Evidence map›Paper›PMID 18622693›Full record

ReviewJournal of bioenergetics and biomembranes2008

Genetic strategies for dissecting mammalian and Drosophila voltage-dependent anion channel functions.

William J Craigen, Brett H Graham

Abstract readReview
In one paragraph

Review in Journal of bioenergetics and biomembranes, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
1.5field-weighted citation impact, top 19% 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

28 citing papers in PubMed, 42 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Article
  5. Article
  6. Targeting Mitochondrial Ion Channels to Fight Cancer.International journal of molecular sciences · 2018
    Review
  7. Article
  8. Dynamic energy dependency ofThe Journal of biological chemistry · 2018
    Article
  9. Article
  10. Article
  11. Review
  12. ACTH Action on StAR Biology.Frontiers in neuroscience · 2016
    Review
  13. Motifs of VDAC2 required for mitochondrial Bak import and tBid-induced apoptosis.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  14. Review
  15. Review
  16. Review
  17. Article
  18. Review
  19. Article
  20. Review
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.

William J CraigenDepartment of Molecular and Human Genetics, Baylor College of Medicine, Houston, TX 77030, USA. wcraigen@bcm.edu
Brett H Graham
Baylor College of Medicine · US

Funding

Drosophila VDAC's Role in Mitochondrial FunctionK08HD044808 · NICHD · BAYLOR COLLEGE OF MEDICINE · PI GRAHAM, BRETT HARRISON · 2003 to 2007
$643k
NICHD NIH HHS K08 HD044808
6 · The paper itself

Abstract

Voltage-dependent anion channels (VDACs), also known as mitochondrial porins, are a family of small pore-forming proteins of the mitochondrial outer membrane that are found in all eukaryotes. VDACs are thought to play important roles in the regulated flux of metabolites between the cytosolic and mitochondrial compartments, in overall energy metabolism via interactions with cytosolic kinases, and a debated role in programmed cell death (apoptosis). The mammalian genome contains three VDAC loci termed Vdac1, Vdac2, and Vdac3, raising the question as to what function each isoform may be performing. Based upon expression studies of the mouse VDACs in yeast, biophysical differences can be identified but the physiologic significance of these differences remains unclear. Creation of "knockout" cell lines and mice that lack one or more VDAC isoforms has led to the characterization of distinct phenotypes that provide a different set of insights into function which must be interpreted in the context of complex physiologic systems. Functions in male reproduction, the central nervous system and glucose homeostasis have been identified and require a deeper and more mechanistic examination. Annotation of the genome sequence of Drosophila melanogaster has recently revealed three additional genes (CG17137, CG17139, CG17140) with homology to porin, the previously described gene that encodes the VDAC of D. melanogaster. Molecular analysis of these novel VDACs has revealed a complex pattern of gene organization and expression. Sequence comparisons with other insect VDAC homologs suggest that this gene family evolved through a mechanism of duplication and divergence from an ancestral VDAC gene during the radiation of the genus Drosophila. Striking similarities to mouse VDAC mutants can be found that emphasize the conservation of function over a long evolutionary time frame.

Indexed as

Evolution, MolecularAnimalsApoptosisCytosolDrosophila melanogasterDrosophila ProteinsGenomeHumansMitochondrial ProteinsPhosphotransferasesProtein IsoformsVoltage-Dependent Anion ChannelsDrosophila ProteinsMitochondrial ProteinsPhosphotransferasesporin protein, DrosophilaProtein IsoformsVoltage-Dependent Anion Channels

Identifiers

PMID18622693
PMCPMC4822497
OpenAlexW2004167073

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.