Evidence map›Paper›PMID 26853937›Full record

ReviewBiochimica et biophysica acta2016

Continuum descriptions of membranes and their interaction with proteins: Towards chemically accurate models.

David Argudo, Neville P Bethel, Frank V Marcoline, Michael Grabe

Abstract readReview
In one paragraph

Review in Biochimica et biophysica acta, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing 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

25 citing papers in PubMed.

  1. Article
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  5. A small-molecule carrier for the intracellular delivery of a membrane-impermeable protein with retained bioactivity.Proceedings of the National Academy of Sciences of the United States of America · 2024
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  8. Review
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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

4 authors.

David ArgudoCardiovascular Research Institute, Department of Pharmaceutical Chemistry, University of California San Francisco, San Francisco, CA 94158, United States.
Neville P BethelCardiovascular Research Institute, Department of Pharmaceutical Chemistry, University of California San Francisco, San Francisco, CA 94158, United States.
Frank V MarcolineCardiovascular Research Institute, Department of Pharmaceutical Chemistry, University of California San Francisco, San Francisco, CA 94158, United States.
Michael GrabeCardiovascular Research Institute, Department of Pharmaceutical Chemistry, University of California San Francisco, San Francisco, CA 94158, United States. Electronic address: michael.grabe@ucsf.edu.

Funding

STRUCTURAL BIOLOGY TRAINING PROGRAMT32GM008284 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI KORTEMME, TANJA · 1988 to 2022
$10.1M
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 GM117593NIGMS NIH HHS R01-GM117593NIGMS NIH HHS T32 GM008284
6 · The paper itself

Abstract

Biological membranes deform in response to resident proteins leading to a coupling between membrane shape and protein localization. Additionally, the membrane influences the function of membrane proteins. Here we review contributions to this field from continuum elastic membrane models focusing on the class of models that couple the protein to the membrane. While 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 accurate representations of the protein. We outline our recent advances along these lines with our hybrid continuum-atomistic model, and we show the model is in excellent agreement with fully-atomistic simulations of the nhTMEM16 lipid scramblase. We believe that the speed and accuracy of continuum-atomistic methodologies will make it possible to simulate large scale, slow biological processes, such as membrane morphological changes, that are currently beyond the scope of other computational approaches. This article is part of a Special Issue entitled: Membrane Proteins edited by J.C. Gumbart and Sergei Noskov.

Indexed as

Molecular Dynamics SimulationBinding SitesCell MembraneComputer SimulationLipid BilayersMembrane ProteinsModels, ChemicalProtein BindingProtein ConformationProtein Interaction MappingQuantum TheoryLipid BilayersMembrane ProteinsBilayerBiological membraneElectrostaticsHydrophobic mismatchTransmembrane protein

Identifiers

PMID26853937
PMCPMC4877259

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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.