메뉴 건너뛰기




Volumn 48, Issue 3, 1997, Pages 145-153

Cyclic nucleotide phosphodiesterases: Diversity, classification, structure function;Fosfodiesterasas de nucleotidos ciclicos: Diversidad, Clasificacion, estructura y funcion

Author keywords

cAMP; cGMP; Phosphodiesterases; Trypanosomatides

Indexed keywords

2',3' CYCLIC NUCLEOTIDE 3' PHOSPHODIESTERASE; CYCLIC AMP; CYCLIC GMP; ISOENZYME;

EID: 0031300632     PISSN: 00015504     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (2)

References (92)
  • 1
    • 0024374367 scopus 로고
    • Presence and properties of cAMP phosphodiesterase from promastigote forms of Leishmania tropica and Leishmania donovani
    • Al-Chalabi, K.A.K., Ziz, L.A. and Al-Khayat, B. Presence and properties of cAMP phosphodiesterase from promastigote forms of Leishmania tropica and Leishmania donovani. Comp. Biochem. Physiol. 93B: 789-792, 1989.
    • (1989) Comp. Biochem. Physiol. , vol.93 B , pp. 789-792
    • Al-Chalabi, K.A.K.1    Ziz, L.A.2    Al-Khayat, B.3
  • 2
    • 0026570927 scopus 로고
    • In vivo differential prenylation of retinal cyclic GMP phosphodiesterase catalytic subunits
    • Anant, J., Ong, O., Xie, H., Clarke, S., O'Brien, P. and Fung, B. In vivo differential prenylation of retinal cyclic GMP phosphodiesterase catalytic subunits. J. Biol. Chem. 267: 687-690, 1992.
    • (1992) J. Biol. Chem. , vol.267 , pp. 687-690
    • Anant, J.1    Ong, O.2    Xie, H.3    Clarke, S.4    O'Brien, P.5    Fung, B.6
  • 3
    • 0016415734 scopus 로고
    • Regulation of cyclic nucleotide phosphodiesterases
    • Appleman, M.M. and Terasaki, W.L. Regulation of cyclic nucleotide phosphodiesterases. Adv. Cycl. Nucl. Res. 5: 153-163, 1975.
    • (1975) Adv. Cycl. Nucl. Res. , vol.5 , pp. 153-163
    • Appleman, M.M.1    Terasaki, W.L.2
  • 4
    • 0018834119 scopus 로고
    • The turnover of cyclic AMP in cultured fibroblast
    • Barber, R. and Butcher, R.W. The turnover of cyclic AMP in cultured fibroblast. J. Cyclic Nucleotide Res. 6: 3-7, 1980.
    • (1980) J. Cyclic Nucleotide Res. , vol.6 , pp. 3-7
    • Barber, R.1    Butcher, R.W.2
  • 5
    • 0019523939 scopus 로고
    • The quantitative relationship between intracellular concentration and egrees of cyclic AMP from cultured cells
    • Barber, R. and Butcher, R.W. The quantitative relationship between intracellular concentration and egrees of cyclic AMP from cultured cells. Mol. Pharmacol. 19: 38-43, 1981.
    • (1981) Mol. Pharmacol. , vol.19 , pp. 38-43
    • Barber, R.1    Butcher, R.W.2
  • 6
    • 0024253227 scopus 로고
    • Multiple isozymes of cyclic nucleotide phosphodiesterase
    • Beavo, J.A. Multiple isozymes of cyclic nucleotide phosphodiesterase. Adv. Sec. Mess. Phos. Res. 22: 1-38, 1988.
    • (1988) Adv. Sec. Mess. Phos. Res. , vol.22 , pp. 1-38
    • Beavo, J.A.1
  • 7
  • 9
    • 0025215525 scopus 로고
    • Primary sequence of cyclic nuclotide phosphodiesrerase isoenzymes and desing of selective inhibitors
    • Beavo, J.A. and Reifsnyder, D.H. Primary sequence of cyclic nuclotide phosphodiesrerase isoenzymes and desing of selective inhibitors. Trends Pharm. Sci. 11: 150-155, 1990.
    • (1990) Trends Pharm. Sci. , vol.11 , pp. 150-155
    • Beavo, J.A.1    Reifsnyder, D.H.2
  • 10
    • 0022401456 scopus 로고
    • Discriminative insulin antagonism of stimulatory effects of various cAMP analogs on adipocyte lipolysis and hepatocyte glycogenolysis
    • Beebe, S.J., Redmon, J.B., Blackmore, P.F. and Corbin, J.D. Discriminative insulin antagonism of stimulatory effects of various cAMP analogs on adipocyte lipolysis and hepatocyte glycogenolysis. J. Biol. Chem. 260: 15781-15788, 1985.
    • (1985) J. Biol. Chem. , vol.260 , pp. 15781-15788
    • Beebe, S.J.1    Redmon, J.B.2    Blackmore, P.F.3    Corbin, J.D.4
  • 11
    • 18144445994 scopus 로고
    • The role of protein phosphorylation in the regulation of cyclic nucleotide phosphodiesterases
    • Beltman, J., Sonnenburg, W.K. and Beavo, J.A. The role of protein phosphorylation in the regulation of cyclic nucleotide phosphodiesterases. Mol. Cell. Biochem. 127/128: 239-253, 1993.
