Evidence map›Paper›PMID 27465729›Full record

ArticleThe Journal of membrane biology2017

The Integrin Receptor in Biologically Relevant Bilayers: Insights from Molecular Dynamics Simulations.

Antreas C Kalli, Tomasz Rog, Ilpo Vattulainen, Iain D Campbell, Mark S P Sansom

Open access · hybridAbstract read
In one paragraph

Article in The Journal of membrane biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
2.4field-weighted citation impact, top 12% 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

23 citing papers in PubMed, 32 citations in OpenAlex.

  1. Article
  2. Environmental Toxicants and Their Disruption of Integrin Signaling in Lipid Rafts.BioEssays : news and reviews in molecular, cellular and developmental biology · 2025
    Review
  3. Contributions of the individual domains of αCytoskeleton (Hoboken, N.J.) · 2024
    Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Significance of Receptor Mobility in Multivalent Binding on Lipid Membranes.Angewandte Chemie (International ed. in English) · 2022
    Review
  9. Article
  10. Modulation of αExperimental & molecular medicine · 2021
    Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Multiscale model of integrin adhesion assembly.PLoS computational biology · 2019
    Article
  16. Article
  17. Review
  18. Review
  19. Review
  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

5 authors at 3 institutions in 3 countries.

Antreas C KalliDepartment of Biochemistry, University of Oxford, South Parks Road, Oxford, OX1 3QU, UK.
Tomasz RogDepartment of Physics, Tampere University of Technology, P.O. Box 692, 33101, Tampere, Finland.
Ilpo VattulainenDepartment of Physics, Tampere University of Technology, P.O. Box 692, 33101, Tampere, Finland.
Iain D CampbellDepartment of Biochemistry, University of Oxford, South Parks Road, Oxford, OX1 3QU, UK.
Mark S P SansomDepartment of Biochemistry, University of Oxford, South Parks Road, Oxford, OX1 3QU, UK. mark.sansom@bioch.ox.ac.uk.
University of Oxford · GBTampere University · FIUniversity of Southern Denmark · DK

Funding

European Research Council 290974Wellcome Trust 092970
6 · The paper itself

Abstract

Integrins are heterodimeric (αβ) cell surface receptors that are potential therapeutic targets for a number of diseases. Despite the existence of structural data for all parts of integrins, the structure of the complete integrin receptor is still not available. We have used available structural data to construct a model of the complete integrin receptor in complex with talin F2-F3 domain. It has been shown that the interactions of integrins with their lipid environment are crucial for their function but details of the integrin/lipid interactions remain elusive. In this study an integrin/talin complex was inserted in biologically relevant bilayers that resemble the cell plasma membrane containing zwitterionic and charged phospholipids, cholesterol and sphingolipids to study the dynamics of the integrin receptor and its effect on bilayer structure and dynamics. The results of this study demonstrate the dynamic nature of the integrin receptor and suggest that the presence of the integrin receptor alters the lipid organization between the two leaflets of the bilayer. In particular, our results suggest elevated density of cholesterol and of phosphatidylserine lipids around the integrin/talin complex and a slowing down of lipids in an annulus of ~30 Å around the protein due to interactions between the lipids and the integrin/talin F2-F3 complex. This may in part regulate the interactions of integrins with other related proteins or integrin clustering thus facilitating signal transduction across cell membranes.

Indexed as

Molecular Dynamics SimulationAmino Acid MotifsBinding SitesCholesterolHumansIntegrin alphaVbeta3Lipid BilayersPhosphatidylcholinesPhosphatidylethanolaminesPhosphatidylserinesPlatelet Glycoprotein GPIIb-IIIa ComplexProtein BindingProtein Conformation, alpha-HelicalProtein Conformation, beta-StrandProtein Interaction Domains and MotifsProtein Multimerization1-palmitoyl-2-oleoylglycero-3-phosphoserine1-palmitoyl-2-oleoylphosphatidylcholine1-palmitoyl-2-oleoylphosphatidylethanolamineCholesterolIntegrin alphaVbeta3Lipid BilayersPhosphatidylcholinesPhosphatidylethanolaminesPhosphatidylserinesPlatelet Glycoprotein GPIIb-IIIa ComplexProtein SubunitsTalinIntegrinLipid diffusionMolecular dynamics simulationsTalin

Identifiers

PMID27465729
PMCPMC5579164
OpenAlexW2502874105

What OpenQuestion holds

Textmetadata
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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.