Zobrazeno 1 - 10
of 14
pro vyhledávání: '"Kennard A. Grimes"'
Publikováno v:
International Journal of Impotence Research. 15:369-372
Sildenafil, the active ingredient in Viagra™, ahs been purified from commercially available tablets. The purification, using Sephadex G25 chromatography under conditions of low ionic strength, is simple and inexpensive. Sildenafil purified accordin
Publikováno v:
Biochemical Journal. 372:419-426
The physiological effects of cGMP are largely determined by the activities of intracellular receptors, including cGMP-dependent protein kinase (PKG) and cGMP-binding cyclic nucleotide phosphodiesterases (PDEs), and the distribution of cGMP among thes
Autor:
Kennard A. Grimes, Paul Chang, Sharron H. Francis, Doss W. Neal, Jackie D. Corbin, Alfreda Beasley, Stephen R. Rannels
Publikováno v:
Current Medical Research and Opinion. 19:747-752
This study evaluated whether sildenafil citrate, an oral treatment for erectile dysfunction and a selective inhibitor of phosphodiesterase type 5 (PDE5) with modest vasodilating properties, affects cardiac contractility in vitro.Slices of freshly obt
Autor:
Emmanuel P. Bessay, Li Liu, Jun Kotera, W. Joseph Thompson, Kennard A. Grimes, Sharron H. Francis, Jackie D. Corbin
Publikováno v:
Journal of Biological Chemistry. 277:47581-47587
Substrate binding to the phosphodiesterase-5 (PDE5) catalytic site increases cGMP binding to the regulatory domain (R domain). The latter promotes PDE5 phosphorylation by cyclic nucleotide-dependent protein kinases, which activates catalysis, enhance
Publikováno v:
Biochemistry. 39:9591-9596
Class I cyclic nucleotide phosphodiesterases (PDEs) share a catalytic domain containing 18 invariant residues. In cGMP-binding cGMP-specific PDE (PDE5), we showed previously that point mutation of nine of these profoundly decreases k(cat) when the as
Publikováno v:
Journal of Biological Chemistry. 274:34613-34620
Phosphodiesterases (PDEs) comprise a superfamily of phosphohydrolases that degrade 3',5'-cyclic nucleotides. All known mammalian PDEs are dimeric, but the functional significance of dimerization is unknown. A deletion mutant of cGMP-binding cGMP-spec
Autor:
Illarion V. Turko, Kennard A. Grimes, Der-Ming Chu, Melissa K. Thomas, Sharron H. Francis, Tamara L. Haik, Alfreda Beasley, Jennifer L. Busch, Jackie D. Corbin
Publikováno v:
Methods. 14:81-92
Three methods have been used to assess the conformational effects associated with ligand binding to two unrelated cyclic nucleotide receptor proteins: the cGMP-binding, cGMP-specific phosphodiesterase (cGB-PDE or PDE5A) and the cGMP-dependent protein
Publikováno v:
Journal of Biological Chemistry. 272:31922-31928
Cyclic nucleotide binding activates cyclic nucleotide-dependent protein kinases, but the molecular mechanism is unknown. In the present studies, cGMP binding to type Ialpha or type Ibeta cGMP-dependent protein kinase (PKG) caused (i) a large electron
Autor:
Jeffrey A. Smith, Kenneth Walsh, Jackie D. Corbin, Santosh Kumar, Sharron H. Francis, Kennard A. Grimes, J. L. Colbran
Publikováno v:
Journal of Biological Chemistry. 271:20748-20755
Autoinhibitory domains in many protein kinases include either a phosphorylatable substrate-like sequence or a pseudosubstrate sequence. This study shows that Iβ cGMP-dependent protein kinase (cGK) autophosphorylates Ser-63, which is in an atypical c
Autor:
Mitsi A. Blount, Jackie D. Corbin, Alfreda Beasley, Roya Zoraghi, Sharron H. Francis, Kennard A. Grimes, Emmanuel P. Bessay
Publikováno v:
The Journal of pharmacology and experimental therapeutics. 325(1)
Phosphodiesterase-5 (PDE5) is phosphorylated at a single serine residue by cyclic nucleotide-dependent protein kinases. To test for a direct effect of phosphorylation on the PDE5 catalytic site, independent of cGMP binding to the allosteric sites of