    • (1993) Mol. Cell. Biochem. , vol.127-128 , pp. 239-253
    • Beltman, J.1    Sonnenburg, W.K.2    Beavo, J.A.3
  • 12
    • 0023879704 scopus 로고
    • Purification of an insulin-sensitive cyclic AMP phosphodiesterase from rat liver
    • Boyes, S. and Loten, E.G. Purification of an insulin-sensitive cyclic AMP phosphodiesterase from rat liver. Eur. J. Biochem. 174: 303-309, 1988.
    • (1988) Eur. J. Biochem. , vol.174 , pp. 303-309
    • Boyes, S.1    Loten, E.G.2
  • 13
    • 33847612208 scopus 로고
    • Adenosine 3′-5′-monophosphate in biological materials
    • Butcher, R.W. and Sutherland, E.W. Adenosine 3′-5′-monophosphate in biological materials. J. Biol. Chem. 237: 1244-1249, 1962.
    • (1962) J. Biol. Chem. , vol.237 , pp. 1244-1249
    • Butcher, R.W.1    Sutherland, E.W.2
  • 14
    • 0025103358 scopus 로고
    • Effects of selective phosphodiesterase inhibition on cyclic AMP hydrolysis in rat cortical slices
    • Challis, R.A. and Nicholson, C.D. Effects of selective phosphodiesterase inhibition on cyclic AMP hydrolysis in rat cortical slices. Br. J. Pharmacol. 99: 47-52, 1990.
    • (1990) Br. J. Pharmacol. , vol.99 , pp. 47-52
    • Challis, R.A.1    Nicholson, C.D.2
  • 15
    • 0001834697 scopus 로고
    • Structure-function relationship among cyclic nucleotide phosphodiesterase
    • J.A. Beavo y M.D. Houslay (Eds.): John Wiley and Sons, Chichester, R.U.
    • Charbonneau, H. Structure-function relationship among cyclic nucleotide phosphodiesterase. En: J.A. Beavo y M.D. Houslay (Eds.): Cyclic Nuclotide Phosphodiesrerases: Estructure, regulation and drug action. John Wiley and Sons, Chichester, R.U. 2: 267-296, 1990.
    • (1990) Cyclic Nuclotide Phosphodiesrerases: Estructure, Regulation and Drug Action , vol.2 , pp. 267-296
    • Charbonneau, H.1
  • 16
    • 0022961581 scopus 로고
    • Identification of a conserved domain among cyclic nucleotide phosphodiesterases from diverse species
    • Charbonneau, H., Beier, N., Walsh, K.A. and Beavo, J.A. Identification of a conserved domain among cyclic nucleotide phosphodiesterases from diverse species. Proc. Natl. Acad. Sci. USA 83: 9308-9312, 1986.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 9308-9312
    • Charbonneau, H.1    Beier, N.2    Walsh, K.A.3    Beavo, J.A.4
  • 17
    • 0022912655 scopus 로고
    • Molecular analysis of cDNA clones and de corresponding genomic coding sequences of the Drosophila dunce gene, the structural gene for cAMP phosphodiesterase
    • Chen, C.N., Denome, S. and Davis, R.L. Molecular analysis of cDNA clones and de corresponding genomic coding sequences of the Drosophila dunce gene, the structural gene for cAMP phosphodiesterase. Proc. Natl. Acad. Sci. USA 83: 9313-9317, 1986.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 9313-9317
    • Chen, C.N.1    Denome, S.2    Davis, R.L.3
  • 18
    • 0022647639 scopus 로고
    • New positive inotropic agents in the treatment of congestive heart failure
    • Colucci, W.S., Wright, R.F. and Braunwald, E. New positive inotropic agents in the treatment of congestive heart failure. N. Engl. J. Med. 314: 290-299, 1986.
    • (1986) N. Engl. J. Med. , vol.314 , pp. 290-299
    • Colucci, W.S.1    Wright, R.F.2    Braunwald, E.3
  • 19
    • 0023927842 scopus 로고
    • Effects of α- And β-adrenergic agonists on Trypanosoma cruzi interaction with host cells
    • Connely, M.C., Ayala, A. and Kierszenbaum, F. Effects of α- and β-adrenergic agonists on Trypanosoma cruzi interaction with host cells. J. Parasitol. 74: 379-386, 1988.
    • (1988) J. Parasitol. , vol.74 , pp. 379-386
    • Connely, M.C.1    Ayala, A.2    Kierszenbaum, F.3
  • 20
    • 0022475760 scopus 로고
    • Effect of phosphodiesterase inhibitors on Sertoli cell refractoriness: Reversal of the impaired androgen aromatization
    • Conti, M., Monaco, L., Geremia, R. and Stefanini, M. Effect of phosphodiesterase inhibitors on Sertoli cell refractoriness: reversal of the impaired androgen aromatization. Endocrinology 118: 901-908, 1986.
    • (1986) Endocrinology , vol.118 , pp. 901-908
    • Conti, M.1    Monaco, L.2    Geremia, R.3    Stefanini, M.4
  • 21
    • 0029009878 scopus 로고
    • Recent progress in understanding the hormonal regulation of phosphodiesterases
    • Conti, M., Nemoz, G., Sette, C. and Vicini, E. Recent progress in understanding the hormonal regulation of phosphodiesterases. Endocrine Rev. 16: 370-389, 1995.
