메뉴 건너뛰기




Volumn 2013, Issue , 2013, Pages

Regulation of PKC autophosphorylation by calponin in contractile vascular smooth muscle tissue

Author keywords

[No Author keywords available]

Indexed keywords

CALPONIN; PHENYLEPHRINE; PROTEIN KINASE C ALPHA; PROTEIN KINASE C EPSILON; RECOMBINANT ENZYME; ACTIN BINDING PROTEIN; ADDUCIN; CALCIUM BINDING PROTEIN; CALMODULIN BINDING PROTEIN; PROTEIN KINASE C;

EID: 84890070693     PISSN: 23146133     EISSN: 23146141     Source Type: Journal    
DOI: 10.1155/2013/358643     Document Type: Article
Times cited : (10)

References (48)
  • 1
    • 57149130977 scopus 로고    scopus 로고
    • Smooth muscle signalling pathways in health and disease: Contractility in health and disease review series
    • 2-s2.0-57149130977 10.1111/j.1582-4934.2008.00552.x
    • Kim H. R., Appel S., Vetterkind S., Gangopadhyay S. S., Morgan K. G., Smooth muscle signalling pathways in health and disease: contractility in health and disease review series. Journal of Cellular and Molecular Medicine 2008 12 6A 2165 2180 2-s2.0-57149130977 10.1111/j.1582-4934.2008.00552.x
    • (2008) Journal of Cellular and Molecular Medicine , vol.12 , Issue.6 , pp. 2165-2180
    • Kim, H.R.1    Appel, S.2    Vetterkind, S.3    Gangopadhyay, S.S.4    Morgan, K.G.5
  • 2
    • 0034921574 scopus 로고    scopus 로고
    • Invited review: Cross-bridge regulation by thin filament-associated proteins
    • Morgan K. G., Gangopadhyay S. S., Signal transduction in smooth muscle: invited review: cross-bridge regulation by thin filament-associated proteins. Journal of Applied Physiology 2001 91 2 953 962 2-s2.0-0034921574 (Pubitemid 32681131)
    • (2001) Journal of Applied Physiology , vol.91 , Issue.2 , pp. 953-962
    • Morgan, K.G.1    Gangopadhyay, S.S.2
  • 5
    • 77955295373 scopus 로고    scopus 로고
    • Protein kinase C - A family of protein kinases, allosteric effectors or both?
    • 2-s2.0-77955295373 10.1016/j.advenzreg.2009.10.004
    • Cameron A. J. M., Parker P. J., Protein kinase C-a family of protein kinases, allosteric effectors or both? Advances in Enzyme Regulation 2010 50 1 169 177 2-s2.0-77955295373 10.1016/j.advenzreg.2009.10.004
    • (2010) Advances in Enzyme Regulation , vol.50 , Issue.1 , pp. 169-177
    • Cameron, A.J.M.1    Parker, P.J.2
  • 7
    • 0026739870 scopus 로고
    • Phenylephrine-induced translocation of protein kinase C and shortening of two types of vascular cells of the ferret
    • 2-s2.0-0026739870
    • Khalil R. A., Morgan K. G., Phenylephrine-induced translocation of protein kinase C and shortening of two types of vascular cells of the ferret. The Journal of Physiology 1992 455 585 599 2-s2.0-0026739870
    • (1992) The Journal of Physiology , vol.455 , pp. 585-599
    • Khalil, R.A.1    Morgan, K.G.2
  • 11
    • 0037337159 scopus 로고    scopus 로고
    • Regulation of the ABC kinases by phosphorylation: Protein kinase C as a paradigm
    • DOI 10.1042/BJ20021626
    • Newton A. C., Regulation of the ABC kinases by phosphorylation: protein kinase C as a paradigm. Biochemical Journal 2003 370, part 2 361 371 2-s2.0-0037337159 10.1042/BJ20021626 (Pubitemid 36315124)
    • (2003) Biochemical Journal , vol.370 , Issue.2 , pp. 361-371
    • Newton, A.C.1
  • 12
    • 0037687307 scopus 로고    scopus 로고
    • Cross-regulation of novel protein kinase C (PKC) isoform function in cardiomyocytes: Role of PKCε in activation loop phosphorylations and PKCδ in hydrophobic motif phosphorylations
    • DOI 10.1074/jbc.M212644200
