Interactions of metarhodopsin II. Arrestin peptides compete with arrestin and transducin. - Wikidata - wikimedia - TriplyDB

Interactions of metarhodopsin II. Arrestin peptides compete with arrestin and transducin.

Interactions of metarhodopsin II. Arrestin peptides compete with arrestin and transducin.

http://www.wikidata.org/entity/Q52969976

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The structural basis of arrestin-mediated regulation of G-protein-coupled receptors Crystal Structure of Arrestin-3 Reveals the Basis of the Difference in Receptor Binding Between Two Non-visual Subtypes Rhodopsin TM6 can interact with two separate and distinct sites on arrestin: evidence for structural plasticity and multiple docking modes in arrestin-rhodopsin binding The effect of arrestin conformation on the recruitment of c-Raf1, MEK1, and ERK1/2 activation Calcium-dependent assembly of centrin-G-protein complex in photoreceptor cells Monomeric rhodopsin is sufficient for normal rhodopsin kinase (GRK1) phosphorylation and arrestin-1 binding Differential interaction of spin-labeled arrestin with inactive and active phosphorhodopsin.Arrestin: roles in the life and death of retinal neurons.Few residues within an extensive binding interface drive receptor interaction and determine the specificity of arrestin proteins.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.Manipulation of very few receptor discriminator residues greatly enhances receptor specificity of non-visual arrestins Phosducin regulates the expression of transducin betagamma subunits in rod photoreceptors and does not contribute to phototransduction adaptation Involvement of distinct arrestin-1 elements in binding to different functional forms of rhodopsin The differential engagement of arrestin surface charges by the various functional forms of the receptor.Critical role of the central 139-loop in stability and binding selectivity of arrestin-1.The role of arrestin alpha-helix I in receptor binding.Functional map of arrestin-1 at single amino acid resolution Custom-designed proteins as novel therapeutic tools? The case of arrestins.Structural determinants of arrestin functions Nonvisual arrestins function as simple scaffolds assembling the MKK4-JNK3α2 signaling complex Arrestin mobilizes signaling proteins to the cytoskeleton and redirects their activity.A model for the solution structure of the rod arrestin tetramer.Mapping the arrestin-receptor interface. Structural elements responsible for receptor specificity of arrestin proteins.Targeting individual GPCRs with redesigned nonvisual arrestins.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.Arrestin-3 binds the MAP kinase JNK3α2 via multiple sites on both domains.Therapeutic potential of small molecules and engineered proteins.Ubiquitin ligase parkin promotes Mdm2-arrestin interaction but inhibits arrestin ubiquitination Enhanced phosphorylation-independent arrestins and gene therapy.Differential manipulation of arrestin-3 binding to basal and agonist-activated G protein-coupled receptors.Signaling states of rhodopsin: absorption of light in active metarhodopsin II generates an all-trans-retinal bound inactive state.Differential conformational requirements for activation of G proteins and the regulatory proteins arrestin and G protein-coupled receptor kinase in the G protein-coupled receptor for parathyroid hormone (PTH)/PTH-related protein.Arrestin and its splice variant Arr1-370A (p44). Mechanism and biological role of their interaction with rhodopsin.Transition of arrestin into the active receptor-binding state requires an extended interdomain hinge.Dynamics of arrestin-rhodopsin interactions: arrestin and retinal release are directly linked events.The arrestin-1 finger loop interacts with two distinct conformations of active rhodopsin.

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P2860

Interactions of metarhodopsin II. Arrestin peptides compete with arrestin and transducin.

http://www.wikidata.org/entity/Q52969976

description

2000 nî lūn-bûn

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2000年の論文

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2000年学术文章

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2000年学术文章

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2000年学术文章

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2000年学术文章

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2000年学术文章

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2000年学术文章

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2000年學術文章

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2000年學術文章

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name

Interactions of metarhodopsin II. Arrestin peptides compete with arrestin and transducin.

@en

Interactions of metarhodopsin II. Arrestin peptides compete with arrestin and transducin.

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type

label

Interactions of metarhodopsin II. Arrestin peptides compete with arrestin and transducin.

@en

Interactions of metarhodopsin II. Arrestin peptides compete with arrestin and transducin.

@nl

prefLabel

Interactions of metarhodopsin II. Arrestin peptides compete with arrestin and transducin.

@en

Interactions of metarhodopsin II. Arrestin peptides compete with arrestin and transducin.

@nl

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P1433

Journal of Biological Chemistry

P1476

Interactions of metarhodopsin II. Arrestin peptides compete with arrestin and transducin.

@en

P2093

A Pulvermüller

http://www.w3.org/2001/XMLSchema#string

K P Hofmann

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K Schroder

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T Fischer

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P2860

Phosphodiesterase activation by photoexcited rhodopsin is quenched when rhodopsin is phosphorylated and binds the intrinsic 48-kDa protein of rod outer segments

A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding

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

Crystal structure of rhodopsin: A G protein-coupled receptor

X-ray crystal structure of arrestin from bovine rod outer segments

Effect of GTP on the rhodopsin-G-protein complex by transient formation of extra metarhodopsin II

Spectroscopic characterization of arrestin interactions with competitive ligands: study of heparin and phytic acid binding.

Identification of regions of arrestin that bind to rhodopsin.

Force probe measurements of antibody-antigen interactions.

Prolonged photoresponses in transgenic mouse rods lacking arrestin.

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37679-37685

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10.1074/JBC.M006776200

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48

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275

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10969086

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