Evidence map›Paper›PMID 33513781›Full record

ReviewInternational journal of molecular sciences2021

Post-Translational Modifications of the Energy Guardian AMP-Activated Protein Kinase.

Ashley J Ovens, John W Scott, Christopher G Langendorf, Bruce E Kemp, Jonathan S Oakhill, William J Smiles

Open access · goldAbstract readReview
In one paragraph

Review in International journal of molecular sciences, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
1.9field-weighted citation impact, top 13% 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

28 citing papers in PubMed, 39 citations in OpenAlex.

  1. Article
  2. Article
  3. Regulation of Glutathione Peroxidase 4 in Diabetic Retinopathy.International journal of molecular sciences · 2026
    Article
  4. Review
  5. Article
  6. Article
  7. Review
  8. Review
  9. Article
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  11. Article
  12. Article
  13. Article
  14. Review
  15. Review
  16. Article
  17. Article
  18. Article
  19. Review
  20. Exercise sustains the hallmarks of health.Journal of sport and health science · 2023
    Review
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 at 1 institution in 1 country.

Ashley J OvensMetabolic Signalling Laboratory, St Vincent's Institute of Medical Research, School of Medicine, University of Melbourne, Fitzroy, VIC 3065, Australia.ORCID 0000-0001-5711-6555
John W ScottMary MacKillop Institute for Health Research, Australian Catholic University, Fitzroy, VIC 3000, Australia.ORCID 0000-0002-1896-9798
Christopher G LangendorfProtein Chemistry & Metabolism, St Vincent's Institute of Medical Research, School of Medicine, University of Melbourne, Fitzroy, VIC 3065, Australia.
Bruce E KempMary MacKillop Institute for Health Research, Australian Catholic University, Fitzroy, VIC 3000, Australia.
Jonathan S OakhillMetabolic Signalling Laboratory, St Vincent's Institute of Medical Research, School of Medicine, University of Melbourne, Fitzroy, VIC 3065, Australia.
William J SmilesMetabolic Signalling Laboratory, St Vincent's Institute of Medical Research, School of Medicine, University of Melbourne, Fitzroy, VIC 3065, Australia.ORCID 0000-0002-6846-689X
The University of Melbourne · AU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Physical exercise elicits physiological metabolic perturbations such as energetic and oxidative stress; however, a diverse range of cellular processes are stimulated in response to combat these challenges and maintain cellular energy homeostasis. AMP-activated protein kinase (AMPK) is a highly conserved enzyme that acts as a metabolic fuel sensor and is central to this adaptive response to exercise. The complexity of AMPK's role in modulating a range of cellular signalling cascades is well documented, yet aside from its well-characterised regulation by activation loop phosphorylation, AMPK is further subject to a multitude of additional regulatory stimuli. Therefore, in this review we comprehensively outline current knowledge around the post-translational modifications of AMPK, including novel phosphorylation sites, as well as underappreciated roles for ubiquitination, sumoylation, acetylation, methylation and oxidation. We provide insight into the physiological ramifications of these AMPK modifications, which not only affect its activity, but also subcellular localisation, nutrient interactions and protein stability. Lastly, we highlight the current knowledge gaps in this area of AMPK research and provide perspectives on how the field can apply greater rigour to the characterisation of novel AMPK regulatory modifications.

Indexed as

Energy MetabolismProtein Processing, Post-TranslationalAcetylationAMP-Activated Protein KinasesAnimalsHomeostasisHumansMethylationOxidation-ReductionOxidative StressPhosphorylationProtein DomainsSignal TransductionUbiquitinationAMP-Activated Protein KinasesAMPKenergy metabolismoxidationphosphorylationubiquitination

Identifiers

PMID33513781
PMCPMC7866021
OpenAlexW3121271451

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.