HCSGD entry for EGFR
1. General information
Official gene symbol | EGFR |
---|---|
Entrez ID | 1956 |
Gene full name | epidermal growth factor receptor |
Other gene symbols | ERBB ERBB1 HER1 PIG61 mENA |
Links to Entrez Gene | Links to Entrez Gene |
2. Neighbors in the network
![color bar](img/red_blue.jpg)
3. Gene ontology annotation
GO ID | GO term | Evidence | Category |
---|---|---|---|
GO:0000139 | Golgi membrane | IEA | cellular_component |
GO:0000165 | MAPK cascade | NAS | biological_process |
GO:0000186 | Activation of MAPKK activity | IEA | biological_process |
GO:0001503 | Ossification | NAS | biological_process |
GO:0001889 | Liver development | IEA | biological_process |
GO:0001892 | Embryonic placenta development | IEA | biological_process |
GO:0001934 | Positive regulation of protein phosphorylation | IDA | biological_process |
GO:0001942 | Hair follicle development | IEA | biological_process |
GO:0001948 | Glycoprotein binding | IEA | molecular_function |
GO:0003682 | Chromatin binding | IDA | molecular_function |
GO:0003690 | Double-stranded DNA binding | NAS | molecular_function |
GO:0004709 | MAP kinase kinase kinase activity | NAS | molecular_function |
GO:0004713 | Protein tyrosine kinase activity | IDA IMP TAS | molecular_function |
GO:0004714 | Transmembrane receptor protein tyrosine kinase activity | IEA TAS | molecular_function |
GO:0004716 | Receptor signaling protein tyrosine kinase activity | IEA | molecular_function |
GO:0004888 | Transmembrane signaling receptor activity | IDA | molecular_function |
GO:0005006 | Epidermal growth factor-activated receptor activity | IDA IEA NAS | molecular_function |
GO:0005178 | Integrin binding | IEA | molecular_function |
GO:0005515 | Protein binding | IPI | molecular_function |
GO:0005524 | ATP binding | IEA | molecular_function |
GO:0005615 | Extracellular space | NAS | cellular_component |
GO:0005634 | Nucleus | IDA IEA | cellular_component |
GO:0005737 | Cytoplasm | IDA | cellular_component |
GO:0005768 | Endosome | IDA IEA | cellular_component |
GO:0005789 | Endoplasmic reticulum membrane | IEA | cellular_component |
GO:0005886 | Plasma membrane | IDA TAS | cellular_component |
GO:0005976 | Polysaccharide metabolic process | IEA | biological_process |
GO:0006412 | Translation | IEA | biological_process |
GO:0006950 | Response to stress | NAS | biological_process |
GO:0006970 | Response to osmotic stress | IEA | biological_process |
GO:0006979 | Response to oxidative stress | IEA | biological_process |
GO:0007165 | Signal transduction | IDA TAS | biological_process |
GO:0007166 | Cell surface receptor signaling pathway | IDA | biological_process |
GO:0007169 | Transmembrane receptor protein tyrosine kinase signaling pathway | IEA | biological_process |
GO:0007173 | Epidermal growth factor receptor signaling pathway | IDA TAS | biological_process |
GO:0007202 | Activation of phospholipase C activity | TAS | biological_process |
GO:0007411 | Axon guidance | TAS | biological_process |
GO:0007435 | Salivary gland morphogenesis | IEA | biological_process |
GO:0007611 | Learning or memory | ISS | biological_process |
GO:0007623 | Circadian rhythm | IEA | biological_process |
GO:0008283 | Cell proliferation | IDA | biological_process |
GO:0008284 | Positive regulation of cell proliferation | IDA | biological_process |
GO:0008543 | Fibroblast growth factor receptor signaling pathway | TAS | biological_process |
GO:0009986 | Cell surface | IEA | cellular_component |
GO:0010008 | Endosome membrane | IEA | cellular_component |
GO:0010960 | Magnesium ion homeostasis | IEA | biological_process |
GO:0016020 | Membrane | IDA | cellular_component |
GO:0016021 | Integral component of membrane | IEA | cellular_component |
