snca-protein

snca-protein

<table class="infobox infobox-protein">
<tr>
<th class="infobox-header" colspan="2">snca-protein</th>
</tr>
<tr>
<td class="label">Mutation</td>
<td>Location</td>
</tr>
<tr>
<td class="label">A53T</td>
<td>Exon 3</td>
</tr>
<tr>
<td class="label">A30P</td>
<td>Exon 3</td>
</tr>
<tr>
<td class="label">E46K</td>
<td>Exon 3</td>
</tr>
<tr>
<td class="label">H50Q</td>
<td>Exon 3</td>
</tr>
<tr>
<td class="label">G51D</td>
<td>Exon 3</td>
</tr>
<tr>
<td class="label">A53E</td>
<td>Exon 3</td>
</tr>
<tr>
<td class="label">Associated Diseases</td>
<td><a href="/wiki/ad" style="color:#ef9a9a">AD</a>, <a href="/wiki/ali" style="color:#ef9a9a">ALI</a>, <a href="/wiki/als" style="color:#ef9a9a">ALS</a>, <a href="/wiki/alzheimer" style="color:#ef9a9a">ALZHEIMER</a>, <a href="/wiki/alzheimer-disease" style="color:#ef9a9a">ALZHEIMER DISEASE</a></td>
</tr>
<tr>
<td class="label">KG Connections</td>
<td><a href="/atlas" style="color:#4fc3f7">1418 edges</a></td>
</tr>
</table>

snca-protein

<table class="infobox infobox-protein">
<tr>
<th class="infobox-header" colspan="2">snca-protein</th>
</tr>
<tr>
<td class="label">Mutation</td>
<td>Location</td>
</tr>
<tr>
<td class="label">A53T</td>
<td>Exon 3</td>
</tr>
<tr>
<td class="label">A30P</td>
<td>Exon 3</td>
</tr>
<tr>
<td class="label">E46K</td>
<td>Exon 3</td>
</tr>
<tr>
<td class="label">H50Q</td>
<td>Exon 3</td>
</tr>
<tr>
<td class="label">G51D</td>
<td>Exon 3</td>
</tr>
<tr>
<td class="label">A53E</td>
<td>Exon 3</td>
</tr>
<tr>
<td class="label">Associated Diseases</td>
<td><a href="/wiki/ad" style="color:#ef9a9a">AD</a>, <a href="/wiki/ali" style="color:#ef9a9a">ALI</a>, <a href="/wiki/als" style="color:#ef9a9a">ALS</a>, <a href="/wiki/alzheimer" style="color:#ef9a9a">ALZHEIMER</a>, <a href="/wiki/alzheimer-disease" style="color:#ef9a9a">ALZHEIMER DISEASE</a></td>
</tr>
<tr>
<td class="label">KG Connections</td>
<td><a href="/atlas" style="color:#4fc3f7">1418 edges</a></td>
</tr>
</table>
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](/proteins/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. [@braak2003]

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: [@stefanis2012]

• 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](/proteins/amyloid-beta) 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: [@iwai1995]

• 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

Normal Physiological Function

Synaptic Biology

Alpha-synuclein is highly enriched in presynaptic terminals where it regulates: [@winner2011]

• 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](/mechanisms/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: [@chartierharlin2004]

• 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: [@pryon2018]

• 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. [@follett2019]

• 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. [@bussiere2019]

• 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. [@bridi2023]

• 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: [@polymeropoulos1997]

Lewy Bodies

Lewy bodies are intraneuronal inclusions composed of: [@zarranz2004]

• 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: [@spillantini1998]

• 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](/entities/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. [@parkkinen2011]

• 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: [@schapira2019]

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](/entities/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. [@voronkov2022]

• 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).

