Arrestin-rhodopsin binding stoichiometry in isolated rod outer segment membranes depends on the percentage of activated receptors.
about
Crystal structure of pre-activated arrestin p44Fluorescence correlation spectroscopy, combined with bimolecular fluorescence complementation, reveals the effects of β-arrestin complexes and endocytic targeting on the membrane mobility of neuropeptide Y receptorsRhodopsin TM6 can interact with two separate and distinct sites on arrestin: evidence for structural plasticity and multiple docking modes in arrestin-rhodopsin bindingNanodomain organization of rhodopsin in native human and murine rod outer segment disc membranes.G protein-coupled receptors--recent advancesThe functional cycle of visual arrestins in photoreceptor cells.Distinct loops in arrestin differentially regulate ligand binding within the GPCR opsin.Conformation of receptor-bound visual arrestin.Involvement of distinct arrestin-1 elements in binding to different functional forms of rhodopsinCritical role of the central 139-loop in stability and binding selectivity of arrestin-1.Functional map of arrestin binding to phosphorylated opsin, with and without agonist.Constitutively active rhodopsin mutants causing night blindness are effectively phosphorylated by GRKs but differ in arrestin-1 bindingFunctional map of arrestin-1 at single amino acid resolutionFluorescence spectroscopy of rhodopsins: insights and approaches.Extensive shape shifting underlies functional versatility of arrestins.The effect of phosphorylation on arrestin-rhodopsin interaction in the squid visual system.Formation and decay of the arrestin·rhodopsin complex in native disc membranes.Crystal structure of a common GPCR-binding interface for G protein and arrestin.Self-association of arrestin family members.Quaternary structures of opsin in live cells revealed by FRET spectrometry.[G protein-coupled receptors in the spot light].
P2860
Q27684457-F1C244FF-7A1A-41FC-A86F-CCB9EC5F1BD1Q30549924-0FDDC9AA-35D6-418E-AA65-0C4D4AB3931AQ33689499-93D4A313-2FC9-4E70-9DB4-BBFED6169245Q34656870-D7586A61-5AD8-43B1-8A55-0E0C01EEF76AQ35065927-889CF312-ACC0-4D52-883E-F09C285E15B6Q35387361-30038070-AE43-47D3-9CF3-8CDD1C5A1652Q36270142-8E006706-8DFB-4128-8B83-CCFC9CDC3C13Q36389593-853A0A9B-A707-4583-A063-5EF94A57E68BQ36545558-AF82E41E-71EB-436C-A83D-177B947E88FDQ36796795-FE1E6A91-42E0-4E31-AE7D-96078C27960FQ37044506-4B3BFAD0-F316-4C57-A09E-C0F0A0677C68Q37174339-33A521FE-977A-4DD6-9737-946A3480BAA8Q37571225-9D98611E-F86C-4B35-AD52-41C88E8D8324Q37662833-3C4DC72A-1858-4DD7-BB3A-04E2CACAD05BQ38200331-A5ABA903-295E-4783-BD05-118AFF17E5C3Q40534961-50B8A201-437A-4287-B13C-E6359BDB4DF1Q40680953-5C1D3FB7-EB1D-4982-A14E-9A06EC43F4A1Q41812263-0E1B1CC0-B8DD-40EF-B90B-7FFEA63D74A5Q41965656-9DCB4D89-8316-4DB0-8F0F-F19CACBDD16EQ42723814-12B326E7-96A5-4A4D-A631-4D665E6CC44CQ46040981-FD552002-4521-47DE-8952-D11F05AF3A2C
P2860
Arrestin-rhodopsin binding stoichiometry in isolated rod outer segment membranes depends on the percentage of activated receptors.
description
2010 nî lūn-bûn
@nan
2010 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
name
Arrestin-rhodopsin binding sto ...... entage of activated receptors.
@ast
Arrestin-rhodopsin binding sto ...... entage of activated receptors.
@en
Arrestin-rhodopsin binding sto ...... entage of activated receptors.
@nl
type
label
Arrestin-rhodopsin binding sto ...... entage of activated receptors.
@ast
Arrestin-rhodopsin binding sto ...... entage of activated receptors.
@en
Arrestin-rhodopsin binding sto ...... entage of activated receptors.
@nl
prefLabel
Arrestin-rhodopsin binding sto ...... entage of activated receptors.
@ast
Arrestin-rhodopsin binding sto ...... entage of activated receptors.
@en
Arrestin-rhodopsin binding sto ...... entage of activated receptors.
@nl
P2093
P2860
P356
P1476
Arrestin-rhodopsin binding sto ...... entage of activated receptors.
@en
P2093
Klaus Peter Hofmann
Martha E Sommer
Martin Heck
P2860
P304
P356
10.1074/JBC.M110.204941
P407
P577
2010-12-17T00:00:00Z