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Article

A splice variant of arrestin. Molecular cloning and localization in bovine retina.

The Journal of biological chemistry - 3 Jun 1994

Smith W C, Milam A H, Dugger D, Arendt A, Hargrave P A, Palczewski K

Abstract excerpt

Inactivation of photolyzed rhodopsin requires phosphorylation of the receptor and binding of the 48-kDa regulatory protein arrestin. We recently isolated a novel form of arrestin, termed p44, that is truncated at the COOH terminus (Palczewski, K., Buczylko, J., Ohguro, H., Annan, R. S., Carr, S. A., Crabb, J. W., Kaplan, M. W., Johnson, R. S., and Walsh, K. A. (1994) Protein Sci. 3, 319-329) and strongly inhibits...

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PMID: 7515057

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A splice variant of arrestin. Molecular cloning and localization in bovine retina.PMID 7515057Read ↗

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Deactivation of phosphorylated and nonphosphorylated rhodopsin by arrestin splice variants.Semantic proximity Read ↗

Functional differences in the interaction of arrestin and its splice variant, p44, with rhodopsin.Semantic proximity Read ↗

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A role for the light-dependent phosphorylation of visual arrestin.Semantic proximity Read ↗

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X‐Arrestin: a new retinal arrestin mapping to the X chromosomeSemantic proximity Read ↗

Targeting arrestin interactions with its partners for therapeutic purposes.Semantic proximity Read ↗

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Arrestin residues involved in the functional binding of arrestin to phosphorylated, photolyzed rhodopsin.Semantic proximity Read ↗

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