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ProteomicsIdentification of novel kinases of Tau using fluorescence complementation mass spectrometry (FCMS)
Hyperphosphorylation of the microtubule-associated protein Tau is a major hallmark of Alzheimer’s disease (AD) and other tauopathies. Understanding the protein kinases that phosphorylate Tau is critical for the development of new drugs that target Tau phosphorylation. At present, the repertoire of t...
ORGANISM(S): Homo Sapiens (human) 
2022-11-10 | PXD036956 | JPOST Repository
ProteomicsProteomics of human tau-transgenic mice reveals protein modules associated with tau pathologies
Abnormally accumulated tau protein aggregates are one of the hallmarks of dementia, including Alzheimer’s disease (AD), and are believed to play a critical role in neurodegeneration. In order to investigate proteomic alteration driven by tau aggregates, we implemented quantitative proteomics to anal...
ORGANISM(S): Mus Musculus (mouse) 
2022-07-05 | PXD031129 | JPOST Repository
ProteomicsTruncated Tau
Tau is a microtubule-associated protein that ensures neuronal shape and function. Besides, Tau is a central player in Alzheimer’s disease (AD) and related Tauopathies where it is found aggregated in degenerating neurons. Mechanisms leading to Tau pathology and its progression are far from being eluc...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2017-04-27 | MSV000081020 | MassIVE
ProteomicsAnalysis of pathological tau associated with a wide range of tauopathies
We have analyzed and compared the post-translational modifications in the pathological tau proteins prepared from a wide range of tauopathies.
ORGANISM(S): Homo Sapiens (human) 
2020-07-15 | PXD020371 | JPOST Repository
ProteomicsProperties of Alzheimer’s disease brain-derived tau aggregates define tau processing by human astrocytes
The templated misfolding of tau proteins accounts for tau pathology spread in Alzheimer’s disease (AD). Post-translational modifications, including phosphorylation at specific residues, are closely linked with tau seeding ability and clinical disease progression. This study investigates the role of ...
ORGANISM(S): Homo sapiens (Human) 
2025-05-07 | PXD056614 | Pride
Tau  alzheimer’s disease  astrocyte 
ModelsYuraszeck2010 - Vulnerabilities in the Tau Network in Tau Pathophysiology
Yuraszeck2010 - Vulnerabilities in the Tau Network in Tau Pathophysiology This model is described in the article: Vulnerabilities in the tau network and the role of ultrasensitive points in tau pathophysiology. Yuraszeck TM, Neveu P, Rodriguez-Fernandez M, Robinson A, Kosik ...
2024-09-02 | BIOMD0000000542 | BioModels
ProteomicsPhosphorylated Tau Interactome in the Human Alzheimers Disease Brain
Accumulation of phosphorylated tau is a key pathological feature of Alzheimers disease. Phosphorylated tau accumulation causes synaptic impairment, neuronal dysfunction and formation of neurofibrillary tangles. The pathological actions of phosphorylated tau are mediated by surrounding neuronal prote...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2020-04-17 | MSV000085305 | MassIVE
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 
GenomicsZeugodacus tau
Zeugodacus tau Raw sequence reads
PRJNA560958 | ENA
GenomicsZeugodacus tau
Zeugodacus tau Raw sequence reads
PRJNA1047290 | ENA
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