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@ARTICLE{Biella:138753,
      author       = {Biella, Gloria and Fusco, Federica and Nardo, Emanuele and
                      Bernocchi, Ottavia and Colombo, Alessio and Lichtenthaler,
                      Stefan F and Forloni, Gianluigi and Albani, Diego},
      title        = {{S}irtuin 2 {I}nhibition {I}mproves {C}ognitive
                      {P}erformance and {A}cts on {A}myloid-β {P}rotein
                      {P}recursor {P}rocessing in {T}wo {A}lzheimer's {D}isease
                      {M}ouse {M}odels.},
      journal      = {Journal of Alzheimer's disease},
      volume       = {53},
      number       = {3},
      issn         = {1387-2877},
      address      = {Amsterdam},
      publisher    = {IOS Press},
      reportid     = {DZNE-2020-05075},
      pages        = {1193-1207},
      year         = {2016},
      abstract     = {The neuropathological hallmarks of Alzheimer's disease (AD)
                      are extracellular plaques built up by the accumulation of
                      the amyloid-β protein precursor (AβPP)-derived peptide β
                      (Aβ), and intracellular tangles of hyperphosphorylated tau
                      protein. Sirtuin 2 (SIRT2) is a member of the sirtuin
                      family, featuring conserved enzymes with deacetylase
                      activity and involved in several cell molecular pathways. We
                      investigated the importance of SIRT2 inhibition in AD. We
                      inhibited SIRT2 by small molecules (AGK-2, AK-7) and
                      examined AβPP metabolism in H4-SW neuroglioma cells
                      overexpressing AβPP and two AD transgenic mouse models
                      (3xTg-AD and APP23). The in vitro studies suggested that the
                      inhibition of SIRT2 reduced Aβ production; in vivo data
                      showed an improvement of cognitive performance in the novel
                      object recognition test, and an effect on AβPP proteolytic
                      processing leading to a reduction of soluble β-AβPP and an
                      increase of soluble α-AβPP protein. In 3xTg-AD mice, we
                      noticed that total tau protein level rose. Overall, our
                      pre-clinical data support a role for SIRT2 inhibition in the
                      improvement of cognitive performance and the modulation of
                      molecular mechanisms relevant for AD, thus deserving
                      attention as possible therapeutic strategy.},
      keywords     = {Alzheimer Disease: complications / Alzheimer Disease:
                      genetics / Alzheimer Disease: pathology / Amyloid
                      beta-Peptides: metabolism / Amyloid beta-Protein Precursor:
                      genetics / Amyloid beta-Protein Precursor: metabolism /
                      Animals / Benzamides: pharmacology / Benzamides: therapeutic
                      use / Brain: drug effects / Brain: metabolism /
                      Calcium-Binding Proteins: metabolism / Cell Line, Tumor /
                      Cognition Disorders: drug therapy / Cognition Disorders:
                      etiology / Cognition Disorders: metabolism / Cognition
                      Disorders: pathology / Disease Models, Animal / Enzyme
                      Inhibitors: pharmacology / Enzyme Inhibitors: therapeutic
                      use / Furans: pharmacology / Furans: therapeutic use / Gene
                      Expression Regulation: drug effects / Gene Expression
                      Regulation: genetics / Glial Fibrillary Acidic Protein:
                      metabolism / Glioma: pathology / Mice / Mice, Inbred C57BL /
                      Mice, Transgenic / Microfilament Proteins: metabolism /
                      Peptide Fragments: metabolism / Phosphorylation: drug
                      effects / Quinolines: pharmacology / Quinolines: therapeutic
                      use / Sirtuin 2: metabolism / Sulfonamides: pharmacology /
                      Sulfonamides: therapeutic use /
                      3-(1-azepanylsulfonyl)-N-(3-bromphenyl)benzamide (NLM
                      Chemicals) / AGK2 compound (NLM Chemicals) / Aif1 protein,
                      mouse (NLM Chemicals) / Amyloid beta-Peptides (NLM
                      Chemicals) / Amyloid beta-Protein Precursor (NLM Chemicals)
                      / Benzamides (NLM Chemicals) / Calcium-Binding Proteins (NLM
                      Chemicals) / Enzyme Inhibitors (NLM Chemicals) / Furans (NLM
                      Chemicals) / Glial Fibrillary Acidic Protein (NLM Chemicals)
                      / Microfilament Proteins (NLM Chemicals) / Peptide Fragments
                      (NLM Chemicals) / Quinolines (NLM Chemicals) / Sulfonamides
                      (NLM Chemicals) / amyloid beta-protein (1-40) (NLM
                      Chemicals) / amyloid beta-protein (1-42) (NLM Chemicals) /
                      Sirtuin 2 (NLM Chemicals)},
      cin          = {AG Lichtenthaler},
      ddc          = {610},
      cid          = {I:(DE-2719)1110006},
      pnm          = {342 - Disease Mechanisms and Model Systems (POF3-342)},
      pid          = {G:(DE-HGF)POF3-342},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:27372638},
      doi          = {10.3233/JAD-151135},
      url          = {https://pub.dzne.de/record/138753},
}