Evidence map›Paper›PMID 22067146›Full record

ArticleBiophysical journal2011

Quantitative modeling of membrane deformations by multihelical membrane proteins: application to G-protein coupled receptors.

Sayan Mondal, George Khelashvili, Jufang Shan, Olaf S Andersen, Harel Weinstein

Abstract 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 53 papers.

0numbers the graph read from it
0cells of the map it votes in
53citing papers in PubMed
–field-weighted citation impact
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

53 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Membrane-Mediated Interactions Between Protein Inclusions.Frontiers in molecular biosciences · 2021
    Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Antidepressants are modifiers of lipid bilayer properties.The Journal of general physiology · 2019
    Article
  18. Article
  19. 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

5 authors.

Sayan MondalDepartment of Physiology and Biophysics, Weill Medical College of Cornell University, New York, New York, USA.
George Khelashvili
Jufang Shan
Olaf S Andersen
Harel Weinstein

Funding

Synthetic Antigen Binder CoreU54GM087519 · NIGMS · UNIVERSITY OF CHICAGO · PI NAKAMOTO, ROBERT K. · 2010 to 2017
$31.9M
STRUCTURE/FUNCTION OF THE HUMAN DOPAMINE TRANSPORTERP01DA012408 · NIDA · WEILL MEDICAL COLL OF CORNELL UNIV · PI WEINSTEIN, HAREL · 1999 to 2015
$14.2M
Energetics of Channel-Bilayer InteractionsR01GM021342 · NIGMS · WEILL MEDICAL COLL OF CORNELL UNIV · PI ANDERSEN, OLAF S. · 1985 to 2021
$9.9M
HALLUCINOGENS IN SPECIFIC SIGNALING AND CIRCUITRYP01DA012923 · NIDA · WEILL MEDICAL COLL OF CORNELL UNIV · PI WEINSTEIN, HAREL · 2000 to 2011
$8.6M
NIDA NIH HHS DA012408NIDA NIH HHS DA012923NIDA NIH HHS P01 DA012408NIDA NIH HHS P01 DA012923NIGMS NIH HHS R01 GM021342NIGMS NIH HHS U54 GM087519
6 · The paper itself

Abstract

The interpretation of experimental observations of the dependence of membrane protein function on the properties of the lipid membrane environment calls for a consideration of the energy cost of protein-bilayer interactions, including the protein-bilayer hydrophobic mismatch. We present a novel (to our knowledge) multiscale computational approach for quantifying the hydrophobic mismatch-driven remodeling of membrane bilayers by multihelical membrane proteins. The method accounts for both the membrane remodeling energy and the energy contribution from any partial (incomplete) alleviation of the hydrophobic mismatch by membrane remodeling. Overcoming previous limitations, it allows for radially asymmetric bilayer deformations produced by multihelical proteins, and takes into account the irregular membrane-protein boundaries. The approach is illustrated by application to two G-protein coupled receptors: rhodopsin in bilayers of different thickness, and the serotonin 5-HT(2A) receptor bound to pharmacologically different ligands. Analysis of the results identifies the residual exposure that is not alleviated by bilayer adaptation, and its quantification at specific transmembrane segments is shown to predict favorable contact interfaces in oligomeric arrays. In addition, our results suggest how distinct ligand-induced conformations of G-protein coupled receptors may elicit different functional responses through differential effects on the membrane environment.

Indexed as

Models, MolecularHydrophobic and Hydrophilic InteractionsLigandsLipid BilayersMolecular Dynamics SimulationProtein Structure, SecondaryReceptor, Serotonin, 5-HT2ARhodopsinThermodynamicsLigandsLipid BilayersReceptor, Serotonin, 5-HT2ARhodopsin

Identifiers

PMID22067146
PMCPMC3207176

What OpenQuestion holds

Textmetadata
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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.