Evidence map›Paper›PMID 25099013›Full record

ReviewMolecular endocrinology (Baltimore, Md.)2014

Minireview: hey U(PS): metabolic and proteolytic homeostasis linked via AMPK and the ubiquitin proteasome system.

Sarah M Ronnebaum, Cam Patterson, Jonathan C Schisler

Open access · bronzeAbstract readReview
In one paragraph

Review in Molecular endocrinology (Baltimore, Md.), 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

20 citing papers in PubMed, 39 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Probiotics and muscle health: the impact ofFrontiers in microbiology · 2025
    Review
  5. Review
  6. Article
  7. Article
  8. Bioactive compounds from Artemisia dracunculus L. activate AMPK signaling in skeletal muscle.Biomedicine & pharmacotherapy = Biomedecine & pharmacotherapie · 2021
    Article
  9. Review
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Proteotoxicity and cardiac dysfunction.Circulation research · 2015
    Review
  20. Proteasome Inhibition After Burn Injury.Journal of burn care & research : official publication of the American Burn Association
    Article
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

3 authors at 2 institutions in 1 country.

Sarah M RonnebaumMcAllister Heart Institute (S.M.R., J.C.S.) and Department of Pharmacology (J.C.S.), The University of North Carolina at Chapel Hill, Chapel Hill, North Carolina 27599; and Presbyterian Hospital/Weill-Cornell Medical Center (C.P.), New York, New York 10065.
Cam Patterson
Jonathan C Schisler
University of North Carolina at Chapel Hill · USCornell University · US

Funding

TOXICOLOGYT32ES007126 · NIEHS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI ILONA JASPERS, Bernard E. Weissman · 1985 to 2026
$13.0M
Myocyte Signaling and the Response to StressR37HL065619 · NHLBI · UNIV OF NORTH CAROLINA CHAPEL HILL · PI PATTERSON, WINSTON C · 2010 to 2019
$3.7M
CHIP: A link between the chaperone &proteasome systemsR01GM061728 · NIGMS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI SCHISLER, JONATHAN C. · 2001 to 2013
$3.4M
NHLBI NIH HHS R37 HL065619NIEHS NIH HHS T32 ES007126NIGMS NIH HHS R01 GM061728NIGMS NIH HHS R01-GM061728
6 · The paper itself

Abstract

One of the master regulators of both glucose and lipid cellular metabolism is 5'-AMP-activated protein kinase (AMPK). As a metabolic pivot that dynamically responds to shifts in nutrient availability and stress, AMPK dysregulation is implicated in the underlying molecular pathology of a variety of diseases, including cardiovascular diseases, diabetes, cancer, neurological diseases, and aging. Although the regulation of AMPK enzymatic activity by upstream kinases is an active area of research, less is known about regulation of AMPK protein stability and activity by components of the ubiquitin-proteasome system (UPS), the cellular machinery responsible for both the recognition and degradation of proteins. Furthermore, there is growing evidence that AMPK regulates overall proteasome activity and individual components of the UPS. This review serves to identify the current understanding of the interplay between AMPK and the UPS and to promote further exploration of the relationship between these regulators of energy use and amino acid availability within the cell.

Indexed as

AMP-Activated Protein KinasesAnimalsEnergy MetabolismHomeostasisHumansProteasome Endopeptidase ComplexProteolysisUbiquitinUbiquitinationAMP-Activated Protein KinasesProteasome Endopeptidase ComplexUbiquitin

Identifiers

PMID25099013
PMCPMC4179629
OpenAlexW2003442116

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.