메뉴 건너뛰기




Volumn 7, Issue 6, 2008, Pages 1007-1018

Comparative proteomics analysis of vascular smooth muscle cells incubated with S- and R-Enantiomers of atenolol using iTRAQ-coupled two-dimensional LC-MS/MS

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA N ACETYLGALACTOSAMINIDASE; ASPARTATE AMINOTRANSFERASE; ATENOLOL; BETA 1 ADRENERGIC RECEPTOR; BETA 2 ADRENERGIC RECEPTOR; CALCIUM BINDING PROTEIN; CALCIUM ION; CALMODULIN; CALPHOBINDIN II; CALVASCULIN; CYTOCHROME B5 REDUCTASE; CYTOSKELETON PROTEIN; GLUTATHIONE TRANSFERASE; NESTIN; NICOTINAMIDE ADENINE DINUCLEOTIDE; PROTEIN S 100; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE; TROPOMYOSIN;

EID: 46749150111     PISSN: 15359476     EISSN: None     Source Type: Journal    
DOI: 10.1074/mcp.M700485-MCP200     Document Type: Article
Times cited : (41)

References (57)
  • 1
    • 29544449036 scopus 로고    scopus 로고
    • Molecular mechanisms of β2-adrenergic receptor function, response, and regulation
    • Johnson, M. (2006) Molecular mechanisms of β2-adrenergic receptor function, response, and regulation. J. Allergy Clin. Immunol. 117, 18-24
    • (2006) J. Allergy Clin. Immunol , vol.117 , pp. 18-24
    • Johnson, M.1
  • 2
    • 0024344941 scopus 로고
    • Identification of two serine residues involved in agonist activation of the p-adrenergic receptor
    • Strader, C. D., Candelore, M. R., Hill, W. S., Sigal, I. S., and Dixon, R. A. (1989) Identification of two serine residues involved in agonist activation of the p-adrenergic receptor. J. Biol. Chem. 264, 13572-13578
    • (1989) J. Biol. Chem , vol.264 , pp. 13572-13578
    • Strader, C.D.1    Candelore, M.R.2    Hill, W.S.3    Sigal, I.S.4    Dixon, R.A.5
  • 3
    • 0031984517 scopus 로고    scopus 로고
    • (199B) The many faces of G protein signaling
    • Hamm, H. E. (199B) The many faces of G protein signaling. J. Biol. Chem. 273, 669-672
    • J. Biol. Chem , vol.273 , pp. 669-672
    • Hamm, H.E.1
  • 4
    • 0021268721 scopus 로고
    • Phosphorylation o f mammalian myosin light chain kinases by the catalytic subunit of cyclic AMP-dependent protein kinase and by cyclic GMP-dependent protein kinase
    • Nishikawa, M., Lanerolle, P., Lincoln, T. M., and Adelstein, R. S. (1984) Phosphorylation o f mammalian myosin light chain kinases by the catalytic subunit of cyclic AMP-dependent protein kinase and by cyclic GMP-dependent protein kinase. J. Biol. Chem. 259, 8429-8436
    • (1984) J. Biol. Chem , vol.259 , pp. 8429-8436
    • Nishikawa, M.1    Lanerolle, P.2    Lincoln, T.M.3    Adelstein, R.S.4
  • 5
    • 0028043535 scopus 로고
    • Signal transduction and regulation in smooth muscle
    • Somlyo, A. P., and Somlyo, A. V. (1994) Signal transduction and regulation in smooth muscle. Nature 372, 231-236
    • (1994) Nature , vol.372 , pp. 231-236
    • Somlyo, A.P.1    Somlyo, A.V.2
  • 6
    • 0025613071 scopus 로고
    • Regulation of heartbeat by G protein-coupled ion channels
    • Brown, A.M. (1990) Regulation of heartbeat by G protein-coupled ion channels. Am. J. Physiol. 259, H1621-H1628
    • (1990) Am. J. Physiol , vol.259
    • Brown, A.M.1
  • 7
    • 0030955316 scopus 로고    scopus 로고
    • GTP-binding-protein-coupled receptor kinases
    • Palczewski, K. (1997) GTP-binding-protein-coupled receptor kinases. Eur. J. Biochem. 248, 261-269
    • (1997) Eur. J. Biochem , vol.248 , pp. 261-269
    • Palczewski, K.1
  • 8
    • 0031747997 scopus 로고    scopus 로고
    • The role of receptor kinases and arrestins in G protein-coupled receptor regulation
