Vanderbilt University School of Medicine

Francis, Sharron H. , Ph.D.
Adjunct Professor of Molecular Physiology and Biophysics

Lab Url: N/A

Phone Number: 615-322-4383

Email Address:sharon.h.francis@Vanderbilt.Edu

Francis, Sharron's picture

Office Address   Mailing Address

766-B Medical Research Building I

766 RRB 0615


Research Keywords
Cyclic Nucleotide Phosphodiesterases, Cyclic GMP- and AMP- dependent Protein Kinases, Signal Transduction, Smooth Muscle Relaxation

Research Specialty
Cyclic Nucleotide Signaling Pathways

Research Description
We are studying the mechanisms that cells use to regulate metabolism and cell function in response to physiological stimuli such as hormones, neurotransmitters, and other signals. These agents work by eliciting changes in the levels of specific intracellular molecules known as second messengers, and these second messengers interact with cellular proteins to bring about changes in carbohydrate and fat metabolism, cardiovascular function, gene expression, and myriad other processes. Cyclic nucleotides, cyclic AMP and cyclic GMP, are important second messengers that are involved in all these processes, and these nucleotides bind to specific intracellular protein receptors which then bring about the changes in cellular function.


In particular, we study two families of intracellular receptors for cyclic nucleotides, cyclic nucleotide-dependent protein kinases and cyclic nucleotide phosphodiesterases. These proteins are present in all mammalian cells and play central roles in integrating the regulation of cellular metabolism. We are interested in determining how these protein families function in the cell to modulate the tissues? physiological responses, how their functions relate to one another, and how these processes are altered in pathological states such as hypertension, asthma, diabetes, and male impotence. We also study these proteins at the molecular level using both purified proteins, as well as proteins that have been modified using site-directed mutagenesis, in order to determine the mechanisms that are critical to determining protein function.


Publications
Bessay, EP, Zoraghi, R, Blount, MA, Grimes, KA, Beasley, A, Francis, SH, Corbin, JD. Phosphorylation of phosphodiesterase-5 is promoted by a conformational change induced by sildenafil, vardenafil, or tadalafil. Front Biosci, 12, 1899-910, 2007.

Blount, MA, Zoraghi, R, Ke, H, Bessay, EP, Corbin, JD, Francis, SH. A 46-amino acid segment in phosphodiesterase-5 GAF-B domain provides for high vardenafil potency over sildenafil and tadalafil and is involved in phosphodiesterase-5 dimerization. Mol Pharmacol, 70(5), 1822-31, 2006.

Richie-Jannetta, R, Busch, JL, Higgins, KA, Corbin, JD, Francis, SH. Isolated regulatory domains of cGMP-dependent protein kinase Ialpha and Ibeta retain dimerization and native cGMP-binding properties and undergo isoform-specific conformational changes. J Biol Chem, 281(11), 6977-84, 2006.

Zoraghi, R, Corbin, JD, Francis, SH. Phosphodiesterase-5 Gln817 is critical for cGMP, vardenafil, or sildenafil affinity: its orientation impacts cGMP but not cAMP affinity. J Biol Chem, 281(9), 5553-8, 2006.

Corbin, JD, Beasley, A, Blount, MA, Francis, SH. High lung PDE5: a strong basis for treating pulmonary hypertension with PDE5 inhibitors. Biochem Biophys Res Commun, 334(3), 930-8, 2005.

Francis, SH. Phosphodiesterase 11 (PDE11): is it a player in human testicular function. Int J Impot Res, 17(5), 467-8, 2005.

Francis, SH, Blount, MA, Zoraghi, R, Corbin, JD. Molecular properties of mammalian proteins that interact with cGMP: protein kinases, cation channels, phosphodiesterases, and multi-drug anion transporters. Front Biosci, 10, 2097-117, 2005.

Francis, SH, Corbin, JD. Sildenafil: efficacy, safety, tolerability and mechanism of action in treating erectile dysfunction. Expert Opin Drug Metab Toxicol, 1(2), 283-93, 2005.

Francis, SH, Corbin, JD. Phosphodiesterase-5 inhibition: the molecular biology of erectile function and dysfunction. Urol Clin North Am, 32(4), 419-29, vi, 2005.

