Evidence map›Paper›PMID 20224398›Full record

ReviewCurrent opinion in lipidology2010

Lipase maturation factor 1: structure and role in lipase folding and assembly.

Mark H Doolittle, Nicole Ehrhardt, Miklós Péterfy

Abstract readReview
In one paragraph

Review in Current opinion in lipidology, 2010. 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
2.7field-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

32 citing papers in PubMed, 75 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Article
  5. Hypertriglyceridemia: Molecular and Genetic Landscapes.International journal of molecular sciences · 2024
    Review
  6. Article
  7. Article
  8. A protein of capillary endothelial cells, GPIHBP1, is crucial for plasma triglyceride metabolism.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  9. Article
  10. Review
  11. Review
  12. Article
  13. Genetic and functional studies of theMolecular genetics and metabolism reports · 2020
    Article
  14. Article
  15. Genetics of Hypertriglyceridemia.Frontiers in endocrinology · 2020
    Review
  16. Review
  17. Review
  18. Structure of lipoprotein lipase in complex with GPIHBP1.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  19. Lipoprotein lipase is active as a monomer.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  20. 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.

Mark H DoolittleDepartment of Medicine, David Geffen School of Medicine, University of California at Los Angeles, Los Angeles, California, USA.
Nicole Ehrhardt
Miklós Péterfy
VA Greater Los Angeles Healthcare System · USCedars-Sinai Medical Center · US

Funding

Systems genomics of metabolic syndrome traitsP01HL028481 · NHLBI · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI REUE, KAREN · 1985 to 2019
$50.2M
NHLBI NIH HHS HL-24841NHLBI NIH HHS P01 HL028481
6 · The paper itself

Abstract

purpose of reviewLipase maturation factor 1 (LMF1) is a membrane-bound protein located in the endoplasmic reticulum. It is essential to the folding and assembly (i.e., maturation) of a selected group of lipases that include lipoprotein lipase, hepatic lipase and endothelial lipase. The purpose of this review is to examine recent studies that have begun to elucidate the structure and function of LMF1 and to place it in the context of lipase folding and assembly. RECENT

findingsRecent studies identified mutations in LMF1 that cause combined lipase deficiency and hypertriglyceridemia in humans. These mutations result in the truncation of a large, evolutionarily conserved domain (DUF1222), which is essential for interaction with lipases and their attainment of enzymatic activity. The structural complexity of LMF1 has been further characterized by solving its topology in the endoplasmic reticulum membrane. Recent studies indicate that in addition to lipoprotein lipase and hepatic lipase, the maturation of endothelial lipase is also dependent on LMF1. Based on its apparent specificity for dimeric lipases, LMF1 is proposed to play an essential role in the assembly and/or stabilization of head-to-tail lipase homodimers. SUMMARY: LMF1 functions in the maturation of a selected group of secreted lipases that assemble into homodimers in the endoplasmic reticulum. These dimeric lipases include lipoprotein lipase, hepatic lipase and endothelial lipase, all of which contribute significantly to plasma triglyceride and high-density lipoprotein cholesterol levels in humans. Future studies involving genetically engineered mouse models will be required to fully elucidate the role of LMF1 in normal physiology and diseases.

Indexed as

Protein FoldingAnimalsDiseaseHumansLipaseMembrane ProteinsMutationProtein BindingLipaseMembrane Proteins

Identifiers

PMID20224398
PMCPMC3924775
OpenAlexW2060592444

What OpenQuestion holds

Textmetadata
LicenceTDM
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.