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ProteomicsIdentification of proteins that interact with extracellularly applied fibrillar Tau assemblies
The microtubule associated protein Tau (MAPT) expressed in neurons is involved in microtubules stabilization, cell morphogenesis and axonal transport. In pathological conditions, Tau assembles into high molecular weight assemblies leading to neuropathological Tau deposits, the hallmark of several n...
ORGANISM(S): Mus musculus (Mouse) 
2019-01-09 | PXD009294 | Pride
Lc-msms Pull-down 1n4r isoform Interacting protein partners Tau fibrils Proteomics 1n3r isoform 
ProteomicsMass spectrometry-based proteomic analysis of virions and fibrils from Mimiviridae
Mimivirus 1.2Mb genome is organized into a 30 nm nucleocapsid-like structure made of two closely related GMC-oxidoreductases, also composing the fibrils decorating its virions. In this work, we used MS-proteomics to characterize the protein content of virions and fibrils from different members of th...
ORGANISM(S): Acanthamoeba castellanii Mimivirus 
2024-06-16 | PXD041298 | Pride
Mimivirus Fibrils Virion Nanolc-ms/ms 
ProteomicsHelical superstructures between amyloid and collagen VI in heart derived fibrils from a patient with Light Chain Amyloidosis
We investigated the N- and C-terminome of the LCs proteoforms in fibrils extracted from the hearts of a patient affected by AL amyloidosis, using a proteomic approach based on N- and C-terminal residues derivatization, followed by mapping of fragmentation sites on the structures of fibrillar LCs
ORGANISM(S): Homo sapiens (Human) 
2024-07-02 | PXD049301 | Pride
Amyloid fibrils  fragmentation sites  immunoglobulin light chains 
ProteomicsStructure of ATTRv-F64S fibrils isolated from skin tissue of a living patient
Transthyretin-derived amyloidosis (ATTR) is a degenerative, systemic disease characterized by transthyretin fibril deposition in organs like the heart, kidneys, liver, and skin. We report the first cryo-EM structure of transthyretin fibrils isolated from skin tissue of a living patient with a rare g...
ORGANISM(S): Homo sapiens (Human) 
2025-11-03 | PXD065685 | Pride
Attr Cryo-em Diagnostic tool Mass spectrometry Transthyretin Amyloidosis 
ProteomicsHelical superstructures between amyloid and collagen VI in heart derived fibrils from a patient with Light Chain Amyloidosis
we investigated the N-glycosylation of the amyloid fibrils extracted from the heart of a patient affected by AL amyloidosis, using a proteomic approach to evaluate indirectly the presence of glycans in immunoglobulin light chains.
ORGANISM(S): Homo sapiens (Human) 
2024-07-02 | PXD049369 | Pride
Immunoglobulin light chains  n-glycosylation  amyloid fibrils 
GenomicsStructural evidence that RNA contributes to polymorphism of tau amyloid fibrils
Structural evidence that RNA contributes to polymorphism of tau amyloid fibrils
PRJNA1425023 | ENA
GenomicsRNAseq analysis of primary astrocyte and microglia under Aβ40WT and Aβ42WT fibrils treatment
RNAseq analysis of primary astrocyte and microglia under Aβ40WT and Aβ42WT fibrils treatment
PRJNA869461 | ENA
ProteomicsStructural mapping of the surfaces of fibrillar 1N3R and 1N4R human tau
The structural characterization of pathogenic tau filaments that accumulate in tauopathies, including Alzheimer disease, is key for understanding their pathogenic function and identify the structural determinants of distinct tau filaments involved in distinct tauopathies. Fibrillar tau surfaces play...
ORGANISM(S): Homo sapiens (Human) 
2022-02-17 | PXD027403 | Pride
Structural proteomics  proteolysis  chemical surface modification  nhs-biotin  nanolc-msms Tau fibrils 
ProteomicsMajor Proteomic Changes Associated with Amyloid Induced Biofilm Formation in Pseudomonas aeruginosa PAO1
The newly identified functional amyloids in Pseudomonas (Fap) are associated with increased aggregation and biofilm formation in the opportunistic pathogen P. aeruginosa. However, whether this phenomenon can be simply ascribed to the mechanical properties of the amyloid fibrils remains...
ORGANISM(S): Pseudomonas Aeruginosa Pao1 (ncbitaxon:208964) 
MSV000082917 | MassIVE
TranscriptomicsStructural evidence that RNA contributes to polymorphism of tau amyloid fibrils
RNA colocalizes with tau deposits in Alzheimer’s disease (AD) and other tauopathies, and drives tau aggregation in vitro. However, molecular details of RNA-tau interactions remain unclear, and in particular whether these interactions contribute to neurodegeneration. Previously, we determined a cryo-...
ORGANISM(S): Mus musculus 
2026-02-17 | GSE319735 | GEO
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