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@ARTICLE{Mentrup:139570,
      author       = {Mentrup, Torben and Loock, Ann-Christine and Fluhrer,
                      Regina and Schröder, Bernd},
      title        = {{S}ignal peptide peptidase and {SPP}-like proteases -
                      {P}ossible therapeutic targets?},
      journal      = {Biochimica et biophysica acta / Molecular cell research},
      volume       = {1864},
      number       = {11},
      issn         = {0167-4889},
      address      = {Amsterdam [u.a.]},
      publisher    = {Elsevier},
      reportid     = {DZNE-2020-05892},
      pages        = {2169-2182},
      year         = {2017},
      abstract     = {Signal peptide peptidase (SPP) and the four homologous
                      SPP-like proteases SPPL2a, SPPL2b, SPPL2c and SPPL3 are
                      GxGD-type intramembrane-cleaving proteases (I-CLIPs). In
                      addition to divergent subcellular localisations, distinct
                      differences in the mechanistic properties and substrate
                      requirements of individual family members have been
                      unravelled. SPP/SPPL proteases employ a catalytic mechanism
                      related to that of the γ-secretase complex. Nevertheless,
                      differential targeting of SPP/SPPL proteases and
                      γ-secretase by inhibitors has been demonstrated.
                      Furthermore, also within the SPP/SPPL family significant
                      differences in the sensitivity to currently available
                      inhibitory compounds have been reported. Though far from
                      complete, our knowledge on pathophysiological functions of
                      SPP/SPPL proteases, in particular based on studies in mice,
                      has been significantly increased over the last years. Based
                      on this, inhibition of distinct SPP/SPPL proteases has been
                      proposed as a novel therapeutic concept e.g. for the
                      treatment of autoimmunity and viral or protozoal infections,
                      as we will discuss in this review. This article is part of a
                      Special Issue entitled: Proteolysis as a Regulatory Event in
                      Pathophysiology edited by Stefan Rose-John.},
      subtyp        = {Review Article},
      keywords     = {Amino Acid Sequence: genetics / Amyloid Precursor Protein
                      Secretases: antagonists $\&$ inhibitors / Amyloid Precursor
                      Protein Secretases: genetics / Aspartic Acid Endopeptidases:
                      antagonists $\&$ inhibitors / Aspartic Acid Endopeptidases:
                      genetics / Humans / Membrane Proteins: antagonists $\&$
                      inhibitors / Membrane Proteins: genetics / Peptides:
                      antagonists $\&$ inhibitors / Peptides: genetics / Peptides:
                      metabolism / Proteolysis / Substrate Specificity / Membrane
                      Proteins (NLM Chemicals) / Peptides (NLM Chemicals) /
                      dermcidin (NLM Chemicals) / Amyloid Precursor Protein
                      Secretases (NLM Chemicals) / Aspartic Acid Endopeptidases
                      (NLM Chemicals) / SPPL2a protein, human (NLM Chemicals) /
                      SPPL2b protein, human (NLM Chemicals)},
      cin          = {AG Fluhrer},
      ddc          = {570},
      cid          = {I:(DE-2719)1110000-2},
      pnm          = {342 - Disease Mechanisms and Model Systems (POF3-342)},
      pid          = {G:(DE-HGF)POF3-342},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:28624439},
      doi          = {10.1016/j.bbamcr.2017.06.007},
      url          = {https://pub.dzne.de/record/139570},
}