β-Synuclein Inhibits α-Synuclein Aggregation

α-Synuclein in Lewy bodies

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Mutation in the α-Synuclein Gene Identified in Families with Parkinson's Disease

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AlaSOPro mutation in the gene encoding α-synuclein in Parkinson's disease

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A Drosophila model of Parkinson's disease

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High-Level Neuronal Expression of Aβ_1–42in Wild-Type Human Amyloid Protein Precursor Transgenic Mice: Synaptotoxicity without Plaque Formation

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Dopaminergic Loss and Inclusion Body Formation in α-Synuclein Mice: Implications for Neurodegenerative Disorders

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Stabilization of α-Synuclein Secondary Structure upon Binding to Synthetic Membranes

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NACP, A Protein Implicated in Alzheimer's Disease and Learning, Is Natively Unfolded

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Accelerated in vitro fibril formation by a mutant α-synuclein linked to early-onset Parkinson disease

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Molecular cloning of cDNA encoding an unrecognized component of amyloid in Alzheimer disease.

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Identification of two distinct synucleins from human brain

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Fiber diffraction of synthetic α-synuclein filaments shows amyloid-like cross-β conformation

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α-Synuclein Fibrillogenesis Is Nucleation-dependent

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α-Synuclein Promotes Mitochondrial Deficit and Oxidative Stress

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Both Familial Parkinson's Disease Mutations Accelerate α-Synuclein Aggregation

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Amyloid diseases: Abnormal protein aggregation in neurodegeneration

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β-Amyloid peptides enhance α-synuclein accumulation and neuronal deficits in a transgenic mouse model linking Alzheimer's disease and Parkinson's disease

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α-Synuclein Membrane Interactions and Lipid Specificity

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Dityrosine Cross-linking Promotes Formation of Stable α-Synuclein Polymers

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α-Synuclein Shares Physical and Functional Homology with 14-3-3 Proteins

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The A53T α-Synuclein Mutation Increases Iron-Dependent Aggregation and Toxicity

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Interaction of Human α-Synuclein and Parkinson's Disease Variants with Phospholipids

Perrin, R. J., Woods, W. S., Clayton, D. F., & George, J. M. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m004851200 · Cited by 432 · see citing works

Oxidative stress induces amyloid-like aggregate formation of NACP/α-synuclein in vitro

Hashimoto, M., Hsu, L. J., Xia, Y., Takeda, A., Sisk, A., Sundsmo, M., & Masliah, E. (1999) · NeuroReport · doi:10.1097/00001756-199903170-00011 · Cited by 429 · see citing works

Abnormal accumulation of NACP/alpha-synuclein in neurodegenerative disorders.

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Copper(II)-induced self-oligomerization of α-synuclein

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NACP, a presynaptic protein, immunoreactivity in Lewy bodies in Parkinson's disease

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Fatal attractions: abnormal protein aggregation and neuron death in Parkinson's disease and Lewy body dementia

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The core Alzheimer's peptide NAC forms amyloid fibrils which seed and are seeded by β-amyloid: is NAC a common trigger or target in neurodegenerative disease?

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Human recombinant NACP/α-synuclein is aggregated and fibrillated in vitro: Relevance for Lewy body disease

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Levels and Alternative Splicing of Amyloid β Protein Precursor (APP) Transcripts in Brains of APP Transgenic Mice and Humans with Alzheimer's Disease

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Alpha‐synuclein in Lewy Body Disease and Alzheimer's Disease

Hashimoto, M., & Masliah, E. (1999) · Brain Pathology · doi:10.1111/j.1750-3639.1999.tb00552.x · Cited by 251 · see citing works

Oxidative damage and protection by antioxidants in the frontal cortex of Alzheimer’s disease is related to the apolipoprotein E genotype

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Non-A.beta. Component of Alzheimer's Disease Amyloid (NAC) is Amyloidogenic

Iwai, A., Yoshimoto, M., Masliah, E., & Saitoh, T. (1995) · Biochemistry · doi:10.1021/bi00032a006 · Cited by 237 · see citing works

Role of Cytochrome c as a Stimulator of α-Synuclein Aggregation in Lewy Body Disease

Hashimoto, M., Takeda, A., Hsu, L. J., Takenouchi, T., & Masliah, E. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.41.28849 · Cited by 236 · see citing works

Inhibition of Fibrillization and Accumulation of Prefibrillar Oligomers in Mixtures of Human and Mouse α-Synuclein

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Interaction between Aβ(1−42) and Aβ(1−40) in Alzheimer's β-Amyloid Fibril Formation in Vitro

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Wild-type but Not Parkinson's Disease-related Ala-53 → Thr Mutant α-Synuclein Protects Neuronal Cells from Apoptotic Stimuli

da Costa, C. A., Ancolio, K., & Checler, F. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m002413200 · Cited by 212 · see citing works

Overexpression of human α-synuclein causes dopamine neuron death in rat primary culture and immortalized mesencephalon-derived cells

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NACP, the precursor protein of the non-amyloid beta/A4 protein (A beta) component of Alzheimer disease amyloid, binds A beta and stimulates A beta aggregation.

