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Volumn 33, Issue 2, 1996, Pages 99-110

Multiple Substrates for cGMP-Dependent Protein Kinase from Bovine Aortic Smooth Muscle: Purification of P132

Author keywords

cGMP; cGMP dependent protein kinase; Phosphoprotein; Phosphorylation; Substrate specificity

Indexed keywords

CYCLIC AMP; CYCLIC GMP; PHOSPHOPROTEIN; PROTEIN KINASE;

EID: 0029914254     PISSN: 10181172     EISSN: 14230135     Source Type: Journal    
DOI: 10.1159/000159137     Document Type: Article
Times cited : (6)

References (55)
  • 1
    • 0021740085 scopus 로고
    • Cyclic nucleotides and regulation of vascular smooth muscle
    • Hardman JG: Cyclic nucleotides and regulation of vascular smooth muscle, J C'ardiovasc Pharmacol 1984:6:S639-S645.
    • (1984) J C'ardiovasc Pharmacol , vol.6 , pp. S639-S645
    • Hardman, J.G.1
  • 2
    • 0024599385 scopus 로고
    • Cyclic GMP and mechanisms of vasodilation
    • Lincoln TM: Cyclic GMP and mechanisms of vasodilation, Pharmacol Ther 1989:41:479-502.
    • (1989) Pharmacol Ther , vol.41 , pp. 479-502
    • Lincoln, T.M.1
  • 3
    • 0026087196 scopus 로고
    • Towards an understanding of the mechanism of action of cyclic AMP and cyclic GMP in smooth muscle relaxation
    • Lincoln TM, Cornwell TL: Towards an understanding of the mechanism of action of cyclic AMP and cyclic GMP in smooth muscle relaxation, Blood Vessels 1991;28:129-137.
    • (1991) Blood Vessels , vol.28 , pp. 129-137
    • Lincoln, T.M.1    Cornwell, T.L.2
  • 4
    • 0021063422 scopus 로고
    • Rndo-thelium-dependent relaxation in rat aorta may be mediated through cyclic GMP-dependent protein phosphorylation
    • Rapoport RM, Draznin MB, Murad F: Rndo-thelium-dependent relaxation in rat aorta may be mediated through cyclic GMP-dependent protein phosphorylation, Nature 1983:306: 174.
    • (1983) Nature , vol.306 , pp. 174
    • Rapoport, R.M.1    Draznin, M.B.2    Murad, F.3
  • 5
    • 0021305911 scopus 로고
    • Possible role of cyclic-GMP-dependent protein kinase in vascular smooth muscle function
    • Lincoln TM, Johnson RM: Possible role of cyclic-GMP-dependent protein kinase in vascular smooth muscle function, Adv Cyclic Nucleotide Protein Phosphorylation Res 1984:17: 285-296.
    • (1984) Adv Cyclic Nucleotide Protein Phosphorylation Res , vol.17 , pp. 285-296
    • Lincoln, T.M.1    Johnson, R.M.2
  • 6
    • 0023803473 scopus 로고
    • Relaxation of vascular and tracheal smooth muscle by cyclic nucleotide analogs that preferentially activate purified cGMP-de-pendent protein kinase
    • Francis SH, Noblett BD, Todd BVV, Wells JN, Corbin JD: Relaxation of vascular and tracheal smooth muscle by cyclic nucleotide analogs that preferentially activate purified cGMP-de-pendent protein kinase, Mol Pharmacol 1988; 34:506-517.
    • (1988) Mol Pharmacol , vol.34 , pp. 506-517
    • Francis, S.H.1    Noblett, B.D.2    Todd, B.3    Wells, J.N.4    Corbin, J.D.5
  • 7
    • 0026570943 scopus 로고
    • Direct evidence for cross-activation of cGMP-dependent protein kinase by cAMP in pig coronary arteries
    • Jiang FI, Colbran JL, Francis SH, Corbin JD: Direct evidence for cross-activation of cGMP-dependent protein kinase by cAMP in pig coronary arteries, J BiolChem 1992:267:1015-1019.
