title: Alpha-Synuclein Protein description: Page for Alpha-Synuclein Protein published: true tags: kind:protein, section:proteins, state:published editor: markdown pageId: 7688 dateCreated: “2026-03-06T08:41:39.609Z” dateUpdated: “2026-03-22T10:01:53.007Z” refs: spillantini1997: authors: Spillantini MG, Schmidt ML, Lee VM, et al title: Alpha-synuclein in Lewy bodies year: 1997 doi: 10.1038/42166 braak2003: authors: Braak H, Tredici KD, Rüb U, et al title: Staging of brain pathology related to sporadic Parkinson’s disease year: 2003 doi: 10.1016/s0197-4580(02 stefanis2012: authors: Stefanis L title: Alpha-Synuclein in Parkinson’s disease year: 2012 doi: 10.1101/cshperspect.a009399 iwai1995: authors: Iwai A, Masliah E, Yoshimoto M, et al title: The precursor protein of non-Aβ component of Alzheimer’s disease amyloid is a presynaptic protein of the central nervous system year: 1995 doi: 10.1016/0896-6273(95 conway2000: authors: Conway KA, Lee SJ, Rochet JC, et al title: ‘Acceleration of oligomerization, not fibrillization, is a shared property of both alpha-synuclein mutations linked to familial Parkinson’‘s disease: a kinetic study’ year: 2000 doi: 10.1073/pnas.97.2.571 winner2011: authors: Winner B, Jappelli R, Maji SK, et al title: In vivo demonstration that alpha-synuclein oligomers are toxic year: 2011 doi: 10.1073/pnas.1100976108 chartierharlin2004: authors: Chartier-Harlin MC, Kachergus J, Roumier C, et al title: Alpha-synuclein locus duplication as a cause of familial Parkinson’s disease year: 2004 doi: 10.1016/s0140-6736(04 polymeropoulos1997: authors: Polymeropoulos MH, Lavedan C, Leroy E, et al title: Mutation in the alpha-synuclein gene identified in families with Parkinson’s disease year: 1997 doi: 10.1126/science.276.5321.2045 zarranz2004: authors: Zarranz JJ, Alegre J, Gómez-Esteban JC, et al title: The new mutation, E46K, of alpha-synuclein causes Parkinson and Lewy body dementia year: 2004 doi: 10.1002/ana.10795 spillantini1998: authors: Spillantini MG, Crowther RA, Jakes R, Hasegawa M, Goedert M title: Alpha-synuclein in filamentous inclusions of Lewy bodies from Parkinson’s disease and dementia with Lewy bodies year: 1998 doi: 10.1073/pnas.95.11.6469 fujiwara2002: authors: Fujiwara H, Hasegawa M, Dohmae N, et al title: alpha-Synuclein is phosphorylated in synucleinopathy lesions year: 2002 doi: 10.1038/ncb841 george2002: authors: George JM title: The synucleins year: 2002 doi: 10.1186/gb-2002-3-1-reviews3002 bussiere2019: authors: Bussiere T, DeVos J, Mishra M, et al title: Amyloid conformation dictates the nature of lesion and clinical phenotype in Lewy body diseases year: 2019 doi: 10.1101/865428 peelaerts2015: authors: Peelaerts W, Baekelandt V title: Alpha-synuclein strains and the diverse pathologies of Parkinson’s disease year: 2015 doi: 10.3233/JAD-158861 pryon2018: authors: Pryor NE, Moss MA, Hyman MW title: Alpha-synuclein can accumulate in the mitochondria and cause dysfunction year: 2018 doi: 10.1016/j.neurobiolaging.2018.01.018 voronkov2022: authors: Voronkov M, Braithwaite SP title: Targeting alpha-synuclein for Parkinson’s disease therapy: the role of microglia year: 2022 doi: 10.1038/s41583-022-00545-0 schapira2019: authors: Schapira AHV, Olanow CW, Greenamyre JT, et al title: Slowing of neurodegeneration in Parkinson’s disease and Huntington’s disease: future therapies year: 2019 doi: 10.1016/S0140-6736(19)31881-1 follett2019: authors: Follett J, Darwent L, Lorig L, et al title: Evaluating the relationship between alpha-synuclein and the cholinergic system in Parkinson’s disease year: 2019 doi: 10.1002/mds.27800 bridi2023: authors: Bridi JC, Hirth F title: Mechanisms of alpha-synuclein propagation: an update on putative prion-like agents year: 2023 doi: 10.1093/brainawes/adab012 parkkinen2011: authors: Parkkinen L, Neumann J, O’Callaghan C, et al title: Is alpha-synuclein neurotoxic in multiple system atrophy? year: 2011 doi: 10.1016/j.neurobiolaging.2011.03.004 spillantini1997:

