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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 
ProteomicsNeuronal interactome changes upon aggregation of Tau
To understand at molecular level how aggregation of Tau modulates its interactions with proteins we reveal key determinant for derailing Tau protein network. By performing quantitative AP-MS we define a new set of interactors which bind Tau upon fibril formation. These interactors contain disordered...
ORGANISM(S): Rattus norvegicus (Rat) 
2020-01-30 | PXD015432 | Pride
Fibrils Tau Molecular chaperones Protein aggregation Hsp90 Protein-protein interactions 
GenomicsStructural evidence that RNA contributes to polymorphism of tau amyloid fibrils
Structural evidence that RNA contributes to polymorphism of tau amyloid fibrils
PRJNA1425023 | ENA
ProteomicsTargeted mass spectrometry of Tau preparations purified from Alzheimer’s Disease brains plus either the deubiquitylase USP21 or its activity-dead mutant C221A.
To characterise the abundance of ubiquitylated Tau peptides in the presence of active or inactive variants (wt 196-565 vs. C221A) of the broad spectrum deubiquitylase USP21. Tau peptides are obtained from Tau fibrils purified from post mortem human brains diagnosed with Alzheimer’s. Their detection ...
ORGANISM(S): Homo sapiens (Human) 
2024-06-18 | PXD046645 | Pride
Alzheimer’s disease (de)ubiquitination/ubiquitylation Neurodegeneration 
ProteomicsPRM and DDA Data for IR5 WIW and WIW Nanobodies
Journal Article: Structure-based design of nanobodies that inhibit seeding of Alzheimer's patient-extracted tau fibrils
ORGANISM(S): Synthetic Antibodies Nanobodies 
2023-06-16 | MSV000092197 | MassIVE
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 
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
ProteomicsPTMs of Endogenous Tau in Wildtype and hAPP Transgenic Mice
Please Note, if a password is required, please try "a", the generic password for Massive. These data are in support of the manuscript: Post-translational Modifications of Endogenous Tau in Wildtype and Human Amyloid Precursor Protein Transgenic Mice Meaghan Morris*a,b, Giselle M. Knudsen*c, Sumi...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) Mus Musculus (ncbitaxon:10090) 
2014-07-30 | MSV000078796 | MassIVE
ProteomicsCross-Beta Helical Fibrils of Tau and TMEM106B in Gray and White Matter of Multiple System Tauopathy with Presenile Dementia
Neurodegenerative diseases characterized by tau aggregates have distinct tau pathological profiles that may differ in relation to the morphology and structure of the filaments, the tau-isoform composition and the cell types and brain areas that are affected. Neurons, dendrites and axonal terminals a...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2022-12-06 | MSV000090845 | MassIVE
ProteomicsMass spectrometry analysis of in vitro Tau ubiquitination by the UBA1/Hsp70/CHIP machinery
We aimed at characterizing which lysines on Tau were ubiquitinated by the UBA1/Hsp70/CHIP machinery. We also determined the ubiquitin linkages of the assembled Tau chains.
ORGANISM(S): Homo sapiens (Human) 
2024-06-18 | PXD034527 | Pride
Ubiquitination Protein degradation Alzheimer’s disease Tau 
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