    • (1992) J Biolchem , vol.267 , pp. 1015-1019
    • Jiang, F.I.1    Colbran, J.L.2    Francis, S.H.3    Corbin, J.D.4
  • 10
    • 0028153785 scopus 로고
    • Rp-8-Br-guanosinc-3',5'-cyclic monophosphorothioate inhibits relaxation elicited by nitroglycerin in rabbit aorta
    • Nakazawa M, Iniai S: Rp-8-Br-guanosinc-3',5'-cyclic monophosphorothioate inhibits relaxation elicited by nitroglycerin in rabbit aorta, Eur J Pharmacol 1994:253:179-181.
    • (1994) Eur J Pharmacol , vol.253 , pp. 179-181
    • Nakazawa, M.1    Iniai, S.2
  • 11
    • 0024593414 scopus 로고
    • Properties of a eGMP-dependent monomeric protein kinase from bovine aorta
    • Wolfe L, Francis SH, Corbin JD: Properties of a eGMP-dependent monomeric protein kinase from bovine aorta, J Biol Chem 1989:264: 4157-4162.
    • (1989) J Biol Chem , vol.264 , pp. 4157-4162
    • Wolfe, L.1    Francis, S.H.2    Corbin, J.D.3
  • 12
    • 0025272150 scopus 로고
    • Taylor AE: CGMP-dependent protein kinase mediates the reduction ofCa by cAMP in vascular smooth muscle cells
    • Lincoln TM, Cornwell TL, Taylor AE: cGMP-dependent protein kinase mediates the reduction ofCa by cAMP in vascular smooth muscle cells Am J Physiol 1990:258:C399-C407.
    • (1990) Am J Physiol , vol.258 , pp. C399-C407
    • Lincoln, T.M.1    Cornwell, T.L.2
  • 13
    • 9044244438 scopus 로고
    • EDRF and cyclic GMP control gating of receptor-operated calcium channels in vascular smooth muscle
    • Godfraind T: EDRF and cyclic GMP control gating of receptor-operated calcium channels in vascular smooth muscle, Eur J Biochem 1986; 116:477-486.
    • (1986) Eur J Biochem , vol.116 , pp. 477-486
    • Godfraind, T.1
  • 14
    • 0025934147 scopus 로고
    • Cyclic GMP-dcpendent protein kinase stimulates the plasma membrane Ca2+ pump ATPasc of vascular smooth muscle via phosphorylation of a 240 kDa protein
    • 2+ pump ATPasc of vascular smooth muscle via phosphorylation of a 240 kDa protein, J Biol Chem 1991.266: 19819-19825.
    • (1991) J Biol Chem , vol.266 , pp. 19819-19825
    • Yoshida, Y.1    Sun, H.T.2    Cai, J.Q.3    Imai, S.4
  • 16
    • 0022612997 scopus 로고
    • Cyclic guanosine monophosphate inhibition of contraction may be mediated through inhibition of phosphatidyl inositol hydrolysis in rat aorta
    • Rapoporl RM: Cyclic guanosine monophosphate inhibition of contraction may be mediated through inhibition of phosphatidyl inositol hydrolysis in rat aorta, Circ Res 1986:58: 407-410.
    • (1986) Circ Res , vol.58 , pp. 407-410
    • Rapoporl, R.M.1
  • 17
    • 0025037794 scopus 로고
    • Mechanism of cyclic GMP inhibition of inositol phosphate formation in rat aorta segments and cultured bovine aortic smooth muscle cells
    • Hirata M, Koohse PK, Chang CH, Ikebe T, Murad F: Mechanism of cyclic GMP inhibition of inositol phosphate formation in rat aorta segments and cultured bovine aortic smooth muscle cells, J Biol Chent 1990;265:1268-1273.