    • Rybin V. O., Sabri A., Short J., Braz J. C., Molkentin J. D., Steinberg S. F., Cross-regulation of novel protein kinase C (PKC) isoform function in cardiomyocytes: role of PKC ε in activation loop phosphorylations and PKC δ in hydrophobic motif phosphorylations. The Journal of Biological Chemistry 2003 278 16 14555 14564 2-s2.0-0037687307 10.1074/jbc.M212644200 (Pubitemid 36800010)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.16 , pp. 14555-14564
    • Rybin, V.O.1    Sabri, A.2    Short, J.3    Braz, J.C.4    Molkentin, J.D.5    Steinberg, S.F.6
  • 13
    • 0035413601 scopus 로고    scopus 로고
    • Protein kinase C: Structural and spatial regulation by phosphorylation, cofactors, and macromolecular interactions
    • DOI 10.1021/cr0002801
    • Newton A. C., Protein kinase C: structural and spatial regulation by phosphorylation, cofactors, and macromolecular interactions. Chemical Reviews 2001 101 8 2353 2364 2-s2.0-0035413601 10.1021/cr0002801 (Pubitemid 35373023)
    • (2001) Chemical Reviews , vol.101 , Issue.8 , pp. 2353-2364
    • Newton, A.C.1
  • 14
    • 0034651539 scopus 로고    scopus 로고
    • Multiple pathways control protein kinase C phosphorylation
    • Parekh D. B., Ziegler W., Parker P. J., Multiple pathways control protein kinase C phosphorylation. The EMBO Journal 2000 19 4 496 503 2-s2.0-0034651539 (Pubitemid 30093722)
    • (2000) EMBO Journal , vol.19 , Issue.4 , pp. 496-503
    • Parekh, D.B.1    Ziegler, W.2    Parker, P.J.3
  • 15
    • 0033198916 scopus 로고    scopus 로고
    • Multisite dephosphorylation and desensitization of conventional protein kinase C isotypes
    • DOI 10.1042/0264-6021:3420337
    • Hansra G., Garcia-Paramio P., Prevostel C., Whelan R. D. H., Bornancin F., Parker P. J., Multisite dephosphorylation and desensitization of conventional protein kinase C isotypes. Biochemical Journal 1999 342, part 2 337 344 2-s2.0-0033198916 10.1042/0264-6021:3420337 (Pubitemid 29425355)
    • (1999) Biochemical Journal , vol.342 , Issue.2 , pp. 337-344
    • Hansra, G.1    Garcia-Paramio, P.2    Prevostel, C.3    Whelan, R.D.H.4    Bornancin, F.5    Parker, P.J.6
  • 16
    • 0036566148 scopus 로고    scopus 로고
    • Regulation of novel protein kinase C ε by phosphorylation
    • DOI 10.1042/0264-6021:3630537
    • Cenni V., Döppler H., Sonnenburg E. D., Maraldi N., Newton A. C., Toker A., Regulation of novel protein kinase C ε by phosphorylation. Biochemical Journal 2002 363, part 3 537 545 2-s2.0-0036566148 10.1042/0264-6021:3630537 (Pubitemid 34526374)
    • (2002) Biochemical Journal , vol.363 , Issue.3 , pp. 537-545
    • Cenni, V.1    Doppler, H.2    Sonnenburg, E.D.3    Maraldi, N.4    Newton, A.C.5    Toker, A.6
  • 17
    • 0033565608 scopus 로고    scopus 로고
    • The hydrophobic phosphorylation motif of conventional protein kinase C is regulated by autophosphorylation
    • DOI 10.1016/S0960-9822(99)80332-7
    • Behn-Krappa A., Newton A. C., The hydrophobic phosphorylation motif of conventional protein kinase C is regulated by autophosphorylation. Current Biology 1999 9 14 728 737 2-s2.0-0033565608 10.1016/S0960-9822(99)80332-7 (Pubitemid 29350851)
    • (1999) Current Biology , vol.9 , Issue.14 , pp. 728-737
    • Behn-Krappa, A.1    Newton, A.C.2
  • 18
    • 0034668932 scopus 로고    scopus 로고
    • Changes in protein kinase C ε phosphorylation status and intracellular localization as 3T3 and 3T6 fibroblasts grow to confluency and quiescence: A role for phosphorylation at ser-729?
