Evidence map›Paper›PMID 25418096›Full record

ArticleBiophysical journal2014

A highly tilted membrane configuration for the prefusion state of synaptobrevin.

Andrew E Blanchard, Mark J Arcario, Klaus Schulten, Emad Tajkhorshid

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2014. 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
2.7field-weighted citation impact, top 11% 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

25 citing papers in PubMed, 38 citations in OpenAlex.

  1. Review
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  3. CaThe journal of physical chemistry. B · 2025
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  7. Review
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  10. Computer simulations of protein-membrane systems.Progress in molecular biology and translational science · 2020
    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

4 authors at 1 institution in 1 country.

Andrew E BlanchardCenter for Biophysics and Computational Biology, Department of Physics, Department of Biochemistry, College of Medicine and Beckman Institute for Advanced Science and Technology, University of Illinois at Urbana-Champaign, Urbana, Illinois.
Mark J ArcarioCenter for Biophysics and Computational Biology, Department of Physics, Department of Biochemistry, College of Medicine and Beckman Institute for Advanced Science and Technology, University of Illinois at Urbana-Champaign, Urbana, Illinois.
Klaus SchultenCenter for Biophysics and Computational Biology, Department of Physics, Department of Biochemistry, College of Medicine and Beckman Institute for Advanced Science and Technology, University of Illinois at Urbana-Champaign, Urbana, Illinois.
Emad TajkhorshidCenter for Biophysics and Computational Biology, Department of Physics, Department of Biochemistry, College of Medicine and Beckman Institute for Advanced Science and Technology, University of Illinois at Urbana-Champaign, Urbana, Illinois. Electronic address: emad@life.illinois.edu.
University of Illinois Urbana-Champaign · US

Funding

Synthetic Antigen Binder CoreU54GM087519 · NIGMS · UNIVERSITY OF CHICAGO · PI ZHOU, MING · 2010 to 2017
$31.9M
WHOLE CELL SIMULATIONP41GM104601 · NIGMS · UNIVERSITY OF ILLINOIS AT URBANA-CHAMPAIGN · PI TAJKHORSHID, EMAD · 2012 to 2021
$19.0M
System-Level Simulation of a Bioenergetic MembraneR01GM067887 · NIGMS · UNIVERSITY OF ILLINOIS URBANA-CHAMPAIGN · PI TAJKHORSHID, EMAD · 2003 to 2018
$4.0M
Molecular Mechanisms of Active Transport Across Cellular MembranesR01GM086749 · NIGMS · UNIVERSITY OF ILLINOIS AT URBANA-CHAMPAIGN · PI TAJKHORSHID, EMAD · 2009 to 2013
$1.5M
Understanding the role of phospholipids in integrin signalingR01GM101048 · NIGMS · UNIVERSITY OF ILLINOIS AT URBANA-CHAMPAIGN · PI SLIGAR, STEPHEN G. · 2012 to 2015
$1.1M
NIGMS NIH HHS P41 GM104601NIGMS NIH HHS P41-GM104601NIGMS NIH HHS R01 GM067887NIGMS NIH HHS R01 GM086749NIGMS NIH HHS R01-GM086749NIGMS NIH HHS R01 GM101048NIGMS NIH HHS R01-GM101048NIGMS NIH HHS U54 GM087519NIGMS NIH HHS U54-GM087519
6 · The paper itself

Abstract

The SNARE complex plays a vital role in vesicle fusion arising during neuronal exocytosis. Key components in the regulation of SNARE complex formation, and ultimately fusion, are the transmembrane and linker regions of the vesicle-associated protein, synaptobrevin. However, the membrane-embedded structure of synaptobrevin in its prefusion state, which determines its interaction with other SNARE proteins during fusion, is largely unknown. This study reports all-atom molecular-dynamics simulations of the prefusion configuration of synaptobrevin in a lipid bilayer, aimed at characterizing the insertion depth and the orientation of the protein in the membrane, as well as the nature of the amino acids involved in determining these properties. By characterizing the structural properties of both wild-type and mutant synaptobrevin, the effects of C-terminal additions on tilt and insertion depth of membrane-embedded synaptobrevin are determined. The simulations suggest a robust, highly tilted state for membrane-embedded synaptobrevin with a helical connection between the transmembrane and linker regions, leading to an apparently new characterization of structural elements in prefusion synaptobrevin and providing a framework for interpreting past mutation experiments.

Indexed as

Amino Acid SequenceLipid BilayersMolecular Dynamics SimulationMutationPhosphatidylcholinesR-SNARE Proteins1-palmitoyl-2-oleoylphosphatidylcholineLipid BilayersPhosphatidylcholinesR-SNARE Proteins

Identifiers

PMID25418096
PMCPMC4223215
OpenAlexW1968194031

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.