J
Juan Codina
Researcher at Baylor College of Medicine
Publications - 104
Citations - 11229
Juan Codina is an academic researcher from Baylor College of Medicine. The author has contributed to research in topics: G protein & Adenylyl cyclase. The author has an hindex of 51, co-authored 104 publications receiving 11096 citations. Previous affiliations of Juan Codina include Baylor University.
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Journal ArticleDOI
Functional reconstitution of the alpha 2-adrenergic receptor with guanine nucleotide regulatory proteins in phospholipid vesicles.
R A Cerione,John W. Regan,H Nakata,Juan Codina,J. L. Benovic,Peter Gierschik,Robert L. Somers,Allen M. Spiegel,Lutz Birnbaumer,Robert J. Lefkowitz +9 more
TL;DR: The successful reconstitution of functional interactions between an inhibitory adenylate cyclase-coupled receptor and various nucleotide-binding regulatory proteins in phospholipid vesicles suggests both of these receptor proteins are capable of promoting the maximal activation of Ni and No while being much less effective in promoting the activation of Ns.
Journal ArticleDOI
Reconstitution of somatostatin and muscarinic receptor mediated stimulation of K+ channels by isolated GK protein in clonal rat anterior pituitary cell membranes.
TL;DR: It is demonstrated that both (SS) and acetylcholine applied through the patch pipette to the extracellular face of a patch activate a 55-picosiemens K+ channel without using a soluble second messenger and that, after patch excision, the active state of the ligand-stimulated channel is dependent on GTP in the bath.
Journal Article
Signal transduction by G proteins.
Book ChapterDOI
Regulation of hormone receptors and adenylyl cyclases by guanine nucleotide binding N proteins.
Lutz Birnbaumer,Juan Codina,Rafael Mattera,Richard A. Cerione,John D. Hildebrandt,T. Sunyer,Francisco J. Rojas,Marc G. Caron,Robert J. Lefkowitz,Ravi Iyengar +9 more
TL;DR: This chapter discusses the transduction mechanism to which Rs- and Ri-type receptors couple to modulate adenylyl cyclase activity and analyzes the known regulation of hormone-receptor interaction by the coupling proteins.
Journal ArticleDOI
A constitutively active mutant beta 2-adrenergic receptor is constitutively desensitized and phosphorylated
TL;DR: It is demonstrated that not only is the mutant beta 2AR constitutively active, it is also constitutically desensitized and down-regulated.