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GenomicsSelection of aptamers against α-synuclein fibrillar polymorphs
Libraries of SELEX against α-synuclein fibrillar polymorphs
PRJEB70964 | ENA
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 
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 
UnknownAptamer binding footprints discriminate α-synuclein fibrillar polymorphs from different synucleinopathies.
Not available
S-EPMC11317169 | biostudies-literature
UnknownMapping the Spatial Distribution of Fibrillar Polymorphs in Human Brain Tissue.
Not available
S-EPMC9198601 | biostudies-literature
UnknownThe differential solvent exposure of N-terminal residues provides "fingerprints" of alpha-synuclein fibrillar polymorphs.
Not available
S-EPMC8163981 | biostudies-literature
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 
UnknownNanomechanical properties of distinct fibrillar polymorphs of the protein α-synuclein.
Not available
S-EPMC5128817 | biostudies-literature
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