Evidence map›Paper›PMID 26946244›Full record

ReviewBiochimica et biophysica acta2016

Lipid interaction sites on channels, transporters and receptors: Recent insights from molecular dynamics simulations.

George Hedger, Mark S P Sansom

Open access · greenAbstract readReview
In one paragraph

Review in Biochimica et biophysica acta, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 84 papers.

0numbers the graph read from it
0cells of the map it votes in
84citing papers in PubMed
14.3field-weighted citation impact, top 1% 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

84 citing papers in PubMed, 179 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Review
  5. The Role of Cholesterol in M2 Clustering and Viral Budding Explained.Journal of chemical theory and computation · 2025
    Article
  6. Review
  7. Article
  8. International journal of molecular sciences · 2024
    Article
  9. Article
  10. Article
  11. Flavonoids as Modulators of Potassium Channels.International journal of molecular sciences · 2023
    Review
  12. Review
  13. Specific Lipid Studies in Complex Membranes by Solid-State NMR Spectroscopy.Chemistry (Weinheim an der Bergstrasse, Germany) · 2022
    Article
  14. Article
  15. Review
  16. Article
  17. Review
  18. Article
  19. Article
  20. Article

24 more citing papers are in PubMed but not listed here.

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

2 authors at 1 institution in 1 country.

George HedgerDepartment 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. Electronic address: mark.sansom@bioch.ox.ac.uk.
University of Oxford · GB

Funding

Wellcome Trust
6 · The paper itself

Abstract

Lipid molecules are able to selectively interact with specific sites on integral membrane proteins, and modulate their structure and function. Identification and characterization of these sites are of importance for our understanding of the molecular basis of membrane protein function and stability, and may facilitate the design of lipid-like drug molecules. Molecular dynamics simulations provide a powerful tool for the identification of these sites, complementing advances in membrane protein structural biology and biophysics. We describe recent notable biomolecular simulation studies which have identified lipid interaction sites on a range of different membrane proteins. The sites identified in these simulation studies agree well with those identified by complementary experimental techniques. This demonstrates the power of the molecular dynamics approach in the prediction and characterization of lipid interaction sites on integral membrane proteins. This article is part of a Special Issue entitled: Biosimulations edited by Ilpo Vattulainen and Tomasz Róg.

Indexed as

Lipid BilayersMembrane ProteinsMembrane Transport ProteinsMolecular Dynamics SimulationLipid BilayersMembrane ProteinsMembrane Transport ProteinsCardiolipinCholesterolLipid binding siteLipid–protein interactionMD simulationPIP(2)

Identifiers

PMID26946244
PMCPMC5589069
OpenAlexW2289069072

What OpenQuestion holds

Textmetadata
LicenceTDM
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.