Modification of C Terminus Provides New Insights into the Mechanism of α-Synuclein Aggregation.

[1]  Vinod Subramaniam,et al.  Distinct Mechanisms Determine α-Synuclein Fibril Morphology during Growth and Maturation. , 2017, ACS chemical neuroscience.

[2]  Virginia Chu,et al.  A Novel Microfluidic Cell Co-culture Platform for the Study of the Molecular Mechanisms of Parkinson's Disease and Other Synucleinopathies , 2016, Front. Neurosci..

[3]  Jeremy S. Lee,et al.  Novel Dimer Compounds That Bind α-Synuclein Can Rescue Cell Growth in a Yeast Model Overexpressing α-Synuclein. A Possible Prevention Strategy for Parkinson's Disease. , 2016, ACS chemical neuroscience.

[4]  T. Aartsma,et al.  The effect of fluorescent labeling on α-synuclein fibril morphology. , 2016, Biochimica et biophysica acta.

[5]  R. Heeren,et al.  The Impact of N-terminal Acetylation of α-Synuclein on Phospholipid Membrane Binding and Fibril Structure* , 2016, The Journal of Biological Chemistry.

[6]  H. Akiyama,et al.  The Effect of Fragmented Pathogenic α-Synuclein Seeds on Prion-like Propagation* , 2016, The Journal of Biological Chemistry.

[7]  Abid Oueslati Implication of Alpha-Synuclein Phosphorylation at S129 in Synucleinopathies: What Have We Learned in the Last Decade? , 2016, Journal of Parkinson's disease.

[8]  K. Luk,et al.  Bent out of shape: α‐Synuclein misfolding and the convergence of pathogenic pathways in Parkinson's disease , 2015, FEBS letters.

[9]  A. Steven,et al.  α-Synuclein Amyloid Fibrils with Two Entwined, Asymmetrically Associated Protofibrils* , 2015, The Journal of Biological Chemistry.

[10]  M. Spillantini,et al.  Parkinson's disease as a member of Prion-like disorders. , 2015, Virus research.

[11]  D. Geschwind,et al.  Evidence for α-synuclein prions causing multiple system atrophy in humans with parkinsonism , 2015, Proceedings of the National Academy of Sciences.

[12]  M. Emanuele,et al.  Mechanisms of Alpha-Synuclein Action on Neurotransmission: Cell-Autonomous and Non-Cell Autonomous Role , 2015, Biomolecules.

[13]  D. Willbold,et al.  Single fibril growth kinetics of α-synuclein. , 2015, Journal of molecular biology.

[14]  S. Linse,et al.  On the lag phase in amyloid fibril formation , 2015, Physical chemistry chemical physics : PCCP.

[15]  V. Subramaniam,et al.  Fibril breaking accelerates α-synuclein fibrillization. , 2015, The journal of physical chemistry. B.

[16]  V. Subramaniam,et al.  Solution conditions define morphological homogeneity of α-synuclein fibrils. , 2014, Biochimica et biophysica acta.

[17]  Alexander K. Buell,et al.  Solution conditions determine the relative importance of nucleation and growth processes in α-synuclein aggregation , 2014, Proceedings of the National Academy of Sciences.

[18]  P. Brundin,et al.  A novel α-synuclein-GFP mouse model displays progressive motor impairment, olfactory dysfunction and accumulation of α-synuclein-GFP , 2013, Neurobiology of Disease.

[19]  D. Brady,et al.  Effects of α-Synuclein Overexpression in Transgenic Caenorhabditis elegans Strains , 2012, CNS & neurological disorders drug targets.

[20]  Y. Kawata,et al.  Role of C-terminal negative charges and tyrosine residues in fibril formation of α-synuclein , 2012, Brain and behavior.

[21]  Jonas Fölling,et al.  Imaging nanometer-sized α-synuclein aggregates by superresolution fluorescence localization microscopy. , 2012, Biophysical journal.

[22]  Jonathan A. Fauerbach,et al.  Supramolecular non-amyloid intermediates in the early stages of α-synuclein aggregation. , 2012, Biophysical journal.

[23]  Vladimir N Uversky,et al.  Α-synuclein misfolding and Parkinson's disease. , 2012, Biochimica et biophysica acta.

[24]  Valerie L. Anderson,et al.  Transmission electron microscopy characterization of fluorescently labelled amyloid β 1-40 and α-synuclein aggregates , 2011, BMC biotechnology.

[25]  Yongwon Jung,et al.  Splitting and self-assembling of far-red fluorescent protein with an engineered beta strand peptide: application for alpha-synuclein imaging in mammalian cells. , 2011, Biomaterials.

[26]  H. Ogi,et al.  Ultrasonication-dependent acceleration of amyloid fibril formation. , 2011, Journal of molecular biology.

[27]  C. Dobson,et al.  Conserved C-terminal charge exerts a profound influence on the aggregation rate of α-synuclein. , 2011, Journal of molecular biology.

[28]  T. Jovin,et al.  Confocal Fluorescence Anisotropy and FRAP Imaging of α-Synuclein Amyloid Aggregates in Living Cells , 2011, PloS one.

[29]  Jennifer C. Lee,et al.  Residue-specific fluorescent probes of α-synuclein: detection of early events at the N- and C-termini during fibril assembly. , 2011, Biochemistry.

