Oleuropein aglycone stabilizes the monomeric α-synuclein and favours the growth of non-toxic aggregates

[1]  G. Sindona,et al.  Synthesis and antioxidant evaluation of lipophilic oleuropein aglycone derivatives. , 2017, Food & function.

[2]  N. A. Santagati,et al.  Antioxidant activity of oleuropein and semisynthetic acetyl‐derivatives determined by measuring malondialdehyde in rat brain , 2017, The Journal of pharmacy and pharmacology.

[3]  S. Murayama,et al.  Prion-Like Seeding of Misfolded α-Synuclein in the Brains of Dementia with Lewy Body Patients in RT-QUIC , 2017, Molecular Neurobiology.

[4]  M. Stefani,et al.  Olive polyphenols: new promising agents to combat aging-associated neurodegeneration , 2017, Expert review of neurotherapeutics.

[5]  D. Krainc,et al.  α-synuclein toxicity in neurodegeneration: mechanism and therapeutic strategies , 2017, Nature Medicine.

[6]  M. Stefani,et al.  Nutraceutical Properties of Olive Oil Polyphenols. An Itinerary from Cultured Cells through Animal Models to Humans , 2016, International journal of molecular sciences.

[7]  S. Doglia,et al.  The polyphenol Oleuropein aglycone hinders the growth of toxic transthyretin amyloid assemblies. , 2016, The Journal of nutritional biochemistry.

[8]  M. Bucciantini,et al.  Molecular insights into cell toxicity of a novel familial amyloidogenic variant of β2‐microglobulin , 2016, Journal of cellular and molecular medicine.

[9]  V. Uversky,et al.  Structural, morphological, and functional diversity of amyloid oligomers , 2015, FEBS letters.

[10]  D. Selkoe,et al.  KTKEGV repeat motifs are key mediators of normal α-synuclein tetramerization: Their mutation causes excess monomers and neurotoxicity , 2015, Proceedings of the National Academy of Sciences.

[11]  M. Giugliano,et al.  α-Synuclein strains cause distinct synucleinopathies after local and systemic administration , 2015, Nature.

[12]  J. Kordower,et al.  The Prion Hypothesis of Parkinson’s Disease , 2015, Current Neurology and Neuroscience Reports.

[13]  M. Dierssen,et al.  Potential Role of Olive Oil Phenolic Compounds in the Prevention of Neurodegenerative Diseases , 2015, Molecules.

[14]  D. Eliezer,et al.  Alpha-Synuclein Function and Dysfunction on Cellular Membranes , 2014, Experimental neurobiology.

[15]  B. Vestergaard,et al.  Protein/lipid coaggregates are formed during α-synuclein-induced disruption of lipid bilayers. , 2014, Biomacromolecules.

[16]  A. Paetau,et al.  A novel α-synuclein mutation A53E associated with atypical multiple system atrophy and Parkinson's disease-type pathology , 2014, Neurobiology of Aging.

[17]  D. Otzen,et al.  How Epigallocatechin Gallate Can Inhibit α-Synuclein Oligomer Toxicity in Vitro♦ , 2014, The Journal of Biological Chemistry.

[18]  F. Gage,et al.  Accumulation of oligomer-prone α-synuclein exacerbates synaptic and neuronal degeneration in vivo. , 2014, Brain : a journal of neurology.

[19]  Patrick Walsh,et al.  The Mechanism of Membrane Disruption by Cytotoxic Amyloid Oligomers Formed by Prion Protein(106–126) Is Dependent on Bilayer Composition* , 2014, The Journal of Biological Chemistry.

[20]  Xavier Salvatella,et al.  Identification of fibril-like tertiary contacts in soluble monomeric α-synuclein. , 2013, Biophysical journal.

[21]  L. Formigli,et al.  A molecular imaging analysis of Cx43 association with Cdo during skeletal myoblast differentiation , 2013, Journal of biophotonics.

[22]  Jiajie Diao,et al.  Properties of native brain α-synuclein , 2013, Nature.

[23]  A. Schapira,et al.  Somatic Alpha-Synuclein Mutations in Parkinson's Disease: Hypothesis and Preliminary Data , 2013, Movement disorders : official journal of the Movement Disorder Society.

[24]  Dhiman Ghosh,et al.  Curcumin modulates α-synuclein aggregation and toxicity. , 2013, ACS chemical neuroscience.

