About: The cadherin cytoplasmic domain is unstructured in the absence of beta-catenin. A possible mechanism for regulating cadherin turnover

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About: The cadherin cytoplasmic domain is unstructured in the absence of beta-catenin. A possible mechanism for regulating cadherin turnover Goto Sponge NotDistinct Permalink

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Attributes	Values
rdf:type	Item
description	artículu científicu espublizáu en 2001 (ast) наукова стаття, опублікована у квітні 2001 (uk) 2001 թուականի Ապրիլին հրատարակուած գիտական յօդուած (hyw) 2001 թվականի ապրիլին հրատարակված գիտական հոդված (hy) wetenschappelijk artikel (gepubliceerd op 2001/04/13) (nl) مقالة علمية (نشرت في 13-4-2001) (ar) im April 2001 veröffentlichter wissenschaftlicher Artikel (de) article publié dans la revue scientifique Journal of Biological Chemistry (fr) scientific journal article (en)
publication date	wds:Q28910197-349D22AB-9FEA-40F9-B45E-6BEA7233BF99
publication date	2001-04-13 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q28910197-DD13FF18-39DC-49D9-83EA-F0D2AD35D825
language of work or name	English
author name string	wds:Q28910197-000BF87D-3E0E-4D9D-9779-655870D863E4 wds:Q28910197-58AB343D-ACAE-430B-8DCC-02AE49F93C62 wds:Q28910197-96042543-28AE-4DDD-A272-85CCC61997C5 wds:Q28910197-CD17A5D2-6384-491B-9A24-0D91E9875738 wds:Q28910197-EB6A7280-AE35-47A4-9850-6C21C043A716
OpenCitations bibliographic resource ID	wds:Q28910197-881EDA11-F72A-48F7-807B-E5542E8F8560
OpenCitations bibliographic resource ID	https://w3id.org/oc/corpus/br/2669096
author name string	W. J. Nelson A. H. Huber W. I. Weis D. V. Laurents D. B. Stewart
OpenCitations bibliographic resource ID	2669096
rdfs:label	The cadherin cytoplasmic domain is unstructured in the absence of beta-catenin. A possible mechanism for regulating cadherin turnover (en) The cadherin cytoplasmic domain is unstructured in the absence of beta-catenin. A possible mechanism for regulating cadherin turnover (ast)
skos:prefLabel	The cadherin cytoplasmic domain is unstructured in the absence of beta-catenin. A possible mechanism for regulating cadherin turnover (en) The cadherin cytoplasmic domain is unstructured in the absence of beta-catenin. A possible mechanism for regulating cadherin turnover (ast)
name	The cadherin cytoplasmic domain is unstructured in the absence of beta-catenin. A possible mechanism for regulating cadherin turnover (en) The cadherin cytoplasmic domain is unstructured in the absence of beta-catenin. A possible mechanism for regulating cadherin turnover (ast)
title	wds:Q28910197-D43EBE20-51DF-4365-9EB1-6CA1C9629939
title	The cadherin cytoplasmic domain is unstructured in the absence of beta-catenin. A possible mechanism for regulating cadherin turnover (en)
page(s)	wds:Q28910197-B78AD62E-275D-4E7F-96CD-3E1408E38F1A
page(s)	12301–12309
instance of	wds:Q28910197-A3711B10-5D31-476B-9239-6ED086E93386
instance of	scholarly article
main subject	wds:Q28910197-24FD9057-A798-4FC3-8BC2-3A144832A23F wds:Q28910197-33F5839C-6E41-4CF7-AE0B-7EAC988096FE wds:Q28910197-62AF7BA0-6C34-472C-800A-3D4386E8B749
main subject	wd:Q14902827 wd:Q21497145 Shotgun Dmel_CG3722
PubMed ID	wds:Q28910197-62373437-4806-4245-9D89-618FC255BAF3
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/11121423
PubMed ID	11121423
published in	wds:Q28910197-8D30653F-3142-4248-8754-0424B2AED5DD
published in	Journal of Biological Chemistry
issue	wds:Q28910197-84C7DC1C-6B94-43A2-AFDB-B6BE7033A4F9
volume	wds:Q28910197-8C790241-45A1-4C02-8B1F-679C6F14B328
issue	15
volume	276
DOI	wds:Q28910197-A16B77EC-BD03-4CB7-AC41-5F44A074873E
DOI	http://dx.doi.org/10.1074/JBC.M010377200
DOI	10.1074/JBC.M010377200
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q28910197
