Sort   by:  
 Page size 
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 
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 
ProteomicsASC and SAA protein interaction profiling by limited proteolysis coupled to mass spectrometry
Upon activation of ASC-containing inflammasomes, intracellular molecular aggregates (ASC specks) are assembled and released from myeloid cells into the extracellular space where they enhance the aggregation of Aβ amyloid in Alzheimer’s disease. This raises the question whether ASC is involved in add...
ORGANISM(S): Homo sapiens (Human) 
2025-05-07 | PXD053372 | Pride
Inflamation Saa Lip-ms Asc 
Sort   by:  
 Page size