Alpha-Synuclein Protein

Introduction

Alpha Synuclein Protein is an important component in the neurobiology of neurodegenerative diseases. This page provides detailed information about its structure, function, and role in disease processes.

Overview

Alpha-synuclein (SNCA) is a small, natively unfolded protein that plays critical roles in synaptic function and is central to the pathogenesis of Parkinson’s disease and related neurodegenerative disorders. As the major component of Lewy bodies, pathological aggregates of alpha-synuclein are a hallmark of several neurodegenerative diseases collectively termed synucleinopathies. ^{1Involvement of precerebellar nuclei in multiple system atrophy.2003 · Neuropathol Appl Neurobiol · DOI 10.1046/j.1365-2990.2003.00432.x · PMID 12581341Open reference}

Structure

Domain Organization

Alpha-synuclein is a 140-amino acid protein encoded by the SNCA gene on chromosome 4q21. The protein comprises three distinct domains: ^{2Targeting intracellular and extracellular alpha-synuclein as a therapeutic strategy in Parkinson's disease and other synucleinopathies.2012 · Expert Opin Ther Targets · DOI doi: 10.1517/14728222.2012.674111 · PMID 22480256Open reference}

• N-terminal domain (residues 1-60): Contains seven imperfect repeats of the sequence KTKEGV, which form an amphipathic alpha-helical structure upon membrane binding. This region is highly conserved and mediates lipid interactions.

• NAC region (residues 61-95): The Non-Aβ Component (NAC) of amyloid plaques contains the hydrophobic core responsible for aggregation propensity. This region is essential for fibril formation.

• C-terminal domain (residues 96-140): Acidic and proline-rich, this region exhibits chaperone-like activity and is involved in protein-protein interactions. It modulates aggregation kinetics.

Isoforms

The SNCA gene produces multiple splice variants: ^{3[RNA ligands for HIV proteins].1995 · Tanpakushitsu Kakusan Koso · PMID 7568944Open reference}

• Alpha-synuclein-140: Full-length isoform, most abundant in the brain

• Alpha-synuclein-126: Lacks exons 3 and 6, associated with cytoskeletal functions

• Alpha-synuclein-115: Lacks exons 3, 5, and 6, primarily developmental

Post-translational modifications including phosphorylation at Ser129, ubiquitination, nitration, and oxidation significantly impact aggregation propensity and pathological properties. ^{4Accelerated oligomerization by Parkinson's disease linked alpha-synuclein mutants.2000 · Ann N Y Acad Sci · DOI 10.1111/j.1749-6632.2000.tb06903.x · PMID 11193175Open reference}

Normal Physiological Function

Synaptic Biology

Alpha-synuclein is highly enriched in presynaptic terminals where it regulates: ^{5In vivo demonstration that alpha-synuclein oligomers are toxic.2011 · Proc Natl Acad Sci U S A · DOI doi: 10.1073/pnas.1100976108 · PMID 21325059Open reference}

• Synaptic vesicle trafficking: Modulates synaptic vesicle pool size and recycling

• Dopamine biosynthesis: Interacts with tyrosine hydroxylase and aromatic L-amino acid decarboxylase

• Neurotransmitter release: Affects SNARE complex assembly and vesicle fusion

• Synaptic plasticity: Participates in long-term potentiation and memory formation

