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ProteomicsAn approach to characterize mechanisms of action of anti-amyloidogenic compounds in vitro and in situ
Amyloid aggregation is associated with neurodegenerative disease and its modulation is a focus of drug development. We developed a pipeline based on limited proteolysis-mass spectrometry (LiP-MS) to probe the mechanism of action of anti-amyloidogenic compounds. Our approach identifies putative inter...
ORGANISM(S): Homo sapiens (Human) Rattus norvegicus (Rat) 
2025-05-26 | PXD063272 | Pride
Alpha-synuclein Anti-amyloidogenic compounds Lip-ms 
ProteomicsAlpha-synuclein fibrils induce budding of mitochondrial-derived vesicles
α-synuclein (α-syn) aggregation is a hallmark of synucleinopathies, a class of neurodegenerative disorders such as Parkinson’s disease (PD). Several lines of evidence indicate the involvement of mitochondria in the disease pathology. Despite extensive study, the link between α-syn aggregation and me...
ORGANISM(S): Homo sapiens (Human) 
2026-06-29 | PXD078690 | Pride
ProteomicsAlpha-synuclein interacts with regulators of ATP homeostasis in mitochondria
Mitochondrial dysfunction and accumulation of α-synuclein aggregates are hallmarks of the neurodegenerative Parkinson’s disease and may be interconnected. In order to investigate the interplay between α-synuclein and brain mitochondria at near atomic structural level we applied NMR and identified α-...
ORGANISM(S): Bos taurus (Bovine) Homo sapiens (Human) 
2025-07-18 | PXD063500 | Pride
Lip-ms Mitochondria Alpha-synuclein 
UnknownVapor phase mediated cellular uptake of sub 5 nm nanoparticles.
Not available
S-EPMC3368743 | 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 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 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 
UnknownObserving a lipid-dependent alteration in single lactose permeases.
Not available
S-EPMC4394043 | biostudies-literature
UnknownImpact of Carbon Fluoroxide Nanoparticles on Cell Proliferation.
Not available
S-EPMC8708860 | biostudies-literature
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