Evidence map›Paper›PMID 23923044›Full record

ArticlePloS one2013

Aggregation of lipid-anchored full-length H-Ras in lipid bilayers: simulations with the MARTINI force field.

Hualin Li, Alemayehu A Gorfe

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2013. 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
2.5field-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

26 citing papers in PubMed, 47 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. RAS GTPases and Interleaflet Coupling in the Plasma Membrane.Cold Spring Harbor perspectives in biology · 2023
    Review
  5. Article
  6. Review
  7. Review
  8. Review
  9. Article
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  11. Article
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  14. Article
  15. Article
  16. Article
  17. Article
  18. Geodesic curvature driven surface microdomain formation.Journal of computational physics · 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

2 authors.

Hualin LiDepartment of Integrative Biology and Pharmacology, University of Texas Medical School at Houston, Houston, Texas, USA.
Alemayehu A Gorfe

Funding

Nanoclusters of Lipid-anchored Proteins in Membranes: How and where they appearR01GM100078 · NIGMS · UNIVERSITY OF TEXAS HLTH SCI CTR HOUSTON · PI GORFE, ALEMAYEHU A. · 2012 to 2016
$1.4M
NIGMS NIH HHS 1R0101GM100078NIGMS NIH HHS R01 GM100078
6 · The paper itself

Abstract

Lipid-anchored Ras oncoproteins assemble into transient, nano-sized substructures on the plasma membrane. These substructures, called nanoclusters, were proposed to be crucial for high-fidelity signal transmission in cells. However, the molecular basis of Ras nanoclustering is poorly understood. In this work, we used coarse-grained (CG) molecular dynamics simulations to investigate the molecular mechanism by which full-length H-ras proteins form nanoclusters in a model membrane. We chose two different conformations of H-ras that were proposed to represent the active and inactive state of the protein, and a domain-forming model bilayer made up of di16:0-PC (DPPC), di18:2-PC (DLiPC) and cholesterol. We found that, irrespective of the initial conformation, Ras molecules assembled into a single large aggregate. However, the two binding modes, which are characterized by the different orientation of the G-domain with respect to the membrane, differ in dynamics and organization during and after aggregation. Some of these differences involve regions of Ras that are important for effector/modulator binding, which may partly explain observed differences in the ability of active and inactive H-ras nanoclusters to recruit effectors. The simulations also revealed some limitations in the CG force field to study protein assembly in solution, which we discuss in the context of proposed potential avenues of improvement.

Indexed as

Molecular Dynamics SimulationHumansLipid BilayersProtein ConformationProtein Interaction Mapsras ProteinsLipid Bilayersras Proteins

Identifiers

PMID23923044
PMCPMC3724741
OpenAlexW1970958467

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.