    • Krupnick, J. G., and Benovic, J. L. (1998) The role of receptor kinases and arrestins in G protein-coupled receptor regulation. Annu. Rev. Pharmacol. Toxicol. 38, 289-319
    • (1998) Annu. Rev. Pharmacol. Toxicol , vol.38 , pp. 289-319
    • Krupnick, J.G.1    Benovic, J.L.2
  • 9
    • 0344528755 scopus 로고    scopus 로고
    • (11999) RGS proteins: More than just GAPs for heterotrimeric G proteins
    • De Vries, L, and Farquhar, M. G. (11999) RGS proteins: more than just GAPs for heterotrimeric G proteins. Trends Cell Biol. 9, 138-144
    • Trends Cell Biol , vol.9 , pp. 138-144
    • De Vries, L.1    Farquhar, M.G.2
  • 10
    • 0018621377 scopus 로고
    • Comparison of β-adrenergic receptor subtypes in mammalian tissues
    • Minneman, K. P., Hedberg, A., and Molinoff, P. B. (1979) Comparison of β-adrenergic receptor subtypes in mammalian tissues. J. Pharmacol. Exp. Ther. 211, 502-508
    • (1979) J. Pharmacol. Exp. Ther , vol.211 , pp. 502-508
    • Minneman, K.P.1    Hedberg, A.2    Molinoff, P.B.3
  • 11
    • 0020569355 scopus 로고
    • Human cardiac β-adrenergic receptor subtype heterogeneity delineated by direct radioligand binding
    • Stiles, G. L., Taylor, S., and Letkowitz, R. J. (1983) Human cardiac β-adrenergic receptor subtype heterogeneity delineated by direct radioligand binding. Life Sci. 33, 476-483
    • (1983) Life Sci , vol.33 , pp. 476-483
    • Stiles, G.L.1    Taylor, S.2    Letkowitz, R.J.3
  • 13
    • 33746367481 scopus 로고    scopus 로고
    • Antihypertensive medications and the risk of incident type 2 diabetes
    • Taylor, E. N., Hu, F. B., and Curhan, G. C. (2006) Antihypertensive medications and the risk of incident type 2 diabetes. Diabetes Care 29, 1065-1070
    • (2006) Diabetes Care , vol.29 , pp. 1065-1070
    • Taylor, E.N.1    Hu, F.B.2    Curhan, G.C.3
  • 14
    • 0141839089 scopus 로고    scopus 로고
    • Gene expression profiles and protein balance in skeletal muscle of burned children after β-adrenergic blockade
    • Hemdon, D. N., Dasu, M. R. K., Wolfe, R. R., and Barrow, R. E. (2003) Gene expression profiles and protein balance in skeletal muscle of burned children after β-adrenergic blockade. Am. J. Physiol. 285, E783-E789
    • (2003) Am. J. Physiol , vol.285
    • Hemdon, D.N.1    Dasu, M.R.K.2    Wolfe, R.R.3    Barrow, R.E.4
  • 16
    • 0034789979 scopus 로고    scopus 로고
    • Quantitative profiling of differentiation-induced microsomal proteins using isotope-coded affinity tags and mass spectrometry
    • Han, D. K., Eng, J., Zhou, H., and Aebersold, R. (2001) Quantitative profiling of differentiation-induced microsomal proteins using isotope-coded affinity tags and mass spectrometry. Nat. Biotechnol. 19, 946-951
    • (2001) Nat. Biotechnol , vol.19 , pp. 946-951
    • Han, D.K.1    Eng, J.2    Zhou, H.3    Aebersold, R.4
  • 17
    • 0036545614 scopus 로고    scopus 로고
    • Complementary profiling of gene expression at the transcriptome and proteome levels in Saccharomyces cerevisiae
    • Griffin, T. J., Gygi, S. P., Ideker, T., Rist, B., Eng, J., Hood, L., and Aebersold, R. (2002) Complementary profiling of gene expression at the transcriptome and proteome levels in Saccharomyces cerevisiae. Mol. Cell. Proteomics 1, 323-333
    • (2002) Mol. Cell. Proteomics , vol.1 , pp. 323-333
    • Griffin, T.J.1    Gygi, S.P.2    Ideker, T.3    Rist, B.4    Eng, J.5    Hood, L.6    Aebersold, R.7
  • 18
    • 22144498137 scopus 로고    scopus 로고
    • A proteomics analysis of cellular proteins associated with HBV genotype-specific HBX: Potential in identification of early diagnostic markers for HCC
