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ProteomicsPhysiological tau interactome in brain and its link to tauopathies_complete submission
Alzheimer's disease (AD) and most of other tauopathies are incurable neurodegenerative diseases with unpleasant symptoms and consequences. The common hallmark of all these diseases is tau pathology but its connection with disease progress has not been completely understood so far. Therefore, uncover...
ORGANISM(S): Rattus norvegicus (Rat) 
2020-05-07 | PXD018687 | Pride
Mass spectrometry Alzheimer's disease In vivo crosslinking Tau interaction partners Tau protein Tauopathies Tau pathology 
ProteomicsRat PC12 wild-type cells with polypharmacological drug PHOX15 treatment that reduces tau phosphorylation at disease-relevant sites and restores its physiological microtubule interaction
In tauopathies such as Alzheimer's disease, the aggregation and increased phosphorylation of tau proteins are key pathological features. These changes in tau are strongly linked to neurodegeneration, making it a prime target for therapeutic intervention. Through chemoinformatic analyses, 2-phenyloxa...
ORGANISM(S): Rattus norvegicus (Rat) 
2024-02-26 | PXD048913 | Pride
Tauopathy Rat Kinase inhibitor Hyperphosphorylation Tau Lfq Tau phosphorylation Phosphorylation Label-free Pc12 
UnknownTau Protein Interaction Partners and Their Roles in Alzheimer's Disease and Other Tauopathies.
Not available
S-EPMC8431036 | biostudies-literature
ProteomicsAxonal Tau sorting depends on the PRR2 domain and 0N4R-specific interactions hint at distinct roles of Tau isoforms in synaptic plasticity
Tau pathology is a major hallmark of Alzheimer’s disease (AD) and related diseases, called tauopathies. While Tau is normally enriched in axons, somatodendritic missorting of the microtubule-associated protein is a key event in early disease development. Tau missorting promotes synaptic loss and neu...
ORGANISM(S): Homo sapiens (Human) 
2024-11-21 | PXD053880 | Pride
Proline-rich region 2 Alzheimer’s disease Tau missorting Tau isoforms Synaptic tau Cdc42 Rab11 
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 
UnknownMolecular crowding and RNA synergize to promote phase separation, microtubule interaction, and seeding of Tau condensates.
Not available
S-EPMC9156969 | biostudies-literature
UnknownSolution structure of Domains IVa and V of the tau subunit of Escherichia coli DNA polymerase III and interaction with the alpha subunit.
Not available
S-EPMC1888800 | biostudies-literature
ProteomicsIdentification of the Tau aggresome in progressive supranuclear palsy by in situ biotinylation by antibody recognition reveals protein networks involved in energy metabolism, cytoskeletal dynamics and protein degradation systems.
Progressive supranuclear palsy (PSP) is a late-onset neurodegenerative disease defined pathologically by the presence of insoluble phosphorylated-Tau (p-Tau) in neurons and glia. Identifying co-aggregating proteins within p-Tau inclusions reveals important insights into processes affected by the agg...
ORGANISM(S): Homo sapiens (Human) 
2023-02-27 | PXD028770 | Pride
Tauopathy  aggresome  biotinylation 
UnknownSpred1 and TESK1--two new interaction partners of the kinase MARKK/TAO1 that link the microtubule and actin cytoskeleton.
Not available
S-EPMC2291396 | biostudies-literature
UnknownLiquid-liquid phase separation of Tau by self and complex coacervation.
Not available
S-EPMC8197434 | biostudies-literature
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