[25]  E. Masliah,et al.  The many faces of α-synuclein: from structure and toxicity to therapeutic target , 2012, Nature Reviews Neuroscience.

[26]  Christopher M. Dobson,et al.  Direct Observation of the Interconversion of Normal and Toxic Forms of α-Synuclein , 2012, Cell.

[27]  F. Chiti,et al.  Protein misfolded oligomers: experimental approaches, mechanism of formation, and structure-toxicity relationships. , 2012, Chemistry & biology.

[28]  Lisa J. Lapidus,et al.  Curcumin Prevents Aggregation in α-Synuclein by Increasing Reconfiguration Rate* , 2012, The Journal of Biological Chemistry.

[29]  M. Bucciantini,et al.  Aβ(1-42) aggregates into non-toxic amyloid assemblies in the presence of the natural polyphenol oleuropein aglycon. , 2011, Current Alzheimer research.

[30]  G. Lippens,et al.  Oleuropein and derivatives from olives as Tau aggregation inhibitors , 2011, Neurochemistry International.

[31]  M. Motilva,et al.  Metabolites involved in oleuropein accumulation and degradation in fruits of Olea europaea L.: Hojiblanca and Arbequina varieties. , 2010, Journal of agricultural and food chemistry.

[32]  T. Südhof,et al.  α-Synuclein Promotes SNARE-Complex Assembly in Vivo and in Vitro , 2010, Science.

[33]  M. Bucciantini,et al.  Oleuropein aglycon prevents cytotoxic amyloid aggregation of human amylin. , 2010, The Journal of nutritional biochemistry.

[34]  D. Zack,et al.  Baicalein reduces E46K α‐synuclein aggregation in vitro and protects cells against E46K α‐synuclein toxicity in cell models of familiar Parkinsonism , 2010, Journal of neurochemistry.

[35]  S. Omar Oleuropein in Olive and its Pharmacological Effects , 2010, Scientia pharmaceutica.

[36]  D. Ehrnhoefer,et al.  EGCG remodels mature α-synuclein and amyloid-β fibrils and reduces cellular toxicity , 2010, Proceedings of the National Academy of Sciences.

[37]  L. Bubacco,et al.  Molecular insights into the interaction between alpha-synuclein and docosahexaenoic acid. , 2009, Journal of molecular biology.

[38]  Michael Wolff,et al.  Seeding induced by α‐synuclein oligomers provides evidence for spreading of α‐synuclein pathology , 2009, Journal of neurochemistry.

[39]  K. Matsuzaki,et al.  Ganglioside‐induced amyloid formation by human islet amyloid polypeptide in lipid rafts , 2009, FEBS letters.

[40]  M. Farrer,et al.  In vivo silencing of alpha-synuclein using naked siRNA , 2008, Molecular neurodegeneration.

[41]  V. Uversky,et al.  Structural characteristics of alpha-synuclein oligomers stabilized by the flavonoid baicalein. , 2008, Journal of molecular biology.

[42]  D. Ehrnhoefer,et al.  EGCG redirects amyloidogenic polypeptides into unstructured, off-pathway oligomers , 2008, Nature Structural &Molecular Biology.

[43]  Wim Jiskoot,et al.  Extrinsic Fluorescent Dyes as Tools for Protein Characterization , 2008, Pharmaceutical Research.

[44]  Vladimir N. Uversky,et al.  Neuropathology, biochemistry, and biophysics of α‐synuclein aggregation , 2007 .

[45]  Mireille Dumoulin,et al.  Identification of the core structure of lysozyme amyloid fibrils by proteolysis. , 2006, Journal of molecular biology.

[46]  T. Iwatsubo,et al.  Small Molecule Inhibitors of α-Synuclein Filament Assembly† , 2006 .

[47]  C. Dobson,et al.  Mapping long-range interactions in alpha-synuclein using spin-label NMR and ensemble molecular dynamics simulations. , 2005, Journal of the American Chemical Society.

[48]  Shubo Han,et al.  The Flavonoid Baicalein Inhibits Fibrillation of α-Synuclein and Disaggregates Existing Fibrils* , 2004, Journal of Biological Chemistry.

[49]  V. Subramaniam,et al.  NMR of α‐synuclein–polyamine complexes elucidates the mechanism and kinetics of induced aggregation , 2004, The EMBO journal.

