Differential interaction of spin-labeled arrestin with inactive and active phosphorhodopsin. - Wikidata - wikimedia - TriplyDB

Differential interaction of spin-labeled arrestin with inactive and active phosphorhodopsin.

Differential interaction of spin-labeled arrestin with inactive and active phosphorhodopsin.

http://www.wikidata.org/entity/Q34596638

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Arrestins: ubiquitous regulators of cellular signaling pathways Analyzing the roles of multi-functional proteins in cells: The case of arrestins and GRKs Crystal structure of rhodopsin bound to arrestin by femtosecond X-ray laser Structural origin of weakly ordered nitroxide motion in spin-labeled proteins Structure of active β-arrestin-1 bound to a G-protein-coupled receptor phosphopeptide Crystal structure of pre-activated arrestin p44 Visualization of arrestin recruitment by a G-protein-coupled receptor Probing Protein Secondary Structure using EPR: Investigating a Dynamic Region of Visual Arrestin.Opposing effects of inositol hexakisphosphate on rod arrestin and arrestin2 self-association.Rhodopsin TM6 can interact with two separate and distinct sites on arrestin: evidence for structural plasticity and multiple docking modes in arrestin-rhodopsin binding Identification of receptor binding-induced conformational changes in non-visual arrestins.Progressive reduction of its expression in rods reveals two pools of arrestin-1 in the outer segment with different roles in photoresponse recovery.The effect of arrestin conformation on the recruitment of c-Raf1, MEK1, and ERK1/2 activation Monomeric rhodopsin is sufficient for normal rhodopsin kinase (GRK1) phosphorylation and arrestin-1 binding Functional competence of a partially engaged GPCR-β-arrestin complex Arrestin-rhodopsin binding stoichiometry in isolated rod outer segment membranes depends on the percentage of activated receptors.Recognition in the face of diversity: interactions of heterotrimeric G proteins and G protein-coupled receptor (GPCR) kinases with activated GPCRs Identification of a functionally important loop in Salmonella typhimurium ArnT G protein-coupled receptors--recent advances Conformational selection and equilibrium governs the ability of retinals to bind opsin.Few residues within an extensive binding interface drive receptor interaction and determine the specificity of arrestin proteins.Structural and dynamical changes in an alpha-subunit of a heterotrimeric G protein along the activation pathway.Identification of arrestin-3-specific residues necessary for JNK3 kinase activation A single mutation in arrestin-2 prevents ERK1/2 activation by reducing c-Raf1 binding.The functional cycle of visual arrestins in photoreceptor cells.Conformational dynamics of helix 8 in the GPCR rhodopsin controls arrestin activation in the desensitization process.Redox proteomic identification of visual arrestin dimerization in photoreceptor degeneration after photic injury.Role of receptor-attached phosphates in binding of visual and non-visual arrestins to G protein-coupled receptors.Silent scaffolds: inhibition OF c-Jun N-terminal kinase 3 activity in cell by dominant-negative arrestin-3 mutant Manipulation of very few receptor discriminator residues greatly enhances receptor specificity of non-visual arrestins Distinct loops in arrestin differentially regulate ligand binding within the GPCR opsin.Interaction of a fragment of the cannabinoid CB1 receptor C-terminus with arrestin-2.Conformation of receptor-bound visual arrestin.Involvement of distinct arrestin-1 elements in binding to different functional forms of rhodopsin Visual and both non-visual arrestins in their "inactive" conformation bind JNK3 and Mdm2 and relocalize them from the nucleus to the cytoplasm.Binding between a distal C-terminus fragment of cannabinoid receptor 1 and arrestin-2.Critical role of the central 139-loop in stability and binding selectivity of arrestin-1.The β-Arrestins: Multifunctional Regulators of G Protein-coupled Receptors Functional map of arrestin binding to phosphorylated opsin, with and without agonist.GPCR monomers and oligomers: it takes all kinds.

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Differential interaction of spin-labeled arrestin with inactive and active phosphorhodopsin.

http://www.wikidata.org/entity/Q34596638

description

2006 nî lūn-bûn

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2006 թուականի Մարտին հրատարակուած գիտական յօդուած

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2006 թվականի մարտին հրատարակված գիտական հոդված

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2006年の論文

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2006年学术文章

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2006年学术文章

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2006年学术文章

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2006年學術文章

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Differential interaction of sp ...... e and active phosphorhodopsin.

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Differential interaction of sp ...... e and active phosphorhodopsin.

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Differential interaction of sp ...... e and active phosphorhodopsin.

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Differential interaction of sp ...... e and active phosphorhodopsin.

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Differential interaction of sp ...... e and active phosphorhodopsin.

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Differential interaction of sp ...... e and active phosphorhodopsin.

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Differential interaction of sp ...... e and active phosphorhodopsin.

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Differential interaction of sp ...... e and active phosphorhodopsin.

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Differential interaction of sp ...... e and active phosphorhodopsin.

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PNAS.0600733103

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Proceedings of the National Academy of Sciences of the United States of America

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Differential interaction of sp ...... e and active phosphorhodopsin.

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Candice S Klug

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Derek J Francis

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Elena A Kolobova

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Sergey A Vishnivetskiy

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Susan M Hanson

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Vsevolod V Gurevich

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P2860

The 2.8 A crystal structure of visual arrestin: a model for arrestin's regulation

Crystal structure of beta-arrestin at 1.9 A: possible mechanism of receptor binding and membrane Translocation

Transduction of receptor signals by beta-arrestins

The molecular acrobatics of arrestin activation

Phosphorylated rhodopsin and heparin induce similar conformational changes in arrestin

Estimation of inter-residue distances in spin labeled proteins at physiological temperatures: experimental strategies and practical limitations.

Motion of spin-labeled side chains in T4 lysozyme. Correlation with protein structure and dynamics.

Defining protein-protein interactions using site-directed spin-labeling: the binding of protein kinase C substrates to calmodulin.

Activation-dependent conformational changes in {beta}-arrestin 2.

Identifying conformational changes with site-directed spin labeling.

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13

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103

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Wayne L. Hubbell

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2006-03-17T00:00:00Z

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7232051

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16547131

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1458767

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