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Functionally active targeting domain of the beta-adrenergic receptor kinase: an inhibitor of G beta gamma-mediated stimulation of type II adenylyl cyclase. 

Inglese, J; Luttrell, LM; Iñiguez-Lluhi, JA; Touhara, K; Koch, WJ; Lefkowitz, RJ (Proc Natl Acad Sci U S A, 1994-04-26)
The beta-adrenergic receptor kinase (beta ARK) phosphorylates its membrane-associated receptor substrates, such as the beta-adrenergic receptor, triggering events leading to receptor desensitization. beta ARK activity is ...

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AuthorInglese, J (1)Iñiguez-Lluhi, JA (1)
Koch, WJ (1)
Lefkowitz, RJ (1)
Luttrell, LM (1)
Touhara, K (1)Date Issued
1994 (1)
Type
Journal article (1)
SubjectAdenylate Cyclase Toxin (1)
Adenylyl Cyclases (1)
Amino Acid Sequence (1)
Animals (1)beta-Adrenergic Receptor Kinases (1)Binding Sites (1)Circular Dichroism (1)
Cyclic AMP-Dependent Protein Kinase Type II (1)
Cyclic AMP-Dependent Protein Kinases (1)
Enzyme Activation (1)
... View MoreAffiliation of Duke Author(s)Basic Science Departments (1)
Biochemistry (1)
Chemistry (1)
Clinical Science Departments (1)
Duke (1)
Duke Cancer Institute (1)Institutes and Centers (1)
Medicine (1)
Medicine, Cardiology (1)
Pathology (1)
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