Quantitative analysis of multi-protein interactions using FRET: application to the SUMO pathway
about
A new trend to determine biochemical parameters by quantitative FRET assaysMechanism of ubiquitylation by dimeric RING ligase RNF4The interaction affinity between vascular cell adhesion molecule-1 (VCAM-1) and very late antigen-4 (VLA-4) analyzed by quantitative FRETVisualization of NO3⁻/NO2⁻ Dynamics in Living Cells by Fluorescence Resonance Energy Transfer (FRET) Imaging Employing a Rhizobial Two-component Regulatory System.FRET based quantification and screening technology platform for the interactions of leukocyte function-associated antigen-1 (LFA-1) with intercellular adhesion molecule-1 (ICAM-1).Caged glutathione - triggering protein interaction by light.Identification of sumoylation sites in CCDC6, the first identified RET partner gene in papillary thyroid carcinoma, uncovers a mode of regulating CCDC6 function on CREB1 transcriptional activity.Development of FRET assay into quantitative and high-throughput screening technology platforms for protein-protein interactions.A spectrophotometric assay for conjugation of ubiquitin and ubiquitin-like proteins.Fluorescence strategies for high-throughput quantification of protein interactionsSUMO regulates p21Cip1 intracellular distribution and with p21Cip1 facilitates multiprotein complex formation in the nucleolus upon DNA damageIn vivo localization and identification of SUMOylated proteins in the brain of His6-HA-SUMO1 knock-in mice.Association of a novel preribosomal complex in Trypanosoma brucei determined by fluorescence resonance energy transferTrafficking of the transcription factor Nrf2 to promyelocytic leukemia-nuclear bodies: implications for degradation of NRF2 in the nucleusInternal calibration Förster resonance energy transfer assay: a real-time approach for determining protease kinetics.SUMO chain-induced dimerization activates RNF4.Networks of ProteinProtein Interactions: From Uncertainty to Molecular Details.Polymeric assemblies and nanoparticles with stimuli-responsive fluorescence emission characteristics.Defining the RNA-protein interactions in the trypanosome preribosomal complex.Regulation of Neuronal Protein Trafficking and Translocation by SUMOylation.Development of a steady-state FRET-based assay to identify inhibitors of the Keap1-Nrf2 protein-protein interaction.A linker strategy for trans-FRET assay to determine activation intermediate of NEDDylation cascade.Protein interaction affinity determination by quantitative FRET technology.In vitro FRET analysis of IRE1 and BiP association and dissociation upon endoplasmic reticulum stress.Structural insights into enzymatic [4+2] aza-cycloaddition in thiopeptide antibiotic biosynthesis.
P2860
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P2860
Quantitative analysis of multi-protein interactions using FRET: application to the SUMO pathway
description
2008 nî lūn-bûn
@nan
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
2008年论文
@zh
2008年论文
@zh-cn
name
Quantitative analysis of multi ...... pplication to the SUMO pathway
@ast
Quantitative analysis of multi ...... pplication to the SUMO pathway
@en
type
label
Quantitative analysis of multi ...... pplication to the SUMO pathway
@ast
Quantitative analysis of multi ...... pplication to the SUMO pathway
@en
prefLabel
Quantitative analysis of multi ...... pplication to the SUMO pathway
@ast
Quantitative analysis of multi ...... pplication to the SUMO pathway
@en
P2860
P50
P356
P1433
P1476
Quantitative analysis of multi ...... pplication to the SUMO pathway
@en
P2093
Sarah F Martin
P2860
P304
P356
10.1110/PS.073369608
P577
2008-04-01T00:00:00Z