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Volumn 51, Issue 1, 2012, Pages 194-204

Erratum: Nucleotidyl cyclase activity of soluble guanylyl cyclase α1β1 (Biochemistry (2012) 51:1 (194-204) DOI: 10.1021/bi201259y);Nucleotidyl cyclase activity of soluble guanylyl cyclase α1β1

Author keywords

[No Author keywords available]

Indexed keywords

AROMATIC COMPOUNDS; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; MASS SPECTROMETRY; NUCLEOTIDES; SUBSTRATES;

EID: 84856847677     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi3002715     Document Type: Erratum
Times cited : (76)

References (69)
  • 1
    • 61749086558 scopus 로고    scopus 로고
    • A short history of cGMP, guanylyl cyclases, and cGMP-dependent protein kinases
    • Kots, A. Y., Martin, E., Sharina, I. G., and Murad, F. (2009) A short history of cGMP, guanylyl cyclases, and cGMP-dependent protein kinases. Handb. Exp. Pharmacol., 191, 1-14.
    • (2009) Handb. Exp. Pharmacol. , vol.191 , pp. 1-14
    • Kots, A.Y.1    Martin, E.2    Sharina, I.G.3    Murad, F.4
  • 3
    • 70350145165 scopus 로고    scopus 로고
    • Distinct molecular requirements for activation or stabilization of soluble guanylyl cyclase upon haem oxidation-induced degradation
    • Hoffmann, L. S., Schmidt, P. M., Keim, Y., Schaefer, S., Schmidt, H. H. H. W., and Stasch, J. P. (2009) Distinct molecular requirements for activation or stabilization of soluble guanylyl cyclase upon haem oxidation-induced degradation. Br. J. Pharmacol. 157, 781-795.
    • (2009) Br. J. Pharmacol. , vol.157 , pp. 781-795
    • Hoffmann, L.S.1    Schmidt, P.M.2    Keim, Y.3    Schaefer, S.4    Schmidt, H.H.H.W.5    Stasch, J.P.6
  • 5
    • 0032190029 scopus 로고    scopus 로고
    • Functional properties of a naturally occurring isoform of soluble guanylyl cyclase
    • Russwurm, M., Behrends, S., Harteneck, C., and Koesling, D. (1998) Functional properties of a naturally occurring isoform of soluble guanylyl cyclase. Biochem. J. 335, 125-130. (Pubitemid 28477058)
    • (1998) Biochemical Journal , vol.335 , Issue.1 , pp. 125-130
    • Russwurm, M.1    Behrends, S.2    Harteneck, C.3    Koesling, D.4
  • 6
    • 79958128614 scopus 로고    scopus 로고
    • Soluble guanylate cyclase as an emerging therapeutic target in cardiopulmonary disease
    • Stasch, J.-P., Pacher, P., and Evgenov, O. V. (2011) Soluble guanylate cyclase as an emerging therapeutic target in cardiopulmonary disease. Circulation 123, 2263-2273.
    • (2011) Circulation , vol.123 , pp. 2263-2273
    • Stasch, J.-P.1    Pacher, P.2    Evgenov, O.V.3
  • 7
    • 0029122910 scopus 로고
    • Potent and selective inhibition of nitric oxide-sensitive guanylyl cyclase by 1H-[1,2,4]oxadiazolo[4,3-a]quinoxalin-1-one
    • Garthwaite, J., Southam, E., Boulton, C. L., Nielsen, E. B., Schmidt, K., and Mayer, B. (1995) Potent and selective inhibition of nitric oxide-sensitive guanylyl cyclase by 1H-[1,2,4]oxadiazolo[4,3-a]quinoxalin-1-one. Mol. Pharmacol. 48, 184-188.