    • (1990) J Biol Chent , vol.265 , pp. 1268-1273
    • Hirata, M.1    Koohse, P.K.2    Chang, C.H.3    Ikebe, T.4    Murad, F.5
  • 18
    • 0027533509 scopus 로고
    • Transfected cGMP-depcndent protein kinase suppresses calcium transients by inhibition of inositol 1.4.5-Tris-phosphate production
    • Ruth P, Wang GX, Boekhoff I, May B, Pfeifer A, Penner R, Korth M, Breer H, Hofmann F: Transfected cGMP-depcndent protein kinase suppresses calcium transients by inhibition of inositol 1.4.5-Tris-phosphate production, Proc Natl Acad Sci USA 1993:90:2623-2627.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 2623-2627
    • Ruth, P.1    Wang, G.X.2    Boekhoff, I.3    May, B.4    Pfeifer, A.5    Penner, R.6    Korth, M.7    Breer, H.8    Hofmann, F.9
  • 19
    • 0024358112 scopus 로고
    • Atrial natriuretic peptidc-depen-dent phosphorylation of smooth muscle cell particulate fraction proteins is mediated by cGMP-dependent protein kinase
    • Sarcevie B, Brookes V, Martin T, Kemp BE, Robinson PJ: Atrial natriuretic peptidc-depen-dent phosphorylation of smooth muscle cell particulate fraction proteins is mediated by cGMP-dependent protein kinase, J Biol Chem 1989;264:20648-20654.
    • (1989) J Biol Chem , vol.264 , pp. 20648-20654
    • Sarcevie, B.1    Brookes, V.2    Martin, T.3    Kemp, B.E.4    Robinson, P.J.5
  • 20
    • 0026319608 scopus 로고
    • Regulation of sarcoplasmic reticulum protein phosphorylation by localised cyclic GMP-dependent protein kinase in vascular smooth muscle cells
    • Cornwell TL, Pryzwansky KB, Wyatt TA, Lincoln TM: Regulation of sarcoplasmic reticulum protein phosphorylation by localised cyclic GMP-dependent protein kinase in vascular smooth muscle cells, Mol Pharmacol 1991:40: 923-931.
    • (1991) Mol Pharmacol , vol.40 , pp. 923-931
    • Cornwell, T.L.1    Pryzwansky, K.B.2    Wyatt, T.A.3    Lincoln, T.M.4
  • 22
    • 0026355413 scopus 로고
    • Protein kinase phosphorylation site sequences and consensus specificity motifs: Tabulations
    • Pearson RB, Kemp BE: Protein kinase phosphorylation site sequences and consensus specificity motifs: Tabulations, Methods Enzyntol 1991:200:62-81.
    • (1991) Methods Enzyntol , vol.200 , pp. 62-81
    • Pearson, R.B.1    Kemp, B.E.2
  • 23
    • 0026661981 scopus 로고
    • A phenylalanine in peptide substrates provides for selectivity between cGMP- and cAMP-dependent protein kinases
    • Colbran JL, Francis SH. Lcach AB, Thomas MK, Jiang H, McAllister LM, Corbin JD: A phenylalanine in peptide substrates provides for selectivity between cGMP- and cAMP-dependent protein kinases, J Biol Chem 1992: 267:9589-9594.
    • (1992) J Biol Chem , vol.267 , pp. 9589-9594
    • Colbran, J.L.1    Francis, S.H.2    Lcach, A.B.3    Thomas, M.K.4    Jiang, H.5    McAllister, L.M.6    Corbin, J.D.7
  • 24
    • 0018967406 scopus 로고
    • Cyclic-GMP-dependcnt protein phosphorylation in intact medial tissue and isolated cells from vascular smooth muscle
    • Casnellic JE, Ives HE, Jamieson JD, Grecn-gard P: Cyclic-GMP-dependcnt protein phosphorylation in intact medial tissue and isolated cells from vascular smooth muscle, J Biol Chem 1980;255:3770-3776.
