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@ARTICLE{Schaap:57095,
      author       = {Schaap, I.A.T. and Hoffmann, B. and Carrasco, C. and
                      Merkel, R. and Schmidt, C. F.},
      title        = {{T}au protein binding forms a 1 nm thick layer along
                      protofilaments without affecting the radial elasticity of
                      microtubules},
      journal      = {Journal of structural biology},
      volume       = {158},
      issn         = {1047-8477},
      address      = {San Diego, Calif.},
      publisher    = {Elsevier},
      reportid     = {PreJuSER-57095},
      pages        = {282 - 292},
      year         = {2007},
      note         = {Record converted from VDB: 12.11.2012},
      abstract     = {Tau 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.},
      keywords     = {Animals / Elasticity / Kinetics / Microscopy, Atomic Force
                      / Microtubule-Associated Proteins: chemistry / Microtubules:
                      chemistry / Protein Binding / Protein Isoforms / Swine:
                      metabolism / tau Proteins: chemistry /
                      Microtubule-Associated Proteins (NLM Chemicals) / Protein
                      Isoforms (NLM Chemicals) / tau Proteins (NLM Chemicals) / J
                      (WoSType)},
      cin          = {IBN-4},
      ddc          = {540},
      cid          = {I:(DE-Juel1)VDB802},
      pnm          = {Kondensierte Materie},
      pid          = {G:(DE-Juel1)FUEK414},
      shelfmark    = {Biochemistry $\&$ Molecular Biology / Biophysics / Cell
                      Biology},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:17329123},
      UT           = {WOS:000246927800003},
      doi          = {10.1016/j.jsb.2006.11.010},
      url          = {https://juser.fz-juelich.de/record/57095},
}