% 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{Hogl:136887,
      author       = {Hogl, Sebastian and van Bebber, Frauke and Dislich, Bastian
                      and Kuhn, Peer-Hendrik and Haass, Christian and Schmid,
                      Bettina and Lichtenthaler, Stefan F},
      title        = {{L}abel-free quantitative analysis of the membrane proteome
                      of {B}ace1 protease knock-out zebrafish brains.},
      journal      = {Practical proteomics},
      volume       = {13},
      number       = {9},
      issn         = {1615-9853},
      address      = {Weinheim},
      publisher    = {Wiley VCH69157},
      reportid     = {DZNE-2020-03209},
      pages        = {1519-1527},
      year         = {2013},
      abstract     = {The aspartyl protease BACE1 cleaves neuregulin 1 and is
                      involved in myelination and is a candidate drug target for
                      Alzheimer's disease, where it acts as the β-secretase
                      cleaving the amyloid precursor protein. However, little is
                      known about other substrates in vivo. Here, we provide a
                      proteomic workflow for BACE1 substrate identification from
                      whole brains, combining filter-aided sample preparation,
                      strong-anion exchange fractionation, and label-free
                      quantification. We used bace1-deficient zebrafish and
                      quantified differences in protein levels between wild-type
                      and bace1 -/- zebrafish brains. Over 4500 proteins were
                      identified with at least two unique peptides and quantified
                      in both wild-type and bace1 -/- zebrafish brains. The
                      majority of zebrafish membrane proteins did not show altered
                      protein levels, indicating that Bace1 has a restricted
                      substrate specificity. Twenty-four membrane proteins
                      accumulated in the bace1 -/- brains and thus represent
                      candidate Bace1 substrates. They include several known BACE1
                      substrates, such as the zebrafish homologs of amyloid
                      precursor protein and the cell adhesion protein L1, which
                      validate the proteomic workflow. Additionally, several
                      candidate substrates with a function in neurite outgrowth
                      and axon guidance, such as plexin A3 and glypican-1 were
                      identified, pointing to a function of Bace1 in
                      neurodevelopment. Taken together, our study provides the
                      first proteomic analysis of knock-out zebrafish tissue and
                      demonstrates that combining gene knock-out models in
                      zebrafish with quantitative proteomics is a powerful
                      approach to address biomedical questions.},
      keywords     = {Amyloid beta-Protein Precursor: genetics / Amyloid
                      beta-Protein Precursor: metabolism / Animals / Animals,
                      Genetically Modified / Aspartic Acid Endopeptidases:
                      genetics / Aspartic Acid Endopeptidases: metabolism / Brain:
                      metabolism / Chemical Fractionation: methods / Glypicans:
                      metabolism / Humans / Membrane Proteins: analysis / Membrane
                      Proteins: genetics / Membrane Proteins: metabolism /
                      Proteome: genetics / Proteome: metabolism / Receptors, Cell
                      Surface: metabolism / Tandem Mass Spectrometry / Workflow /
                      Zebrafish: genetics / Zebrafish: metabolism / Zebrafish
                      Proteins: analysis / Zebrafish Proteins: genetics /
                      Zebrafish Proteins: metabolism / Amyloid beta-Protein
                      Precursor (NLM Chemicals) / Glypicans (NLM Chemicals) /
                      Membrane Proteins (NLM Chemicals) / Plxna3 protein,
                      zebrafish (NLM Chemicals) / Proteome (NLM Chemicals) /
                      Receptors, Cell Surface (NLM Chemicals) / Zebrafish Proteins
                      (NLM Chemicals) / Aspartic Acid Endopeptidases (NLM
                      Chemicals)},
      cin          = {AG Lichtenthaler / AG Haass old / Zebrafish Models ; AG
                      Schmid ; AG Schmid München},
      ddc          = {540},
      cid          = {I:(DE-2719)1110006 / I:(DE-2719)1110007 /
                      I:(DE-2719)1140002},
      pnm          = {342 - Disease Mechanisms and Model Systems (POF3-342)},
      pid          = {G:(DE-HGF)POF3-342},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:23457027},
      doi          = {10.1002/pmic.201200582},
      url          = {https://pub.dzne.de/record/136887},
}