Evidence map›Paper›PMID 18487292›Full record

ArticleBiophysical journal2008

Molecular simulations of lipid-mediated protein-protein interactions.

Frédérick Jean-Marie de Meyer, Maddalena Venturoli, Berend Smit

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.

0numbers the graph read from it
0cells of the map it votes in
47citing papers in PubMed
6.3field-weighted citation impact, top 3% 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

47 citing papers in PubMed, 174 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Membrane-Mediated Interactions Between Protein Inclusions.Frontiers in molecular biosciences · 2021
    Review
  6. Review
  7. Article
  8. A Multi-Scale Approach to Membrane Remodeling Processes.Frontiers in molecular biosciences · 2019
    Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Organization and Dynamics of Receptor Proteins in a Plasma Membrane.Journal of the American Chemical Society · 2015
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Small scale membrane mechanics.Biomechanics and modeling in mechanobiology · 2014
    Article
  19. Water-mediated ion-ion interactions are enhanced at the water vapor-liquid interface.Proceedings of the National Academy of Sciences of the United States of America · 2014
    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 3 countries.

Frédérick Jean-Marie de MeyerCentre Européen de Calcul Atomique et Moléculaire, Ecole Normale Supérieure, Lyon, France. frederick.demeyer@yahoo.com
Maddalena Venturoli
Berend Smit
École Normale Supérieure de Lyon · FRUniversity of Amsterdam · NL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Recent experimental results revealed that lipid-mediated interactions due to hydrophobic forces may be important in determining the protein topology after insertion in the membrane, in regulating the protein activity, in protein aggregation and in signal transduction. To gain insight into the lipid-mediated interactions between two intrinsic membrane proteins, we developed a mesoscopic model of a lipid bilayer with embedded proteins, which we studied with dissipative particle dynamics. Our calculations of the potential of mean force between transmembrane proteins show that hydrophobic forces drive long-range protein-protein interactions and that the nature of these interactions depends on the length of the protein hydrophobic segment, on the three-dimensional structure of the protein and on the properties of the lipid bilayer. To understand the nature of the computed potentials of mean force, the concept of hydrophilic shielding is introduced. The observed protein interactions are interpreted as resulting from the dynamic reorganization of the system to maintain an optimal hydrophilic shielding of the protein and lipid hydrophobic parts, within the constraint of the flexibility of the components. Our results could lead to a better understanding of several membrane processes in which protein interactions are involved.

Indexed as

Models, BiologicalModels, ChemicalCell MembraneComputer SimulationLipid BilayersMembrane ProteinsProtein BindingProtein Interaction MappingLipid BilayersMembrane Proteins

Identifiers

PMID18487292
PMCPMC2483748
OpenAlexW2169210766

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.