Evidence map›Paper›PMID 15883844›Full record

ArticleEuropean biophysics journal : EBJ2005

Role of lipid protrusions in the function of interfacial enzymes.

Avi Halperin, Ole G Mouritsen

Abstract read
PubMed Publisher
In one paragraph

Article in European biophysics journal : EBJ, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
1.3field-weighted citation impact, top 22% 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

10 citing papers in PubMed, 29 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Lipids, curvature, and nano-medicine.European journal of lipid science and technology : EJLST · 2011
    Article
  7. Article
  8. Article
  9. Article
  10. H-ras protein in a bilayer: interaction and structure perturbation.Journal of the American Chemical Society · 2007
    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

2 authors at 1 institution in 1 country.

Avi HalperinUMR 5819, DRFMC/SI3M, CEA-CENG, 17 Rue des Martyrs, 38054 Grenoble Cedex 9, France.
Ole G Mouritsen
University of Southern Denmark · DK

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Secretory phospholipase A(2) (sPLA(2)) is a class of interfacially active enzymes that selectively hydrolyze lipid molecules organized at interfaces like membranes. We present a simple theoretical model that relates the sPLA(2) action to the protrusions of the lipid molecules. The model explains (1) the observed enhancement of enzymatic activity by lipids with flexible, neutral, water-soluble polymers linked to their head groups and (2) the lag-burst kinetics of sPLA(2). It yields qualitative predictions of the effect of the initial composition of the membrane, the molecular weight of the polymer, and the composition of the hydrolysis products.

Indexed as

Models, BiologicalModels, ChemicalCell Surface ExtensionsComputer SimulationGroup II Phospholipases A2Lipid BilayersMembrane FluidityMembrane LipidsMembrane ProteinsPhospholipases AGroup II Phospholipases A2Lipid BilayersMembrane LipidsMembrane ProteinsPhospholipases A

Identifiers

PMID15883844
OpenAlexW2033716575

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.