    • 2-s2.0-0034668932 10.1042/0264-6021:3520019
    • England K., Rumsby M. G., Changes in protein kinase C ε phosphorylation status and intracellular localization as 3T3 and 3T6 fibroblasts grow to confluency and quiescence: a role for phosphorylation at ser-729? Biochemical Journal 2000 352, part 1 19 26 2-s2.0-0034668932 10.1042/0264-6021:3520019
    • (2000) Biochemical Journal , vol.3521 , pp. 19-26
    • England, K.1    Rumsby, M.G.2
  • 19
    • 2442498430 scopus 로고    scopus 로고
    • Stimulus-specific Differences in Protein Kinase Cδ Localization and Activation Mechanisms in Cardiomyocytes
    • DOI 10.1074/jbc.M311096200
    • Rybin V. O., Guo J., Sabri A., Elouardighi H., Schaefer E., Steinberg S. F., Stimulus-specific differences in protein kinase C δ localization and activation mechanisms in cardiomyocytes. The Journal of Biological Chemistry 2004 279 18 19350 19361 2-s2.0-2442498430 10.1074/jbc.M311096200 (Pubitemid 38623366)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.18 , pp. 19350-19361
    • Rybin, V.O.1    Guo, J.2    Sabri, A.3    Elouardighi, H.4    Schaefer, E.5    Steinberg, S.F.6
  • 22
    • 0035577288 scopus 로고    scopus 로고
    • Calponin is required for agonist-induced signal transduction - Evidence from an antisense approach in ferret smooth muscle
    • DOI 10.1111/j.1469-7793.2001.00567.x
    • Je H.-D., Gangopadhyay S. S., Ashworth T. D., Morgan K. G., Calponin is required for agonist-induced signal transduction-evidence from an antisense approach in ferret smooth muscle. The Journal of Physiology 2001 537, part 2 567 577 2-s2.0-0035577288 10.1111/j.1469-7793.2001.00567.x (Pubitemid 33130510)
    • (2001) Journal of Physiology , vol.537 , Issue.2 , pp. 567-577
    • Je, H.-D.1    Gangopadhyay, S.S.2    Ashworth, T.D.3    Morgan, K.G.4
  • 23
    • 0030868556 scopus 로고    scopus 로고
    • Calponin and mitogen-activated protein kinase signaling in differentiated vascular smooth muscle
    • DOI 10.1074/jbc.272.40.25157
    • Menice C. B., Hulvershorn J., Adam L. P., Wang C.-L. A., Morgan K. G., Calponin and mitogen-activated protein kinase signaling in differentiated vascular smooth muscle. The Journal of Biological Chemistry 1997 272 40 25157 25161 2-s2.0-0030868556 10.1074/jbc.272.40.25157 (Pubitemid 27415700)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.40 , pp. 25157-25161
    • Menice, C.B.1    Hulvershorn, J.2    Adam, L.P.3    Wang, C.-L.A.4    Morgan, K.G.5
  • 24
    • 0032483386 scopus 로고    scopus 로고
    • Inhibition of membrane lipid-independent protein kinase Cα activity by phorbol esters, diacylglycerols, and bryostatin-1
    • DOI 10.1074/jbc.273.36.23160
    • Slater S. J., Taddeo F. J., Mazurek A., Stagliano B. A., Milano S. K., Kelly M. B., Ho C., Stubbs C. D., Inhibition of membrane lipid-independent protein kinase C α activity by phorbol esters, diacylglycerols, and bryostatin-1. The Journal of Biological Chemistry 1998 273 36 23160 23168 2-s2.0-0032483386 10.1074/jbc.273.36.23160 (Pubitemid 28417499)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.36 , pp. 23160-23168
    • Slater, S.J.1    Taddeo, F.J.2    Mazurek, A.3    Stagliano, B.A.4    Milano, S.K.5    Kelly, M.B.6    Ho, C.7    Stubbs, C.D.8
  • 25
    • 0032856159 scopus 로고    scopus 로고
    • Resveratrol preferentially inhibits protein kinase C-catalyzed phosphorylation of a cofactor-independent, arginine-rich protein substrate by a novel mechanism
    • DOI 10.1021/bi990875u
