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phosphosite cbn pc11 biopax bel_lc signor biogrid tas lincs_drug hprd trrust | geneways tees isi trips rlimsp medscan sparser reach
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EGF increases the amount of EGFR. 7 / 106
2 | 88
reach
"Both EGF and linoleic acid strongly stimulated the expression of EGF receptor mRNA in C2BBe1 cells at 48 h compared with the control and combined groups."
reach
"Selective toxicity of TGF-alpha-PE40 to EGFR positive cell lines : selective protection of low EGFR expressing cell lines by EGF."
reach
"We also found that PTPRO suppression inhibits down-regulation of EGFR expression triggered by EGF stimulation."
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"EGFR mRNA level was enhanced fourfold by EGF while alpha-subunit mRNA was reduced by EGF."
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"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."
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"Combination of EGF and PGE2 promotes the transcription of nuclear EGFR target genes up to 8 hours."
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"To determine whether dynein also regulates the nuclear trafficking of EGFR, we treated cells with its inhibitors, vanadate and EHNA, and found that disruption of dynein ATPase activity decreased EGF induced nuclear localization of EGFR and protein level of EGFR in the nucleus (XREF_SUPPLEMENTARY)."
EGF increases the amount of EGFR bound to ERBB2. 6 / 6
3 3 |
bel
"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. "
bel
"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)."
bel
"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."
bel
"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)."
bel
"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."
bel
"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."
EGF increases the amount of EGFR bound to ERBB3. 2 / 2
1 1 |
bel
"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."
bel
"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."
EGF increases the amount of phosphorylated EGFR. 2 / 2
| 2
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"Although addition of EGF increased levels of phosphorylated EGFR (pEGFR), no obvious molecular weight upshift of EGFR was observed."
reach
"As shown in XREF_FIG, EGF increased the level of phosphorylated EGFR significantly in ESCC cells whether they had high or low EGFR expression."
EGF increases the amount of EGFR bound to EGFR. 2 / 2
2 |
bel
"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."
bel
"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)."
Transcriptionally active EGF increases the amount of EGFR. 2 / 2
2 |
biopax:ctd
No evidence text available
biopax:ctd
No evidence text available
EGF increases the amount of EGFR bound to TNK2. 2 / 2
2 |
bel
"Upon cell stimulation with EGF or PDGF, Ack is tyrosine-phosphorylated and recruited to activated EGF or PDGF receptors, respectively."
bel
"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. "
Catalytically active EGF increases the amount of EGFR bound to ERRFI1. 1 / 1
1 |
bel
"Upon EGF stimulation Mig-6 binds to the EGFR involving a highly acidic region between amino acids 985-995."
EGF increases the amount of EGFR bound to GAB1. 1 / 1
1 |
bel
"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."
Modified EGF increases the amount of EGFR. 1 / 1
| 1
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"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."
EGF increases the amount of modified EGFR. 1 / 1
| 1
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"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."
EGF increases the amount of EGFR bound to ERBB4. 1 / 1
1 |
bel
"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."
EGF increases the amount of EGFR bound to TNS3. 1 / 1
1 |
bel
"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."
EGF increases the amount of ubiquitinated EGFR. 1 / 1
| 1
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"In control fibroblasts, low levels of ubiquitinated EGFR were detected in the absence of ligand, whereas EGF treatment increased ubiquitinated EGFR levels (XREF_FIG)."
EGF increases the amount of EGFR bound to SHC1. 1 / 1
1 |
bel
"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."