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@ARTICLE{Fluhrer:136321,
      author       = {Fluhrer, Regina and Kamp, Frits and Grammer, Gudula and
                      Nuscher, Brigitte and Steiner, Harald and Beyer, Klaus and
                      Haass, Christian},
      title        = {{T}he {N}icastrin ectodomain adopts a highly thermostable
                      structure.},
      journal      = {Biological chemistry},
      volume       = {392},
      number       = {11},
      issn         = {1437-4315},
      address      = {Berlin [u.a.]},
      publisher    = {de Gruyter},
      reportid     = {DZNE-2020-02643},
      pages        = {995–1001},
      year         = {2011},
      abstract     = {Nicastrin is a type I transmembrane glycoprotein, which is
                      part of the high molecular weight γ-secretase complex.
                      γ-Secretase is one of the key players associated with the
                      generation of Alzheimer's disease pathology, since it
                      liberates the neurotoxic amyloid β-peptide. Four proteins
                      Nicastrin, anterior pharynx-defective-1 (Aph-1), presenilin
                      enhancer-2 (Pen-2) and Presenilin are essential to form the
                      active γ-secretase complex. Recently it has been shown,
                      that Nicastrin has a key function in stabilizing the mature
                      γ-secretase complex and may also be involved in substrate
                      recognition. So far no structural data for the Nicastrin
                      ectodomain or any other γ-secretase component are
                      available. We therefore used Circular Dichroism (CD)
                      spectroscopy to demonstrate that Nicastrin, similar to its
                      homologues, the Streptomyces griseus aminopeptidase (SGAP)
                      and the transferrin receptor (TfR), adopts a thermostable
                      secondary structure. Furthermore, the Nicastrin ectodomain
                      has an exceptionally high propensity to refold after thermal
                      denaturation. These findings provide evidence to further
                      support the hypothesis that Nicastrin may share evolutionary
                      conserved properties with the aminopeptidase and the
                      transferrin receptor family.},
      keywords     = {Alzheimer Disease: metabolism / Aminopeptidases: chemistry
                      / Amyloid Precursor Protein Secretases: chemistry / Cell
                      Line / Circular Dichroism / Humans / Membrane Glycoproteins:
                      chemistry / Protein Refolding / Protein Stability / Protein
                      Structure, Secondary / Protein Structure, Tertiary /
                      Receptors, Transferrin: chemistry / Streptomyces griseus:
                      enzymology / Temperature / Membrane Glycoproteins (NLM
                      Chemicals) / Receptors, Transferrin (NLM Chemicals) /
                      nicastrin protein (NLM Chemicals) / Amyloid Precursor
                      Protein Secretases (NLM Chemicals) / Aminopeptidases (NLM
                      Chemicals)},
      cin          = {AG Fluhrer / AG Steiner / AG Haass},
      ddc          = {570},
      cid          = {I:(DE-2719)1110000-2 / I:(DE-2719)1110000-1 /
                      I:(DE-2719)1110007},
      pnm          = {342 - Disease Mechanisms and Model Systems (POF3-342)},
      pid          = {G:(DE-HGF)POF3-342},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:21848507},
      doi          = {10.1515/BC.2011.169},
      url          = {https://pub.dzne.de/record/136321},
}