Evidence map›Paper›PMID 28715126›Full record

ArticleThe FEBS journal2017

An engineered photoswitchable mammalian pyruvate kinase.

Stefanie Gehrig, Jamie A Macpherson, Paul C Driscoll, Alastair Symon, Stephen R Martin, James I MacRae, Jens Kleinjung, Franca Fraternali, Dimitrios Anastasiou

Open access · hybridAbstract readEditorial
In one paragraph

Article in The FEBS journal, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.9field-weighted citation impact, top 15% 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

16 citing papers in PubMed, 32 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Review
  5. Article
  6. Article
  7. Engineering an Allosteric Control of Protein Function.The journal of physical chemistry. B · 2021
    Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. A critical review of the role of MBiochimica et biophysica acta. Reviews on cancer · 2019
    Review
  13. Engineering Allostery into Proteins.Advances in experimental medicine and biology · 2019
    Review
  14. Review
  15. Review
  16. 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

9 authors at 2 institutions in 1 country.

Stefanie GehrigCancer Metabolism Laboratory, The Francis Crick Institute, London, UK.
Jamie A MacphersonCancer Metabolism Laboratory, The Francis Crick Institute, London, UK.
Paul C DriscollMetabolomics Science Technology Platform, The Francis Crick Institute, London, UK.
Alastair SymonInstrument Prototyping Science Technology Platform, The Francis Crick Institute, London, UK.
Stephen R MartinStructural Biology Science Technology Platform, The Francis Crick Institute, London, UK.
James I MacRaeMetabolomics Science Technology Platform, The Francis Crick Institute, London, UK.
Jens KleinjungComputational Biology, The Francis Crick Institute, London, UK.
Franca FraternaliRandall Division of Cell and Molecular Biophysics, King's College, London, UK.
Dimitrios AnastasiouCancer Metabolism Laboratory, The Francis Crick Institute, London, UK.ORCID 0000-0002-1269-843X
The Francis Crick Institute · GBKing's College London · GB

Funding

Cancer Research UK FC001033Medical Research Council MC_U117533887Medical Research Council MC_UP_1202/1Wellcome Trust FC001033
6 · The paper itself

Abstract

Changes in allosteric regulation of glycolytic enzymes have been linked to metabolic reprogramming involved in cancer. Remarkably, allosteric mechanisms control enzyme function at significantly shorter time-scales compared to the long-term effects of metabolic reprogramming on cell proliferation. It remains unclear if and how the speed and reversibility afforded by rapid allosteric control of metabolic enzymes is important for cell proliferation. Tools that allow specific, dynamic modulation of enzymatic activities in mammalian cells would help address this question. Towards this goal, we have used molecular dynamics simulations to guide the design of mPKM2 internal light/oxygen/voltage-sensitive domain 2 (LOV2) fusion at position D24 (PiL[D24]), an engineered pyruvate kinase M2 (PKM2) variant that harbours an insertion of the light-sensing LOV2 domain from Avena Sativa within a region implicated in allosteric regulation by fructose 1,6-bisphosphate (FBP). The LOV2 photoreaction is preserved in the PiL[D24] chimera and causes secondary structure changes that are associated with a 30% decrease in the K

Indexed as

Allosteric RegulationAllosteric SiteAmino Acid MotifsApoproteinsAvenaBinding SitesCarrier ProteinsCrystallography, X-RayDNA-Binding ProteinsEscherichia coliFructosediphosphatesGene ExpressionHumansKineticsLightMembrane ProteinsApoproteinsCarrier ProteinsDNA-Binding Proteinsfructose-1,6-diphosphateFructosediphosphatesMembrane ProteinsPlant ProteinsRecombinant Fusion ProteinsThyroid Hormone-Binding ProteinsThyroid HormonesLOV2metabolismmolecular dynamicsoptogeneticsPKM2

Identifiers

PMID28715126
PMCPMC5637921
OpenAlexW2735799196

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.