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Subcellular orchestration of alpha-synuclein variants in Parkinson’s disease brains revealed by 3D multicolor STED microscopy

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Outgoing claims: the papers this work cites, builds on, or argues with.

inferredcites →https://doi.org/10.1001/archneur.1969.00480180071006openalex-snapshot

Sphingomyelin in Lewy Inclusion Bodies in Parkinson's Disease

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Lysosomal Dysfunction and α‐Synuclein Aggregation in Parkinson's Disease: Diagnostic Links

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Label‐free identification of myopathological features with coherent anti‐Stokes Raman scattering

inferredcites →https://doi.org/10.1006/exnr.2000.7527openalex-snapshot

In Situ and in Vitro Study of Colocalization and Segregation of α-Synuclein, Ubiquitin, and Lipids in Lewy Bodies

inferredcites →https://doi.org/10.1006/jmbi.2001.4538openalex-snapshot

Conformational properties of α-synuclein in its free and lipid-associated states 1 1Edited by P. E. Wright

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Kinetic Screening in the Antibody Development Process

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An antibody with high reactivity for disease-associated α-synuclein reveals extensive brain pathology

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BrainNet Europe’s Code of Conduct for brain banking

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The Lewy Body in Parkinson’s Disease and Related Neurodegenerative Disorders

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Characterization of a novel protein regulated during the critical period for song learning in the zebra finch

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The precursor protein of non-Aβ component of Alzheimer's disease amyloid is a presynaptic protein of the central nervous system

inferredcites →https://doi.org/10.1016/j.ajpath.2012.11.018openalex-snapshot

Axonopathy in an α-Synuclein Transgenic Model of Lewy Body Disease Is Associated with Extensive Accumulation of C-Terminal–Truncated α-Synuclein

inferredcites →https://doi.org/10.1016/j.arr.2014.07.002openalex-snapshot

Clearance of misfolded and aggregated proteins by aggrephagy and implications for aggregation diseases

inferredcites →https://doi.org/10.1016/j.bpj.2014.03.025openalex-snapshot

Automated Identification of Subcellular Organelles by Coherent Anti-Stokes Raman Scattering

inferredcites →https://doi.org/10.1016/j.jmb.2013.03.031openalex-snapshot

The Mysterious C-Terminal Tail of Alpha-Synuclein: Nanobody's Guess

inferredcites →https://doi.org/10.1016/j.nbd.2015.12.018openalex-snapshot

Dynamic structural flexibility of α-synuclein

inferredcites →https://doi.org/10.1016/j.nbd.2018.02.019openalex-snapshot

Lysosomal response in relation to α-synuclein pathology differs between Parkinson's disease and multiple system atrophy

inferredcites →https://doi.org/10.1016/j.neuron.2011.08.033openalex-snapshot

Exogenous α-Synuclein Fibrils Induce Lewy Body Pathology Leading to Synaptic Dysfunction and Neuron Death

inferredcites →https://doi.org/10.1016/j.neuroscience.2011.10.042openalex-snapshot

α-synuclein phosphorylation and truncation are normal events in the adult human brain

inferredcites →https://doi.org/10.1016/j.plipres.2015.10.005openalex-snapshot

Interaction of α-synuclein with biomembranes in Parkinson's disease —role of cardiolipin

inferredcites →https://doi.org/10.1016/s0022-510x(03)00144-8openalex-snapshot

A paced visual serial addition test for fMRI

inferredcites →https://doi.org/10.1016/s0079-6123(10)83007-9openalex-snapshot

Role of post-translational modifications in modulating the structure, function and toxicity of α-synuclein

inferredcites →https://doi.org/10.1016/s0091-679x(08)60963-2openalex-snapshot

Chapter 16 The Use of Fluorescent DNA-Binding Agent for Detecting and Separating Yeast Mitochondrial DNA

inferredcites →https://doi.org/10.1016/s0197-4580(02)00065-9openalex-snapshot

Staging of brain pathology related to sporadic Parkinson’s disease

inferredcites →https://doi.org/10.1016/s0962-8924(00)01852-3openalex-snapshot

Aggresomes, inclusion bodies and protein aggregation

inferredcites →https://doi.org/10.1016/s1474-4422(04)00827-0openalex-snapshot

Lewy-body formation is an aggresome-related process: a hypothesis

inferredcites →https://doi.org/10.1016/s1474-4422(15)00006-xopenalex-snapshot

Targeting α-synuclein for treatment of Parkinson's disease: mechanistic and therapeutic considerations