    • (1995) Endocrine Rev. , vol.16 , pp. 370-389
    • Conti, M.1    Nemoz, G.2    Sette, C.3    Vicini, E.4
  • 22
    • 0020117728 scopus 로고
    • Regulation of follicle-stimulating hormone and dibutiryl adenosine 3′-5′-monophosphate of a phosphodiesterase isoenzime of the Sertoli cell
    • Conti, M., Toscano, M.V., Petrelli, L., Geremia, R. and Stefanini, M. Regulation of follicle-stimulating hormone and dibutiryl adenosine 3′-5′-monophosphate of a phosphodiesterase isoenzime of the Sertoli cell. Endocrinology 110: 1189-1196, 1982.
    • (1982) Endocrinology , vol.110 , pp. 1189-1196
    • Conti, M.1    Toscano, M.V.2    Petrelli, L.3    Geremia, R.4    Stefanini, M.5
  • 23
    • 0020554240 scopus 로고
    • Involvement of phosphodiesterase in the refractoriness of Sertoli cell
    • Conti, M., Toscano, M.V., Petrelli, L., Geremia, R. and Stefanini, M. Involvement of phosphodiesterase in the refractoriness of Sertoli cell. Endocrinology 113: 1845-1853, 1983.
    • (1983) Endocrinology , vol.113 , pp. 1845-1853
    • Conti, M.1    Toscano, M.V.2    Petrelli, L.3    Geremia, R.4    Stefanini, M.5
  • 25
    • 0023475546 scopus 로고
    • Trypanosoma cruzi: Adrenergic modulation of cAMP role in proliferation and differentiation in vitro
    • De Castro, S.L., Meirelles, M.N.L. and Oliveira, M.M. Trypanosoma cruzi: adrenergic modulation of cAMP role in proliferation and differentiation in vitro. Exp. Parasitol. 64: 368-375, 1987.
    • (1987) Exp. Parasitol. , vol.64 , pp. 368-375
    • De Castro, S.L.1    Meirelles, M.N.L.2    Oliveira, M.M.3
  • 26
    • 0023226133 scopus 로고
    • Radioligand binding characterization of β-adrenergic receptors in the protozoa Trypanosoma cruzi
    • De Castro, S.L. and Oliveira, M.M. Radioligand binding characterization of β-adrenergic receptors in the protozoa Trypanosoma cruzi. Comp. Biochem. Physiol. C87: 5-8, 1987.
    • (1987) Comp. Biochem. Physiol. , vol.C87 , pp. 5-8
    • De Castro, S.L.1    Oliveira, M.M.2
  • 27
    • 0023178721 scopus 로고
    • Purification of a putative hormone-sensitive AMPc phosphodiesterase from rat adipose tissue using a derivative of cilostamide as a novel affinity chromatography
    • Degerman E., Belfrage P., Newman A.H., Rice K.C. and Manganiello, V.C. Purification of a putative hormone-sensitive AMPc phosphodiesterase from rat adipose tissue using a derivative of cilostamide as a novel affinity chromatography. J. Biol. Chem. 262(2): 5797-5807, 1987.
    • (1987) J. Biol. Chem. , vol.262 , Issue.2 , pp. 5797-5807
    • Degerman, E.1    Belfrage, P.2    Newman, A.H.3    Rice, K.C.4    Manganiello, V.C.5
  • 30
    • 0027219228 scopus 로고
    • Characterization of a Periplamic 3′-5′-cyclic nucleotide phosphodiesterase gene, cpdP, from the marine simbiotic bacterium Vibrio fischeri
    • Dunlap. P.V. and Callahan, S.M. Characterization of a Periplamic 3′-5′-cyclic nucleotide phosphodiesterase gene, cpdP, from the marine simbiotic bacterium Vibrio fischeri. J. Bacteriol. 175: 4615-4624, 1993.
    • (1993) J. Bacteriol. , vol.175 , pp. 4615-4624
    • Dunlap, P.V.1    Callahan, S.M.2
  • 31
    • 0001037707 scopus 로고
    • Phosphodiesterases in visual transduction by rods and cones
    • J. Beavo, y M.D. Houslay (Eds.): John Wiley & Sons, Chichester
    • Gillespie, P.G. Phosphodiesterases in visual transduction by rods and cones. En: J. Beavo, y M.D. Houslay (Eds.): Cyclic Nucleotide Phosphodiesterases: Structure, Regulation and Drug Action, John Wiley & Sons, Chichester, 1990. pp. 161-184.
    • (1990) Cyclic Nucleotide Phosphodiesterases: Structure, Regulation and Drug Action , pp. 161-184
    • Gillespie, P.G.1
  • 32
    • 0023062991 scopus 로고
    • G-Proteins: Transducers of receptor-generated signals
    • Gilman, A.G. G-Proteins: transducers of receptor-generated signals. Ann. Rev. Biochem. 56: 615-649, 1987.
    • (1987) Ann. Rev. Biochem. , vol.56 , pp. 615-649
    • Gilman, A.G.1
  • 33
    • 0019006824 scopus 로고
    • cAMP phosphodiesterase and activator protein of mammalian cAMP phosphodiesterase from Trypanosoma cruzi
    • Gonçalves, M.F., Zingales, B. and Colli, W. cAMP phosphodiesterase and activator protein of mammalian cAMP phosphodiesterase from Trypanosoma cruzi. Mol. Biochem. Parasitol. 1: 107-118, 1980.
