Evidence map›Paper›PMID 25998378›Full record

ReviewThe Journal of membrane biology2015

Efficient Exploration of Membrane-Associated Phenomena at Atomic Resolution.

Josh V Vermaas, Javier L Baylon, Mark J Arcario, Melanie P Muller, Zhe Wu, Taras V Pogorelov, Emad Tajkhorshid

Open access · greenAbstract readReview
In one paragraph

Review in The Journal of membrane biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
2.4field-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

28 citing papers in PubMed, 42 citations in OpenAlex.

  1. Article
  2. Article
  3. CaThe journal of physical chemistry. B · 2025
    Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. CHARMM-GUIJournal of chemical theory and computation · 2023
    Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. A network of phosphatidylinositol 4,5-bisphosphate binding sites regulates gating of the CaProceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  15. Review
  16. Article
  17. Article
  18. Lipid specificity of the membrane binding domain of coagulation factor X.Journal of thrombosis and haemostasis : JTH · 2017
    Article
  19. Article
  20. Review
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

7 authors at 1 institution in 1 country.

Josh V VermaasDepartment of Biochemistry, and Center for Biophysics and Computational Biology, Beckman Institute, University of Illinois at Urbana-Champaign, 405 N. Mathews Ave., Urbana, IL, 61801, USA.
Javier L Baylon
Mark J Arcario
Melanie P Muller
Zhe Wu
Taras V Pogorelov
Emad Tajkhorshid
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
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 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

Biological membranes constitute a critical component in all living cells. In addition to providing a conducive environment to a wide range of cellular processes, including transport and signaling, mounting evidence has established active participation of specific lipids in modulating membrane protein function through various mechanisms. Understanding lipid-protein interactions underlying these mechanisms at a sufficiently high resolution has proven extremely challenging, partly due to the semi-fluid nature of the membrane. In order to address this challenge computationally, multiple methods have been developed, including an alternative membrane representation termed highly mobile membrane mimetic (HMMM) in which lateral lipid diffusion has been significantly enhanced without compromising atomic details. The model allows for efficient sampling of lipid-protein interactions at atomic resolution, thereby significantly enhancing the effectiveness of molecular dynamics simulations in capturing membrane-associated phenomena. In this review, after providing an overview of HMMM model development, we will describe briefly successful application of the model to study a variety of membrane processes, including lipid-dependent binding and insertion of peripheral proteins, the mechanism of phospholipid insertion into lipid bilayers, and characterization of optimal tilt angle of transmembrane helices. We conclude with practical recommendations for proper usage of the model in simulation studies of membrane processes.

Indexed as

Molecular Dynamics SimulationAnimalsCell MembraneCell Membrane PermeabilityHumansHydrophobic and Hydrophilic InteractionsLipid BilayersMembrane LipidsMembrane ProteinsSolventsLipid BilayersMembrane LipidsMembrane ProteinsSolvents

Identifiers

PMID25998378
PMCPMC4490090
OpenAlexW259266290

What OpenQuestion holds

Textmetadata
LicenceTDM
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.