    • (1995) Mol. Pharmacol. , vol.48 , pp. 184-188
    • Garthwaite, J.1    Southam, E.2    Boulton, C.L.3    Nielsen, E.B.4    Schmidt, K.5    Mayer, B.6
  • 9
    • 2442506761 scopus 로고    scopus 로고
    • Differential inhibition of adenylyl cyclase isoforms and soluble guanylyl cyclase by purine and pyrimidine nucleotides
    • DOI 10.1074/jbc.M312560200
    • Gille, A., Lushington, G. H., Mou, T.-C., Doughty, M. B., Johnson, R. A., and Seifert, R. (2004) Differential inhibition of adenylyl cyclase isoforms and soluble guanylyl cyclase by purine and pyrimidine nucleotides. J. Biol. Chem. 279, 19955-19969. (Pubitemid 38623438)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.19 , pp. 19955-19969
    • Gille, A.1    Lushington, G.H.2    Mou, T.-C.3    Doughty, M.B.4    Johnson, R.A.5    Seifert, R.6
  • 11
    • 79960380978 scopus 로고    scopus 로고
    • Structureactivity relationships for the interactions of 2'-and 3'-(O)-(Nmethyl) anthraniloyl-substituted purine and pyrimidine nucleotides with mammalian adenylyl cyclases
    • Pinto, C., Lushington, G. H., Richter, M., Gille, A., Geduhn, J., König, B., Mou, T.-C., Sprang, S. R., and Seifert, R. (2011) Structureactivity relationships for the interactions of 2'-and 3'-(O)-(Nmethyl) anthraniloyl-substituted purine and pyrimidine nucleotides with mammalian adenylyl cyclases. Biochem. Pharmacol. 82, 358-370.
    • (2011) Biochem. Pharmacol. , vol.82 , pp. 358-370
    • Pinto, C.1    Lushington, G.H.2    Richter, M.3    Gille, A.4    Geduhn, J.5    König, B.6    Mou, T.-C.7    Sprang, S.R.8    Seifert, R.9
  • 12
    • 0014670941 scopus 로고
    • Guanyl cyclase, an enzyme catalyzing the formation of guanosine 3',5'-monophosphate from guanosine triphosphate
    • Hardman, J. G., and Sutherland, E. W. (1969) Guanyl cyclase, an enzyme catalyzing the formation of guanosine 3',5'-monophosphate from guanosine triphosphate. J. Biol. Chem. 244, 6363-6370.
    • (1969) J. Biol. Chem. , vol.244 , pp. 6363-6370
    • Hardman, J.G.1    Sutherland, E.W.2
  • 13
    • 0019436231 scopus 로고
    • Rat brain guanylate cyclase. Purification, amphiphilic properties and immunological characterization
    • Zwiller, J., Basset, P., and Mandel, P. (1981) Rat brain guanylate cyclase. Purification, amphiphilic properties and immunological characterization. Biochim. Biophys. Acta 658, 64-75. (Pubitemid 11145387)
    • (1981) Biochimica et Biophysica Acta , vol.658 , Issue.1 , pp. 64-75
    • Zwiller, J.1    Basset, P.2    Mandel, P.3
  • 14
    • 0018429261 scopus 로고
    • Synthesis of adenosine 3',5'-monophosphate by guanylate cyclase: A new pathway for its formation
    • Mittal, C. K., Braughler, J. M., Ichihara, K., and Murad, F. (1979) Synthesis of adenosine 3',5'-monophosphate by guanylate cyclase, a new pathway for its formation. Biochim. Biophys. Acta 585, 333-342. (Pubitemid 9209697)
    • (1979) Biochimica et Biophysica Acta , vol.585 , Issue.3 , pp. 333-342
    • Mittal, C.K.1    Braughler, J.M.2    Ichihara, K.3    Murad, F.4
  • 15
    • 68249125117 scopus 로고    scopus 로고
    • Nucleotide regulation of soluble guanylate cyclase substrate specificity
    • Derbyshire, E. R., Fernhoff, N. B., Deng, S., and Marletta, M. A. (2009) Nucleotide regulation of soluble guanylate cyclase substrate specificity. Biochemistry 48, 7519-7524.
    • (2009) Biochemistry , vol.48 , pp. 7519-7524
    • Derbyshire, E.R.1    Fernhoff, N.B.2    Deng, S.3    Marletta, M.A.4
  • 16
    • 0016431380 scopus 로고
    • Enzymatic formation of inosine 3',5'-monophosphate and of 2'-deoxyguanosine 3',5'-monophosphate. Inosinate and deoxyguanylate cyclase activity
    • Garbers, D. L., Suddath, J. L., and Hardman, J. G. (1975) Enzymatic formation of inosine 3',5'-monophosphate and of 2'-deoxyguanosine 3',5'-monophosphate. Inosinate and deoxyguanylate cyclase activity. Biochim. Biophys. Acta 377, 174-185.
    • (1975) Biochim. Biophys. Acta , vol.377 , pp. 174-185
    • Garbers, D.L.1    Suddath, J.L.2    Hardman, J.G.3
  • 17
    • 0019879880 scopus 로고
    • Soluble guanylate cyclase purified from bovine lung contains heme and copper
    • Gerzer, R., Böhme, E., Hofmann, F., and Schultz, G. (1981) Soluble guanylate cyclase purified from bovine lung contains heme and copper. FEBS Lett. 132, 71-74.
