Binding of GTP to transducin is not inhibited by arrestin and phosphorylated rhodopsin

[1]  Y. Fukada,et al.  Beta gamma-subunit of bovine transducin composed of two components with distinctive gamma-subunits. , 1989, The Journal of biological chemistry.

[2]  N. Bennett,et al.  Inactivation of photoexcited rhodopsin in retinal rods: the roles of rhodopsin kinase and 48-kDa protein (arrestin). , 1988, Biochemistry.

[3]  I. Weyand,et al.  Rapid affinity purification of retinal arrestin (48 kDa protein) via its light‐dependent binding to phosphorylated rhodopsin , 1986, FEBS letters.

[4]  R. Zuckerman,et al.  A 48 kDa protein arrests cGMP phosphodiesterase activation in retinal rod disk membranes , 1986, FEBS letters.

[5]  A. Sitaramayya.  Rhodopsin kinase prepared from bovine rod disk membranes quenches light activation of cGMP phosphodiesterase in a reconstituted system. , 1986, Biochemistry.

[6]  S. W. Hall,et al.  Phosphodiesterase activation by photoexcited rhodopsin is quenched when rhodopsin is phosphorylated and binds the intrinsic 48-kDa protein of rod outer segments. , 1986, Proceedings of the National Academy of Sciences of the United States of America.

[7]  C. Craft,et al.  Sequence analysis of bovine retinal S‐antigen , 1986 .

[8]  S. W. Hall,et al.  Light‐induced binding of 48‐kDa protein to photoreceptor membranes is highly enhanced by phosphorylation of rhodopsin , 1984, FEBS letters.

[9]  U Wilden,et al.  Light-dependent phosphorylation of rhodopsin: number of phosphorylation sites. , 1982, Biochemistry.

[10]  L. Stryer,et al.  Photolyzed rhodopsin catalyzes the exchange of GTP for bound GDP in retinal rod outer segments. , 1980, Proceedings of the National Academy of Sciences of the United States of America.

[11]  U. K. Laemmli,et al.  Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4 , 1970, Nature.