Membrane Interactions

The N-terminal domain binds to curved membrane surfaces, particularly synaptic vesicles. This interaction is thought to: ^{6Alpha-synuclein locus duplication as a cause of familial Parkinson's disease.2004 · Lancet · DOI 10.1016/S0140-6736(04)17103-1 · PMID 15451224Open reference}

• Facilitate vesicle clustering at presynaptic terminals

• Regulate the reserve pool of synaptic vesicles

• Protect against oxidative stress

Additional Functions

• Molecular chaperone activity: The C-terminal domain exhibits anti-aggregational properties

• Calcium homeostasis: Modulates calcium influx through voltage-gated calcium channels

• Mitochondrial function: Associates with mitochondrial membranes and affects electron transport chain complex I activity

• Lipid metabolism: Participates in lipid droplet formation and trafficking

Mitochondrial Interactions

Alpha-synuclein localizes to mitochondria where it exerts significant functional effects. Under physiological conditions, low levels of mitochondrial alpha-synuclein support electron transport chain function and mitochondrial dynamics. However, pathological accumulation disrupts mitochondrial homeostasis through multiple mechanisms:

• Complex I inhibition: Alpha-synuclein binds to and inhibits mitochondrial complex I, reducing ATP production and increasing reactive oxygen species (ROS) generation

• Mitochondrial dynamics: Pathological alpha-synuclein impairs mitophagy by interfering with Parkin and PINK1 signaling

• Membrane potential loss: Oligomeric alpha-synuclein forms ion channels in mitochondrial membranes, dissipating the proton gradient

• DNA damage: ROS-induced oxidative damage accumulates in mitochondrial DNA

Cholinergic System Interactions

The relationship between alpha-synuclein pathology and cholinergic system degeneration has significant implications for cognitive decline in Parkinson’s disease. ^{7Endosomal trafficking leads the way in Parkinson's disease.2019 · Mov Disord · DOI doi: 10.1002/mds.27647 · PMID 30812061Open reference}

• Basal forebrain cholinergic neurons are vulnerable to Lewy body pathology

• Cholinergic dysfunction correlates with attention and memory deficits

• Lewy body pathology in pedunculopontine nucleus affects cholinergic neurotransmission

Pathological Aggregation

Alpha-Synuclein Strains

The concept of “strains”—distinct fibril conformations with different biological properties—has revolutionized understanding of synucleinopathies. Different amyloid conformations produce distinct pathological and clinical phenotypes. ^{8Nonclinical safety evaluation of erenumab, a CGRP receptor inhibitor for the prevention of migraine.2019 · Regul Toxicol Pharmacol · DOI doi: 10.1016/j.yrtph.2019.05.013 · PMID 31085251Open reference}

• PD-type strains: Classic Lewy body pathology, slower progression

• MSA-type strains: More aggressive, glia-directed pathology

• DLB-type strains: Mixed Alzheimer-like pathology

• Strain characteristics: Fibril morphology, seeded aggregation kinetics, and cellular targeting vary by strain

Prion-Like Propagation

Alpha-synuclein exhibits prion-like properties, spreading between neurons in a templated manner. ^{9Innovative multiple nanoemulsion (W/O/W) based on Chilean honeybee pollen improves their permeability, antioxidant and antibacterial activity.2023 · Food Res Int · DOI doi: 10.1016/j.foodres.2023.112767 · PMID 37120217Open reference}

• Template-based seeding: Pathological alpha-synuclein can template native protein into misfolded conformations

• Interneuronal transmission: Propagation occurs via synaptic connections

• Exosome release: Extracellular vesicles mediate spread between cells

• Substrate vulnerability: Different brain regions show varying susceptibility

• Strain-specific tropism: Each strain exhibits preferred cellular targets

Aggregation Mechanism

Alpha-synuclein aggregation follows a nucleation-dependent polymerization pathway: ^{10Mutation in the alpha-synuclein gene identified in families with Parkinson's disease.1997 · Science · PMID 9197268Open reference}

