Quantitative characterization of the large-scale association of ErbB1 and ErbB2 by flow cytometric homo-FRET measurements.
about
Comparative analysis of fluorescence resonance energy transfer (FRET) and proximity ligation assay (PLA)Homo-FRET imaging enables quantification of protein cluster sizes with subcellular resolutionStructure-function relationships of ErbB RTKs in the plasma membrane of living cellsUnderstanding FRET as a research tool for cellular studiesManipulating the lateral diffusion of surface-anchored EGF demonstrates that receptor clustering modulates phosphorylation levelsCoclustering of ErbB1 and ErbB2 revealed by FRET-sensitized acceptor bleaching.Distribution of resting and ligand-bound ErbB1 and ErbB2 receptor tyrosine kinases in living cells using number and brightness analysisMonitoring the size and lateral dynamics of ErbB1 enriched membrane domains through live cell plasmon coupling microscopy.Quantification of differential ErbB1 and ErbB2 cell surface expression and spatial nanoclustering through plasmon coupling.Time-domain microfluidic fluorescence lifetime flow cytometry for high-throughput Förster resonance energy transfer screening.Functional isolation of activated and unilaterally phosphorylated heterodimers of ERBB2 and ERBB3 as scaffolds in ligand-dependent signaling.Distinct ErbB2 receptor populations differentially interact with beta1 integrin in breast cancer cell models.EGFP oligomers as natural fluorescence and hydrodynamic standards.The Dipole Potential Modifies the Clustering and Ligand Binding Affinity of ErbB Proteins and Their Signaling Efficiency.Transmembrane helix-helix interactions involved in ErbB receptor signaling.Single-spanning transmembrane domains in cell growth and cell-cell interactions: More than meets the eye?Mathematical simulation of membrane protein clustering for efficient signal transductionThe Epidermal Growth Factor Receptor Forms Location-Dependent Complexes in Resting Cells.Maximum likelihood estimation of FRET efficiency and its implications for distortions in pixelwise calculation of FRET in microscopy.Regulation of PKR by RNA: formation of active and inactive dimers.Monte Carlo simulations of plasma membrane corral-induced EGFR clustering.Flow Cytometric FRET Analysis of Protein Interactions.The Effect of Fluorophore Conjugation on Antibody Affinity and the Photophysical Properties of Dyes.Single molecule localization microscopy coupled with touch preparation for the quantification of trastuzumab-bound HER2
P2860
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P2860
Quantitative characterization of the large-scale association of ErbB1 and ErbB2 by flow cytometric homo-FRET measurements.
description
2008 nî lūn-bûn
@nan
2008年の論文
@ja
2008年学术文章
@wuu
2008年学术文章
@zh-cn
2008年学术文章
@zh-hans
2008年学术文章
@zh-my
2008年学术文章
@zh-sg
2008年學術文章
@yue
2008年學術文章
@zh
2008年學術文章
@zh-hant
name
Quantitative characterization ...... metric homo-FRET measurements.
@en
Quantitative characterization ...... metric homo-FRET measurements.
@nl
type
label
Quantitative characterization ...... metric homo-FRET measurements.
@en
Quantitative characterization ...... metric homo-FRET measurements.
@nl
prefLabel
Quantitative characterization ...... metric homo-FRET measurements.
@en
Quantitative characterization ...... metric homo-FRET measurements.
@nl
P2860
P1433
P1476
Quantitative characterization ...... ometric homo-FRET measurements
@en
P2093
Agnes Szabó
János Szöllosi
P2860
P304
P356
10.1529/BIOPHYSJ.108.133371
P407
P577
2008-05-16T00:00:00Z