    • (1980) Mol. Biochem. Parasitol. , vol.1 , pp. 107-118
    • Gonçalves, M.F.1    Zingales, B.2    Colli, W.3
  • 34
    • 0021359546 scopus 로고
    • Purification and characterization of a human platelet cyclic nucleotide phosphodiesterase
    • Grant, P. and Colman, R.W. Purification and characterization of a human platelet cyclic nucleotide phosphodiesterase. Biochemistry 23: 1801-1807, 1984.
    • (1984) Biochemistry , vol.23 , pp. 1801-1807
    • Grant, P.1    Colman, R.W.2
  • 37
    • 0022454622 scopus 로고
    • Isolation and characterization of bovine cardiac muscle cGMP-inhibited phosphodiesterase: A receptor for new cardiotonic drugs
    • Harrison, S.A., Reifsnyder, D.H., Gallis, B., Cadd, G.S. and Beavo, J.A. Isolation and characterization of bovine cardiac muscle cGMP-inhibited phosphodiesterase: a receptor for new cardiotonic drugs. Mol. Pharmacol. 29: 506-514, 1986.
    • (1986) Mol. Pharmacol. , vol.29 , pp. 506-514
    • Harrison, S.A.1    Reifsnyder, D.H.2    Gallis, B.3    Cadd, G.S.4    Beavo, J.A.5
  • 38
    • 0025072451 scopus 로고
    • A cyclic AMP inducible gene expressed during the development of infective stages of Trypanosoma cruzi
    • Heath, S., Hieny, S. and Sher, A. A cyclic AMP inducible gene expressed during the development of infective stages of Trypanosoma cruzi. Mol. Biochem. Parasitol. 43: 133-142, 1990.
    • (1990) Mol. Biochem. Parasitol. , vol.43 , pp. 133-142
    • Heath, S.1    Hieny, S.2    Sher, A.3
  • 39
    • 0017254947 scopus 로고
    • Human blood platelet 3′-5′ cyclic nucleotide phosphodiesterase
    • Hidaka, H. and Asano, T. Human blood platelet 3′-5′ cyclic nucleotide phosphodiesterase. Biochim. Biophys. Acta 429: 485-497, 1976.
    • (1976) Biochim. Biophys. Acta , vol.429 , pp. 485-497
    • Hidaka, H.1    Asano, T.2
  • 40
    • 0021295772 scopus 로고
    • Selective inhibitors of three forms of cyclic nucleotide phosphodiesterase-basic and potential clinical applications
    • Hidaka, H. and Endo, T. Selective inhibitors of three forms of cyclic nucleotide phosphodiesterase-basic and potential clinical applications. Adv. Cyclic. Nucleotide Res. 16: 245-259, 1984.
    • (1984) Adv. Cyclic. Nucleotide Res. , vol.16 , pp. 245-259
    • Hidaka, H.1    Endo, T.2
  • 41
    • 0028037682 scopus 로고
    • A Candida albicans cyclic nucleotide phosphodiesterase: Cloning and expression in Saccharomyces cerevisiae and biochemical characterization of the recombinant enzyme
    • Hoyer, L.L., Cieslinski, L.B., McLaughlin, M.M., Torphy, T.J., Shatzman, A.R. and Livi, G.P. A Candida albicans cyclic nucleotide phosphodiesterase: cloning and expression in Saccharomyces cerevisiae and biochemical characterization of the recombinant enzyme. Microbiology 140: 1533-1542, 1994.
    • (1994) Microbiology , vol.140 , pp. 1533-1542
    • Hoyer, L.L.1    Cieslinski, L.B.2    McLaughlin, M.M.3    Torphy, T.J.4    Shatzman, A.R.5    Livi, G.P.6
  • 42
    • 0026689109 scopus 로고
    • Signal transduction enzymes of vertebrate photoreceptors
    • Hurley, J.B. Signal transduction enzymes of vertebrate photoreceptors. J. Bioenerg. Biomembr. 24: 219-226, 1992.
    • (1992) J. Bioenerg. Biomembr. , vol.24 , pp. 219-226
    • Hurley, J.B.1
  • 43
    • 0020076352 scopus 로고
    • Biochemical studies on the mechanism of cardiotonic activity of MDL 17,043
    • Kariya, T., Willie, L.J. and Dage, R.C. Biochemical studies on the mechanism of cardiotonic activity of MDL 17,043. J. Cardiovasc. Pharmacol. 4: 509-514, 1982.
    • (1982) J. Cardiovasc. Pharmacol. , vol.4 , pp. 509-514
    • Kariya, T.1    Willie, L.J.2    Dage, R.C.3
  • 44
    • 0021814803 scopus 로고
    • Proteolytic activation of calmodulin-dependent cyclic nucleotide phosphodiesterase
    • Kincaid, R.L., Stith-Coleman, I.E. and Vaughan, M. Proteolytic activation of calmodulin-dependent cyclic nucleotide phosphodiesterase. J. Biol. Chem. 260: 9009-9015, 1985.
    • (1985) J. Biol. Chem. , vol.260 , pp. 9009-9015
    • Kincaid, R.L.1    Stith-Coleman, I.E.2    Vaughan, M.3
  • 45
    • 0023007633 scopus 로고
    • Molecular cloning and developmental expression of the cyclic nucleotide phosphodiesterase gene of Dictyostelium discoideum
    • Lacombe, M.L., Podgorski, G., Franke, J. and Kessin, R. Molecular cloning and developmental expression of the cyclic nucleotide phosphodiesterase gene of Dictyostelium discoideum. J. Biol. Chem. 261: 16811-16817, 1986.
