Bimolecular fluorescence complementation (BiFC) analysis as a probe of protein interactions in living cells.
about
Hepatitis C virus NS4B protein targets STING and abrogates RIG-I-mediated type I interferon-dependent innate immunityProteomic mapping of ER-PM junctions identifies STIMATE as a regulator of Ca²⁺ influxDiscovery of cellular regulation by protein degradationNew technologies for 21st century plant scienceDirect visualization of trans-synaptic neurexin-neuroligin interactions during synapse formationElucidating the Role of Effectors in Plant-Fungal Interactions: Progress and ChallengesFundamentals of protein interaction network mappingFine-tuning multiprotein complexes using small moleculesER-bound protein tyrosine phosphatase PTP1B interacts with Src at the plasma membrane/substrate interfaceThe RhoGEF TEM4 Regulates Endothelial Cell Migration by Suppressing Actomyosin ContractilityPolarized Exocytosis Induces Compensatory Endocytosis by Sec4p-Regulated Cortical Actin PolymerizationHeterotrimeric G-protein Signaling Is Critical to Pathogenic Processes in Entamoeba histolyticaLigand-dependent localization and function of ORP-VAP complexes at membrane contact sites.The budding yeast point centromere associates with two Cse4 molecules during mitosis.Dissecting BAR domain function in the yeast Amphiphysins Rvs161 and Rvs167 during endocytosis.Trs20 is required for TRAPP II assembly.In Vivo Analysis of Protein-Protein Interactions with Bioluminescence Resonance Energy Transfer (BRET): Progress and ProspectsApplications of phototransformable fluorescent proteins for tracking the dynamics of cellular componentsAutophagy mediates degradation of nuclear laminaVisualization by BiFC of different C/EBPβ dimers and their interaction with HP1α reveals a differential subnuclear distribution of complexes in living cellsNucleolus-tethering system (NoTS) reveals that assembly of photobodies follows a self-organization modelInteraction with the Src homology (SH3-SH2) region of the Src-family kinase Hck structures the HIV-1 Nef dimer for kinase activation and effector recruitmentThe budding yeast amphiphysin complex is required for contractile actin ring (CAR) assembly and post-contraction GEF-independent accumulation of Rho1-GTPThe accessory factor Nef links HIV-1 to Tec/Btk kinases in an Src homology 3 domain-dependent manner.Targeting and functional mechanisms of the cytokinesis-related F-BAR protein Hof1 during the cell cycleDock mediates Scar- and WASp-dependent actin polymerization through interaction with cell adhesion molecules in founder cells and fusion-competent myoblasts.Harnessing the unique structural properties of isolated α-helices.Fluorescence applications in molecular neurobiologyWnt-11 and Fz7 reduce cell adhesion in convergent extension by sequestration of PAPC and C-cadherin.WAVE forms hetero- and homo-oligomeric complexes at integrin junctions in Drosophila visualized by bimolecular fluorescence complementation.Visualization of protein interactions in living Drosophila embryos by the bimolecular fluorescence complementation assayTargeting and imaging single biomolecules in living cells by complementation-activated light microscopy with split-fluorescent proteins.Quantitative time-lapse fluorescence microscopy in single cells.Single-molecule pull-down for studying protein interactions.The actin-microtubule cross-linking activity of Drosophila Short stop is regulated by intramolecular inhibitionFluorescence correlation spectroscopy, combined with bimolecular fluorescence complementation, reveals the effects of β-arrestin complexes and endocytic targeting on the membrane mobility of neuropeptide Y receptorsDimerization of ABCG2 analysed by bimolecular fluorescence complementation.The C-terminal domain of CENP-C displays multiple and critical functions for mammalian centromere formation.Development and validation of a high-content bimolecular fluorescence complementation assay for small-molecule inhibitors of HIV-1 Nef dimerization.In vitro visualization and characterization of wild type and mutant IDH homo- and heterodimers using Bimolecular Fluorescence Complementation.
P2860
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P2860
Bimolecular fluorescence complementation (BiFC) analysis as a probe of protein interactions in living cells.
description
2008 nî lūn-bûn
@nan
2008 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2008 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2008年の論文
@ja
2008年論文
@yue
2008年論文
@zh-hant
2008年論文
@zh-hk
2008年論文
@zh-mo
2008年論文
@zh-tw
2008年论文
@wuu
name
Bimolecular fluorescence compl ...... interactions in living cells.
@ast
Bimolecular fluorescence compl ...... interactions in living cells.
@en
type
label
Bimolecular fluorescence compl ...... interactions in living cells.
@ast
Bimolecular fluorescence compl ...... interactions in living cells.
@en
prefLabel
Bimolecular fluorescence compl ...... interactions in living cells.
@ast
Bimolecular fluorescence compl ...... interactions in living cells.
@en
P2860
P1476
Bimolecular fluorescence compl ...... interactions in living cells.
@en
P2860
P304
P356
10.1146/ANNUREV.BIOPHYS.37.032807.125842
P577
2008-01-01T00:00:00Z