Evidence map›Paper›PMID 22994893›Full record

ArticleJournal of the American Chemical Society2012

Formation and domain partitioning of H-ras peptide nanoclusters: effects of peptide concentration and lipid composition.

Zhenlong Li, Lorant Janosi, Alemayehu A Gorfe

Open access · greenAbstract read
In one paragraph

Article in Journal of the American Chemical Society, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
2.7field-weighted citation impact, top 10% 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

34 citing papers in PubMed, 62 citations in OpenAlex.

  1. Review
  2. Article
  3. RAS GTPases and Interleaflet Coupling in the Plasma Membrane.Cold Spring Harbor perspectives in biology · 2023
    Review
  4. Review
  5. Review
  6. Review
  7. Unveiling the Dynamics of KRAS4b on Lipid Model Membranes.The Journal of membrane biology · 2021
    Article
  8. Review
  9. Review
  10. Molecular Dynamics Simulation of Lipid-Modified Signaling Proteins.Methods in molecular biology (Clifton, N.J.) · 2021
    Article
  11. Review
  12. Article
  13. Review
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
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  20. 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 1 institution in 1 country.

Zhenlong LiDepartment of Integrative Biology and Pharmacology, The University of Texas Health Science Center at Houston, 6431 Fannin St., Houston, Texas 77030, USA.
Lorant Janosi
Alemayehu A Gorfe
The University of Texas Health Science Center at Houston · 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 1R01GM10078NIGMS NIH HHS R01 GM100078
6 · The paper itself

Abstract

Experiments have shown that homologous Ras proteins containing different lipid modification, which is required for membrane binding, form nonoverlapping nanoclusters on the plasma membrane. However, the physical basis for clustering and lateral organization remains poorly understood. We have begun to tackle this issue using coarse-grained molecular dynamics simulations of the H-ras lipid anchor (tH), a triply lipid-modified heptapeptide embedded in a domain-forming mixed lipid bilayer [Janosi L. et al. Proc. Natl. Acad. Sci. U.S.A. 2012, 109, 8097]. Here we use the same simulation approach to investigate the effect of peptide concentration and bilayer composition on the clustering and lateral distribution of tH. We found no major difference in the clustering behavior of tH above a certain concentration. However, the simulations predict the existence of a critical concentration below which tH does not form nanoclusters. Moreover, our data demonstrate that cholesterol enhances the stability of tH nanoclusters but is not required for their formation. Finally, analyses of peptide distributions and partition free energies allowed us to quantitatively describe how clustering facilitates the accumulation of tH at the interface between ordered and disordered domains of the simulated bilayer systems. These thermodynamic insights represent some of the key elements for a comprehensive understanding of the molecular basis for the formation and stability of Ras signaling platforms.

Indexed as

LipidsModels, MolecularMolecular Dynamics SimulationNanostructuresPeptide Fragmentsras ProteinsThermodynamicsLipidsPeptide Fragmentsras Proteins

Identifiers

PMID22994893
PMCPMC3479155
OpenAlexW2030360450

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.