    • Stewart J. R., Ward N. E., Ioannides C. G., O'brian C. A., Resveratrol preferentially inhibits protein kinase C-catalyzed phosphorylation of a cofactor-independent, arginine-rich protein substrate by a novel mechanism. Biochemistry 1999 38 40 13244 13251 2-s2.0-0032856159 10.1021/bi990875u (Pubitemid 29477437)
    • (1999) Biochemistry , vol.38 , Issue.40 , pp. 13244-13251
    • Stewart, J.R.1    Ward, N.E.2    Ioannides, C.G.3    O'Brian, C.A.4
  • 26
    • 0033564497 scopus 로고    scopus 로고
    • Isozyme-specific inhibitors of protein kinase C translocation: Effects on contractility of single permeabilized vascular muscle cells of the ferret
    • DOI 10.1111/j.1469-7793.1999.0709s.x
    • Lee Y.-H., Kim I., Laporte R., Walsh M. P., Morgan K. G., Isozyme-specific inhibitors of protein kinase C translocation: effects on contractility of single permeabilized vascular muscle cells of the ferret. The Journal of Physiology 1999 517, part 3 709 720 2-s2.0-0033564497 10.1111/j.1469-7793.1999.0709s.x (Pubitemid 29306458)
    • (1999) Journal of Physiology , vol.517 , Issue.3 , pp. 709-720
    • Lee, Y.-H.1    Kim, I.2    Laporte, R.3    Walsh, M.P.4    Morgan, K.G.5
  • 27
    • 70350452174 scopus 로고    scopus 로고
    • Activation of the PDK-1/Akt/eNOS pathway involved in aortic endothelial function differs between hyperinsulinemic and insulin-deficient diabetic rats
    • 2-s2.0-70350452174 10.1152/ajpheart.00536.2009
    • Kobayashi T., Taguchi K., Nemoto S., Nogami T., Matsumoto T., Kamata K., Activation of the PDK-1/Akt/eNOS pathway involved in aortic endothelial function differs between hyperinsulinemic and insulin-deficient diabetic rats. The American Journal of Physiology-Heart and Circulatory Physiology 2009 297 5 H1767 H1775 2-s2.0-70350452174 10.1152/ajpheart.00536.2009
    • (2009) The American Journal of Physiology - Heart and Circulatory Physiology , vol.297 , Issue.5
    • Kobayashi, T.1    Taguchi, K.2    Nemoto, S.3    Nogami, T.4    Matsumoto, T.5    Kamata, K.6
  • 28
    • 14844357714 scopus 로고    scopus 로고
    • Phosphoinositide-dependent phosphorylation of PDK1 regulates nuclear translocation
    • DOI 10.1128/MCB.25.6.2347-2363.2005
    • Scheid M. P., Parsons M., Woodgett J. R., Phosphoinositide-dependent phosphorylation of PDK1 regulates nuclear translocation. Molecular and Cellular Biology 2005 25 6 2347 2363 2-s2.0-14844357714 10.1128/MCB.25.6.2347-2363.2005 (Pubitemid 40354630)
    • (2005) Molecular and Cellular Biology , vol.25 , Issue.6 , pp. 2347-2363
    • Scheid, M.P.1    Parsons, M.2    Woodgett, J.R.3
  • 29
    • 0036529835 scopus 로고    scopus 로고
    • Adducin in platelets: Activation-induced phosphorylation by PKC and proteolysis by calpain
    • DOI 10.1182/blood.V99.7.2418
    • Gilligan D. M., Sarid R., Weese J., Adducin in platelets: activation-induced phosphorylation by PKC and proteolysis by calpain. Blood 2002 99 7 2418 2426 2-s2.0-0036529835 10.1182/blood.V99.7.2418 (Pubitemid 34525427)
    • (2002) Blood , vol.99 , Issue.7 , pp. 2418-2426
    • Gilligan, D.M.1    Sarid, R.2    Weese, J.3
  • 30
    • 0033581954 scopus 로고    scopus 로고
    • Increased protein kinase C δ in mammary tumor cells: Relationship to transformation and metastatic progression
    • 2-s2.0-0033581954
    • Kiley S. C., Clark K. J., Duddy S. K., Welch D. R., Jaken S., Increased protein kinase C δ in mammary tumor cells: relationship to transformation and metastatic progression. Oncogene 1999 18 48 6748 6757 2-s2.0-0033581954
    • (1999) Oncogene , vol.18 , Issue.48 , pp. 6748-6757
    • Kiley, S.C.1    Clark, K.J.2    Duddy, S.K.3    Welch, D.R.4    Jaken, S.5
  • 31
    • 0033571710 scopus 로고    scopus 로고