    • (1981) FEBS Lett. , vol.132 , pp. 71-74
    • Gerzer, R.1    Böhme, E.2    Hofmann, F.3    Schultz, G.4
  • 18
    • 0019377619 scopus 로고
    • Purification of soluble guanylate cyclase without loss of stimulation by sodium nitroprusside
    • Gerzer, R., Hofmann, F., Böhme, E., Ivanova, K., Spies, C., and Schultz, G. (1981) Purification of soluble guanylate cyclase without loss of stimulation by sodium nitroprusside. Adv. Cyclic Nucleotide Res. 14, 255-261.
    • (1981) Adv. Cyclic Nucleotide Res. , vol.14 , pp. 255-261
    • Gerzer, R.1    Hofmann, F.2    Böhme, E.3    Ivanova, K.4    Spies, C.5    Schultz, G.6
  • 19
    • 0019495457 scopus 로고
    • Purification of a soluble, sodium nitroprusside-stimulated guanylate cyclase from bovine lung
    • DOI 10.1111/j.1432-1033.1981.tb05361.x
    • Gerzer, R., Hofmann, F., and Schultz, G. (1981) Purification of a soluble, sodium-nitroprusside-stimulated guanylate cyclase from bovine lung. Eur. J. Biochem. 116, 479-486. (Pubitemid 11055723)
    • (1981) European Journal of Biochemistry , vol.116 , Issue.3 , pp. 479-486
    • Gerzer, R.1    Hofmann, F.2    Schultz, G.3
  • 20
    • 0021749668 scopus 로고
    • Atrial natriuretic factor selectively activates particulate guanylate cyclase and elevates cyclic GMP in rat tissues
    • Waldman, S. A., Rapoport, R. M., and Murad, F. (1984) Atrial natriuretic factor selectively activates particulate guanylate cyclase and elevates cyclic GMP in rat tissues. J. Biol. Chem. 259, 14332-14334. (Pubitemid 15222241)
    • (1984) Journal of Biological Chemistry , vol.259 , Issue.23 , pp. 14332-14334
    • Waldman, S.A.1    Rapoport, R.M.2    Murad, F.3
  • 21
    • 0026782219 scopus 로고
    • Enzyme immunoassays for the estimation of adenosine 3',5'-cyclic monophosphate and guanosine 3',5'-cyclic monophosphate in biological fluids
    • Horton, J. K., Martin, R. C., Kalinka, S., Cushing, A., Kitcher, J. P., O'Sullivan, M. J., and Baxendale, P. M. (1992) Enzyme immunoassays for the estimation of adenosine 3',5'-cyclic monophosphate and guanosine 3',5'-cyclic monophosphate in biological fluids. J. Immunol. Methods 155, 31-40.
    • (1992) J. Immunol. Methods , vol.155 , pp. 31-40
    • Horton, J.K.1    Martin, R.C.2    Kalinka, S.3    Cushing, A.4    Kitcher, J.P.5    O'Sullivan, M.J.6    Baxendale, P.M.7
  • 22
    • 79961168055 scopus 로고    scopus 로고
    • Quantification of cAMP and cGMP analogs in intact cells: Pitfalls in enzyme immunoassays for cyclic nucleotides
    • Werner, K., Schwede, F., Genieser, H.-G., Geiger, J., and Butt, E. (2011) Quantification of cAMP and cGMP analogs in intact cells: Pitfalls in enzyme immunoassays for cyclic nucleotides. Naunyn-Schmiedeberg's Arch. Pharmacol. 384, 169-176.
