IndraLab

"EGF induced proliferation was observed in all EGFR expressing PC cells except PC3, indicating that EGFR expression does not unequivocally trigger proliferation following EGF stimulation."

"EGF stimulation increased the expression of EGFR, iNOS, EP1, EP2, and EP4 in astrocytes."

"Combination of EGF and PGE2 promotes the transcription of nuclear EGFR target genes up to 8 hours."

"Repetitive injections of exogenous epidermal growth factor during the interval of rapid growth in rats increased the lung volume, weight and epidermal growth factor receptor expression as compared with untreated animals [XREF_BIBR]."

"In conclusion, in ovo application of EGF increased EGFR expression but had no effect on posthatch growth performance, DM retention, and intestinal development."

"This led to a delay in EGF-induced EGFR degradation in Huh7.5 cells and could, at least partly, restore the declined EGFR levels observed in GABARAP SKO cells in response to EGF stimulation shown in Figure 2A, as the total EGFR levels were only significantly reduced after 60 min."

"In addition, the physical interaction between MUC15 and EGFR effectively prevented the EGF induced dimerization of EGFR and the cell surface expression of EGFR and enhanced the EGF induced endocytosis[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

"[XREF_BIBR] Here, we demonstrated that the amount of EGFR expression in response to EGF was reduced in the absence of Le y modification."

"In parental and EGFR -/- A549 cells bearing EGFR WT plasmid, EGF promoted the expression of nuclear EGFR target genes with a peak at 2 h and declined to baseline at 4-8 h, whereas PGE 2 mimicked the EGF effect on target genes with a peak at 4 h and declined toward the baseline at 8-12 h."

"Importantly, ephrinA1 seemed to reduce EGF induced cell viability in U373 cells expressing low EGFR levels."

"Although the growth factors epidermal growth factor (EGF) and neuregulin (NRG) 1 similarly stimulated Erk1/2 in MDA-MB-361 cells, EGF acting through an EGF receptor/ErbB2 heterodimer preferentially stimulated protein kinase C, and NRG1beta acting through an ErbB2/ErbB3 heterodimer preferentially stimulated Akt. "

"Table 2: Classification of ligands according to their relative affinities toward ErbB-IgGs. I only too the High affinity (1-100 nM) and Very high affinity (<1 nM)."

"Table 2: Classification of ligands according to their relative affinities toward ErbB-IgGs. I only too the High affinity (1-100 nM) and Very high affinity (<1 nM)."

"Figure 1 | ERBB receptors, ligands, dimers and downstream signalling pathways. a | Members of the epidermal growth factor (EGF) family of growth factors are ligands for the ERBB receptors. Ligand binding to ERBB receptors induces the formation of receptor homo- and heterodimers and the activation of the intrinsic kinase domain, resulting in phosphorylation on specific tyrosine residues within the cytoplasmic tail. These phosphorylated residues serve as docking sites for a range of proteins, the recruitment of which leads to the activation of intracellular signalling pathways. None of the ligands bind ERBB2, but ERBB2 is the preferred dimerization partner for all the other ERBB receptors. ERBB3 has impaired kinase activity and only acquires signalling potential when it is dimerized with another ERBB receptor, such as ERBB2. Overexpression of ERBB2 in tumours leads to constitutive activation of ERBB2, presumably because of increased receptor concentrations at the plasma membrane. Many of these tumours contain phosphorylated ERBB3, which couples ERBB2 to the phosphatidylinositol 3-kinase (PI3K)?AKT pathway128."

"Although the growth factors epidermal growth factor (EGF) and neuregulin (NRG) 1 similarly stimulated Erk1/2 in MDA-MB-361 cells, EGF acting through an EGF receptor/ErbB2 heterodimer preferentially stimulated protein kinase C, and NRG1beta acting through an ErbB2/ErbB3 heterodimer preferentially stimulated Akt."

"Figure 1 | ERBB receptors, ligands, dimers and downstream signalling pathways. a | Members of the epidermal growth factor (EGF) family of growth factors are ligands for the ERBB receptors. Ligand binding to ERBB receptors induces the formation of receptor homo- and heterodimers and the activation of the intrinsic kinase domain, resulting in phosphorylation on specific tyrosine residues within the cytoplasmic tail. These phosphorylated residues serve as docking sites for a range of proteins, the recruitment of which leads to the activation of intracellular signalling pathways. None of the ligands bind ERBB2, but ERBB2 is the preferred dimerization partner for all the other ERBB receptors. ERBB3 has impaired kinase activity and only acquires signalling potential when it is dimerized with another ERBB receptor, such as ERBB2. Overexpression of ERBB2 in tumours leads to constitutive activation of ERBB2, presumably because of increased receptor concentrations at the plasma membrane. Many of these tumours contain phosphorylated ERBB3, which couples ERBB2 to the phosphatidylinositol 3-kinase (PI3K)?AKT pathway128."

