Evidence map›Paper›PMID 23163284›Full record

ArticleBiochemistry2012

Curvature forces in membrane lipid-protein interactions.

Michael F Brown

Open access · greenAbstract read
In one paragraph

Article in Biochemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 91 papers.

0numbers the graph read from it
0cells of the map it votes in
91citing papers in PubMed
4.2field-weighted citation impact, top 5% 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

91 citing papers in PubMed, 194 citations in OpenAlex.

  1. Design of Lipopeptides and dsRNA-Lipopeptide Complexes for Sprayable RNAi-Based Plant Protection.Journal of peptide science : an official publication of the European Peptide Society · 2026
    Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. The Interplay of Lipids and Peptides in Membrane Merger.Advances in experimental medicine and biology · 2026
    Review
  9. Review
  10. Homeostatic regulation of intrinsic lipid curvature in eukaryotic cells.bioRxiv : the preprint server for biology · 2025
    Article
  11. Review
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Article
  20. Review

31 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

1 author at 1 institution in 1 country.

Michael F BrownDepartment of Chemistry and Biochemistry and Department of Physics, University of Arizona, Tucson, AZ 85721, USA. mfbrown@u.arizona.edu
University of Arizona · US

Funding

MEMBRANE BASIS OF VISUAL EXCITATIONR01EY012049 · NEI · UNIVERSITY OF ARIZONA · PI BROWN, MICHAEL F · 1998 to 2012
$3.3M
LIPID MODULATION OF RHODOPSIN SIGNALING IN MEMBRANESR01EY018891 · NEI · UNIVERSITY OF ARIZONA · PI BROWN, MICHAEL F · 2008 to 2010
$1.1M
NEI NIH HHS EY12049NEI NIH HHS EY18891NEI NIH HHS R01 EY012049NEI NIH HHS R01 EY018891
6 · The paper itself

Abstract

Membrane biochemists are becoming increasingly aware of the role of lipid-protein interactions in diverse cellular functions. This review describes how conformational changes in membrane proteins, involving folding, stability, and membrane shape transitions, potentially involve elastic remodeling of the lipid bilayer. Evidence suggests that membrane lipids affect proteins through interactions of a relatively long-range nature, extending beyond a single annulus of next-neighbor boundary lipids. It is assumed the distance scale of the forces is large compared to the molecular range of action. Application of the theory of elasticity to flexible soft surfaces derives from classical physics and explains the polymorphism of both detergents and membrane phospholipids. A flexible surface model (FSM) describes the balance of curvature and hydrophobic forces in lipid-protein interactions. Chemically nonspecific properties of the lipid bilayer modulate the conformational energetics of membrane proteins. The new biomembrane model challenges the standard model (the fluid mosaic model) found in biochemistry texts. The idea of a curvature force field based on data first introduced for rhodopsin gives a bridge between theory and experiment. Influences of bilayer thickness, nonlamellar-forming lipids, detergents, and osmotic stress are all explained by the FSM. An increased awareness of curvature forces suggests that research will accelerate as structural biology becomes more closely entwined with the physical chemistry of lipids in explaining membrane structure and function.

Indexed as

Membrane LipidsMembrane ProteinsModels, MolecularProtein BindingSurface PropertiesMembrane LipidsMembrane Proteins

Identifiers

PMID23163284
PMCPMC5176250
OpenAlexW2334503806

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.