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Review: Sporadic Parkinson's disease: development and distribution ofα‐synuclein pathology

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Interaction of α-Synuclein with Divalent Metal Ions Reveals Key Differences: A Link between Structure, Binding Specificity and Fibrillation Enhancement

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α-Synuclein–induced lysosomal dysfunction occurs through disruptions in protein trafficking in human midbrain synucleinopathy models

Mazzulli, J. R., Zunke, F., Ole Isacson, A., Studer, L., & Krainc, D. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1520335113 · Cited by 382 · see citing works

Mechanisms of α-Synuclein Induced Synaptopathy in Parkinson's Disease

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De novo designed peptide-based amyloid fibrils

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α-synuclein in the pathophysiology of Alzheimer’s disease

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Multiple Tight Phospholipid-Binding Modes of α-Synuclein Revealed by Solution NMR Spectroscopy

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The E46K Mutation in α-Synuclein Increases Amyloid Fibril Formation

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Ubiquitination of α-Synuclein in Lewy Bodies Is a Pathological Event Not Associated with Impairment of Proteasome Function

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Role of α-Synuclein Carboxy-Terminus on Fibril Formation in Vitro

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Misfolded proteinase K–resistant hyperphosphorylated α-synuclein in aged transgenic mice with locomotor deterioration and in human α-synucleinopathies

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Lipid droplets: a classic organelle with new outfits

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Two new polymorphic structures of human full-length alpha-synuclein fibrils solved by cryo-electron microscopy

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Ferroptosis and cell death mechanisms in Parkinson's disease

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Targeting Alpha-Synuclein as a Therapy for Parkinson’s Disease

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Seeded Aggregation and Toxicity of α-Synuclein and Tau

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Structural Organization of α-Synuclein Fibrils Studied by Site-directed Spin Labeling

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Intramuscular injection of α-synuclein induces CNS α-synuclein pathology and a rapid-onset motor phenotype in transgenic mice

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Lewy Body-like α-Synuclein Aggregates Resist Degradation and Impair Macroautophagy

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α‐Synuclein and Parkinson's disease

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Formation and Removal of α-Synuclein Aggregates in Cells Exposed to Mitochondrial Inhibitors

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Aggregated α-Synuclein Mediates Dopaminergic Neurotoxicity In Vivo

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α-Synuclein and dopamine at the crossroads of Parkinson's disease

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Alpha-synuclein: from secretion to dysfunction and death

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The vermiform appendix impacts the risk of developing Parkinson’s disease

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Reversible Inhibition of α-Synuclein Fibrillization by Dopaminochrome-mediated Conformational Alterations

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Role of Nitric Oxide Synthases in Parkinson’s Disease: A Review on the Antioxidant and Anti-inflammatory Activity of Polyphenols

Aquilano, K., Baldelli, S., Rotilio, G., & Ciriolo, M. R. (2008) · Neurochemical Research · doi:10.1007/s11064-008-9697-6 · Cited by 267 · see citing works

Part II: α-synuclein and its molecular pathophysiological role in neurodegenerative disease

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Alpha-Synuclein Aggregation in Parkinson's Disease

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Biochemical Characterization of the Core Structure of α-Synuclein Filaments

Miake, H., Mizusawa, H., Iwatsubo, T., & Hasegawa, M. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m110551200 · Cited by 255 · see citing works

Residual Structure and Dynamics in Parkinson's Disease-associated Mutants of α-Synuclein

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Molecular pathogenesis of Parkinson's disease

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NMR of α‐synuclein–polyamine complexes elucidates the mechanism and kinetics of induced aggregation

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Propagation of alpha-synuclein pathology: hypotheses, discoveries, and yet unresolved questions from experimental and human brain studies

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Relationships between the Sequence of α-Synuclein and its Membrane Affinity, Fibrillization Propensity, and Yeast Toxicity

Volles, M. J., & Lansbury, P. T. (2006) · Journal of Molecular Biology · doi:10.1016/j.jmb.2006.12.044 · Cited by 247 · see citing works

