Single-molecule analysis of fluorescently labeled G-protein-coupled receptors reveals complexes with distinct dynamics and organization
about
Total internal reflection fluorescence quantification of receptor pharmacologyFluorescent approaches for understanding interactions of ligands with G protein coupled receptorsQuaternary structure of a G-protein-coupled receptor heterotetramer in complex with Gi and Gs.Preferred supramolecular organization and dimer interfaces of opioid receptors from simulated self-associationVisualization and ligand-induced modulation of dopamine receptor dimerization at the single molecule level.Techniques for studying protein trafficking and molecular motors in neuronsMembrane-Mediated Oligomerization of G Protein Coupled Receptors and Its Implications for GPCR FunctionStructural-Functional Features of the Thyrotropin Receptor: A Class A G-Protein-Coupled Receptor at WorkMultiple motifs regulate apical sorting of p75 via a mechanism that involves dimerization and higher-order oligomerization.Membrane driven spatial organization of GPCRs.Segregation of family A G protein-coupled receptor protomers in the plasma membraneSingle Molecule Imaging Deciphers the Relation between Mobility and Signaling of a Prototypical G Protein-coupled Receptor in Living Cells.Single-Molecule Imaging Reveals the Activation Dynamics of Intracellular Protein Smad3 on Cell Membrane.Apelin receptor homodimer-oligomers revealed by single-molecule imaging and novel G protein-dependent signaling.Estimating the anomalous diffusion exponent for single particle tracking data with measurement errors - An alternative approachNot just an oil slick: how the energetics of protein-membrane interactions impacts the function and organization of transmembrane proteins.Evaluation of fluorophores to label SNAP-tag fused proteins for multicolor single-molecule tracking microscopy in live cells.The specific monomer/dimer equilibrium of the corticotropin-releasing factor receptor type 1 is established in the endoplasmic reticulumCoupling of g proteins to reconstituted monomers and tetramers of the M2 muscarinic receptorHeterologous regulation of Mu-opioid (MOP) receptor mobility in the membrane of SH-SY5Y cells.The GPCR heterotetramer: challenging classical pharmacology.Application of BRET to monitor ligand binding to GPCRs.Dynamic Regulation of Quaternary Organization of the M1 Muscarinic Receptor by Subtype-selective Antagonist Drugs.Targeting the dopamine D3 receptor: an overview of drug design strategies.Methods used to study the oligomeric structure of G-protein-coupled receptors.Ligand-induced dynamics of neurotrophin receptors investigated by single-molecule imaging approaches.Multiplex detection of functional G protein-coupled receptors harboring site-specifically modified unnatural amino acidsSingle molecule analysis of functionally asymmetric G protein-coupled receptor (GPCR) oligomers reveals diverse spatial and structural assemblies.Native serotonin 5-HT2C receptors are expressed as homodimers on the apical surface of choroid plexus epithelial cellsExperimental verification of the kinetic theory of FRET using optical microspectroscopy and obligate oligomers.Improved methodical approach for quantitative BRET analysis of G Protein Coupled Receptor dimerizationDemonstration of a direct interaction between β2-adrenergic receptor and insulin receptor by BRET and bioinformatics.BRET evidence that β2 adrenergic receptors do not oligomerize in cells.Regulation of oligomeric organization of the serotonin 5-hydroxytryptamine 2C (5-HT2C) receptor observed by spatial intensity distribution analysisDistinct Agonist Regulation of Muscarinic Acetylcholine M2-M3 Heteromers and Their Corresponding Homomers.Bax monomers form dimer units in the membrane that further self-assemble into multiple oligomeric speciesAdvances in receptor conformation research: the quest for functionally selective conformations focusing on the β2-adrenoceptorDiscrete spatial organization of TGFβ receptors couples receptor multimerization and signaling to cellular tensionMicroplate-compatible total internal reflection fluorescence microscopy for receptor pharmacology.The prevalence, maintenance, and relevance of G protein-coupled receptor oligomerization
P2860
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P2860
Single-molecule analysis of fluorescently labeled G-protein-coupled receptors reveals complexes with distinct dynamics and organization
description
2012 nî lūn-bûn
@nan
2012 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2012 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
2012年の論文
@ja
2012年論文
@yue
2012年論文
@zh-hant
2012年論文
@zh-hk
2012年論文
@zh-mo
2012年論文
@zh-tw
2012年论文
@wuu
name
Single-molecule analysis of fl ...... inct dynamics and organization
@ast
Single-molecule analysis of fl ...... inct dynamics and organization
@en
type
label
Single-molecule analysis of fl ...... inct dynamics and organization
@ast
Single-molecule analysis of fl ...... inct dynamics and organization
@en
prefLabel
Single-molecule analysis of fl ...... inct dynamics and organization
@ast
Single-molecule analysis of fl ...... inct dynamics and organization
@en
P2093
P2860
P50
P356
P1476
Single-molecule analysis of fl ...... inct dynamics and organization
@en
P2093
Alexander Zürn
Finn Rieken
Julia Wagner
Titiwat Sungkaworn
Ulrike Zabel
P2860
P304
P356
10.1073/PNAS.1205798110
P407
P577
2012-12-24T00:00:00Z