% 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{Stellato:80585,
      author       = {Stellato, F. and Menestrina, G. and Serra, M. D. and
                      Potrich, C. and Tomazzolli, R. and Meyer Klaucke, W. and
                      Morante, S. and DESY},
      title        = {{M}etal binding in amyloid beta-peptides shows intra- and
                      inter-peptide coordination modes.},
      journal      = {European biophysics journal},
      volume       = {35},
      issn         = {0175-7571},
      address      = {Berlin},
      publisher    = {Springer},
      reportid     = {PHPPUBDB-2651},
      pages        = {12},
      year         = {2006},
      abstract     = {X-ray absorption spectroscopy data show different metal
                      binding site structures in beta-amyloid peptides according
                      to whether they are complexed with Cu(2+) or Zn(2+) ions.
                      While the geometry around copper is stably consistent with
                      an intra-peptide binding with three metal-coordinated
                      Histidine residues, the zinc coordination mode depends on
                      specific solution conditions. In particular, different
                      sample preparations are seen to lead to different geometries
                      around the absorber that are compatible with either an
                      intra- or an inter-peptide coordination mode. This result
                      reinforces the hypothesis that assigns different
                      physiological roles to the two metals, with zinc favoring
                      peptide aggregation and, as a consequence, plaque
                      formation.},
      keywords     = {Amyloid beta-Peptides: chemistry / Cations, Divalent /
                      Copper: chemistry / Fourier Analysis / Histidine: chemistry
                      / Imidazoles: chemistry / Models, Molecular / Protein
                      Binding / Protein Conformation / Spectrum Analysis: methods
                      / X-Rays / Zinc: chemistry / Amyloid beta-Peptides (NLM
                      Chemicals) / Cations, Divalent (NLM Chemicals) / Imidazoles
                      (NLM Chemicals) / Histidine (NLM Chemicals) / Copper (NLM
                      Chemicals) / Zinc (NLM Chemicals) / imidazole (NLM
                      Chemicals)},
      cin          = {EMBL},
      ddc          = {570},
      cid          = {$I:(DE-H253)EMBL_-2012_-20130307$},
      pnm          = {Facility (machine) DORIS/PETRA (POF1-DORIS-PETRA-20130405)},
      pid          = {G:(DE-H253)POF1-DORIS-PETRA-20130405},
      experiment   = {EXP:(DE-H253)DORISIII(machine)-20150101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:16404590},
      UT           = {WOS:000235900400005},
      doi          = {10.1007/s00249-005-0041-7},
      url          = {https://bib-pubdb1.desy.de/record/80585},
}