GO:0016101 | Diterpenoid metabolic process | IEA | biological_process |
GO:0016323 | Basolateral plasma membrane | IDA IEA | cellular_component |
GO:0016324 | Apical plasma membrane | IEA | cellular_component |
GO:0016337 | Cell-cell adhesion | IMP | biological_process |
GO:0018108 | Peptidyl-tyrosine phosphorylation | IDA IMP NAS TAS | biological_process |
GO:0019694 | Alkanesulfonate metabolic process | IEA | biological_process |
GO:0019899 | Enzyme binding | IPI | molecular_function |
GO:0019901 | Protein kinase binding | IEA | molecular_function |
GO:0019903 | Protein phosphatase binding | IPI | molecular_function |
GO:0021795 | Cerebral cortex cell migration | IEA | biological_process |
GO:0023014 | Signal transduction by phosphorylation | NAS | biological_process |
GO:0030122 | AP-2 adaptor complex | TAS | cellular_component |
GO:0030139 | Endocytic vesicle | IEA | cellular_component |
GO:0030235 | Nitric-oxide synthase regulator activity | IDA | molecular_function |
GO:0030324 | Lung development | IEA | biological_process |
GO:0030335 | Positive regulation of cell migration | IMP | biological_process |
GO:0031659 | Positive regulation of cyclin-dependent protein serine/threonine kinase activity involved in G1/S transition of mitotic cell cycle | IDA | biological_process |
GO:0031965 | Nuclear membrane | IEA | cellular_component |
GO:0032355 | Response to estradiol | IEA | biological_process |
GO:0032930 | Positive regulation of superoxide anion generation | IEA | biological_process |
GO:0033590 | Response to cobalamin | IEA | biological_process |
GO:0033594 | Response to hydroxyisoflavone | IEA | biological_process |
GO:0035413 | Positive regulation of catenin import into nucleus | IMP | biological_process |
GO:0035690 | Cellular response to drug | IEA | biological_process |
GO:0038095 | Fc-epsilon receptor signaling pathway | TAS | biological_process |
GO:0042059 | Negative regulation of epidermal growth factor receptor signaling pathway | TAS | biological_process |
GO:0042177 | Negative regulation of protein catabolic process | IDA | biological_process |
GO:0042327 | Positive regulation of phosphorylation | IDA | biological_process |
GO:0042698 | Ovulation cycle | IEA | biological_process |
GO:0042743 | Hydrogen peroxide metabolic process | IEA | biological_process |
GO:0042802 | Identical protein binding | IPI | molecular_function |
GO:0043006 | Activation of phospholipase A2 activity by calcium-mediated signaling | TAS | biological_process |
GO:0043066 | Negative regulation of apoptotic process | IEA IMP | biological_process |
GO:0043235 | Receptor complex | IDA | cellular_component |
GO:0043406 | Positive regulation of MAP kinase activity | IDA | biological_process |
GO:0043586 | Tongue development | IEA | biological_process |
GO:0045087 | Innate immune response | TAS | biological_process |
GO:0045121 | Membrane raft | IDA | cellular_component |
GO:0045429 | Positive regulation of nitric oxide biosynthetic process | IDA | biological_process |
GO:0045739 | Positive regulation of DNA repair | IDA | biological_process |
GO:0045740 | Positive regulation of DNA replication | IDA | biological_process |
GO:0045907 | Positive regulation of vasoconstriction | IEA | biological_process |
GO:0045909 | Positive regulation of vasodilation | IEA | biological_process |
GO:0045930 | Negative regulation of mitotic cell cycle | IEA | biological_process |
GO:0045944 | Positive regulation of transcription from RNA polymerase II promoter | IDA | biological_process |
GO:0046777 | Protein autophosphorylation | IEA IMP | biological_process |
GO:0046982 | Protein heterodimerization activity | IDA IEA | molecular_function |
GO:0048011 | Neurotrophin TRK receptor signaling pathway | TAS | biological_process |