    • (2011) Naunyn-Schmiedeberg's Arch. Pharmacol. , vol.384 , pp. 169-176
    • Werner, K.1    Schwede, F.2    Genieser, H.-G.3    Geiger, J.4    Butt, E.5
  • 23
    • 0033016797 scopus 로고    scopus 로고
    • Purified soluble guanylyl cyclase expressed in a baculovirus/Sf9 system: Stimulation by YC-1, nitric oxide, and carbon monoxide
    • Hoenicka, M., Becker, E. M., Apeler, H., Sirichoke, T., Schröder, H., Gerzer, R., and Stasch, J. P. (1999) Purified soluble guanylyl cyclase expressed in a baculovirus/Sf9 system: Stimulation by YC-1, nitric oxide, and carbon monoxide. J. Mol. Med. 77, 14-23. (Pubitemid 29146177)
    • (1999) Journal of Molecular Medicine , vol.77 , Issue.1 , pp. 14-23
    • Hoenicka, M.1    Becker, E.-M.2    Apeler, H.3    Sirichoke, T.4    Schroder, H.5    Gerzer, R.6    Stasch, J.-P.7
  • 29
    • 15744395310 scopus 로고    scopus 로고
    • Nitric oxide-dependent allosteric inhibitory role of a second nucleotide binding site in soluble guanylyl cyclase
    • DOI 10.1074/jbc.M412203200
    • Chang, F.-J., Lemme, S., Sun, Q., Sunahara, R. K., and Beuve, A. (2005) Nitric oxide-dependent allosteric inhibitory role of a second nucleotide binding site in soluble guanylyl cyclase. J. Biol. Chem. 280, 11513-11519. (Pubitemid 40418462)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.12 , pp. 11513-11519
    • Chang, F.-J.1    Lemme, S.2    Sun, Q.3    Sunahara, R.K.4    Beuve, A.5
  • 31
    • 0038175019 scopus 로고    scopus 로고
    • Mechanisms of nitric oxide independent activation of soluble guanylyl cyclase
    • DOI 10.1016/S0014-2999(03)01674-1
    • Schmidt, P., Schramm, M., Schröder, H., and Stasch, J.-P. (2003) Mechanisms of nitric oxide independent activation of soluble guanylyl cyclase. Eur. J. Pharmacol. 468, 167-174. (Pubitemid 36712896)
    • (2003) European Journal of Pharmacology , vol.468 , Issue.3 , pp. 167-174
    • Schmidt, P.1    Schramm, M.2    Schroder, H.3    Stasch, J.-P.4
  • 33
    • 0030796164 scopus 로고    scopus 로고
    • Purification of bovine soluble guanylate cyclase and ADP-ribosylation on its small subunit by bacterial toxins
    • Tomita, T., Tsuyama, S., Imai, Y., and Kitagawa, T. (1997) Purification of bovine soluble guanylate cyclase and ADP-ribosylation on its small subunit by bacterial toxins. J. Biochem. 122, 531-536. (Pubitemid 27443228)
    • (1997) Journal of Biochemistry , vol.122 , Issue.3 , pp. 531-536
    • Tomita, T.1    Tsuyama, S.2    Imai, Y.3    Kitagawa, T.4
  • 34
    • 0028861061 scopus 로고
    • Heme stoichiometry of heterodimeric soluble guanylate cyclase
    • Stone, J. R., and Marletta, M. A. (1995) Heme stoichiometry of heterodimeric soluble guanylate cyclase. Biochemistry 34, 14668-14674.
    • (1995) Biochemistry , vol.34 , pp. 14668-14674
    • Stone, J.R.1    Marletta, M.A.2
  • 36
    • 0020198013 scopus 로고
    • Purification and properties of heme-deficient hepatic soluble guanylate cyclase: Effects of heme and other factors on enzyme activation by NO, NO-heme, and protoporphyrin IX
    • Ohlstein, E. H., Wood, K. S., and Ignarro, L. J. (1982) Purification and properties of heme-deficient hepatic soluble guanylate cyclase: Effects of heme and other factors on enzyme activation by NO, NO-heme, and protoporphyrin IX. Arch. Biochem. Biophys. 218, 187-198.
    • (1982) Arch. Biochem. Biophys. , vol.218 , pp. 187-198
    • Ohlstein, E.H.1    Wood, K.S.2    Ignarro, L.J.3
  • 37
    • 0020485917 scopus 로고
    • Activation of purified guanylate cyclase by nitric oxide requires heme. Comparison of heme-deficient, hemereconstituted and heme-containing forms of soluble enzyme from bovine lung
    • Ignarro, L. J., Degnan, J. N., Baricos, W. H., Kadowitz, P. J., and Wolin, M. S. (1982) Activation of purified guanylate cyclase by nitric oxide requires heme. Comparison of heme-deficient, hemereconstituted and heme-containing forms of soluble enzyme from bovine lung. Biochim. Biophys. Acta 718, 49-59.
