Extracellular domains drive homo- but not hetero-dimerization of erbB receptors - Test2 - elhamkhani - TriplyDB

Extracellular domains drive homo- but not hetero-dimerization of erbB receptors

Extracellular domains drive homo- but not hetero-dimerization of erbB receptors

http://www.wikidata.org/entity/Q34488149

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Identification of a region within the ErbB2/HER2 intracellular domain that is necessary for ligand-independent association Mechanism of activation and inhibition of the HER4/ErbB4 kinase Epidermal growth factor receptor dimerization and activation require ligand-induced conformational changes in the dimer interface The extracellular region of ErbB4 adopts a tethered conformation in the absence of ligand.Matuzumab Binding to EGFR Prevents the Conformational Rearrangement Required for Dimerization ErbB2 resembles an autoinhibited invertebrate epidermal growth factor receptor Structural Evaluation of EGFR Inhibition Mechanisms for Nanobodies/VHH Domains RYK, a catalytically inactive receptor tyrosine kinase, associates with EphB2 and EphB3 but does not interact with AF-6 Argos inhibits epidermal growth factor receptor signalling by ligand sequestration Dynamically varying interactions between heregulin and ErbB proteins detected by single-molecule analysis in living cells Selective formation of ErbB-2/ErbB-3 heterodimers depends on the ErbB-3 affinity of epidermal growth factor-like ligands.GxxxG motifs within the amyloid precursor protein transmembrane sequence are critical for the etiology of Abeta42.Populations of radial glial cells respond differently to reelin and neuregulin1 in a ferret model of cortical dysplasia.Survey of the year 2000 commercial optical biosensor literature.A system for quantifying dynamic protein interactions defines a role for Herceptin in modulating ErbB2 interactions.Complex relationship between ligand binding and dimerization in the epidermal growth factor receptor.Carboxyl-group footprinting maps the dimerization interface and phosphorylation-induced conformational changes of a membrane-associated tyrosine kinase.Role of extracellular subdomains of p185c-neu and the epidermal growth factor receptor in ligand-independent association and transactivation Effect of sialylation on EGFR phosphorylation and resistance to tyrosine kinase inhibition Ligand regulation of a constitutively dimeric EGF receptor.The role of distinct p185neu extracellular subdomains for dimerization with the epidermal growth factor (EGF) receptor and EGF-mediated signaling.N-cadherin enhances APP dimerization at the extracellular domain and modulates Aβ production.The epidermal growth factor receptor gene family as a target for therapeutic intervention in numerous cancers: what's genetics got to do with it?Design and development of masked therapeutic antibodies to limit off-target effects: application to anti-EGFR antibodies.Targeting HER2/neu with a fully human IgE to harness the allergic reaction against cancer cells.Ligand-induced ErbB receptor dimerization.Structure-based view of epidermal growth factor receptor regulation.Dynamic transition states of ErbB1 phosphorylation predicted by spatial stochastic modeling Interaction of antibodies with ErbB receptor extracellular regions.erbB3 is an active tyrosine kinase capable of homo- and heterointeractions.Molecular determinants of KA1 domain-mediated autoinhibition and phospholipid activation of MARK1 kinase.Transmembrane helix-helix interactions involved in ErbB receptor signaling.Links between Schwann cells and melanocytes in development and disease.The EGFR family: not so prototypical receptor tyrosine kinases.Platelet endothelial aggregation receptor 1 (PEAR1), a novel epidermal growth factor repeat-containing transmembrane receptor, participates in platelet contact-induced activation.Two motifs within a transmembrane domain, one for homodimerization and the other for heterodimerization.Blockade of a key region in the extracellular domain inhibits HER2 dimerization and signaling.Extracellular region of epidermal growth factor receptor: a potential target for anti-EGFR drug discovery.Suppression of heregulin β signaling by the single N-glycan deletion mutant of soluble ErbB3 protein.Piecing it together: Unraveling the elusive structure-function relationship in single-pass membrane receptors.

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Extracellular domains drive homo- but not hetero-dimerization of erbB receptors

http://www.wikidata.org/entity/Q34488149

description

2000 nî lūn-bûn

@nan

2000 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած

@hyw

2000 թվականի սեպտեմբերին հրատարակված գիտական հոդված

@hy

2000年の論文

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2000年論文

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2000年論文

@zh-hant

2000年論文

@zh-hk

2000年論文

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2000年論文

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2000年论文

@wuu

name

Extracellular domains drive homo- but not hetero-dimerization of erbB receptors

@ast

Extracellular domains drive homo- but not hetero-dimerization of erbB receptors

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Extracellular domains drive homo- but not hetero-dimerization of erbB receptors

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type

label

Extracellular domains drive homo- but not hetero-dimerization of erbB receptors

@ast

Extracellular domains drive homo- but not hetero-dimerization of erbB receptors

@en

Extracellular domains drive homo- but not hetero-dimerization of erbB receptors

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prefLabel

Extracellular domains drive homo- but not hetero-dimerization of erbB receptors

@ast

Extracellular domains drive homo- but not hetero-dimerization of erbB receptors

@en

Extracellular domains drive homo- but not hetero-dimerization of erbB receptors

@nl

P1433

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The EMBO Journal

P1476

Extracellular domains drive homo- but not hetero-dimerization of erbB receptors

@en

P2093

K M Ferguson

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

M J Mohan

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

P J Darling

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

T L Macatee

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

P2860

Neuregulin-4: a novel growth factor that acts through the ErbB-4 receptor tyrosine kinase

Coexpression of erbB2 and erbB3 proteins reconstitutes a high affinity receptor for heregulin

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

HER4-mediated biological and biochemical properties in NIH 3T3 cells. Evidence for HER1-HER4 heterodimers

Identification of heregulin, a specific activator of p185erbB2

SH2 domains recognize specific phosphopeptide sequences

Transformation of NIH 3T3 cells by HER3 or HER4 receptors requires the presence of HER1 or HER2

The epidermal growth factor receptor couples transforming growth factor-alpha, heparin-binding epidermal growth factor-like factor, and amphiregulin to Neu, ErbB-3, and ErbB-4

ErbB4 signaling in the mammary gland is required for lobuloalveolar development and Stat5 activation during lactation

The cellular response to neuregulins is governed by complex interactions of the erbB receptor family

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4632-4643

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scholarly article

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10.1093/EMBOJ/19.17.4632

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17

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19

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2000-09-01T00:00:00Z

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12350966

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10970856

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302059

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