Evidence map›Paper›PMID 31872229›Full record

ReviewBiochemical Society transactions2020

The energetics of protein-lipid interactions as viewed by molecular simulations.

Robin A Corey, Phillip J Stansfeld, Mark S P Sansom

Open access · hybridAbstract readReview
In one paragraph

Review in Biochemical Society transactions, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
3.5field-weighted citation impact, top 6% 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

37 citing papers in PubMed, 72 citations in OpenAlex.

  1. Article
  2. Hysteretic Conductance in Ion Channel Gating.Entropy (Basel, Switzerland) · 2026
    Review
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Cooperative Membrane Binding of HIV-1 Matrix Proteins.The journal of physical chemistry. B · 2024
    Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Supramolecular organization and dynamics of mannosylated phosphatidylinositol lipids in the mycobacterial plasma membrane.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  18. Protein-mediated interactions in the dynamic regulation of acute inflammation.Biocell : official journal of the Sociedades Latinoamericanas de Microscopia Electronica ... et. al · 2023
    Article
  19. Dissecting peripheral protein-membrane interfaces.PLoS computational biology · 2022
    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 1 country.

Robin A CoreyDepartment of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, U.K.
Phillip J StansfeldDepartment of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, U.K.
Mark S P SansomDepartment of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, U.K.
University of Oxford · GBUniversity of Warwick · GB

Funding

Biotechnology and Biological Sciences Research Council BB/P01948X/1Biotechnology and Biological Sciences Research Council BB/R00126X/1Biotechnology and Biological Sciences Research Council BB/R002517/1Biotechnology and Biological Sciences Research Council BB/S003339/1Medical Research Council MR/S009213/1Wellcome TrustWellcome Trust 208361/Z/17/Z
6 · The paper itself

Abstract

Membranes are formed from a bilayer containing diverse lipid species with which membrane proteins interact. Integral, membrane proteins are embedded in this bilayer, where they interact with lipids from their surroundings, whilst peripheral membrane proteins bind to lipids at the surface of membranes. Lipid interactions can influence the function of membrane proteins, either directly or allosterically. Both experimental (structural) and computational approaches can reveal lipid binding sites on membrane proteins. It is, therefore, important to understand the free energies of these interactions. This affords a more complete view of the engagement of a particular protein with the biological membrane surrounding it. Here, we describe many computational approaches currently in use for this purpose, including recent advances using both free energy and unbiased simulation methods. In particular, we focus on interactions of integral membrane proteins with cholesterol, and with anionic lipids such as phosphatidylinositol 4,5-bis-phosphate and cardiolipin. Peripheral membrane proteins are exemplified via interactions of PH domains with phosphoinositide-containing membranes. We summarise the current state of the field and provide an outlook on likely future directions of investigation.

Indexed as

Molecular Dynamics SimulationThermodynamicsBinding SitesCell MembraneCholesterolEnergy TransferHumansLipid BilayersPleckstrin Homology DomainsProtein BindingReceptors, G-Protein-CoupledCholesterolLipid BilayersReceptors, G-Protein-Coupledfree energylipidmembrane proteinmolecular dynamicssimulation

Identifiers

PMID31872229
PMCPMC7054751
OpenAlexW2995816366

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.