See Also

• [Parkinson's Disease](/diseases/parkinsons-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- [Dopamine](/mechanisms/dopaminergic-signaling)ogenic mechanisms
• [Dopamine](/mechanisms/dopaminergic-signaling) Neurotransmitter affected in PD
• Synaptic Vesicle Trafficking - Normal function of alpha-synuclein

External Links

• [Alpha-Synuclein on UniProt](https://www.uniprot.org/p37840)
• [SNCA Gene on NCBI](https://www.ncbi.nlm.nih.gov/gene/6622)
• [Alpha-Synuclein and Parkinson's Disease - Nature Reviews](https://www.nature.com/articles/nrd.2015.5)
• [Michael J. Fox Foundation - Alpha-Synuclein Research](https://www.michaeljfox.org/)

[@braak2003]: 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

[@stefanis2012]: Stefanis L. Alpha-Synuclein in Parkinson's disease. Cold Spring Harb Perspect Med. 2012;2(2):a009399. [DOI:10.1101/cshperspect.a009399](https://doi.org/10.1101/cshperspect.a009399)

[@iwai1995]: 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

[@conway2000]: 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](https://doi.org/10.1073/pnas.97.2.571)

[@winner2011]: 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](https://doi.org/10.1073/pnas.1100976108)

[@chartierharlin2004]: 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

[@polymeropoulos1997]: 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](https://doi.org/10.1126/science.276.5321.2045)

[@zarranz2004]: 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](https://doi.org/10.1002/ana.10795)

[@spillantini1998]: 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](https://doi.org/10.1073/pnas.95.11.6469)

[@fujiwara2002]: 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](https://doi.org/10.1038/ncb841)

[@george2002]: George JM. The synucleins. Genome Biol. 2002;3(1):reviews3002. [DOI:10.1186/gb-2002-3-1-reviews3002](https://doi.org/10.1186/gb-2002-3-1-reviews3002)
[@bussiere2019]: 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](https://doi.org/10.1101/865428)
[@peelaerts2015]: 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](https://doi.org/10.3233/JAD-158861)
[@pryon2018]: Pryor NE, Moss MA, Hyman MW. Alpha-synuclein can accumulate in the mitochondria and cause dysfunction. Neurobiol Aging. 2018;62:192.e1-192.e14. [DOI:10.1016/j.neurobiolaging.2018.01.018](https://doi.org/10.1016/j.neurobiolaging.2018.01.018)
[@voronkov2022]: Voronkov M, Braithwaite SP. Targeting alpha-synuclein for Parkinson's disease therapy: the role of microglia. Nat Rev Neurol. 2022;18(7):387-388. [DOI:10.1038/s41583-022-00545-0](https://doi.org/10.1038/s41583-022-00545-0)
[@schapira2019]: Schapira AHV, Olanow CW, Greenamyre JT, et al. Slowing of neurodegeneration in Parkinson's disease and Huntington's disease: future therapies. Lancet. 2019;393(10173):992-1002. [DOI:10.1016/S0140-6736(19)31881-1](https://doi.org/10.1016/S0140-6736(19)31881-1)
[@follett2019]: Follett J, Darwent L, Lorig L, et al. Evaluating the relationship between alpha-synuclein and the cholinergic system in Parkinson's disease. Mov Disord. 2019;34(10):1480-1489. [DOI:10.1002/mds.27800](https://doi.org/10.1002/mds.27800)
[@bridi2023]: Bridi JC, Hirth F. Mechanisms of alpha-synuclein propagation: an update on putative prion-like agents. Brain Behav. 2023;13(3):e2827. [DOI:10.1093/brainawes/adab012](https://doi.org/10.1093/brainawes/adab012)
[@parkkinen2011]: Parkkinen L, Neumann J, O'Callaghan C, et al. Is alpha-synuclein neurotoxic in multiple system atrophy? Neurobiol Aging. 2011;32(12):2325.e1-2325.e9. [DOI:10.1016/j.neurobiolaging.2011.03.004](https://doi.org/10.1016/j.neurobiolaging.2011.03.004)

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.

References