Evidence map›Paper›PMID 21494142›Full record

ReviewCurrent opinion in lipidology2011

Recent insights into the structure and function of comparative gene identification-58.

Monika Oberer, Andras Boeszoermenyi, Harald M Nagy, Rudolf Zechner

Abstract readReview
In one paragraph

Review in Current opinion in lipidology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
2.9field-weighted citation impact, top 10% 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

25 citing papers in PubMed, 39 citations in OpenAlex.

  1. Article
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  5. Article
  6. Phospholipids: Identification and Implication in Muscle Pathophysiology.International journal of molecular sciences · 2021
    Review
  7. Article
  8. Review
  9. Article
  10. CGI-58: Versatile Regulator of Intracellular Lipid Droplet Homeostasis.Advances in experimental medicine and biology · 2020
    Review
  11. Review
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Review
  20. 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

4 authors at 1 institution in 1 country.

Monika ObererInstitute of Molecular Biosciences, University of Graz, Graz, Austria. m.oberer@uni-graz.at
Andras Boeszoermenyi
Harald M Nagy
Rudolf Zechner
University of Graz · AT

Funding

Austrian Science Fund FWF F 3001Austrian Science Fund FWF F 3002Austrian Science Fund FWF F 3016Austrian Science Fund FWF P 22170Austrian Science Fund FWF W 901
6 · The paper itself

Abstract

purpose of reviewComparative gene identification-58 (CGI-58) is an important player in lipid metabolism. It acts as activator of triglyceride hydrolases and as acyl-CoA-dependent lysophosphatidic acid acyltransferase. This review aims at establishing a structure-function relationship of this still rather enigmatic protein based on recent studies characterizing different functions of CGI-58. RECENT

findingsNovel studies confirm the important regulatory role of CGI-58 as activator of the triglyceride hydrolase adipose triglyceride lipase. New evidence, corroborated by the characterization of a CGI-58 knockout mouse model, also suggests the existence of yet unknown lipases that are activated by CGI-58. Additionally, CGI-58 was identified to exert acyl-CoA-dependent lysophosphatidic acid acyltransferase activity, which implies possible roles in triglyceride or phospholipid synthesis or signaling processes. Unlike mammalian CGI-58 proteins, orthologs from plants and yeast additionally act as weak triglyceride and phospholipid hydrolases. A first three-dimensional model was calculated and allows preliminary structural considerations for the functions of CGI-58. SUMMARY: Despite important progress concerning the different biochemical functions of CGI-58, the physiological importance of these activities requires better characterization. Furthermore, three-dimensional structural data for CGI-58 are required to unveil the molecular mechanism of how CGI-58 acts as activator of lipases and exerts its enzymatic functions.

Indexed as

1-Acylglycerol-3-Phosphate O-AcyltransferaseAmino Acid SequenceAnimalsGene ExpressionHumansLipid MetabolismLipolysisLiverMolecular Sequence DataOrgan SpecificityProtein ConformationSequence AlignmentSkin1-Acylglycerol-3-Phosphate O-AcyltransferaseABHD5 protein, human

Identifiers

PMID21494142
PMCPMC5808844
OpenAlexW2017466835

What OpenQuestion holds

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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.