Weeks, JL, Blount, MA, Beasley, A, Zoraghi, R, Thomas, MK, Sekhar, KR, Corbin, JD, Francis, SH. Radiolabeled ligand binding to the catalytic or allosteric sites of PDE5 and PDE11. Methods Mol Biol, 307, 239-62, 2005.

Zoraghi, R, Bessay, EP, Corbin, JD, Francis, SH. Structural and functional features in human PDE5A1 regulatory domain that provide for allosteric cGMP binding, dimerization, and regulation. J Biol Chem, 280(12), 12051-63, 2005.

Blount, MA, Beasley, A, Zoraghi, R, Sekhar, KR, Bessay, EP, Francis, SH, Corbin, JD. Binding of tritiated sildenafil, tadalafil, or vardenafil to the phosphodiesterase-5 catalytic site displays potency, specificity, heterogeneity, and cGMP stimulation. Mol Pharmacol, 66(1), 144-52, 2004.

Corbin, JD, Beasley, A, Blount, MA, Francis, SH. Vardenafil: structural basis for higher potency over sildenafil in inhibiting cGMP-specific phosphodiesterase-5 (PDE5). Neurochem Int, 45(6), 859-63, 2004.

Kotera, Jun, Francis, Sharron H, Grimes, Kennard A, Rouse, Alfreda, Blount, Mitsi A, Corbin, Jackie D. Allosteric sites of phosphodiesterase-5 sequester cyclic GMP. Front Biosci, 9, 378-86, 2004.

Weeks, JL, Zoraghi, R, Beasley, A, Sekhar, KR, Francis, SH, Corbin, JD. High biochemical selectivity of tadalafil, sildenafil and vardenafil for human phosphodiesterase 5A1 (PDE5) over PDE11A4 suggests the absence of PDE11A4 cross-reaction in patients. Int J Impot Res, 17(1), 5-9, 2004.

Zhu, CB, Hewlett, WA, Francis, SH, Corbin, JD, Blakely, RD. Stimulation of serotonin transport by the cyclic GMP phosphodiesterase-5 inhibitor sildenafil. Eur J Pharmacol, 504(1-2), 1-6, 2004.

Zoraghi, Roya, Corbin, Jackie D, Francis, Sharron H. Properties and functions of GAF domains in cyclic nucleotide phosphodiesterases and other proteins. Mol Pharmacol, 65(2), 267-78, 2004.

Corbin, Jackie D, Blount, Mitsi A, Weeks, James L, Beasley, Alfreda, Kuhn, Karl P, Ho, Yew S J, Saidi, Layla F, Hurley, James H, Kotera, Jun, Francis, Sharron H. [3H]sildenafil binding to phosphodiesterase-5 is specific, kinetically heterogeneous, and stimulated by cGMP. Mol Pharmacol, 63(6), 1364-72, 2003.

Corbin, Jackie D, Francis, Sharron H. Molecular biology and pharmacology of PDE-5-inhibitor therapy for erectile dysfunction. J Androl, 24(6 Suppl), S38-41, 2003.

Francis, S H, Sekhar, K Raja, Rouse, A B, Grimes, K A, Corbin, J D. Single step isolation of sildenafil from commercially available Viagra tablets. Int J Impot Res, 15(5), 369-72, 2003.

Francis, Sharron H, Corbin, Jackie D. Molecular mechanisms and pharmacokinetics of phosphodiesterase-5 antagonists. Curr Urol Rep, 4(6), 457-65, 2003.

Kotera, Jun, Grimes, Kennard A, Corbin, Jackie D, Francis, Sharron H. cGMP-dependent protein kinase protects cGMP from hydrolysis by phosphodiesterase-5. Biochem J, 372(Pt 2), 419-26, 2003. PMCID:1223414

Richie-Jannetta, Robyn, Francis, Sharron H, Corbin, Jackie D. Dimerization of cGMP-dependent protein kinase Ibeta is mediated by an extensive amino-terminal leucine zipper motif, and dimerization modulates enzyme function. J Biol Chem, 278(50), 50070-9, 2003.