GO:0048015 | Phosphatidylinositol-mediated signaling | TAS | biological_process |
GO:0048143 | Astrocyte activation | IEA | biological_process |
GO:0048146 | Positive regulation of fibroblast proliferation | IEA | biological_process |
GO:0048408 | Epidermal growth factor binding | IEA | molecular_function |
GO:0048471 | Perinuclear region of cytoplasm | IEA | cellular_component |
GO:0048546 | Digestive tract morphogenesis | IEA | biological_process |
GO:0048661 | Positive regulation of smooth muscle cell proliferation | IEA | biological_process |
GO:0048812 | Neuron projection morphogenesis | IEA | biological_process |
GO:0050679 | Positive regulation of epithelial cell proliferation | IDA IEA | biological_process |
GO:0050729 | Positive regulation of inflammatory response | IEA | biological_process |
GO:0050730 | Regulation of peptidyl-tyrosine phosphorylation | IEA IMP | biological_process |
GO:0050999 | Regulation of nitric-oxide synthase activity | IDA | biological_process |
GO:0051015 | Actin filament binding | IDA | molecular_function |
GO:0051205 | Protein insertion into membrane | TAS | biological_process |
GO:0051592 | Response to calcium ion | IEA | biological_process |
GO:0051897 | Positive regulation of protein kinase B signaling | IMP | biological_process |
GO:0051968 | Positive regulation of synaptic transmission, glutamatergic | IEA | biological_process |
GO:0060571 | Morphogenesis of an epithelial fold | IEA | biological_process |
GO:0070141 | Response to UV-A | IDA | biological_process |
GO:0070374 | Positive regulation of ERK1 and ERK2 cascade | IDA | biological_process |
GO:0070435 | Shc-EGFR complex | ISS | cellular_component |
GO:0071260 | Cellular response to mechanical stimulus | IEA | biological_process |
GO:0071363 | Cellular response to growth factor stimulus | IEA | biological_process |
GO:0071364 | Cellular response to epidermal growth factor stimulus | ISS | biological_process |
GO:0071392 | Cellular response to estradiol stimulus | IDA | biological_process |
GO:0071549 | Cellular response to dexamethasone stimulus | IEA | biological_process |
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4. Expression levels in datasets
- Meta-analysis result
p-value up | p-value down | FDR up | FDR down |
---|---|---|---|
0.0223557274 | 0.9615435698 | 0.3573167374 | 1.0000000000 |
- Individual experiment result
( "-" represent NA in the specific microarray platform )
( "-" represent NA in the specific microarray platform )
Data source | Up or down | Log fold change |
---|---|---|
GSE11954 | Up | 0.0964499087 |
GSE13712_SHEAR | Down | -0.0443399929 |
GSE13712_STATIC | Up | 0.1818799462 |
GSE19018 | Up | 0.1214152605 |
GSE19899_A1 | Up | 0.3643212692 |
GSE19899_A2 | Up | 0.7559463489 |
PubMed_21979375_A1 | Up | 0.4142138987 |
PubMed_21979375_A2 | Up | 0.7343675614 |
GSE35957 | Up | 0.5265372072 |
GSE36640 | Down | -0.2189520420 |
GSE54402 | Down | -0.2435580891 |
GSE9593 | Up | 0.3734447179 |
GSE43922 | Up | 0.1263406313 |
GSE24585 | Up | 0.1728687224 |
GSE37065 | Down | -0.2172226177 |
GSE28863_A1 | Up | 0.8753358749 |
GSE28863_A2 | Up | 0.9760360349 |
GSE28863_A3 | Up | 0.1116951969 |
GSE28863_A4 | Down | -0.1342190671 |
GSE48662 | Down | -0.1628021784 |
5. Regulation relationships with compounds/drugs/microRNAs
- Compounds
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- Drugs
Name | Drug | Accession number |
---|---|---|
Cetuximab | DB00002 | BTD00071 | BIOD00071 |
Trastuzumab | DB00072 | BTD00098 | BIOD00098 |
Lidocaine | DB00281 | APRD00479 | DB05291 |
Gefitinib | DB00317 | APRD00997 | DB07998 |
Erlotinib | DB00530 | APRD00951 |
Panitumumab | DB01269 | - |
Flavopiridol | DB03496 | EXPT00998 |
IGN311 | DB04988 | - |
