Identifying novel targets of oncogenic EGF receptor signaling in lung cancer through global phosphoproteomics. - Wikidata - awgldk - TriplyDB

Identifying novel targets of oncogenic EGF receptor signaling in lung cancer through global phosphoproteomics.

Identifying novel targets of oncogenic EGF receptor signaling in lung cancer through global phosphoproteomics.

http://www.wikidata.org/entity/Q38420747

about

MAP4K4: an emerging therapeutic target in cancer SELPHI: correlation-based identification of kinase-associated networks from global phospho-proteomics data sets.Using activation status of signaling pathways as mechanism-based biomarkers to predict drug sensitivity Dysregulation of splicing proteins in head and neck squamous cell carcinoma.The current state of the art of quantitative phosphoproteomics and its applications to diabetes research The expression of SALL4 is significantly associated with EGFR, but not KRAS or EML4-ALK mutations in lung cancer.Understanding cell signaling in cancer stem cells for targeted therapy - can phosphoproteomics help to reveal the secrets?Glycoproteomic Approach Identifies KRAS as a Positive Regulator of CREG1 in Non-small Cell Lung Cancer Cells.Notch Signaling Components: Diverging Prognostic Indicators in Lung Adenocarcinoma.Harnessing Integrative Omics to Facilitate Molecular Imaging of the Human Epidermal Growth Factor Receptor Family for Precision Medicine.Proteomics Insights into Autophagy.iPTMnet: an integrated resource for protein post-translational modification network discovery.Quantitative Tyrosine Phosphoproteomics of Epidermal Growth Factor Receptor (EGFR) Tyrosine Kinase Inhibitor-treated Lung Adenocarcinoma Cells Reveals Potential Novel Biomarkers of Therapeutic Response.Integrative annotation and knowledge discovery of kinase post-translational modifications and cancer-associated mutations through federated protein ontologies and resources.

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Identifying novel targets of oncogenic EGF receptor signaling in lung cancer through global phosphoproteomics.

http://www.wikidata.org/entity/Q38420747

description

2015 nî lūn-bûn

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2015年の論文

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2015年論文

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2015年論文

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2015年論文

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2015年論文

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2015年论文

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2015年论文

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2015年论文

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name

Identifying novel targets of o ...... ough global phosphoproteomics.

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Identifying novel targets of o ...... ough global phosphoproteomics.

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Identifying novel targets of o ...... ough global phosphoproteomics.

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Identifying novel targets of o ...... rough global phosphoproteomics

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Abhilash Venugopalan

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Akhilesh Pandey

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Harrys Kishore Charles Jacob

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Min-Sik Kim

http://www.w3.org/2001/XMLSchema#string

Natalya Belkina

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Patrick G Shaw

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Raghothama Chaerkady

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Romi Biswas

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Tapan Maity

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Udayan Guha

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P2860

A proteomics strategy to elucidate functional protein-protein interactions applied to EGF signaling

Phosphorylation and regulation of Akt/PKB by the rictor-mTOR complex

Network organization of the human autophagy system

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

Regulation of 4E-BP1 phosphorylation: a novel two-step mechanism

PhosphoSitePlus: a comprehensive resource for investigating the structure and function of experimentally determined post-translational modifications in man and mouse

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

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

EGFR mutation and resistance of non-small-cell lung cancer to gefitinib.

Allelic dilution obscures detection of a biologically significant resistance mutation in EGFR-amplified lung cancer.

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340-355

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scholarly article

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10.1002/PMIC.201400315

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2-3

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15

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25404012

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