% 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{Gravagnuolo:821017,
      author       = {Gravagnuolo, Alfredo Maria and Longobardi, Sara and
                      Luchini, Alessandra and Appavou, Marie-Sousai and De
                      Stefano, Luca and Notomista, Eugenio and Paduano, Luigi and
                      Giardina, Paola},
      title        = {{C}lass {I} {H}ydrophobin {V}mh2 {A}dopts {A}typical
                      {M}echanisms to {S}elf-{A}ssemble into {F}unctional
                      {A}myloid {F}ibrils},
      journal      = {Biomacromolecules},
      volume       = {17},
      number       = {3},
      issn         = {1526-4602},
      address      = {Columbus, Ohio},
      publisher    = {American Chemical Soc.},
      reportid     = {FZJ-2016-06274},
      pages        = {954 - 964},
      year         = {2016},
      abstract     = {Hydrophobins are fungal proteins whose functions are mainly
                      based on their capability to self-assemble into amphiphilic
                      films at hydrophobic–hydrophilic interfaces (HHI). It is
                      widely accepted that class I hydrophobins form amyloid-like
                      structures, named rodlets, which are hundreds of nanometers
                      long, packed into ordered lateral assemblies and do not
                      exhibit an overall helical structure. We studied the
                      self-assembly of the Class I hydrophobin Vmh2 from Pleurotus
                      ostreatus in aqueous solutions by dynamic light scattering
                      (DLS), thioflavin T (ThT), fluorescence assay, circular
                      dichroism (CD), cryogenic trasmission electron microscopy
                      (cryo-TEM), and TEM. Vmh2 does not form fibrillar aggregates
                      at HHI. It exhibits spherical and fibrillar assemblies whose
                      ratio depends on the protein concentration when freshly
                      solubilized at pH ≥ 7. Moreover, it spontaneously
                      self-assembles into isolated, micrometer long, and twisted
                      amyloid fibrils, observed for the first time in fungal
                      hydrophobins. This process is promoted by acidic pH,
                      temperature, and Ca2+ ions. A model of self-assembly into
                      amyloid-like structures has been proposed.},
      cin          = {JCNS (München) ; Jülich Centre for Neutron Science JCNS
                      (München) ; JCNS-FRM-II / Neutronenstreuung ; JCNS-1},
      ddc          = {540},
      cid          = {I:(DE-Juel1)JCNS-FRM-II-20110218 /
                      I:(DE-Juel1)JCNS-1-20110106},
      pnm          = {6G15 - FRM II / MLZ (POF3-6G15) / 6G4 - Jülich Centre for
                      Neutron Research (JCNS) (POF3-623)},
      pid          = {G:(DE-HGF)POF3-6G15 / G:(DE-HGF)POF3-6G4},
      experiment   = {EXP:(DE-MLZ)TEM-MLZ-20151210},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000372391800027},
      pubmed       = {pmid:26828412},
      doi          = {10.1021/acs.biomac.5b01632},
      url          = {https://juser.fz-juelich.de/record/821017},
}