Evidence map›Paper›PMID 15240503›Full record

ArticleBiophysical journal2004

Analysis of functional coupling: mitochondrial creatine kinase and adenine nucleotide translocase.

Marko Vendelin, Maris Lemba, Valdur A Saks

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
3.1field-weighted citation impact, top 8% 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

31 citing papers in PubMed, 75 citations in OpenAlex.

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  6. International journal of molecular sciences · 2020
    Review
  7. Metabolic compartmentation in rainbow trout cardiomyocytes: coupling of hexokinase but not creatine kinase to mitochondrial respiration.Journal of comparative physiology. B, Biochemical, systemic, and environmental physiology · 2017
    Article
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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 3 institutions in 2 countries.

Marko VendelinLaboratory of Fundamental and Applied Bioenergetics, Institut National de la Santé et de la Recherche Médicale E0221, Joseph Fourier University, Grenoble, France. markov@ioc.ee
Maris Lemba
Valdur A Saks
Laboratory of Fundamental and Applied Bioenergetics · FRTallinn University of Technology · EEUniversité Joseph Fourier · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The mechanism of functional coupling between mitochondrial creatine kinase (MiCK) and adenine nucleotide translocase (ANT) in isolated heart mitochondria is analyzed. Two alternative mechanisms are studied: 1), dynamic compartmentation of ATP and ADP, which assumes the differences in concentrations of the substrates between intermembrane space and surrounding solution due to some diffusion restriction and 2), direct transfer of the substrates between MiCK and ANT. The mathematical models based on these possible mechanisms were composed and simulation results were compared with the available experimental data. The first model, based on a dynamic compartmentation mechanism, was not sufficient to reproduce the measured values of apparent dissociation constants of MiCK reaction coupled to oxidative phosphorylation. The second model, which assumes the direct transfer of substrates between MiCK and ANT, is shown to be in good agreement with experiments--i.e., the second model reproduced the measured constants and the estimated ADP flux, entering mitochondria after the MiCK reaction. This model is thermodynamically consistent, utilizing the free energy profiles of reactions. The analysis revealed the minimal changes in the free energy profile of the MiCK-ANT interaction required to reproduce the experimental data. A possible free energy profile of the coupled MiCK-ANT system is presented.

Indexed as

Models, TheoreticalOxidative PhosphorylationAdenosine DiphosphateAdenosine TriphosphateAnimalsComputer SimulationCreatine KinaseCreatine Kinase, Mitochondrial FormDiffusionHumansIsoenzymesMitochondriaMitochondrial ADP, ATP TranslocasesThermodynamicsAdenosine DiphosphateAdenosine TriphosphateCreatine KinaseCreatine Kinase, Mitochondrial FormIsoenzymesMitochondrial ADP, ATP Translocases

Identifiers

PMID15240503
PMCPMC1304393
OpenAlexW2004464716

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.