inferredcites →https://doi.org/10.1021/bi027363ropenalex-snapshot

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

inferredcites →https://doi.org/10.1021/bi048453uopenalex-snapshot

Impact of the Acidic C-Terminal Region Comprising Amino Acids 109−140 on α-Synuclein Aggregation in Vitro

inferredcites →https://doi.org/10.1038/ncb748openalex-snapshot

α-Synuclein is phosphorylated in synucleinopathy lesions

inferredcites →https://doi.org/10.1038/ncomms11359openalex-snapshot

Phosphorylation modifies the molecular stability of β-amyloid deposits

inferredcites →https://doi.org/10.1038/nrn3406openalex-snapshot

The many faces of α-synuclein: from structure and toxicity to therapeutic target

inferredcites →https://doi.org/10.1038/s41593-019-0423-2openalex-snapshot

Lewy pathology in Parkinson’s disease consists of crowded organelles and lipid membranes

inferredcites →https://doi.org/10.1038/srep05797openalex-snapshot

Quantitative Measurement of Intact Alpha-Synuclein Proteoforms from Post-Mortem Control and Parkinson's Disease Brain Tissue by Intact Protein Mass Spectrometry

inferredcites →https://doi.org/10.1039/c6an02072kopenalex-snapshot

Virtual staining of colon cancer tissue by label-free Raman micro-spectroscopy

inferredcites →https://doi.org/10.1073/pnas.0406976102openalex-snapshot

Aggregation promoting C-terminal truncation of α-synuclein is a normal cellular process and is enhanced by the familial Parkinson's disease-linked mutations

inferredcites →https://doi.org/10.1073/pnas.1309991110openalex-snapshot

Polo-like kinase 2 regulates selective autophagic α-synuclein clearance and suppresses its toxicity in vivo

inferredcites →https://doi.org/10.1073/pnas.1610099113openalex-snapshot

Caspase-1 causes truncation and aggregation of the Parkinson’s disease-associated protein α-synuclein

inferredcites →https://doi.org/10.1073/pnas.95.11.6469openalex-snapshot

α-Synuclein in filamentous inclusions of Lewy bodies from Parkinson’s disease and dementia with Lewy bodies

inferredcites →https://doi.org/10.1074/jbc.m116.759373openalex-snapshot

Dissecting the Molecular Pathway Involved in PLK2 Kinase-mediated α-Synuclein-selective Autophagic Degradation

inferredcites →https://doi.org/10.1074/jbc.m208046200openalex-snapshot

Phosphorylated α-Synuclein Is Ubiquitinated in α-Synucleinopathy Lesions

inferredcites →https://doi.org/10.1074/jbc.m501508200openalex-snapshot

A Precipitating Role for Truncated α-Synuclein and the Proteasome in α-Synuclein Aggregation

inferredcites →https://doi.org/10.1074/jbc.m600933200openalex-snapshot

Phosphorylation of Ser-129 Is the Dominant Pathological Modification of α-Synuclein in Familial and Sporadic Lewy Body Disease

inferredcites →https://doi.org/10.1074/jbc.m800747200openalex-snapshot

Phosphorylation at Ser-129 but Not the Phosphomimics S129E/D Inhibits the Fibrillation of α-Synuclein

inferredcites →https://doi.org/10.1074/mcp.r113.032730openalex-snapshot

Alpha-synuclein Post-translational Modifications as Potential Biomarkers for Parkinson Disease and Other Synucleinopathies

inferredcites →https://doi.org/10.1093/hmg/ddu112openalex-snapshot

Overexpression of the calpain-specific inhibitor calpastatin reduces human alpha-Synuclein processing, aggregation and synaptic impairment in [A30P]αSyn transgenic mice

inferredcites →https://doi.org/10.1093/jnen/62.12.1241openalex-snapshot

Morphogenesis of Lewy Bodies: Dissimilar Incorporation of α-Synuclein, Ubiquitin, and p62

