Two EGF molecules contribute additively to stabilization of the EGFR dimer - Wikidata - wikimedia - TriplyDB

Two EGF molecules contribute additively to stabilization of the EGFR dimer

Two EGF molecules contribute additively to stabilization of the EGFR dimer

http://www.wikidata.org/entity/Q33885990

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Epidermal growth factor receptor dimerization and activation require ligand-induced conformational changes in the dimer interface Clathrin-dependent endocytosis Reaching out for signals: filopodia sense EGF and respond by directed retrograde transport of activated receptors Computational modeling reveals molecular details of epidermal growth factor binding Identifying activating mutations in the EGFR gene: prognostic and therapeutic implications in non-small cell lung cancer Structure-function relationships of ErbB RTKs in the plasma membrane of living cells Crystal structure of human epidermal growth factor and its dimerization Matuzumab Binding to EGFR Prevents the Conformational Rearrangement Required for Dimerization Structural Basis for Negative Cooperativity in Growth Factor Binding to an EGF Receptor Glycosylation-induced conformational modification positively regulates receptor-receptor association: a study with an aberrant epidermal growth factor receptor (EGFRvIII/DeltaEGFR) expressed in cancer cells.Kinetic analysis of the interleukin-13 receptor complex Decorin binds to a narrow region of the epidermal growth factor (EGF) receptor, partially overlapping but distinct from the EGF-binding epitope Identification of a heregulin binding site in HER3 extracellular domain Binding interaction of the heregulinbeta egf domain with ErbB3 and ErbB4 receptors assessed by alanine scanning mutagenesis Modified epidermal growth factor receptor (EGFR)-bearing liposomes (MRBLs) are sensitive to EGF in solution Activation of ErbB4 by the bifunctional epidermal growth factor family hormone epiregulin is regulated by ErbB2 Kit receptor dimerization is driven by bivalent binding of stem cell factor Seeing the light: preassembly and ligand-induced changes of the interferon gamma receptor complex in cells Characterization of membrane protein interactions in plasma membrane derived vesicles with quantitative imaging Förster resonance energy transfer The ErbB signaling network: receptor heterodimerization in development and cancer A new approach for determining the stability of recombinant human epidermal growth factor by thermal Fourier transform infrared (FTIR) microspectroscopy.Single-molecule imaging and fluorescence lifetime imaging microscopy show different structures for high- and low-affinity epidermal growth factor receptors in A431 cells.Direct selection of EGF mutants displayed on filamentous phage using cells overexpressing EGF receptor.Study of calcium signaling in non-excitable cells.Selective formation of ErbB-2/ErbB-3 heterodimers depends on the ErbB-3 affinity of epidermal growth factor-like ligands.Y-box-binding protein 1 confers EGF independence to human mammary epithelial cells.Selection of heregulin variants having higher affinity for the ErbB3 receptor by monovalent phage display.Disulfide bond structure of human epidermal growth factor receptor.Exact model reduction of combinatorial reaction networks.Activation of Neu (ErbB-2) mediated by disulfide bond-induced dimerization reveals a receptor tyrosine kinase dimer interface.Complexity of signal transduction mediated by ErbB2: clues to the potential of receptor-targeted cancer therapy.Epidermal growth factor receptor mutation in combination with expression of MIG6 alters gefitinib sensitivity.Role of receptor tyrosine kinases and their ligands in glioblastoma.Mechanisms of activation of receptor tyrosine kinases: monomers or dimers.Bivalence of EGF-like ligands drives the ErbB signaling network Rhomboid and Star facilitate presentation and processing of the Drosophila TGF-alpha homolog Spitz Single-molecule imaging of EGFR signalling on the surface of living cells.Heterogeneity of epidermal growth factor binding kinetics on individual cells.Potato carboxypeptidase inhibitor, a T-knot protein, is an epidermal growth factor antagonist that inhibits tumor cell growth.Expression of herstatin, an autoinhibitor of HER-2/neu, inhibits transactivation of HER-3 by HER-2 and blocks EGF activation of the EGF receptor.

P2860

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P2860

Two EGF molecules contribute additively to stabilization of the EGFR dimer

http://www.wikidata.org/entity/Q33885990

description

1997 nî lūn-bûn

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1997 թուականի Յունուարին հրատարակուած գիտական յօդուած

@hyw

1997 թվականի հունվարին հրատարակված գիտական հոդված

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1997年の論文

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1997年論文

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1997年論文

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1997年論文

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1997年論文

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1997年論文

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1997年论文

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name

Two EGF molecules contribute additively to stabilization of the EGFR dimer

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Two EGF molecules contribute additively to stabilization of the EGFR dimer

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type

label

Two EGF molecules contribute additively to stabilization of the EGFR dimer

@ast

Two EGF molecules contribute additively to stabilization of the EGFR dimer

@en

prefLabel

Two EGF molecules contribute additively to stabilization of the EGFR dimer

@ast

Two EGF molecules contribute additively to stabilization of the EGFR dimer

@en

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The EMBO Journal

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Two EGF molecules contribute additively to stabilization of the EGFR dimer

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D M Engelman

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D Pinchasi

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I Lax

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J Schlessinger

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M Zhou

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Z Bu

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P2860

Human growth hormone and extracellular domain of its receptor: crystal structure of the complex

Binding of Neu differentiation factor with the extracellular domain of Her2 and Her3

A heparin-binding growth factor secreted by macrophage-like cells that is related to EGF

Mechanism of platelet-derived growth factor (PDGF) AA, AB, and BB binding to alpha and beta PDGF receptor

The amphiregulin gene encodes a novel epidermal growth factor-related protein with tumor-inhibitory activity

Crystal structure of the tyrosine kinase domain of the human insulin receptor

A recombinant ectodomain of the receptor for the stem cell factor (SCF) retains ligand-induced receptor dimerization and antagonizes SCF-stimulated cellular responses

Cytokine signal transduction

Dimerization of the extracellular domain of granuloycte-colony stimulating factor receptor by ligand binding: a monovalent ligand induces 2:2 complexes

Crystal structure of a complex between interferon-gamma and its soluble high-affinity receptor

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281-294

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10.1093/EMBOJ/16.2.281

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2

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16

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John E. Ladbury

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1997-01-01T00:00:00Z

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14181142

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9029149

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1169635

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