Matuzumab | DB05101 | - |
HuMax-EGFr | DB05324 | - |
CDX-110 | DB05374 | - |
CI-1033 | DB05424 | - |
IMC-11F8 | DB05774 | - |
INSM-18 | DB05900 | - |
S-{3-[(4-ANILINOQUINAZOLIN-6-YL)AMINO]-3-OXOPROPYL}-L-CYSTEINE | DB07602 | - |
N-[4-(3-BROMO-PHENYLAMINO)-QUINAZOLIN-6-YL]-ACRYLAMIDE | DB07662 | - |
Afatinib | DB08916 | - |
Osimertinib | DB09330 | - |
Necitumumab | DB09559 | - |
- MicroRNAs
- mirTarBase
MiRNA_name | mirBase ID | miRTarBase ID | Experiment | Support type | References (Pubmed ID) |
---|---|---|---|---|---|
hsa-miR-542-5p | MIMAT0003340 | MIRT006330 | Luciferase reporter assay//qRT-PCR//Western blot | Functional MTI | 22426479 |
hsa-miR-1 | MIMAT0000416 | MIRT001370 | pSILAC//Proteomics;Other | Functional MTI (Weak) | 18668040 |
hsa-miR-16-5p | MIMAT0000069 | MIRT001470 | pSILAC//Proteomics;Other | Functional MTI (Weak) | 18668040 |
hsa-miR-7-5p | MIMAT0000252 | MIRT002289 | real-time RT-PCR//Reporter assay//Western blot//Luciferase reporter assay//Reporter assay;Western blot;qRT-PCR;Other | Functional MTI | 18483236 |
hsa-miR-7-5p | MIMAT0000252 | MIRT002289 | Luciferase reporter assay//qRT-PCR//Western blot//Reporter assay;Western blot;qRT-PCR;Microarray;Other | Functional MTI | 19073608 |
hsa-miR-7-5p | MIMAT0000252 | MIRT002289 | Luciferase reporter assay | Functional MTI | 19029026 |
hsa-miR-7-5p | MIMAT0000252 | MIRT002289 | Luciferase reporter assay | Functional MTI | 19033458 |
hsa-miR-7-5p | MIMAT0000252 | MIRT002289 | Luciferase reporter assay//Microarray//Western blot | Functional MTI | 20864407 |
hsa-miR-7-5p | MIMAT0000252 | MIRT002289 | Microarray | Functional MTI (Weak) | 17612493 |
hsa-miR-7-5p | MIMAT0000252 | MIRT002289 | Western blot | Functional MTI | 22853714 |
hsa-miR-128-3p | MIMAT0000424 | MIRT004353 | Western blot | Functional MTI | 22853714 |
hsa-miR-146a-5p | MIMAT0000449 | MIRT004730 | qRT-PCR//Western blot | Functional MTI | 20124483 |
hsa-miR-146a-5p | MIMAT0000449 | MIRT004730 | Luciferase reporter assay//Western blot | Functional MTI | 21632853 |
hsa-miR-146a-5p | MIMAT0000449 | MIRT004730 | Luciferase reporter assay//qRT-PCR//Western blot | Functional MTI | 22161865 |
hsa-miR-146a-5p | MIMAT0000449 | MIRT004730 | Western blot | Functional MTI | 19190326 |
hsa-miR-21-5p | MIMAT0000076 | MIRT005807 | Luciferase reporter assay//Microarray//Western blot | Functional MTI | 20864407 |
hsa-miR-21-5p | MIMAT0000076 | MIRT005807 | Western blot;Other | Functional MTI | 20048743 |
hsa-miR-133a-3p | MIMAT0000427 | MIRT007032 | Luciferase reporter assay | Functional MTI | 23069713 |
hsa-miR-133b | MIMAT0000770 | MIRT007069 | Flow//In situ hybridization//Luciferase reporter assay//qRT-PCR//Western blot | Functional MTI | 22883469 |
hsa-miR-27a-3p | MIMAT0000084 | MIRT007360 | Luciferase reporter assay | Functional MTI | 23559009 |
hsa-miR-335-5p | MIMAT0000765 | MIRT018378 | Microarray | Functional MTI (Weak) | 18185580 |
hsa-miR-155-5p | MIMAT0000646 | MIRT020911 | Proteomics | Functional MTI (Weak) | 18668040 |
hsa-miR-30a-5p | MIMAT0000087 | MIRT028600 | Proteomics | Functional MTI (Weak) | 18668040 |
hsa-let-7a-5p | MIMAT0000062 | MIRT035541 | Luciferase reporter assay | Functional MTI | 23032975 |
hsa-miR-301b | MIMAT0004958 | MIRT036702 | CLASH | Functional MTI (Weak) | 23622248 |
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- mirRecord
MicroRNA name | mirBase ID | Target site number | MiRNA mature ID | Test method inter | MiRNA regulation site | Reporter target site | Pubmed ID |
---|---|---|---|---|---|---|---|
hsa-miR-7-5p | MIMAT0000252 | 3 | hsa-miR-7 | {Western blot} | {overexpression by miRNA precursor transfection} | 18483236 | |
hsa-miR-7-5p | MIMAT0000252 | 2 | hsa-miR-7 | {Western blot} | {overexpression by miRNA precursor transfection} | 18483236 | |
