Journal ArticleDOI
Epidermal growth factor receptors: critical mediators of multiple receptor pathways.
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TLDR
The receptor for epidermal growth factor was identified as a downstream element in different signaling pathways, expanding its classical function as a receptor for EGF-like ligands to a role as mediator of diverse signaling systems and as a switch point of a cellular communication network.About:
This article is published in Current Opinion in Cell Biology.The article was published on 1999-04-01. It has received 618 citations till now. The article focuses on the topics: Growth factor receptor & Growth factor receptor inhibitor.read more
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Journal ArticleDOI
Cell signaling by receptor-tyrosine kinases
TL;DR: Understanding of the complex signaling networks downstream from RTKs and how alterations in these networks are translated into cellular responses provides an important context for therapeutically countering the effects of pathogenic RTK mutations in cancer and other diseases.
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The ErbB signaling network: receptor heterodimerization in development and cancer
TL;DR: The role of ErbB receptors as normal signal transducers and their contribution to the process of malignant transformation during tumor development are concentrated on.
PatentDOI
EGF receptor transactivation by G-protein-coupled receptors requires metalloproteinase cleavage of proHB-EGF
TL;DR: In this article, agents and methods for growth factor receptor activation by modulating the G-protein mediated signal transduction pathway were described, and a method to activate the growth factor receptors was proposed.
Journal ArticleDOI
Epidermal growth factor receptor: mechanisms of activation and signalling.
Robert N. Jorissen,Francesca Walker,Francesca Walker,Normand Pouliot,Thomas P. J. Garrett,Thomas P. J. Garrett,Colin W. Ward,Colin W. Ward,Antony W. Burgess,Antony W. Burgess +9 more
TL;DR: The structure and function of the EGFR is reviewed, from ligand binding to the initiation of intracellular signalling pathways that lead to changes in the biochemical state of the cell.
Journal ArticleDOI
The protein tyrosine kinase family of the human genome.
TL;DR: The completion of the human tyrosine kinase family tree provides a framework for further advances in biomedical science and identifies several novel genes and enabled the creation of a nonredundant catalog of tyrosines kinase genes.
References
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STATs and Gene Regulation
TL;DR: The discovery of a STAT in Drosophila, and most recently in Dictyostelium discoideum, implies an ancient evolutionary origin for this dual-function set of proteins.
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Requirement for Generation of H2O2 for Platelet-Derived Growth Factor Signal Transduction
TL;DR: The results suggest that H2O2 may act as a signal-transducing molecule, and they suggest a potential mechanism for the cardioprotective effects of antioxidants.
Journal ArticleDOI
Activation of the Estrogen Receptor Through Phosphorylation by Mitogen-Activated Protein Kinase
Shigeaki Kato,Hideki Endoh,Yoshikazu Masuhiro,Takuya Kitamoto,Shimami Uchiyama,Haruna Sasaki,Shoichi Masushige,Yukiko Gotoh,Eisuke Nishida,Hiroyuki Kawashima,Daniel Metzger,Pierre Chambon +11 more
TL;DR: The phosphorylation of the human estrogen receptor (ER) serine residue at position 118 is required for full activity of the ER activation function 1 (AF-1), which is modulated by the phosphorylated Ser118 through the Ras-MAPK cascade of the growth factor signaling pathways.
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ErbB‐2, the preferred heterodimerization partner of all ErbB receptors, is a mediator of lateral signaling
TL;DR: Analysis of ErbB receptor interplay induced by the epidermal growth factor (EGF)‐related peptides provides the first biochemical evidence that a given Erb B receptor has distinct signaling properties depending on its dimerization.
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Role of transactivation of the EGF receptor in signalling by G-protein-coupled receptors
TL;DR: It is reported here that the epidermal growth factor receptor (EGFR) and the neu oncoprotein become rapidly tyrosine-phosphorylated upon stimulation of Rat-1 cells with the GPCR agonists endothelin-1, lysophosphatic acid and thrombin, suggesting that there is an intracellular mechanism for transactivation.