Zobrazeno 1 - 10
of 21
pro vyhledávání: '"Alfreda Beasley"'
Publikováno v:
Biochemical and Biophysical Research Communications. 334:930-938
[3H]Vardenafil (Levitra) or [3H]tadalafil (Cialis) binding was used to quantify PDE5 in rat lung and heart tissue. Each radioligand bound to purified recombinant phosphodiesterase-5 (PDE5) or to PDE5 in crude extracts with strong affinity, high speci
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5c92d2e0d2e830c995a58a83b343ddb0
https://doi.org/10.1016/j.bbrc.2005.06.183
https://doi.org/10.1016/j.bbrc.2005.06.183
Autor:
Jackie D. Corbin, Roya Zoraghi, James L. Weeks, Sharron H. Francis, Alfreda Beasley, Konjeti R. Sekhar
Publikováno v:
International Journal of Impotence Research. 17:5-9
The physiological role of phosphodiesterase (PDE)11 is unknown and its biochemical characteristics are poorly understood. We have expressed human His-tagged PDE11A4 and purified the enzyme to apparent homogeneity. PDE11A4 displays K(m) values of 0.97
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c2c913c369a08abdc46c2d96cc494a64
https://doi.org/10.1038/sj.ijir.3901283
https://doi.org/10.1038/sj.ijir.3901283
Autor:
James L. Weeks, Karl P. Kuhn, Layla F. Saidi, Jackie D. Corbin, Mitsi A. Blount, Yew Seng Jonathan Ho, Alfreda Beasley, James H. Hurley, Sharron H. Francis, Jun Kotera
Publikováno v:
Molecular Pharmacology. 63:1364-1372
Sildenafil (Viagra) potentiates penile erection by acting as a nonhydrolyzable analog of cGMP and competing with this nucleotide for catalysis by phosphodiesterase-5 (PDE5), but the characteristics of direct binding of radiolabeled sildenafil to PDE5
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f9373ca23a8cb017ee313e22095103a8
https://doi.org/10.1124/mol.63.6.1364
https://doi.org/10.1124/mol.63.6.1364
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
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3d2746860ca3ca1b3f7c471534204ce6
https://doi.org/10.1185/030079903125002522
https://doi.org/10.1185/030079903125002522
Publikováno v:
European Journal of Biochemistry. 267:2760-2767
In addition to its cGMP-selective catalytic site, cGMP-binding cGMP-specific phosphodiesterase (PDE5) contains two allosteric cGMP-binding sites and at least one phosphorylation site (Ser92) on each subunit [Thomas, M.K., Francis, S.H. & Corbin, J.D.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::999458f99a85a8c0aae1661aefd10dbc
https://doi.org/10.1046/j.1432-1327.2000.01297.x
https://doi.org/10.1046/j.1432-1327.2000.01297.x
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
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a1be2726b3cb7609581e66f12f7439d8
https://doi.org/10.1074/jbc.274.49.34613
https://doi.org/10.1074/jbc.274.49.34613
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
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3fea35072d8cf26ee5f3764c86ece9e6
https://doi.org/10.1006/meth.1997.0567
https://doi.org/10.1006/meth.1997.0567
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
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a1b431c6962acd50091d919fb5fe89f1
https://pubmed.ncbi.nlm.nih.gov/18199808
https://pubmed.ncbi.nlm.nih.gov/18199808
Autor:
Alfreda Beasley, Roya Zoraghi, Jackie D. Corbin, Mitsi A. Blount, Sharron H. Francis, Emmanuel P. Bessay
Publikováno v:
The Journal of pharmacology and experimental therapeutics. 323(2)
Phosphodiesterase-5 (PDE5) specifically hydrolyzes cGMP, thereby contributing to modulation of intracellular levels of this nucleotide. In the present study, preincubation with cGMP increased PDE5 catalytic activity for cGMP degradation, and it conve
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::99018983815839109598ca95792e97d9
https://pubmed.ncbi.nlm.nih.gov/17690252
https://pubmed.ncbi.nlm.nih.gov/17690252
Autor:
James L, Weeks, Mitsi A, Blount, Alfreda, Beasley, Roya, Zoraghi, Melissa K, Thomas, Konjeti Raja, Sekhar, Jackie D, Corbin, Sharron H, Francis
Publikováno v:
Methods in molecular biology (Clifton, N.J.). 307
Cyclic nucleotide phosphodiesterases (PDEs) have been investigated for years as targets for therapeutic intervention in a number of pathophysiological processes. Phosphodiesterase-5 (PDE5), which is highly specific for guanosine 3'-5'-cyclic-monophos
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::6554f648b47990e74cc130baca17cf6d
https://pubmed.ncbi.nlm.nih.gov/15988068
https://pubmed.ncbi.nlm.nih.gov/15988068