    • (1980) J Biol Chem , vol.255 , pp. 3770-3776
    • Casnellic, J.E.1    Ives, H.E.2    Jamieson, J.D.3    Grecn-Gard, P.4
  • 25
    • 0018933757 scopus 로고
    • Subccllular localization of cyclic-GMP-dependent protein kinase and its substrates in vascular smooth muscle
    • Ives HE, Casnellie JE, Greengard P, Jamieson JD: Subccllular localization of cyclic-GMP-dependent protein kinase and its substrates in vascular smooth muscle, J Biol Chem 1980: 255:3777-3785.
    • (1980) J Biol Chem , vol.255 , pp. 3777-3785
    • Ives, H.E.1    Casnellie, J.E.2    Greengard, P.3    Jamieson, J.D.4
  • 26
    • 0023351646 scopus 로고
    • The cyclic nucleotide-dependent phosphorylation of aortic smooth muscle membrane proteins
    • Parks TP, Naim AG, Greengard P, Jamieson JD: The cyclic nucleotide-dependent phosphorylation of aortic smooth muscle membrane proteins, Arch Biochem Biophys 1987: 255:361-371.
    • (1987) Arch Biochem Biophys , vol.255 , pp. 361-371
    • Parks, T.P.1    Naim, A.G.2    Greengard, P.3    Jamieson, J.D.4
  • 27
    • 0025083471 scopus 로고
    • The smooth muscle 132 kDa cyclic GMP-dependcnt protein kinase substrate is not myosin light chain kinase or caldesmon
    • Sarcevic B, Robinson PJ, Pearson RB, Kemp BE: The smooth muscle 132 kDa cyclic GMP-dependcnt protein kinase substrate is not myosin light chain kinase or caldesmon, Biochem J 1990:271:493-499.
    • (1990) Biochem J , vol.271 , pp. 493-499
    • Sarcevic, B.1    Robinson, P.J.2    Pearson, R.B.3    Kemp, B.E.4
  • 28
    • 0027404913 scopus 로고
    • Intracellular cyclic GMP receptor proteins
    • Lincoln TM, Cornwell TL: Intracellular cyclic GMP receptor proteins, FASEB J 1993:7:328- 338.
    • (1993) FASEB J , vol.7
    • Lincoln, T.M.1    Cornwell, T.L.2
  • 29
    • 0028206486 scopus 로고
    • Purification and characterization of 240-kDa cGMP-depcndent protein kinase substrate of vascular smooth muscle, Close resemblance to inositol 1.4.5-Tris-phosphatc receptor
    • Koga T, Yoshida Y, Cai J-Q, Islam MO, Imai S: Purification and characterization of 240-kDa cGMP-depcndent protein kinase substrate of vascular smooth muscle, Close resemblance to inositol 1.4.5-Tris-phosphatc receptor, J Biol Chem 1994:269:11640-11647.
    • (1994) J Biol Chem , vol.269 , pp. 11640-11647
    • Koga, T.1    Yoshida, Y.2    Cai, J.-Q.3    Islam, M.O.4    Imai, S.5
  • 30
    • 0028307619 scopus 로고
    • Phosphorylation of the inositol 1.4.5-Tris-phosphate receptor by cyclic GMP-dcpendent protein kinase
    • Komalavilas P, Lincoln TM: Phosphorylation of the inositol 1.4.5-Tris-phosphate receptor by cyclic GMP-dcpendent protein kinase, J Biol Chem 1994;269:8701-8707.
