Evidence map›Paper›PMID 29343628›Full record

ReviewJournal of the Royal Society, Interface2018

Keeping the home fires burning: AMP-activated protein kinase.

D Grahame Hardie

Open access · hybridAbstract readReview
In one paragraph

Review in Journal of the Royal Society, Interface, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 105 papers.

0numbers the graph read from it
0cells of the map it votes in
105citing papers in PubMed
9.8field-weighted citation impact, top 1% 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

105 citing papers in PubMed, 182 citations in OpenAlex.

  1. Article
  2. International journal of medical sciences · 2026
    Article
  3. Frontiers in veterinary science · 2026
    Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Five unaddressed questions about cytokinin biosynthesis.Journal of experimental botany · 2025
    Review
  10. Article
  11. Sleep deprivation stimulates adaptive thermogenesis by activating AMPK pathway in mice.Journal of comparative physiology. B, Biochemical, systemic, and environmental physiology · 2025
    Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article

45 more citing papers are in PubMed but not listed here.

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

1 author at 1 institution in 2 countries.

D Grahame HardieDivision of Cell Signalling and Immunology, School of Life Sciences, University of Dundee, Dow Street, Dundee, DD1 5EH, UK d.g.hardie@dundee.ac.uk.ORCID 0000-0002-8373-7379
Google (United States) · US

Funding

Cancer Research UK 15101Cancer Research UK C37030/A15101Wellcome Trust 204766/Z/16/Z
6 · The paper itself

Abstract

Living cells obtain energy either by oxidizing reduced compounds of organic or mineral origin or by absorbing light. Whichever energy source is used, some of the energy released is conserved by converting adenosine diphosphate (ADP) to adenosine triphosphate (ATP), which are analogous to the chemicals in a rechargeable battery. The energy released by the conversion of ATP back to ADP is used to drive most energy-requiring processes, including cell growth, cell division, communication and movement. It is clearly essential to life that the production and consumption of ATP are always maintained in balance, and the AMP-activated protein kinase (AMPK) is one of the key cellular regulatory systems that ensures this. In eukaryotic cells (cells with nuclei and other internal membrane-bound structures, including human cells), most ATP is produced in mitochondria, which are thought to have been derived by the engulfment of oxidative bacteria by a host cell not previously able to use molecular oxygen. AMPK is activated by increasing AMP or ADP (AMP being generated from ADP whenever ADP rises) coupled with falling ATP. Relatives of AMPK are found in essentially all eukaryotes, and it may have evolved to allow the host cell to monitor the output of the newly acquired mitochondria and step their ATP production up or down according to the demand. Structural studies have illuminated how AMPK achieves the task of detecting small changes in AMP and ADP, despite the presence of much higher concentrations of ATP. Recently, it has been shown that AMPK can also sense the availability of glucose, the primary carbon source for most eukaryotic cells, via a mechanism independent of changes in AMP or ADP. Once activated by energy imbalance or glucose lack, AMPK modifies many target proteins by transferring phosphate groups to them from ATP. By this means, numerous ATP-producing processes are switched on (including the production of new mitochondria) and ATP-consuming processes are switched off, thus restoring energy homeostasis. Drugs that modulate AMPK have great potential in the treatment of metabolic disorders such as obesity and Type 2 diabetes, and even cancer. Indeed, some existing drugs such as metformin and aspirin, which were derived from traditional herbal remedies, appear to work, in part, by activating AMPK.

Indexed as

Diabetes Mellitus, Type 2Energy MetabolismMitochondriaNeoplasmsObesityAMP-Activated Protein KinasesAnimalsCell LineHomeostasisHumansNeoplasm ProteinsPhosphorylationAMP-Activated Protein KinasesNeoplasm Proteinsadenosine triphosphateAMP-activated protein kinasecell signallingenergy homeostasismitochondria

Identifiers

PMID29343628
PMCPMC5805978
OpenAlexW2783896167

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.