hsa-miR-7-5p | MIMAT0000252 | 1 | hsa-miR-7 | {Western blot} | {overexpression by miRNA precursor transfection} | 18483236 | |
hsa-miR-7-5p | MIMAT0000252 | 1 | hsa-miR-7 | 19073608 | |||
hsa-miR-7-5p | MIMAT0000252 | 2 | hsa-miR-7 | 19073608 | |||
hsa-miR-7-5p | MIMAT0000252 | NA | hsa-miR-7 | {Western blot} | {overexpression by miRNA precursor transfection} | 21156648 |
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6. Text-mining results about the gene
Gene occurances in abstracts of cellular senescence-associated articles: 35 abstracts the gene occurs.
PubMed ID of the article | Sentenece the gene occurs |
---|---|
26977878 | This relieves feedback inhibition of upstream EGFR family kinases, resensitizing tumors to EGFR/HER2 blockade |
26977878 | Consequently, dual inhibition of EGFR/HER2 and CDK4/6 invokes a more potent suppression of TSC2 phosphorylation and hence mTORC1/S6K/S6RP activity |
26899446 | A computational approach demonstrated that predicted target genes of the miRNA profile were found to be mainly involved in processes including cell adhesion, collagen synthesis, positive or negative regulation of transcription, as well as pathways such as insulin signaling pathway, ErbB (Erythroblastic Leukemia Viral Oncogene Homolog) signaling pathway and Focal adhesion pathway |
26420897 | BACKGROUND: In glioblastoma (GBM), the gene for epidermal growth factor receptor (EGFR) is frequently amplified |
26420897 | EGFR mutations also are common, including a truncation mutation that yields a constitutively active variant called EGFR variant (v)III |
26420897 | EGFRvIII-positive GBM progresses rapidly; however, the reason for this is not clear because the activity of EGFRvIII is attenuated compared with EGF-ligated wild-type EGFR |
26420897 | RESULTS: In human GBM, EGFR overexpression and EGFRvIII positivity were associated with increased VEGFR2 expression |
26420897 | Coexpression of VEGFR2 by GBM cells in which EGFR signaling is activated may contribute to the aggressive nature of these cells |
26420857 | PURPOSE: Aberrant regulation of the EGF receptor family (EGFR, HER2, HER3, HER4) contributes to tumorigenesis and metastasis in epithelial cancers |
26420857 | Pan-HER represents a novel molecular targeted therapeutic composed of a mixture of six monoclonal antibodies against EGFR, HER2, and HER3 |
26360782 | Bradykinin inhibits oxidative stress-induced senescence of endothelial progenitor cells through the B2R/AKT/RB and B2R/EGFR/RB signal pathways |
25594009 | In addition, TBK1-II cooperated with lapatinib, a EGFR/HER2 inhibitor, to accelerate apoptosis in vitro and suppress tumor growth in a xenograft model of HER2(+) BC |
25504754 | In glioblastoma cells treated with berberine, the level of epidermal growth factor receptor (EGFR) was greatly reduced |
25504754 | Examination of the activities of the kinases downstream of EGFR revealed that the RAF-MEK-ERK signaling pathway was remarkably inhibited, whereas AKT phosphorylation was not altered |
25504754 | Pharmacologic inhibition or RNA interference of EGFR similarly induced cellular senescence of glioblastoma cells |
25504754 | Berberine also potently inhibited the growth of tumor xenografts, which was accompanied by downregulation of EGFR and induction of senescence |
25504754 | Because EGFR is commonly upregulated in glioblastoma, the demonstration of effective inhibition of EGFR by berberine points to the possibility of using berberine in the treatment of patients with glioblastoma |
25077560 | Here we show in different models of senescence that the metalloprotease A disintegrin and metalloproteinase 17 (ADAM17) is activated and releases the epidermal growth factor receptor ligand amphiregulin and tumor necrosis factor receptor I (TNFRI) from the surface of senescent cells by ectodomain shedding |
