RNA helicase A is a DNA-binding partner for EGFR-mediated transcriptional activation in the nucleus.
about
Epidermal growth factor receptor potentiates MCM7-mediated DNA replication through tyrosine phosphorylation of Lyn kinase in human cancersNuclear ErbB2 enhances translation and cell growth by activating transcription of ribosomal RNA genesThe biology of DHX9 and its potential as a therapeutic targetNon-canonical signaling mode of the epidermal growth factor receptor familySolution structures of the double-stranded RNA-binding domains from RNA helicase ATargeting the EGFR/PCNA signaling suppresses tumor growth of triple-negative breast cancer cells with cell-penetrating PCNA peptidesSuppression of the DHX9 helicase induces premature senescence in human diploid fibroblasts in a p53-dependent manner.HMGN2 inducibly binds a novel transactivation domain in nuclear PRLr to coordinate Stat5a-mediated transcription.Epidermal Growth Factor Receptor Cell Proliferation Signaling PathwaysDependence of p53-deficient cells on the DHX9 DExH-box helicase.A functional nuclear epidermal growth factor receptor, SRC and Stat3 heteromeric complex in pancreatic cancer cellsEGFR modulates DNA synthesis and repair through Tyr phosphorylation of histone H4.RNA helicases: emerging roles in viral replication and the host innate response.Targeting the EGFR signaling pathway in cancer therapy.The translocon Sec61beta localized in the inner nuclear membrane transports membrane-embedded EGF receptor to the nucleus.saRNA-guided Ago2 targets the RITA complex to promoters to stimulate transcriptionActivation of Keap1/Nrf2 signaling pathway by nuclear epidermal growth factor receptor in cancer cells.Nuclear translocation of epidermal growth factor receptor by Akt-dependent phosphorylation enhances breast cancer-resistant protein expression in gefitinib-resistant cells.The Drosophila Helicase Maleless (MLE) is Implicated in Functions Distinct From its Role in Dosage CompensationMT1-MMP regulates the PI3Kδ·Mi-2/NuRD-dependent control of macrophage immune function.Landscape of EGFR signaling network in human cancers: biology and therapeutic response in relation to receptor subcellular locationsThe nuclear epidermal growth factor receptor signaling network and its role in cancer.Membrane-bound trafficking regulates nuclear transport of integral epidermal growth factor receptor (EGFR) and ErbB-2.Proteolytic cleavage, trafficking, and functions of nuclear receptor tyrosine kinases.On mammary gland growth factors: roles in normal development and in cancerNuclear functions and subcellular trafficking mechanisms of the epidermal growth factor receptor familyThe DEAD-Box RNA Helicase DDX3 Interacts with NF-κB Subunit p65 and Suppresses p65-Mediated TranscriptionPML represses lung cancer metastasis by suppressing the nuclear EGFR-mediated transcriptional activation of MMP2.Nuclear EGFR suppresses ribonuclease activity of polynucleotide phosphorylase through DNAPK-mediated phosphorylation at serine 776.Access to the nucleus and functional association with c-Myc is required for the full oncogenic potential of ΔEGFR/EGFRvIIIEGFR Signaling Enhances Aerobic Glycolysis in Triple-Negative Breast Cancer Cells to Promote Tumor Growth and Immune Escape.Tumor cell survival dependence on the DHX9 DExH-box helicaseWHSC1L1-mediated EGFR mono-methylation enhances the cytoplasmic and nuclear oncogenic activity of EGFR in head and neck cancer.The Pharmacogenetic Rescue of Side-Lined Anticancer Drugs to the Front-Line: Gefitinib as a Case Example.Nuclear EGFR as a molecular target in cancer.Compartmentalization of TNF-related apoptosis-inducing ligand (TRAIL) death receptor functions: emerging role of nuclear TRAIL-R2.EGFR targeted therapies and radiation: Optimizing efficacy by appropriate drug scheduling and patient selection.A data mining approach for identifying pathway-gene biomarkers for predicting clinical outcome: A case study of erlotinib and sorafenib.The role of HER2, EGFR, and other receptor tyrosine kinases in breast cancer.Multidrug-resistant cells overexpressing P-glycoprotein are susceptible to DNA crosslinking agents due to attenuated Src/nuclear EGFR cascade-activated DNA repair activity.
