IndraLab

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TGFA binds EGF and EGFR. 71 / 71
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"Nimotuzumab is a recombinant humanized monoclonal IgG1 antibody against human EGFR and it can effectively block the binding of EGF and transforming growth factor-alpha to EGFR."

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"Korc, M.; Chandrasekar, B.; Yamanaka, Y.; Friess, H.; Btichler, M.; Beger, H. G. Overexpression of the epidermal growth factor receptor in human pancreatic cancer is associated with concomitant increa[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

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"Consistent with this, phosphorylated ERK levels were also unaffected by incubation of cells with an antibody that blocks binding of EGF and TGFα to wild-type EGF receptor (data not shown)."

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"For example, the concomitant presence in the cancer cells of EGFR and either EGF or TGF-α is associated with disease progression and decreased survival of PDAC patients [ xref ]."

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"The EGF and TGFα bind solely to erbB1 while HB-EGF and epiregulin bind to both erbB1 and erbB4 [8] ."

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"Epigen and epiregulin consequently promote the formation of weaker EGFR dimers than EGF and TGFα."

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"EGF and TGF-α interact with the target cell through binding to the EGFR [3, 12, 13] ."

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"In stratified squamous epithelial cells, these receptors include epidermal growth factor receptor (EGFR) that binds both EGF and transforming growth factor alpha (TGFalpha), and c-met whose ligand is hepatocyte growth factor/scatter factor (HGF/SF)."

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"T1E is a chimeric polypeptide that takes benefit from different ErbB ligand properties: epidermal growth factor (EGF) and TGF-α selectively bind to ErbB-1 with high affinity but weaker or no affinity for ErbB-2/ErbB-3 heterodimers, respectively."

sparser
"These findings prompted us to investigate two questions: 1) Is epidermal growth factor (EGF) or transforming growth factor alpha (TGFalpha), which binds to the EGF receptor, present in the GDR?"

sparser
"This monoclonal antibody blocks EGF and TGF-α binding to the extracellular domain of EGFR, which results in cell-growth inhibition, induction of apoptosis and decreased production of EGF [ xref ]."

sparser
"EGF and TGFα bind to the EGF receptor to stimulate an intact RAS/RAF/MAPK pathway, leading to the transcription of genes associated with cell proliferation, invasion and metastasis."

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"Although both epidermal growth factor (EGF) and TGF-α interact with EGFR to exert their cellular actions, TGF-α expression is more prevalent than EGF, indicating that the former is the predominant EGFR ligand in the CNS ( xref )."

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"In addition we have examined the genes and transcripts coding for the pre-pro forms of epidermal growth factor and transforming growth factor alpha, the two endogenous EGFR ligands."

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"ABX-EGF blocks binding of both epidermal growth factor and transforming growth factor alpha to the EGFR, inhibits tyrosine phosphorylation of the EGFR, and inhibits cellular proliferation."

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"To characterize the effects of ligand binding on the conformations of the EGFR dimers, we compared structures generated during simulation runs to previously solved x-ray structures of EGFR bound to TGF-α and EGF, and the recently solved structure of another ErbB4-ligand complex xref , xref , xref ."

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"EGF and TGF-α can interact with EGF-R via homodimerization or heterodimerization [ xref ]."

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"EGF and TGF-α bind directly only to EGFR, while neuregulins (also known as heregulins or neu differentiation factors) are specific to ErbB-3 and ErbB-4."

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"EGF and TGFα bind to EGFR to stimulate an intact RAS/RAF/MAPK pathway, leading to transcription of genes associated with cell proliferation, invasion and metastasis."

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"Surprisingly, p75+ supporting cells have high levels of transcripts for two ligands that preferentially bind EGFR, EGF and TGFα."

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"10 Lung cancer cells may produce EGFR ligands, such as epidermal growth factor (EGF) and transforming growth factor alpha, which then bind to the EGFR, leading to paracrine and[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

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"Binding of epidermal growth factor (EGF) or transforming growth factor alpha (TGF α ) to the extracellular domain of EGFR produces a number of downstream effects that affect phenotypic cell behavior including proliferation, invasion, metastasis, and inhibition of apoptosis [ xref ]."

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"The EGF-R binds two structurally related ligands, epidermal growth factor (EGF) and transforming growth factor-a (TGF-ct)."

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"Cetuximab, a chimerized antibody of the IgG1 subclass, was originally derived from a mouse myeloma cell line. xref Cetuximab blocks binding of EGF and TGFα to EGFR and inhibits ligand-induced activation of this tyrosine kinase receptor."

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"Our goal was also to determine whether HB-EGF alters growth or differentiation of human cytotrophoblasts and to compare its activity with that of EGF and TGF-α, which bind only to HER1."

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"The stoichiometry of binding of the EGFR extracellular domain to EGF and TGF-alpha was examined by band-shift analysis on non-denaturing PAGE and was estimated to be 1:1."