[50]  C. Dobson,et al.  Protein aggregation and amyloid fibril formation by an SH3 domain probed by limited proteolysis. , 2003, Journal of molecular biology.

[51]  Janel O. Johnson,et al.  α-Synuclein Locus Triplication Causes Parkinson's Disease , 2003, Science.

[52]  Reinhard Jahn,et al.  A Broken α-Helix in Folded α-Synuclein* , 2003, The Journal of Biological Chemistry.

[53]  P. Lansbury,et al.  Alpha-synuclein, especially the Parkinson's disease-associated mutants, forms pore-like annular and tubular protofibrils. , 2002, Journal of molecular biology.

[54]  V. Uversky,et al.  Evidence for a Partially Folded Intermediate in α-Synuclein Fibril Formation* , 2001, The Journal of Biological Chemistry.

[55]  D. Eliezer,et al.  Conformational properties of alpha-synuclein in its free and lipid-associated states. , 2001, Journal of molecular biology.

[56]  P. Lansbury,et al.  Fibrils formed in vitro from alpha-synuclein and two mutant forms linked to Parkinson's disease are typical amyloid. , 2000, Biochemistry.

[57]  J. Trojanowski,et al.  A panel of epitope‐specific antibodies detects protein domains distributed throughout human α‐synuclein in lewy bodies of Parkinson's disease , 2000, Journal of neuroscience research.

[58]  M. Spillantini Parkinson's disease, dementia with Lewy bodies and multiple system atrophy are alpha-synucleinopathies. , 1999, Parkinsonism & related disorders.

[59]  J Q Trojanowski,et al.  Axon pathology in Parkinson's disease and Lewy body dementia hippocampus contains alpha-, beta-, and gamma-synuclein. , 1999, Proceedings of the National Academy of Sciences of the United States of America.

[60]  R. Krüger,et al.  Genetic dissection of familial Parkinson's disease. , 1998, Molecular medicine today.

[61]  R. Crowther,et al.  α-Synuclein in filamentous inclusions of Lewy bodies from Parkinson’s disease and dementia with Lewy bodies , 1998 .

[62]  Robert L. Nussbaum,et al.  Mutation in the α-Synuclein Gene Identified in Families with Parkinson's Disease , 1997 .

[63]  P. Lansbury,et al.  NACP, a protein implicated in Alzheimer's disease and learning, is natively unfolded. , 1996, Biochemistry.

[64]  E. Masliah,et al.  Molecular cloning of cDNA encoding an unrecognized component of amyloid in Alzheimer disease. , 1993, Proceedings of the National Academy of Sciences of the United States of America.

[65]  G. Anantharamaiah,et al.  The amphipathic helix in the exchangeable apolipoproteins: a review of secondary structure and function. , 1992, Journal of lipid research.

[66]  P. V. von Hippel,et al.  Calculation of protein extinction coefficients from amino acid sequence data. , 1989, Analytical biochemistry.

[67]  T. Mosmann Rapid colorimetric assay for cellular growth and survival: application to proliferation and cytotoxicity assays. , 1983, Journal of immunological methods.

[68]  W. Ebeling,et al.  Proteinase K from Tritirachium album Limber. , 1974, European journal of biochemistry.

[69]  A. Diaspro,et al.  Amyloid and membrane complexity: The toxic interplay revealed by AFM. , 2018, Seminars in cell & developmental biology.

[70]  S. Maeda,et al.  IVbteA Modified Colorimetric MTT Assay Adapted fbr Application to Proliferation and Cytotoxicity Assays , 2018 .

[71]  Anthony H V Schapira,et al.  Neurobiology and treatment of Parkinson's disease. , 2009, Trends in pharmacological sciences.

[72]  P. Picotti,et al.  Probing protein structure by limited proteolysis. , 2004, Acta biochimica Polonica.

[73]  J. Trojanowski,et al.  Axon pathology in Parkinson ’ s disease and Lewy body dementia hippocampus contains a-, b-, and g-synuclein , 1999 .

[74]  H. Levine Quantification of beta-sheet amyloid fibril structures with thioflavin T. , 1999, Methods in enzymology.

[75]  R A Crowther,et al.  alpha-Synuclein in filamentous inclusions of Lewy bodies from Parkinson's disease and dementia with lewy bodies. , 1998, Proceedings of the National Academy of Sciences of the United States of America.