Evidence map›Paper›PMID 28302767›Full record

ArticleThe Biochemical journal2017

Effect of different γ-subunit isoforms on the regulation of AMPK.

Robin Willows, Naveenan Navaratnam, Ana Lima, Jon Read, David Carling

Open access · hybridAbstract readComparative Study
In one paragraph

Article in The Biochemical journal, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed
1.8field-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

40 citing papers in PubMed, 56 citations in OpenAlex.

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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

5 authors at 4 institutions in 2 countries.

Robin WillowsCellular Stress Group, Medical Research Council London Institute of Medical Sciences, Hammersmith Hospital, Imperial College, London W12 0NN, U.K.
Naveenan NavaratnamCellular Stress Group, Medical Research Council London Institute of Medical Sciences, Hammersmith Hospital, Imperial College, London W12 0NN, U.K.
Ana LimaCellular Stress Group, Medical Research Council London Institute of Medical Sciences, Hammersmith Hospital, Imperial College, London W12 0NN, U.K.
Jon ReadAstraZeneca R&D, Discovery Sciences, Darwin Building, 310 Cambridge Science Park, Milton Road, Cambridge CB4 0WG, U.K.
David CarlingCellular Stress Group, Medical Research Council London Institute of Medical Sciences, Hammersmith Hospital, Imperial College, London W12 0NN, U.K.
Hammersmith Hospital · GBAstraZeneca (Singapore) · SGImperial College London · GBMedical Research Council · GB

Funding

British Heart FoundationMedical Research Council G0301081Medical Research Council MC_U120027537MRF_ MRF-023-0004-S-WILLO
6 · The paper itself

Abstract

AMP-activated protein kinase (AMPK) plays a key role in integrating metabolic pathways in response to energy demand. AMPK activation results in a wide range of downstream responses, many of which are associated with improved metabolic outcome, making AMPK an attractive target for the treatment of metabolic diseases. AMPK is a heterotrimeric complex consisting of a catalytic subunit (α) and two regulatory subunits (β and γ). The γ-subunit harbours the nucleotide-binding sites and plays an important role in AMPK regulation in response to cellular energy levels. In mammals, there are three isoforms of the γ-subunit and these respond differently to regulation by nucleotides, but there is limited information regarding their role in activation by small molecules. Here, we determined the effect of different γ-isoforms on AMPK by a direct activator, 991. In cells, 991 led to a greater activation of γ2-containing AMPK complexes compared with either γ1 or γ3. This effect was dependent on the long N-terminal region of the γ2-isoform. We were able to rule out an effect of Ser

Indexed as

Allosteric RegulationAmino Acid SubstitutionAminopyridinesAMP-Activated Protein KinasesBenzimidazolesBenzoatesBinding SitesCRISPR-Cas SystemsEnzyme ActivationEnzyme ActivatorsHEK293 CellsHumansIndolesIsoenzymesLigandsMutation5-((6-chloro-5-(1-methylindol-5-yl)-1H-benzimidazol-2-yl)oxy)-2-methylbenzoic acidAminopyridinesAMP-Activated Protein KinasesBenzimidazolesBenzoatesEnzyme ActivatorsIndolesIsoenzymesLigandsPF-249PRKAG1 protein, humanPRKAG2 protein, humanPRKAG3 protein, humanRecombinant ProteinsThreonineAMPKmetabolic regulationprotein–serine–threonine kinases

Identifiers

PMID28302767
PMCPMC5423082
OpenAlexW2596621042

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.