Francis, S.H. and Corbin, J.D. (2000) Structure and function of cyclic nucleotide phosphodiesterases. In:Progress in Nucleic Acid Research and Molecular Biology, W. E. Cohn and K. Moldavie, Eds. Academic Press (in press).

Francis, S.H., Turko, I.V., Grimes, K.A., and Corbin, J.D.Histidine-607 and histidine-643 provide important interactions for metal support of catalysis in phosphodiesterase-5. Biochemistry (in press).

Busch, Jennifer L, Bessay, Emmanuel P, Francis, Sharron H, Corbin, Jackie D. A conserved serine juxtaposed to the pseudosubstrate site of type I cGMP-dependent protein kinase contributes strongly to autoinhibition and lower cGMP affinity. J Biol Chem, 277(37), 34048-54, 2002.

Corbin, J D, Francis, S H. Pharmacology of phosphodiesterase-5 inhibitors. Int J Clin Pract, 56(6), 453-9, 2002.

Corbin, Jackie D, Francis, Sharron H, Webb, David J. Phosphodiesterase type 5 as a pharmacologic target in erectile dysfunction. Urology, 60(2 Suppl 2), 4-11, 2002.

Francis, Sharron H, Bessay, Emmanuel P, Kotera, Jun, Grimes, Kennard A, Liu, Li, Thompson, W Joseph, Corbin, Jackie D. Phosphorylation of isolated human phosphodiesterase-5 regulatory domain induces an apparent conformational change and increases cGMP binding affinity. J Biol Chem, 277(49), 47581-7, 2002.

Francis, Sharron H, Poteet-Smith, Celeste, Busch, Jennifer L, Richie-Jannetta, Robyn, Corbin, Jackie D. Mechanisms of autoinhibition in cyclic nucleotide-dependent protein kinases. Front Biosci, 7, d580-92, 2002.

Francis, S H, Turko, I V, Corbin, J D. Cyclic nucleotide phosphodiesterases: relating structure and function. Prog Nucleic Acid Res Mol Biol, 65, 1-52, 2001.

Gopal, V K, Francis, S H, Corbin, J D. Allosteric sites of phosphodiesterase-5 (PDE5). A potential role in negative feedback regulation of cGMP signaling in corpus cavernosum. Eur J Biochem, 268(11), 3304-12, 2001.

Corbin, J D, Turko, I V, Beasley, A, Francis, S H. Phosphorylation of phosphodiesterase-5 by cyclic nucleotide-dependent protein kinase alters its catalytic and allosteric cGMP-binding activities. Eur J Biochem, 267(9), 2760-7, 2000.

Corbin, J.D., Turko, I.V., Beasley, A., and Francis, S.H. Phosphorylation by cGMP-dependent protein kinase causes activation of phosphodiesterase-5. Eur. J. Biochem. , 267, 2760-2767, 2000.

Francis, S H, Turko, I V, Grimes, K A, Corbin, J D. Histidine-607 and histidine-643 provide important interactions for metal support of catalysis in phosphodiesterase-5. Biochemistry, 39(31), 9591-6, 2000.

Smith, J A, Reed, R B, Francis, S H, Grimes, K, Corbin, J D. Distinguishing the roles of the two different cGMP-binding sites for modulating phosphorylation of exogenous substrate (heterophosphorylation) and autophosphorylation of cGMP-dependent protein kinase. J Biol Chem, 275(1), 154-8, 2000.

Smith, J.A., Reed, R.B., Grimers, K.A., Francis, S.H., and Corbin, J.D. Distinguishing the roles of the two different cGMP-binding sites for modulating phosphoryaltion of exogenous substrate (heterophosphorylation) and autophosphorylation of cGMP-dependent protein kinases. J. Biol. Chem., 275, 154-158, 2000.

Corbin, J D, Francis, S H. Cyclic GMP phosphodiesterase-5: target of sildenafil. J Biol Chem, 274(20), 13729-32, 1999.

Corbin, J.D. and Francis, S.H. Cyclic GMP phosphodiesterase-5:target of sildenafil. J.Biol. Chem., 274, 13729-13732, 1999.