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"EGFR binds EGF and TGF-α with high affinity, and both ligands are overexpressed in pancreatic cancer [ xref ]."

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"Several approaches have been developed to achieve EGFR blockade as an anticancer treatment strategy, including the anti-EGFR monoclonal antibody IMC-C225, which competitively binds to the extracellular receptor site and prevents binding by the natural EGFR ligands EGF and transforming growth factor-alpha."

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"EGF and transforming growth factor-a (TGF-a) bound to the mutant EGFR with high affinity and enhanced the intrinsic mutant EGFR kinase activity."

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"By contrast, EGF and TGF-α were also found to be a potent chemotactic factors for these thyroid carcinoma cells like HB-EGF ( xref – xref ), but these growth factors are different from HB-EGF in that EGF or TGF-α binds to HER1 alone and that HB-EGF bears a heparin binding site, which binds to cell surface heparin sulfate proteoglycan, but not EGF or TGF-α."

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"The EGFr, which binds both EGF and TGF-α, is structurally related to the transforming protein encoded by the v-erbB oncogene of avian erythroblastosis virus."

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"EGF and TGF-α which both bind to the EGF receptor stimulate epithelial proliferation and differentiation and TGF-β1 inhibits epithelial proliferation."

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"Binding of ligand—either EGF or transforming growth factor-alpha (TGF-α)—to the extracellular domain of the EGF receptor results in activation of this intrinsic kinase activity and leads to autophosph[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

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"It blocked the binding of EGF and TGF-α to EGFR and subsequent phosphorylation of EGFR tyrosine kinase."

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"One precedent for differential traffic induced by ligand is TGFα and EGF binding to EGFR."

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"The N-terminus of EGF and TGFα bind to the L1 domain of the EGFR [18,19] ."

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"MAb ICR62 is a rat monoclonal antibody that blocks binding of EGF and TGFα to EGFR."

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"Agents that inhibit the EGFR have demonstrated clinical activity as single agents and in combination with chemotherapy and the most promising of these agents is cetuximab, which blocks the binding of EGF and transforming growth factor-alpha (TGF-alpha) to EGFR."

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"We also show that the binding of neuregulin-1beta to ErbB4 and ErbB3 and the binding of betacellulin to both ErbB4 and ErbB1 does not decrease at low pH, unlike the binding of epidermal growth factor and transforming growth factor-alpha to ErbB1."

sparser
"As a result, Cetuximab and Panitumumab, monoclonal antibody biological drugs, which block binding of EGF and transforming growth factor alpha (TGF-α) to EGFR have been frequently used in chemotherapy resistant CRC patients [ xref , xref ]."

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"EGFR binds to EGF and TGF-α with similar affinity, but generates different signals from these ligands."

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"159 8 Korc, M., Chandrasekar, B., Yamanaka, Y., Friess, H., Buchler, M. and Beger, H.G. (1992) Overexpression of the epidermal growth factor receptor in human pancreatic cancer is associate[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

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"Epidermal growth factor (EGF) and transforming growth factor alpha (TGF-alpha), both of which bind the EGF receptor (EGFR), are expressed in human and rodent developing prostate."

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"mAb 2F8 effectively blocked binding of EGF and TGF-alpha to the EGF-R. At saturating concentrations, 2F8 completely blocked EGF-R signaling and inhibited the in vitro proliferation of EGF-R-overexpressing A431 cells."

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"These findings point to dissimilar interactions of EGF and TGF-alpha with the EGF receptor in T3M4 cells, which may lead to differential activation of signal transduction pathways by these ligands."

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"We conclude that antibodies which block the binding of EGF and transforming growth factor alpha to the EGFR can inhibit the growth of EGFR-overexpressing tumors by directing terminal differentiation and that a further therapeutic benefit may be obtained via immunological mechanisms with rat IgG2b mAbs such as ICR62."

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"Binding of TGFα or EGF to EGFR promotes the activation of selected pathways: Ras/RAF/MAPK, PI3K/Akt-1, and signal transducer and transcription-activating (STAT) pathways [ xref , xref , xref , xref ]."

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"To address the mechanistic basis of this phenomenon, we have carried out cryo-EM analyses of human EGFR bound to EGF and TGF-α."

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"Panitumumab is a fully humanized IgG2 mAb that binds with high affinity to the ligand-binding domain of EGFR. xref Panitumumab, similarly to cetuximab, competitively blocks the binding of EGF and TGFα to EGFR, thus inhibiting autophosphorylation induced by EGFR ligands. xref Cetuximab and panitumumab were recently launched and marketed for colon, head and neck, and/or lung cancers, covering a limited range of solid tumors. xref , xref Necitumumab (IMC-11F8), designed to bind and block the ligand-binding site of EGFR, is another IgG1 antibody which is currently under investigation in clinical trials of patients with NSCLC. xref , xref "

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"The EGFR ligands, EGF and TGF-α bind to EGFR, resulting in the stimulation and activation of signaling complexes, leading to cell cycle progression, reduced apoptosis, angiogenesis, and metastatic potential xref ."

