{
  "annotation_id": "6b2925be-6493-4cea-bf0b-99eade647c5d",
  "date_created": "2026-03-02T18:01:30.963000Z",
  "date_modified": "2026-03-02T18:01:30.963000Z",
  "file_hash": "b1e05cf3045c557dfe615c09515d5e32c4e4a15e24486e480399b37daf20ddb8",
  "private": false,
  "record": {
    "abstract": "A theoretical model of stabilization of a microtubule assembly due to\nmicrotubule-associated-proteins(MAP) is presented. MAPs are assumed to bind to\nthe microtubule filaments, thus preventing their disintegration following\nhydrolysis and enhancing further polymerization. Using mean-field rate\nequations and explicit numerical simulations, we show that the density of MAP\n(number of MAP per tubulin in the microtubule) has to exceed a critical value\n$\\rho_{c}$ to stabilize the structure against de-polymerization. At lower\ndensities $\\rho \u003c \\rho_{c}$, the microtubule population consists mostly of\nshort polymers with exponentially decaying length distribution, whereas at\n$\\rho \u003e \\rho_{c}$ the average length increases linearly with time and the\nmicrotubules ultimately extend to the cell boundary. Using experimentally\nmeasured values of various parameters, the critical ratio of MAP to tubulin\nrequired for unlimited growth is seen to be of the order of 1:100 or even\nsmaller.",
    "arxiv_id": "q-bio/0312008",
    "authors": [
      "Bindu S. Govindan",
      "William B. Spillman, Jr."
    ],
    "categories": [
      "q-bio.SC",
      "q-bio.CB"
    ],
    "title": "Stabilization of microtubules due to microtubule-associated proteins: A   simple model",
    "url": "https://arxiv.org/abs/q-bio/0312008"
  },
  "schema_id": "dorsal/arxiv",
  "source": {
    "execution_id": "d2351d43-36e3-45a9-8f9e-36939edf2f17",
    "id": "arXiv Dataset IDs",
    "type": "Model",
    "variant": "snapshot-2026-03-01",
    "version": "0.1.0"
  },
  "user_id": 1000002
}