Evidence map›Paper›PMID 35462078›Full record

ArticleBiophysical journal2022

Millisecond molecular dynamics simulations of KRas-dimer formation and interfaces.

Van A Ngo, Angel E Garcia

Abstract read
In one paragraph

Article in Biophysical journal, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
–field-weighted citation impact
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

7 citing papers in PubMed.

  1. Review
  2. Review
  3. Article
  4. Structural modifications and kinetic effects ofFrontiers in molecular biosciences · 2024
    Article
  5. Revealing KRas4b topology on the membrane surface.Biochemical and biophysical research communications · 2023
    Article
  6. Article
  7. Biophysics of cancer.Biophysical journal · 2022
    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

2 authors.

Van A NgoAdvanced Computing for Life Sciences and Engineering Group, Science Engagement Section, National Center for Computational Sciences, Oak Ridge National Lab, Oak Ridge, Tennessee; Center for Nonlinear Studies (CNLS), Los Alamos National Laboratory, Los Alamos, New Mexico.
Angel E GarciaCenter for Nonlinear Studies (CNLS), Los Alamos National Laboratory, Los Alamos, New Mexico. Electronic address: agarcia@lanl.gov.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Ras dimers have been proposed as building blocks for initiating the extracellular signal-regulated kinase (ERK)/mitogen-activated protein kinase (MAPK) cellular signaling pathway. To better examine the structure of possible dimer interfaces, the dynamics of Ras dimerization, and its potential signaling consequences, we performed molecular dynamics simulations totaling 1 ms of sampling, using an all-atom model of two full-length, farnesylated, guanosine triphosphate (GTP)-bound, wild-type KRas4b proteins diffusing on 29%POPS (1-palmitoyl-2-oleoyl-sn-glycero-3-phospho-L-serine)-mixed POPC (1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine) membranes. Our simulations unveil an ensemble of thermodynamically weak KRas dimers spanning multiple conformations. The most stable conformations, having the largest interface areas, involve helix α

Indexed as

Lipid BilayersMolecular Dynamics SimulationArginineExtracellular Signal-Regulated MAP KinasesGTPase-Activating ProteinsGuanosine TriphosphatePhosphatesraf KinasesSerineArginineExtracellular Signal-Regulated MAP KinasesGTPase-Activating ProteinsGuanosine TriphosphateLipid BilayersPhosphatesraf KinasesSerine

Identifiers

PMID35462078
PMCPMC9617078

What OpenQuestion holds

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Registered trials

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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.