Activation egfr review




















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J Cell Sci 24 : — Cite Icon Cite. View large Download slide. Enzymatic reduction of disulfide bonds in lysosomes: characterization of a gamma-interferon-inducible lysosomal thiol reductase GILT. Azimzadeh Irani. On the tertiary structure of the extracellular domains of the epidermal growth factor and insulin receptors.

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Regulation of postendocytic traficking of the epidermal growth factor receptor through endosomal retention. Evidence that autophosphorylation of solubilized receptors for epidermal growth factor is mediated by intramolecular cross-phosphorylation. Tyrosine phosphorylation of the beta2 subunit of clathrin adaptor complex AP-2 reveals the role of a di-leucine motif in the epidermal growth factor receptor trafficking. Differential regulation of EGF receptor internalization and degradation by multiubiquitination within the kinase domain.

PTP1b-dependent regulation of receptor tyrosine kinase signaling by the actin-binding protein Mena. Single particle tracking reveals that EGFR signaling activity is amplified in clathrin-coated pits. Grb2 regulates internalization of EGF receptors through clathrin-coated pits.

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Email alerts Article activity alert. Accepted manuscripts alert. Table of contents alert. Latest published articles alert. View Metrics. Cited by Web of Science The application deadline is 31 January Kovacs E. A structural perspective on the regulation of the epidermal growth factor receptor. Cold Spring Harb. Roskoski R. Bessman N. Putting together structures of epidermal growth factor receptors.

Bae J. Asymmetric tyrosine kinase arrangements in activation or autophosphorylation of receptor tyrosine kinases. Yarden Y. Epidermal growth factor induces rapid, reversible aggregation of the purified epidermal growth factor receptor.

Boni-Schnetzler M. Mechanism of epidermal growth factor receptor autophosphorylation and high-affinity binding. Cochet C. Demonstration of epidermal growth factor-induced receptor dimerization in living cells using a chemical covalent cross-linking agent. Schlessinger J. Weiss F. Novel mechanisms of RTK signal generation. Signal transduction by receptors with tyrosine kinase activity.

Activation of transmembrane cell-surface receptors via a common mechanism? Moriki T. Activation of preformed EGF receptor dimers by ligand-induced rotation of the transmembrane domain. Liu P. Investigation of the dimerization of proteins from the epidermal growth factor receptor family by single wavelength fluorescence cross-correlation spectroscopy. Clayton A. Ligand-induced dimer-tetramer transition during the activation of the cell surface epidermal growth factor receptor-A multidimensional microscopy analysis.

Martin-Fernandez M. Preformed oligomeric epidermal growth factor receptors undergo an ectodomain structure change during signaling. Saffarian S. Oligomerization of the EGF receptor investigated by live cell fluorescence intensity distribution analysis.

Yavas S. The epidermal growth factor receptor forms location-dependent complexes in resting cells. Elite Ed. Hofman E. Ligand-induced EGF receptor oligomerization is kinase-dependent and enhances internalization.

Bader A. Homo-FRET imaging enables quantification of protein cluster sizes with subcellular resolution. Teramura Y. Single-molecule analysis of epidermal growth factor binding on the surface of living cells. Tao R. Cell Sci. Yang K. Luciferase fragment complementation imaging of conformational changes in the epidermal growth factor receptor.

Macdonald-Obermann J. Dynamic analysis of the epidermal growth factor EGF receptor-ErbB2-ErbB3 protein network by luciferase fragment complementation imaging. Knebel A. Dephosphorylation of receptor tyrosine kinases as target of regulation by radiation, oxidants or alkylating agents. Yamashita H. Valley C. Enhanced dimerization drives ligand-independent activity of mutant epidermal growth factor receptor in lung cancer.

Chung I. Spatial control of EGF receptor activation by reversible dimerization on living cells. Huang Y. Molecular basis for multimerization in the activation of the epidermal growth factor receptor. Needham S. EGFR oligomerization organizes kinase-active dimers into competent signalling platforms.

Ferguson K. EGF activates its receptor by removing interactions that autoinhibit ectodomain dimerization. Structure-based view of epidermal growth factor receptor regulation.

Cho H. Structure of the extracellular region of HER3 reveals an interdomain tether. Bouyain S. The extracellular region of ErbB4 adopts a tethered conformation in the absence of ligand. Berezov A. Disabling receptor ensembles with rationally designed interface peptidomimetics. Jura N. Mechanism for activation of the EGF receptor catalytic domain by the juxtamembrane segment. Zhang X. An allosteric mechanism for activation of the kinase domain of epidermal growth factor receptor.

