Evidence map›Paper›PMID 17720730›Full record

ArticleBiophysical journal2007

Effects of hydrophobic surfactant proteins on collapse of pulmonary surfactant monolayers.

Florence Lhert, Wenfei Yan, Samares C Biswas, Stephen B Hall

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
2.4field-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

12 citing papers in PubMed, 29 citations in OpenAlex.

  1. Article
  2. The Equilibrium Spreading Tension of Pulmonary Surfactant.Langmuir : the ACS journal of surfaces and colloids · 2015
    Article
  3. Article
  4. Article
  5. Optical factors in the rapid analysis of captive bubbles.Langmuir : the ACS journal of surfaces and colloids · 2012
    Article
  6. Article
  7. Article
  8. Review
  9. Pulmonary surfactant: an immunological perspective.Cellular physiology and biochemistry : international journal of experimental cellular physiology, biochemistry, and pharmacology · 2010
    Review
  10. Article
  11. The biophysical function of pulmonary surfactant.Respiratory physiology & neurobiology · 2008
    Review
  12. 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

4 authors at 1 institution in 1 country.

Florence LhertDepartment of Biochemistry and Molecular Biology, Oregon Health & Science University, Portland, Oregon 97239, USA.
Wenfei Yan
Samares C Biswas
Stephen B Hall
Oregon Health & Science University · US

Funding

INTERFACIAL PHASE BEHAVIOR OF PULMONARY SURFACTANTR01HL060914 · NHLBI · OREGON HEALTH & SCIENCE UNIVERSITY · PI HALL, STEPHEN B · 1998 to 2011
$3.7M
NHLBI NIH HHS HL60914NHLBI NIH HHS R01 HL060914
6 · The paper itself

Abstract

To determine if hydrophobic surfactant proteins affect the stability of pulmonary surfactant monolayers at an air/water interface, the studies reported here compared the kinetics of collapse for the complete set of lipids in calf surfactant with and without the proteins. Monomolecular films spread at the surface of captive bubbles were compressed at 37 degrees C to surface pressures above 46 mN/m, at which collapse first occurred. The rate of area-compression required to maintain a constant surface pressure was measured to directly determine the rate of collapse. For films with and without the proteins, higher surface pressures initially produced faster collapse, but the rates then reached a maximum and decreased to values <0.04 min(-1) above 53 mN/m. The maximum rate for the lipids with the proteins (1.22 +/- 0.28 min(-1)) was almost twice the value for the lipids alone (0.71 +/- 0.15 min(-1)). Because small increments in surface pressure produced large shifts in the rate close to the fastest collapse, compressions at a series of constant speeds also established the threshold rate required to achieve high surface pressure as an indirect indication of the fastest collapse. Both samples produced a sharply defined threshold that occurred at slightly faster compression with the proteins present, supporting the conclusion of the direct measurements that the proteins produce a faster maximum rate of collapse. Our results indicate that at 47-53 mN/m, the hydrophobic surfactant proteins destabilize the compressed monolayers and tend to limit access to the higher surface pressures at which the lipid films become metastable.

Indexed as

Membranes, ArtificialHydrophobic and Hydrophilic InteractionsMolecular ConformationPhase TransitionPhospholipidsPulmonary Surfactant-Associated ProteinsPulmonary SurfactantsSurface PropertiesMembranes, ArtificialPhospholipidsPulmonary Surfactant-Associated ProteinsPulmonary Surfactants

Identifiers

PMID17720730
PMCPMC2098737
OpenAlexW2018165343

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.