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@ARTICLE{IbanezdeOpakua:165219,
      author       = {Ibanez de Opakua, Alain and Geraets, James A and Frieg,
                      Benedikt and Dienemann, Christian and Savastano, Adriana and
                      Rankovic, Marija and Cima-Omori, Maria-Sol and Schröder,
                      Gunnar F and Zweckstetter, Markus},
      title        = {{M}olecular interactions of {FG} nucleoporin repeats at
                      high resolution.},
      journal      = {Nature chemistry},
      volume       = {14},
      number       = {11},
      issn         = {1755-4330},
      address      = {London},
      publisher    = {Nature Publishing Group},
      reportid     = {DZNE-2022-01516},
      pages        = {1278 - 1285},
      year         = {2022},
      note         = {CC BY: https://creativecommons.org/licenses/by/4.0/},
      abstract     = {Proteins that contain repeat phenylalanine-glycine (FG)
                      residues phase separate into oncogenic transcription factor
                      condensates in malignant leukaemias, form the permeability
                      barrier of the nuclear pore complex and mislocalize in
                      neurodegenerative diseases. Insights into the molecular
                      interactions of FG-repeat nucleoporins have, however,
                      remained largely elusive. Using a combination of NMR
                      spectroscopy and cryoelectron microscopy, we have identified
                      uniformly spaced segments of transient β-structure and a
                      stable preformed α-helix recognized by messenger RNA export
                      factors in the FG-repeat domain of human nucleoporin 98
                      (Nup98). In addition, we have determined at high resolution
                      the molecular organization of reversible FG-FG interactions
                      in amyloid fibrils formed by a highly aggregation-prone
                      segment in Nup98. We have further demonstrated that
                      amyloid-like aggregates of the FG-repeat domain of Nup98
                      have low stability and are reversible. Our results provide
                      critical insights into the molecular interactions underlying
                      the self-association and phase separation of FG-repeat
                      nucleoporins in physiological and pathological cell
                      activities.},
      keywords     = {Humans / Cryoelectron Microscopy / Nuclear Pore: chemistry
                      / Nuclear Pore: metabolism / Nuclear Pore Complex Proteins:
                      genetics / Nuclear Pore Complex Proteins: analysis / Nuclear
                      Pore Complex Proteins: chemistry / Phenylalanine: chemistry
                      / Repetitive Sequences, Amino Acid / Nuclear Pore Complex
                      Proteins (NLM Chemicals) / Phenylalanine (NLM Chemicals) /
                      Nup98 protein, human (NLM Chemicals)},
      cin          = {AG Zweckstetter},
      ddc          = {540},
      cid          = {I:(DE-2719)1410001},
      pnm          = {352 - Disease Mechanisms (POF4-352)},
      pid          = {G:(DE-HGF)POF4-352},
      typ          = {PUB:(DE-HGF)16},
      pmc          = {pmc:PMC9630130},
      pubmed       = {pmid:36138110},
      doi          = {10.1038/s41557-022-01035-7},
      url          = {https://pub.dzne.de/record/165219},
}