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@ARTICLE{Kornreich:126901,
      author       = {M. Kornreich and E. Malka-Gibor and A. Laser-Azogui and O.
                      Doron and H. Herrmann$^*$ and R. Beck},
      title        = {{C}omposite bottlebrush mechanics: α-internexin fine-tunes
                      neurofilament network properties.},
      journal      = {Soft matter},
      volume       = {11},
      number       = {29},
      issn         = {1744-6848},
      address      = {London},
      publisher    = {Royal Soc. of Chemistry},
      reportid     = {DKFZ-2017-02929},
      pages        = {5839 - 5849},
      year         = {2015},
      abstract     = {Neuronal cytoplasmic intermediate filaments are principal
                      structural and mechanical elements of the axon. Their
                      expression during embryonic development follows a
                      differential pattern, while their unregulated expression is
                      correlated to neurodegenerative diseases. The largest
                      neurofilament proteins of medium (NF-M) and high molecular
                      weight (NF-H) were shown to modulate the axonal architecture
                      and inter-filament spacing. However, the individual roles of
                      the remaining α-internexin (α-Inx) and neurofilament of
                      low molecular weight (NF-L) proteins in composite filaments
                      remained elusive. In contrast to previous predictions, we
                      show that when co-assembled with NF-M, the shortest and the
                      least charged α-Inx protein increases inter-filament
                      spacing. These findings suggest a novel structural
                      explanation for the expression pattern of neurofilament
                      proteins during embryonic development. We explain our
                      results by an analysis of ionic cross-links between the
                      disordered polyampholytic C-terminal tails and suggest that
                      a collapsed conformation of the α-Inx tail domain
                      interferes with tail cross-linking near the filament
                      backbone.},
      keywords     = {Intermediate Filament Proteins (NLM Chemicals) /
                      Neurofilament Proteins (NLM Chemicals) / Recombinant
                      Proteins (NLM Chemicals) / alpha-internexin (NLM Chemicals)
                      / Hydrogel (NLM Chemicals)},
      cin          = {B065},
      ddc          = {530},
      cid          = {I:(DE-He78)B065-20160331},
      pnm          = {312 - Functional and structural genomics (POF3-312)},
      pid          = {G:(DE-HGF)POF3-312},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:26100609},
      doi          = {10.1039/C5SM00662G},
      url          = {https://inrepo02.dkfz.de/record/126901},
}