Evidence map›Paper›PMID 19377834›Full record

ReviewJournal of bioenergetics and biomembranes2009

Recent advances in structure-functional studies of mitochondrial factor B.

Grigory I Belogrudov

Open access · greenAbstract readReview
In one paragraph

Review in Journal of bioenergetics and biomembranes, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
0.9field-weighted citation impact, top 26% 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

10 citing papers in PubMed, 17 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Review
  5. Regulation of mitochondrial ATP synthase in cardiac pathophysiology.American journal of cardiovascular disease · 2015
    Review
  6. Article
  7. Cardiac mitochondrial matrix and respiratory complex protein phosphorylation.American journal of physiology. Heart and circulatory physiology · 2012
    Review
  8. Mitochondrial ATP synthase: architecture, function and pathology.Journal of inherited metabolic disease · 2012
    Review
  9. Article
  10. Coupling factor B affects the morphology of mitochondria.Journal of bioenergetics and biomembranes · 2010
    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

1 author at 1 institution in 1 country.

Grigory I BelogrudovWest Los Angeles Veterans Administration Medical Center, 11301 Wilshire Blvd., Los Angeles, CA 90073, USA. gbelo@ucla.edu
West Los Angeles College · US

Funding

Factor B and energy coupling in mitochondriaR01GM066085 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI BELOGRUDOV, GRIGORY I · 2003 to 2007
$1.0M
NIGMS NIH HHS R01 GM066085
6 · The paper itself

Abstract

Since the early studies on the resolution and reconstitution of the oxidative phosphorylation system from animal mitochondria, coupling factor B was recognized as an essential component of the machinery responsible for energy-driven ATP synthesis. At the phenomenological level, factor B was agreed to lie at the interface of energy transfer between the respiratory chain and the ATP synthase complex. However, biochemical characterization of the factor B polypeptide has proved difficult. It was not until 1990 that the N-terminal amino acid sequence of bovine mitochondrial factor B was reported, which followed, a decade later, by the report describing the amino acid sequence of full-length human factor B and its functional characterization. The present review summarizes the recent advances in structure-functional studies of factor B, including its recently determined crystal structure at 0.96 A resolution. Ectopic expression of human factor B in cultured animal cells has unexpectedly revealed its role in shaping mitochondrial morphology. The supramolecular assembly of ATP synthase as dimer ribbons at highly curved apices of the mitochondrial cristae was recently suggested to optimize ATP synthesis under proton-limited conditions. We propose that the binding of the ATP synthase dimers with factor B tetramers could be a means to enhance the efficiency of the terminal step of oxidative phosphorylation in animal mitochondria.

Indexed as

Oxidative PhosphorylationAdenosine TriphosphateAnimalsATP Synthetase ComplexesCattleCell LineElectron TransportHumansMitochondriaMitochondrial Proton-Translocating ATPasesOxidative Phosphorylation Coupling FactorsProtein Structure, QuaternaryProtein Structure, TertiaryStructure-Activity RelationshipAdenosine TriphosphateATP Synthetase Complexescoupling factor BMitochondrial Proton-Translocating ATPasesOxidative Phosphorylation Coupling Factors

Identifiers

PMID19377834
PMCPMC2880480
OpenAlexW2041429755

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.