Fink, T L, Francis, S H, Beasley, A, Grimes, K A, Corbin, J D. Expression of an active, monomeric catalytic domain of the cGMP-binding cGMP-specific phosphodiesterase (PDE5). J Biol Chem, 274(49), 34613-20, 1999.

Fink, T.L., Francis, S.H., Beasley, A., Grimes, K.A., and Corbin, J.D. Expression of a fully active, monomeric catalytic domain of the cGMP-binding cGMP-specific phosphodiesterase (PDE5). J. Biol. Chem., 274, 34613-34620, 1999.

Francis, S H, Corbin, J D. Cyclic nucleotide-dependent protein kinases: intracellular receptors for cAMP and cGMP action. Crit Rev Clin Lab Sci, 36(4), 275-328, 1999.

Francis, S.H. and Corbin, J.D. Cyclic nucleotide-dependent protein kinases:intracellular receptors for cAMP and cGMP action. Crit. Rev. Clin. Lab. Sci., 36(4), 275-328, 1999.

Francis, S.H., Chu, D-M., Thomas, M.K., Beasley, A., Grimes, K.A., Busch, J.L., Turko, I.V., Haik, T.L., and Corbin, J.D. Ligand-induced conformational changes in cyclic nucleotide phosphodiesterases and cyclic nucleotide-dependent protein kinases. METHODS: A Companion to Methods in Enzymology: Methods in Phophodiesterase Research?, M. Conti, ed., Academic Press, New York , , 81-92, 1999.

Turko, I V, Ballard, S A, Francis, S H, Corbin, J D. Inhibition of cyclic GMP-binding cyclic GMP-specific phosphodiesterase (Type 5) by sildenafil and related compounds. Mol Pharmacol, 56(1), 124-30, 1999.

Turko, I V, Francis, S H, Corbin, J D. Studies of the molecular mechanism of discrimination between cGMP and cAMP in the allosteric sites of the cGMP-binding cGMP-specific phosphodiesterase (PDE5). J Biol Chem, 274(41), 29038-41, 1999.

Turko, I.V., Ballard, S.A., Francis, S.H., and Corbin, J.D. Inhibition of cyclic GMP-binding cGMP specific phosphodiesterase (type 5) by sildenafil and related compounds. Mol. Pharm., 56, 124-130, 1999.

Turko, I.V., Francis, S.H., and Corbin, J.D. Studies of the molecular mechanism of discrimination between cGMP and cAMP in the allosteric sites of the cGMP-binding cGMP-specific phosphodiesterase (PDE5). J. Biol. Chem., 274, 29038-29041, 1999.

Wallis, R.M., Corbin, J.D., Francis, S.H., and Ellis, P. Tissue distribution of phosphodiesterase families and the effects of sildenafil on tissue cyclic nucleotides, platelet function, and the contractile responses of trabeculae carneae and aortic rings in vitro. Am. J. Cardiol., 84(5A), 3C-12C, 1999.

Chu, D-M., Francis, S.H., Thomas, J., Maksymovitch, E., and Corbin, J.D. (1998) Activation by autophosphorylation or cGMP binding produces a similar apparent conformational change in cGMP-dependent protein kinase. J. Biol. Chem. 273:14649-14656.

Chu, D M, Francis, S H, Thomas, J W, Maksymovitch, E A, Fosler, M, Corbin, J D. Activation by autophosphorylation or cGMP binding produces a similar apparent conformational change in cGMP-dependent protein kinase. J Biol Chem, 273(23), 14649-56, 1998.

Corbin, J D, Beasley, A, Turko, I V, Haik, T L, Mangum, K A, Wells, J N, Francis, S H, Sekhar, K R. A photoaffinity probe covalently modifies the catalytic site of the cGMP-binding cGMP-specific phosphodiesterase (PDE-5). Cell Biochem Biophys, 29(1-2), 145-57, 1998.

Corbin, J.D., Beasley, A., Turko, I.V., Haik, T.L., Mangum, K.A., Wells, J.N., Francis, S.H., and Sekhar, K.R. A photoaffinity probe covalently modifies the catalytic site of the cGMP-binding phosphodiesterase (PDE5). Cell Biochem. and Biophys., 29, 145-157, 1998.

