% 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{Mazzitelli:138852,
      author       = {Mazzitelli, Sonia and Filipello, Fabia and Rasile, Marco
                      and Lauranzano, Eliana and Starvaggi-Cucuzza, Chiara and
                      Tamborini, Matteo and Pozzi, Davide and Barajon, Isabella
                      and Giorgino, Toni and Natalello, Antonino and Matteoli,
                      Michela},
      title        = {{A}myloid-β 1-24 {C}-terminal truncated fragment promotes
                      amyloid-β 1-42 aggregate formation in the healthy brain.},
      journal      = {Acta Neuropathologica Communications},
      volume       = {4},
      number       = {1},
      issn         = {2051-5960},
      address      = {London},
      publisher    = {Biomed Central},
      reportid     = {DZNE-2020-05174},
      pages        = {110},
      year         = {2016},
      abstract     = {Substantial data indicate that amyloid-β (Aβ), the major
                      component of senile plaques, plays a central role in
                      Alzheimer's Disease and indeed the assembly of naturally
                      occurring amyloid peptides into cytotoxic aggregates is
                      linked to the disease pathogenesis. Although Aβ42 is a
                      highly aggregating form of Aβ, the co-occurrence of shorter
                      Aβ peptides might affect the aggregation potential of the
                      Aβ pool. In this study we aimed to assess whether the
                      structural behavior of human Aβ42 peptide inside the brain
                      is influenced by the concomitant presence of N-terminal
                      fragments produced by the proteolytic activity of glial
                      cells. We show that the occurrence of the human C-terminal
                      truncated 1-24 Aβ fragment impairs Aβ42 clearance through
                      blood brain barrier and promotes the formation of Aβ42
                      aggregates even in the healthy brain. By showing that
                      Aβ1-24 has seeding properties for aggregate formation in
                      intracranially injected wild type mice, our study provide
                      the proof-of-concept that peptides produced upon Aβ42
                      cleavage by activated glial cells may cause phenotypic
                      defects even in the absence of genetic mutations associated
                      with Alzheimer's Disease, possibly contributing to the
                      development of the sporadic form of the pathology.},
      keywords     = {Alzheimer Disease: metabolism / Alzheimer Disease:
                      pathology / Amyloid beta-Peptides: administration $\&$
                      dosage / Amyloid beta-Peptides: metabolism / Animals /
                      Brain: metabolism / Brain: pathology / Disease Models,
                      Animal / Humans / Learning Disabilities: metabolism /
                      Learning Disabilities: pathology / Matrix Metalloproteinase
                      9: genetics / Matrix Metalloproteinase 9: metabolism /
                      Memory Disorders: metabolism / Memory Disorders: pathology /
                      Mice / Mice, Inbred BALB C / Mice, Inbred C57BL / Mice,
                      Knockout / Mice, Transgenic / Microglia: metabolism /
                      Microglia: pathology / Motor Activity: physiology / Peptide
                      Fragments: administration $\&$ dosage / Peptide Fragments:
                      metabolism / Plaque, Amyloid: metabolism / Plaque, Amyloid:
                      pathology / Protein Folding / Protein Multimerization /
                      Social Behavior / Amyloid beta-Peptides (NLM Chemicals) /
                      Peptide Fragments (NLM Chemicals) / amyloid beta-peptide
                      (1-24) (NLM Chemicals) / amyloid beta-protein (1-42) (NLM
                      Chemicals) / Matrix Metalloproteinase 9 (NLM Chemicals) /
                      Mmp9 protein, mouse (NLM Chemicals)},
      cin          = {AG Heutink},
      ddc          = {610},
      cid          = {I:(DE-2719)1210002},
      pnm          = {345 - Population Studies and Genetics (POF3-345)},
      pid          = {G:(DE-HGF)POF3-345},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:27724899},
      pmc          = {pmc:PMC5057504},
      doi          = {10.1186/s40478-016-0381-9},
      url          = {https://pub.dzne.de/record/138852},
}