Evidence map›Paper›PMID 21806937›Full record

ArticleBiophysical journal2011

Aggregation of model membrane proteins, modulated by hydrophobic mismatch, membrane curvature, and protein class.

Daniel L Parton, Jochen W Klingelhoefer, Mark S P Sansom

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
6.0field-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

44 citing papers in PubMed, 125 citations in OpenAlex.

  1. Hydrophobic mismatch induces lipid sorting based on tail unsaturation.bioRxiv : the preprint server for biology · 2026
    Article
  2. Article
  3. Review
  4. Molecular Dynamics Simulations in Protein-Protein Docking.Methods in molecular biology (Clifton, N.J.) · 2024
    Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Viral Induced Protein Aggregation: A Mechanism of Immune Evasion.International journal of molecular sciences · 2021
    Review
  10. Local Bilayer Hydrophobicity Modulates Membrane Protein Stability.Journal of the American Chemical Society · 2021
    Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Biophysics of membrane curvature remodeling at molecular and mesoscopic lengthscales.Journal of physics. Condensed matter : an Institute of Physics journal · 2018
    Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. CURVATURE-DRIVEN MOLECULAR FLOW ON MEMBRANE SURFACE.SIAM journal on applied mathematics · 2017
    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 1 institution in 1 country.

Daniel L PartonDepartment of Biochemistry, University of Oxford, Oxford, United Kingdom.
Jochen W Klingelhoefer
Mark S P Sansom
University of Oxford · GB

Funding

Biotechnology and Biological Sciences Research CouncilWellcome Trust
6 · The paper itself

Abstract

Aggregation of transmembrane proteins is important for many biological processes, such as protein sorting and cell signaling, and also for in vitro processes such as two-dimensional crystallization. We have used large-scale simulations to study the lateral organization and dynamics of lipid bilayers containing multiple inserted proteins. Using coarse-grained molecular dynamics simulations, we have studied model membranes comprising ∼7000 lipids and 16 identical copies of model cylindrical proteins of either α-helical or β-barrel types. Through variation of the lipid tail length and hence the degree of hydrophobic mismatch, our simulations display levels of protein aggregation ranging from negligible to extensive. The nature and extent of aggregation are shown to be influenced by membrane curvature and the shape or orientation of the protein. Interestingly, a model β-barrel protein aggregates to form one-dimensional strings within the bilayer plane, whereas a model α-helical bundle forms two-dimensional clusters. Overall, it is clear that the nature and extent of membrane protein aggregation is dependent on several aspects of the proteins and lipids, including hydrophobic mismatch, protein class and shape, and membrane curvature.

Indexed as

Hydrophobic and Hydrophilic InteractionsMolecular Dynamics SimulationProtein MultimerizationAmino Acid SequenceCell MembraneDiffusionLipid BilayersMembrane ProteinsMolecular Sequence DataPorosityProtein Structure, SecondaryUnilamellar LiposomesLipid BilayersMembrane ProteinsUnilamellar Liposomes

Identifiers

PMID21806937
PMCPMC3145270
OpenAlexW2013652494

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.