Evidence map›Paper›PMID 1380507›Full record

ReviewJournal of bioenergetics and biomembranes1992

Toward the molecular structure of the mitochondrial channel, VDAC.

C A Mannella, M Forte, M Colombini

Abstract readReview
PubMed Publisher
In one paragraph

Review in Journal of bioenergetics and biomembranes, 1992. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.

0numbers the graph read from it
0cells of the map it votes in
47citing papers in PubMed
–field-weighted citation impact
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

47 citing papers in PubMed.

  1. Review
  2. Review
  3. Article
  4. Article
  5. Review
  6. Review
  7. Article
  8. Article
  9. VDAC structure, selectivity, and dynamics.Biochimica et biophysica acta · 2012
    Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Mini review on the structure and supramolecular assembly of VDAC.Journal of bioenergetics and biomembranes · 2008
    Review
  15. Regulation of hexokinase binding to VDAC.Journal of bioenergetics and biomembranes · 2008
    Review
  16. Structure of the voltage dependent anion channel: state of the art.Journal of bioenergetics and biomembranes · 2008
    Review
  17. Article
  18. Article
  19. Article
  20. The voltage-dependent anion channel, a major component of the tRNA import machinery in plant mitochondria.Proceedings of the National Academy of Sciences of the United States of America · 2006
    Article
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.

C A MannellaWadsworth Center for Laboratories and Research, New York State Department of Health, Albany 12201-0509.
M Forte
M Colombini

Funding

NIGMS NIH HHS GM 35759
6 · The paper itself

Abstract

A summary is presented of the most recent information about the structure and mechanism of closure of the mitochondrial channel, VDAC. Considerable information has come from studies involving electron microscopy of two-dimensional crystals and from electrophysiological studies of wild-type channels and site-directed mutants. Available evidence points to a beta-barrel as the basic structural model for VDAC. Two models for voltage- or effector- induced closure have been proposed, the first involving removal of strands from the wall of the pore, the second invoking movement of protein domains into the lumen. Experimental strategies to resolve the actual mechanism are presented.

Indexed as

PorinsAmino Acid SequenceIon Channel GatingIon ChannelsMembrane ProteinsMitochondriaMolecular Sequence DataProtein ConformationVoltage-Dependent Anion ChannelsIon ChannelsMembrane ProteinsPorinsVoltage-Dependent Anion Channels

Identifiers

PMID1380507

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.