1. Misfolding: Native unfolded conformation transitions to β-sheet rich structure

2. Oligomerization: Formation of soluble oligomeric intermediates (protofibrils)

3. Fibrillation: Further aggregation into insoluble amyloid fibrils

4. Deposition: Fibrils accumulate in intracellular inclusions

Lewy Bodies

Lewy bodies are intraneuronal inclusions composed of: ^{2Targeting intracellular and extracellular alpha-synuclein as a therapeutic strategy in Parkinson's disease and other synucleinopathies.2012 · Expert Opin Ther Targets · DOI doi: 10.1517/14728222.2012.674111 · PMID 22480256Open reference}0

• Fibrillar core: Cross-β-sheet amyloid fibrils

• Halo region: Peripheral radiating filaments

• Associated proteins: Ubiquitin, synphilin-1, neurofilaments, chaperones

Oligomers

Soluble oligomeric intermediates are considered the most toxic species: ^{2Targeting intracellular and extracellular alpha-synuclein as a therapeutic strategy in Parkinson's disease and other synucleinopathies.2012 · Expert Opin Ther Targets · DOI doi: 10.1517/14728222.2012.674111 · PMID 22480256Open reference}1

• Membrane permeability: Form pore-like structures increasing calcium influx

• Synaptic dysfunction: Impair neurotransmitter release and vesicle recycling

• ** mitochondrial damage**: Disrupt mitochondrial membrane potential

• Spread mechanism: Exosome-mediated propagation between neurons

Post-Translational Modifications in Pathology

• Ser129 phosphorylation: Found in >90% of Lewy body pathology

• Ubiquitination: Marks proteins for proteasomal degradation

• Nitrination: Promotes aggregation and oxidative damage

• Oxidation: Increases aggregation propensity

Genetics

Disease-Causing Mutations

Gene Multiplications

• SNCA duplications: Autosomal dominant PD, variable penetrance

• SNCA triplications: Early-onset PD, severe phenotype, higher expression

Risk Polymorphisms

Common variants in the SNCA promoter (REP1 microsatellite) and 3’ region influence expression levels and disease risk.

Disease Associations

Parkinson’s Disease

• Constitutes up to 95% of Lewy body protein content

• Pathological spreading follows Braak staging (enteric nervous system → brainstem → cortex)

• Correlates with dopaminergic neuron loss in substantia nigra

• Associated with motor and non-motor symptoms

Dementia with Lewy Bodies

• Cortical and limbic Lewy bodies predominant

• Combined alpha-synuclein and amyloid pathology common

• Associated with fluctuations, visual hallucinations, parkinsonism

Multiple System Atrophy

Alpha-synuclein pathology in MSA exhibits distinct characteristics from Parkinson’s disease, with aggressive progression and poor treatment response. ^{2Targeting intracellular and extracellular alpha-synuclein as a therapeutic strategy in Parkinson's disease and other synucleinopathies.2012 · Expert Opin Ther Targets · DOI doi: 10.1517/14728222.2012.674111 · PMID 22480256Open reference}2

• Glial cytoplasmic inclusions (Papp-Lantos bodies) in oligodendrocytes

• More rapid clinical progression than typical PD

• Predominant autonomic failure (orthostatic hypotension, urinary dysfunction)

• Poor levodopa responsiveness

• Cell-to-cell propagation via oligodendrocyte networks

Pure Autonomic Failure

• Peripheral autonomic neuron involvement

• Often considered prodromal synucleinopathy

Interaction Network

Alpha-synuclein interacts with numerous proteins:

• Synaptic proteins: Synaptophysin, synaptotagmin, CSPα

• Dopaminergic markers: Tyrosine hydroxylase, VMAT2

• Chaperones: Hsp70, Hsp90, Hsp40

• Ubiquitin-proteasome components: Parkin, UCHL1

• Mitochondrial proteins: Complex I subunits, TOM40

Therapeutic Approaches

Disease-Modifying Therapies Under Development

Multiple therapeutic strategies targeting alpha-synuclein are in various stages of clinical development: ^{2Targeting intracellular and extracellular alpha-synuclein as a therapeutic strategy in Parkinson's disease and other synucleinopathies.2012 · Expert Opin Ther Targets · DOI doi: 10.1517/14728222.2012.674111 · PMID 22480256Open reference}3

