% IMPORTANT: The following is UTF-8 encoded.  This means that in the presence
% of non-ASCII characters, it will not work with BibTeX 0.99 or older.
% Instead, you should use an up-to-date BibTeX implementation like “bibtex8” or
% “biber”.

@ARTICLE{Salinas:454475,
      author       = {Salinas, Nir and Tayeb-Fligelman, Einav and Sammito,
                      Massimo D. and Bloch, Daniel and Jelinek, Raz and Noy, Dror
                      and Usón, Isabel and Landau, Meytal},
      title        = {{T}he amphibian antimicrobial peptide uperin 3.5 is a
                      cross-α/cross-β chameleon functional amyloid},
      journal      = {Proceedings of the National Academy of Sciences of the
                      United States of America},
      volume       = {118},
      number       = {3},
      issn         = {1091-6490},
      address      = {Washington, DC},
      publisher    = {National Acad. of Sciences},
      reportid     = {PUBDB-2021-00549},
      pages        = {e2014442118 (1-8)},
      year         = {2021},
      abstract     = {Antimicrobial activity is being increasingly linked to
                      amyloid fibril formation, suggesting physiological roles for
                      some human amyloids, which have historically been viewed as
                      strictly pathological agents. This work reports on formation
                      of functional cross-α amyloid fibrils of the amphibian
                      antimicrobial peptide uperin 3.5 at atomic resolution, an
                      architecture initially discovered in the bacterial PSMα3
                      cytotoxin. The fibrils of uperin 3.5 and PSMα3 comprised
                      antiparallel and parallel helical sheets, respectively,
                      recapitulating properties of β-sheets. Uperin 3.5
                      demonstrated chameleon properties of a secondary structure
                      switch, forming mostly cross-β fibrils in the absence of
                      lipids. Uperin 3.5 helical fibril formation was largely
                      induced by, and formed on, bacterial cells or membrane
                      mimetics, and led to membrane damage and cell death. These
                      findings suggest a regulation mechanism, which includes
                      storage of inactive peptides as well as environmentally
                      induced activation of uperin 3.5, via chameleon cross-α/β
                      amyloid fibrils.},
      cin          = {EMBL-User / CSSB-EMBL / CSSB-F},
      ddc          = {500},
      cid          = {I:(DE-H253)EMBL-User-20120814 /
                      I:(DE-H253)CSSB-EMBL-20141216 / I:(DE-H253)CSSB-F-20230420},
      pnm          = {6G3 - PETRA III (DESY) (POF4-6G3)},
      pid          = {G:(DE-HGF)POF4-6G3},
      experiment   = {EXP:(DE-H253)P-P14-20150101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:33431675},
      UT           = {WOS:000609633900031},
      doi          = {10.1073/pnas.2014442118},
      url          = {https://bib-pubdb1.desy.de/record/454475},
}