Evidence map›Paper›PMID 25258314›Full record

ArticleThe Journal of biological chemistry2014

A peptide derived from G0/G1 switch gene 2 acts as noncompetitive inhibitor of adipose triglyceride lipase.

Ines K Cerk, Barbara Salzburger, Andras Boeszoermenyi, Christoph Heier, Christoph Pillip, Matthias Romauch, Martina Schweiger, Irina Cornaciu, Achim Lass, Robert Zimmermann and 2 more

Open access · hybridAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed, 1 pooled it
2.7field-weighted citation impact, top 11% 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

30 citing papers in PubMed, 1 synthesis or guideline pooled it, 44 citations in OpenAlex.

  1. Guideline
  2. Article
  3. Review
  4. Review
  5. Recent advances on the role of G0S2.Discover oncology · 2025
    Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Review
  14. Review
  15. Article
  16. Review
  17. Article
  18. Review
  19. Review
  20. Identification of an intrinsic lysophosphatidic acid acyltransferase activity in the lipolytic inhibitor GFASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2019
    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

12 authors at 1 institution in 1 country.

Ines K CerkFrom the Institute of Molecular Biosciences, University of Graz, 8010 Graz, Austria.
Barbara SalzburgerFrom the Institute of Molecular Biosciences, University of Graz, 8010 Graz, Austria.
Andras BoeszoermenyiFrom the Institute of Molecular Biosciences, University of Graz, 8010 Graz, Austria.
Christoph HeierFrom the Institute of Molecular Biosciences, University of Graz, 8010 Graz, Austria.
Christoph PillipFrom the Institute of Molecular Biosciences, University of Graz, 8010 Graz, Austria.
Matthias RomauchFrom the Institute of Molecular Biosciences, University of Graz, 8010 Graz, Austria.
Martina SchweigerFrom the Institute of Molecular Biosciences, University of Graz, 8010 Graz, Austria.
Irina CornaciuFrom the Institute of Molecular Biosciences, University of Graz, 8010 Graz, Austria.
Achim LassFrom the Institute of Molecular Biosciences, University of Graz, 8010 Graz, Austria.
Robert ZimmermannFrom the Institute of Molecular Biosciences, University of Graz, 8010 Graz, Austria.
Rudolf ZechnerFrom the Institute of Molecular Biosciences, University of Graz, 8010 Graz, Austria.
Monika ObererFrom the Institute of Molecular Biosciences, University of Graz, 8010 Graz, Austria m.oberer@uni-graz.at.
University of Graz · AT

Funding

Austrian Science Fund FWF P 25193
6 · The paper itself

Abstract

The protein G0/G1 switch gene 2 (G0S2) is a small basic protein that functions as an endogenous inhibitor of adipose triglyceride lipase (ATGL), a key enzyme in intracellular lipolysis. In this study, we identified a short sequence covering residues Lys-20 to Ala-52 in G0S2 that is still fully capable of inhibiting mouse and human ATGL. We found that a synthetic peptide corresponding to this region inhibits ATGL in a noncompetitive manner in the nanomolar range. This peptide is highly selective for ATGL and does not inhibit other lipases, including hormone-sensitive lipase, monoacylglycerol lipase, lipoprotein lipase, and patatin domain-containing phospholipases 6 and 7. Because increased lipolysis is linked to the development of metabolic disorders, the inhibition of ATGL by G0S2-derived peptides may represent a novel therapeutic tool to modulate lipolysis.

Indexed as

1-Acylglycerol-3-Phosphate O-AcyltransferaseAcyltransferasesAmino Acid SequenceAnimalsCell Cycle ProteinsChlorocebus aethiopsCOS CellsDose-Response Relationship, DrugHumansLipaseMice, KnockoutMolecular Sequence DataPeptidesRecombinant Proteins1-Acylglycerol-3-Phosphate O-AcyltransferaseAbhd5 protein, mouseAcyltransferasesCell Cycle ProteinsG0S2 protein, humanLipasePeptidesPNPLA2 protein, humanPNPLA2 protein, mouseRecombinant ProteinsAdipose Triglyceride Lipase (ATGL)AtglistatinEnzyme InhibitorG0/G1 Switch Gene 2 (G0S2)hGW2052LipidLipid MetabolismLipolysisNoncompetitive InhibitionPeptides

Identifiers

PMID25258314
PMCPMC4239610
OpenAlexW1994146146

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.