    • Tan, T. L., and Chen, W. (2005) A proteomics analysis of cellular proteins associated with HBV genotype-specific HBX: potential in identification of early diagnostic markers for HCC. J. Clin. Virol. 33, 293-298
    • (2005) J. Clin. Virol , vol.33 , pp. 293-298
    • Tan, T.L.1    Chen, W.2
  • 20
    • 8644220590 scopus 로고    scopus 로고
    • N-terminal isotope tagging strategy for quantitative proteomics: Results-driven analysis of protein abundance changes
    • Zappacosta, F., and Annan, R. (2004) N-terminal isotope tagging strategy for quantitative proteomics: results-driven analysis of protein abundance changes. Anal. Chem. 76, 6618-6627
    • (2004) Anal. Chem , vol.76 , pp. 6618-6627
    • Zappacosta, F.1    Annan, R.2
  • 21
    • 19944432197 scopus 로고    scopus 로고
    • Ross, P., Huang, Y., Marchese, J., Williamson, B., Parker, K, Hattan, S., Khainovski, Pillai, S., Dey, S., Daniels, S., Purkayastha, S., Juhasz, P., Martin, S., Bartlet-Jones, M., He, F., Jacobson, A., and Pappin, D. (2004) Multiplexed protein quantitation in Saccharomyces cerevisiae using amine-reactive isobaric tagging reagents. Mol, Cell. Proteomics 3, 1154-1169
    • Ross, P., Huang, Y., Marchese, J., Williamson, B., Parker, K, Hattan, S., Khainovski, Pillai, S., Dey, S., Daniels, S., Purkayastha, S., Juhasz, P., Martin, S., Bartlet-Jones, M., He, F., Jacobson, A., and Pappin, D. (2004) Multiplexed protein quantitation in Saccharomyces cerevisiae using amine-reactive isobaric tagging reagents. Mol, Cell. Proteomics 3, 1154-1169
  • 22
    • 34548409217 scopus 로고    scopus 로고
    • Experimental and statistical considerations to avoid false conclusions in proteomics studies using differential in-gel electrophoresis
    • Karp, N. A., McCormick, P. S., Russell, M. R., and Lilley, K S. (2007) Experimental and statistical considerations to avoid false conclusions in proteomics studies using differential in-gel electrophoresis. Mol. Cell. Proteomics 6, 1354-1364
    • (2007) Mol. Cell. Proteomics , vol.6 , pp. 1354-1364
    • Karp, N.A.1    McCormick, P.S.2    Russell, M.R.3    Lilley, K.S.4
  • 23
    • 0035829361 scopus 로고    scopus 로고
    • Controlling the false discovery rate in behavior genetics research
    • Benjamini, Y., Drai, D., Elmer, G., Kafkafi, N., and Golani, I. (2001) Controlling the false discovery rate in behavior genetics research. Behav. Brain Res. 125, 279-284
    • (2001) Behav. Brain Res , vol.125 , pp. 279-284
    • Benjamini, Y.1    Drai, D.2    Elmer, G.3    Kafkafi, N.4    Golani, I.5
  • 24
    • 0346736511 scopus 로고    scopus 로고
    • Thio sugars. VII. Effect of 3-cleoxy-4-S-(β-D-gluco- and β-o-galactopyranosyl)-4-thiodisaccharides and their sulfoxides and sulfones on the viability and growth of selected murine and human tumor cell lines
    • Witczak, Z. J., Kaplon, P., and Day, M. (2003) Thio sugars. VII. Effect of 3-cleoxy-4-S-(β-D-gluco- and β-o-galactopyranosyl)-4-thiodisaccharides and their sulfoxides and sulfones on the viability and growth of selected murine and human tumor cell lines. Carbohydr. Res. 338, 11-18
    • (2003) Carbohydr. Res , vol.338 , pp. 11-18
    • Witczak, Z.J.1    Kaplon, P.2    Day, M.3
  • 25
    • 0017671589 scopus 로고
    • The pathway of glutamate metabolism in rat brain mitochondria
    • Dennis, S. C., and Clark, J. B. (1977) The pathway of glutamate metabolism in rat brain mitochondria. Biochem. J. 168, 521-527
    • (1977) Biochem. J , vol.168 , pp. 521-527