    • (1986) J. Biol. Chem. , vol.261 , pp. 16811-16817
    • Lacombe, M.L.1    Podgorski, G.2    Franke, J.3    Kessin, R.4
  • 46
    • 0025866974 scopus 로고
    • Selective inhibition of cGMP-inhibited and cGMP-noninhibited cyclic nucleotide phosphodiesterases and relaxation of rat aorta
    • Lindgren, S., Rascón, A., Andersson, K.E., Manganiello, V.C. and Degerman, E. Selective inhibition of cGMP-inhibited and cGMP-noninhibited cyclic nucleotide phosphodiesterases and relaxation of rat aorta. Biochem. Pharmacol. 42, 545-552, 1991.
    • (1991) Biochem. Pharmacol. , vol.42 , pp. 545-552
    • Lindgren, S.1    Rascón, A.2    Andersson, K.E.3    Manganiello, V.C.4    Degerman, E.5
  • 47
    • 0022870844 scopus 로고
    • The antilipolytic effect of insulin in human adipocytes requires activation of the phosphodiesterase
    • Lönnroth, P. and Smith, U. The antilipolytic effect of insulin in human adipocytes requires activation of the phosphodiesterase. Biochem. Biophys. Res. Commun. 141: 1157-1161, 1986.
    • (1986) Biochem. Biophys. Res. Commun. , vol.141 , pp. 1157-1161
    • Lönnroth, P.1    Smith, U.2
  • 48
    • 0026032745 scopus 로고
    • High concentrations of cGMP-stimulated phosphodiesterase mediate ANP-induced decreases in cAMP and steroidogenesis in adrenal glomerulosa cells
    • MacFarland, R.T., Zelus, B.D. and Beavo, J.A. High concentrations of cGMP-stimulated phosphodiesterase mediate ANP-induced decreases in cAMP and steroidogenesis in adrenal glomerulosa cells. J. Biol. Chem. 266: 136-142, 1991.
    • (1991) J. Biol. Chem. , vol.266 , pp. 136-142
    • MacFarland, R.T.1    Zelus, B.D.2    Beavo, J.A.3
  • 50
    • 0019571794 scopus 로고
    • Cyclic 3′-5′-adenosine monophosphate levels during developmental cycle of Trypanosoma brucei brucei in the rat
    • Mancini, P.E. y Patton, C.L. Cyclic 3′-5′-adenosine monophosphate levels during developmental cycle of Trypanosoma brucei brucei in the rat. Mol. Biochem. Parasitol. 3: 19-31, 1981.
    • (1981) Mol. Biochem. Parasitol. , vol.3 , pp. 19-31
    • Mancini, P.E.1    Patton, C.L.2
  • 51
    • 0023543342 scopus 로고
    • Subcellular localization and biological function of specific cyclic nucleotide phosphodiesterases
    • Manganiello, V.C. Subcellular localization and biological function of specific cyclic nucleotide phosphodiesterases. J. Mol. Cel. Cardiol. 19: 1037-1040, 1987.
    • (1987) J. Mol. Cel. Cardiol. , vol.19 , pp. 1037-1040
    • Manganiello, V.C.1
  • 52
    • 0023002533 scopus 로고
    • Regulation of particulate cAMP phosphodiesterase activity in 3T3-L1 adipocytes: The role of particulate phosphodiesterase in the antilipolytic action of insulin
    • P. Belfrage, J. Donnér y P. Stralfors (Eds.): Elsevier Sci. Publishers, Amsterdam
    • Manganiello, V.C. and Elks, M.L. Regulation of particulate cAMP phosphodiesterase activity in 3T3-L1 adipocytes: The role of particulate phosphodiesterase in the antilipolytic action of insulin. En: P. Belfrage, J. Donnér y P. Stralfors (Eds.): Mechanism of insulin action. Elsevier Sci. Publishers, Amsterdam, 1986. pp. 147-166.
    • (1986) Mechanism of Insulin Action , pp. 147-166
    • Manganiello, V.C.1    Elks, M.L.2
  • 54
    • 0018078641 scopus 로고
    • Adenylate cyclase in bloodstream forms of Trypanosoma brucei brucei
    • Martin, B.R., Voorheis, H.P. and Kennedy, E.L. Adenylate cyclase in bloodstream forms of Trypanosoma brucei brucei. Biochem. J. 175: 207-212, 1978.
    • (1978) Biochem. J. , vol.175 , pp. 207-212
    • Martin, B.R.1    Voorheis, H.P.2    Kennedy, E.L.3
  • 55
    • 0026718951 scopus 로고
    • Gustducin is a taste-cell-specific G protein closely related to the transducins
    • McLauglin, S.K., McKinnon, P.J. and Margolskee, R.F. Gustducin is a taste-cell-specific G protein closely related to the transducins. Nature 357: 563-569, 1992.
    • (1992) Nature , vol.357 , pp. 563-569
    • McLauglin, S.K.1    McKinnon, P.J.2    Margolskee, R.F.3
  • 56
    • 0020582818 scopus 로고
    • Muscarinic cholinergic receptor-mediated activation of phosphodiesterase
    • Meeker, R.B. and Hardin, T.K. Muscarinic cholinergic receptor-mediated activation of phosphodiesterase. Mol. Pharmacol. 23: 384-392, 1982.
