Evidence map›Paper›PMID 17273938›Full record

ArticleAnnals of biomedical engineering2007

A multiscale computational approach to dissect early events in the Erb family receptor mediated activation, differential signaling, and relevance to oncogenic transformations.

Yingting Liu, Jeremy Purvis, Andrew Shih, Joshua Weinstein, Neeraj Agrawal, Ravi Radhakrishnan

Open access · bronzeAbstract read
In one paragraph

Article in Annals of biomedical engineering, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
4.1field-weighted citation impact, top 6% 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

19 citing papers in PubMed, 43 citations in OpenAlex.

  1. Article
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  3. Cancer informatics · 2022
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  6. Journal of biosciences · 2018
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  7. Discovery of novel dual inhibitors of receptor tyrosine kinases EGFR and IGF-1R.Journal of enzyme inhibition and medicinal chemistry · 2017
    Article
  8. Article
  9. Article
  10. Structural systems biology and multiscale signaling models.Annals of biomedical engineering · 2012
    Review
  11. Multiscale cancer modeling.Annual review of biomedical engineering · 2011
    Review
  12. Article
  13. Cancer Cell: Linking Oncogenic Signaling to Molecular Structure.Chapman & Hall/CRC mathematical & computational biology series · 2011
    Article
  14. Article
  15. Article
  16. Multi-scale, multi-resolution brain cancer modeling.Mathematics and computers in simulation · 2009
    Article
  17. Article
  18. Article
  19. 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

6 authors at 2 institutions in 1 country.

Yingting LiuDepartment of Bioengineering, University of Pennsylvania, Philadelphia, PA 19104, USA.
Jeremy Purvis
Andrew Shih
Joshua Weinstein
Neeraj Agrawal
Ravi Radhakrishnan
University of Pennsylvania · USStanford University · US

Funding

YEAST ER MOLECULAR CHAPERONE TRANSLOCATION: GENOME DATABANK HOMOLOGSP41RR006009 · NCRR · MELLON PITTS CORPORATION (MPC CORP) · PI KNOLL, ERIC · 1990 to 2011
$22.0M
NCRR NIH HHS P41 RR006009
6 · The paper itself

Abstract

We describe a hierarchical multiscale computational approach based on molecular dynamics simulations, free energy-based molecular docking simulations, deterministic network-based kinetic modeling, and hybrid discrete/continuum stochastic dynamics protocols to study the dimer-mediated receptor activation characteristics of the Erb family receptors, specifically the epidermal growth factor receptor (EGFR). Through these modeling approaches, we are able to extend the prior modeling of EGF-mediated signal transduction by considering specific EGFR tyrosine kinase (EGFRTK) docking interactions mediated by differential binding and phosphorylation of different C-terminal peptide tyrosines on the RTK tail. By modeling signal flows through branching pathways of the EGFRTK resolved on a molecular basis, we are able to transcribe the effects of molecular alterations in the receptor (e.g., mutant forms of the receptor) to differing kinetic behavior and downstream signaling response. Our molecular dynamics simulations show that the drug sensitizing mutation (L834R) of EGFR stabilizes the active conformation to make the system constitutively active. Docking simulations show preferential characteristics (for wildtype vs. mutant receptors) in inhibitor binding as well as preferential enhancement of phosphorylation of particular substrate tyrosines over others. We find that in comparison to the wildtype system, the L834R mutant RTK preferentially binds the inhibitor erlotinib, as well as preferentially phosphorylates the substrate tyrosine Y1068 but not Y1173. We predict that these molecular level changes result in preferential activation of the Akt signaling pathway in comparison to the Erk signaling pathway for cells with normal EGFR expression. For cells with EGFR over expression, the mutant over activates both Erk and Akt pathways, in comparison to wildtype. These results are consistent with qualitative experimental measurements reported in the literature. We discuss these consequences in light of how the network topology and signaling characteristics of altered (mutant) cell lines are shaped differently in relationship to native cell lines.

Indexed as

Gene Expression Regulation, NeoplasticModels, BiologicalSignal TransductionAnimalsCell Transformation, NeoplasticComputer SimulationEpidermal Growth FactorErbB ReceptorsHumansProtein Interaction MappingEpidermal Growth FactorErbB Receptors

Identifiers

PMID17273938
PMCPMC3021414
OpenAlexW2099383058

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.