Evidence map›Paper›PMID 19191415›Full record

ArticleThe Journal of chemical physics2009

Stability of protein-decorated mixed lipid membranes: The interplay of lipid-lipid, lipid-protein, and protein-protein interactions.

Stephan Loew, Anne Hinderliter, Sylvio May

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of chemical physics, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
0.8field-weighted citation impact, top 29% 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

7 citing papers in PubMed, 24 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Dynamics and instabilities of lipid bilayer membrane shapes.Advances in colloid and interface science · 2014
    Review
  5. Article
  6. Multi-scale modeling in biology: how to bridge the gaps between scales?Progress in biophysics and molecular biology · 2011
    Review
  7. Adsorption of proteins on a lipid bilayer.European biophysics journal : EBJ · 2010
    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.

Stephan LoewDepartment of Physics, North Dakota State University, Fargo, North Dakota 58105-5566, USA.
Anne Hinderliter
Sylvio May
North Dakota State University · USUniversity of Minnesota, Duluth · US

Funding

Trans-monolayer coupling of membrane domainsR15GM077184 · NIGMS · NORTH DAKOTA STATE UNIVERSITY · PI MAY, SYLVIO E · 2006 to 2006
$214k
NIGMS NIH HHS GM077184NIGMS NIH HHS R15 GM077184
6 · The paper itself

Abstract

Membrane-associated proteins are likely to contribute to the regulation of the phase behavior of mixed lipid membranes. To gain insight into the underlying mechanism, we study a thermodynamic model for the stability of a protein-decorated binary lipid layer. Here, proteins interact preferentially with one lipid species and thus locally sequester that species. We aim to specify conditions that lead to an additional macroscopic phase separation of the protein-decorated lipid membrane. Our model is based on a standard mean-field lattice-gas description for both the lipid mixture and the adsorbed protein layer. Besides accounting for the lipid-protein binding strength, we also include attractive lipid-lipid and protein-protein interactions. Our analysis characterizes the decrease in the membrane's critical interaction parameter as a function of the lipid-protein binding strength. For small and large binding strengths we provide analytical expressions; numerical results cover the intermediate range. Our results reiterate the crucial importance of the line tension associated with protein-induced compositional gradients and the presence of attractive lipid-lipid interactions within the membrane. Direct protein-protein attraction effectively increases the line tension and thus tends to further destabilize the membrane.

Indexed as

Biophysical PhenomenaComputational BiologyEnzyme StabilityLipidsMembrane FluidityMembrane ProteinsMembranesProteinsStructure-Activity RelationshipThermodynamicsLipidsMembrane ProteinsProteins

Identifiers

PMID19191415
PMCPMC2671212
OpenAlexW2040374398

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.