    • (1982) Biochim. Biophys. Acta , vol.718 , pp. 49-59
    • Ignarro, L.J.1    Degnan, J.N.2    Baricos, W.H.3    Kadowitz, P.J.4    Wolin, M.S.5
  • 38
    • 33746824191 scopus 로고    scopus 로고
    • Functional characterization of two nucleotide-binding sites in soluble guanylate cyclase
    • DOI 10.1074/jbc.M508983200
    • Yazawa, S., Tsuchiya, H., Hori, H., and Makino, R. (2006) Functional characterization of two nucleotide-binding sites in soluble guanylate cyclase. J. Biol. Chem. 281, 21763-21770. (Pubitemid 44181880)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.31 , pp. 21763-21770
    • Yazawa, S.1    Tsuchiya, H.2    Hori, H.3    Makino, R.4
  • 39
    • 0017709382 scopus 로고
    • Cytidine 3',5' monophosphate (cyclic CMP) formation in mammalian tissues
    • Cech, S. Y., and Ignarro, L. J. (1977) Cytidine 3',5'-monophosphate (cyclic CMP) formation in mammalian tissues. Science 198, 1063-1065. (Pubitemid 8239007)
    • (1977) Science , vol.198 , Issue.4321 , pp. 1063-1065
    • Cech, S.Y.1    Ignarro, L.J.2
  • 40
    • 0018790489 scopus 로고
    • Cytidylate cyclase: The product isolated by the method of Cech and Ignarro is not cytidine 3',5'-monophosphate
    • Gaion, R. M., and Krishna, G. (1979) Cytidylate cyclase: The product isolated by the method of Cech and Ignarro is not cytidine 3',5'-monophosphate. Biochem. Biophys. Res. Commun. 86, 105-111.
    • (1979) Biochem. Biophys. Res. Commun. , vol.86 , pp. 105-111
    • Gaion, R.M.1    Krishna, G.2
  • 41
    • 0020424976 scopus 로고
    • Cyclic cytidine 3',5'-monophosphate (cCMP) in cell regulation
    • DOI 10.1016/0303-7207(82)90134-4
    • Anderson, T. R. (1982) Cyclic cytidine 3',5'-monophosphate (cCMP) in cell regulation. Mol. Cell. Endocrinol. 28, 373-385. (Pubitemid 13253568)
    • (1982) Molecular and Cellular Endocrinology , vol.28 , Issue.3 , pp. 373-385
    • Anderson, T.R.1
  • 42
    • 0024408678 scopus 로고
    • Cytidylate cyclase activity in mouse tissues: The enzymatic conversion of cytidine 5'-triphosphate to cytidine 3',5'-cyclic monophosphate (cyclic CMP)
    • DOI 10.1016/0304-4165(89)90163-3
    • Yamamoto, I., Takai, T., and Mori, S. (1989) Cytidylate cyclase activity in mouse tissues: The enzymatic conversion of cytidine 5'-triphosphate to cytidine 3',5'-cyclic monophosphate (cyclic CMP). Biochim. Biophys. Acta 993, 191-198. (Pubitemid 20004636)
    • (1989) Biochimica et Biophysica Acta - General Subjects , vol.993 , Issue.2-3 , pp. 191-198
    • Yamamoto, I.1    Takai, T.2    Mori, S.3
  • 43
    • 0025141725 scopus 로고
    • Cytidylate cyclase: development of assay and determination of kinetic properties of a cytidine 3',5'-cyclic monophosphate-synthesizing enzyme
    • Newton, R. P., Salvage, B. J., and Hakeem, N. A. (1990) Cytidylate cyclase: Development of assay and determination of kinetic properties of a cytidine 3',5'-cyclic monophosphate-synthesizing enzyme. Biochem. J. 265, 581-586. (Pubitemid 20042006)
    • (1990) Biochemical Journal , vol.265 , Issue.2 , pp. 581-586
    • Newton, R.P.1    Salvage, B.J.2    Hakeem, N.A.3
  • 44
    • 0027219857 scopus 로고
    • Cytidylate cyclase activity is stimulated via activation of a guanine nucleotide-binding protein
    • DOI 10.1016/0024-3205(93)90283-9
    • Muto, N., Kanoh, M., and Yamamoto, I. (1993) Cytidylate cyclase activity is stimulated via activation of a guanine nucleotidebinding protein. Life Sci. 52, 13-20. (Pubitemid 223039978)
    • (1993) Life Sciences , vol.52 , Issue.1 , pp. 13-20
    • Muto, N.1    Kanoh, M.2    Yamamoto, I.3
  • 45