    • (1994) J Biol Chem , vol.269 , pp. 8701-8707
    • Komalavilas, P.1    Lincoln, T.M.2
  • 31
    • 0021251669 scopus 로고
    • Effects of cAMP- and cGMP-dependent protein kinases, and calmodulin on Ca2+ uptake by highly purified sarcolemmal vesicles of vascular smooth muscle
    • 2+ uptake by highly purified sarcolemmal vesicles of vascular smooth muscle, Biochim Biophys Acta 1984;773:83-90
    • (1984) Biochim Biophys Acta , vol.773 , pp. 83-90
    • Sucmatsu, F.1    Hirata, M.2    Kurivama, H.3
  • 32
    • 0011713014 scopus 로고
    • Sodium nitroprusside-induced protein phosphorylation in intact rat aorta is mimicked by 8-bromo cyclic GMP
    • Rapoport RM, Draznin MB, Murad F: Sodium nitroprusside-induced protein phosphorylation in intact rat aorta is mimicked by 8-bromo cyclic GMP, Proc Natl Acad Sci USA 1982:79: 6470-6474.
    • (1982) Proc Natl Acad Sci USA , vol.79 , pp. 6470-6474
    • Rapoport, R.M.1    Draznin, M.B.2    Murad, F.3
  • 33
    • 0024445576 scopus 로고
    • Purification of a vasodilator-regulated phosphoprotein from human platelets
    • Halbrugge M, Walter U: Purification of a vasodilator-regulated phosphoprotein from human platelets, EurJ Biochem 1989;185:41-50
    • (1989) Eurj Biochem , vol.185 , pp. 41-50
    • Halbrugge, M.1    Walter, U.2
  • 34
    • 0026563095 scopus 로고
    • The 46/50 kDa phosphoprotein VASP purified from human platelets is a novel protein associated with actin filaments and focal contacts
    • Reinhard M, Halbriigge M, Scheer U, Wiegand C, Jockusch BM, Waller U: The 46/50 kDa phosphoprotein VASP purified from human platelets is a novel protein associated with actin filaments and focal contacts, EMBO J 1992; 11: 2063-2070
    • (1992) EMBO J , vol.11 , pp. 2063-2070
    • Reinhard, M.1    Halbriigge, M.2    Scheer, U.3    Wiegand, C.4    Jockusch, B.M.5    Waller, U.6
  • 35
    • 0023161301 scopus 로고
    • Protein kinase C-mediated phosphorylation in intact cells
    • Witters LA, Blackshcar PJ: Protein kinase C-mediated phosphorylation in intact cells, Methods Enzymol 1987:141:412-424.
    • (1987) Methods Enzymol , vol.141 , pp. 412-424
    • Witters, L.A.1    Blackshcar, P.J.2
  • 36
    • 0027175638 scopus 로고
    • Activation of protein kinase C in vitro and in intact cells or synaplosomcs detenuined by acetic acid extraction of MARCKS
    • Robinson PJ, Liu J-P, Chen W, Wenzel T: Activation of protein kinase C in vitro and in intact cells or synaplosomcs detenuined by acetic acid extraction of MARCKS, Anal Biochem 1993:210:172-178.
    • (1993) Anal Biochem , vol.210 , pp. 172-178
    • Robinson, P.J.1    Liu, J.-P.2    Chen, W.3    Wenzel, T.4
  • 38
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of the bacteriophage T4
    • Laemmli UK: Cleavage of structural proteins during the assembly of the head of the bacteriophage T4. Nature 1970:227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 39
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein
    • Bradford MM: A rapid and sensitive method for the quantitation of microgram quantities of protein, Anal Biochem 1976:72:248-254.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 40
    • 0025036471 scopus 로고
    • Substrates of cGMP kinase in vascular smooth muscle and their role in the relaxation process
    • Baltensperger K, Chics M, Carafoli E: Substrates of cGMP kinase in vascular smooth muscle and their role in the relaxation process, Biochemistry 1990:29:9753-9760
    • (1990) Biochemistry , vol.29 , pp. 9753-9760
    • Baltensperger, K.1    Chics, M.2    Carafoli, E.3
  • 42
    • 0024546285 scopus 로고
    • Protein kinase C substrates from bovine brain, Purification and characterization of ncuromodulin, a neuron-specific calmodulin-binding protein
    • Baudier J, Bronner C, Kligman D, Cole RD: Protein kinase C substrates from bovine brain, Purification and characterization of ncuromodulin, a neuron-specific calmodulin-binding protein, J Biol Chem 1989;264:1824-1828.
