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UnknownThe tau isoform 1N4R confers vulnerability of MAPT knockout human iPSC-derived neurons to amyloid beta and phosphorylated tau-induced neuronal dysfunction.
Not available
S-EPMC12089071 | biostudies-literature
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 
UnknownAnti-fibrillization effects of sulfonamide derivatives on α-synuclein and hyperphosphorylated tau isoform 1N4R.
Not available
S-EPMC9614895 | biostudies-literature
UnknownEvaluation of N- and O-Linked Indole Triazines for a Dual Effect on α-Synuclein and Tau Aggregation.
Not available
S-EPMC10624178 | biostudies-literature
UnknownTubulin-binding region alters tau-lipid interactions and changes toxicity of tau fibrils formed in the presence of phosphatidylserine lipids.
Not available
S-EPMC11187861 | biostudies-literature
UnknownExploring the rhodanine universe: Design and synthesis of fluorescent rhodanine-based derivatives as anti-fibrillar and anti-oligomer agents against α-synuclein and 2N4R tau.
Not available
S-EPMC11645236 | biostudies-literature
UnknownHuman wildtype tau expression in cholinergic pedunculopontine tegmental neurons is sufficient to produce PSP-like behavioural deficits and neuropathology.
Not available
S-EPMC9355171 | biostudies-literature
UnknownAmyloid β and tau pathology in brains of aged pinniped species (sea lion, seal, and walrus).
Not available
S-EPMC7792306 | biostudies-literature
Unknown1,4-Diurea- and 1,4-Dithiourea-Substituted Aromatic Derivatives Selectively Inhibit α-Synuclein Oligomer Formation In Vitro.
Not available
S-EPMC10785335 | biostudies-literature
ProteomicsTarget engagement of Tau antibodies induces reversal of proteomic dyshomeostasis in a mouse model of tauopathy
The microtubule-associated protein Tau is a driver of neuronal dysfunction in Alzheimer’s disease and numerous other tauopathies. In this process, Tau initially undergoes subtle changes to its abundance, subcellular localization and a vast array of post-translational modifications, including phospho...
ORGANISM(S): Mus musculus (Mouse) 
2025-05-06 | PXD045799 | Pride
Mouse Alzheimer’s disease Antibody Proteomics Tau Phosphoproteomics Tauopathies 
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