Cell binding function of E-cadherin is regulated by the cytoplasmic domain - Wikidata - thesis-toulmin - TriplyDB

Cell binding function of E-cadherin is regulated by the cytoplasmic domain

Cell binding function of E-cadherin is regulated by the cytoplasmic domain

http://www.wikidata.org/entity/Q24564118

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Identification of a novel intracellular interaction domain essential for Bves function Genomic structure and alternative splicing of murine R2B receptor protein tyrosine phosphatases (PTPkappa, mu, rho and PCP-2)The catenin p120(ctn) interacts with Kaiso, a novel BTB/POZ domain zinc finger transcription factor Plakoglobin, or an 83-kD homologue distinct from beta-catenin, interacts with E-cadherin and N-cadherin Protocadherins: a large family of cadherin-related molecules in central nervous system Epithelial cell adhesion molecule (Ep-CAM) modulates cell-cell interactions mediated by classic cadherins Dynamic interaction of PTPmu with multiple cadherins in vivo The 220-kD protein colocalizing with cadherins in non-epithelial cells is identical to ZO-1, a tight junction-associated protein in epithelial cells: cDNA cloning and immunoelectron microscopy E-cadherin and APC compete for the interaction with beta-catenin and the cytoskeleton Diversity of the cadherin family: evidence for eight new cadherins in nervous tissue Molecular cloning of a human Ca2+-dependent cell-cell adhesion molecule homologous to mouse placental cadherin: its low expression in human placental tissues Cytoplasmic tail regulates the intercellular adhesion function of the epithelial cell adhesion molecule Molecular cloning and characterization of PTP pi, a novel receptor-like protein-tyrosine phosphatase Identification of amino acid sequence motifs in desmocollin, a desmosomal glycoprotein, that are required for plakoglobin binding and plaque formation The cytoplasmic domain of the cell adhesion molecule uvomorulin associates with three independent proteins structurally related in different species Vezatin, a novel transmembrane protein, bridges myosin VIIA to the cadherin-catenins complex Alpha-catenin is a molecular switch that binds E-cadherin-beta-catenin and regulates actin-filament assembly.Re-solving the cadherin-catenin-actin conundrum Receptor tyrosine phosphatase R-PTP-kappa mediates homophilic binding Structure of the axonal surface recognition molecule neurofascin and its relationship to a neural subgroup of the immunoglobulin superfamily Regulation of connexin 43-mediated gap junctional intercellular communication by Ca2+ in mouse epidermal cells is controlled by E-cadherin Receptor protein tyrosine phosphatase PTPmu associates with cadherins and catenins in vivo Dynamics of cadherin/catenin complex formation: novel protein interactions and pathways of complex assembly beta-Catenin associates with the actin-bundling protein fascin in a noncadherin complex Interaction of alpha-actinin with the cadherin/catenin cell-cell adhesion complex via alpha-catenin Association of p120, a tyrosine kinase substrate, with E-cadherin/catenin complexes Involvement of ZO-1 in cadherin-based cell adhesion through its direct binding to alpha catenin and actin filaments Direct Ca2+-dependent heterophilic interaction between desmosomal cadherins, desmoglein and desmocollin, contributes to cell-cell adhesion Quantitative analysis of cadherin-catenin-actin reorganization during development of cell-cell adhesion delta-catenin, an adhesive junction-associated protein which promotes cell scattering The nonreceptor protein tyrosine phosphatase PTP1B binds to the cytoplasmic domain of N-cadherin and regulates the cadherin-actin linkage The juxtamembrane region of the cadherin cytoplasmic tail supports lateral clustering, adhesive strengthening, and interaction with p120ctn Selective uncoupling of p120(ctn) from E-cadherin disrupts strong adhesion Differential localization of VE- and N-cadherins in human endothelial cells: VE-cadherin competes with N-cadherin for junctional localization E-cadherin's dark side: possible role in tumor progression The role of Eph receptors in lens function and disease Synapse adhesion: a dynamic equilibrium conferring stability and flexibility Synaptopodin couples epithelial contractility to α-actinin-4-dependent junction maturation Crystal structure of the M-fragment of alpha-catenin: implications for modulation of cell adhesion E-cadherin roles in animal biology: A perspective on thyroid hormone-influence

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Cell binding function of E-cadherin is regulated by the cytoplasmic domain

http://www.wikidata.org/entity/Q24564118

description

1988 nî lūn-bûn

@nan

1988 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած

@hyw

1988 թվականի դեկտեմբերին հրատարակված գիտական հոդված

@hy

1988年の論文

@ja

1988年学术文章

@wuu

1988年学术文章

@zh-cn

1988年学术文章

@zh-hans

1988年学术文章

@zh-my

1988年学术文章

@zh-sg

1988年學術文章

@yue

name

Cell binding function of E-cadherin is regulated by the cytoplasmic domain

@ast

Cell binding function of E-cadherin is regulated by the cytoplasmic domain

@en

Cell binding function of E-cadherin is regulated by the cytoplasmic domain

@nl

type

label

Cell binding function of E-cadherin is regulated by the cytoplasmic domain

@ast

Cell binding function of E-cadherin is regulated by the cytoplasmic domain

@en

Cell binding function of E-cadherin is regulated by the cytoplasmic domain

@nl

prefLabel

Cell binding function of E-cadherin is regulated by the cytoplasmic domain

@ast

Cell binding function of E-cadherin is regulated by the cytoplasmic domain

@en

Cell binding function of E-cadherin is regulated by the cytoplasmic domain

@nl

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The EMBO Journal

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Cell binding function of E-cadherin is regulated by the cytoplasmic domain

@en

P2093

A Nagafuchi

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

M Takeichi

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

P2860

The nucleotide sequence and transcript map of the herpes simplex virus thymidine kinase gene

Cadherin cell adhesion molecules with distinct binding specificities share a common structure.

The structure of cell adhesion molecule uvomorulin. Insights into the molecular mechanism of Ca2+-dependent cell adhesion.

Isolation of placental cadherin cDNA: identification of a novel gene family of cell-cell adhesion molecules

Sequence analysis of a cDNA clone encoding the liver cell adhesion molecule, L-CAM.

A-CAM: a 135-kD receptor of intercellular adherens junctions. I. Immunoelectron microscopic localization and biochemical studies.

A-CAM: a 135-kD receptor of intercellular adherens junctions. II. Antibody-mediated modulation of junction formation

The cadherins: cell-cell adhesion molecules controlling animal morphogenesis.

Functional correlation between cell adhesive properties and some cell surface proteins.

Cloning and expression of cDNA encoding a neural calcium-dependent cell adhesion molecule: its identity in the cadherin gene family.

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3679-84

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scholarly article

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2669132

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12

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7

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1988-12-01T00:00:00Z

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3061804

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454940

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