    • Extracellular regulated kinase (ERK) interaction with actin and the calponin homology (CH) domain of actin-binding proteins
    • 2-s2.0-0033571710 10.1042/0264-6021:3440117
    • Leinweber B. D., Leavis P. C., Grabarek Z., Wang C.-L. A., Morgan K. G., Extracellular regulated kinase (ERK) interaction with actin and the calponin homology (CH) domain of actin-binding proteins. Biochemical Journal 1999 344, part 1 117 123 2-s2.0-0033571710 10.1042/0264-6021:3440117
    • (1999) Biochemical Journal , vol.3441 , pp. 117-123
    • Leinweber, B.D.1    Leavis, P.C.2    Grabarek, Z.3    Wang, C.-L.A.4    Morgan, K.G.5
  • 32
    • 0025832399 scopus 로고
    • 2+-independent change in phosphorylation of the myosin light chain during relaxation of ferret aorta by vasodilators
    • 2-s2.0-0025832399
    • 2+-independent change in phosphorylation of the myosin light chain during relaxation of ferret aorta by vasodilators. The Journal of Physiology 1991 440 85 93 2-s2.0-0025832399
    • (1991) The Journal of Physiology , vol.440 , pp. 85-93
    • Suematsu, E.1    Resnick, M.2    Morgan, K.G.3
  • 37
    • 34248188618 scopus 로고    scopus 로고
    • Phosphorylation of adducin by protein kinase Cδ promotes cell motility
    • DOI 10.1242/jcs.03408
    • Chen C.-L., Hsieh Y.-T., Chen H.-C., Phosphorylation of adducin by protein kinase C δ promotes cell motility. Journal of Cell Science 2007 120 7 1157 1167 2-s2.0-34248188618 10.1242/jcs.03408 (Pubitemid 46711834)
    • (2007) Journal of Cell Science , vol.120 , Issue.7 , pp. 1157-1167
    • Chen, C.-L.1    Hsieh, Y.-T.2    Chen, H.-C.3
  • 38
    • 0032055970 scopus 로고    scopus 로고
    • Cytoskeletal targeting of calponin in differentiated, contractile smooth muscle cells of the ferret
    • Parker C. A., Takahashi K., Tang J. X., Tao T., Morgan K. G., Cytoskeletal targeting of calponin in differentiated, contractile smooth muscle cells of the ferret. The Journal of Physiology 1998 508 1 187 198 2-s2.0-0032055970 (Pubitemid 28167581)
    • (1998) Journal of Physiology , vol.508 , Issue.1 , pp. 187-198
    • Parker, C.A.1    Takahashi, K.2    Tang, J.X.3    Tao, T.4    Morgan, K.G.5
  • 39
    • 0023804107 scopus 로고
    • Photocrosslinking of calmodulin and/or actin to chicken gizzard caldesmon
    • DOI 10.1016/S0006-291X(88)80948-3
    • Wang C.-L. A., Photocrosslinking of calmodulin and/or actin to chicken gizzard caldesmon. Biochemical and Biophysical Research Communications 1988 156 2 1033 1038 2-s2.0-0023804107 (Pubitemid 18263934)
    • (1988) Biochemical and Biophysical Research Communications , vol.156 , Issue.2 , pp. 1033-1038
    • Wang, C.-L.A.1
  • 41
    • 0035749892 scopus 로고    scopus 로고
    • Caldesmon and smooth-muscle regulation
    • DOI 10.1385/CBB:35:3:275
    • Wang C.-L. A., Caldesmon and smooth-muscle regulation. Cell Biochemistry and Biophysics 2001 35 3 275 288 2-s2.0-0035749892 10.1385/CBB:35:3:275 (Pubitemid 33614134)
    • (2001) Cell Biochemistry and Biophysics , vol.35 , Issue.3 , pp. 275-288
    • Wang, C.-L.A.1
  • 42
    • 0037081849 scopus 로고    scopus 로고
    • Phosphorylation of the protein kinase C-theta activation loop and hydrophobic motif regulates its kinase activity, but only activation loop phosphorylation is critical to in vivo nuclear-factor-κB induction
    • DOI 10.1042/0264-6021:3610255
    • Liu Y., Graham C., Li A., Fisher R. J., Shaw S., Phosphorylation of the protein kinase C-theta activation loop and hydrophobic motif regulates its kinase activity, but only activation loop phosphorylation is critical to in vivo nuclear-factor- B induction. Biochemical Journal 2002 361 2 255 265 2-s2.0-0037081849 10.1042/0264-6021:3610255 (Pubitemid 34174492)