    • (1982) Mol. Pharmacol. , vol.23 , pp. 384-392
    • Meeker, R.B.1    Hardin, T.K.2
  • 57
    • 0027164208 scopus 로고
    • Isolation and characterization of a previously undetected human cAMP phosphodiesterase by complementation of cAMP phosphodiesterase-deficient Saccharomyces cerevisiae
    • Michaeli, T., Bloom, T.J., Martins, T., Loughney, K., Ferguson, K., Riggs, M., Rodgers, L., Beavo, J.A. and Wigler, M. Isolation and characterization of a previously undetected human cAMP phosphodiesterase by complementation of cAMP phosphodiesterase-deficient Saccharomyces cerevisiae. J. Biol. Chem. 268: 12925-12932, 1993.
    • (1993) J. Biol. Chem. , vol.268 , pp. 12925-12932
    • Michaeli, T.1    Bloom, T.J.2    Martins, T.3    Loughney, K.4    Ferguson, K.5    Riggs, M.6    Rodgers, L.7    Beavo, J.A.8    Wigler, M.9
  • 59
    • 0026008409 scopus 로고
    • Differential modulation of tissue function and therapeutic potential of selective inhibitors of cyclic nucleotide phosphodiesterase isoenzymes
    • Nicholson, C.D., Challis, R. and Shahid, M. Differential modulation of tissue function and therapeutic potential of selective inhibitors of cyclic nucleotide phosphodiesterase isoenzymes. Trends Pharmacol. 12: 19-27, 1991.
    • (1991) Trends Pharmacol. , vol.12 , pp. 19-27
    • Nicholson, C.D.1    Challis, R.2    Shahid, M.3
  • 60
    • 0023427567 scopus 로고
    • Cloning and characterization of the low-affinity cyclic AMP phosphodiesterase gene of Saccharomyces cerevisiae
    • Nikawa, J., Sass, P. and Wigler, M. Cloning and characterization of the low-affinity cyclic AMP phosphodiesterase gene of Saccharomyces cerevisiae. Mol. Cell. Biol. 7: 3629-3636, 1987.
    • (1987) Mol. Cell. Biol. , vol.7 , pp. 3629-3636
    • Nikawa, J.1    Sass, P.2    Wigler, M.3
  • 61
    • 0026047745 scopus 로고
    • Identification of the retinal cyclic GMP phosphodiesterase inhibitory gamma-subunit interaction sites on the catalytic alpha-subunit
    • Oppert, B., Cunnick, J.M., Hurt, D. and Takemoto, D.U. Identification of the retinal cyclic GMP phosphodiesterase inhibitory gamma-subunit interaction sites on the catalytic alpha-subunit. J. Biol. Chem. 266: 16607-16613, 1991.
    • (1991) J. Biol. Chem. , vol.266 , pp. 16607-16613
    • Oppert, B.1    Cunnick, J.M.2    Hurt, D.3    Takemoto, D.U.4
  • 62
    • 0023860998 scopus 로고
    • Cyclic AMP and Cyclic GMP phosphodiesterases: Target for Drug Development
    • Pang. D.C. Cyclic AMP and Cyclic GMP phosphodiesterases: Target for Drug Development. Drug. Dev. Res. 12: 85-92, 1988.
    • (1988) Drug. Dev. Res. , vol.12 , pp. 85-92
    • Pang, D.C.1
  • 64
    • 0021099659 scopus 로고
    • The cAMP receptor protein of Trypanosoma cruzi
    • Rangel-Aldao, R., Tovar, G. and De Ruiz, M.L. The cAMP receptor protein of Trypanosoma cruzi. J. Biol. Chem. 258: 6976-6983, 1983.
    • (1983) J. Biol. Chem. , vol.258 , pp. 6976-6983
    • Rangel-Aldao, R.1    Tovar, G.2    De Ruiz, M.L.3
  • 67
    • 0028237055 scopus 로고
    • Identification of the phosphorylation site in vitro for cAMP-dependent protein kinase on the rat adipocite cGMP-inhibited cAMP phosphodiesterase
    • Rascón, A., Degerman, E., Taira, M., Meacci, E., Smith, C.J., Manganiello, V., Beifrage, P. and Tornqvist, H. Identification of the phosphorylation site in vitro for cAMP-dependent protein kinase on the rat adipocite cGMP-inhibited cAMP phosphodiesterase. J. Biol. Chem. 269(16): 11962-11966, 1994.
    • (1994) J. Biol. Chem. , vol.269 , Issue.16 , pp. 11962-11966
    • Rascón, A.1    Degerman, E.2    Taira, M.3    Meacci, E.4    Smith, C.J.5    Manganiello, V.6    Beifrage, P.7    Tornqvist, H.8
  • 68
    • 0022859343 scopus 로고
    • Cloning and characterization of the high affinity cAMP phosphodiesterase of Saccharomyces cereviciae
    • Sass, P., Field, J., Nikawa, J., Toda, T. and Wigler, M. Cloning and characterization of the high affinity cAMP phosphodiesterase of Saccharomyces cereviciae. Proc. Natl. Acad. Sci. USA 83: 9308-9307, 1986.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 9308-19307
    • Sass, P.1    Field, J.2    Nikawa, J.3    Toda, T.4    Wigler, M.5
  • 70
    • 0016702153 scopus 로고
    • Adenosine 3′-5′-monophosphate in reproducing and differentiated Trypanosomes
    • Strickler, J.E. and Patton, C.L. Adenosine 3′-5′-monophosphate in reproducing and differentiated Trypanosomes. Science 190: 1110-1112, 1975.
