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Molecular cloning and expression of the cDNA for the hamster alpha 1-adrenergic receptor.
(Proc Natl Acad Sci U S A, 1988-10)
The cDNA for the Syrian hamster alpha 1-adrenergic receptor has been cloned with oligonucleotides
corresponding to the partial amino acid sequence of the receptor protein purified
from DDT1MF-2 smooth muscle cells. The deduced ...
cAMP stimulates transcription of the beta 2-adrenergic receptor gene in response to short-term agonist exposure.
(Proc Natl Acad Sci U S A, 1989-07)
In addition to conveying cellular responses to an effector molecule, receptors are
often themselves regulated by their effectors. We have demonstrated that epinephrine
modulates both the rate of transcription of the beta ...
Phorbol esters promote alpha 1-adrenergic receptor phosphorylation and receptor uncoupling from inositol phospholipid metabolism.
(Proc Natl Acad Sci U S A, 1985-09)
DDT1 MF-2 cells, which are derived from hamster vas deferens smooth muscle, contain
alpha 1-adrenergic receptors (54,800 +/- 2700 sites per cell) that are coupled to
stimulation of inositol phospholipid metabolism. Incubation ...
cDNA for the human beta 2-adrenergic receptor: a protein with multiple membrane-spanning domains and encoded by a gene whose chromosomal location is shared with that of the receptor for platelet-derived growth factor.
(Proc Natl Acad Sci U S A, 1987-01)
We have isolated and sequenced a cDNA encoding the human beta 2-adrenergic receptor.
The deduced amino acid sequence (413 residues) is that of a protein containing seven
clusters of hydrophobic amino acids suggestive of ...
Beta-adrenergic receptor kinase: identification of a novel protein kinase that phosphorylates the agonist-occupied form of the receptor.
(Proc Natl Acad Sci U S A, 1986-05)
Agonist-promoted desensitization of adenylate cyclase is intimately associated with
phosphorylation of the beta-adrenergic receptor in mammalian, avian, and amphibian
cells. However, the nature of the protein kinase(s) involved ...
Inhibition of beta-adrenergic receptor kinase prevents rapid homologous desensitization of beta 2-adrenergic receptors.
(Proc Natl Acad Sci U S A, 1989-05)
Homologous (agonist-specific) desensitization of beta-adrenergic receptors (beta ARs)
is accompanied by and appears to require phosphorylation of the receptors. We have
recently described a novel protein kinase, beta AR ...