A structure-based model for ligand binding and dimerization of EGF receptors.
about
Computational modeling reveals molecular details of epidermal growth factor bindingReversibly bound chloride in the atrial natriuretic peptide receptor hormone-binding domain: Possible allosteric regulation and a conserved structural motif for the chloride-binding siteStructural Basis for Negative Cooperativity in Growth Factor Binding to an EGF ReceptorHigh- and low-affinity epidermal growth factor receptor-ligand interactions activate distinct signaling pathwaysSingle-molecule analysis of epidermal growth factor binding on the surface of living cells.Single-molecule imaging and fluorescence lifetime imaging microscopy show different structures for high- and low-affinity epidermal growth factor receptors in A431 cells.Dimerization of VEGF receptors and implications for signal transduction: a computational study.Dynamically varying interactions between heregulin and ErbB proteins detected by single-molecule analysis in living cellsNative structure-based modeling and simulation of biomolecular systems per mouse click.Critical appraisal of the role of gefitinib in the management of locally advanced or metastatic non-small cell lung cancerMechanisms of activation of receptor tyrosine kinases: monomers or dimers.Impaired degradation followed by enhanced recycling of epidermal growth factor receptor caused by hypo-phosphorylation of tyrosine 1045 in RBE cells.On the nature of low- and high-affinity EGF receptors on living cells.Fluorescent affibody peptide penetration in glioma margin is superior to full antibodyRegulation of the catalytic activity of the EGF receptor.The tethered configuration of the EGF receptor extracellular domain exerts only a limited control of receptor function.Sulfiredoxin Promotes Colorectal Cancer Cell Invasion and Metastasis through a Novel Mechanism of Enhancing EGFR SignalingHeterogeneity in EGF-binding affinities arises from negative cooperativity in an aggregating system.Understanding cytokine and growth factor receptor activation mechanisms.The kinetics of the hydrogen/deuterium exchange of epidermal growth factor receptor ligands.Contacts between membrane proximal regions of the PDGF receptor ectodomain are required for receptor activation but not for receptor dimerization.Quantum dots implementation as a label for analysis of early stages of EGF receptor endocytosis: a comparative study on cultured cellsNegative co-operativity in the EGF receptor.The ERBB3 receptor in cancer and cancer gene therapyLigand-induced ErbB receptor dimerization.Structure-based view of epidermal growth factor receptor regulation.Interaction of antibodies with ErbB receptor extracellular regions.Metabolism, cell surface organization, and disease.Computational modelling of the BRI1 receptor system.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.The strength and cooperativity of KIT ectodomain contacts determine normal ligand-dependent stimulation or oncogenic activation in cancer.Rinsing paired-agent model (RPAM) to quantify cell-surface receptor concentrations in topical staining applications of thick tissues.EGFR-activated Src family kinases maintain GAB1-SHP2 complexes distal from EGFR.Piecing it together: Unraveling the elusive structure-function relationship in single-pass membrane receptors.Ligand binding induces a conformational change in epidermal growth factor receptor dimers.Identification of disulfide-linked dimers of the receptor tyrosine kinase DDR1.Heterogeneities in EGF receptor density at the cell surface can lead to concave up scatchard plot of EGF binding.Oligomers of ERBB3 have two distinct interfaces that differ in their sensitivity to disruption by heregulin.Intracoronary administration of FGF-2: a computational model of myocardial deposition and retention.
P2860
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P2860
A structure-based model for ligand binding and dimerization of EGF receptors.
description
2004 nî lūn-bûn
@nan
2004年の論文
@ja
2004年論文
@yue
2004年論文
@zh-hant
2004年論文
@zh-hk
2004年論文
@zh-mo
2004年論文
@zh-tw
2004年论文
@wuu
2004年论文
@zh
2004年论文
@zh-cn
name
A structure-based model for ligand binding and dimerization of EGF receptors.
@ast
A structure-based model for ligand binding and dimerization of EGF receptors.
@en
type
label
A structure-based model for ligand binding and dimerization of EGF receptors.
@ast
A structure-based model for ligand binding and dimerization of EGF receptors.
@en
prefLabel
A structure-based model for ligand binding and dimerization of EGF receptors.
@ast
A structure-based model for ligand binding and dimerization of EGF receptors.
@en
P2860
P356
P1476
A structure-based model for ligand binding and dimerization of EGF receptors.
@en
P2093
Dawn Mattoon
Peter Klein
P2860
P304
P356
10.1073/PNAS.0307285101
P407
P577
2004-01-19T00:00:00Z