    • (1975) Science , vol.190 , pp. 1110-1112
    • Strickler, J.E.1    Patton, C.L.2
  • 71
    • 0024374907 scopus 로고
    • Direct photolabeling of the cGMP-stimulated cyclic nucleotide phosphodiesterase
    • Stroop, S.D., Charbonneau, H. and Beavo, J. Direct photolabeling of the cGMP-stimulated cyclic nucleotide phosphodiesterase. J. Biol. Chem. 264: 13718-13725, 1989.
    • (1989) J. Biol. Chem. , vol.264 , pp. 13718-13725
    • Stroop, S.D.1    Charbonneau, H.2    Beavo, J.3
  • 72
    • 0025822625 scopus 로고
    • Visual excitation and recovery
    • Stryer, L. Visual excitation and recovery. J. Biol. Chem. 266: 10711-10714, 1991.
    • (1991) J. Biol. Chem. , vol.266 , pp. 10711-10714
    • Stryer, L.1
  • 73
    • 0001559662 scopus 로고
    • Fractionation and characterization of a cyclic adenine ribonucleotide formed by tissue particles
    • Sutherland, E.W. and Rall, T.W. Fractionation and characterization of a cyclic adenine ribonucleotide formed by tissue particles. J. Biol. Chem. 232: 1077, 1958.
    • (1958) J. Biol. Chem. , vol.232 , pp. 1077
    • Sutherland, E.W.1    Rall, T.W.2
  • 74
    • 0027283557 scopus 로고
    • Molecular cloning of the rat adipocyte hormone-sensitive cyclic GMP-inhibited cyclic nucleotide phosphodiesterase
    • Taira, M., Hockman, S., Calvo., U.C., Taira M., Beifrage, P. and Manganiello, V.C. Molecular cloning of the rat adipocyte hormone-sensitive cyclic GMP-inhibited cyclic nucleotide phosphodiesterase. J. Biol. Chem. 268: 18573-18579, 1993.
    • (1993) J. Biol. Chem. , vol.268 , pp. 18573-18579
    • Taira, M.1    Hockman, S.2    Calvo, U.C.3    Taira, M.4    Beifrage, P.5    Manganiello, V.C.6
  • 76
    • 0015231739 scopus 로고
    • Multiple cyclic nucleotide phosphodiesterase activities from rat brain
    • Thompson, W.J. and Appleman, M.M. Multiple cyclic nucleotide phosphodiesterase activities from rat brain. Biochemistry 10: 311-316, 1971.
    • (1971) Biochemistry , vol.10 , pp. 311-316
    • Thompson, W.J.1    Appleman, M.M.2
  • 77
    • 0015239529 scopus 로고
    • Characterization of cyclic nucleotide phosphodiesterase of rat tissues
    • Thompson, W.J. and Appleman, M.M. Characterization of cyclic nucleotide phosphodiesterase of rat tissues. J. Biol. Chem. 246: 3145-3150, 1971a.
    • (1971) J. Biol. Chem. , vol.246 , pp. 3145-3150
    • Thompson, W.J.1    Appleman, M.M.2
  • 78
    • 0025999955 scopus 로고
    • Cyclic nucleotide phosphodiesterases: Pharmacology, biochemistry and function
    • Thompson, W.J. Cyclic nucleotide phosphodiesterases: Pharmacology, biochemistry and function. Pharm. Ther. 51: 13-33, 1991.
    • (1991) Pharm. Ther. , vol.51 , pp. 13-33
    • Thompson, W.J.1
  • 79
    • 0021295771 scopus 로고
    • Biochemical properties of high-affinity cyclic AMP phosphodies terases
    • Thompson, W.J., Pratt, M.L. and Strada, S.J. Biochemical properties of high-affinity cyclic AMP phosphodies terases. Adv. Cyclic Nucleotide Res. 16: 137-148, 1984.
    • (1984) Adv. Cyclic Nucleotide Res. , vol.16 , pp. 137-148
    • Thompson, W.J.1    Pratt, M.L.2    Strada, S.J.3
  • 80
    • 0025756130 scopus 로고
    • Role of cyclic nucleotide phosphodiesterase isozymes in intact canine trachealis
    • Torphy, T.J., Zhou, H.L., Burman, M. and Huang, L.B.F. Role of cyclic nucleotide phosphodiesterase isozymes in intact canine trachealis. Mol. Pharmacol. 39: 376-384, 1991.
    • (1991) Mol. Pharmacol. , vol.39 , pp. 376-384
    • Torphy, T.J.1    Zhou, H.L.2    Burman, M.3    Huang, L.B.F.4
  • 81
    • 0019877278 scopus 로고
    • The effect of proteolysis on the calmodulin activation of cyclic nucleotide phosphodiesterase
    • Tucker, M.M., Robinson, J.B. and Stellwagen, E. The effect of proteolysis on the calmodulin activation of cyclic nucleotide phosphodiesterase. J. Biol. Chem. 256: 9051, 1981.
    • (1981) J. Biol. Chem. , vol.256 , pp. 9051
    • Tucker, M.M.1    Robinson, J.B.2    Stellwagen, E.3
  • 83
    • 0016313001 scopus 로고
    • 3′-5′ cyclic AMP phosphodiesterase from Trypanosoma gambiense
    • Walter, R.D. 3′-5′ cyclic AMP phosphodiesterase from Trypanosoma gambiense. Hoppe-Seyler's Z. Physiol. Chem. 355: 1443-1450, 1974.
