Evidence map›Paper›PMID 26682805›Full record

ArticleBiophysical journal2015

Reversible Effects of Peptide Concentration and Lipid Composition on H-Ras Lipid Anchor Clustering.

Xubo Lin, Zhenlong Li, Alemayehu A Gorfe

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
1.7field-weighted citation impact, top 16% 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

12 citing papers in PubMed, 25 citations in OpenAlex.

  1. Review
  2. Molecular Dynamics Simulation of Lipid-Modified Signaling Proteins.Methods in molecular biology (Clifton, N.J.) · 2021
    Article
  3. Review
  4. Article
  5. Review
  6. Article
  7. Ras and the Plasma Membrane: A Complicated Relationship.Cold Spring Harbor perspectives in medicine · 2018
    Review
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
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

3 authors at 2 institutions in 1 country.

Xubo LinDepartment of Integrative Biology and Pharmacology, Medical School, The University of Texas Health Science Center at Houston, Houston, Texas.
Zhenlong LiDepartment of Integrative Biology and Pharmacology, Medical School, The University of Texas Health Science Center at Houston, Houston, Texas.
Alemayehu A GorfeDepartment of Integrative Biology and Pharmacology, Medical School, The University of Texas Health Science Center at Houston, Houston, Texas. Electronic address: alemayehu.g.abebe@uth.tmc.edu.
The University of Texas Health Science Center at Houston · USTexas Medical Center · US

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 R01 GM100078
6 · The paper itself

Abstract

Dynamic clusters of lipid-anchored Ras proteins are important for high-fidelity signal transduction in cells. The average size of Ras nanoclusters was reported to be independent of protein expression levels, and cholesterol depletion is commonly used to test the raft-preference of nanoclusters. However, whether protein concentration and membrane domain stability affect Ras clustering in a reversible manner is not well understood. We used coarse-grained molecular dynamics simulations to examine the reversibility of the effects of peptide and cholesterol concentrations as well as a lipid domain-perturbing nanoparticle (C60) on the dynamics and stability of H-Ras lipid-anchor nanoclusters. By comparing results from these simulations with previous observations from the literature, we show that effects of peptide/cholesterol concentrations on the dynamics and stability of H-Ras peptide nanoclusters are reversible. Our results also suggest a correlation between the stabilities of lipid domains and Ras nanoclusters, which is supported by our finding that C60 penetrates into the liquid-disordered domain of the bilayer, destabilizing lipid domains and thereby the stability of the nanoclusters.

Indexed as

Dose-Response Relationship, DrugLipidsMolecular Dynamics SimulationNanoparticlesPeptidesProtein BindingProtein ConformationProtein Stabilityras ProteinsLipidsPeptidesras Proteins

Identifiers

PMID26682805
PMCPMC4699922
OpenAlexW2208733198

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.