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@ARTICLE{Bcker:602188,
      author       = {Bücker, Robert and Seuring, Carolin and Cazey, Cornelia
                      and Veith, Katharina and García-Alai, Maria and Gruenewald,
                      Kay and Landau, Meytal},
      title        = {{T}he {C}ryo-{EM} structures of two amphibian antimicrobial
                      cross-β amyloid fibrils},
      journal      = {Nature Communications},
      volume       = {13},
      number       = {1},
      issn         = {2041-1723},
      address      = {[London]},
      publisher    = {Nature Publishing Group UK},
      reportid     = {PUBDB-2024-00514},
      pages        = {4356},
      year         = {2022},
      abstract     = {The amyloid-antimicrobial link hypothesis is based on
                      antimicrobial properties found in human amyloids involved in
                      neurodegenerative and systemic diseases, along with
                      amyloidal structural properties found in antimicrobial
                      peptides (AMPs). Supporting this hypothesis, we here
                      determined the fibril structure of two AMPs from amphibians,
                      uperin 3.5 and aurein 3.3, by cryogenic electron microscopy
                      (cryo-EM), revealing amyloid cross-β fibrils of mated
                      β-sheets at atomic resolution. Uperin 3.5 formed a 3-blade
                      symmetrical propeller of nine peptides per fibril layer
                      including tight β-sheet interfaces. This cross-β cryo-EM
                      structure complements the cross-α fibril conformation
                      previously determined by crystallography, substantiating a
                      secondary structure switch mechanism of uperin 3.5. The
                      aurein 3.3 arrangement consisted of six peptides per fibril
                      layer, all showing kinked β-sheets allowing a rounded
                      compactness of the fibril. The kinked β-sheets are similar
                      to LARKS (Low-complexity, Amyloid-like, Reversible, Kinked
                      Segments) found in human functional amyloids.},
      cin          = {CSSB-LIV-KG / CSSB-CF-CRYO / CSSB-F},
      ddc          = {500},
      cid          = {I:(DE-H253)CSSB-LIV-KG-20220525 /
                      I:(DE-H253)CSSB-CF-CRYO-20210520 /
                      I:(DE-H253)CSSB-F-20230420},
      pnm          = {899 - ohne Topic (POF4-899)},
      pid          = {G:(DE-HGF)POF4-899},
      experiment   = {EXP:(DE-MLZ)NOSPEC-20140101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:35896552},
      UT           = {WOS:000831732000020},
      doi          = {10.1038/s41467-022-32039-z},
      url          = {https://bib-pubdb1.desy.de/record/602188},
}