Evidence map›Paper›PMID 30979775›Full record

ArticleThe EMBO journal2019

The yeast mitochondrial pyruvate carrier is a hetero-dimer in its functional state.

Sotiria Tavoulari, Chancievan Thangaratnarajah, Vasiliki Mavridou, Michael E Harbour, Jean-Claude Martinou, Edmund Rs Kunji

Open access · hybridAbstract read
In one paragraph

Article in The EMBO journal, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.

0numbers the graph read from it
0cells of the map it votes in
51citing papers in PubMed
3.3field-weighted citation impact, top 7% 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

51 citing papers in PubMed, 70 citations in OpenAlex.

  1. 6PPD and 6PPD-Q Induce Mitochondrial Dysfunction inInternational journal of molecular sciences · 2026
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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

6 authors at 2 institutions in 2 countries.

Sotiria TavoulariMedical Research Council Mitochondrial Biology Unit, University of Cambridge, Cambridge, UK st632@mrc-mbu.cam.ac.uk ek@mrc-mbu.cam.ac.uk.ORCID 0000-0002-4263-8905
Chancievan ThangaratnarajahMedical Research Council Mitochondrial Biology Unit, University of Cambridge, Cambridge, UK.
Vasiliki MavridouMedical Research Council Mitochondrial Biology Unit, University of Cambridge, Cambridge, UK.
Michael E HarbourMedical Research Council Mitochondrial Biology Unit, University of Cambridge, Cambridge, UK.
Jean-Claude MartinouDepartment of Cell Biology, University of Geneva, Genève 4, Switzerland.
Edmund Rs KunjiMedical Research Council Mitochondrial Biology Unit, University of Cambridge, Cambridge, UK st632@mrc-mbu.cam.ac.uk ek@mrc-mbu.cam.ac.uk.ORCID 0000-0002-0610-4500
University of Cambridge · GBUniversity of Geneva · CH

Funding

Cancer Research UK 21617Medical Research Council MC_U105663139Medical Research Council MC_UU_00015/1
6 · The paper itself

Abstract

The mitochondrial pyruvate carrier (MPC) is critical for cellular homeostasis, as it is required in central metabolism for transporting pyruvate from the cytosol into the mitochondrial matrix. MPC has been implicated in many diseases and is being investigated as a drug target. A few years ago, small membrane proteins, called MPC1 and MPC2 in mammals and Mpc1, Mpc2 and Mpc3 in yeast, were proposed to form large protein complexes responsible for this function. However, the MPC complexes have never been isolated and their composition, oligomeric state and functional properties have not been defined. Here, we identify the functional unit of MPC from

Indexed as

Anion Transport ProteinsMitochondrial Membrane Transport ProteinsMonocarboxylic Acid TransportersSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsGene Expression Regulation, FungalMultiprotein ComplexesOrganisms, Genetically ModifiedProtein MultimerizationProtein Structure, QuaternaryPyruvic AcidStructure-Activity RelationshipTemperatureAnion Transport ProteinsFMP37 protein, S cerevisiaeFMP43 protein, S cerevisiaeMitochondrial Membrane Transport ProteinsMonocarboxylic Acid TransportersMPC2 protein, S cerevisiaeMultiprotein ComplexesPyruvic AcidSaccharomyces cerevisiae Proteinsmitochondriaoligomeric stateprotein complexpyruvatetransport proteins

Identifiers

PMID30979775
PMCPMC6517818
OpenAlexW2939652298

What Socratic holds

Textmetadata
LicenceCC BY
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 Socratic graph.