Evidence map›Paper›PMID 24187138›Full record

ArticleThe Journal of biological chemistry2013

Chemoproteomic analysis of intertissue and interspecies isoform diversity of AMP-activated protein kinase (AMPK).

Jiang Wu, Dinesh Puppala, Xidong Feng, Mara Monetti, Amanda Lee Lapworth, Kieran F Geoghegan

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
3.0field-weighted citation impact, top 9% 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

32 citing papers in PubMed, 64 citations in OpenAlex.

  1. Review
  2. Review
  3. Review
  4. SIRT1 in Liver Diseases: Mechanistic Insights and Therapeutic Prospects.International journal of biological sciences · 2025
    Review
  5. Review
  6. Review
  7. Review
  8. Review
  9. Review
  10. Article
  11. Article
  12. Article
  13. Review
  14. Review
  15. Article
  16. Review
  17. Activation of AMPK under Hypoxia: Many Roads Leading to Rome.International journal of molecular sciences · 2020
    Review
  18. AMPK promotes induction of the tumor suppressor FLCN through activation of TFEB independently of mTOR.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2019
    Article
  19. Review
  20. AMP-Activated Protein Kinase and Host Defense against Infection.International journal of molecular sciences · 2018
    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.

Jiang WuFrom Pfizer Worldwide Research, Groton, Connecticut 06340 and.
Dinesh Puppala
Xidong Feng
Mara Monetti
Amanda Lee Lapworth
Kieran F Geoghegan
Pfizer (United States) · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

AMP-activated protein kinase (AMPK) is a heterotrimeric enzyme that senses and governs changes in the cellular energy balance represented by concentrations of AMP, ADP, and ATP. Each of its three chains (α, β, and γ) exists as either two or three subtypes, theoretically allowing up to 12 different forms of the complete enzyme. Tissue specificity in the distribution of AMPK subtypes is believed to underpin a range of biological functions for AMPK, a central regulator of metabolic function and response. It is of particular interest for drug discovery purposes to compare AMPK isoforms that are most prevalent in human liver and muscle with isoforms present in key preclinical species. To complement immunocapture/immunodetection methods, which for AMPK are challenged by sequence similarities and difficulties of obtaining accurate relative quantitation, AMPK was captured from lysates of a range of cells and tissues using the ActivX ATP probe. This chemical probe covalently attaches desthiobiotin to one or more conserved lysyl residues in the ATP-binding sites of protein kinases, including AMPK, while also labeling a wide range of ATP-utilizing proteins. Affinity-based recovery of labeled proteins followed by gel-based fractionation of the captured sample was followed by proteomic characterization of AMPK polypeptides. In agreement with transcript-based analysis and previous indications from immunodetection, the results indicated that the predominant AMPK heterotrimer in human liver is α1β2γ1 but that dog and rat livers mainly contain the α1β1γ1 and α2β1γ1 forms, respectively. Differences were not detected between the AMPK profiles of normal and diabetic human liver tissues.

Indexed as

ProteomicsAmino Acid SequenceAMP-Activated Protein KinasesAnimalsCell LineDogsHEK293 CellsHepatocytesHumansIsoenzymesModels, MolecularMolecular Sequence DataMuscle, SkeletalMyocardiumOrgan SpecificityProtein Structure, QuaternaryAMP-Activated Protein KinasesIsoenzymesRNA, MessengerAMP-activated Kinase (AMPK)Chemical BiologyChemical ModificationDrug DiscoveryMass Spectrometry (MS)

Identifiers

PMID24187138
PMCPMC3861640
OpenAlexW2019478137

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.