    • (2002) Biochemical Journal , vol.361 , Issue.2 , pp. 255-265
    • Liu, Y.1    Graham, C.2    Li, A.3    Fisher, R.J.4    Shaw, S.5
  • 43
    • 0028108027 scopus 로고
    • Threonine-497 is a critical site for permissive activation of protein kinase Cα
    • Cazaubon S., Bornancin F., Parker P. J., Threonine-497 is a critical site for permissive activation of protein kinase C α Biochemical Journal 1994 301 2 443 448 2-s2.0-0028108027 (Pubitemid 24231947)
    • (1994) Biochemical Journal , vol.301 , Issue.2 , pp. 443-448
    • Cazaubon, S.1    Bornancin, F.2    Parker, P.J.3
  • 44
    • 0030250879 scopus 로고    scopus 로고
    • Phosphorylation of threonine 638 critically controls the dephosphorylation and inactivation of protein kinase Cα
    • DOI 10.1016/S0960-9822(02)70678-7
    • Bornancin F., Parker P. J., Phosphorylation of threonine 638 critically controls the dephosphorylation and inactivation of protein kinase C α Current Biology 1996 6 9 1114 1123 2-s2.0-0030250879 10.1016/S0960-9822(02) 70678-7 (Pubitemid 26368745)
    • (1996) Current Biology , vol.6 , Issue.9 , pp. 1114-1123
    • Bornancin, F.1    Parker, P.J.2
  • 45
    • 0344141205 scopus 로고    scopus 로고
    • Requirements of protein kinase Cδ for catalytic function: Role of glutamic acid 500 and autophosphorylation on serine 643
    • DOI 10.1074/jbc.274.13.8886
    • Stempka L., Schnölzer M., Radke S., Rincke G., Marks F., Gschwendt M., Requirements of protein kinase C δ for catalytic function: role of glutamic acid 500 and autophosphorylation on serine 643. The Journal of Biological Chemistry 1999 274 13 8886 8892 2-s2.0-0344141205 10.1074/jbc.274.13.8886 (Pubitemid 29164689)
    • (1999) Journal of Biological Chemistry , vol.274 , Issue.13 , pp. 8886-8892
    • Stempka, L.1    Schnolzer, M.2    Radke, S.3    Rincke, G.4    Marks, F.5    Gschwendt, M.6
  • 46
    • 0033168515 scopus 로고    scopus 로고
    • Protein kinase C δ involvement in mammary tumor cell metastasis
    • Kiley S. C., Clark K. J., Goodnough M., Welch D. R., Jaken S., Protein kinase C δ involvement in mammary tumor cell metastasis. Cancer Research 1999 59 13 3230 3238 2-s2.0-0033168515 (Pubitemid 29316027)
    • (1999) Cancer Research , vol.59 , Issue.13 , pp. 3230-3238
    • Kiley, S.C.1    Clark, K.J.2    Goodnough, M.3    Welch, D.R.4    Jaken, S.5
  • 47
    • 0031722643 scopus 로고    scopus 로고
    • A role for MAP kinase in differentiated smooth muscle contraction evoked by α -adrenoceptor stimulation
    • 2-s2.0-0031722643
    • Dessy C., Kim I., Sougnez C. L., Laporte R., Morgan K. G., A role for MAP kinase in differentiated smooth muscle contraction evoked by α -adrenoceptor stimulation. The American Journal of Physiology-Cell Physiology 1998 275 4 C1081 C1086 2-s2.0-0031722643
    • (1998) The American Journal of Physiology - Cell Physiology , vol.275 , Issue.4
    • Dessy, C.1    Kim, I.2    Sougnez, C.L.3    Laporte, R.4    Morgan, K.G.5
  • 48
    • 1542311511 scopus 로고    scopus 로고
    • Alpha1-adrenergic signaling mechanisms in contraction of resistance arteries
    • 2-s2.0-1542311511
    • Wier W. G., Morgan K. G., Alpha1-adrenergic signaling mechanisms in contraction of resistance arteries. Reviews of Physiology, Biochemistry and Pharmacology 2003 150 91 139 2-s2.0-1542311511
    • (2003) Reviews of Physiology, Biochemistry and Pharmacology , vol.150 , pp. 91-139
    • Wier, W.G.1    Morgan, K.G.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.