Immunotherapy

• Active vaccination: AFFITOPE PD-01A (peptide-based) aims to generate antibodies against alpha-synuclein

• Passive immunotherapy: Cinmerlimab (ABBV-0805), PRX002 (roneumunab), and pavinemab target aggregated alpha-synuclein

• Antibody mechanisms: Clear circulating oligomers, block cell-to-cell transmission

Small Molecule Aggregation Inhibitors

• Molecular tweezers: CLR01 (lysine-specific) prevents oligomer formation

• EGCG derivatives: Modified epigallocatechin gallate with improved brain penetration

• Anle138b: Blocks alpha-synuclein oligomer formation in mouse models

Gene Therapy Approaches

• SNCA silencing: ASO and siRNA approaches to reduce protein expression

• GCH1 gene therapy: Restore dopamine synthesis in affected neurons

• AAV-delivered neurotrophic factors: GDNF, BDNF delivery

Aggregation Inhibitors

• Small molecules: Curcumin, EGCG, rifampicin derivatives

• Peptide inhibitors: Designed β-sheet breakers

• Antibodies: Passive immunization (cinmerlimab, pavinemab)

Clearance Enhancement

• Autophagy inducers: Rapamycin, trehalose

• Proteostasis activators: Hsp70 modulators

• Gene therapy: RNAi targeting SNCA expression

Neuroprotective Strategies

• Antioxidants: Reduce oxidative stress-mediated aggregation

• Calcium channel blockers: Prevent calcium dysregulation

• Mitochondrial protectants: Maintain neuronal energy metabolism

Microglia and Neuroinflammation

Microglial activation plays a crucial role in alpha-synuclein pathology progression. ^{2Targeting intracellular and extracellular alpha-synuclein as a therapeutic strategy in Parkinson's disease and other synucleinopathies.2012 · Expert Opin Ther Targets · DOI doi: 10.1517/14728222.2012.674111 · PMID 22480256Open reference}4

• TLR2 recognition: Microglia recognize alpha-synuclein via Toll-like receptor 2

• NF-κB activation: Triggers pro-inflammatory cytokine release (IL-1β, TNF-α)

• NLRP3 inflammasome: Activated by oligomeric alpha-synuclein

• Phagocytic clearance: Normally removes extracellular alpha-synuclein but becomes impaired

• Chronic inflammation: Sustained microglial activation drives disease progression

• Therapeutic targeting: TREM2 agonists and CSF1R antagonists in development

Background

The study of Alpha Synuclein Protein has evolved significantly over the past decades. Research in this area has revealed important insights into the underlying mechanisms of neurodegeneration and continues to drive therapeutic development.

Historical context and key discoveries in this field have shaped our current understanding and will continue to guide future research directions.

Pathway & Interaction Diagram

Interactive diagram showing SNCA’s key relationships in the SciDEX knowledge graph (15 connections shown).

flowchart TD
    SNCA(["SNCA"])
    ALPHA_SYNUCLEIN(["ALPHA_SYNUCLEIN"])
    alpha_synuclein(["alpha-synuclein"])
    PARKINSON_S_DISEASE(["PARKINSON'S DISEASE"])
    P["arkinson_s_diseaseParkinson's disease"]
    a["utophagyautophagy"]
    P["I3K_AKT_CyclinD1PI3K/AKT/CyclinD1"]
    cell_proliferation("cell proliferation")
    NEUROTOXICITY(["NEUROTOXICITY"])
    PARP1(["PARP1"])
    h_072b2f5d["h-072b2f5d"]
    h_74777459["h-74777459"]
    h_2e7eb2ea["h-2e7eb2ea"]
    ASO{"ASO"}
    MITOCHONDRIAL_DYSFUNCTION(["MITOCHONDRIAL DYSFUNCTION"])

