Evidence map›Paper›PMID 30833561›Full record

ArticleNature communications2019

Synthetic energy sensor AMPfret deciphers adenylate-dependent AMPK activation mechanism.

Martin Pelosse, Cécile Cottet-Rousselle, Cécile M Bidan, Aurélie Dupont, Kapil Gupta, Imre Berger, Uwe Schlattner

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2019. 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
5.3field-weighted citation impact, top 3% 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, 94 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. FRET-Based Sensor for Measuring Adenine Nucleotide Binding to AMPK.Methods in molecular biology (Clifton, N.J.) · 2025
    Article
  5. Article
  6. Autophagy and cancer therapy.Cancer letters · 2024
    Review
  7. Review
  8. Article
  9. Review
  10. Review
  11. Review
  12. Article
  13. 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

7 authors at 3 institutions in 2 countries.

Martin PelosseUniversity of Grenoble Alpes and INSERM U1055, Laboratory of Fundamental and Applied Bioenergetics (LBFA) and SFR Environmental and Systems Biology (BEeSy), Rue de la Piscine, Domaine Universitaire, 38610, Gières, France.
Cécile Cottet-RousselleUniversity of Grenoble Alpes and INSERM U1055, Laboratory of Fundamental and Applied Bioenergetics (LBFA) and SFR Environmental and Systems Biology (BEeSy), Rue de la Piscine, Domaine Universitaire, 38610, Gières, France.
Cécile M BidanUniversity of Grenoble Alpes, CNRS, Laboratoire Interdisciplinaire de Physique (LIPhy), 140 Rue de la Physique, 38402, Saint-Martin-d'Hères, France.ORCID http://orcid.org/0000-0002-6243-562X
Aurélie DupontUniversity of Grenoble Alpes, CNRS, Laboratoire Interdisciplinaire de Physique (LIPhy), 140 Rue de la Physique, 38402, Saint-Martin-d'Hères, France.
Kapil GuptaBristol Synthetic Biology Centre BrisSynBio, Biomedical Sciences, University of Bristol, 1 Tankard's Close, Bristol, BS8 1TD, UK.
Imre BergerBristol Synthetic Biology Centre BrisSynBio, Biomedical Sciences, University of Bristol, 1 Tankard's Close, Bristol, BS8 1TD, UK. imre.berger@bristol.ac.uk.ORCID http://orcid.org/0000-0001-7518-9045
Uwe SchlattnerUniversity of Grenoble Alpes and INSERM U1055, Laboratory of Fundamental and Applied Bioenergetics (LBFA) and SFR Environmental and Systems Biology (BEeSy), Rue de la Piscine, Domaine Universitaire, 38610, Gières, France. uwe.schlattner@univ-grenoble-alpes.fr.ORCID http://orcid.org/0000-0003-1159-5911
Inserm · FRCentre National de la Recherche Scientifique · FRUniversity of Bristol · GB

Funding

Biotechnology and Biological Sciences Research Council BB/L01386X/1
6 · The paper itself

Abstract

AMP-activated protein kinase AMPK senses and regulates cellular energy state. AMPK activation by increasing AMP and ADP concentrations involves a conformational switch within the heterotrimeric complex. This is exploited here for the construction of a synthetic sensor of cellular energetics and allosteric AMPK activation, AMPfret. Based on engineered AMPK fused to fluorescent proteins, the sensor allows direct, real-time readout of the AMPK conformational state by fluorescence resonance energy transfer (FRET). AMPfret faithfully and dynamically reports the binding of AMP and ADP to AMPK γ-CBS sites, competed by Mg

Indexed as

Protein Engineering3T3 CellsAdenosine DiphosphateAdenosine MonophosphateAdenosine TriphosphateAllosteric RegulationAMP-Activated Protein KinasesAnimalsBinding SitesEnzyme ActivationEnzyme AssaysFluorescence Resonance Energy TransferHeLa CellsHumansKineticsLuminescent ProteinsAdenosine DiphosphateAdenosine MonophosphateAdenosine TriphosphateAMP-Activated Protein KinasesLuminescent ProteinsPRKAA2 protein, human

Identifiers

PMID30833561
PMCPMC6399333
OpenAlexW2920392167

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.