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@ARTICLE{IbezdeOpakua:912260,
      author       = {Ibáñez de Opakua, Alain and Geraets, James 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     = {FZJ-2022-05457},
      pages        = {1278 - 1285},
      year         = {2022},
      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.},
      cin          = {IBI-7},
      ddc          = {540},
      cid          = {I:(DE-Juel1)IBI-7-20200312},
      pnm          = {5244 - Information Processing in Neuronal Networks
                      (POF4-524)},
      pid          = {G:(DE-HGF)POF4-5244},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {36138110},
      UT           = {WOS:000856606900001},
      doi          = {10.1038/s41557-022-01035-7},
      url          = {https://juser.fz-juelich.de/record/912260},
}