Concentration-dependent tetramerization of bovine visual arrestin.
about
Crystal Structure of Arrestin-3 Reveals the Basis of the Difference in Receptor Binding Between Two Non-visual SubtypesBeta-arrestins: multifunctional cellular mediatorsTransport and localization of signaling proteins in ciliated cellsOpposing effects of inositol hexakisphosphate on rod arrestin and arrestin2 self-association.Analysis of self-associating proteins by singular value decomposition of solution scattering dataArrestin can act as a regulator of rhodopsin photochemistry.Progressive reduction of its expression in rods reveals two pools of arrestin-1 in the outer segment with different roles in photoresponse recovery.Arrestin-1 expression level in rods: balancing functional performance and photoreceptor health.Robust self-association is a common feature of mammalian visual arrestin-1.Few residues within an extensive binding interface drive receptor interaction and determine the specificity of arrestin proteins.The functional cycle of visual arrestins in photoreceptor cells.Each rhodopsin molecule binds its own arrestinSteric volume exclusion sets soluble protein concentrations in photoreceptor sensory cilia.Arrestin 1 and Cone Arrestin 4 Have Unique Roles in Visual Function in an All-Cone Mouse Retina.Involvement of distinct arrestin-1 elements in binding to different functional forms of rhodopsinEngineering visual arrestin-1 with special functional characteristicsVisual arrestin binding to microtubules involves a distinct conformational changeCritical role of the central 139-loop in stability and binding selectivity of arrestin-1.Regulation of arrestin binding by rhodopsin phosphorylation level.Protein sorting, targeting and trafficking in photoreceptor cellsMonomeric rhodopsin is the minimal functional unit required for arrestin binding.Custom-designed proteins as novel therapeutic tools? The case of arrestins.β-Arrestins: multifunctional signaling adaptors in type 2 diabetes.The cytoplasmic rhodopsin-protein interface: potential for drug discovery.Structural determinants of arrestin functionsStructure and function of the visual arrestin oligomer.A model for the solution structure of the rod arrestin tetramer.Elucidation of inositol hexaphosphate and heparin interaction sites and conformational changes in arrestin-1 by solution nuclear magnetic resonance.Self-association of arrestin family members.Rapid degeneration of rod photoreceptors expressing self-association-deficient arrestin-1 mutant.Arrestins in apoptosis.Arrestin competition influences the kinetics and variability of the single-photon responses of mammalian rod photoreceptors.Dynamics of arrestin-rhodopsin interactions: arrestin and retinal release are directly linked events.Nonvisual arrestin oligomerization and cellular localization are regulated by inositol hexakisphosphate binding.Presence of the propeptide on recombinant lysosomal dipeptidase controls both activation and dimerization.
P2860
Q27666519-B2CEEBBF-06E2-4655-BD60-783EEA2F59E2Q28268438-9E47CE6A-ECCE-4724-85E2-EA87F37BB618Q30420687-85663047-2EE5-4163-A3E2-A1BDF4C3D260Q30839922-42E3B6B0-A19C-4212-9F8D-7D9C7C00E973Q33315748-43ECCD58-9245-4E52-A281-00E1F88E5106Q33879152-90FF5638-A555-4A79-9151-E7B9346B4234Q33983455-E11A14DA-DB6F-4599-AB22-D90E53CEB274Q34486390-1163BC1B-4D7B-49B1-99C3-7F4EC6BD8982Q34708925-B0DD5D8D-F177-437C-BE90-BC591685AC86Q35085144-78D294F4-7162-407E-B419-AD7D9A495648Q35387361-272CC9D9-8236-4503-A298-B410CCFDC723Q35652316-17CE308A-7B0F-43ED-A563-39282E34BC30Q35657676-7BE10041-7F5C-4D5D-8008-2D62D95DCE83Q36347393-E059B87F-B546-4063-BFAC-E9CAD8AF9004Q36545558-025EEB41-C813-4AFF-859A-663C164F97F6Q36579557-AC9DC914-6469-409C-80E3-9BD216DFFBC8Q36726921-984C7E6F-AAFF-4EAA-ADD5-07917861B88DQ36796795-1908E376-6F95-4493-BFA2-D5C5EF2C7509Q37089132-03B441C3-18A9-4767-AE5F-B0AF4FFA2607Q37138123-CCCDAC87-E908-48A2-ACE4-DD957BC358A5Q37360145-FF24F0E3-51E4-480F-A2CF-0FB4063F1304Q37735949-A1DA7AA3-6ABD-4B8B-B8BD-D9D7BBA0769FQ37810522-EC34A9D7-5F9F-456D-830E-E6257CCD6AF9Q37903343-35A5D431-F52C-4E9A-8CA7-4AB139BDDDE3Q38114211-4F7C9318-7DAB-467E-9DBE-8513E911107EQ38304145-B778C378-A03B-4B58-A8AA-275A36863C91Q40262832-254C1664-1C0C-41E1-9680-1965F4BF32F0Q41894869-E8BEBB7C-FE29-4452-8D19-32454B552F3AQ41965656-7E60208B-E5E0-4100-A642-A2025891117CQ42044999-C7BDA8CF-888D-45F3-8D21-80588A872CE2Q42089456-00237D18-1F33-4877-9C39-C8C402C8D150Q42668381-5A801264-66CD-47ED-A36B-CF3EB3CEA256Q45182666-8D7A2A80-8A23-4ABA-BF63-F8C414E83D59Q46913508-37D8BD1F-0147-4214-9464-E497AAD3A45BQ54448759-EA11AC9C-81D6-4D32-91DA-65BBA53B97C3
P2860
Concentration-dependent tetramerization of bovine visual arrestin.
description
2003 nî lūn-bûn
@nan
2003年の論文
@ja
2003年論文
@yue
2003年論文
@zh-hant
2003年論文
@zh-hk
2003年論文
@zh-mo
2003年論文
@zh-tw
2003年论文
@wuu
2003年论文
@zh
2003年论文
@zh-cn
name
Concentration-dependent tetramerization of bovine visual arrestin.
@en
type
label
Concentration-dependent tetramerization of bovine visual arrestin.
@en
prefLabel
Concentration-dependent tetramerization of bovine visual arrestin.
@en
P2093
P2860
P1433
P1476
Concentration-dependent tetramerization of bovine visual arrestin.
@en
P2093
Chie Tamura
Hironari Kamikubo
Mikio Kataoka
Yasushi Imamoto
P2860
P304
P356
10.1016/S0006-3495(03)74554-8
P407
P577
2003-08-01T00:00:00Z