Evidence map›Paper›PMID 22062421›Full record

ReviewBiochimica et biophysica acta2012

The role of VDAC in cell death: friend or foe?

Kyle S McCommis, Christopher P Baines

Abstract readReview
In one paragraph

Review in Biochimica et biophysica acta, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 71 papers.

0numbers the graph read from it
0cells of the map it votes in
71citing papers in PubMed
4.0field-weighted citation impact, top 5% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

71 citing papers in PubMed, 140 citations in OpenAlex.

  1. Review
  2. Article
  3. Frontiers in pharmacology · 2026
    Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Review
  9. Review
  10. Article
  11. Article
  12. Mitochondrial Permeability Transition in Stem Cells, Development, and Disease.Advances in experimental medicine and biology · 2023
    Review
  13. Article
  14. VDAC2 and the BCL-2 family of proteins.Biochemical Society transactions · 2021
    Review
  15. Review
  16. Review
  17. Review
  18. Article
  19. VDAC-A Primal Perspective.International journal of molecular sciences · 2021
    Review
  20. Article

11 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

2 authors at 1 institution in 1 country.

Kyle S McCommisDepartment of Biomedical Sciences, University of Missouri, USA.
Christopher P Baines
University of Missouri · US

Funding

Molecular Identity of the Cardiac Mitochondrial PoreR01HL094404 · NHLBI · UNIVERSITY OF MISSOURI-COLUMBIA · PI BAINES, CHRISTOPHER P · 2009 to 2018
$3.6M
NHLBI NIH HHS HL094404NHLBI NIH HHS R01 HL094404
6 · The paper itself

Abstract

As the voltage-dependent anion channel (VDAC) forms the interface between mitochondria and the cytosol, its importance in metabolism is well understood. However, research on VDAC's role in cell death is a rapidly growing field, unfortunately with much confusing and contradictory results. The fact that VDAC plays a role in outer mitochondrial membrane permeabilization is undeniable, however, the mechanisms behind this remain very poorly understood. In this review, we will summarize the studies that show evidence of VDAC playing a role in cell death. To begin, we will discuss the evidence for and against VDAC's involvement in mitochondrial permeability transition (MPT) and attempt to clarify that VDAC is not an essential component of the MPT pore (MPTP). Next, we will evaluate the remaining literature on VDAC in cell death which can be divided into three models: proapoptotic agents escaping through VDAC, VDAC homo- or hetero-oligomerization, or VDAC closure resulting in outer mitochondrial membrane permeabilization through an unknown pathway. We will then discuss the growing list of modulators of VDAC activity that have been associated with induction/protection against cell death. This article is part of a Special Issue entitled: VDAC structure, function, and regulation of mitochondrial metabolism.

Indexed as

AnimalsCell DeathHumansMitochondrial Membrane Transport ProteinsMitochondrial Permeability Transition PoreModels, BiologicalModels, GeneticPermeabilityVoltage-Dependent Anion ChannelsMitochondrial Membrane Transport ProteinsMitochondrial Permeability Transition PoreVoltage-Dependent Anion Channels

Identifiers

PMID22062421
PMCPMC3288473
OpenAlexW2098713453

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

None linked

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.