Kit receptor dimerization is driven by bivalent binding of stem cell factor
about
Structural basis of semaphorin-plexin recognition and viral mimicry from Sema7A and A39R complexes with PlexinC1Structure of macrophage colony stimulating factor bound to FMS: diverse signaling assemblies of class III receptor tyrosine kinasesStructural and functional properties of platelet-derived growth factor and stem cell factor receptorsFunctional deregulation of KIT: link to mast cell proliferative diseases and other neoplasmsStructure of the active core of human stem cell factor and analysis of binding to its receptor KitCrystal structure of human stem cell factor: implication for stem cell factor receptor dimerization and activationStructural basis for stem cell factor–KIT signaling and activation of class III receptor tyrosine kinasesStructural basis for KIT receptor tyrosine kinase inhibition by antibodies targeting the D4 membrane-proximal regionAllosteric competitive inactivation of hematopoietic CSF-1 signaling by the viral decoy receptor BARF1Mode of receptor binding and activation by plasminogen-related growth factors.Human Trop-2 is a tumor-associated calcium signal transducerStructure-function analysis of FLT3 ligand-FLT3 receptor interactions using a rapid functional screenStructure of Full-Length Human PDGFRβ Bound to Its Activating Ligand PDGF-B as Determined by Negative-Stain Electron Microscopy.Gene Duplication of the zebrafish kit ligand and partitioning of melanocyte development functions to kit ligand a.Recent advances in the understanding of mastocytosis: the role of KIT mutations.Extracellular complexes of the hematopoietic human and mouse CSF-1 receptor are driven by common assembly principles.Therapeutic targeting of receptor tyrosine kinases in lung cancer.Kit ligand and c-Kit have diverse roles during mammalian oogenesis and folliculogenesis.Role of dimerization of the membrane-associated growth factor kit ligand in juxtacrine signaling: the Sl17H mutation affects dimerization and stability-phenotypes in hematopoiesis.Contacts between membrane proximal regions of the PDGF receptor ectodomain are required for receptor activation but not for receptor dimerization.C-kit and its ligand stem cell factor: potential contribution to prostate cancer bone metastasisAdvanced systemic mastocytosis: the impact of KIT mutations in diagnosis, treatment, and progressionStructure, domain organization, and different conformational states of stem cell factor-induced intact KIT dimers.The SCF/c-KIT system in the male: Survival strategies in fertility and cancer.Identification of the residues in the extracellular region of KDR important for interaction with vascular endothelial growth factor and neutralizing anti-KDR antibodies.c-kit(+) cells: the tell-tale heart of cardiac regeneration?The strength and cooperativity of KIT ectodomain contacts determine normal ligand-dependent stimulation or oncogenic activation in cancer.The stem cell factor (SCF)/c-KIT signalling in testis and prostate cancer.Multiple novel alterations in Kit tyrosine kinase in patients with gastrointestinally pronounced systemic mast cell activation disorder.Surface binding inhibitors of the SCF-KIT protein-protein interaction.A novel recombinant dual human SCF expressed in and purified from silkworm, Bombyx mori, possesses higher bioactivity than recombinant monomeric human SCF.Identification of a novel nonsense mutation on the Pax3 gene in ENU-derived white belly spotting mice and its genetic interaction with c-Kit.Requirements for binding and signaling of the kinase domain receptor for vascular endothelial growth factor.Interaction of KIT and sSCFDimerization of KIT upon SCF binding
P2860
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P2860
Kit receptor dimerization is driven by bivalent binding of stem cell factor
description
1997 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
1997 թվականի մարտին հրատարակված գիտական հոդված
@hy
article publié dans la revue scientifique Journal of Biological Chemistry
@fr
artículu científicu espublizáu en 1997
@ast
im März 1997 veröffentlichter wissenschaftlicher Artikel
@de
scientific journal article
@en
vedecký článok (publikovaný 1997/03/07)
@sk
vědecký článek publikovaný v roce 1997
@cs
wetenschappelijk artikel (gepubliceerd op 1997/03/07)
@nl
наукова стаття, опублікована в березні 1997
@uk
name
Kit receptor dimerization is driven by bivalent binding of stem cell factor
@ast
Kit receptor dimerization is driven by bivalent binding of stem cell factor
@en
Kit receptor dimerization is driven by bivalent binding of stem cell factor
@nl
type
label
Kit receptor dimerization is driven by bivalent binding of stem cell factor
@ast
Kit receptor dimerization is driven by bivalent binding of stem cell factor
@en
Kit receptor dimerization is driven by bivalent binding of stem cell factor
@nl
prefLabel
Kit receptor dimerization is driven by bivalent binding of stem cell factor
@ast
Kit receptor dimerization is driven by bivalent binding of stem cell factor
@en
Kit receptor dimerization is driven by bivalent binding of stem cell factor
@nl
P2093
P2860
P356
P1476
Kit receptor dimerization is driven by bivalent binding of stem cell factor
@en
P2093
P2860
P304
P356
10.1074/JBC.272.10.6311
P407
P577
1997-03-01T00:00:00Z