Direct contacts between extracellular membrane-proximal domains are required for VEGF receptor activation and cell signaling
about
Targeted disruption of heparan sulfate interaction with hepatocyte and vascular endothelial growth factors blocks normal and oncogenic signalingEndorepellin, the angiostatic module of perlecan, interacts with both the α2β1 integrin and vascular endothelial growth factor receptor 2 (VEGFR2): a dual receptor antagonismStructures of a platelet-derived growth factor/propeptide complex and a platelet-derived growth factor/receptor complexTargeting extracellular domains D4 and D7 of vascular endothelial growth factor receptor 2 reveals allosteric receptor regulatory sitesVascular endothelial growth factor-B in physiology and diseaseStructural Basis for Ligand Recognition and Activation of RAGEStructural Basis for Selective Vascular Endothelial Growth Factor-A (VEGF-A) Binding to Neuropilin-1Structural and mechanistic insights into VEGF receptor 3 ligand binding and activationStructural basis for KIT receptor tyrosine kinase inhibition by antibodies targeting the D4 membrane-proximal regionStructural basis of Tie2 activation and Tie2/Tie1 heterodimerization.New inhibitors of VEGFR-2 targeting the extracellular domain dimerization process.β-hairpin peptide that targets vascular endothelial growth factor (VEGF) receptors: design, NMR characterization, and biological activitySoluble VEGFR-2: an antilymphangiogenic variant of VEGF receptors.Extracellular complexes of the hematopoietic human and mouse CSF-1 receptor are driven by common assembly principles.VEGFR-2 conformational switch in response to ligand binding.VEGFR and type-V RTK activation and signalingDistinct cellular properties of oncogenic KIT receptor tyrosine kinase mutants enable alternative courses of cancer cell inhibitionStructure, domain organization, and different conformational states of stem cell factor-induced intact KIT dimers.Physical-chemical principles underlying RTK activation, and their implications for human disease.The lymphatic vasculature in disease.Function of members of the neuropilin family as essential pleiotropic cell surface receptors.Platelet-derived growth factors and their receptors: structural and functional perspectives.Fully quantified spectral imaging reveals in vivo membrane protein interactions.The strength and cooperativity of KIT ectodomain contacts determine normal ligand-dependent stimulation or oncogenic activation in cancer.Site-Specific N-Glycosylation of Endothelial Cell Receptor Tyrosine Kinase VEGFR-2.The basis for the distinct biological activities of vascular endothelial growth factor receptor-1 ligands.Characterization of the interaction between endostatin short peptide and VEGF receptor 3.Real-time analysis of the binding of fluorescent VEGF165a to VEGFR2 in living cells: Effect of receptor tyrosine kinase inhibitors and fate of internalized agonist-receptor complexesNovel antagonists of heparin binding growth factors.Cooperative interactions between VEGFR2 extracellular Ig-like subdomains ensure VEGFR2 dimerization.Structure and function of vascular endothelial growth factor and its receptor system.Positive and Negative Regulation of Angiogenesis by Soluble Vascular Endothelial Growth Factor Receptor-1.Immunoglobulin-like domain 4-mediated ligand-independent dimerization triggers VEGFR-2 activation in HUVECs and VEGFR2-positive breast cancer cells.Molecular Pharmacology of VEGF-A Isoforms: Binding and Signalling at VEGFR2.ScFvs as Allosteric Inhibitors of VEGFR-2: Novel Tools to Harness VEGF Signaling.Allosteric targeting of receptor tyrosine kinases.
P2860
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P2860
Direct contacts between extracellular membrane-proximal domains are required for VEGF receptor activation and cell signaling
description
2010 nî lūn-bûn
@nan
2010 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
name
Direct contacts between extrac ...... activation and cell signaling
@ast
Direct contacts between extrac ...... activation and cell signaling
@en
Direct contacts between extrac ...... activation and cell signaling
@nl
type
label
Direct contacts between extrac ...... activation and cell signaling
@ast
Direct contacts between extrac ...... activation and cell signaling
@en
Direct contacts between extrac ...... activation and cell signaling
@nl
prefLabel
Direct contacts between extrac ...... activation and cell signaling
@ast
Direct contacts between extrac ...... activation and cell signaling
@en
Direct contacts between extrac ...... activation and cell signaling
@nl
P2093
P2860
P3181
P356
P1476
Direct contacts between extrac ...... activation and cell signaling
@en
P2093
Yarden Opatowsky
P2860
P304
P3181
P356
10.1073/PNAS.0914052107
P407
P577
2010-02-02T00:00:00Z