P2860
Q24294953-8F43CFC4-EB3D-4C3B-9831-4AA5A4B9D545Q24301779-45932B57-4ED5-4D82-B0D0-1D48B26EE314Q26749166-ADD34D28-233A-4CBE-976A-FCCBDA6C89EDQ26773754-5F3DF92F-E201-4C85-B05D-717374C844F1Q27678235-9735A70C-9DF3-481F-BC46-451327DCFD13Q28486075-167082BC-25B5-4DE3-A219-F958593B29F3Q33112680-594DC0A5-C2FC-458A-B4C7-F236A23B9A73Q33636880-3CE6F9BD-C737-431B-B509-CA222632C3FEQ33737298-BF7B6F0F-C79F-4B1D-BA19-846EE75E8E01Q33761586-0C08DD23-2F8A-4147-AD6E-278C1BE335E1Q33900776-6CC4DB18-80B3-464F-8EE0-61AFC7427EA6Q34109344-58362E69-D8C0-475F-85E1-DF442D83C307Q34155934-12EF0615-A702-468A-895C-FAC407D898CFQ34246558-737D35FF-F28A-4B4A-A4CD-625D3A85EBFAQ34352437-451A6011-E310-48E5-AEA6-74991F7211AFQ34515078-F4A075A1-838E-4934-80B1-EF11F08016F2Q34978749-427D331B-9B05-4459-A899-7A62FDBBD9E0Q35063410-67E8410F-6380-4475-890E-717C79D5EC28Q35692093-96728105-0CE1-4144-A039-962C2A0A6140Q35788951-6A1CAEC2-40A6-45B2-A700-0FCF0623054CQ35831012-9014DE6B-119C-4848-A5B5-A56891A7F284Q35834849-7AE0D919-ACE7-495A-BDB9-7AB2B92C6E69Q35956440-3B5B1E2B-BEB0-4F66-9B53-8F1E6C2CBFDFQ36113481-5D22E6A5-0F60-4FBB-96FC-E4A8CDD9BCD2Q36119485-02F829BA-5FA1-4FA9-9403-B21D4EA62A84Q36162605-EF87BC28-EE78-493F-9B25-A05D8B978CAAQ36162844-11CA4CEF-BD4B-4095-AA83-4C57B6AF5503Q36187706-C8326913-6B26-40B8-B418-2953C8368701Q36225686-0E346D77-14BE-44DF-85DD-526838480CF3Q36579570-5FAEF8A7-5B98-4186-AF20-0931945DFA80Q36642685-EC069365-E58A-4A5E-A22B-4CBEE68D10C8Q37256287-601A1FB0-BAA7-4E21-8B3F-9A33DD4849A6Q37593319-AB70B65D-B2D4-4CD0-8536-AC22D6A22EF8Q37838120-5E0C5942-386F-41A2-AD88-C41916D9EA71Q38119635-35164BF9-E38A-4AAF-B949-1D7923C63E34Q38244150-26126C1D-5D37-435F-990F-6776E0471CB0Q38552978-167387BB-BF4D-497C-8547-59D2E5046192Q38632417-DF49FDC6-53D3-4D75-8175-5AA804D09B30Q39028181-4A66E3D3-B2E2-451C-A998-751E39EAAB0EQ39360651-202D3CE7-D1E0-4286-A76B-99DC56FF97EE
P2860
RNA helicase A is a DNA-binding partner for EGFR-mediated transcriptional activation in the nucleus.
description
2010 nî lūn-bûn
@nan
2010 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
name
RNA helicase A is a DNA-bindin ...... nal activation in the nucleus.
@ast
RNA helicase A is a DNA-bindin ...... nal activation in the nucleus.
@en
RNA helicase A is a DNA-bindin ...... nal activation in the nucleus.
@nl
type
label
RNA helicase A is a DNA-bindin ...... nal activation in the nucleus.
@ast
RNA helicase A is a DNA-bindin ...... nal activation in the nucleus.
@en
RNA helicase A is a DNA-bindin ...... nal activation in the nucleus.
@nl
prefLabel
RNA helicase A is a DNA-bindin ...... nal activation in the nucleus.
@ast
RNA helicase A is a DNA-bindin ...... nal activation in the nucleus.
@en
RNA helicase A is a DNA-bindin ...... nal activation in the nucleus.
@nl
P2093
P2860
P356
P1476
RNA helicase A is a DNA-bindin ...... nal activation in the nucleus.
@en
P2093
Chang-Hai Tsai
Chien-Chen Lai
Chung-Hsuan Chen
Long-Yuan Li
Longfei Huo
Mien-Chie Hung
Ming-Chuan Hsu
Qingqing Ding
Sheng-Chieh Hsu
Tzu-Hsuan Huang
P2860
P304
16125-16130
P356
10.1073/PNAS.1000743107
P407
P577
2010-08-27T00:00:00Z