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@ARTICLE{Rder:878602,
      author       = {Röder, Christine and Kupreichyk, Tatsiana and Gremer,
                      Lothar and Schäfer, Luisa U. and Pothula, Karunakar R. and
                      Ravelli, Raimond B. G. and Willbold, Dieter and Hoyer,
                      Wolfgang and Schröder, Gunnar F.},
      title        = {{C}ryo-{EM} structure of islet amyloid polypeptide fibrils
                      reveals similarities with amyloid-β fibrils},
      journal      = {Nature structural $\&$ molecular biology},
      volume       = {27},
      number       = {7},
      issn         = {1545-9985},
      address      = {London [u.a.]},
      publisher    = {Nature Publishing Group},
      reportid     = {FZJ-2020-02940},
      pages        = {660 - 667},
      year         = {2020},
      abstract     = {Amyloid deposits consisting of fibrillar islet amyloid
                      polypeptide (IAPP) in pancreatic islets are associated with
                      beta-cell loss and have been implicated in type 2 diabetes
                      (T2D). Here, we applied cryo-EM to reconstruct densities of
                      three dominant IAPP fibril polymorphs, formed in vitro from
                      synthetic human IAPP. An atomic model of the main polymorph,
                      built from a density map of 4.2-Å resolution, reveals two
                      S-shaped, intertwined protofilaments. The segment
                      21-NNFGAIL-27, essential for IAPP amyloidogenicity, forms
                      the protofilament interface together with Tyr37 and the
                      amidated C terminus. The S-fold resembles polymorphs of
                      Alzheimer's disease (AD)-associated amyloid-β (Aβ)
                      fibrils, which might account for the epidemiological link
                      between T2D and AD and reports on IAPP-Aβ cross-seeding in
                      vivo. The results structurally link the early-onset T2D IAPP
                      genetic polymorphism (encoding Ser20Gly) with the AD Arctic
                      mutation (Glu22Gly) of Aβ and support the design of
                      inhibitors and imaging probes for IAPP fibrils.},
      cin          = {IBI-7},
      ddc          = {570},
      cid          = {I:(DE-Juel1)IBI-7-20200312},
      pnm          = {551 - Functional Macromolecules and Complexes (POF3-551)},
      pid          = {G:(DE-HGF)POF3-551},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {32541895},
      UT           = {WOS:000543557100001},
      doi          = {10.1038/s41594-020-0442-4},
      url          = {https://juser.fz-juelich.de/record/878602},
}