    SNCA -->|"encodes"| ALPHA_SYNUCLEIN
    SNCA -->|"produces"| alpha_synuclein
    SNCA -->|"associated with"| PARKINSON_S_DISEASE
    SNCA -->|"causes"| Parkinson_s_disease
    SNCA -->|"activates"| autophagy
    SNCA -->|"activates"| PI3K_AKT_CyclinD1
    SNCA -->|"increases risk"| cell_proliferation
    SNCA -->|"causes"| NEUROTOXICITY
    SNCA -->|"activates"| PARP1
    h_072b2f5d -->|"targets gene"| SNCA
    h_74777459 -->|"targets gene"| SNCA
    h_2e7eb2ea -->|"targets gene"| SNCA
    ASO -.->|"inhibits"| SNCA
    SNCA -->|"causes"| MITOCHONDRIAL_DYSFUNCTION
    SNCA -->|"associated with"| MITOCHONDRIAL_DYSFUNCTION

    style SNCA fill:#006494,stroke:#4fc3f7,stroke-width:3px,color:#e0e0e0

See Also

• Parkinson’s Disease Primary disease associated with alpha-synuclein pathology

• Lewy Body Dementia - Another synucleinopathy

• SNCA Gene - Gene encoding alpha-synuclein

• Synucleinopathies - Category of neurodegenerative diseases

• Parkinson’s Disease Mecha- Dopamineogenic mechanisms

• Dopamine Neurotransmitter affected in PD

• Synaptic Vesicle Trafficking - Normal function of alpha-synuclein

External Links

• Alpha-Synuclein on UniProt

• SNCA Gene on NCBI

• Alpha-Synuclein and Parkinson’s Disease - Nature Reviews

• Michael J. Fox Foundation - Alpha-Synuclein Research

^{2Targeting intracellular and extracellular alpha-synuclein as a therapeutic strategy in Parkinson's disease and other synucleinopathies.2012 · Expert Opin Ther Targets · DOI doi: 10.1517/14728222.2012.674111 · PMID 22480256Open reference}5: Spillantini MG, Schmidt ML, Lee VM, et al. Alpha-synuclein in Lewy bodies. Nature. 1997;388(6645):839-840. DOI:10.1038/42166

^{2Targeting intracellular and extracellular alpha-synuclein as a therapeutic strategy in Parkinson's disease and other synucleinopathies.2012 · Expert Opin Ther Targets · DOI doi: 10.1517/14728222.2012.674111 · PMID 22480256Open reference}6: Braak H, Tredici KD, Rüb U, et al. Staging of brain pathology related to sporadic Parkinson’s disease. Neurobiol Aging. 2003;24(2):197-211. [DOI:10.1016/s0197-4580(02)(https://doi.org/10.1016/s0197-4580(02))00065-9

^{2Targeting intracellular and extracellular alpha-synuclein as a therapeutic strategy in Parkinson's disease and other synucleinopathies.2012 · Expert Opin Ther Targets · DOI doi: 10.1517/14728222.2012.674111 · PMID 22480256Open reference}7: Stefanis L. Alpha-Synuclein in Parkinson’s disease. Cold Spring Harb Perspect Med. 2012;2(2):a009399. DOI:10.1101/cshperspect.a009399

^{2Targeting intracellular and extracellular alpha-synuclein as a therapeutic strategy in Parkinson's disease and other synucleinopathies.2012 · Expert Opin Ther Targets · DOI doi: 10.1517/14728222.2012.674111 · PMID 22480256Open reference}8: Iwai A, Masliah E, Yoshimoto M, et al. The precursor protein of non-Aβ component of Alzheimer’s disease amyloid is a presynaptic protein of the central nervous system. Neuron. 1995;14(2):467-475. [DOI:10.1016/0896-6273(95)(https://doi.org/10.1016/0896-6273(95))90302-x

