{
  "abstract": "This work provides a reassessment of VBIT-4, a compound previously proposed to inhibit oligomerization of the crucial protein known as the mitochondrial voltage-dependent anion channel. Combining complementary experimental approaches with molecular dynamics simulations, the authors provide compelling evidence that VBIT-4 primarily disrupts lipid membranes and induces channel-independent cytotoxicity. The study has fundamental implications for interpreting previous work using VBIT-4 as a probe of channel function and highlights the need to consider membranedisruptive effects when evaluating drug mechanisms.",
  "abstract_shown": true,
  "affiliations": [],
  "article_type": null,
  "arxiv": null,
  "author_total": 17,
  "authors": [
    {
      "name": "Varun Ravishankar"
    },
    {
      "name": "Luís Borges-Araújo"
    },
    {
      "name": "Megha Rajendran"
    },
    {
      "name": "Elodie Lafargue"
    },
    {
      "name": "Deborah Byrne"
    },
    {
      "name": "Nicolas Buzhinsky"
    },
    {
      "name": "Mya S Wolfe"
    },
    {
      "name": "Wendy Fitzgerald"
    },
    {
      "name": "Nina A Bautista"
    },
    {
      "name": "Bethel G Beyene"
    },
    {
      "name": "Motahareh G Larimi"
    },
    {
      "name": "Jean-Pierre Duneau"
    },
    {
      "name": "James Sturgis"
    },
    {
      "name": "Sergey M Bezrukov"
    },
    {
      "name": "Ignacio Casuso"
    },
    {
      "name": "Tatiana K Rostovtseva"
    },
    {
      "name": "Lucie Bergdoll"
    }
  ],
  "bibtex": "https://research.draconitic.com/paper/46kxav4m2z1kd.bib",
  "cited_by": 4,
  "doi": "10.7554/elife.111980",
  "fulltext_url": null,
  "id": "46kxav4m2z1kd",
  "issns": [
    "2050-084X"
  ],
  "landing_url": "https://hal.science/hal-05793971v1",
  "language": "en",
  "licence": "CC-BY-4.0",
  "licence_label": "CC BY 4.0",
  "licence_source": "article",
  "licence_url": "https://creativecommons.org/licenses/by/4.0/",
  "metadata_licence": null,
  "native_subjects": [
    [
      "hal",
      "0.sdv"
    ],
    [
      "hal",
      "1.sdv.bbm"
    ],
    [
      "hal",
      "2.sdv.bbm.bp"
    ],
    [
      "openalex",
      "1312|Lipid Membrane Structure and Behavior"
    ]
  ],
  "openalex": "W4411988241",
  "pdf_url": "https://hal.science/hal-05793971/document",
  "pmcid": null,
  "pmid": null,
  "published": "2026-10-09",
  "publisher": "eLife Sciences Publication",
  "ris": "https://research.draconitic.com/paper/46kxav4m2z1kd.ris",
  "sources": [
    {
      "first_seen": "2026-10-30T12:17:54Z",
      "native_id": "hal-05793971",
      "source": "hal",
      "url": "https://hal.science/hal-05793971v1"
    }
  ],
  "subjects": [
    {
      "field": "biochemistry",
      "origin": "hal:2.sdv.bbm.bp",
      "subfield": "biophysics"
    },
    {
      "field": "biology",
      "origin": "hal:0.sdv",
      "subfield": "general"
    }
  ],
  "title": "A membrane-disruptive action of VBIT-4 challenges its role as a widely used VDAC1 oligomerization inhibitor",
  "title_text": "A membrane-disruptive action of VBIT-4 challenges its role as a widely used VDAC1 oligomerization inhibitor",
  "type": "peer-reviewed",
  "updated_at": "2026-10-30T12:17:54Z",
  "url": "https://research.draconitic.com/paper/46kxav4m2z1kd",
  "venue": "eLife",
  "versions": []
}