    • (1989) J Biol Chem , vol.264 , pp. 1824-1828
    • Baudier, J.1    Bronner, C.2    Kligman, D.3    Cole, R.D.4
  • 43
    • 0016725653 scopus 로고
    • Effect of dcnaturation on the susceptibility of proteins to enzymic phosphorylation
    • Bylund DB, Krebs EG: Effect of dcnaturation on the susceptibility of proteins to enzymic phosphorylation, J Biol Chem 1975:250:6355-6361.
    • (1975) J Biol Chem , vol.250 , pp. 6355-6361
    • Bylund, D.B.1    Krebs, E.G.2
  • 44
    • 0024848484 scopus 로고
    • Physiological role of cGMP and cGMP-dependent protein kinase in the cardiovascular system
    • Walter U: Physiological role of cGMP and cGMP-dependent protein kinase in the cardiovascular system, Rev Physiol Biochem Pharmacol 1989:113:41-88.
    • (1989) Rev Physiol Biochem Pharmacol , vol.113 , pp. 41-88
    • Walter, U.1
  • 45
    • 0019320651 scopus 로고
    • Regulatory subunit of the type 1 cAMP-depcndcnt protein kinase as an inhibitor and substrate of the cGMP-depen-denl protein kinase
    • Gcahlen R, Krebs EG: Regulatory subunit of the type 1 cAMP-depcndcnt protein kinase as an inhibitor and substrate of the cGMP-depen-denl protein kinase, J Biol Chem 1980:255: 1164-1169.
    • (1980) J Biol Chem , vol.255 , pp. 1164-1169
    • Gcahlen, R.1    Krebs, E.G.2
  • 46
    • 0020349491 scopus 로고
    • Cyclic GMP-dependent protein phosphorylation in mammalian cerebellum
    • Schlichter DJ: Cyclic GMP-dependent protein phosphorylation in mammalian cerebellum, Prog Brain Res 1982:56:105-123.
    • (1982) Prog Brain Res , vol.56 , pp. 105-123
    • Schlichter, D.J.1
  • 47
    • 0025143899 scopus 로고
    • Substrate- and kinase-directed regulation of phosphorylation of a cGMP-binding phosphodiesterase by cGMP
    • Thomas MK, Francis SH, Corbin JD: Substrate- and kinase-directed regulation of phosphorylation of a cGMP-binding phosphodiesterase by cGMP, J Biol Chem 1990:265: 14964-14970
    • (1990) J Biol Chem , vol.265 , pp. 14964-14970
    • Thomas, M.K.1    Francis, S.H.2    Corbin, J.D.3
  • 48
    • 0028303913 scopus 로고
    • CAMP- and cGMP-depen-dent protein kinase phosphorylation sites of the focal adhesion vasodilator-stimulated phosphoprotein (VASP) in vitro and in intact human platelets
    • Butt E, Abel K, Krieger M, Palm D, Hoppe V, Hoppe J, Waller U: cAMP- and cGMP-depen-dent protein kinase phosphorylation sites of the focal adhesion vasodilator-stimulated phosphoprotein (VASP) in vitro and in intact human platelets, J Biol Chem 1994:269:14509- 14517.
    • (1994) J Biol Chem , vol.269
    • Butt, E.1    Abel, K.2    Krieger, M.3    Palm, D.4    Hoppe, V.5    Hoppe, J.6    Waller, U.7
  • 49
    • 0023716254 scopus 로고
    • Cyclic GMP-dependent protein kinase stimulates the plasmalemmal Ca2+ pump of smooth muscle via phosphorylation of phosphatidylinositol
    • 2+ pump of smooth muscle via phosphorylation of phosphatidylinositol, Biochem J 1988; 255:855-863.