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Expression of mutant alpha-synuclein causes increased susceptibility to dopamine toxicity

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Enhanced vulnerability to oxidative stress by α-synuclein mutations and C-terminal truncation

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Parkinson's Disease-associated α-Synuclein Is More Fibrillogenic than β- and γ-Synuclein and Cannot Cross-seed Its Homologs

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A new brain‐specific 14‐kDa protein is a phosphoprotein

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Stimulation of breast cancer invasion and metastasis by synuclein gamma.

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Altered presynaptic protein NACP is associated with plaque formation and neurodegeneration in Alzheimer's disease.

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Altered expression of the synuclein family mRNA in Lewy body and Alzheimer’s disease

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Binding of Aβ to α- and β-synucleins: identification of segments in α-synuclein/NAC precursor that bind Aβ and NAC

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New magnetic resonance imaging methods for cerebrovascular disease: Emerging clinical applications

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Oxidative stress in Parkinson's disease and other neurodegenerative disorders.

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alpha-Synuclein forms a complex with transcription factor Elk-1

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Residues in the synuclein consensus motif of the α-synuclein fragment, NAC, participate in transglutaminase-catalysed cross-linking to Alzheimer-disease amyloid βA4 peptide

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Synoretin—A New Protein Belonging to the Synuclein Family

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Review: Formation and Properties of Amyloid-like Fibrils Derived from α-Synuclein and Related Proteins

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Properties of NACP/α-synuclein and its role in Alzheimer’s disease

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Reduced Neuritic Outgrowth and Cell Adhesion in Neuronal Cells Transfected with Human α-Synuclein

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Self‐oligomerization of NACP, the precursor protein of the non‐amyloid β/A4 protein (Aβ) component of Alzheimer's disease amyloid, observed in the presence of a C‐terminal Aβ fragment (residues 25–35)

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Recent advances in the understanding of the role of synaptic proteins in Alzheimer's Disease and other neurodegenerative disorders

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Polyglutamine Expansions

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Intracellular Polymerization

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Molecular Pathways of Neurodegeneration in Parkinson's Disease

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-Synuclein in Parkinson's Disease

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MOLECULAR PATHOPHYSIOLOGY OF PARKINSON'S DISEASE

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Kinetic Stabilization of the α-Synuclein Protofibril by a Dopamine-α-Synuclein Adduct

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Increased Expression of α-Synuclein Reduces Neurotransmitter Release by Inhibiting Synaptic Vesicle Reclustering after Endocytosis

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The function of α-synuclein

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Parkinson’s disease: genetics and pathogenesis

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Dopamine-dependent neurotoxicity of α-synuclein: A mechanism for selective neurodegeneration in Parkinson disease

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Dementia with Lewy bodies.

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THE BIOCHEMISTRY OF PARKINSON'S DISEASE

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α-Synuclein misfolding and Parkinson's disease

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Neuropathology of Parkinson disease

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Beclin 1 Gene Transfer Activates Autophagy and Ameliorates the Neurodegenerative Pathology in α-Synuclein Models of Parkinson's and Lewy Body Diseases

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Neuropathology, biochemistry, and biophysics of α‐synuclein aggregation

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The Formation of Highly Soluble Oligomers of α-Synuclein Is Regulated by Fatty Acids and Enhanced in Parkinson's Disease

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Parkin Protects against the Toxicity Associated with Mutant α-Synuclein

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The fold of α-synuclein fibrils

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Effects of α-Synuclein Immunization in a Mouse Model of Parkinson’s Disease

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The Aggregation and Fibrillation of α-Synuclein

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Parkinson’s disease induced pluripotent stem cells with triplication of the α-synuclein locus

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Mechanisms of Parkinson's Disease Linked to Pathological α-Synuclein: New Targets for Drug Discovery

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Amyloid Precursor Protein, Presenilins, and α-Synuclein: Molecular Pathogenesis and Pharmacological Applications in Alzheimer’s Disease

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Biophysical Properties of the Synucleins and Their Propensities to Fibrillate

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Double-knockout mice for α- and β-synucleins: Effect on synaptic functions

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A Structural and Functional Role for 11-mer Repeats in α-Synuclein and Other Exchangeable Lipid Binding Proteins

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Are amyloid diseases caused by protein aggregates that mimic bacterial pore-forming toxins?

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Proteasomal Inhibition by α-Synuclein Filaments and Oligomers

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Aβ40 Inhibits Amyloid Deposition<i>In Vivo</i>

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Pathological roles of α-synuclein in neurological disorders

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