Francis, S H, Chu, D M, Thomas, M K, Beasley, A, Grimes, K, Busch, J L, Turko, I V, Haik, T L, Corbin, J D. Ligand-induced conformational changes in cyclic nucleotide phosphodiesterases and cyclic nucleotide-dependent protein kinases. Methods, 14(1), 81-92, 1998.

Granovsky, A.E., Natochin, M., McEntaffer, R., Haik, T.L., Francis, S.H., Corbin, J.D., and Artemyev, N.O. Probing domain functions of chimeric PDE6a ?/PDE5 cGMP-phosphodiesterase. J. Biol. Chem., 273, 24485-24490, 1998.

Loughney, K., Hill, T.R., Florio, V.A., Uher, L., Rosman, G.J., Wolda, S.L., Jones, B.A., Howard, M.L., McAllister-Lucas, L.M., Sonnenberg, W.K., Francis, S.H., Corbin, J.D., Beavo, J.A., and Ferguson, K. Isolation and characterization of cDNAs encoding PDE5A, a human cGMP-binding, cGMP-specific 3', 5'-cyclic nucleotide phosphodiesterase. Gene, 216, 139-147, 1998.

Turko, I V, Francis, S H, Corbin, J D. Potential roles of conserved amino acids in the catalytic domain of the cGMP-binding cGMP-specific phosphodiesterase. J Biol Chem, 273(11), 6460-6, 1998.

Turko, I V, Francis, S H, Corbin, J D. Binding of cGMP to both allosteric sites of cGMP-binding cGMP-specific phosphodiesterase (PDE5) is required for its phosphorylation. Biochem J, 329 ( Pt 3), 505-10, 1998. PMCID:1219070

Turko, I V, Francis, S H, Corbin, J D. Hydropathic analysis and mutagenesis of the catalytic domain of the cGMP-binding cGMP-specific phosphodiesterase (PDE5). cGMP versus cAMP substrate selectivity. Biochemistry, 37(12), 4200-5, 1998.

Turko, I.V., Francis, S.H. and Corbin, J.D. Binding of cGMP to both binding sites of cGMP-binding cGMP-specific phosphodiesterase is required for its phosphorylation. Biochemical J, 505-510, 329, 1998.

Turko, I.V., Francis, S.H., and Corbin, J.D. Hydropathic analysis and mutagenesis of the catalytic domain of the cGMP-binding cGMP-specific phosphodiesterase (PDE5). cGMP versus cAMP substrate specificity. Biochemistry, 37, 4200-4205, 1998.

Turko, I.V., Francis, S.H., and Corbin, J.D . The potential roles of conserved amino acids in the catalytic domain of the cGMP-binding cGMP-specific phosphodiesterase (PDE5). J. Biol. Chem, 273, 6460-6466, 1998.

Wyatt, T A, Naftilan, A J, Francis, S H, Corbin, J D. ANF elicits phosphorylation of the cGMP phosphodiesterase in vascular smooth muscle cells. Am J Physiol, 274(2 Pt 2), H448-55, 1998.

Chu, D M, Corbin, J D, Grimes, K A, Francis, S H. Activation by cyclic GMP binding causes an apparent conformational change in cGMP-dependent protein kinase. J Biol Chem, 272(50), 31922-8, 1997.

Poteet-Smith, C E, Corbin, J D, Francis, S H. The pseudosubstrate sequences alone are not sufficient for potent autoinhibition of cAMP- and cGMP-dependent protein kinases as determined by synthetic peptide analysis. Adv Second Messenger Phosphoprotein Res, 31, 219-35, 1997.

Poteet-Smith, C E, Shabb, J B, Francis, S H, Corbin, J D. Identification of critical determinants for autoinhibition in the pseudosubstrate region of type I alpha cAMP-dependent protein kinase. J Biol Chem, 272(1), 379-88, 1997.

Reed, R B, Sandberg, M, Jahnsen, T, Lohmann, S M, Francis, S H, Corbin, J D. Structural order of the slow and fast intrasubunit cGMP-binding sites of type I alpha cGMP-dependent protein kinase. Adv Second Messenger Phosphoprotein Res, 31, 205-17, 1997.