25077541 | ADCY5 repression by miR-17 also facilitated the translocation of EGFR and MKP7 from membrane into cytoplasmic and mitochondrial fractions |
24055032 | METHOD: We have constructed multiple shRNA expression vectors of targeting EGFR, IGF1R and Bcl-xl, which were transfected to the CNE2 cells |
24055032 | The growth of the cells, cell cycle progression, apoptosis of the cells, senescent tumor cells and the proteins of EGFR, IGF1R and Bcl-xl were analyzed by MTT, flow cytometry, cytochemical therapy or Western blot |
24055032 | RESULTS: In group of simultaneously blocking EGFR, IGF1R and Bcl-xl genes, the mRNA of EGFR, IGF1R and Bcl-xl expression was decreased by (66 |
24055032 | CONCLUSIONS: Simultaneously blocking EGFR, IGF1R and Bcl-xl genes is capable of altering the balance between proliferating versus apoptotic and senescent cells in the favor of both of apoptosis and senescence and, therefore, the tumor cells regression |
24047696 | Cellular senescence or EGFR signaling induces Interleukin 6 (IL-6) receptor expression controlled by mammalian target of rapamycin (mTOR) |
24047696 | Moreover, aberrant EGF receptor (EGFR) activation triggered IL-6 synthesis |
23974111 | EGFR inhibitors exacerbate differentiation and cell cycle arrest induced by retinoic acid and vitamin D3 in acute myeloid leukemia cells |
23974111 | By means of an unbiased, automated fluorescence microscopy-based screen, we identified the epidermal growth factor receptor (EGFR) inhibitors erlotinib and gefitinib as potent enhancers of the differentiation of HL-60 acute myeloid leukemia (AML) cells exposed to suboptimal concentrations of vitamin A (all-trans retinoic acid, ATRA) or vitamin D (1alpha,25-hydroxycholecalciferol, VD) |
23974111 | Altogether, these findings point to a new regimen for the treatment of AML, in which naturally occurring pro-differentiation agents (ATRA or VD) may be combined with EGFR inhibitors |
23746120 | Furthermore, our results showed that Mig-6 induction of senescence is related to its inhibition of EGF receptor (EGFR)/Erb B signalling |
21934682 | BACKGROUND: Epidermal growth factor receptor (EGFR) signalling is frequently altered during glioblastoma de novo pathogenesis |
21852385 | The mechanisms by which inhibition of the epidermal growth factor receptor (EGFR) sensitizes non-small cell lung cancer (NSCLC) cells to ionizing radiation remain poorly understood |
21852385 | Unexpectedly, EGFR inhibition led to pronounced cellular senescence but not apoptosis of irradiated cells, both in vitro and in vivo |
21852385 | This effect of EGFR inhibition was at least partially mediated by disruption of the MEK-ERK pathway |
21627565 | In the present study, we investigated the expression of human telomerase reverse transcriptase (hTERT) and TA and their regulation, as well as apoptotic rates and correlation with the presence of human epidermal growth factor receptor 2 (HER2), in irradiated tumour-derived breast cancer cells |
21286718 | Cetuximab enhances the activities of irinotecan on gastric cancer cell lines through downregulating the EGFR pathway upregulated by irinotecan |
21286718 | The epidermal growth factor receptor (EGFR) monoclonal antibody cetuximab inhibits the growth of several human cancer cells but has been tested rarely for the treatment of GC |
21286718 | The effects of cetuximab or irinotecan as single agents or the combination on the expression of p53, p16, and EGFR signaling pathways were also studied |
21286718 | Irinotecan increases phosphorylation of EGFR, MAPK, and AKT and decreases the expression of P27(Kip1), which could be all abrogated by its combination with cetuximab |