    • 35548977224 scopus 로고    scopus 로고
    • Dimerization region of soluble guanylate cyclase characterized by bimolecular fluorescence complementation in vivo
    • DOI 10.1124/mol.107.036368
    • Rothkegel, C., Schmidt, P. M., Atkins, D.-J., Hoffmann, L. S., Schmidt, H. H. H. W., Schröder, H., and Stasch, J.-P. (2007) Dimerization region of soluble guanylate cyclase characterized by bimolecular fluorescence complementation in vivo. Mol. Pharmacol. 72, 1181-1190. (Pubitemid 350012592)
    • (2007) Molecular Pharmacology , vol.72 , Issue.5 , pp. 1181-1190
    • Rothkegel, C.1    Schmidt, P.M.2    Atkins, D.-J.3    Hoffmann, L.S.4    Schmidt, H.H.H.W.5    Schroder, H.6    Stasch, J.-P.7
  • 46
    • 0021233449 scopus 로고
    • Extraction, purification and identification of cytidine 3',5'-cyclic monophosphate from rat tissues
    • Newton, R. P., Salih, S. G., Salvage, B. J., and Kingston, E. E. (1984) Extraction, purification and identification of cytidine 3',5'-cyclic monophosphate from rat tissues. Biochem. J. 221, 665-673. (Pubitemid 14061648)
    • (1984) Biochemical Journal , vol.221 , Issue.3 , pp. 665-673
    • Newton, R.P.1    Salih, S.G.2    Salvage, B.J.3    Kingston, E.E.4
  • 47
    • 0022449218 scopus 로고
    • Extraction, purification, identification and metabolism of 3',5'-cyclic UMP, 3',5'-cyclic IMP and 3',5'-cyclic dTMP from rat tissues
    • Newton, R. P., Kingston, E. E., Hakeem, N. A., Salih, S. G., Beynon, J. H., and Moyse, C. D. (1986) Extraction, purification, identification and metabolism of 3',5'-cyclic UMP, 3',5'-cyclic IMP and 3',5'-cyclic dTMP from rat tissues. Biochem. J. 236, 431-439. (Pubitemid 16036989)
    • (1986) Biochemical Journal , vol.236 , Issue.2 , pp. 431-439
    • Newton, R.P.1    Kingston, E.E.2    Hakeem, N.A.3
  • 48
    • 0025924062 scopus 로고
    • Differential modulation by N4,2'-O-dibutyryl cytidine 3':5'-cyclic monophosphate of neutrophil activation
    • Ervens, J., and Seifert, R. (1991) Differential modulation by N4,2'-O-dibutyryl cytidine 3':5'-cyclic monophosphate of neutrophil activation. Biochem. Biophys. Res. Commun. 174, 258-267.
    • (1991) Biochem. Biophys. Res. Commun. , vol.174 , pp. 258-267
    • Ervens, J.1    Seifert, R.2
  • 49
    • 77956908953 scopus 로고    scopus 로고
    • Cyclic cytidine 3',5'-monophosphate (cCMP) signals via cGMP kinase i
    • Desch, M., Schinner, E., Kees, F., Hofmann, F., Seifert, R., and Schlossmann, J. (2010) Cyclic cytidine 3',5'-monophosphate (cCMP) signals via cGMP kinase I. FEBS Lett. 584, 3979-3984.
    • (2010) FEBS Lett. , vol.584 , pp. 3979-3984
    • Desch, M.1    Schinner, E.2    Kees, F.3    Hofmann, F.4    Seifert, R.5    Schlossmann, J.6
  • 50
    • 80054064690 scopus 로고    scopus 로고
    • Human cyclic nucleotide phosphodiesterases possess a much broader substrate-specificity than previously appreciated
    • Reinecke, D., Burhenne, H., Sandner, P., Kaever, V., and Seifert, R. (2011) Human cyclic nucleotide phosphodiesterases possess a much broader substrate-specificity than previously appreciated. FEBS Lett. 585, 3259-3262.
    • (2011) FEBS Lett. , vol.585 , pp. 3259-3262
    • Reinecke, D.1    Burhenne, H.2    Sandner, P.3    Kaever, V.4    Seifert, R.5
  • 51
    • 84855880193 scopus 로고    scopus 로고
    • Differential activation of cAMP-and cGMP-dependent protein kinases by cyclic purine and pyrimidine nucleotides
    • Wolter, S., Golombek, M., and Seifert, R. (2011) Differential activation of cAMP-and cGMP-dependent protein kinases by cyclic purine and pyrimidine nucleotides. Biochem. Biophys. Res. Commun., 415, 563-566.
