The Juxtamembrane Region of the EGF Receptor Functions as an Activation Domain - Test2 - elhamkhani - TriplyDB

The Juxtamembrane Region of the EGF Receptor Functions as an Activation Domain

The Juxtamembrane Region of the EGF Receptor Functions as an Activation Domain

http://www.wikidata.org/entity/Q27646344

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Conformational coupling across the plasma membrane in activation of the EGF receptor Cell signaling by receptor tyrosine kinases ErbB3/HER3 intracellular domain is competent to bind ATP and catalyze autophosphorylation Adaptive resistance to targeted therapies in cancer Structure-function relationships of ErbB RTKs in the plasma membrane of living cells Design principles underpinning the regulatory diversity of protein kinases Enhanced dimerization drives ligand-independent activity of mutant epidermal growth factor receptor in lung cancer Inhibition of Receptor Dimerization as a Novel Negative Feedback Mechanism of EGFR Signaling Coarse-grained molecular simulation of epidermal growth factor receptor protein tyrosine kinase multi-site self-phosphorylation Single Particle Tracking Reveals that EGFR Signaling Activity Is Amplified in Clathrin-Coated Pits Structural analysis of the catalytically inactive kinase domain of the human EGF receptor 3 Structural Basis for Negative Cooperativity in Growth Factor Binding to an EGF Receptor ErbB polymorphisms: insights and implications for response to targeted cancer therapeutics Crucial roles of RSK in cell motility by catalysing serine phosphorylation of EphA2 Overexpression of CARMA3 in non-small-cell lung cancer is linked for tumor progression A potential peptide therapeutic derived from the juxtamembrane domain of the epidermal growth factor receptor Mitogen-Inducible Gene-6 Mediates Feedback Inhibition from Mutated BRAF towards the Epidermal Growth Factor Receptor and Thereby Limits Malignant Transformation Characterization of membrane protein interactions in plasma membrane derived vesicles with quantitative imaging Förster resonance energy transfer Structure-based network analysis of activation mechanisms in the ErbB family of receptor tyrosine kinases: the regulatory spine residues are global mediators of structural stability and allosteric interactions.Computational modeling of allosteric communication reveals organizing principles of mutation-induced signaling in ABL and EGFR kinases.The energy landscape analysis of cancer mutations in protein kinases Lineage-specific co-evolution of the Egf receptor/ligand signaling system.A highly efficient peptide substrate for EGFR activates the kinase by inducing aggregation Her4 and Her2/neu tyrosine kinase domains dimerize and activate in a reconstituted in vitro system Conformational changes in receptor tyrosine kinase signaling: an ErbB garden of delights Synthesis and biochemical characterization of EGF receptor in a water-soluble membrane model system Co-conserved features associated with cis regulation of ErbB tyrosine kinases.Structural and mechanistic underpinnings of the differential drug sensitivity of EGFR mutations in non-small cell lung cancer.Mechanisms of activation of receptor tyrosine kinases: monomers or dimers.Phosphorylation-dependent differential regulation of plant growth, cell death, and innate immunity by the regulatory receptor-like kinase BAK1.Simultaneous visualization of the extracellular and cytoplasmic domains of the epidermal growth factor receptor.EGF receptor exposed to oxidative stress acquires abnormal phosphorylation and aberrant activated conformation that impairs canonical dimerization Asp-960/Glu-961 controls the movement of the C-terminal tail of the epidermal growth factor receptor to regulate asymmetric dimer formation.Human epidermal growth factor receptor (HER1) aligned on the plasma membrane adopts key features of Drosophila EGFR asymmetry.Investigating extracellular in situ EGFR structure and conformational changes using FRET microscopy.Convergence between Wnt-β-catenin and EGFR signaling in cancer.Trafficking of epidermal growth factor receptor ligands in polarized epithelial cells.Plakophilin-2 promotes activation of epidermal growth factor receptor.Kinase-mediated quasi-dimers of EGFR Allosteric communication across the native and mutated KIT receptor tyrosine kinase.

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The Juxtamembrane Region of the EGF Receptor Functions as an Activation Domain

http://www.wikidata.org/entity/Q27646344

description

2009 nî lūn-bûn

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2009 թուականի Յունիսին հրատարակուած գիտական յօդուած

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2009 թվականի հունիսին հրատարակված գիտական հոդված

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2009年の論文

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2009年論文

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2009年論文

@zh-hant

2009年論文

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2009年論文

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2009年論文

@zh-tw

2009年论文

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name

The Juxtamembrane Region of the EGF Receptor Functions as an Activation Domain

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The Juxtamembrane Region of the EGF Receptor Functions as an Activation Domain

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The Juxtamembrane Region of the EGF Receptor Functions as an Activation Domain

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label

The Juxtamembrane Region of the EGF Receptor Functions as an Activation Domain

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The Juxtamembrane Region of the EGF Receptor Functions as an Activation Domain

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The Juxtamembrane Region of the EGF Receptor Functions as an Activation Domain

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prefLabel

The Juxtamembrane Region of the EGF Receptor Functions as an Activation Domain

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The Juxtamembrane Region of the EGF Receptor Functions as an Activation Domain

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The Juxtamembrane Region of the EGF Receptor Functions as an Activation Domain

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J.MOLCEL.2009.04.034

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The Juxtamembrane Region of the EGF Receptor Functions as an Activation Domain

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Ambra Pozzi

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Diego Alvarado

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Graham Carpenter

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Katarina Moravcevic

http://www.w3.org/2001/XMLSchema#string

Monica Red Brewer

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Sung Hee Choi

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P2860

An allosteric mechanism for activation of the kinase domain of epidermal growth factor receptor

Mechanism of activation and inhibition of the HER4/ErbB4 kinase

Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination

Structural basis for autoinhibition of the Ephb2 receptor tyrosine kinase by the unphosphorylated juxtamembrane region

Structure of the epidermal growth factor receptor kinase domain alone and in complex with a 4-anilinoquinazoline inhibitor

Structure of a c-kit product complex reveals the basis for kinase transactivation

The structural basis for autoinhibition of FLT3 by the juxtamembrane domain

Structures of Lung Cancer-Derived EGFR Mutants and Inhibitor Complexes: Mechanism of Activation and Insights into Differential Inhibitor Sensitivity

6-Ethynylthieno[3,2-d]- and 6-ethynylthieno[2,3-d]pyrimidin-4-anilines as tunable covalent modifiers of ErbB kinases

Cell signaling by receptor tyrosine kinases

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641-51

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scholarly article

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2122414

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10.1016/J.MOLCEL.2009.04.034

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6

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34

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2009-06-26T00:00:00Z

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26324569

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19560417

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