Sort   by:  
 Page size 
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
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 
ProteomicsStructure-function relationship of alpha-synuclein fibrillar polymorphs derived from distinct synucleinopathies (Part 2)
Structure-function relationship of alpha-synuclein fibrillar polymorphs derived from distinct synucleinopathies (Part 2) Abstract of the entire work: The aggregation of the protein alpha-synuclein (αSyn) is a common feature of multiple neurodegenerative diseases collectively called synucleinopathie...
ORGANISM(S): Homo sapiens (Human) 
2026-06-08 | PXD058443 | Pride
Fibrillar polymorphs Alpha-synuclein Interactome 
UnknownSelective vulnerability in α-synucleinopathies.
Not available
S-EPMC6800835 | biostudies-literature
ProteomicsStructure-function relationship of alpha-synuclein fibrillar polymorphs derived from distinct synucleinopathies (Part 5)
The aggregation of the protein alpha-synuclein (αSyn) is a common feature of multiple neurodegenerative diseases collectively called synucleinopathies, for which the pathobiology is not well understood. The different phenotypic characteristics of the synucleinopathies Parkinson’s disease (PD), Demen...
ORGANISM(S): Homo sapiens (Human) 
2026-06-08 | PXD058444 | Pride
Fibrillar polymorphs Alpha-synuclein Interactome 
ProteomicsStructure-function relationship of alpha-synuclein fibrillar polymorphs derived from distinct synucleinopathies (Part 4)
The aggregation of the protein alpha-synuclein (αSyn) is a common feature of multiple neurodegenerative diseases collectively called synucleinopathies, for which the pathobiology is not well understood. The different phenotypic characteristics of the synucleinopathies Parkinson’s disease (PD), Demen...
ORGANISM(S): Homo sapiens (Human) 
2026-06-08 | PXD058440 | Pride
Fibrillar polymorphs Alpha-synuclein Interactome 
ProteomicsStructure-function relationship of alpha-synuclein fibrillar polymorphs derived from distinct synucleinopathies (Part 3)
The aggregation of the protein alpha-synuclein (αSyn) is a common feature of multiple neurodegenerative diseases collectively called synucleinopathies, for which the pathobiology is not well understood. The different phenotypic characteristics of the synucleinopathies Parkinson’s disease (PD), Demen...
ORGANISM(S): Homo sapiens (Human) 
2026-06-08 | PXD058439 | Pride
Fibrillar polymorphs Alpha-synuclein Interactome 
ProteomicsStructure-function relationship of alpha-synuclein fibrillar polymorphs derived from distinct synucleinopathies (Part 1)
The aggregation of the protein alpha-synuclein (αSyn) is a common feature of multiple neurodegenerative diseases collectively called synucleinopathies, for which the pathobiology is not well understood. The different phenotypic characteristics of the synucleinopathies Parkinson’s disease (PD), Demen...
ORGANISM(S): Homo sapiens (Human) 
2026-06-08 | PXD058124 | Pride
Synucleopathies Structural proteomics  mass spectrometry  chemical surface modification  nhs-biotin  nanolc-msms Amplified synuclein fibrils 
UnknownSex differences in alpha-synucleinopathies: a systematic review.
Not available
S-EPMC10398394 | biostudies-literature
Unknownα-Synuclein interacts directly but reversibly with psychosine: implications for α-synucleinopathies.
Not available
S-EPMC6102231 | biostudies-literature
Sort   by:  
 Page size