    • (2011) Biochem. Biophys. Res. Commun. , vol.415 , pp. 563-566
    • Wolter, S.1    Golombek, M.2    Seifert, R.3
  • 52
    • 0033553404 scopus 로고    scopus 로고
    • Activation of distinct cAMP-dependent and cGMP-dependent pathways by nitric oxide in cardiac myocytes
    • Vila-Petroff, M. G., Younes, A., Egan, J., Lakatta, E. G., and Sollott, S. J. (1999) Activation of distinct cAMP-dependent and cGMP-dependent pathways by nitric oxide in cardiac myocytes. Circ. Res. 84, 1020-1031. (Pubitemid 29227681)
    • (1999) Circulation Research , vol.84 , Issue.9 , pp. 1020-1031
    • Vila-Petroff, M.G.1    Younes, A.2    Egan, J.3    Lakatta, E.G.4    Sollott, S.J.5
  • 54
    • 0038273373 scopus 로고    scopus 로고
    • Nitric oxide protects neuroblastoma cells from apoptosis induced by serum deprivation through cAMP-response element-binding protein (CREB) activation
    • DOI 10.1074/jbc.M206177200
    • Ciani, E., Guidi, S., Della Valle, G., Perini, G., Bartesaghi, R., and Contestabile, A. (2002) Nitric oxide protects neuroblastoma cells from apoptosis induced by serum deprivation through cAMP-response element-binding protein (CREB) activation. J. Biol. Chem. 277, 49896-49902. (Pubitemid 36014438)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.51 , pp. 49896-49902
    • Ciani, E.1    Guidi, S.2    Della Valle, G.3    Perini, G.4    Bartesaghi, R.5    Contestabile, A.6
  • 56
    • 22744452514 scopus 로고    scopus 로고
    • Bacillus anthracis oedema toxin as a cause of tissue necrosis and cell type-specific cytotoxicity
    • DOI 10.1111/j.1462-5822.2005.00539.x
    • Voth, D. E., Hamm, E. E., Nguyen, L. G., Tucker, A. E., Salles, I. I., Ortiz-Leduc, W., and Ballard, J. D. (2005) Bacillus anthracis oedema toxin as a cause of tissue necrosis and cell type-specific cytotoxicity. Cell. Microbiol. 7, 1139-1149. (Pubitemid 41030939)
    • (2005) Cellular Microbiology , vol.7 , Issue.8 , pp. 1139-1149
    • Voth, D.E.1    Hamm, E.E.2    Nguyen, L.G.3    Tucker, A.E.4    Salles, I.I.5    Ortiz-Leduc, W.6    Ballard, J.D.7
  • 58
    • 0034938530 scopus 로고    scopus 로고
    • Potential mechanisms for the inhibition of tumor cell growth by manganese superoxide dismutase
    • Kim, K. H., Rodriguez, A. M., Carrico, P. M., and Melendez, J. A. (2001) Potential mechanisms for the inhibition of tumor cell growth by manganese superoxide dismutase. Antioxid. Redox Signaling 3, 361-373. (Pubitemid 32646028)
    • (2001) Antioxidants and Redox Signaling , vol.3 , Issue.3 , pp. 361-373
    • Kim, K.-H.1    Rodriguez, A.M.2    Carrico, P.M.3    Melendez, J.A.4
  • 60
    • 77955246054 scopus 로고    scopus 로고
    • Trace element status in hemodialysis patients
    • Rucker, D., Thadhani, R., and Tonelli, M. (2010) Trace element status in hemodialysis patients. Semin. Dial. 23, 389-395.
    • (2010) Semin. Dial. , vol.23 , pp. 389-395
    • Rucker, D.1    Thadhani, R.2    Tonelli, M.3
  • 61
    • 70349562761 scopus 로고    scopus 로고
    • Manganese and birth outcome
    • Wood, R. J. (2009) Manganese and birth outcome. Nutr. Rev. 67, 416-420.
    • (2009) Nutr. Rev. , vol.67 , pp. 416-420
    • Wood, R.J.1
  • 63
    • 79957857244 scopus 로고    scopus 로고
    • Intracellular cAMP signaling by soluble adenylyl cyclase
    • Tresguerres, M., Levin, L. R., and Buck, J. (2011) Intracellular cAMP signaling by soluble adenylyl cyclase. Kidney Int. 79, 1277-1288.
