ArticleProceedings of the National Academy of Sciences of the United States of America1991
Difference between the tau protein of Alzheimer paired helical filament core and normal tau revealed by epitope analysis of monoclonal antibodies 423 and 7.51.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1991. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 67 papers.
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Who cites it
67 citing papers in PubMed, 210 citations in OpenAlex.
- MAPT mutations associated with familial tauopathies lead to formation of conformationally distinct oligomers that have cross-seeding ability.Protein science : a publication of the Protein Society · 2024Article
- Assays for the Screening and Characterization of Tau Aggregation Inhibitors.Methods in molecular biology (Clifton, N.J.) · 2024Article
- JNK3 Overexpression in the Entorhinal Cortex Impacts on the Hippocampus and Induces Cognitive Deficiencies and Tau Misfolding.ACS chemical neuroscience · 2023Article
- JNK Activation in Alzheimer's Disease Is Driven by Amyloid β and Is Associated with Tau Pathology.ACS chemical neuroscience · 2023Article
- Aggregation of Disordered Proteins Associated with Neurodegeneration.International journal of molecular sciences · 2023Review
- An Additive-Free Model for Tau Self-Assembly.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Regional distribution and maturation of tau pathology among phenotypic variants of Alzheimer's disease.Acta neuropathologica · 2022Article
- Specific Peptide from the Novel W-Tau Isoform Inhibits Tau and Amyloid β Peptide AggregationACS chemical neuroscience · 2022Article
- Tau as a Biomarker of Neurodegeneration.International journal of molecular sciences · 2022Review
- Genome-wide association study and functional validation implicates JADE1 in tauopathy.Acta neuropathologica · 2022Article
- A new non-aggregative splicing isoform of human Tau is decreased in Alzheimer's disease.Acta neuropathologica · 2021Article
- Tau Is Truncated in Five Regions of the Normal Adult Human Brain.International journal of molecular sciences · 2021Article
- Molecular Processing of Tau Protein in Progressive Supranuclear Palsy: Neuronal and Glial Degeneration.Journal of Alzheimer's disease : JAD · 2021Article
- Phosphorylation and Dephosphorylation of Tau Protein by the Catalytic Subunit of PKA, as Probed by Electrophoretic Mobility Retard.Journal of Alzheimer's disease : JAD · 2021Article
- Differential compartmental processing and phosphorylation of pathogenic human tau and native mouse tau in the line 66 model of frontotemporal dementia.The Journal of biological chemistry · 2020Article
- Tau (297-391) forms filaments that structurally mimic the core of paired helical filaments in Alzheimer's disease brain.FEBS letters · 2020Article
- Tau Filament Self-Assembly and Structure: Tau as a Therapeutic Target.Frontiers in neurology · 2020Review
- FUNDAMANT: an interventional 72-week phase 1 follow-up study of AADvac1, an active immunotherapy against tau protein pathology in Alzheimer's disease.Alzheimer's research & therapy · 2018Article
- Relevance of Phosphorylation and Truncation of Tau to the Etiopathogenesis of Alzheimer's Disease.Frontiers in aging neuroscience · 2018Article
- Amyloid-β and tau complexity - towards improved biomarkers and targeted therapies.Nature reviews. Neurology · 2018Review
7 more citing papers are in PubMed but not listed here.
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The microtubule-associated protein tau that is incorporated into paired helical filaments (PHFs) undergoes some form of aberrant posttranslational processing in Alzheimer disease. Difficulties in deciding which changes are critical for PHF formation stem in part from the lack of immunochemical markers specific for PHF tau. The only monoclonal antibody (mAb) that is known to react with PHF tau but not with the predominant normal adult tau species is mAb 423. Another mAb (7.51, described in this paper) recognizes a segment of tau that is included in the minimal recognition unit required by mAb 423. Unlike 423, which is PHF tau-specific, mAb 7.51 recognizes all PHF core-derived tau as well as native soluble tau and recombinant tau expressed in bacteria and so serves as a generic tau marker. Both epitopes are in the 12-kDa fragment released from the Pronase-resistant core of the PHF (which encompasses the tandem repeat region). The mAb 7.51 epitope requires segments located in the last two repeats, which are common to all tau isoforms. The mAb 423 epitope requires sequences located near both the N and the C terminus of the 12-kDa fragment common to three- and four-repeat tau isoforms. Fragments denatured by concentrated formic acid and SDS regain 423 reactivity when denaturing agents are removed. Since the primary amino acid sequences of PHF tau and normal tau are identical in the repeat region, we conclude that 423 reactivity also requires a modification(s) occurring within an approximately 90-residue segment that are not present in tau proteins so far described in the human brain.
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