The T790M mutation in EGFR kinase causes drug resistance by increasing the affinity for ATP - Test2 - elhamkhani - TriplyDB

The T790M mutation in EGFR kinase causes drug resistance by increasing the affinity for ATP

The T790M mutation in EGFR kinase causes drug resistance by increasing the affinity for ATP

http://www.wikidata.org/entity/Q24649549

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MED12 controls the response to multiple cancer drugs through regulation of TGF-β receptor signaling Nitrile-containing pharmaceuticals: efficacious roles of the nitrile pharmacophore EGFR-mutant lung adenocarcinomas treated first-line with the novel EGFR inhibitor, XL647, can subsequently retain moderate sensitivity to erlotinib Classic and contemporary approaches to modeling biochemical reactions Targeting the PI3K signaling pathway in cancer Cancer pharmacogenomics, challenges in implementation, and patient-focused perspectives Non-Invasive Methods to Monitor Mechanisms of Resistance to Tyrosine Kinase Inhibitors in Non-Small-Cell Lung Cancer: Where Do We Stand?Overcoming resistance to first/second generation epidermal growth factor receptor tyrosine kinase inhibitors and ALK inhibitors in oncogene-addicted advanced non-small cell lung cancer Role of gefitinib in the targeted treatment of non-small-cell lung cancer in Chinese patients Implications of MicroRNAs in the Treatment of Gefitinib-Resistant Non-Small Cell Lung Cancer Somatic DNA mutation analysis in targeted therapy of solid tumours Circulating DNA in diagnosis and monitoring EGFR gene mutations in advanced non-small cell lung cancer Overcoming resistance to targeted therapies in NSCLC: current approaches and clinical application The latest therapeutic strategies after resistance to first generation epidermal growth factor receptor tyrosine kinase inhibitors (EGFR TKIs) in patients with non-small cell lung cancer (NSCLC)Predictive biomarkers in precision medicine and drug development against lung cancer Transformation from non-small-cell lung cancer to small-cell lung cancer: molecular drivers and cells of origin EGFR mutations as a prognostic and predictive marker in non-small-cell lung cancer Rational approaches to improving selectivity in drug design Targeting cancer with kinase inhibitors Irreversible EGFR-TKIs: dreaming perfection Resistance to receptor tyrosine kinase inhibition in cancer: molecular mechanisms and therapeutic strategies Profile of neratinib and its potential in the treatment of breast cancer Tumor heterogeneity and resistance to EGFR-targeted therapy in advanced nonsmall cell lung cancer: challenges and perspectives The role of irreversible HER family inhibition in the treatment of patients with non-small cell lung cancer Molecular mechanisms of disease-causing missense mutations Signaling cross-talk in the resistance to HER family receptor targeted therapy Enhanced dimerization drives ligand-independent activity of mutant epidermal growth factor receptor in lung cancer In vitro selection of mutant HDM2 resistant to Nutlin inhibition CIViC database Activation of tyrosine kinases by mutation of the gatekeeper threonine KIT kinase mutants show unique mechanisms of drug resistance to imatinib and sunitinib in gastrointestinal stromal tumor patients Equally Potent Inhibition of c-Src and Abl by Compounds that Recognize Inactive Kinase Conformations Novel mutant-selective EGFR kinase inhibitors against EGFR T790M Erlotinib binds both inactive and active conformations of the EGFR tyrosine kinase domain Structural basis for the altered drug sensitivities of non-small cell lung cancer-associated mutants of human epidermal growth factor receptor Structural and Spectroscopic Analysis of the Kinase Inhibitor Bosutinib and an Isomer of Bosutinib Binding to the Abl Tyrosine Kinase Domain Mechanism for activation of mutated epidermal growth factor receptors in lung cancer Structural, Biochemical, and Clinical Characterization of Epidermal Growth Factor Receptor (EGFR) Exon 20 Insertion Mutations in Lung Cancer Oncogenic RET Kinase Domain Mutations Perturb the Autophosphorylation Trajectory by Enhancing Substrate Presentation In trans Mechanisms of drug resistance in kinases.

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The T790M mutation in EGFR kinase causes drug resistance by increasing the affinity for ATP

http://www.wikidata.org/entity/Q24649549

description

2008 nî lūn-bûn

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2008 թուականի Փետրուարին հրատարակուած գիտական յօդուած

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2008 թվականի փետրվարին հրատարակված գիտական հոդված

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2008年の論文

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2008年論文

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2008年論文

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2008年論文

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2008年論文

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2008年論文

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2008年论文

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name

The T790M mutation in EGFR kin ...... ncreasing the affinity for ATP

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The T790M mutation in EGFR kin ...... ncreasing the affinity for ATP

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The T790M mutation in EGFR kin ...... ncreasing the affinity for ATP

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label

The T790M mutation in EGFR kin ...... ncreasing the affinity for ATP

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The T790M mutation in EGFR kin ...... ncreasing the affinity for ATP

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The T790M mutation in EGFR kin ...... ncreasing the affinity for ATP

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The T790M mutation in EGFR kin ...... ncreasing the affinity for ATP

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The T790M mutation in EGFR kin ...... ncreasing the affinity for ATP

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The T790M mutation in EGFR kin ...... ncreasing the affinity for ATP

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PNAS.0709662105

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Proceedings of the National Academy of Sciences of the United States of America

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The T790M mutation in EGFR kin ...... ncreasing the affinity for ATP

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Angela V Toms

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Cai-Hong Yun

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Kristen E Mengwasser

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Michael J Eck

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Michele S Woo

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P2860

An allosteric mechanism for activation of the kinase domain of epidermal growth factor receptor

EGF receptor gene mutations are common in lung cancers from "never smokers" and are associated with sensitivity of tumors to gefitinib and erlotinib

Acquired resistance of lung adenocarcinomas to gefitinib or erlotinib is associated with a second mutation in the EGFR kinase domain

Oncogenic transformation by inhibitor-sensitive and -resistant EGFR mutants

Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination

Processing of X-ray diffraction data collected in oscillation mode

Development of new mouse lung tumor models expressing EGFR T790M mutants associated with clinical resistance to kinase inhibitors

Structure of the epidermal growth factor receptor kinase domain alone and in complex with a 4-anilinoquinazoline inhibitor

Structures of Lung Cancer-Derived EGFR Mutants and Inhibitor Complexes: Mechanism of Activation and Insights into Differential Inhibitor Sensitivity

EGFR mutations in lung cancer: correlation with clinical response to gefitinib therapy.

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10.1073/PNAS.0709662105

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Matthew Meyerson

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2008-02-12T00:00:00Z

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