[30]  R. Tsien,et al.  Fluorescent labeling of tetracysteine-tagged proteins in intact cells , 2010, Nature Protocols.

[31]  Kingshuk Ghosh,et al.  What drives amyloid molecules to assemble into oligomers and fibrils? , 2010, Biophysical journal.

[32]  M. Biancalana,et al.  Molecular mechanism of Thioflavin-T binding to amyloid fibrils. , 2010, Biochimica et biophysica acta.

[33]  Jonathan A. Fauerbach,et al.  Fluorescent ratiometric MFC probe sensitive to early stages of alpha-synuclein aggregation. , 2010, Journal of the American Chemical Society.

[34]  Yves Engelborghs,et al.  Early aggregation steps in alpha-synuclein as measured by FCS and FRET: evidence for a contagious conformational change. , 2010, Biophysical journal.

[35]  C. Dobson,et al.  Towards multiparametric fluorescent imaging of amyloid formation: studies of a YFP model of alpha-synuclein aggregation. , 2010, Journal of molecular biology.

[36]  Vladimir N Uversky,et al.  Biophysics of Parkinson's disease: structure and aggregation of alpha-synuclein. , 2009, Current protein & peptide science.

[37]  V. Subramaniam,et al.  Concentration dependence of alpha-synuclein fibril length assessed by quantitative atomic force microscopy and statistical-mechanical theory. , 2008, Biophysical journal.

[38]  J. Udgaonkar,et al.  Evidence for stepwise formation of amyloid fibrils by the mouse prion protein. , 2008, Journal of molecular biology.

[39]  Henning Stahlberg,et al.  The fold of α-synuclein fibrils , 2008, Proceedings of the National Academy of Sciences.

[40]  Jun Hu,et al.  Assembly of alpha-synuclein fibrils in nanoscale studied by peptide truncation and AFM. , 2008, Biochemical and biophysical research communications.

[41]  J. Hahn,et al.  Dequalinium-Induced Cell Death of Yeast Expressing α-Synuclein-GFP Fusion Protein , 2008, Neurochemical Research.

[42]  Y. Goto,et al.  Seed-dependent accelerated fibrillation of alpha-synuclein induced by periodic ultrasonication treatment. , 2007, Journal of microbiology and biotechnology.

[43]  A. Fink,et al.  Role of Different Regions of α-Synuclein in the Assembly of Fibrils† , 2007 .

[44]  I. Segers-Nolten,et al.  Quantitative Characterization of Protein Nanostructures Using Atomic Force Microscopy , 2007, 2007 29th Annual International Conference of the IEEE Engineering in Medicine and Biology Society.

[45]  T. Jovin,et al.  Fluorescence imaging of amyloid formation in living cells by a functional, tetracysteine-tagged α-synuclein , 2007, Nature Methods.

[46]  M. Fändrich Absolute correlation between lag time and growth rate in the spontaneous formation of several amyloid-like aggregates and fibrils. , 2007, Journal of molecular biology.

[47]  V. Subramaniam,et al.  Quantitative morphological analysis reveals ultrastructural diversity of amyloid fibrils from alpha-synuclein mutants. , 2006, Biophysical journal.

[48]  A. Fink The Aggregation and Fibrillation of α-Synuclein , 2006 .

[49]  M. Gobbi,et al.  Gerstmann-Sträussler-Scheinker Disease Amyloid Protein Polymerizes According to the “Dock-and-Lock” Model* , 2006, Journal of Biological Chemistry.

[50]  E. Masliah,et al.  Lysosomal pathology associated with α‐synuclein accumulation in transgenic models using an eGFP fusion protein , 2005, Journal of neuroscience research.

[51]  V. Subramaniam,et al.  Impact of the acidic C-terminal region comprising amino acids 109-140 on alpha-synuclein aggregation in vitro. , 2004, Biochemistry.

[52]  Adam Douglass,et al.  Mechanism of Prion Propagation: Amyloid Growth Occurs by Monomer Addition , 2004, PLoS biology.

[53]  V. Subramaniam,et al.  Rapid self-assembly of α-synuclein observed by in situ atomic force microscopy , 2004 .

[54]  Ralf Langen,et al.  Structural Organization of α-Synuclein Fibrils Studied by Site-directed Spin Labeling* , 2003, Journal of Biological Chemistry.

[55]  P. Axelsen,et al.  Role of α-Synuclein Carboxy-Terminus on Fibril Formation in Vitro† , 2003 .

[56]  V. Subramaniam,et al.  Cellular Polyamines Promote the Aggregation of α-Synuclein* , 2003, The Journal of Biological Chemistry.

[57]  V. Subramaniam,et al.  Dependence of α-synuclein aggregate morphology on solution conditions , 2002 .

[58]  B. Hyman,et al.  α-Synuclein–enhanced green fluorescent protein fusion proteins form proteasome sensitive inclusions in primary neurons , 2001, Neuroscience.

[59]  J R Ghilardi,et al.  Alzheimer's disease amyloid propagation by a template-dependent dock-lock mechanism. , 2000, Biochemistry.

[60]  H. Lashuel,et al.  Role of post-translational modifications in modulating the structure, function and toxicity of alpha-synuclein: implications for Parkinson's disease pathogenesis and therapies. , 2010, Progress in brain research.