Evidence map›Paper›PMID 23442862›Full record

ArticleBiophysical journal2013

Understanding the role of amphipathic helices in N-BAR domain driven membrane remodeling.

Haosheng Cui, Carsten Mim, Francisco X Vázquez, Edward Lyman, Vinzenz M Unger, Gregory A Voth

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.

0numbers the graph read from it
0cells of the map it votes in
48citing papers in PubMed
6.4field-weighted citation impact, top 3% 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

48 citing papers in PubMed, 86 citations in OpenAlex.

  1. The bacterial ESCRT-III PspA rods thin lipid tubules and increase membrane curvature through helix α0 interactions.Proceedings of the National Academy of Sciences of the United States of America · 2025
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  10. Mechanisms of negative membrane curvature sensing and generation by ESCRT III subunit Snf7.Protein science : a publication of the Protein Society · 2020
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  14. Multiconfigurational Coarse-Grained Molecular Dynamics.Journal of chemical theory and computation · 2019
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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

6 authors at 4 institutions in 1 country.

Haosheng CuiDepartment of Chemistry, Institute for Biophysical Dynamics, James Franck Institute, and Computation Institute, University of Chicago, Chicago, Illinois, USA.
Carsten Mim
Francisco X Vázquez
Edward Lyman
Vinzenz M Unger
Gregory A Voth
Chicago Institute for Psychoanalysis · USNorthwestern University · USUniversity of Chicago · USUniversity of Delaware · US

Funding

TRD #3: An automated and streamlined pipeline for in-situ molecular microscopyP41GM103310 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI DE MARCO, ALEX, KIEFT, JEFFREY S · 2012 to 2021
$14.7M
WORKSHOPS AND TRAININGP41RR017573 · NCRR · SCRIPPS RESEARCH INSTITUTE, THE · PI CARRAGHER, BRIDGET OLIVIA · 2002 to 2011
$14.2M
New Method for Biomembrane SimulationsR01GM063796 · NIGMS · UNIVERSITY OF UTAH · PI VOTH, GREGORY A. · 2001 to 2025
$6.3M
Structural Biology of Membrane ScaffoldsR01GM094479 · NIGMS · NORTHWESTERN UNIVERSITY · PI UNGER, VINZENZ · 2010 to 2013
$1.6M
Structural Biology of Presynaptic ScaffoldsR21DA024101 · NIDA · YALE UNIVERSITY · PI UNGER, VINZENZ · 2008 to 2009
$331k
NCRR NIH HHS P41 RR017573NCRR NIH HHS RR017573NIDA NIH HHS DA24101NIDA NIH HHS R21 DA024101NIGMS NIH HHS GM063796NIGMS NIH HHS GM094479NIGMS NIH HHS P41 GM103310NIGMS NIH HHS R01 GM063796NIGMS NIH HHS R01 GM094479
6 · The paper itself

Abstract

Endophilin N-BAR (N-terminal helix and Bin/amphiphysin/Rvs) domain tubulates and vesiculates lipid membranes in vitro via its crescent-shaped dimer and four amphipathic helices that penetrate into membranes as wedges. Like F-BAR domains, endophilin N-BAR also forms a scaffold on membrane tubes. Unlike F-BARs, endophilin N-BARs have N-terminal H0 amphipathic helices that are proposed to interact with other N-BARs in oligomer lattices. Recent cryo-electron microscopy reconstructions shed light on the organization of the N-BAR lattice coats on a nanometer scale. However, because of the resolution of the reconstructions, the precise positioning of the amphipathic helices is still ambiguous. In this work, we applied a coarse-grained model to study various membrane remodeling scenarios induced by endophilin N-BARs. We found that H0 helices of N-BARs prefer to align in an antiparallel manner at two ends of the protein to form a stable lattice. The deletion of H0 helices causes disruption of the lattice. In addition, we analyzed the persistence lengths of the protein-coated tubes and found that the stiffness of endophilin N-BAR-coated tubules qualitatively agrees with previous experimental work studying N-BAR-coated tubules. Large-scale simulations on membrane liposomes revealed a systematic relation between H0 helix density and local membrane curvature fluctuations. The data also suggest that the H0 helix is required for BARs to form organized structures on the liposome, further illustrating its important function.

Indexed as

AcyltransferasesAnimalsCell MembraneLiposomesMolecular Dynamics SimulationNerve Tissue ProteinsProtein StabilityProtein Structure, SecondaryProtein Structure, TertiaryRats2-acylglycerophosphate acyltransferaseAcyltransferasesamphiphysinLiposomesNerve Tissue Proteins

Identifiers

PMID23442862
PMCPMC3552260
OpenAlexW2036579313

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.