Sorkin A. Epidermal growth factor receptor interaction with clathrin adaptors is mediated by the Tyrcontaining internalization motif. Red Brewer M. The juxtamembrane region of the EGF receptor functions as an activation domain. Huse M. The conformational plasticity of protein kinases. Ligand-induced, receptor-mediated dimerization and activation of EGF receptor. Allosteric regulation of the epidermal growth factor receptor kinase. Macdonald J.

Heterogeneity in EGF-binding affinities arises from negative cooperativity in an aggregating system. The intracellular juxtamembrane domain of the epidermal growth factor EGF receptor is responsible for the allosteric regulation of EGF binding. Wofsy C. Implications of epidermal growth factor EGF induced egf receptor aggregation.

De Meyts P. Insulin interactions with its receptors: Experimental evidence for negative cooperativity. Alvarado D. Structural basis for negative cooperativity in growth factor binding to an EGF receptor. A single ligand is sufficient to activate EGFR dimers. Adak S. The tethering arm of the EGF receptor is required for negative cooperativity and signal transduction. The membrane-proximal intracellular domain of the epidermal growth factor receptor underlies negative cooperativity in ligand binding.

Shoyab M. Biologically active phorbol esters specifically alter affinity of epidermal growth factor membrane receptors. Magun B. Epidermal growth factor. Ability of tumor promoter to alter its degradation, receptor affinity and receptor number.

Hunter T. Protein kinase C phosphorylation of the EGF receptor at a threonine residue close to the cytoplasmic face of the plasma membrane.

Downward J. Autophosphorylation and protein kinase C phosphorylation of the epidermal growth factor receptor. Effect on tyrosine kinase activity and ligand binding affinity. Thiel K. Epidermal growth factor receptor juxtamembrane region regulates allosteric tyrosine kinase activation. Chen L. Energetics of ErbB1 transmembrane domain dimerization in lipid bilayers. Bocharov E. Helix-helix interactions in membrane domains of bitopic proteins: Specificity and role of lipid environment.

Conformational transitions and interactions underlying the function of membrane embedded receptor protein kinases. Receptor Guanylyl Cyclases in Sensory Processing. Alternative packing of EGFR transmembrane domain suggests that protein-lipid interactions underlie signal conduction across membrane.

Predominance of activated EGFR higher-order oligomers on the cell surface. Growth Factors. Kozer N. Curran T. Saito T. Differential activation of epidermal growth factor EGF receptor downstream signaling pathways by betacellulin and EGF. Different epidermal growth factor EGF receptor ligands show distinct kinetics and biased or partial agonism for homodimer and heterodimer formation.

Roepstorff K. Differential effects of EGFR ligands on endocytic sorting of the receptor. Prenzel N. The epidermal growth factor receptor family as a central element for cellular signal transduction and diversification. Zandi R. Mechanisms for oncogenic activation of the epidermal growth factor receptor. Cell Signal. Pedersen M. Expression of a naturally occurring constitutively active variant of the epidermal growth factor receptor in mouse fibroblasts increases motility.

Analysis of the epidermal growth factor receptor specific transcriptome: Effect of receptor expression level and an activating mutation. Nicholson R. EGFR and cancer prognosis. Bhargava R. Suzuki S. Protein overexpression and gene amplification of epidermal growth factor receptor in nonsmall cell lung carcinomas.

An immunohistochemical and fluorescence in situ hybridization study. Wong A. Increased expression of the epidermal growth factor receptor gene in malignant gliomas is invariably associated with gene amplification. Furgason J. Whole genome sequencing of glioblastoma multiforme identifies multiple structural variations involved in EGFR activation. Sheikh M. Identification of an additional presponsive site in the human epidermal growth factor receptor gene promotor.

Ludes-Meyers J. Transcriptional activation of the human epidermal growth factor receptor promoter by human p McInerney J. Chrysogelos S. Chromatin structure of the EGFR gene suggests a role for intron 1 sequences in its regulation in breast cancer cells. Nucleic Acids Res. Gebhardt F. Modulation of epidermal growth factor receptor gene transcription by a polymorphic dinucleotide repeat in intron 1.

Buerger H. Allelic length of a CA dinucleotide repeat in the egfr gene correlates with the frequency of amplifications of this sequence—First results of an inter-ethnic breast cancer study. Amador M. An epidermal growth factor receptor intron 1 polymorphism mediates response to epidermal growth factor receptor inhibitors. Cancer Res. Johnston D. Elevation of the epidermal growth factor receptor and dependent signaling in human papillomavirus-infected laryngeal papillomas. Structural alterations of the epidermal growth factor receptor gene in human gliomas.



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