ArticleThe Journal of cell biology1989
Expression of multiple tau isoforms and microtubule bundle formation in fibroblasts transfected with a single tau cDNA.
Article in The Journal of cell biology, 1989. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 88 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
88 citing papers in PubMed, 355 citations in OpenAlex.
- FGF-Mediated Axon Guidance: Role of Downstream Signaling Pathways in Cytoskeletal Control.Cells · 2025Review
- Tau is required for glial lipid droplet formation and resistance to neuronal oxidative stress.Nature neuroscience · 2024Article
- Effects of three microtubule-associated proteins (MAP2, MAP4, and Tau) on microtubules' physical properties and neurite morphology.Scientific reports · 2023Article
- Towards a Mechanistic Model of Tau-Mediated Pathology in Tauopathies: What Can We Learn from Cell-Based In Vitro Assays?International journal of molecular sciences · 2022Review
- Importin-Mediated Pathological Tau Nuclear Translocation Causes Disruption of the Nuclear Lamina, TDP-43 Mislocalization and Cell Death.Frontiers in molecular neuroscience · 2022Article
- Hyperphosphorylated Human Tau Accumulates at the Synapse, Localizing on Synaptic Mitochondrial Outer Membranes and Disrupting Respiration in a Mouse Model of Tauopathy.Frontiers in molecular neuroscience · 2022Article
- Microtubule-associated proteins (MAPs) in microtubule cytoskeletal dynamics and spermatogenesis.Histology and histopathology · 2021Review
- Asparagine residue 368 is involved in Alzheimer's disease tau strain-specific aggregation.The Journal of biological chemistry · 2020Article
- Tau interferes with axonal neurite stabilization and cytoskeletal composition independently of its ability to associate with microtubules.Biology open · 2020Article
- T-complex protein 1-ring complex enhances retrograde axonal transport by modulating tau phosphorylation.Traffic (Copenhagen, Denmark) · 2018Article
- Anti-aggregant tau mutant promotes neurogenesis.Molecular neurodegeneration · 2017Article
- Analysis of isoform-specific tau aggregates suggests a common toxic mechanism involving similar pathological conformations and axonal transport inhibition.Neurobiology of aging · 2016Article
- Role of tau in the spatial organization of axonal microtubules: keeping parallel microtubules evenly distributed despite macromolecular crowding.Cellular and molecular life sciences : CMLS · 2016Article
- The endocrine dyscrasia that accompanies menopause and andropause induces aberrant cell cycle signaling that triggers re-entry of post-mitotic neurons into the cell cycle, neurodysfunction, neurodegeneration and cognitive disease.Hormones and behavior · 2015Review
- Cellular Models of Aggregation-dependent Template-directed Proteolysis to Characterize Tau Aggregation Inhibitors for Treatment of Alzheimer Disease.The Journal of biological chemistry · 2015Article
- Tau phosphorylation affects its axonal transport and degradation.Neurobiology of aging · 2013Article
- Mechanical properties of doubly stabilized microtubule filaments.Biophysical journal · 2013Article
- Global axonal transport rates are unaltered in htau mice in vivo.Journal of Alzheimer's disease : JAD · 2013Article
- PACSIN1, a Tau-interacting protein, regulates axonal elongation and branching by facilitating microtubule instability.The Journal of biological chemistry · 2012Article
- Regulation of mitochondrial transport and inter-microtubule spacing by tau phosphorylation at the sites hyperphosphorylated in Alzheimer's disease.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2012Article
28 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
8 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Tau proteins are a class of low molecular mass microtubule-associated proteins that are specifically expressed in the nervous system. A cDNA clone of adult rat tau was isolated and sequenced. To analyze functions of tau proteins in vivo, we carried out transfection experiments. A fibroblast cell line, which was transfected with the cDNA, expressed three bands of tau, while six bands were expressed in rat brain. After dephosphorylation, one of the three bands disappeared, demonstrating directly that phosphorylation was involved in the multiplicity of tau. Morphologically, we observed a thick bundle formation of microtubules in the transiently and stably tau-gene-transfected cells. In addition, we found that the production of tubulin was prominently enhanced in the stably transfected cells. Thus, we suppose that tau proteins promote polymerization of tubulin, form bundles of microtubules in vivo, and play important roles in growing and maintaining nerve cell processes.
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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.