Evidence map›Paper›PMID 19940001›Full record

ReviewJournal of the Royal Society, Interface2010

Lipid bilayer regulation of membrane protein function: gramicidin channels as molecular force probes.

Jens A Lundbaek, Shemille A Collingwood, Helgi I Ingólfsson, Ruchi Kapoor, Olaf S Andersen

Open access · bronzeAbstract readReview
In one paragraph

Review in Journal of the Royal Society, Interface, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 167 papers.

0numbers the graph read from it
0cells of the map it votes in
167citing papers in PubMed
7.1field-weighted citation impact, top 2% 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

167 citing papers in PubMed, 330 citations in OpenAlex.

  1. Article
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  10. Electromechanically induced membrane restructuring enables learning and memory.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  11. Review
  12. Review
  13. Article
  14. Capturing the native structure of membrane proteins using vesicles.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  15. Review
  16. Review
  17. Review
  18. Article
  19. Review
  20. Capsaicin: beyond TRPV1.Frontiers in nutrition · 2025
    Review

107 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

5 authors at 1 institution in 2 countries.

Jens A LundbaekDepartment of Physiology and Biophysics, Weill Cornell Medical College, New York, NY 10065, USA. lundbaek@dadlnet.dk
Shemille A Collingwood
Helgi I Ingólfsson
Ruchi Kapoor
Olaf S Andersen
Cornell University · US

Funding

Weill Cornell/Rockefeller/Sloan-Kettering MST ProgramT32GM007739 · NIGMS · WEILL MEDICAL COLL OF CORNELL UNIV · PI HSU, KATHARINE C · 1985 to 2023
$51.1M
Energetics of Channel-Bilayer InteractionsR01GM021342 · NIGMS · WEILL MEDICAL COLL OF CORNELL UNIV · PI ANDERSEN, OLAF S. · 1985 to 2021
$9.9M
NIGMS NIH HHS GM21342NIGMS NIH HHS R01 GM021342NIGMS NIH HHS T32 GM007739
6 · The paper itself

Abstract

Membrane protein function is regulated by the host lipid bilayer composition. This regulation may depend on specific chemical interactions between proteins and individual molecules in the bilayer, as well as on non-specific interactions between proteins and the bilayer behaving as a physical entity with collective physical properties (e.g. thickness, intrinsic monolayer curvature or elastic moduli). Studies in physico-chemical model systems have demonstrated that changes in bilayer physical properties can regulate membrane protein function by altering the energetic cost of the bilayer deformation associated with a protein conformational change. This type of regulation is well characterized, and its mechanistic elucidation is an interdisciplinary field bordering on physics, chemistry and biology. Changes in lipid composition that alter bilayer physical properties (including cholesterol, polyunsaturated fatty acids, other lipid metabolites and amphiphiles) regulate a wide range of membrane proteins in a seemingly non-specific manner. The commonality of the changes in protein function suggests an underlying physical mechanism, and recent studies show that at least some of the changes are caused by altered bilayer physical properties. This advance is because of the introduction of new tools for studying lipid bilayer regulation of protein function. The present review provides an introduction to the regulation of membrane protein function by the bilayer physical properties. We further describe the use of gramicidin channels as molecular force probes for studying this mechanism, with a unique ability to discriminate between consequences of changes in monolayer curvature and bilayer elastic moduli.

Indexed as

GramicidinHydrophobic and Hydrophilic InteractionsKineticsLipid BilayersMembrane FluidityMembrane ProteinsMembrane Transport ProteinsModels, BiologicalMolecular ProbesGramicidinLipid BilayersMembrane ProteinsMembrane Transport ProteinsMolecular Probes

Identifiers

PMID19940001
PMCPMC2842803
OpenAlexW2115896474

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.