    • (1988) Biochem J , vol.255 , pp. 855-863
    • Vrolix, M.1    Raeymaekers, L.2    Wuytack, F.3    Hofmann, F.4    Casteels, R.5
  • 50
    • 0023818957 scopus 로고
    • The Ca2+-pumping ATPasc and the major substrates of the cGMP-dependent protein kinase in smooth muscle sarcolemma arc distinct entities
    • 2+-pumping ATPasc and the major substrates of the cGMP-dependent protein kinase in smooth muscle sarcolemma arc distinct entities, EurJ Biochem 1988:172:7-16.
    • (1988) Eurj Biochem , vol.172 , pp. 7-16
    • Baltenspcrger, K.1    Carafoli, E.2    Chicsi, M.3
  • 51
    • 0343405412 scopus 로고
    • Guanosine 3':5 -cyclic monophosphate-dependent phosphorylation of endogenous substrate proteins in membranes of mammalian smooth muscle
    • Casnellie JE, Greengard P: Guanosine 3':5 -cyclic monophosphate-dependent phosphorylation of endogenous substrate proteins in membranes of mammalian smooth muscle, Proc Nall Acad Sci USA 1974:71:1891-1895.
    • (1974) Proc Nall Acad Sci USA , vol.71 , pp. 1891-1895
    • Casnellie, J.E.1    Greengard, P.2
  • 52
    • 0018192635 scopus 로고
    • Cyclic AMP-dependent phosphorylation of filamin in mammalian smooth muscle
    • Wallach D, Davies PJA, Pastan I: Cyclic AMP-dependent phosphorylation of filamin in mammalian smooth muscle, J Biol Chem 1978:253: 4739-4745.
    • (1978) J Biol Chem , vol.253 , pp. 4739-4745
    • Wallach, D.1    Davies, P.2    Pastan, I.3
  • 53
    • 0022452904 scopus 로고
    • Atrial natriuretic factor induced phosphorylation of human placental membrane protein: An effect mimicked by guano-sinc 3':5'-cyclic monophosphate
    • Sen I, Roy P: Atrial natriuretic factor induced phosphorylation of human placental membrane protein: An effect mimicked by guano-sinc 3':5'-cyclic monophosphate, Biochem Biophys Res Commun 1986:139:431-438.
    • (1986) Biochem Biophys Res Commun , vol.139 , pp. 431-438
    • Sen, I.1    Roy, P.2
  • 54
    • 0020052356 scopus 로고
    • Concerted phosphorylation of endogenous tracheal smooth muscle membrane proteins by Ca2+ calmodulin-, cyclic GMP- and cyclic AMP-dependent protein kinases
    • 2+ calmodulin-, cyclic GMP- and cyclic AMP-dependent protein kinases, FEBS Lett 1982;139:309-312.
    • (1982) FEBS Lett , vol.139 , pp. 309-312
    • Hogaboom, G.K.1    Emler, C.A.2    Butcher, F.R.3    Fcdan, J.S.4
  • 55
    • 0022501109 scopus 로고
    • Demonstration of cGMP-dependent protein kinase and cGMP-dependent phosphorylation in cell-free extracts of platelets
    • Waldmann R, Bauer S, Gobel C, Hofmann F, Jakobs KH, Walter U: Demonstration of cGMP-dependent protein kinase and cGMP-dependent phosphorylation in cell-free extracts of platelets, EurJ Biochem 1986;158:203-210.
    • (1986) Eurj Biochem , vol.158 , pp. 203-210
    • Waldmann, R.1    Bauer, S.2    Gobel, C.3    Hofmann, F.4    Jakobs, K.H.5    Walter, U.6


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