057095 8567_ $$uhttp://dx.doi.org/10.1016/j.jsb.2006.11.010
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000057095 915__ $$0StatID:(DE-HGF)0010$$aJCR/ISI refereed
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