inferredcites →https://doi.org/10.1097/00005072-196507000-00003openalex-snapshot

PHASE AND ELECTRON MICROSCOPIC OBSERVATIONS OF LEWY BODIES AND MELANIN GRANULES IN THE SUBSTANTIA NIGRA AND LOCUS CAERULEUS IN PARKINSONʼS DISEASE

inferredcites →https://doi.org/10.1097/00005072-199603000-00001openalex-snapshot

Neuropathology of Parkinsonʼs Disease

inferredcites →https://doi.org/10.1097/nen.0b013e3181633526openalex-snapshot

Assessment of α-Synuclein Pathology: A Study of the BrainNet Europe Consortium

inferredcites →https://doi.org/10.1101/500058openalex-snapshot

The making of a Lewy body: the role of alpha-synuclein post-fibrillization modifications in regulating the formation and the maturation of pathological inclusions.

inferredcites →https://doi.org/10.1101/cshperspect.a024091openalex-snapshot

Cell Biology and Pathophysiology of α-Synuclein

inferredcites →https://doi.org/10.1111/bpa.12344openalex-snapshot

L ewy Bodies and the Mechanisms of Neuronal Cell Death in P arkinson's Disease and Dementia with L ewy Bodies

inferredcites →https://doi.org/10.1111/j.1750-3639.2008.00140.xopenalex-snapshot

Three‐Layered Structure Shared Between Lewy Bodies and Lewy Neurites—Three‐Dimensional Reconstruction of Triple‐Labeled Sections

inferredcites →https://doi.org/10.1111/j.1750-3639.2011.00509.xopenalex-snapshot

Pale Neurites, Premature α‐Synuclein Aggregates with Centripetal Extension from Axon Collaterals

inferredcites →https://doi.org/10.1111/j.1750-3639.2012.00585.xopenalex-snapshot

Biochemical Increase in Phosphorylated Alpha‐Synuclein Precedes Histopathology of Lewy‐Type Synucleinopathies

inferredcites →https://doi.org/10.1111/j.1750-3639.2012.00597.xopenalex-snapshot

Critical Role of Truncated α‐Synuclein and Aggregates in Parkinson's Disease and Incidental Lewy Body Disease

inferredcites →https://doi.org/10.1523/jneurosci.08-08-02804.1988openalex-snapshot

Synuclein: a neuron-specific protein localized to the nucleus and presynaptic nerve terminal

inferredcites →https://doi.org/10.1523/jneurosci.5314-13.2014openalex-snapshot

Reducing C-Terminal-Truncated Alpha-Synuclein by Immunotherapy Attenuates Neurodegeneration and Propagation in Parkinson's Disease-Like Models

inferredcites →https://doi.org/10.2353/ajpath.2007.061232openalex-snapshot

Calpain-Cleavage of α-Synuclein

inferredcites →https://doi.org/10.3233/jpd-160779openalex-snapshot

Implication of Alpha-Synuclein Phosphorylation at S129 in Synucleinopathies: What Have We Learned in the Last Decade?

What points at this work

Incoming claims: where this work appears in other papers’ reference lists and arguments.

inferred← citeshttps://doi.org/10.1002/mds.27897openalex-snapshot

CSF or Serum Neurofilament Light Added to α‐Synuclein Panel Discriminates Parkinson's From Controls

inferred← citeshttps://doi.org/10.1007/s00401-021-02313-3openalex-snapshot

LRP10 interacts with SORL1 in the intracellular vesicle trafficking pathway in non-neuronal brain cells and localises to Lewy bodies in Parkinson’s disease and dementia with Lewy bodies

inferred← citeshttps://doi.org/10.1016/j.nbd.2020.104876openalex-snapshot

Do Lewy bodies contain alpha-synuclein fibrils? and Does it matter? A brief history and critical analysis of recent reports

inferred← citeshttps://doi.org/10.1038/s41531-022-00357-0openalex-snapshot

Opportunities and challenges of alpha-synuclein as a potential biomarker for Parkinson’s disease and other synucleinopathies

inferred← citeshttps://doi.org/10.1038/s41531-023-00604-yopenalex-snapshot

Development and validation of an expanded antibody toolset that captures alpha-synuclein pathological diversity in Lewy body diseases

inferred← citeshttps://doi.org/10.1038/s41531-025-01084-yopenalex-snapshot

Differential role of C-terminal truncations on alpha-synuclein pathology and Lewy body formation

inferred← citeshttps://doi.org/10.1038/s41583-020-00416-6openalex-snapshot

Reverse engineering Lewy bodies: how far have we come and how far can we go?

