{
  "annotation_id": "f1c507c5-ce0e-401c-a20d-7c57d0297c65",
  "date_created": "2026-03-02T18:01:24.756000Z",
  "date_modified": "2026-03-02T18:01:24.756000Z",
  "file_hash": "56b6277999b024f68ba36580c57b7a29cbf5f7ccc3c6f84963bdfd47a2fae36a",
  "private": false,
  "record": {
    "abstract": "Retinoic acid receptor (RAR) is a ligand-dependent transcription factor that\nregulates the expression of genes involved in cell growth, differentiation, and\ndevelopment. Binding of the retinoic acid hormone to RAR is accompanied by\nconformational changes in the protein which induce transactivation or\ntransrepression of the target genes. In this paper we present a study of the\nhormone binding/unbinding process in order to clarify the role of some of the\namino acid contacts and identify possible pathways of the all-trans retinoic\nacid binding/unbinding to/from human retinoic acid receptor (hRAR)-g. Three\npossible pathways were explored using steered molecular dynamics simulations.\nUnbinding was induced on a time scale of 1 ns by applying external forces to\nthe hormone. The simulations suggest that the hormone may employ one pathway\nfor binding and an alternative \"back door\" pathway for unbinding.",
    "arxiv_id": "physics/9903050",
    "authors": [
      "Dorina Kosztin",
      "Sergei Izrailev",
      "Klaus Schulten"
    ],
    "categories": [
      "physics.bio-ph",
      "physics.comp-ph",
      "q-bio"
    ],
    "doi": "10.1016/S0006-3495(99)77188-2",
    "journal_ref": "Biophysical Journal 76, 188 (1999)",
    "title": "Unbinding of Retinoic Acid from its Receptor Studied by Steered   Molecular Dynamics",
    "url": "https://arxiv.org/abs/physics/9903050"
  },
  "schema_id": "dorsal/arxiv",
  "source": {
    "execution_id": "6be54ea7-794f-4850-95dd-fb26fa9a6889",
    "id": "arXiv Dataset IDs",
    "type": "Model",
    "variant": "snapshot-2026-03-01",
    "version": "0.1.0"
  },
  "user_id": 1000002
}