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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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The stimulatory G protein of adenylyl cyclase, Gs, also stimulates dihydropyridine-sensitive Ca2+ channels. Evidence for direct regulation independent of phosphorylation by cAMP-dependent protein kinase or stimulation by a dihydropyridine agonist.

TL;DR: It is concluded that the responses seen are due to Gs rather than a contaminant, that the effect on Ca2+ channel activity is that of a true stimulation, akin to that on adenylyl cyclase, and that a given G protein may regulate more than one effector system.
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The mammalian beta 2-adrenergic receptor: reconstitution of functional interactions between pure receptor and pure stimulatory nucleotide binding protein of the adenylate cyclase system

TL;DR: The established hormone responsive activity retains the beta 2-adrenergic specificity conferred by the pure receptor, and similar extents of stimulation are observed with pure receptor from frog erythrocytes, indicating a similar efficiency of coupling between receptors from different species and NS.
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Newly identified brain potassium channels gated by the guanine nucleotide binding protein Go

TL;DR: Brain Go can couple diverse brain potassium channels to neurotransmitter receptors, and four distinct types of potassium channels were activated by both isolated brain G0 and recombinant Go alpha.
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Pertussis toxin substrate, the putative Ni component of adenylyl cyclases, is an alpha beta heterodimer regulated by guanine nucleotide and magnesium

TL;DR: This work believes that it has purified a guanine nucleotide- and Mg2+-binding inhibitory regulatory component of adenylyl cyclases--i.e., the Ni.
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Ns and Ni, the stimulatory and inhibitory regulatory components of adenylyl cyclases. Purification of the human erythrocyte proteins without the use of activating regulatory ligands.

TL;DR: Methods were developed to adequately extract, separate and, without the use of NaF as stabilizing agent, purify to better than 90% purity human erythrocyte Ns and Ni, the stimulatory and inhibitory guanine nucleotide- and Mg-binding regulatory components of adenylyl cyclases, as well as a protein containing Mr = 35,000 subunits.