21286718 | CONCLUSIONS : Cetuximab enhances the activities of irinotecan on GC cells via the downregulation of the EGFR pathway upregulated by irinotecan |
20890302 | Reversion-inducing cysteine-rich protein with Kazal motifs interferes with epidermal growth factor receptor signaling |
20890302 | In addition, we observed that epidermal growth factor receptor (EGFR) activity was transiently upregulated by RECK depletion in MEFs, and continuously downregulated by RECK overexpression in colon cancer cells |
20890302 | These findings indicate that RECK is a novel modulator of EGFR signaling |
20668675 | Importantly, we show that despite being membrane-bound signalling molecules, class III neuregulins transform via a cell intrinsic mechanism, as a result of constitutive, elevated levels of ErbB signalling at high cell density and in anchorage-free conditions |
20424117 | Epidermal growth factor receptor and mutant p53 expand an esophageal cellular subpopulation capable of epithelial-to-mesenchymal transition through ZEB transcription factors |
20424117 | We have found that both epidermal growth factor receptor (EGFR) overexpression and mutant p53 tumor suppressor genes contribute to the enrichment of an EMT-competent cellular subpopulation among telomerase-immortalized human esophageal epithelial cells during malignant transformation |
20424117 | EGFR overexpression triggers oncogene-induced senescence, accompanied by the induction of cyclin-dependent kinase inhibitors p15(INK4B), p16(INK4A), and p21 |
20424117 | Interestingly, a subpopulation of cells emerges by negating senescence without loss of EGFR overexpression |
20424117 | Thus, senescence checkpoint functions activated by EGFR and p53 may be evaded through the induction of ZEB, thereby allowing the expansion of an EMT-competent unique cellular subpopulation, providing novel mechanistic insights into the role of ZEB in esophageal carcinogenesis |
20300111 | These data show that Jun is of critical importance for cellular protection against oxidative stress in fetal livers and fibroblasts, and Jun-dependent cellular senescence can be restored by activation of the epidermal growth factor receptor pathway |
19938640 | Several molecular targeting therapies are described by activation and blocking distinct developmental signaling cascade elements, such as BRCA1, EGFR, hedgehog, Wnt/beta-catenin, and/or Notch pathways, which are frequently upregulated in cancer progenitor cells during the initiation and development of breast cancer |
19686285 | MGs of ganp(Low) expression displayed more malignant characteristics, with loss of heterozygosity on chromosome 10, epidermal growth factor receptor gene amplification, and significantly poorer prognosis than the ganp(High) group |
17251932 | This concept has received clinical validation by the development of active anticancer drugs that specifically inhibit the function of oncoproteins such as BCR-ABL, c-KIT and EGFR |
14499637 | A key stimulus for human dermal fibroblasts are ligands for the epidermal growth factor receptor (EGFR) |
14499637 | We have shown earlier that EGFR expression decreases by about half in near senescent fibroblasts (Shiraha et al |
14499637 | Herein, we show that EGFR signaling as determined by receptor autophosphorylation is diminished over 80%, with a corresponding decrease in the phosphorylation of the immediate postreceptor adaptor Shc |
14499637 | Interestingly, we found that this was due at least in part to increased dephosphorylation of EGFR |
14499637 | Last, inhibition of protein tyrosine phosphatases by sodium orthovanadate in near senescent cells resulted in increased EGFR phosphorylation |