    • Dennis, S.C.1    Clark, J.B.2
  • 26
    • 0023173876 scopus 로고
    • Mechanism of action of glutathione-dependent enzymes
    • Douglas, K. T. (1987) Mechanism of action of glutathione-dependent enzymes. Adv. Enzymol. Relat. Areas Mol. Biol. 59, 103-167
    • (1987) Adv. Enzymol. Relat. Areas Mol. Biol , vol.59 , pp. 103-167
    • Douglas, K.T.1
  • 27
    • 0014980147 scopus 로고
    • A function of cytochrome b5 in fatty acid desaturation by rat liver. microsomes
    • Oshino, N., Imai, Y., and Sato, R. (1971) A function of cytochrome b5 in fatty acid desaturation by rat liver. microsomes. J. Biochem. 69, 155-167
    • (1971) J. Biochem , vol.69 , pp. 155-167
    • Oshino, N.1    Imai, Y.2    Sato, R.3
  • 28
    • 0019298353 scopus 로고
    • Biochemical properties of cytochrome b5-dependent microsomal fatty acid elongation and identification of products
    • Keyes, S. R., and Cinti, D. L. (1980) Biochemical properties of cytochrome b5-dependent microsomal fatty acid elongation and identification of products. J. Biol. Chem. 255, 1357-1364
    • (1980) J. Biol. Chem , vol.255 , pp. 1357-1364
    • Keyes, S.R.1    Cinti, D.L.2
  • 29
    • 0028176116 scopus 로고
    • Regulation of the Yp subunit of glutathione S-transferase P in rat embryos and yolk sacs during organogenesis
    • Hales, B. F., and Huang, C. (1994) Regulation of the Yp subunit of glutathione S-transferase P in rat embryos and yolk sacs during organogenesis. Biochem. Pharmarcol. 47, 2029-2037
    • (1994) Biochem. Pharmarcol , vol.47 , pp. 2029-2037
    • Hales, B.F.1    Huang, C.2
  • 30
    • 0017391211 scopus 로고
    • Mechanism of C-5 double bond introduction in the blosynthesis of cholesterol by rat liver microsomes: Evidence for the participation of microsomal cytochrome b5
    • Reddy, V. V. R., Kupfer, D., and Capsi, E. (1977) Mechanism of C-5 double bond introduction in the blosynthesis of cholesterol by rat liver microsomes: evidence for the participation of microsomal cytochrome b5. J. Biol. Chem. 252, 2797-2801
    • (1977) J. Biol. Chem , vol.252 , pp. 2797-2801
    • Reddy, V.V.R.1    Kupfer, D.2    Capsi, E.3
  • 31
    • 0015032258 scopus 로고
    • Evidence for the participation of cytochrome b 5 in hepatic microsomal mixed-function oxidation reactions
    • Hildebrandt, A., and Estabrook, R. W. (1971) Evidence for the participation of cytochrome b 5 in hepatic microsomal mixed-function oxidation reactions. Arch. Biochem. Biophys. 143, 66-79
    • (1971) Arch. Biochem. Biophys , vol.143 , pp. 66-79
    • Hildebrandt, A.1    Estabrook, R.W.2
  • 32
    • 0028788940 scopus 로고
    • Uterine and fetal hemodynamics and fetal cardiac function after atenolol and pindolol infusion
    • Rasanen, J., and Jouppila, P. (1995) Uterine and fetal hemodynamics and fetal cardiac function after atenolol and pindolol infusion. Eur. J. Obstet. Gynecol. Reprod. Biol. 62, 195-201
    • (1995) Eur. J. Obstet. Gynecol. Reprod. Biol , vol.62 , pp. 195-201
    • Rasanen, J.1    Jouppila, P.2
  • 33
    • 0021797851 scopus 로고
    • Purification, induction, and distribution of placental glutathione S-transferase: A new marker enzyme for preneoplastic cells in rat chemical hepatocarcinogenesis
    • Satoh, K., Kitahara, A., Soma, Y., Inaba, Y., Hatayama, I., and Sato, K. (1984) Purification, induction, and distribution of placental glutathione S-transferase: a new marker enzyme for preneoplastic cells in rat chemical hepatocarcinogenesis. Proc. Natl. Acad. Sci. U. S. A. 85, 3964-3968
    • (1984) Proc. Natl. Acad. Sci. U. S. A , vol.85 , pp. 3964-3968
