Oleuropein aglycone stabilizes the monomeric α-synuclein and favours the growth of non-toxic aggregates
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M. Bucciantini | M. Stefani | Giovanni Bisello | P. Polverino de Laureto | M. Leri | L. Palazzi | E. Bruzzone | Giovanni Bisello
[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.