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
At least three alternatively spliced mRNAs encoding two alpha subunits of the Go GTP-binding protein can be expressed in a single tissue.
TL;DR: It is demonstrated that untranslated regions of mRNAs need not exhibit high degrees of species variation, and that the sequences of the untrans translated regions are highly conserved among three species (rat, hamster, and brain).
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Guanosine 5'-O-(3-thiotriphosphate) reduces ADP-ribosylation of the inhibitory guanine nucleotide-binding regulatory protein of adenylyl cyclase (Ni) by pertussis toxin without causing dissociation of the subunits of Ni. Evidence of existence of heterotrimeric pt+ and pt- conformations of Ni.
TL;DR: Two conformations of heterotrimeric Ni are defined: one -pt+, ADP-ribosylated by pertussis toxin, and the other pt-, poorly or not ADP
Journal ArticleDOI
Requirement for intramolecular domain interaction in activation of G protein alpha subunit by aluminum fluoride and GDP but not by GTP gamma S.
Juan Codina,Lutz Birnbaumer +1 more
TL;DR: An ion-counterion interaction between the lysine of the NKXD motif in the GTPase domain and an aspartate in the inserted helical domain of alpha subunits of heterotrimeric G proteins is shown to be essential for activation by AlF4- and partially so for interaction with beta gamma dimers and activation by GTP and receptor.
Journal ArticleDOI
Transducin and the inhibitory nucleotide regulatory protein inhibit the stimulatory nucleotide regulatory protein mediated stimulation of adenylate cyclase in phospholipid vesicle systems.
Richard A. Cerione,Juan Codina,Brian F. Kilpatrick,Claudia Staniszewski,Peter Gierschik,Robert L. Somers,Allen M. Spiegel,Lutz Birnbaumer,Marc G. Caron,Robert J. Lefkowitz +9 more
TL;DR: As is the case in intact membranes, the reconstituted inhibition of the Ns-stimulated C activity extends into the steady-state phase of time courses of activity and is highly sensitive to the MgCl2 concentration.
Journal Article
Peptide inhibitors of ADP-ribosylation by pertussis toxin are substrates with affinities comparable to those of the trimeric GTP-binding proteins.
TL;DR: It is reported the rather unexpected discovery that synthetic peptides encompassing the last 10-20 amino acids of alpha subunits of PTX-sensitive G proteins are substrates for PTX by themselves and in the absence of beta gamma dimers.