ArticleThe Journal of cell biology1988
Tau proteins: the molecular structure and mode of binding on microtubules.
Article in The Journal of cell biology, 1988. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 107 papers.
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Who cites it
107 citing papers in PubMed, 376 citations in OpenAlex.
- Prospect in Alzheimer's disease integrative therapy targeting both amyloid-beta and tau.Neural regeneration research · 2026Article
- Article
- Advances in research on pharmacological mechanisms of anatabine: from nicotinic modulation to multitarget therapeutic potential.Experimental biology and medicine (Maywood, N.J.) · 2026Review
- Meta-cancer phosphoproteomic analysis unveils association of Tau phosphosites with DNA damage response.Frontiers in systems biology · 2026Article
- Cellular and molecular mechanisms of pathological tau phosphorylation in traumatic brain injury: implications for chronic traumatic encephalopathy.Molecular neurodegeneration · 2025Review
- Diverse influences on tau aggregation and implications for disease progression.Genes & development · 2025Review
- Calcineurin inhibition may prevent Alzheimer disease in people with Down syndrome.Alzheimer's & dementia : the journal of the Alzheimer's Association · 2025Review
- Strategies of positron emission tomography (PET) tracer development for imaging of tau and α-synuclein in neurodegenerative disorders.RSC medicinal chemistry · 2025Review
- Tau, Glial Fibrillary Acidic Protein, and Neurofilament Light Chain as Brain Protein Biomarkers in Cerebrospinal Fluid and Blood for Diagnosis of Neurobiological Diseases.International journal of molecular sciences · 2024Review
- The six brain-specific TAU isoforms and their role in Alzheimer's disease and related neurodegenerative dementia syndromes.Alzheimer's & dementia : the journal of the Alzheimer's Association · 2024Review
- Chemical Synthesis of Microtubule-Associated Protein Tau.Journal of the American Chemical Society · 2023Article
- Cooperative melting in double-stranded peptide chains through local mechanical interactions.Journal of the Royal Society, Interface · 2023Article
- Nasal administration of mesenchymal stem cells prevents accelerated age-related tauopathy after chemotherapy in mice.Immunity & ageing : I & A · 2023Article
- The Interplay between GSK3β and Tau Ser262 Phosphorylation during the Progression of Tau Pathology.International journal of molecular sciences · 2022Article
- Microtubule-binding core of the tau protein.Science advances · 2022Article
- Article
- The pathogenic R5L mutation disrupts formation of Tau complexes on the microtubule by altering local N-terminal structure.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- The century-old picture of a nerve spike is wrong: filaments fire, before membrane.Communicative & integrative biology · 2022Review
- Viscoelastic damage evaluation of the axon.Frontiers in bioengineering and biotechnology · 2022Article
- Non-Canonical Roles of Tau and Their Contribution to Synaptic Dysfunction.International journal of molecular sciences · 2021Review
47 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Tau is a family of closely related proteins (55,000-62,000 mol wt) which are contained in the nerve cells and copolymerize with tubulin to induce the formation of microtubules in vitro. All information so far has indicated that tau is closely apposed to the microtubule lattice, and there was no indication of domains projecting from the microtubule polymer lattice. We have studied the molecular structure of the tau factor and its mode of binding on microtubules using the quick-freeze, deep-etch method (QF.DE) and low angle rotary shadowing technique. Phosphocellulose column-purified tubulin from porcine brain was polymerized with tau and the centrifuged pellets were processed by QF.DE. We observed periodic armlike elements (18.7 +/- 4.8 nm long) projecting from the microtubule surface. Most of the projections appeared to cross-link adjacent microtubules. We measured the longitudinal periodicity of tau projections on the microtubules and found it to match the 6-dimer pattern better than the 12-dimer pattern. The stoichiometry of tau versus tubulin in preparations of tau saturated microtubules was 1:approximately 5.0 (molar ratio). Tau molecules adsorbed on mica took on rodlike forms (56.1 +/- 14.1 nm long). Although both tau and MAP1 are contained in axons, competitive binding studies demonstrated that the binding sites of tau and MAP1A on the microtubule surfaces are most distinct, although they may partially overlap.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.