Toxic prefibrillar α-synuclein amyloid oligomers adopt a distinctive antiparallel β-sheet structure

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Role of α-Synuclein in Inducing Innate and Adaptive Immunity in Parkinson Disease

Allen Reish, H. E., & Standaert, D. G. (2015) · Journal of Parkinson’s Disease · doi:10.3233/jpd-140491 · Cited by 244 · see citing works

Molecular mechanisms of α-synuclein neurodegeneration

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Selective Insolubility of α-Synuclein in Human Lewy Body Diseases Is Recapitulated in a Transgenic Mouse Model

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Alpha-Synuclein in Parkinson’s Disease: From Pathogenetic Dysfunction to Potential Clinical Application

Xu, L., & Pu, J. (2016) · Parkinson s Disease · doi:10.1155/2016/1720621 · Cited by 237 · see citing works

Investigation of α-Synuclein Fibril Structure by Site-directed Spin Labeling

Chen, M., Margittai, M., Chen, J., & Langen, R. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m700368200 · Cited by 233 · see citing works

Specificity and Regulation of Casein Kinase-Mediated Phosphorylation of ??-Synuclein

Waxman, E. A., & Giasson, B. I. (2008) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/nen.0b013e3186fc995 · Cited by 232 · see citing works

α-Synuclein activates stress signaling protein kinases in THP-1 cells and microglia

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Differential Phospholipid Binding of α-Synuclein Variants Implicated in Parkinson’s Disease Revealed by Solution NMR Spectroscopy

Bodner, C. R., Maltsev, A. S., Dobson, C. M., & Bax, A. (2009) · Biochemistry · doi:10.1021/bi901723p · Cited by 227 · see citing works

Reversible Conformational Conversion of α-Synuclein into Toxic Assemblies by Glucosylceramide

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In Vivo Cross-linking Reveals Principally Oligomeric Forms of α-Synuclein and β-Synuclein in Neurons and Non-neural Cells

Dettmer, U., Newman, A. J., Luth, E. S., Bartels, T., & Selkoe, D. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.403311 · Cited by 221 · see citing works

Nitration of Tau Protein Is Linked to Neurodegeneration in Tauopathies

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Impact of N-Terminal Acetylation of α-Synuclein on Its Random Coil and Lipid Binding Properties

Maltsev, A. S., Ying, J., & Bax, A. (2012) · Biochemistry · doi:10.1021/bi300642h · Cited by 217 · see citing works

Tyrosine and serine phosphorylation of α-synuclein have opposing effects on neurotoxicity and soluble oligomer formation

Chen, L., Periquet, M., Wang, X., Negro, A., McLean, P. J., Hyman, B. T., & Feany, M. Β. (2009) · Journal of Clinical Investigation · doi:10.1172/jci39088 · Cited by 213 · see citing works

Structure based aggregation studies reveal the presence of helix-rich intermediate during α-Synuclein aggregation

Ghosh, D., Singh, P. K., Sahay, S., Jha, N. N., Jacob, R. S., Sen, S., Kumar, A., Riek, R., & Maji, S. K. (2015) · Scientific Reports · doi:10.1038/srep09228 · Cited by 213 · see citing works

Mapping hydrophobicity at the nanoscale: Applications to heterogeneous surfaces and proteins

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Characterization of Hydrophobic Residue Requirements for α-Synuclein Fibrillization

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A Peptide Motif Consisting of Glycine, Alanine, and Valine Is Required for the Fibrillization and Cytotoxicity of Human α-Synuclein

Du, H., Tang, L., Luo, X., Li, H., Hu, J., Zhou, J., & Hu, H. (2003) · Biochemistry · doi:10.1021/bi034028+ · Cited by 155 · see citing works

Sequence determinants regulating fibrillation of human α-synuclein

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Sequence Determinants for Amyloid Fibrillogenesis of Human α-Synuclein

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A de novo designed α-helical peptide forms amyloid fibrils which are not neurotoxic

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