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@ARTICLE{Mori:136809,
      author       = {Mori, Kohji and Lammich, Sven and Mackenzie, Ian R A and
                      Forné, Ignasi and Zilow, Sonja and Kretzschmar, Hans and
                      Edbauer, Dieter and Janssens, Jonathan and Kleinberger,
                      Gernot and Cruts, Marc and Herms, Jochen and Neumann,
                      Manuela and Van Broeckhoven, Christine and Arzberger, Thomas
                      and Haass, Christian},
      title        = {hn{RNP} {A}3 binds to {GGGGCC} repeats and is a constituent
                      of p62-positive/{TDP}43-negative inclusions in the
                      hippocampus of patients with {C}9orf72 mutations.},
      journal      = {Acta neuropathologica},
      volume       = {125},
      number       = {3},
      issn         = {0001-6322},
      address      = {Heidelberg},
      publisher    = {Springer},
      reportid     = {DZNE-2020-03131},
      pages        = {413-423},
      year         = {2013},
      abstract     = {Genetic analysis revealed the hexanucleotide repeat
                      expansion GGGGCC within the regulatory region of the gene
                      C9orf72 as the most common cause of familial amyotrophic
                      lateral sclerosis and the second most common cause of
                      frontotemporal lobar degeneration. Since repeat expansions
                      might cause RNA toxicity via sequestration of RNA-binding
                      proteins, we searched for proteins capable of binding to
                      GGGGCC repeats. In vitro-transcribed biotinylated RNA
                      containing hexanucleotide GGGGCC or, as control, AAAACC
                      repeats were incubated with nuclear protein extracts. Using
                      stringent filtering protocols 20 RNA-binding proteins with a
                      variety of different functions in RNA metabolism,
                      translation and transport were identified. A subset of these
                      proteins was further investigated by immunohistochemistry in
                      human autopsy brains. This revealed that hnRNP A3 formed
                      neuronal cytoplasmic and intranuclear inclusions in the
                      hippocampus of patients with C9orf72 repeat extensions.
                      Confocal microcopy showed that these inclusions belong to
                      the group of the so far enigmatic p62-positive/TDP-43
                      negative inclusions characteristically seen in autopsy cases
                      of diseased C9orf72 repeat expansion carriers. Thus, we have
                      identified one protein component of these pathognomonic
                      inclusions.},
      keywords     = {Adaptor Proteins, Signal Transducing: metabolism /
                      Amyotrophic Lateral Sclerosis: genetics / Amyotrophic
                      Lateral Sclerosis: metabolism / Amyotrophic Lateral
                      Sclerosis: pathology / C9orf72 Protein / Chromatography,
                      High Pressure Liquid / DNA-Binding Proteins: metabolism /
                      Frontotemporal Lobar Degeneration: genetics / Frontotemporal
                      Lobar Degeneration: metabolism / Frontotemporal Lobar
                      Degeneration: pathology / Gene Expression Regulation:
                      genetics / HEK293 Cells / Heterogeneous-Nuclear
                      Ribonucleoprotein Group A-B: metabolism / Hippocampus:
                      pathology / Humans / Inclusion Bodies: metabolism /
                      Inclusion Bodies: pathology / Mass Spectrometry / Mutation:
                      genetics / Proteins: genetics / RNA, Small Interfering:
                      metabolism / Repetitive Sequences, Nucleic Acid: physiology
                      / Sequestosome-1 Protein / Transfection / Adaptor Proteins,
                      Signal Transducing (NLM Chemicals) / C9orf72 Protein (NLM
                      Chemicals) / C9orf72 protein, human (NLM Chemicals) /
                      DNA-Binding Proteins (NLM Chemicals) / HNRNPA3 protein,
                      human (NLM Chemicals) / Heterogeneous-Nuclear
                      Ribonucleoprotein Group A-B (NLM Chemicals) / Proteins (NLM
                      Chemicals) / RNA, Small Interfering (NLM Chemicals) / SQSTM1
                      protein, human (NLM Chemicals) / Sequestosome-1 Protein (NLM
                      Chemicals)},
      cin          = {AG Edbauer / AG Herms / AG Neumann},
      ddc          = {610},
      cid          = {I:(DE-2719)1110004 / I:(DE-2719)1110001 /
                      I:(DE-2719)1210003},
      pnm          = {342 - Disease Mechanisms and Model Systems (POF3-342) / 344
                      - Clinical and Health Care Research (POF3-344)},
      pid          = {G:(DE-HGF)POF3-342 / G:(DE-HGF)POF3-344},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:23381195},
      doi          = {10.1007/s00401-013-1088-7},
      url          = {https://pub.dzne.de/record/136809},
}