Evidence map›Paper›PMID 23054077›Full record

ReviewJournal of bioenergetics and biomembranes2013

The mitochondrial oxoglutarate carrier: from identification to mechanism.

Magnus Monné, Daniela Valeria Miniero, Vito Iacobazzi, Faustino Bisaccia, Giuseppe Fiermonte

Erratum issuedOpen access · greenAbstract readReview
PubMed Publisher
In one paragraph

Review in Journal of bioenergetics and biomembranes, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
1.3field-weighted citation impact, top 20% 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

36 citing papers in PubMed, 57 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Clinical Translation of HyperpolarizedAJNR. American journal of neuroradiology · 2025
    Review
  5. Article
  6. Redirecting Intermediary Metabolism to Counteract Cyanide Poisoning.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2025
    Review
  7. Review
  8. Review
  9. Article
  10. Review
  11. Review
  12. Review
  13. Review
  14. Article
  15. The SLC25A47 locus controls gluconeogenesis and energy expenditure.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  16. Article
  17. Review
  18. Structures ofScience (New York, N.Y.) · 2022
    Article
  19. Review
  20. Article
4 · The record

Corrections and comments

  • Erratum issued
    Iacobazzi, Vito [added]
5 · Who and what money

Authors and funding

5 authors at 2 institutions in 1 country.

Magnus MonnéDepartment of Biosciences, Biotechnology and Pharmacological Sciences, Laboratory of Biochemistry and Molecular Biology, University of Bari, Via E. Orabona 4, 70125 Bari, Italy. magmon@farmbiol.uniba.it
Daniela Valeria Miniero
Vito Iacobazzi
Faustino Bisaccia
Giuseppe Fiermonte
University of Bari Aldo Moro · ITUniversity of Basilicata · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The 2-oxoglutarate carrier (OGC) belongs to the mitochondrial carrier protein family whose members are responsible for the exchange of metabolites, cofactors and nucleotides between the cytoplasm and mitochondrial matrix. Initially, OGC was characterized by determining substrate specificity, kinetic parameters of transport, inhibitors and molecular probes that form covalent bonds with specific residues. It was shown that OGC specifically transports oxoglutarate and certain carboxylic acids. The substrate specificity combination of OGC is unique, although many of its substrates are also transported by other mitochondrial carriers. The abundant recombinant expression of bovine OGC in Escherichia coli and its ability to functionally reconstitute into proteoliposomes made it possible to deduce the individual contribution of each and every residue of OGC to the transport activity by a complete set of cys-scanning mutants. These studies give experimental support for a substrate binding site constituted by three major contact points on the even-numbered α-helices and identifies other residues as important for transport function through their crucial positions in the structure for conserved interactions and the conformational changes of the carrier during the transport cycle. The results of these investigations have led to utilize OGC as a model protein for understanding the transport mechanism of mitochondrial carriers.

Indexed as

CytoplasmKetoglutaric AcidsMembrane Transport ProteinsMitochondriaMitochondrial ProteinsModels, BiologicalAmino Acid SubstitutionAnimalsBiological Transport, ActiveCattleEscherichia coliHumansMutagenesisMutation, MissenseProtein Structure, SecondaryProtein Structure, TertiaryKetoglutaric AcidsMembrane Transport ProteinsMitochondrial Proteinsoxoglutarate translocatorRecombinant Proteins

Identifiers

PMID23054077
OpenAlexW2077950462

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.