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@ARTICLE{Perov:872752,
      author       = {Perov, Sergei and Lidor, Ofir and Salinas, Nir and Golan,
                      Nimrod and Tayeb- Fligelman, Einav and Deshmukh, Maya and
                      Willbold, Dieter and Landau, Meytal},
      title        = {{S}tructural {I}nsights into {C}urli {C}sg{A} {C}ross-β
                      {F}ibril {A}rchitecture {I}nspire {R}epurposing of
                      {A}nti-amyloid {C}ompounds as {A}nti-biofilm {A}gents},
      journal      = {PLoS pathogens},
      volume       = {15},
      number       = {8},
      issn         = {1553-7374},
      address      = {Lawrence, Kan.},
      publisher    = {PLoS},
      reportid     = {FZJ-2020-00230},
      pages        = {e1007978 -},
      year         = {2019},
      abstract     = {Curli amyloid fibrils secreted by Enterobacteriaceae
                      mediate host cell adhesion and contribute to biofilm
                      formation, thereby promoting bacterial resistance to
                      environmental stressors. Here, we present crystal structures
                      of amyloid-forming segments from the major curli subunit,
                      CsgA, revealing steric zipper fibrils of tightly mated
                      β-sheets, demonstrating a structural link between curli and
                      human pathological amyloids. D-enantiomeric peptides,
                      originally developed to interfere with Alzheimer's
                      disease-associated amyloid-β, inhibited CsgA fibrillation
                      and reduced biofilm formation in Salmonella typhimurium.
                      Moreover, as previously shown, CsgA fibrils cross-seeded
                      fibrillation of amyloid-β, providing support for the
                      proposed structural resemblance and potential for
                      cross-species amyloid interactions. The presented findings
                      provide structural insights into amyloidogenic regions
                      important for curli formation, suggest a novel strategy for
                      disrupting amyloid-structured biofilms, and hypothesize on
                      the formation of self-propagating prion-like species
                      originating from a microbial source that could influence
                      neurodegenerative diseases},
      cin          = {ICS-6},
      ddc          = {610},
      cid          = {I:(DE-Juel1)ICS-6-20110106},
      pnm          = {553 - Physical Basis of Diseases (POF3-553)},
      pid          = {G:(DE-HGF)POF3-553},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:31469892},
      UT           = {WOS:000488322100029},
      doi          = {10.1371/journal.ppat.1007978},
      url          = {https://juser.fz-juelich.de/record/872752},
}