    • Satoh, K.1    Kitahara, A.2    Soma, Y.3    Inaba, Y.4    Hatayama, I.5    Sato, K.6
  • 34
    • 0024490605 scopus 로고
    • Glutathione S-transferases as markers of preneoplasia and neoplasia
    • Sato, K. (1990) Glutathione S-transferases as markers of preneoplasia and neoplasia. Adv. Cancer Res. 52, 205-255
    • (1990) Adv. Cancer Res , vol.52 , pp. 205-255
    • Sato, K.1
  • 35
    • 0029873749 scopus 로고    scopus 로고
    • Medium-term liver and multi-organ carcinogenesis and chemopreventive agents
    • Ito, N., Hasegawa, R., Imaida, K., Hirose, M., and Shirai, T. (1996) Medium-term liver and multi-organ carcinogenesis and chemopreventive agents. Exp. Toxicol. Pathol. 48, 113-119
    • (1996) Exp. Toxicol. Pathol , vol.48 , pp. 113-119
    • Ito, N.1    Hasegawa, R.2    Imaida, K.3    Hirose, M.4    Shirai, T.5
  • 36
    • 0021365095 scopus 로고
    • The identification of the heat-stable microsomal protein required for methoxyflurane metabolism as cytochrome b5
    • Canova, D. E., and Waskell, L. (1984) The identification of the heat-stable microsomal protein required for methoxyflurane metabolism as cytochrome b5. J. Biol. Chem. 259, 2541-2546
    • (1984) J. Biol. Chem , vol.259 , pp. 2541-2546
    • Canova, D.E.1    Waskell, L.2
  • 37
    • 0028834424 scopus 로고
    • The elemental principles of calcium signaling
    • Bootman, M. D., and Berridge, M. J. (1995) The elemental principles of calcium signaling. Cell 83, 675-678
    • (1995) Cell , vol.83 , pp. 675-678
    • Bootman, M.D.1    Berridge, M.J.2
  • 38
    • 0023874795 scopus 로고
    • 2+-transporting ATPase from rat brain
    • 2+-transporting ATPase from rat brain. J. Biol. Chem. 263, 8646-8657
    • (1988) J. Biol. Chem , vol.263 , pp. 8646-8657
    • Shull, G.E.1    Greeb, J.2
  • 39
    • 0034695103 scopus 로고    scopus 로고
    • Regulation of G protein-coupled receptor kinase subtypes by calcium sensor proteins
    • Sallese, M., and Iacovelli, L. (2000) Regulation of G protein-coupled receptor kinase subtypes by calcium sensor proteins. Biochim. Biophys. Acta 1498, 112-121
    • (2000) Biochim. Biophys. Acta , vol.1498 , pp. 112-121
    • Sallese, M.1    Iacovelli, L.2
  • 43
    • 0021028848 scopus 로고
    • Calcium control of actin-myosin based contraction in Triton models of mouse 3T3 fibroblasts is mediated by the myosin light chain kinase (MLCKI-calmodulin complex
    • Holzapfel, G., Wehland, J., and Weber, K. (1983) Calcium control of actin-myosin based contraction in Triton models of mouse 3T3 fibroblasts is mediated by the myosin light chain kinase (MLCKI-calmodulin complex. Exp. Cell Res. 148, 117-126
    • (1983) Exp. Cell Res , vol.148 , pp. 117-126
    • Holzapfel, G.1    Wehland, J.2    Weber, K.3
  • 44
    • 16344396507 scopus 로고    scopus 로고
    • Nestin structure and predicted function in cellular cytoskeletall organization
    • Michalczyk, K., and Ziman, M. (2005) Nestin structure and predicted function in cellular cytoskeletall organization. Histol. Histopathol. 20, 665-671
    • (2005) Histol. Histopathol , vol.20 , pp. 665-671
    • Michalczyk, K.1    Ziman, M.2
  • 45
    • 0026218642 scopus 로고
    • The molecular basis for tropomyosin isoform diversity
    • Lees, M., and Helfman, D. (1991) The molecular basis for tropomyosin isoform diversity. BioEssays 13, 429-437
    • (1991) BioEssays , vol.13 , pp. 429-437
    • Lees, M.1    Helfman, D.2
  • 47
    • 0036131467 scopus 로고    scopus 로고
    • Cloning of a differentially expressed tropomyosin isoform from cultured rabbit aortic smooth muscle cells