    • (2011) Kidney Int. , vol.79 , pp. 1277-1288
    • Tresguerres, M.1    Levin, L.R.2    Buck, J.3
  • 64
    • 33749665081 scopus 로고    scopus 로고
    • Compartmentation of cyclic nucleotide signaling in the heart: The role of cyclic nucleotide phosphodiesterases
    • DOI 10.1161/01.RES.0000246118.98832.04, PII 0000301220061013000007
    • Fischmeister, R., Castro, L. R. V., Abi-Gerges, A., Rochais, F., Jurevicius, J., Leroy, J., and Vandecasteele, G. (2006) Compartmentation of cyclic nucleotide signaling in the heart: The role of cyclic nucleotide phosphodiesterases. Circ. Res. 99, 816-828. (Pubitemid 44556380)
    • (2006) Circulation Research , vol.99 , Issue.8 , pp. 816-828
    • Fischmeister, R.1    Castro, L.R.V.2    Abi-Gerges, A.3    Rochais, F.4    Jurevicius, J.5    Leroy, J.6    Vandecasteele, G.7
  • 65
    • 80255125995 scopus 로고    scopus 로고
    • Impact of divalent metal ions on regulation of adenylyl cyclase isoforms by forskolin analogs
    • Erdorf, M., Mou, T.-C., and Seifert, R. (2011) Impact of divalent metal ions on regulation of adenylyl cyclase isoforms by forskolin analogs. Biochem. Pharmacol. 82, 1673-1681.
    • (2011) Biochem. Pharmacol. , vol.82 , pp. 1673-1681
    • Erdorf, M.1    Mou, T.-C.2    Seifert, R.3
  • 66
    • 33847111062 scopus 로고    scopus 로고
    • Biochemical and pharmacological characterization of P-site inhibitors on homodimeric guanylyl cyclase domain from natriuretic peptide receptor-A
    • DOI 10.1016/j.bcp.2006.12.008, PII S0006295206008148
    • Joubert, S., McNicoll, N., and De Léan, A. (2007) Biochemical and pharmacological characterization of P-site inhibitors on homodimeric guanylyl cyclase domain from natriuretic peptide receptor-A. Biochem. Pharmacol. 73, 954-963. (Pubitemid 46283581)
    • (2007) Biochemical Pharmacology , vol.73 , Issue.7 , pp. 954-963
    • Joubert, S.1    McNicoll, N.2    De Lean, A.3
  • 67
    • 33747624168 scopus 로고    scopus 로고
    • Broad specificity of mammalian adenylyl cyclase for interaction with 2',3'-substituted purine- and pyrimidine nucleotide inhibitors
    • DOI 10.1124/mol.106.026427
    • Mou, T.-C., Gille, A., Suryanarayana, S., Richter, M., Seifert, R., and Sprang, S. R. (2006) Broad specificity of mammalian adenylyl cyclase for interaction with 2',3'-substituted purine and pyrimidine nucleotide inhibitors. Mol. Pharmacol. 70, 878-886. (Pubitemid 44268445)
    • (2006) Molecular Pharmacology , vol.70 , Issue.3 , pp. 878-886
    • Mou, T.-C.1    Gille, A.2    Suryanarayana, S.3    Richter, M.4    Seifert, R.5    Sprang, S.R.6
  • 68
    • 14844299755 scopus 로고    scopus 로고
    • Structural basis for the inhibition of mammalian membrane adenylyl cyclase by 2'(3')-O-(N-methylanthraniloyl)-guanosine 5'-triphosphate
    • DOI 10.1074/jbc.M409076200
    • Mou, T.-C., Gille, A., Fancy, D. A., Seifert, R., and Sprang, S. R. (2005) Structural basis for the inhibition of mammalian membrane adenylyl cyclase by 2'(3')-O-(N-methylanthraniloyl)-guanosine 5'-triphosphate. J. Biol. Chem. 280, 7253-7261. (Pubitemid 40341283)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.8 , pp. 7253-7261
    • Mou, T.-C.1    Gille, A.2    Fancy, D.A.3    Seifert, R.4    Sprang, S.R.5
  • 69
    • 79959307998 scopus 로고    scopus 로고
    • Structural basis for the high-affinity inhibition of mammalian membranous adenylyl cyclase by 2',3'-O-(N-methylanthraniloyl)-inosine 5'-triphosphate
    • Hübner, M., Dixit, A., Mou, T.-C., Lushington, G. H., Pinto, C., Gille, A., Geduhn, J., König, B., Sprang, S. R., and Seifert, R. (2011) Structural basis for the high-affinity inhibition of mammalian membranous adenylyl cyclase by 2',3'-O-(N-methylanthraniloyl)-inosine 5'-triphosphate. Mol. Pharmacol. 80, 87-96.
    • (2011) Mol. Pharmacol. , vol.80 , pp. 87-96
    • Hübner, M.1    Dixit, A.2    Mou, T.-C.3    Lushington, G.H.4    Pinto, C.5    Gille, A.6    Geduhn, J.7    König, B.8    Sprang, S.R.9    Seifert, R.10


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