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"Therefore, the binding of EGFR with EGF or TGF-α in the airway mucosa could lead to different biological outcomes, as it has done it for HRV-14 replication bronchial epithelial cells."

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"EGF and TGFα both bind EGFR, but with different affinities."

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"For the second, even though EGF and TGFα bind to the same EGF receptor, their penetration of the BBB is quite different in that EGF has a rapid and saturable transport system whereas TGFα is trapped i[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

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"Neuregulin binding to these receptors is thought to promote an extension of the molecule (and exposure of the dimerization arm) similar to that seen when EGF or TGFα bind to EGFR, and this has been confirmed by X-ray scattering studies of the ErbB3 extracellular region in solution [ xref ]."

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"Binding of the EGF or transforming growth factor alpha ligand to EGFR triggers downstream signaling pathways that mediate a variety of cellular responses, including cellular proliferation, angiogenesis and apoptosis( xref )."

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"Zalutumumab is a fully human IgG1 mAb that targets EGFR domain III and inhibits binding of EGF and TGF-α to EGFR. xref Zalutumumab also prevents conformational changes in EGFR that are necessary for its activation. xref An open-label, randomized, Phase III trial investigated zalutumumab plus best supportive care (BSC) vs BSC alone in 286 patients with R/M HNSCC after failure of platinum-based chemotherapy. xref Zalutumumab prolonged median PFS compared with BSC alone (9.9 vs 8.4 weeks; P =0.0012)."

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"The natural ligands EGF and TGF-α bind to the extracellular domain of EGFR, and activate the receptor and its downstream signal proteins, ultimately causing activation or modulation of various cellular processes [ xref ]."

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"TGFα and EGF bind EGFR with comparable affinity at physiological pH, but TGFα binding is more sensitive to pH changes."

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"r to demonstrate autocrine stimulation of choriocarcinoma proliferation via a TGF-a-EGFR regulatory loop, we attempted to disrupt EGFR ligand- receptor interactions in JAr cells by culturing them in [MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

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"Both EGF and TGFα binding to the EGFR lead to endocytosis of EGFR, but receptor-EGF complexes are predominantly trafficked for degradation in lysosomes, while TGFα-bound receptor is predominantly recycled back to the cell surface. xref Thus, changes in ligand-dependent activation can radically impact growth factor receptor signaling."

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"EGFr binds the mitogenic polypeptide hormone epidermal growth factor (EGF) as well as EGF-related transforming growth factor-alpha (TGF-alpha)."

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"The extracellular domain of EGFR binds to either EGF or TGF-α, resulting in receptor dimerization."

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"Next, we wanted to examine, whether the same mechanism applies to other growth factors that are able to induce keratinocyte motility, namely EGF and TGF-α that bind to EGFR, as well as TGF-β1 and KGF [MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

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"During the binding of EGFR with TGF-α or EGF, EFGR can homodimerize or heterodimerize with other members belonging to the EGFR family [18] ."

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"It blocks the binding of EGF and transforming growth factor-alpha to EGFR and thus inhibits tumor cell growth, angiogenesis, and apoptosis. xref xref xref – xref In contrast to other approved anti-vascular endothelial growth factor agents including cetuximab and panitumumab, nimotuzumab needs bivalent binding for stable attachment to the cellular surface, leading to higher clinical efficiency and better safety. xref xref xref xref xref xref – xref Nimotuzumab has therefore been approved for the treatment of advanced head and neck cancer, nasopharyngeal cancer (NPC), glioma, and esophageal cancer in 30 countries. xref xref xref xref xref xref – xref In China, nimotuzumab was approved as a drug in combination with radiotherapy for the treatment of NPC in 2008 and was recommended by the Chinese edition of the National Comprehensive Cancer Network (NCCN) guidelines as a targeted therapy for NPC in 2009. xref "

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"Binding of EGF or transforming growth factor alpha ligands to the EGFR results in homodimerization of EGFR, and this change in conformation leads to autophosphorylation of the intracellular receptor d[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

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"One possible mechanism for the down regulation of EGFr content in prostate cancer may be competitive binding of EGFr by autocrine epidermal growth factor (EGF) or transforming growth factor alpha [MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

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"The three-dimensional structures of the EGF- and TGFα-bound EGFR ectodomain fragments show that EGF and TGFα bind to the EGFR in the same mode [18,19] ."

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"Specific ligands, such as epidermal growth factor (EGF) and transforming growth factor alpha (TGFα), bind and activate EGFR, triggering autophosphorylation of the intracytoplasmic EGFR tyrosine kinase domain xref , xref ."

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"Residues S418 and G471, while not predicted to affect the interaction of EGFR with endogenous ligands EGF and TGF-α, may be important for interaction with one or more of the remaining five endogenous ligands such that mutation at these residues reduces clonal fitness and persistence."

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"These data suggest that direct interaction of EGF or TGF-α with the EGFR ligand-binding domain modulates HCV entry."