Evidence map›Paper›PMID 29748232›Full record

ArticleThe Biochemical journal2018

An allostatic mechanism for M2 pyruvate kinase as an amino-acid sensor.

Meng Yuan, Iain W McNae, Yiyuan Chen, Elizabeth A Blackburn, Martin A Wear, Paul A M Michels, Linda A Fothergill-Gilmore, Ted Hupp, Malcolm D Walkinshaw

Open access · hybridAbstract read
In one paragraph

Article in The Biochemical journal, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

38 citing papers in PubMed, 63 citations in OpenAlex.

  1. Article
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  8. Animal amino acid sensor - A review.Animal bioscience · 2025
    Article
  9. Review
  10. Article
  11. Review
  12. Metabolically regulated spiking could serve neuronal energy homeostasis and protect from reactive oxygen species.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  13. S-lactoyl modification of KEAP1 by a reactive glycolytic metabolite activates NRF2 signaling.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  14. Article
  15. 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

9 authors at 2 institutions in 1 country.

Meng YuanCentre for Translational and Chemical Biology, School of Biological Sciences, University of Edinburgh, Michael Swann Building, Max Born Crescent, Edinburgh EH9 3BF, U.K.ORCID 0000-0001-9754-4503
Iain W McNaeCentre for Translational and Chemical Biology, School of Biological Sciences, University of Edinburgh, Michael Swann Building, Max Born Crescent, Edinburgh EH9 3BF, U.K.
Yiyuan ChenCentre for Translational and Chemical Biology, School of Biological Sciences, University of Edinburgh, Michael Swann Building, Max Born Crescent, Edinburgh EH9 3BF, U.K.
Elizabeth A BlackburnCentre for Translational and Chemical Biology, School of Biological Sciences, University of Edinburgh, Michael Swann Building, Max Born Crescent, Edinburgh EH9 3BF, U.K.
Martin A WearCentre for Translational and Chemical Biology, School of Biological Sciences, University of Edinburgh, Michael Swann Building, Max Born Crescent, Edinburgh EH9 3BF, U.K.
Paul A M MichelsCentre for Translational and Chemical Biology, School of Biological Sciences, University of Edinburgh, Michael Swann Building, Max Born Crescent, Edinburgh EH9 3BF, U.K.ORCID 0000-0003-3726-6104
Linda A Fothergill-GilmoreCentre for Translational and Chemical Biology, School of Biological Sciences, University of Edinburgh, Michael Swann Building, Max Born Crescent, Edinburgh EH9 3BF, U.K.ORCID 0000-0002-7218-4393
Ted HuppCell Signalling Unit, p53 Signal Transduction Laboratories, Institute of Genetics and Molecular Medicine, University of Edinburgh Cancer Research Centre, Edinburgh EH4 2XR, U.K.
Malcolm D WalkinshawCentre for Translational and Chemical Biology, School of Biological Sciences, University of Edinburgh, Michael Swann Building, Max Born Crescent, Edinburgh EH9 3BF, U.K. m.walkinshaw@ed.ac.uk.ORCID 0000-0001-5955-9325
Wellcome Centre for Cell Biology · GBEdinburgh Cancer Research · GB

Funding

Biotechnology and Biological Sciences Research CouncilMedical Research Council MC_PC_16043Wellcome Trust 101527/Z/13/Z
6 · The paper itself

Abstract

We have tested the effect of all 20 proteinogenic amino acids on the activity of the M2 isoenzyme of pyruvate kinase (M2PYK) and show that, within physiologically relevant concentrations, phenylalanine, alanine, tryptophan, methionine, valine, and proline act as inhibitors, while histidine and serine act as activators. Size exclusion chromatography has been used to show that all amino acids, whether activators or inhibitors, stabilise the tetrameric form of M2PYK. In the absence of amino-acid ligands an apparent tetramer-monomer dissociation

Indexed as

Allosteric RegulationAmino AcidsCatalytic DomainCell ProliferationCrystallography, X-RayHumansProtein ConformationProtein MultimerizationPyruvate KinaseAmino AcidsPyruvate Kinaseallostatic regulationamino-acid regulationenzyme mechanismpyruvate kinase

Identifiers

PMID29748232
PMCPMC5980995
OpenAlexW2801250283

What OpenQuestion 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 OpenQuestion graph.