Evidence map›Paper›PMID 19117541›Full record

ArticleCell metabolism2009

Branching out on AMPK Regulation.

David Carling

Open access · bronzeAbstract readComment
PubMed Publisher
In one paragraph

Article in Cell metabolism, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
0.4field-weighted citation impact, top 38% 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

5 citing papers in PubMed, 9 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

1 author at 1 institution in 1 country.

David CarlingCellular Stress Group, MRC Clinical Sciences Centre, Imperial College, Hammersmith Hospital Campus, DuCane Road, London W12 0NN, UK. dcarling@imperial.ac.uk
Hammersmith Hospital · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

AMP-activated protein kinase (AMPK) regulates cellular metabolism in response to available energy at both the cellular and whole-body levels. In this issue, McBride et al. (2009) show that AMPK is inhibited by glycogen, adding another tier to its regulation and suggesting that it can act as a glycogen sensor.

Indexed as

Allosteric RegulationAMP-Activated Protein KinasesBinding SitesEnergy MetabolismGlycogenGlycogen SynthasePhosphorylationAMP-Activated Protein KinasesGlycogenGlycogen Synthase

Identifiers

PMID19117541
OpenAlexW1977987328

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.