Kinetic analysis of antagonist-occupied adenosine-A3 receptors within membrane microdomains of individual cells provides evidence of receptor dimerization and allosterism.
about
Basic Pharmacological and Structural Evidence for Class A G-Protein-Coupled Receptor HeteromerizationNative serotonin 5-HT2C receptors are expressed as homodimers on the apical surface of choroid plexus epithelial cellsLighting up G protein-coupled purinergic receptors with engineered fluorescent ligands.Quantitative analysis of receptor allosterism and its implication for drug discovery.Revealing G-protein-coupled receptor oligomerization at the single-molecule level through a nanoscopic lens: methods, dynamics and biological function.The use of fluorescence correlation spectroscopy to characterize the molecular mobility of fluorescently labelled G protein-coupled receptors.Extracellular purines, purinergic receptors and tumor growth.Investigation of GPCR allosterism and dimerization in single living cells using fluorescent ligands.Use of a new proximity assay (NanoBRET) to investigate the ligand-binding characteristics of three fluorescent ligands to the human β1-adrenoceptor expressed in HEK-293 cells.Real-time analysis of the binding of fluorescent VEGF165a to VEGFR2 in living cells: Effect of receptor tyrosine kinase inhibitors and fate of internalized agonist-receptor complexesNegative cooperativity across β1-adrenoceptor homodimers provides insights into the nature of the secondary low-affinity CGP 12177 β1-adrenoceptor binding conformation.Development of novel fluorescent histamine H1-receptor antagonists to study ligand-binding kinetics in living cells.Protein-ligand (un)binding kinetics as a new paradigm for drug discovery at the crossroad between experiments and modelling
P2860
Q26749791-C77F356F-F004-4C6F-BE7A-112F64B17DFEQ35198061-920C8304-6DAD-4CBC-86F9-16EEBA9F8D9BQ36171090-D9DDBBE5-8F55-47AC-B3CD-729C19AEBCDFQ38451155-2C27ADAA-F018-4519-986F-FCBD9A2A6B49Q38618328-B48ECEBE-0575-484A-B07A-EB78C2360743Q38805872-9AA23860-A7BB-4076-9EF0-5E1313726E0BQ38870205-F98D2ACA-CA60-4EA1-99C5-2793DAFD19E5Q39150893-DBAEE07D-3872-45BE-901E-00F7BA9A92C4Q39428983-F1B9C6A4-2A07-4E48-BA34-678472F4372AQ42076724-5133C4F7-0663-45FA-9F68-A43D33251268Q42149596-B3485749-2964-4BFB-A0F0-564E43271C65Q47711109-58926C41-8C91-47FE-889E-2EE8388F400EQ56961708-648A784B-CD87-4694-9F3B-7965EF94FEBB
P2860
Kinetic analysis of antagonist-occupied adenosine-A3 receptors within membrane microdomains of individual cells provides evidence of receptor dimerization and allosterism.
description
2014 nî lūn-bûn
@nan
2014年の論文
@ja
2014年論文
@yue
2014年論文
@zh-hant
2014年論文
@zh-hk
2014年論文
@zh-mo
2014年論文
@zh-tw
2014年论文
@wuu
2014年论文
@zh
2014年论文
@zh-cn
name
Kinetic analysis of antagonist ...... dimerization and allosterism.
@en
Kinetic analysis of antagonist ...... dimerization and allosterism.
@nl
type
label
Kinetic analysis of antagonist ...... dimerization and allosterism.
@en
Kinetic analysis of antagonist ...... dimerization and allosterism.
@nl
prefLabel
Kinetic analysis of antagonist ...... dimerization and allosterism.
@en
Kinetic analysis of antagonist ...... dimerization and allosterism.
@nl
P2860
P50
P356
P1433
P1476
Kinetic analysis of antagonist ...... dimerization and allosterism.
@en
P2093
Laura E Kilpatrick
Ross Corriden
P2860
P304
P356
10.1096/FJ.13-247270
P407
P577
2014-06-26T00:00:00Z