Evidence map›Paper›PMID 39992503›Full record

ArticleMethods in molecular biology (Clifton, N.J.)2025

FRET-Based Sensor for Measuring Adenine Nucleotide Binding to AMPK.

Roland Abi Nahed, Martin Pelosse, Francesco Aulicino, Florine Cottaz, Imre Berger, Uwe Schlattner

Abstract read
PubMed Publisher
In one paragraph

Article in Methods in molecular biology (Clifton, N.J.), 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
–field-weighted citation impact
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

1 citing paper in PubMed.

  1. 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

6 authors.

Roland Abi NahedUniv. Grenoble Alpes, INSERM U1055, Laboratory of Fundamental and Applied Bioenergetics (LBFA), 2280 Rue de la Piscine, Domaine Universitaire Gières, Grenoble, France.
Martin PelosseUniv. Grenoble Alpes, INSERM U1055, Laboratory of Fundamental and Applied Bioenergetics (LBFA), 2280 Rue de la Piscine, Domaine Universitaire Gières, Grenoble, France.
Francesco AulicinoBristol Synthetic Biology Centre BrisSynBio, Biomedical Sciences, School of Biochemistry, University of Bristol, 1 Tankard's Close, Bristol BSH 1TD, United Kingdom, Bristol, UK.
Florine CottazUniv. Grenoble Alpes, INSERM U1055, Laboratory of Fundamental and Applied Bioenergetics (LBFA), 2280 Rue de la Piscine, Domaine Universitaire Gières, Grenoble, France.
Imre BergerBristol Synthetic Biology Centre BrisSynBio, Biomedical Sciences, School of Biochemistry, University of Bristol, 1 Tankard's Close, Bristol BSH 1TD, United Kingdom, Bristol, UK.
Uwe SchlattnerUniv. Grenoble Alpes, INSERM U1055, Laboratory of Fundamental and Applied Bioenergetics (LBFA), 2280 Rue de la Piscine, Domaine Universitaire Gières, Grenoble, France. uwe.schlattner@univ-grenoble-alpes.fr.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

AMP-activated protein kinase (AMPK) has evolved to detect a critical increase in cellular AMP/ATP and ADP/ATP concentration ratios as a signal for limiting energy supply. Such energy stress then leads to AMPK activation and downstream events that maintain cellular energy homeostasis. AMPK activation by AMP, ADP, or pharmacological activators involves a conformational switch within the AMPK heterotrimeric complex. We have engineered an AMPK-based sensor, AMPfret, which translates the activating conformational switch into a fluorescence signal, based on increased fluorescence resonance energy transfer (FRET) between donor and acceptor fluorophores. Here we describe how this sensor can be used to analyze direct AMPK activation by small molecules in vitro using a fluorimeter, or to estimate changes in the energy state of cells using standard fluorescence or confocal microscopy.

Indexed as

Adenine NucleotidesAMP-Activated Protein KinasesBiosensing TechniquesFluorescence Resonance Energy TransferEnzyme ActivationHumansProtein BindingAdenine NucleotidesAMP-Activated Protein KinasesADPAMPAMP-activated protein kinaseATPCellular energy stateFluorescence resonance energy transferGenetically encoded sensorsLarge cargo vectors

Identifiers

PMID39992503

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.