inferred← citeshttps://doi.org/10.1073/pnas.1913904117openalex-snapshot

The process of Lewy body formation, rather than simply α-synuclein fibrillization, is one of the major drivers of neurodegeneration

inferred← citeshttps://doi.org/10.1073/pnas.2011196118openalex-snapshot

Mechanistic basis for receptor-mediated pathological α-synuclein fibril cell-to-cell transmission in Parkinson's disease

inferred← citeshttps://doi.org/10.1073/pnas.2114405119openalex-snapshot

In situ proximity labeling identifies Lewy pathology molecular interactions in the human brain

inferred← citeshttps://doi.org/10.1088/1478-3975/ab694eopenalex-snapshot

Advanced fluorescence imaging of in situ protein aggregation

inferred← citeshttps://doi.org/10.1101/2021.04.25.441304openalex-snapshot

Super-resolution microscopy informs on the molecular architecture of alpha-synuclein inclusions in model systems and in the human brain

inferred← citeshttps://doi.org/10.1101/2022.06.08.495286openalex-snapshot

Human pericytes degrade α-synuclein aggregates in a strain-dependent manner

inferred← citeshttps://doi.org/10.1101/2023.07.16.549189openalex-snapshot

Altered TFEB subcellular localization in nigral dopaminergic neurons of subjects with prodromal, sporadic and GBA -related Parkinson’s disease and Dementia with Lewy bodies

inferred← citeshttps://doi.org/10.1101/2024.11.29.625993openalex-snapshot

Dissecting the differential role of C-terminal truncations in the regulation of aSyn pathology formation and the biogenesis of Lewy bodies

inferred← citeshttps://doi.org/10.1101/654582openalex-snapshot

Two new polymorphic structures of alpha-synuclein solved by cryo-electron microscopy

inferred← citeshttps://doi.org/10.1111/jnc.14965openalex-snapshot

Synucleinopathies: Where we are and where we need to go

inferred← citeshttps://doi.org/10.1146/annurev-neuro-100720-034518openalex-snapshot

Parkinson's Disease Genetics and Pathophysiology

inferred← citeshttps://doi.org/10.1155/2023/8848642openalex-snapshot

Dyrk1a Phosphorylation of α-Synuclein Mediating Apoptosis of Dopaminergic Neurons in Parkinson’s Disease

inferred← citeshttps://doi.org/10.1186/s40478-020-01091-5openalex-snapshot

Label-free vibrational imaging of different Aβ plaque types in Alzheimer’s disease reveals sequential events in plaque development

inferred← citeshttps://doi.org/10.3389/fnagi.2021.690293openalex-snapshot

Alpha-Synuclein Post-translational Modifications: Implications for Pathogenesis of Lewy Body Disorders

inferred← citeshttps://doi.org/10.3389/fnins.2021.689938openalex-snapshot

Neurofilament Proteins as Biomarkers to Monitor Neurological Diseases and the Efficacy of Therapies

inferred← citeshttps://doi.org/10.3389/fnins.2021.690013openalex-snapshot

Neurofilament Levels Are Reflecting the Loss of Presynaptic Dopamine Receptors in Movement Disorders

inferred← citeshttps://doi.org/10.3410/f.737400163.793571512openalex-snapshot

Faculty Opinions recommendation of The process of Lewy body formation, rather than simply α-synuclein fibrillization, is one of the major drivers of neurodegeneration.

inferred← citeshttps://doi.org/10.4103/1673-5374.264453openalex-snapshot

Study of alpha-synuclein fibrillation: state of the art and expectations

inferred← citeshttps://doi.org/10.7554/elife.48907openalex-snapshot

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

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