12717449 | Furthermore, we show that inhibiting expression of one of these genes, the epidermal growth factor receptor (EGFR), reverses the enhanced proliferation caused by telomerase |
12593448 | Addition of epidermal growth factors receptor (EGFR) antibody to cells exposed to media devoid of EGF and media supplemented with TGF-alpha showed marked suppression of proliferation of target cells |
11976184 | In those senescent cells, we found an increased level of caveolin proteins and strong interactions between caveolin-1 and EGFR |
11795531 | Caveolin proteins directly interact with signaling molecules including EGF receptor and suppress the activation of EGFR upon EGF stimulation |
11795531 | We also demonstrated up-regulated caveolin proteins were co-localized with EGFR proteins in detergent-insoluble fractions |
11431323 | These alterations together, however, cooperated with ras pathway activation (initiated by expression of mutant H-Ras), but not with phosphatidylinositol 3-kinase pathway activation (initiated by expression of myristoylated Akt) or epidermal growth factor receptor activation, to allow for the formation of intracranial tumors strongly resembling p53/pRb pathway-deficient, telomerase-positive, ras-activated human grade III anaplastic astrocytomas |
10764734 | Aged cells presented decreased levels of EGFR, although insulin receptor and transferrin receptor levels were relatively unchanged |
10764734 | EGFR mRNA levels and production of new transcripts decreased during aging, suggesting that this preferential loss of EGFR was due to diminished production, which more than counteracts the reduced ligand-induced receptor loss |
10764734 | Since these data suggested that the decrement in EGF was rate-limiting, higher levels of EGFR were established in near senescent cells by electroporation of EGFR cDNA |
10764734 | These cells presented higher levels of EGFR and recovered their EGF-induced migration and proliferation responsiveness |
10764734 | Thus, the defect in EGF responsiveness of aged dermal fibroblasts is secondary to reduced EGFR message transcription |
10764734 | Our experimental model suggests that EGFR gene delivery might be an effective future therapy for compromised wound healing |
8893868 | Amplification and/or overexpression of the oncogenes epidermal growth factor receptor and erbB2 are associated with later stage disease |
8077280 | Cleavage of the epidermal growth factor receptor by a membrane-bound leupeptin-sensitive protease active in nonionic detergent lysates of senescent but not young human diploid fibroblasts |
8223996 | In contrast, we now report striking differences in EGF receptor (EGFR) number, affinity, and rate of EGF/EGFR internalization in early-passage dermal fibroblasts derived from newborn versus young adult versus old adult donors |
3012222 | Cellular responsiveness to epidermal growth factor (EGF) and the structure of the receptor for epidermal growth factor (EGF-R) were compared in young and senescent human fibroblast (HF) cells |
3012222 | Biosynthetic labeling of HF cells with [35S] methionine followed by immunoprecipitation with EGF-R antibody revealed the presence of Mr 170 000 EGF-R in cells from both stages |
3012222 | Autophosphorylation of EGF-R in response to EGF was identical in young and senescent cells |
3012222 | Phosphoamino acid analysis of the autophosphorylated EGF-R indicated that tyrosine residues were phosphorylated in each preparation |
3012222 | Two-dimensional peptide mapping of [125I]EGF-R from young and senescent cells showed essentially the same pattern, indicating that EGF-R does not apparently undergo detectable changes in senescent human fibroblasts |
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