Molecular and Biological Compatibility with Host Alpha-Synuclein Influences Fibril Pathogenicity.

[1]  V. Subramaniam,et al.  Conformational Compatibility Is Essential for Heterologous Aggregation of α-Synuclein. , 2016, ACS chemical neuroscience.

[2]  D. Selkoe,et al.  New insights into cellular α-synuclein homeostasis in health and disease , 2016, Current Opinion in Neurobiology.

[3]  Elliott W. Dirr,et al.  Intrastriatal injection of pre-formed mouse α-synuclein fibrils into rats triggers α-synuclein pathology and bilateral nigrostriatal degeneration , 2015, Neurobiology of Disease.

[4]  T. Südhof,et al.  Propagation of prions causing synucleinopathies in cultured cells , 2015, Proceedings of the National Academy of Sciences.

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

[6]  R. Tycko.  Amyloid Polymorphism: Structural Basis and Neurobiological Relevance , 2015, Neuron.

[7]  Vivek K Unni,et al.  Progressive aggregation of alpha-synuclein and selective degeneration of Lewy inclusion-bearing neurons in a mouse model of parkinsonism , 2015, Cell reports.

[8]  K. Luk,et al.  Addition of exogenous α-synuclein preformed fibrils to primary neuronal cultures to seed recruitment of endogenous α-synuclein to Lewy body and Lewy neurite–like aggregates , 2014, Nature Protocols.

[9]  J. Trojanowski,et al.  α-Synuclein Immunotherapy Blocks Uptake and Templated Propagation of Misfolded α-Synuclein and Neurodegeneration , 2014, Cell reports.

[10]  S. Supattapone.  Synthesis of High Titer Infectious Prions with Cofactor Molecules* , 2014, The Journal of Biological Chemistry.

[11]  E. Bézard,et al.  Lewy body extracts from Parkinson disease brains trigger α‐synuclein pathology and neurodegeneration in mice and monkeys , 2014, Annals of neurology.

[12]  B. Meier,et al.  Structural and functional characterization of two alpha-synuclein strains , 2013, Nature Communications.

[13]  Mathias Jucker,et al.  Self-propagation of pathogenic protein aggregates in neurodegenerative diseases , 2013, Nature.

[14]  Bin Zhang,et al.  Distinct α-Synuclein Strains Differentially Promote Tau Inclusions in Neurons , 2013, Cell.

[15]  Masato Hasegawa,et al.  Prion-like spreading of pathological α-synuclein in brain , 2013, Brain : a journal of neurology.

[16]  P. Brundin,et al.  What’s to like about the prion-like hypothesis for the spreading of aggregated α-synuclein in Parkinson disease? , 2013, Prion.

[17]  J. Trojanowski,et al.  Pathological α-Synuclein Transmission Initiates Parkinson-like Neurodegeneration in Nontransgenic Mice , 2012, Science.

[18]  J. Trojanowski,et al.  Intracerebral inoculation of pathological α-synuclein initiates a rapidly progressive neurodegenerative α-synucleinopathy in mice , 2012, The Journal of experimental medicine.

[19]  C. Sigurdson,et al.  Structure of the β2‐α2 loop and interspecies prion transmission , 2012, FASEB journal : official publication of the Federation of American Societies for Experimental Biology.

[20]  Tapan P. Patel,et al.  Exogenous α-Synuclein Fibrils Induce Lewy Body Pathology Leading to Synaptic Dysfunction and Neuron Death , 2011, Neuron.

[21]  M. Vendruscolo,et al.  The A53T mutation is key in defining the differences in the aggregation kinetics of human and mouse α-synuclein. , 2011, Journal of the American Chemical Society.

[22]  J. Castilla,et al.  Prion Strain Mutation Determined by Prion Protein Conformational Compatibility and Primary Structure , 2010, Science.

[23]  J. Trojanowski,et al.  Exogenous α-synuclein fibrils seed the formation of Lewy body-like intracellular inclusions in cultured cells , 2009, Proceedings of the National Academy of Sciences.

[24]  M. Bertelsen,et al.  Threonine 53 in alpha-synuclein is conserved in long-living non-primate animals. , 2009, Biochemical and biophysical research communications.

[25]  Brian Spencer,et al.  Inclusion formation and neuronal cell death through neuron-to-neuron transmission of α-synuclein , 2009, Proceedings of the National Academy of Sciences.

[26]  Nathan J. Cobb,et al.  Prion diseases and their biochemical mechanisms. , 2009, Biochemistry.

[27]  E. Waxman,et al.  Characterization of antibodies that selectively detect α-synuclein in pathological inclusions , 2008, Acta Neuropathologica.

[28]  John Collinge,et al.  A General Model of Prion Strains and Their Pathogenicity , 2007, Science.

[29]  S. Lindquist,et al.  Prion recognition elements govern nucleation, strain specificity and species barriers , 2007, Nature.

[30]  J. Trojanowski,et al.  Mechanisms of Parkinson's Disease Linked to Pathological α-Synuclein: New Targets for Drug Discovery , 2006, Neuron.

[31]  E. M. Jones,et al.  Fibril Conformation as the Basis of Species- and Strain-Dependent Seeding Specificity of Mammalian Prion Amyloids , 2005, Cell.

[32]  C. Griesinger,et al.  Release of long-range tertiary interactions potentiates aggregation of natively unstructured alpha-synuclein. , 2005, Proceedings of the National Academy of Sciences of the United States of America.

[33]  H. Braak,et al.  Staging of brain pathology related to sporadic Parkinson’s disease , 2003, Neurobiology of Aging.

[34]  T. Iwatsubo,et al.  Biochemical Characterization of the Core Structure of α-Synuclein Filaments* , 2002, The Journal of Biological Chemistry.

[35]  E. Masliah,et al.  α-Synuclein is phosphorylated in synucleinopathy lesions , 2002, Nature Cell Biology.

[36]  T. Iwatsubo,et al.  Biochemical characterization of the core structure of alpha-synuclein filaments. , 2002, The Journal of biological chemistry.

[37]  E. Masliah,et al.  alpha-Synuclein is phosphorylated in synucleinopathy lesions. , 2002, Nature cell biology.

[38]  J Q Trojanowski,et al.  A Hydrophobic Stretch of 12 Amino Acid Residues in the Middle of α-Synuclein Is Essential for Filament Assembly* , 2001, The Journal of Biological Chemistry.

[39]  M. Citron,et al.  Parkinson's Disease-associated α-Synuclein Is More Fibrillogenic than β- and γ-Synuclein and Cannot Cross-seed Its Homologs* , 2000, The Journal of Biological Chemistry.

[40]  P. Lansbury,et al.  Amyloid fibrillogenesis: themes and variations. , 2000, Current opinion in structural biology.

[41]  Heidi Phillips,et al.  Mice Lacking α-Synuclein Display Functional Deficits in the Nigrostriatal Dopamine System , 2000, Neuron.

[42]  J. Weissman,et al.  Molecular Basis of a Yeast Prion Species Barrier , 2000, Cell.

[43]  D. Sulzer,et al.  Mice lacking alpha-synuclein display functional deficits in the nigrostriatal dopamine system. , 2000, Neuron.

[44]  M. Citron,et al.  alpha-synuclein fibrillogenesis is nucleation-dependent. Implications for the pathogenesis of Parkinson's disease. , 1999, The Journal of biological chemistry.

[45]  S. Prusiner,et al.  Propagation of prions with artificial properties in transgenic mice expressing chimeric PrP genes , 1993, Cell.