^{2Targeting intracellular and extracellular alpha-synuclein as a therapeutic strategy in Parkinson's disease and other synucleinopathies.2012 · Expert Opin Ther Targets · DOI doi: 10.1517/14728222.2012.674111 · PMID 22480256Open reference}9: Conway KA, Lee SJ, Rochet JC, et al. Acceleration of oligomerization, not fibrillization, is a shared property of both alpha-synuclein mutations linked to familial Parkinson’s disease: a kinetic study. Proc Natl Acad Sci U S A. 2000;97(2):571-576. DOI:10.1073/pnas.97.2.571

^{3[RNA ligands for HIV proteins].1995 · Tanpakushitsu Kakusan Koso · PMID 7568944Open reference}0: Winner B, Jappelli R, Maji SK, et al. In vivo demonstration that alpha-synuclein oligomers are toxic. Proc Natl Acad Sci U S A. 2011;108(10):4194-4199. DOI:10.1073/pnas.1100976108

^{3[RNA ligands for HIV proteins].1995 · Tanpakushitsu Kakusan Koso · PMID 7568944Open reference}1: Chartier-Harlin MC, Kachergus J, Roumier C, et al. Alpha-synuclein locus duplication as a cause of familial Parkinson’s disease. Lancet. 2004;364(9440):1167-1169. [DOI:10.1016/s0140-6736(04)(https://doi.org/10.1016/s0140-6736(04))17103-1

^{3[RNA ligands for HIV proteins].1995 · Tanpakushitsu Kakusan Koso · PMID 7568944Open reference}2: Polymeropoulos MH, Lavedan C, Leroy E, et al. Mutation in the alpha-synuclein gene identified in families with Parkinson’s disease. Science. 1997;276(5321):2045-2047. DOI:10.1126/science.276.5321.2045

^{3[RNA ligands for HIV proteins].1995 · Tanpakushitsu Kakusan Koso · PMID 7568944Open reference}3: Zarranz JJ, Alegre J, Gómez-Esteban JC, et al. The new mutation, E46K, of alpha-synuclein causes Parkinson and Lewy body dementia. Ann Neurol. 2004;55(2):164-173. DOI:10.1002/ana.10795

^{3[RNA ligands for HIV proteins].1995 · Tanpakushitsu Kakusan Koso · PMID 7568944Open reference}4: Spillantini MG, Crowther RA, Jakes R, Hasegawa M, Goedert M. Alpha-synuclein in filamentous inclusions of Lewy bodies from Parkinson’s disease and dementia with Lewy bodies. Proc Natl Acad Sci U S A. 1998;95(11):6469-6473. DOI:10.1073/pnas.95.11.6469

^{3[RNA ligands for HIV proteins].1995 · Tanpakushitsu Kakusan Koso · PMID 7568944Open reference}5: Fujiwara H, Hasegawa M, Dohmae N, et al. alpha-Synuclein is phosphorylated in synucleinopathy lesions. Nat Cell Biol. 2002;4(2):160-164. DOI:10.1038/ncb841

^{3[RNA ligands for HIV proteins].1995 · Tanpakushitsu Kakusan Koso · PMID 7568944Open reference}6: George JM. The synucleins. Genome Biol. 2002;3(1):reviews3002. DOI:10.1186/gb-2002-3-1-reviews3002 ^{3[RNA ligands for HIV proteins].1995 · Tanpakushitsu Kakusan Koso · PMID 7568944Open reference}7: Bussiere T, DeVos J, Mishra M, et al. Amyloid conformation dictates the nature of lesion and clinical phenotype in Lewy body diseases. bioRxiv. 2019. DOI:10.1101/865428 ^{3[RNA ligands for HIV proteins].1995 · Tanpakushitsu Kakusan Koso · PMID 7568944Open reference}8: Peelaerts W, Baekelandt V. Alpha-synuclein strains and the diverse pathologies of Parkinson’s disease. J Parkinsons Dis. 2015;5(4):761-770. DOI:10.3233/JAD-158861

Upcoming Conferences

MDS 2026

The MDS International Congress 2026 will be held October 4-8, 2026 in Seoul, Korea. See MDS 2026 — Parkinson’s Disease Sessions for coverage of alpha-synuclein research presentations expected at the congress.