Christine Pountney Bibliography Mla


The deposition of amyloid in brain tissue in the context of neurodegenerative diseases involves the formation of intermediate species—termed oligomers—of lower molecular mass and with structures that deviate from those of mature amyloid fibrils. Because these oligomers are thought to be primarily responsible for the subsequent disease pathogenesis, the elucidation of their structure is of enormous interest. Nevertheless, because of the high aggregation propensity and the polydispersity of oligomeric species formed by the proteins or peptides in question, the preparation of appropriate samples for high-resolution structural methods has proven to be rather difficult. This is why theoretical approaches have been of particular importance in gaining insights into possible oligomeric structures for some time. Only recently has it been possible to achieve some progress with regard to the experimentally based structural characterization of defined oligomeric species. Here we discuss how theory and experiment are used to determine oligomer structures and what can be done to improve the integration of the two disciplines.

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  • Synthesis of a Bis-thio-acetone (BTA) Analogue of the Lysine Isopeptide Bond and its Application to Investigate the Effects of Ubiquitination and SUMOylation on α-Synuclein Aggregation and Toxicity

    Yuka E.LewisTharindumalaAbeywardanaYu HsuanLinAnaGalesicMatthew R.Pratt

    ACS Chemical Biology201611 (4), 931-942

    Abstract | Full Text HTML | PDF | PDF w/ Links

  • Extranuclear SUMOylation in Neurons

    Jeremy M.HenleyRuth E.CarmichaelKevin A.Wilkinson

    Trends in Neurosciences2018,

  • Failed mitochondrial import and impaired proteostasis trigger SUMOylation of mitochondrial proteins

    FlorianPaaschFabianden BraveIvanPsakhyeBorisPfanderStefanJentsch

    Journal of Biological Chemistry2018293 (2), 599-609

  • Post translational modification of Parkin


    Biology Direct201712 (1),

  • O-GlcNAc modification inhibits the calpain-mediated cleavage of α-synuclein

    Paul M.LevineCesar A.De LeonAnaGalesicAaronBalanaNicholas P.MarottaYuka E.LewisMatthew R.Pratt

    Bioorganic & Medicinal Chemistry201725 (18), 4977-4982

  • Glycation, glycolysis, and neurodegenerative diseases: Is there any connection?

    V. I.MuronetzA. K.MelnikovaZ. N.SeferbekovaK. V.BarinovaE. V.Schmalhausen

    Biochemistry (Moscow)201782 (8), 874-886

  • α-synuclein aggregation and its modulation

    DhimanGhoshSurabhiMehraShrutiSahayPradeep K.SinghSamir K.Maji

    International Journal of Biological Macromolecules2017100, 37-54

  • Hypothermia exerts early neuroprotective effects involving protein conjugation of SUMO-2/3 in a rat model of middle cerebral artery occlusion


    Molecular Medicine Reports201716 (3), 3217-3223

  • Sumoylation: Implications for Neurodegenerative Diseases

    Dina B.AndersonCamila A.ZanellaJeremy M.HenleyHelenaCimarosti


  • Ubiquitin-dependent and independent roles of SUMO in proteostasis

    FraukeLiebeltAlfred C. O.Vertegaal

    American Journal of Physiology-Cell Physiology2016311 (2), C284-C296

  • SUMO-regulated mitochondrial function in Parkinson's disease

    Ana CristinaGuerra de SouzaRui DanielPredigerHelenaCimarosti

    Journal of Neurochemistry2016137 (5), 673-686

  • Lysines, Achilles’ heel in alpha-synuclein conversion to a deadly neuronal endotoxin


    Ageing Research Reviews201626, 62-71

  • Inhibition effects of tanshinone on the aggregation of α-synuclein


    Food & Function20167 (1), 409-416

  • Synthetic Proteins and Peptides for the Direct Interrogation of α-Synuclein Posttranslational Modifications


    Biomolecules20155 (4), 1210-1227

  • Direct and/or Indirect Roles for SUMO in Modulating Alpha-Synuclein Toxicity


    Biomolecules20155 (4), 1697-1716

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