Reed, R.B., Sandberg, M., Jahnsen, T., Lohmann, S.M., Francis, S.H., and Corbin, J.D. Structural order of the slow and fast intrasubunit cGMP-binding sites of type I ? cGMP-dependent protein kinase. Adv. in Second Mess. and Phosphoproteins, 31, 205-217, 1997.

Smith, C.P., Corbin, J.D., and Francis, S.H. Autoinhibition of cAMP- and cGMP- dependent protein kinases involves multiple structural components as determined by synthetic peptide analysis. Signal , , 219-235, 1997.

Wyatt, T.A., Naftilan, A.J., Francis, S.H., and Corbin, J.D. ANF elicits phosphorylation of the cGMP phosphodiesterase (PDE5) in vascular smooth muscle cells. Am. J. Physiol, 273, H448-H455, 1997.

Zhao, J., Trewhella, J., Corbin, J.D., Francis, S.H., Mitchell, R., Brushia, R., and Walsh, D. Progressive cyclic nucleotide-induced conformational changes in the cGMP-dependent protein kinase studied by small angle x-ray scattering in solution. J. Biol. Chem., 272, 31929-31936, 1997.

Francis, S H, Smith, J A, Colbran, J L, Grimes, K, Walsh, K A, Kumar, S, Corbin, J D. Arginine 75 in the pseudosubstrate sequence of type Ibeta cGMP-dependent protein kinase is critical for autoinhibition, although autophosphorylated serine 63 is outside this sequence. J Biol Chem, 271(34), 20748-55, 1996.

Francis, S.H., Smith, J.A., Colbran, J.L., Grimes, K., Walsh, K.A., Kumar, S., and Corbin, J.D. Arginine-75 in the Pseudosubstrate Sequence of Type Ib cGMP-Dependent Protein Kinase Is Critical for Autoinhibition, Although Autophosphory- lated Serine-63 Is Outside This Sequence. J. Biol. Chem., 271, 20748-20755, 1996.

Reed, R B, Sandberg, M, Jahnsen, T, Lohmann, S M, Francis, S H, Corbin, J D. Fast and slow cyclic nucleotide-dissociation sites in cAMP-dependent protein kinase are transposed in type Ibeta cGMP-dependent protein kinase. J Biol Chem, 271(29), 17570-5, 1996.

Smith, J A, Francis, S H, Walsh, K A, Kumar, S, Corbin, J D. Autophosphorylation of type Ibeta cGMP-dependent protein kinase increases basal catalytic activity and enhances allosteric activation by cGMP or cAMP. J Biol Chem, 271(34), 20756-62, 1996.

Turko, I V, Haik, T L, McAllister-Lucas, L M, Burns, F, Francis, S H, Corbin, J D. Identification of key amino acids in a conserved cGMP-binding site of cGMP-binding phosphodiesterases. A putative NKXnD motif for cGMP binding. J Biol Chem, 271(36), 22240-4, 1996.

Yan, X., Lawrence, D.S., Corbin, J.D., and Francis, S.H. Distinguishing between closely related protein kinases: A variation on the bisubstrate inhibitor theme. J. of Am. Chem. Soc., 118, 6321-6322, 1996.

McAllister-Lucas, L M, Haik, T L, Colbran, J L, Sonnenburg, W K, Seger, D, Turko, I V, Beavo, J A, Francis, S H, Corbin, J D. An essential aspartic acid at each of two allosteric cGMP-binding sites of a cGMP-specific phosphodiesterase. J Biol Chem, 270(51), 30671-9, 1995.

Francis, S H, Colbran, J L, McAllister-Lucas, L M, Corbin, J D. Zinc interactions and conserved motifs of the cGMP-binding cGMP-specific phosphodiesterase suggest that it is a zinc hydrolase. J Biol Chem, 269(36), 22477-80, 1994.

Francis, S H, Corbin, J D. Structure and function of cyclic nucleotide-dependent protein kinases. Annu Rev Physiol, 56, 237-72, 1994.

Francis, S H, Corbin, J D. Progress in understanding the mechanism and function of cyclic GMP-dependent protein kinase. Adv Pharmacol, 26, 115-70, 1994.