is cites work of	Alpha-catenin is a molecular switch that binds E-cadherin-beta-catenin and regulates actin-filament assembly. beta-Catenin is a Nek2 substrate involved in centrosome separation Novel membrane protein shrew-1 targets to cadherin-mediated junctions in polarized epithelial cells ICAT inhibits beta-catenin binding to Tcf/Lef-family transcription factors and the general coactivator p300 using independent structural modules Thermodynamics of beta-catenin-ligand interactions: the roles of the N- and C-terminal tails in modulating binding affinity Mechanism of phosphorylation-dependent binding of APC to beta-catenin and its role in beta-catenin degradation Wingless signalling alters the levels, subcellular distribution and dynamics of Armadillo and E-cadherin in third instar larval wing imaginal discs FoxM1 regulates re-annealing of endothelial adherens junctions through transcriptional control of beta-catenin expression Biochemical and structural analysis of alpha-catenin in cell-cell contacts Compromised E-cadherin adhesion and epithelial barrier function with activation of G protein-coupled receptors is rescued by Y-to-F mutations in beta-catenin Ankyrin-G is a molecular partner of E-cadherin in epithelial cells and early embryos Coupling of folding and binding for unstructured proteins Role for ICAT in β-catenin-dependent nuclear signaling and cadherin functions Cell adhesion. The minimal cadherin-catenin complex binds to actin filaments under force Molecular characterization of Rab11 interactions with members of the family of Rab11-interacting proteins Regulation of proto-Dbl by intracellular membrane targeting and protein stability Origin of metazoan cadherin diversity and the antiquity of the classical cadherin/β-catenin complex Pre-metazoan origins and evolution of the cadherin adhesome The cytoplasmic face of cell contact sites Molecular mechanisms of beta-catenin recognition by adenomatous polyposis coli revealed by the structure of an APC-beta-catenin complex A novel role for p120 catenin in E-cadherin function Intrinsically unstructured proteins and their functions The structure of the beta-catenin/E-cadherin complex and the molecular basis of diverse ligand recognition by beta-catenin Intercellular adhesion in morphogenesis: molecular and biophysical considerations Linking beta-catenin to androgen-signaling pathway Looking beyond the Wnt pathway for the deep nature of β-catenin. Cadherin-mediated cell sorting not determined by binding or adhesion specificity VE-cadherin: adhesion at arm's length Role of beta-catenin in the developing cortical and hippocampal neuroepithelium. Phospho-regulation of Beta-catenin adhesion and signaling functions. Distinct molecular forms of beta-catenin are targeted to adhesive or transcriptional complexes Systematic peptide array-based delineation of the differential beta-catenin interaction with Tcf4, E-cadherin, and adenomatous polyposis coli. Wnt-5a-CKI{alpha} signaling promotes {beta}-catenin/E-cadherin complex formation and intercellular adhesion in human breast epithelial cells A dileucine motif targets E-cadherin to the basolateral cell surface in Madin-Darby canine kidney and LLC-PK1 epithelial cells. Interactions of Plakoglobin and -Catenin with Desmosomal Cadherins: BASIS OF SELECTIVE EXCLUSION OF - AND -CATENIN FROM DESMOSOMES Deconstructing the cadherin-catenin-actin complex Biochemical and Structural Characterization of β-Catenin Interactions with Nonphosphorylated and CK2-Phosphorylated Lef-1 Bench to bedside and back again: molecular mechanisms of alpha-catenin function and roles in tumorigenesis Nemo kinase phosphorylates β-catenin to promote ommatidial rotation and connects core PCP factors to E-cadherin-β-catenin. CCN1 induces a reversible epithelial-mesenchymal transition in gastric epithelial cells Turn-off, drop-out: functional state switching of cadherins E-cadherin is under constitutive actomyosin-generated tension that is increased at cell-cell contacts upon externally applied stretch

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