Evidence map›Paper›PMID 28538153›Full record

ArticleBiophysical journal2017

New Continuum Approaches for Determining Protein-Induced Membrane Deformations.

David Argudo, Neville P Bethel, Frank V Marcoline, Charles W Wolgemuth, Michael Grabe

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
2.2field-weighted citation impact, top 12% 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

26 citing papers in PubMed, 41 citations in OpenAlex.

  1. Review
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  9. Value of models for membrane budding.Current opinion in cell biology · 2021
    Review
  10. Membrane-Mediated Interactions Between Protein Inclusions.Frontiers in molecular biosciences · 2021
    Review
  11. Article
  12. Article
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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 2 institutions in 1 country.

David ArgudoCardiovascular Research Institute, Department of Pharmaceutical Chemistry, University of California San Francisco, San Francisco, California.
Neville P BethelCardiovascular Research Institute, Department of Pharmaceutical Chemistry, University of California San Francisco, San Francisco, California.
Frank V MarcolineCardiovascular Research Institute, Department of Pharmaceutical Chemistry, University of California San Francisco, San Francisco, California.
Charles W WolgemuthDepartments of Molecular and Cellular Biology and Physics, University of Arizona, Tucson, Arizona.
Michael GrabeCardiovascular Research Institute, Department of Pharmaceutical Chemistry, University of California San Francisco, San Francisco, California. Electronic address: michael.grabe@ucsf.edu.
University of California, San Francisco · USUniversity of Arizona · US

Funding

Integrative Program in Complex Biological System (ipCBS)T32EB009383 · NIBIB · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI MARSHALL, WALLACE, WEINER, ORION D · 2009 to 2022
$3.2M
A Multiscale Model of Protein Mediated Changes in membrane MorphologyR01GM117593 · NIGMS · COLORADO STATE UNIVERSITY · PI ZHOU, YONGCHENG · 2015 to 2019
$1.8M
NIBIB NIH HHS T32 EB009383NIGMS NIH HHS R01 GM117593
6 · The paper itself

Abstract

The influence of the membrane on transmembrane proteins is central to a number of biological phenomena, notably the gating of stretch activated ion channels. Conversely, membrane proteins can influence the bilayer, leading to the stabilization of particular membrane shapes, topological changes that occur during vesicle fission and fusion, and shape-dependent protein aggregation. Continuum elastic models of the membrane have been widely used to study protein-membrane interactions. These mathematical approaches produce physically interpretable membrane shapes, energy estimates for the cost of deformation, and a snapshot of the equilibrium configuration. Moreover, elastic models are much less computationally demanding than fully atomistic and coarse-grained simulation methodologies; however, it has been argued that continuum models cannot reproduce the distortions observed in fully atomistic molecular dynamics simulations. We suggest that this failure can be overcome by using chemically and geometrically accurate representations of the protein. Here, we present a fast and reliable hybrid continuum-atomistic model that couples the protein to the membrane. We show that the model is in excellent agreement with fully atomistic simulations of the ion channel gramicidin embedded in a POPC membrane. Our continuum calculations not only reproduce the membrane distortions produced by the channel but also accurately determine the channel's orientation. Finally, we use our method to investigate the role of membrane bending around the charged voltage sensors of the transient receptor potential cation channel TRPV1. We find that membrane deformation significantly stabilizes the energy of insertion of TRPV1 by exposing charged residues on the S4 segment to solution.

Indexed as

Models, BiologicalCell MembraneComputer SimulationElasticityGramicidinHydrophobic and Hydrophilic InteractionsLipid BilayersMembrane ProteinsMolecular Dynamics SimulationPhosphatidylcholinesSurface TensionTRPV Cation Channels1-palmitoyl-2-oleoylphosphatidylcholineGramicidinLipid BilayersMembrane ProteinsPhosphatidylcholinesTRPV Cation Channels

Identifiers

PMID28538153
PMCPMC5448241
OpenAlexW2620004662

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.