Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Effects of oncogenic mutations on the conformational free-energy landscape of EGFR kinase.

Proceedings of the National Academy of Sciences of the United States of America - 25 Jun 2013

Sutto Ludovico, Gervasio Francesco Luigi

Abstract excerpt

Activating mutations in the epidermal growth factor receptor (EGFR) tyrosine kinase are frequently found in many cancers. It has been suggested that changes in the equilibrium between its active and inactive conformations are linked to its oncogenic potential. Here, we quantify the effects of some of the most common single (L858R and T790M) and double (T790M-L858R) oncogenic mutations on the conformational...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Molecular Dynamics Simulation
Share to Amino Acid Substitution

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Catalytic Domain

Share to Computer Simulation

Share to ErbB Receptors

Share to Oncogenes

Share to Protein Conformation

Share to Thermodynamics

Source

Open in PubMed Open full text

Identifiers

PMID: 23754386
DOI: 10.1073/pnas.1221953110
PMCID: PMC3696764

Genes

EGFR

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Effects of oncogenic mutations on the conformational free-energy landscape of EGFR kinase.PMID 23754386Read ↗

A Molecular Dynamics Protocol for Rapid Prediction of EGFR Overactivation and Its Application to the Rare Mutations S768I, S768N, D761NSemantic proximity Read ↗

Structural Stability and Flexibility Direct the Selection of Activating Mutations in Epidermal Growth Factor Receptor Kinase.Semantic proximity Read ↗

The free energy landscape in translational science: how can somatic mutations result in constitutive oncogenic activation?Semantic proximity Read ↗

Structural basis of the effect of activating mutations on the EGF receptor.Semantic proximity Read ↗

Molecular dynamics simulation reveals structural and thermodynamic features of kinase activation by cancer mutations within the epidermal growth factor receptor.Semantic proximity Read ↗

Oncogenic mutations at the EGFR ectodomain structurally converge to remove a steric hindrance on a kinase-coupled cryptic epitopeSemantic proximity Read ↗

Hierarchical modeling of activation mechanisms in the ABL and EGFR kinase domains: thermodynamic and mechanistic catalysts of kinase activation by cancer mutations.Semantic proximity Read ↗

Structural signature of the G719S-T790M double mutation in the EGFR kinase domain and its response to inhibitors.Semantic proximity Read ↗

Genotype-determined EGFR-RTK heterodimerization and its effects on drug resistance in lung Cancer treatment revealed by molecular dynamics simulations.Semantic proximity Read ↗

Uncovering the Molecular Basis for the Better Gefitinib Sensitivity of EGFR with Complex Mutations over Single Rare Mutation: Insights from Molecular Simulations.Semantic proximity Read ↗

Computational and Experimental Characterization of Patient Derived Mutations Reveal an Unusual Mode of Regulatory Spine Assembly and Drug Sensitivity in EGFR Kinase.Semantic proximity Read ↗

Deciphering the Structural Effects of Activating EGFR Somatic Mutations with Molecular Dynamics Simulation.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.