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ProteomicsIdentification of post-translational modifications on soluble alpha-Synuclein purified from various alpha-Synucleinopathies by LC-MSMS
LC-MS/MS analyses were performed on soluble alpha-Syn purified from PD and various alpha-Synucleinopathies to systematically explore the landscape of post-translational modifications (PTMs) on soluble alpha-Syn, leading to the identification of a large number of novel alpha-Syn PTMs.
ORGANISM(S): Homo sapiens (Human) 
2023-02-02 | PXD037994 | Pride
Human Post-translational modification Brain Soluble a-synuclein Alpha-synucleinopathies 
ProteomicsIdentification of post-translational modifications on soluble alpha-Syn purified from various alpha-Synucleinopathies
LC-MS/MS analyses were performed on soluble alpha-Syn purified from PD and various alpha-Synucleinopathies to systematically explore the landscape of post-translational modifications (PTMs) on soluble alpha-Syn, leading to the identification of a large number of novel alpha-Syn PTMs.
ORGANISM(S): Human 
2022-10-30 | MSV000090618 | MassIVE
ProteomicsTDP-43 pathology is associated with divergent protein profiles in ALS brain and spinal cord
Neuronal and glial cytoplasmic inclusions positive for TAR DNA-binding protein 43 (TDP-43) are the defining pathological hallmark of 97% of amyotrophic lateral sclerosis (ALS) and 50% of frontotemporal dementia (FTD). The ALS-FTD clinicopathological spectrum variably involves cortical and spinal ant...
ORGANISM(S): Homo sapiens (Human) 
2025-08-25 | PXD067060 | Pride
Proteomics Tissue Brain Tdp-43 Amyotrophic lateral sclerosis Spinal cord 
UnknownBiochemical Fractionation of Human α-Synuclein in a Drosophila Model of Synucleinopathies.
Not available
S-EPMC11011978 | biostudies-literature
UnknownBiochemical fractionation of human α-Synuclein in a Drosophila model of synucleinopathies.
Not available
S-EPMC10871193 | biostudies-literature
ProteomicsNuclear-injuries by aberrant dynein-forces defeat proteostatic purposes of Lewy Body-like InclusionsNuclear-injuries by aberrant dynein-forces defeat proteostatic purposes of Lewy Body-like Inclusions
Biogenesis of inclusion bodies (IBs) facilitates protein quality control (PQC). Canonical aggresomes execute degradation of misfolded proteins while non-degradable amyloids quarantine into Insoluble Protein Deposits. Lewy Bodies (LBs) are well-known neurodegenerative IBs of α-Synuclein but PQC-benef...
ORGANISM(S): Homo sapiens (Human) Mus musculus (Mouse) 
2024-04-04 | PXD028941 | Pride
-synuclein Syn-aggresomes Nuclear envelope injury Inclusion bodies Lewy body Proteostasis over-saturation 
UnknownA Capped Peptide of the Aggregation Prone NAC 71-82 Amino Acid Stretch of α-Synuclein Folds into Soluble β-Sheet Oligomers at Low and Elevated Peptide Concentrations.
Not available
S-EPMC7084662 | biostudies-literature
UnknownPropofol Attenuates α-Synuclein Aggregation and Neuronal Damage in a Mouse Model of Ischemic Stroke.
Not available
S-EPMC7056784 | biostudies-literature
UnknownAlpha-synuclein seeding shows a wide heterogeneity in multiple system atrophy.
Not available
S-EPMC8819887 | biostudies-literature
UnknownA prolyl oligopeptidase inhibitor, KYP-2047, reduces α-synuclein protein levels and aggregates in cellular and animal models of Parkinson's disease.
Not available
S-EPMC3417432 | biostudies-literature
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