ArticleThe American journal of pathology2017
Exposure of the Amino Terminus of Tau Is a Pathological Event in Multiple Tauopathies.
Article in The American journal of pathology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers, 1 of them a synthesis that pooled it.
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Who cites it
27 citing papers in PubMed, 1 synthesis or guideline pooled it, 31 citations in OpenAlex.
- Neuropathology in chronic traumatic encephalopathy: a systematic review of comparative post-mortem histology literature.Acta neuropathologica communications · 2022Pooled it
- Patient-derived forebrain cortical organoids reveal biphasic tau-MAP6-microtubule axis dysfunction in tauopathy.Alzheimer's & dementia : the journal of the Alzheimer's Association · 2026Article
- Inhibition of pathogenic tau signaling via blocking of the phosphatase-activating domain by novel small molecules.Frontiers in pharmacology · 2026Article
- Pretangle tau pathology accrual in the default mode network during the progression of Alzheimer's disease.Molecular neurodegeneration advances · 2026Article
- Seeding Alzheimer's disease-associated tau pathology in MAPT knock-in primary neurons causes early axonopathy and synaptic dysfunction.Scientific reports · 2025Article
- Polyamination with spermidine enhances pathogenic tau conformations while reducing filamentous aggregate formation in vitro.The Biochemical journal · 2025Article
- Distinct subcellular localization of tau and alpha-synuclein in lewy body disease.Acta neuropathologica communications · 2025Article
- Temporal progression of tau pathology and neuroinflammation in a rhesus monkey model of Alzheimer's disease.Alzheimer's & dementia : the journal of the Alzheimer's Association · 2024Article
- Precision proteoform design for 4R tau isoform selective templated aggregation.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Precision Proteoform Design for 4R Tau Isoform Selective Templated Aggregation.bioRxiv : the preprint server for biology · 2023Article
- Phosphomimetics at Ser199/Ser202/Thr205 in Tau Impairs Axonal Transport in Rat Hippocampal Neurons.Molecular neurobiology · 2023Article
- Tau phosphorylation and PAD exposure in regulation of axonal growth.Frontiers in cell and developmental biology · 2022Article
- Genome-wide association study and functional validation implicates JADE1 in tauopathy.Acta neuropathologica · 2022Article
- Frontotemporal Lobar Dementia Mutant Tau Impairs Axonal Transport through a Protein Phosphatase 1γ-Dependent Mechanism.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2021Article
- Interaction of tau with HNRNPA2B1 and NMolecular cell · 2021Article
- Tau: A Signaling Hub Protein.Frontiers in molecular neuroscience · 2021Article
- Editorial: Tau Protein: Mechanisms From Health to Degeneration.Frontiers in molecular neuroscience · 2021Article
- Tau and Alpha Synuclein Synergistic Effect in Neurodegenerative Diseases: When the Periphery Is the Core.International journal of molecular sciences · 2020Review
- Alterations in Tau Metabolism in ALS and ALS-FTSD.Frontiers in neurology · 2020Review
- Defined Tau Phosphospecies Differentially Inhibit Fast Axonal Transport Through Activation of Two Independent Signaling Pathways.Frontiers in molecular neuroscience · 2020Article
Corrections and comments
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Authors and funding
2 authors at 2 institutions in 1 country.
Funding
Abstract
Pathological changes to the tau protein, including conformational changes and aggregation, are major hallmarks of a group of neurodegenerative disorders known as tauopathies. Among the conformational changes are alterations involving the extreme amino terminus of the protein, known as the phosphatase-activating domain (PAD). Aberrant PAD exposure induces a signaling cascade that leads to disruption of axonal transport, a critical function for neuronal survival. Conformational display of PAD is an early marker of pathological tau in Alzheimer disease (AD), but its role in other tauopathies has yet to be firmly established. We used a relatively novel N-terminal, conformation-sensitive antibody, TNT2, to determine whether misfolding in the amino terminus (ie, PAD exposure) occurs in non-AD tauopathies. We found that TNT2 specifically labeled pathological tau in post-mortem human brain tissue from Pick disease, progressive supranuclear palsy, corticobasal degeneration, and chronic traumatic encephalopathy, but did not label nonpathological, parenchymal tau. Tau13, another N-terminal antibody, was not sensitive to pathological N-terminal conformations. Tau13 did not readily distinguish between normal (ie, parenchymal tau) and pathological tau species and showed a range of effectiveness at identifying tau pathologies in the non-AD tauopathies. These findings demonstrate that the conformational display of the PAD in tau represents a common pathological event in many tauopathies.
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