Corbin, J D, Woodall, C C, Colbran, J L, McAllister, L M, Sekhar, K R, Francis, S H. Identifying protein kinases in crude extracts that phosphorylate cyclic GMP-binding cyclic-GMP specific phosphodiesterase. Agents Actions Suppl, 43, 27-33, 1993.

McAllister-Lucas, L M, Sonnenburg, W K, Kadlecek, A, Seger, D, Trong, H L, Colbran, J L, Thomas, M K, Walsh, K A, Francis, S H, Corbin, J D. The structure of a bovine lung cGMP-binding, cGMP-specific phosphodiesterase deduced from a cDNA clone. J Biol Chem, 268(30), 22863-73, 1993.

Smith, J A, Francis, S H, Corbin, J D. Autophosphorylation: a salient feature of protein kinases. Mol Cell Biochem, 127-128, 51-70, 1993.

Colbran, J L, Francis, S H, Leach, A B, Thomas, M K, Jiang, H, McAllister, L M, Corbin, J D. A phenylalanine in peptide substrates provides for selectivity between cGMP- and cAMP-dependent protein kinases. J Biol Chem, 267(14), 9589-94, 1992.

Jiang, H, Colbran, J L, Francis, S H, Corbin, J D. Direct evidence for cross-activation of cGMP-dependent protein kinase by cAMP in pig coronary arteries. J Biol Chem, 267(2), 1015-9, 1992.

Sekhar, K R, Hatchett, R J, Shabb, J B, Wolfe, L, Francis, S H, Wells, J N, Jastorff, B, Butt, E, Chakinala, M M, Corbin, J D. Relaxation of pig coronary arteries by new and potent cGMP analogs that selectively activate type I alpha, compared with type I beta, cGMP-dependent protein kinase. Mol Pharmacol, 42(1), 103-8, 1992.

Thomas, M K, Francis, S H, Beebe, S J, Gettys, T W, Corbin, J D. Partial mapping of cyclic nucleotide sites and studies of regulatory mechanisms of phosphodiesterases using cyclic nucleotide analogues. Adv Second Messenger Phosphoprotein Res, 25, 45-53, 1992.

Corbin, J D, Thomas, M K, Wolfe, L, Shabb, J B, Woodford, T A, Francis, S H. New insights into cGMP action. Adv Second Messenger Phosphoprotein Res, 24, 411-8, 1990.

Thomas, M K, Francis, S H, Corbin, J D. Substrate- and kinase-directed regulation of phosphorylation of a cGMP-binding phosphodiesterase by cGMP. J Biol Chem, 265(25), 14971-8, 1990.

Wolfe, L, Corbin, J D, Francis, S H. Characterization of a novel isozyme of cGMP-dependent protein kinase from bovine aorta. J Biol Chem, 264(13), 7734-41, 1989.

Wolfe, L, Francis, S H, Corbin, J D. Properties of a cGMP-dependent monomeric protein kinase from bovine aorta. J Biol Chem, 264(7), 4157-62, 1989.

Corbin, J D, Cobb, C E, Beebe, S J, Granner, D K, Koch, S R, Gettys, T W, Blackmore, P F, Francis, S H, Wells, J N. Mechanism and function of cAMP- and cGMP-dependent protein kinases. Adv Second Messenger Phosphoprotein Res, 21, 75-86, 1988.

Francis, S H, Noblett, B D, Todd, B W, Wells, J N, Corbin, J D. Relaxation of vascular and tracheal smooth muscle by cyclic nucleotide analogs that preferentially activate purified cGMP-dependent protein kinase. Mol Pharmacol, 34(4), 506-17, 1988.

Francis, S H, Woodford, T A, Wolfe, L, Corbin, J D. Types I alpha and I beta isozymes of cGMP-dependent protein kinase: alternative mRNA splicing may produce different inhibitory domains. Second Messengers Phosphoproteins, 12(5-6), 301-10, 1988.

Wolfe, L, Francis, S H, Landiss, L R, Corbin, J D. Interconvertible cGMP-free and cGMP-bound forms of cGMP-dependent protein kinase in mammalian tissues. J Biol Chem, 262(35), 16906-13, 1987.


Postdoctoral Position Available
No

Postdoctoral Position Details
N/A

Updated Date
04/26/2007



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