Evidence map›Paper›PMID 16167170›Full record

ArticleJournal of bioenergetics and biomembranes2005

On the role of VDAC in apoptosis: fact and fiction.

Tatiana K Rostovtseva, Wenzhi Tan, Marco Colombini

Abstract read
PubMed Publisher
In one paragraph

Article in Journal of bioenergetics and biomembranes, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 106 papers.

0numbers the graph read from it
0cells of the map it votes in
106citing papers in PubMed
8.8field-weighted citation impact, top 1% 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

106 citing papers in PubMed, 238 citations in OpenAlex.

  1. Review
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  3. Review
  4. Review
  5. Article
  6. Pepsin enhances glycolysis to promote malignant transformation of vocal fold leukoplakia epithelial cells with dysplasia.European archives of oto-rhino-laryngology : official journal of the European Federation of Oto-Rhino-Laryngological Societies (EUFOS) : affiliated with the German Society for Oto-Rhino-Laryngology - Head and Neck Surgery · 2023
    Article
  7. Review
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  9. Article
  10. Review
  11. Article
  12. Involvement of Bcl-xL in Neuronal Function and Development.International journal of molecular sciences · 2021
    Review
  13. Review
  14. Article
  15. Review
  16. Review
  17. Miro: A molecular switch at the center of mitochondrial regulation.Protein science : a publication of the Protein Society · 2020
    Review
  18. Review
  19. Article
  20. Article

46 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

3 authors at 2 institutions in 2 countries.

Tatiana K RostovtsevaLaboratory of Physical and Structural Biology, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20892, USA. rostovtt@mail.nih.gov
Wenzhi Tan
Marco Colombini
University of Maryland, College Park · USNational Institutes of Health · US

Funding

Channel Formation by Ceramides: Implication on ApoptosisR01NS042025 · NINDS · UNIV OF MARYLAND, COLLEGE PARK · PI COLOMBINI, MARCO · 2003 to 2006
$841k
NINDS NIH HHS NS 42025
6 · The paper itself

Abstract

Research on VDAC has accelerated as evidence grows of its importance in mitochondrial function and in apoptosis. New investigators entering the field are often confounded by the VDAC literature and its many apparent conflicts and contradictions. This review is an effort to shed light on the situation and identify reliable information from more questionable claims. Our views on the most important controversial issues are as follows: VDAC is only present in the mitochondrial outer membrane. VDAC functions as a monomer. VDAC functions normally with or without Ca(2+). It does not form channels that mediate the flux of proteins through membranes (peptides and unfolded proteins are excluded from this statement). Closure of VDAC, not VDAC opening, leads to mitochondria outer membrane permeabilization and apoptosis.

Indexed as

AnimalsApoptosisCalciumDimerizationHexokinaseHumansIon Channel GatingIon ChannelsMitochondriaMitochondrial MembranesMitochondrial Membrane Transport ProteinsMitochondrial Permeability Transition PoreProto-Oncogene Proteins c-bcl-2Reactive Oxygen SpeciesVoltage-Dependent Anion ChannelsCalciumHexokinaseIon ChannelsMitochondrial Membrane Transport ProteinsMitochondrial Permeability Transition PoreProto-Oncogene Proteins c-bcl-2Reactive Oxygen SpeciesVoltage-Dependent Anion Channels

Identifiers

PMID16167170
OpenAlexW2043364216

What OpenQuestion holds

Textmetadata
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.