The junction-associated protein AF-6 interacts and clusters with specific Eph receptor tyrosine kinases at specialized sites of cell-cell contact in the brain
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Regulation of c-Src by binding to the PDZ domain of AF-6Platelet-derived growth factor receptor association with Na(+)/H(+) exchanger regulatory factor potentiates receptor activityInteractions between Eph kinases and ephrins provide a mechanism to support platelet aggregation once cell-to-cell contact has occurred.Roles of Eph receptors and ephrins in segmental patterningThe Bcr kinase downregulates Ras signaling by phosphorylating AF-6 and binding to its PDZ domainEphBs: an integral link between synaptic function and synaptopathiesEphA receptor signaling--complexity and emerging themesMonomeric structure of the human EphB2 sterile alpha motif domainSolution structure and backbone dynamics of the AF-6 PDZ domain/Bcr peptide complexNectin-3, a new member of immunoglobulin-like cell adhesion molecules that shows homophilic and heterophilic cell-cell adhesion activitiesReplacing two conserved tyrosines of the EphB2 receptor with glutamic acid prevents binding of SH2 domains without abrogating kinase activity and biological responsesA PDZ domain protein interacts with the C-terminal tail of the insulin-like growth factor-1 receptor but not with the insulin receptorDistinct binding specificity of the multiple PDZ domains of INADL, a human protein with homology to INAD from Drosophila melanogasterRYK, a catalytically inactive receptor tyrosine kinase, associates with EphB2 and EphB3 but does not interact with AF-6Ephrin regulation of synapse formation, function and plasticityAstrocytic Ephrin-B1 Regulates Synapse Remodeling Following Traumatic Brain InjuryMultiple EphB receptor tyrosine kinases shape dendritic spines in the hippocampusTwo cell adhesion molecules, nectin and cadherin, interact through their cytoplasmic domain-associated proteinsExpression of Eph receptors and their ligands, ephrins, during lipopolysaccharide fever in ratsNectin: an adhesion molecule involved in formation of synapsesNectin4/PRR4, a new afadin-associated member of the nectin family that trans-interacts with nectin1/PRR1 through V domain interactionComplex formation of EphB1/Nck/Caskin1 leads to tyrosine phosphorylation and structural changes of the Caskin1 SH3 domainPDZ domain proteins: plug and play!Retrograde signaling at central synapsesSignaling between the actin cytoskeleton and the postsynaptic density of dendritic spines.Eph receptors and ephrin ligands: embryogenesis to tumorigenesis.Minding the gaps to promote thrombus growth and stabilityMolecular heterogeneity of central synapses: afferent and target regulation.AF6 negatively regulates Rap1-induced cell adhesion.The AF-6 homolog canoe acts as a Rap1 effector during dorsal closure of the Drosophila embryo.Diverse roles for the Eph family of receptor tyrosine kinases in carcinogenesis.Eph/ephrin signaling in epithelial development and homeostasisContact-dependent signaling during the late events of platelet activation.Genetic ablation of afadin causes mislocalization and deformation of Paneth cells in the mouse small intestinal epithelium.Cadherin-based transsynaptic networks in establishing and modifying neural connectivity.Afadin, a Ras/Rap effector that controls cadherin function, promotes spine and excitatory synapse density in the hippocampusEph receptor and ephrin signaling in developing and adult brain of the honeybee (Apis mellifera).Afadin: A key molecule essential for structural organization of cell-cell junctions of polarized epithelia during embryogenesis.Afadin is required for maintenance of dendritic structure and excitatory tone.Profiling Eph receptor expression in cells and tissues: a targeted mass spectrometry approach
P2860
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P2860
The junction-associated protein AF-6 interacts and clusters with specific Eph receptor tyrosine kinases at specialized sites of cell-cell contact in the brain
description
1999 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի հունվարին հրատարակված գիտական հոդված
@hy
artículu científicu espublizáu en 1999
@ast
im Januar 1999 veröffentlichter wissenschaftlicher Artikel
@de
scientific journal article
@en
vedecký článok (publikovaný 1999/01/25)
@sk
vědecký článek publikovaný v roce 1999
@cs
wetenschappelijk artikel (gepubliceerd op 1999/01/25)
@nl
наукова стаття, опублікована в січні 1999
@uk
مقالة علمية نشرت في 25-1-1999 حول موضوع: دماغ
@ar
name
The junction-associated protei ...... cell-cell contact in the brain
@ast
The junction-associated protei ...... cell-cell contact in the brain
@en
The junction-associated protei ...... cell-cell contact in the brain
@nl
type
label
The junction-associated protei ...... cell-cell contact in the brain
@ast
The junction-associated protei ...... cell-cell contact in the brain
@en
The junction-associated protei ...... cell-cell contact in the brain
@nl
prefLabel
The junction-associated protei ...... cell-cell contact in the brain
@ast
The junction-associated protei ...... cell-cell contact in the brain
@en
The junction-associated protei ...... cell-cell contact in the brain
@nl
P2093
P2860
P356
P1476
The junction-associated protei ...... cell-cell contact in the brain
@en
P2093
C. M. Hovens
E. Canaani
K. Moelling
M. Buchert
M. T. Adams
S. Schneider
V. Meskenaite
P2860
P304
P356
10.1083/JCB.144.2.361
P407
P577
1999-01-25T00:00:00Z