Kühn H - Search Results

1

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

Wilden U, Hall SW, Kühn H. Wilden U, et al. Among authors: kuhn h. Proc Natl Acad Sci U S A. 1986 Mar;83(5):1174-8. doi: 10.1073/pnas.83.5.1174. Proc Natl Acad Sci U S A. 1986. PMID: 3006038 Free PMC article.

We report here that deactivation of PDEase in rod outer segment suspensions is highly enhanced by addition of ATP and purified 48-kDa protein, which is an intrinsic rod outer segment protein that is soluble in the dark but binds to photolyzed rhodopsin that has been phosphorylate …

We report here that deactivation of PDEase in rod outer segment suspensions is highly enhanced by addition of ATP and purified 48-kDa protei …

2

Rapid affinity purification of retinal arrestin (48 kDa protein) via its light-dependent binding to phosphorylated rhodopsin.

Wilden U, Wüst E, Weyand I, Kühn H. Wilden U, et al. Among authors: kuhn h. FEBS Lett. 1986 Oct 27;207(2):292-5. doi: 10.1016/0014-5793(86)81507-1. FEBS Lett. 1986. PMID: 3770202 Free article.

3

Light-induced binding of 48-kDa protein to photoreceptor membranes is highly enhanced by phosphorylation of rhodopsin.

Kühn H, Hall SW, Wilden U. Kühn H, et al. FEBS Lett. 1984 Oct 29;176(2):473-8. doi: 10.1016/0014-5793(84)81221-1. FEBS Lett. 1984. PMID: 6436059 Free article.

4

Purification and properties of guanylate kinase from bovine retinas and rod outer segments.

Hall SW, Kühn H. Hall SW, et al. Among authors: kuhn h. Eur J Biochem. 1986 Dec 15;161(3):551-6. doi: 10.1111/j.1432-1033.1986.tb10477.x. Eur J Biochem. 1986. PMID: 3024975 Free article.

5

Deactivation of photoactivated rhodopsin by rhodopsin-kinase and arrestin.

Kühn H, Wilden U. Kühn H, et al. J Recept Res. 1987;7(1-4):283-98. doi: 10.3109/10799898709054990. J Recept Res. 1987. PMID: 3040978

6

Light-dependent phosphorylation of rhodopsin: number of phosphorylation sites.

Wilden U, Kühn H. Wilden U, et al. Among authors: kuhn h. Biochemistry. 1982 Jun 8;21(12):3014-22. doi: 10.1021/bi00541a032. Biochemistry. 1982. PMID: 6980670 No abstract available.

7

Assay of phosphorylation of rhodopsin in vitro and in vivo.

Kühn H, Wilden U. Kühn H, et al. Methods Enzymol. 1982;81:489-96. doi: 10.1016/s0076-6879(82)81066-5. Methods Enzymol. 1982. PMID: 7047991 No abstract available.

8

Interactions between photoexcited rhodopsin and GTP-binding protein: kinetic and stoichiometric analyses from light-scattering changes.

Kühn H, Bennett N, Michel-Villaz M, Chabre M. Kühn H, et al. Proc Natl Acad Sci U S A. 1981 Nov;78(11):6873-7. doi: 10.1073/pnas.78.11.6873. Proc Natl Acad Sci U S A. 1981. PMID: 6273893 Free PMC article.

9

Functional desensitization of the isolated beta-adrenergic receptor by the beta-adrenergic receptor kinase: potential role of an analog of the retinal protein arrestin (48-kDa protein).

Benovic JL, Kühn H, Weyand I, Codina J, Caron MG, Lefkowitz RJ. Benovic JL, et al. Among authors: kuhn h. Proc Natl Acad Sci U S A. 1987 Dec;84(24):8879-82. doi: 10.1073/pnas.84.24.8879. Proc Natl Acad Sci U S A. 1987. PMID: 2827157 Free PMC article.

10

Activation of retinal rod cyclic GMP-phosphodiesterase by transducin: characterization of the complex formed by phosphodiesterase inhibitor and transducin alpha-subunit.

Deterre P, Bigay J, Robert M, Pfister C, Kühn H, Chabre M. Deterre P, et al. Among authors: kuhn h. Proteins. 1986 Oct;1(2):188-93. doi: 10.1002/prot.340010210. Proteins. 1986. PMID: 2835763

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