Evidence map›Paper›PMID 21553808›Full record

ArticleBiochemistry2011

Lipoprotein-associated phospholipase A(2) interacts with phospholipid vesicles via a surface-disposed hydrophobic α-helix.

Jian Cao, Yuan-Hao Hsu, Sheng Li, Virgil L Woods, Edward A Dennis

Open access · greenAbstract read
In one paragraph

Article in Biochemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.3field-weighted citation impact, top 20% 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

19 citing papers in PubMed, 39 citations in OpenAlex.

  1. Review
  2. Review
  3. Review
  4. Article
  5. Review
  6. Lipoprotein-associated phospholipase AProceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  7. Review
  8. Article
  9. Review
  10. Review
  11. Review of four major distinct types of human phospholipase AAdvances in biological regulation · 2018
    Review
  12. Review
  13. Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. 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

5 authors at 1 institution in 1 country.

Jian CaoDepartment of Chemistry and Biochemistry and Pharmacology, University of California, La Jolla, CA 92093-0601, USA.
Yuan-Hao Hsu
Sheng Li
Virgil L Woods
Edward A Dennis
University of California, San Diego · US

Funding

ACTION OF LIPOLYTIC ENZYMESR01GM020501 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI DENNIS, EDWARD A · 1985 to 2020
$7.3M
Current Generation Integrated Instrumentation for H-D Exchange LC-MSS10RR029388 · NCRR · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI WOODS, VIRGIL L · 2010 to 2010
$1.0M
Sensitive Deuterium Exchange MS for Membrane ProteinsR01GM093325 · NIGMS · BECKMAN RESEARCH INSTITUTE/CITY OF HOPE · PI HANDEL, TRACY M, LEE, TERRY D. · 2010 to 2012
$965k
NCRR NIH HHS S10 RR029388NCRR NIH HHS S10-RR029388NIGMS NIH HHS R01 GM020501NIGMS NIH HHS R01 GM093325NIGMS NIH HHS R01-GM093325NIGMS NIH HHS R01-GM20501
6 · The paper itself

Abstract

Lipoprotein-associated phospholipase A(2) (Lp-PLA(2)) plays important roles in both the inhibition and promotion of inflammation in human disease. It catalyzes the hydrolytic inactivation of plasma platelet activating factor (PAF) and is also known as PAF acetylhydrolase. High levels of PAF are implicated in a variety of inflammatory diseases such as asthma, necrotizing enterocolitis, and sepsis. Lp-PLA(2) also associates with lipoproteins in human plasma where it hydrolyzes oxidized phospholipids to produce pro-inflammatory lipid mediators that can promote inflammation and the development of atherosclerosis. Lp-PLA(2) plasma levels have recently been identified as a biomarker of vascular inflammation, atherosclerotic vulnerability, and future cardiovascular events. The enzyme is thus a prominent target for the development of inflammation and atherosclerosis-modulating therapeutics. While the crystallographically determined structure of the enzyme is known, the enzyme's mechanism of interaction with PAF and the function-modulating lipids in lipoproteins is unknown. We have employed peptide amide hydrogen-deuterium exchange mass spectrometry (DXMS) to characterize the association of Lp-PLA(2) with dimyristoylphosphatidylcholine (DMPC) vesicles and found that specific residues 113-120 in one of the enzyme's surface-disposed hydrophobic α-helices likely mediate liposome binding.

Indexed as

1-Alkyl-2-acetylglycerophosphocholine EsteraseCatalysisDeuterium Exchange MeasurementHumansHydrophobic and Hydrophilic InteractionsModels, MolecularPhospholipidsProtein Structure, SecondarySurface Properties1-Alkyl-2-acetylglycerophosphocholine EsterasePhospholipids

Identifiers

PMID21553808
PMCPMC3110720
OpenAlexW2320750442

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.