Browsing by Author "Codina, J"
Now showing items 1-2 of 2
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A constitutively active mutant beta 2-adrenergic receptor is constitutively desensitized and phosphorylated.
(Proc Natl Acad Sci U S A, 1994-03-29)The beta 2-adrenergic receptor (beta 2AR) can be constitutively activated by mutations in the third intracellular loop. Whereas the wild-type receptor exists predominantly in an inactive conformation (R) in the absence of ... -
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).
(Proc Natl Acad Sci U S A, 1987-12)The beta-adrenergic receptor kinase is an enzyme, possibly analogous to rhodopsin kinase, that multiply phosphorylates the beta-adrenergic receptor only when it is occupied by stimulatory agonists. Since this kinase may ...