"Here we report that ACK1 interacted with epidermal growth factor receptor (EGFR) upon EGF stimulation via a region at carboxy terminus that is highly homologous to Gene-33/Mig-6/RALT. "

"Upon cell stimulation with EGF or PDGF, Ack is tyrosine-phosphorylated and recruited to activated EGF or PDGF receptors, respectively."

"Figure 1 | ERBB receptors, ligands, dimers and downstream signalling pathways. a | Members of the epidermal growth factor (EGF) family of growth factors are ligands for the ERBB receptors. Ligand binding to ERBB receptors induces the formation of receptor homo- and heterodimers and the activation of the intrinsic kinase domain, resulting in phosphorylation on specific tyrosine residues within the cytoplasmic tail. These phosphorylated residues serve as docking sites for a range of proteins, the recruitment of which leads to the activation of intracellular signalling pathways. None of the ligands bind ERBB2, but ERBB2 is the preferred dimerization partner for all the other ERBB receptors. ERBB3 has impaired kinase activity and only acquires signalling potential when it is dimerized with another ERBB receptor, such as ERBB2. Overexpression of ERBB2 in tumours leads to constitutive activation of ERBB2, presumably because of increased receptor concentrations at the plasma membrane. Many of these tumours contain phosphorylated ERBB3, which couples ERBB2 to the phosphatidylinositol 3-kinase (PI3K)?AKT pathway128."

"Table 2: Classification of ligands according to their relative affinities toward ErbB-IgGs. I only too the High affinity (1-100 nM) and Very high affinity (<1 nM)."

"In this paper, we present a comprehensive pathway map of EGFR signaling and other related pathways. The map reveals that the overall architecture of the pathway is a bow-tie (or hourglass) structure with several feedback loops. See figure 2: The bow-tie architecture of the EGFR signaling pathway."

"In this paper, we present a comprehensive pathway map of EGFR signaling and other related pathways. The map reveals that the overall architecture of the pathway is a bow-tie (or hourglass) structure with several feedback loops. See figure 2: The bow-tie architecture of the EGFR signaling pathway."

"Although addition of EGF increased levels of phosphorylated EGFR (pEGFR), no obvious molecular weight upshift of EGFR was observed."

"As shown in XREF_FIG, EGF increased the level of phosphorylated EGFR significantly in ESCC cells whether they had high or low EGFR expression."

"we demonstrate that EGF (i) increased the binding affinity of EGFR to Gab1 Tyr-627 and Shc Tyr-317 sites in purified GST fusion proteins approximately 4-6-fold, and (ii) EGF significantly enhanced the phosphorylation of these sites, relative to EGFR autophosphorylation, in cell lysates containing the full-length Gab1 and Shc proteins."

"Upon EGF stimulation Mig-6 binds to the EGFR involving a highly acidic region between amino acids 985-995."

"we demonstrate that EGF (i) increased the binding affinity of EGFR to Gab1 Tyr-627 and Shc Tyr-317 sites in purified GST fusion proteins approximately 4-6-fold, and (ii) EGF significantly enhanced the phosphorylation of these sites, relative to EGFR autophosphorylation, in cell lysates containing the full-length Gab1 and Shc proteins."

"When GH3 cells were stably transfected with an expression vector containing a constitutively active form of ErbB2cDNA (HER2CA) which express tenfold higher HER2 protein, higher levels of phosphorylated EGFR, higher EGF induced levels of EGFR and MAPK, and higher HRG induced phosphorylated ErbB3 and AKT levels were observed."

"It is therefore very feasible that the EGFR expressed on the membrane of these neoplastic cells can be directly activated by EGF in SP to induce IL-1alpha expression."

"In this paper, we present a comprehensive pathway map of EGFR signaling and other related pathways. The map reveals that the overall architecture of the pathway is a bow-tie (or hourglass) structure with several feedback loops. See figure 2: The bow-tie architecture of the EGFR signaling pathway."

"Addition of EGF to the cells induces dephosphorylation of these two molecules, leads to disassociation of the tensin3-focal adhesion kinase-p130Cas complex, and enhances the interaction between tensin3 and EGF receptor."

"In control fibroblasts, low levels of ubiquitinated EGFR were detected in the absence of ligand, whereas EGF treatment increased ubiquitinated EGFR levels (XREF_FIG)."