    • (1974) Hoppe-Seyler's Z. Physiol. Chem. , vol.355 , pp. 1443-1450
    • Walter, R.D.1
  • 84
    • 0018166498 scopus 로고
    • Adenosine 3′-5′-cyclic monophosphate-binding proteins from Trypanosoma gambiense
    • Walter, R.D. Adenosine 3′-5′-cyclic monophosphate-binding proteins from Trypanosoma gambiense. Hoppe-Seylers Z. Physiol. Chem. 359: 607-612, 1978.
    • (1978) Hoppe-Seylers Z. Physiol. Chem. , vol.359 , pp. 607-612
    • Walter, R.D.1
  • 85
    • 0020352579 scopus 로고
    • Subcellular distribution of adenylate cyclase, cAMP phosphodiesterase, protein kinase and phosphoprotein phosphatase in Trypanosoma brucei
    • Walter, R.D. and Opperdoes, F.R. Subcellular distribution of adenylate cyclase, cAMP phosphodiesterase, protein kinase and phosphoprotein phosphatase in Trypanosoma brucei. Mol. Biochem. Parasitol. 6: 287-295, 1982.
    • (1982) Mol. Biochem. Parasitol. , vol.6 , pp. 287-295
    • Walter, R.D.1    Opperdoes, F.R.2
  • 86
    • 0039282082 scopus 로고
    • Regulation of cAMP metabolism in Leishmania promastigotes and amastigotes
    • D. Slutszky (Ed.): Pergamon Press, Oxford.
    • Walter, R.D. Regulation of cAMP metabolism in Leishmania promastigotes and amastigotes. En: D. Slutszky (Ed.): The biochemistry of parasites. Pergamon Press, Oxford. 1981. pp. 151-167.
    • (1981) The Biochemistry of Parasites , pp. 151-167
    • Walter, R.D.1
  • 87
    • 0018158805 scopus 로고
    • Effect of cAMP on transformation and proliferation of Leishmania cells
    • Walter, R.D., Buse, E., Ebert, F. Effect of cAMP on transformation and proliferation of Leishmania cells. Tropenmed. Parasit. 29: 439-447, 1978.
    • (1978) Tropenmed. Parasit. , vol.29 , pp. 439-447
    • Walter, R.D.1    Buse, E.2    Ebert, F.3
  • 89
    • 0022460551 scopus 로고
    • Multiple molecular forms of cyclic nucleotide phosphodiesterase in cardiac, smooth muscle and in platelets. Isolation, characterization, and effects of various reference phosphodiesterase inhibitors and cardiotonic agents
    • Weishaar, R.E., Burrows, S.D., Kobylarz, D.C., Quade, M.M. and Evans, D.B. Multiple molecular forms of cyclic nucleotide phosphodiesterase in cardiac, smooth muscle and in platelets. Isolation, characterization, and effects of various reference phosphodiesterase inhibitors and cardiotonic agents. Biochem. Pharmacol. 35: 787-800, 1986.
    • (1986) Biochem. Pharmacol. , vol.35 , pp. 787-800
    • Weishaar, R.E.1    Burrows, S.D.2    Kobylarz, D.C.3    Quade, M.M.4    Evans, D.B.5
  • 90
    • 0021941937 scopus 로고
    • A new generation of phosphodiesterase inhibitors: Multiple molecular forms of phosphodiesterase and the potential for drug selectivity
    • Weishaar, R.E., Cam, M.H. and Bristol, J.A. A new generation of phosphodiesterase inhibitors: multiple molecular forms of phosphodiesterase and the potential for drug selectivity. J. Med. Chem. 28: 537-545, 1985.
    • (1985) J. Med. Chem. , vol.28 , pp. 537-545
    • Weishaar, R.E.1    Cam, M.H.2    Bristol, J.A.3
  • 91
    • 0021350047 scopus 로고
    • Selective inhibition of two adenosine cyclic 3′-5′-phosphate phosphodiesterases partially purified from calf liver
    • Yamamoto, T., Lieberman, F., Osborne, J.C., Jr., Manganiello, V.C., Vaughan, M. and Hidaka, H. Selective inhibition of two adenosine cyclic 3′-5′-phosphate phosphodiesterases partially purified from calf liver. Biochemistry 23: 670-675, 1984.
    • (1984) Biochemistry , vol.23 , pp. 670-675
    • Yamamoto, T.1    Lieberman, F.2    Osborne Jr., J.C.3    Manganiello, V.C.4    Vaughan, M.5    Hidaka, H.6
  • 92
    • 0029845929 scopus 로고    scopus 로고
    • The calmodulin-dependent phosphodiesterase gene PDE1C encodes several functionally different splice variants in a tissue-specific manner
    • Van, C., Zhao, A.Z., Bentley, J.K. and Beavo., J.A. The calmodulin-dependent phosphodiesterase gene PDE1C encodes several functionally different splice variants in a tissue-specific manner. J. Biol. Chem. 271: 25699-25706, 1996.
    • (1996) J. Biol. Chem. , vol.271 , pp. 25699-25706
    • Van, C.1    Zhao, A.Z.2    Bentley, J.K.3    Beavo, J.A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.