Evidence map›Paper›PMID 20708406›Full record

ReviewTrends in biochemical sciences2010

The 3D structures of VDAC represent a native conformation.

Sebastian Hiller, Jeff Abramson, Carmen Mannella, Gerhard Wagner, Kornelius Zeth

Abstract readReview
In one paragraph

Review in Trends in biochemical sciences, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 68 papers.

0numbers the graph read from it
0cells of the map it votes in
68citing 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

68 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. VDAC-A Primal Perspective.International journal of molecular sciences · 2021
    Review
  19. Review
  20. Article

8 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

5 authors.

Sebastian HillerDepartment of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, 240 Longwood Ave., Boston, MA 02115, USA.
Jeff Abramson
Carmen Mannella
Gerhard Wagner
Kornelius Zeth

Funding

T CELL SPECIFIC TRANSCRIPTION COMPLEXESP01GM047467 · NIGMS · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI WAGNER, GERHARD · 1992 to 2017
$28.6M
Structures of sodium glucose transporters by cryo electron microscopyR01GM078844 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI ABRAMSON, JEFFREY S · 2006 to 2018
$5.3M
Structure and interactions of the Voltage-Dependent Anion Channel(VDAC)R01GM075879 · NIGMS · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI WAGNER, GERHARD · 2005 to 2013
$2.3M
NIGMS NIH HHS GM075879NIGMS NIH HHS P01 GM047467NIGMS NIH HHS R01 GM075879NIGMS NIH HHS R01 GM078844
6 · The paper itself

Abstract

The most abundant protein of the mitochondrial outer membrane is the voltage-dependent anion channel (VDAC), which facilitates the exchange of ions and molecules between mitochondria and cytosol and is regulated by interactions with other proteins and small molecules. VDAC has been studied extensively for more than three decades, and last year three independent investigations revealed a structure of VDAC-1 exhibiting 19 transmembrane beta-strands, constituting a unique structural class of beta-barrel membrane proteins. Here, we provide a historical perspective on VDAC research and give an overview of the experimental design used to obtain these structures. Furthermore, we validate the protein refolding approach and summarize the biochemical and biophysical evidence that links the 19-stranded structure to the native form of VDAC.

Indexed as

AnimalsHumansMicroscopy, Atomic ForceMicroscopy, ElectronMitochondrial ProteinsProtein FoldingVoltage-Dependent Anion ChannelsMitochondrial ProteinsVoltage-Dependent Anion Channels

Identifiers

PMID20708406
PMCPMC2933295

What OpenQuestion holds

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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.