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@ARTICLE{Wegmann:141184,
      author       = {Wegmann, Susanne and Muller, Daniel J and Mandelkow,
                      Eckhard},
      title        = {{I}nvestigating fibrillar aggregates of {T}au protein by
                      atomic force microscopy.},
      journal      = {Methods in molecular biology},
      volume       = {849},
      issn         = {1064-3745},
      address      = {[Heidelberg]},
      publisher    = {[Springer]},
      reportid     = {DZNE-2020-07506},
      isbn         = {978-1-61779-550-3 (print)},
      series       = {Methods in Molecular Biology},
      pages        = {169-183},
      year         = {2012},
      comment      = {Amyloid Proteins / Sigurdsson, Einar M. (Editor) ; Totowa,
                      NJ : Humana Press, 2012, Chapter 12 ; ISSN:
                      1064-3745=1940-6029 ; ISBN:
                      978-1-61779-550-3=978-1-61779-551-0 ;
                      doi:10.1007/978-1-61779-551-0},
      booktitle     = {Amyloid Proteins / Sigurdsson, Einar
                       M. (Editor) ; Totowa, NJ : Humana
                       Press, 2012, Chapter 12 ; ISSN:
                       1064-3745=1940-6029 ; ISBN:
                       978-1-61779-550-3=978-1-61779-551-0 ;
                       doi:10.1007/978-1-61779-551-0},
      abstract     = {Atomic force microscopy (AFM) has been used in numerous
                      studies to visualize and analyze the structure and
                      conformation of biological samples, from single molecules to
                      biopolymers to cells. The possibility to analyze native
                      samples without fixation, staining and in physiological
                      buffer conditions, combined with the sub-nanometer
                      resolution, makes AFM a versatile tool for the analysis of
                      protein aggregation and amyloid structures. Here, we
                      describe the application of AFM to study fibrillar Tau
                      protein aggregates.},
      keywords     = {Adsorption / Aluminum Silicates: chemistry / Glutaral:
                      chemistry / Humans / Microscopy, Atomic Force: methods /
                      Protein Multimerization / Protein Structure, Secondary /
                      Surface Properties / Time Factors / tau Proteins: chemistry
                      / Aluminum Silicates (NLM Chemicals) / tau Proteins (NLM
                      Chemicals) / Glutaral (NLM Chemicals) / mica (NLM
                      Chemicals)},
      cin          = {AG (Eckhard) Mandelkow},
      ddc          = {570},
      cid          = {I:(DE-2719)1013014},
      pnm          = {342 - Disease Mechanisms and Model Systems (POF3-342)},
      pid          = {G:(DE-HGF)POF3-342},
      typ          = {PUB:(DE-HGF)3 / PUB:(DE-HGF)16},
      pubmed       = {pmid:22528090},
      doi          = {10.1007/978-1-61779-551-0_12},
      url          = {https://pub.dzne.de/record/141184},
}