H. Kühn

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

Ursula Wilden, S W Hall, H. Kühn · Proceedings of the National Academy of Sciences · 1986 · 793 citations · Full text

Life Sciences, Biochemistry, Molecular Biology +16

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).

Jeffrey Benovic, H. Kühn, Ingo Weyand et al. · Proceedings of the National Academy of Sciences · 1987 · 489 citations · Full text

Life Sciences, Biochemistry, Physiology +16

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

H. Kühn, S W Hall, Ursula Wilden · FEBS Letters · 1984 · 370 citations

Life Sciences, Biochemistry, Molecular Biology +14

Complex formation between metarhodopsin II and GTP‐binding protein in bovine protoreceptor membranes leads to a shift of the photoproduct equilibrium

D. Emeis, H. Kühn, J. Reichert et al. · FEBS Letters · 1982 · 261 citations

Life Sciences, Biochemistry, Biophysics +9

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

H. Kühn, Nelly Bennett, M. Michel-Villaz et al. · Proceedings of the National Academy of Sciences · 1981 · 249 citations · Full text

Natural Sciences, Biochemistry, Biophysics +15