Next-generation active immunization approach for synucleinopathies: implications for Parkinson’s disease clinical trials.
DOI 10.1007/s00401-014-1256-4; Title Next-generation active immunization approach for synucleinopathies: implications for Parkinson’s disease clinical trials Print ISSN 0001-6322 Online ISSN 1432-0533 Publisher Springer Berlin Heidelberg.
Molecular Basis for Preventing α-Synuclein Aggregation by a Molecular Tweezer.
The Journal of Biological Chemistry; doi: 10.1074/jbc.M113.524520.
Comparable Autoantibody Serum Levels against Amyloid- and Inflammation-Associated Proteins in Parkinson’s Disease Patients and Controls.
PLoS ONE; DOI: 10.1371/journal.pone.0088604.
Resistance of naturally secreted -synuclein to proteolysis.
FEBS Journal; doi: 10.1096/fj.13-245852.
Extracellular α-Synuclein Leads to Microtubule Destabilization via GSK-3β-Dependent Tau Phosphorylation in PC12 Cells.
PLOS One; DOI: 10.1371/journal.pone.0094259.
Cu(II) and dopamine bind to α-Synuclein and cause large conformational changes.
FEBS Journal; DOI: 10.1111/febs.12817 (Pay to View).
Aldehyde dehydrogenase 1 defines and protects a nigrostriatal dopaminergic neuron subpopulation.
JCI: The Journal of Clinical Investigation; doi:10.1172/JCI72176..
Multifunctional D2/D3 Agonist D-520 with High in Vivo Efficacy: Modulator of Toxicity of Alpha-Synuclein Aggregates.
ACS Publications; DOI: 10.1021/cn500084x.
The use of nanopore analysis for discovering drugs which bind to α-synuclein for treatment of Parkinson's disease.
Science Direct; DOI: 10.1016/j.ejmech.2014.07.090.
Quantitative Measurement of Intact Alpha-Synuclein Proteoforms from Post-Mortem Control and Parkinson's Disease Brain Tissue by Intact Protein Mass Spectrometry.
Scientific Reports; doi:10.1038/srep05797.