E-cadherin interactome complexity and robustness resolved by quantitative proteomics
about
Synaptopodin couples epithelial contractility to α-actinin-4-dependent junction maturationA protein interaction map for cell-cell adhesion regulators identifies DUSP23 as a novel phosphatase for β-catenin.The integrin adhesome network at a glanceFormin-mediated actin polymerization at cell-cell junctions stabilizes E-cadherin and maintains monolayer integrity during wound repair.Identifying Protein-Protein Associations at the Nuclear Envelope with BioID.E-cadherin junction formation involves an active kinetic nucleation process.BioID Identification of Lamin-Associated Proteins.An improved smaller biotin ligase for BioID proximity labeling.Proximity-Directed Labeling Reveals a New Rapamycin-Induced Heterodimer of FKBP25 and FRB in Live Cells.Downregulation of BZW2 inhibits osteosarcoma cell growth by inactivating the Akt/mTOR signaling pathway.Sustained α-catenin Activation at E-cadherin Junctions in the Absence of Mechanical Force.Filling the Void: Proximity-Based Labeling of Proteins in Living Cells.YAP and TAZ in epithelial stem cells: A sensor for cell polarity, mechanical forces and tissue damage.Cell-cell junctional mechanotransduction in endothelial remodeling.Integration of Cadherin Adhesion and Cytoskeleton at Adherens Junctions.Proximity labeling of interacting proteins: Application of BioID as a discovery tool.Rho GTPases and actomyosin: Partners in regulating epithelial cell-cell junction structure and function.Proximity biotinylation provides insight into the molecular composition of focal adhesions at the nanometer scale.Changes in E-cadherin rigidity sensing regulate cell adhesionNovel peptides for deciphering structural and signalling functions of E-cadherin in mouse embryonic stem cells.Sorbin and SH3 domain-containing protein 2 (SORBS2) is a component of the acto-myosin ring at the apical junctional complex in epithelial cells.Multiscale View of Cytoskeletal Mechanoregulation of Cell and Tissue Polarity.Long-range self-organization of cytoskeletal myosin II filament stacks.Correlation between E-cadherin interactions, survivin expression, and apoptosis in MDCK and ts-Src MDCK cell culture models.TRIP6 inhibits Hippo signaling in response to tension at adherens junctions.EphA2 proteomics in human keratinocytes reveals a novel association with afadin and epidermal tight junctions.A Rac1-FMNL2 signaling module affects cell-cell contact formation independent of Cdc42 and membrane protrusions.Close encounters of the RNAi kind: the silencing life of the adherens junctions.The proximity-labeling technique BioID identifies sorting nexin 6 as a member of the insulin-like growth factor 1 (IGF1)-IGF1 receptor pathway.Translating epithelial mesenchymal transition markers into the clinic: Novel insights from proteomics.
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P2860
E-cadherin interactome complexity and robustness resolved by quantitative proteomics
description
2014 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2014 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
artículu científicu espublizáu en 2014
@ast
im Dezember 2014 veröffentlichter wissenschaftlicher Artikel
@de
scientific journal article
@en
vedecký článok (publikovaný 2014/12/02)
@sk
vědecký článek publikovaný v roce 2014
@cs
wetenschappelijk artikel (gepubliceerd op 2014/12/02)
@nl
наукова стаття, опублікована в грудні 2014
@uk
مقالة علمية (نشرت في 2-12-2014)
@ar
name
E-cadherin interactome complexity and robustness resolved by quantitative proteomics
@ast
E-cadherin interactome complexity and robustness resolved by quantitative proteomics
@en
E-cadherin interactome complexity and robustness resolved by quantitative proteomics
@nl
type
label
E-cadherin interactome complexity and robustness resolved by quantitative proteomics
@ast
E-cadherin interactome complexity and robustness resolved by quantitative proteomics
@en
E-cadherin interactome complexity and robustness resolved by quantitative proteomics
@nl
prefLabel
E-cadherin interactome complexity and robustness resolved by quantitative proteomics
@ast
E-cadherin interactome complexity and robustness resolved by quantitative proteomics
@en
E-cadherin interactome complexity and robustness resolved by quantitative proteomics
@nl
P2093
P2860
P3181
P1433
P1476
E-cadherin interactome complexity and robustness resolved by quantitative proteomics
@en
P2093
Hang Zhong
Lisa J Neilson
Paul S Murray
Zhenhuan Guo
P2860
P3181
P356
10.1126/SCISIGNAL.2005473
P577
2014-12-02T00:00:00Z