    • Girjes, A. A., Keriakous, D., and Cockerill, G. W. (2002) Cloning of a differentially expressed tropomyosin isoform from cultured rabbit aortic smooth muscle cells. Int. J. Biochem. Cell Biol. 34, 505-515
    • (2002) Int. J. Biochem. Cell Biol , vol.34 , pp. 505-515
    • Girjes, A.A.1    Keriakous, D.2    Cockerill, G.W.3
  • 48
    • 0027196279 scopus 로고
    • Cytoskeletal role for contractile dysfunction of hypertrophied myocardium
    • Tsutsul, H., Ishihara, K., and Cooper, G. (1993) Cytoskeletal role for contractile dysfunction of hypertrophied myocardium. Science 200, 682-687
    • (1993) Science , vol.200 , pp. 682-687
    • Tsutsul, H.1    Ishihara, K.2    Cooper, G.3
  • 49
    • 0028225258 scopus 로고
    • Role of microtubules in contractile dysfunction of hypertrophied cardiocytes
    • Tsutsui, H., Tagawa, H., and Kent, R. L. (1994) Role of microtubules in contractile dysfunction of hypertrophied cardiocytes. Circulation 90, 533-555
    • (1994) Circulation , vol.90 , pp. 533-555
    • Tsutsui, H.1    Tagawa, H.2    Kent, R.L.3
  • 50
  • 51
    • 0030198980 scopus 로고    scopus 로고
    • The role of the cytoskeleton in left ventricular pressure overload hypertrophy and failure
    • Collins, J. F., Pawloski-Dahm, C., and Davie, M. G. (1996) The role of the cytoskeleton in left ventricular pressure overload hypertrophy and failure. J. Mol. Cell. Cardiol. 28, 1435-1443
    • (1996) J. Mol. Cell. Cardiol , vol.28 , pp. 1435-1443
    • Collins, J.F.1    Pawloski-Dahm, C.2    Davie, M.G.3
  • 52
    • 0031194198 scopus 로고    scopus 로고
    • Cellular basis of contractile derangements of hypertrophied ventricular myocytes
    • Bailey, B. A., Dipla, K., Li, S., and Houser, S. R. (1997) Cellular basis of contractile derangements of hypertrophied ventricular myocytes. J. Mol. Cell. Cardiol. 29, 1823-1835
    • (1997) J. Mol. Cell. Cardiol , vol.29 , pp. 1823-1835
    • Bailey, B.A.1    Dipla, K.2    Li, S.3    Houser, S.R.4
  • 54
    • 0038024241 scopus 로고    scopus 로고
    • ROCKs: Multifunctional kinases in cell behaviour
    • Riento, K., and Ridley, A. J. (2003) ROCKs: multifunctional kinases in cell behaviour. Nat. Rev. Mol. Cell Biol. 4, 446-456
    • (2003) Nat. Rev. Mol. Cell Biol , vol.4 , pp. 446-456
    • Riento, K.1    Ridley, A.J.2
  • 55
    • 28444461454 scopus 로고    scopus 로고
    • Inhibition of RhoA/Rho kinase pathway is involved in the beneficial effect of sildenafil on pulmonary hypertension
    • Guilluy, C., Sauzeau, V., Rolli-Derkinderen, M., Guerin, P., Sagan, C., Pacaud, P., and Loirand, G. (2005) Inhibition of RhoA/Rho kinase pathway is involved in the beneficial effect of sildenafil on pulmonary hypertension. Br. J. Pharmacol. 146, 1010-1018
    • (2005) Br. J. Pharmacol , vol.146 , pp. 1010-1018
    • Guilluy, C.1    Sauzeau, V.2    Rolli-Derkinderen, M.3    Guerin, P.4    Sagan, C.5    Pacaud, P.6    Loirand, G.7
  • 56
    • 18044396920 scopus 로고    scopus 로고
    • Contractile properties of the cultured vascular smooth muscle cells - the crucial role played by RhoA in the regulation of contractility
    • Bi, D., Nishimura, J., Niiro, N., Hirano, K., and Kanaide, H. (2005) Contractile properties of the cultured vascular smooth muscle cells - the crucial role played by RhoA in the regulation of contractility. Circ. Res. 96, 890-897
    • (2005) Circ. Res , vol.96 , pp. 890-897
    • Bi, D.1    Nishimura, J.2    Niiro, N.3    Hirano, K.4    Kanaide, H.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.