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Volumn 9, Issue 24, 1999, Pages 1468-1476

Urokinase-induced mitogenesis is mediated by casein kinase 2 and nucleolin

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EID: 0033576631     PISSN: 09609822     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0960-9822(00)80116-5     Document Type: Article
Times cited : (83)

References (52)
  • 1
    • 0027241856 scopus 로고
    • The pathogenesis of atherosclerosis: A perspective for the 1990s
    • Ross R: The pathogenesis of atherosclerosis: a perspective for the 1990s. Nature 1993, 362:801-809.
    • (1993) Nature , vol.362 , pp. 801-809
    • Ross, R.1
  • 2
    • 0026534274 scopus 로고
    • Platelet-derived growth factor promotes smooth muscle cell migration and intimai thickening in a rat model of balloon angioplasty
    • Jawien A, Bowen-Pope DF, Lindner V, Schwartz SM, Clowes AW: Platelet-derived growth factor promotes smooth muscle cell migration and intimai thickening in a rat model of balloon angioplasty. J Clin Invest 1992, 89:507-511.
    • (1992) J Clin Invest , vol.89 , pp. 507-511
    • Jawien, A.1    Bowen-Pope, D.F.2    Lindner, V.3    Schwartz, S.M.4    Clowes, A.W.5
  • 3
    • 0027197246 scopus 로고
    • Recombinant fibroblast growth factor-1 promotes intimal hyperplasia and angiogenesis in arteries in vivo
    • Nabel EG, Yang ZY, Plautz G, Forough R, Zhan X, Haudenschild CC, et al.: Recombinant fibroblast growth factor-1 promotes intimal hyperplasia and angiogenesis in arteries in vivo. Nature 1993, 362:844-846.
    • (1993) Nature , vol.362 , pp. 844-846
    • Nabel, E.G.1    Yang, Z.Y.2    Plautz, G.3    Forough, R.4    Zhan, X.5    Haudenschild, C.C.6
  • 4
    • 0027476105 scopus 로고
    • Prevention of smooth muscle cell outgrowth from human atherosclerotic plaque by a recombinant cytotoxin specific for epidermal growth factor receptor
    • Pickering JG, Bacha PA, Weir L, Jekanowski J, Nichols JC, Isner JM: Prevention of smooth muscle cell outgrowth from human atherosclerotic plaque by a recombinant cytotoxin specific for epidermal growth factor receptor. J Clin Invest 1993, 91:724-729.
    • (1993) J Clin Invest , vol.91 , pp. 724-729
    • Pickering, J.G.1    Bacha, P.A.2    Weir, L.3    Jekanowski, J.4    Nichols, J.C.5    Isner, J.M.6
  • 5
    • 0030759096 scopus 로고    scopus 로고
    • uPA, uPAR, PAI-1 : Key intersection of proteolytic, adhesive and hemotactic highways?
    • Blasi F: upa, uPAR, PAI-1 : Key intersection of proteolytic, adhesive and hemotactic highways? Immunol Today 1997, 18:415-417.
    • (1997) Immunol Today , vol.18 , pp. 415-417
    • Blasi, F.1
  • 6
    • 0030842795 scopus 로고    scopus 로고
    • Plasminogen activators, integrins, and the coordinated regulation of cell adhesion and migration
    • Chapman H: Plasminogen activators, integrins, and the coordinated regulation of cell adhesion and migration. Curr Opin Cell Biol 1997, 9:714-724.
    • (1997) Curr Opin Cell Biol , vol.9 , pp. 714-724
    • Chapman, H.1
  • 7
    • 0023603282 scopus 로고
    • Proliferation of a human epidermal tumor cell line stimulated by urokinase
    • Kirchheimer JC, Wojta J, Christ G, Binder B: Proliferation of a human epidermal tumor cell line stimulated by urokinase. FASEB J 1987, 1:125-128.
    • (1987) FASEB J , vol.1 , pp. 125-128
    • Kirchheimer, J.C.1    Wojta, J.2    Christ, G.3    Binder, B.4
  • 9
    • 0026643491 scopus 로고
    • Structural requirements for the growth factor activity of the aminoterminal domain of urokinase
    • Rabbani S, Mazar AP, Bernier SM, Haq M, Bolivar I, Henkin J, Golzman D: Structural requirements for the growth factor activity of the aminoterminal domain of urokinase. J Biol Chem 1992, 267:14151-14156.
    • (1992) J Biol Chem , vol.267 , pp. 14151-14156
    • Rabbani, S.1    Mazar, A.P.2    Bernier, S.M.3    Haq, M.4    Bolivar, I.5    Henkin, J.6    Golzman, D.7
  • 10
    • 0031471689 scopus 로고    scopus 로고
    • Induction of vascular SMC proliferation by urokinase indicates a novel mechanism of action in vasoproliferative disorders
    • Kanse SM, Benzakour O, Kanthou C, Kost C, Lijnen HR, Preissner KT: Induction of vascular SMC proliferation by urokinase indicates a novel mechanism of action in vasoproliferative disorders. Arterioscler Thromb Vasc Biol 1997, 17:2848-2854.
    • (1997) Arterioscler Thromb Vasc Biol , vol.17 , pp. 2848-2854
    • Kanse, S.M.1    Benzakour, O.2    Kanthou, C.3    Kost, C.4    Lijnen, H.R.5    Preissner, K.T.6
  • 11
    • 0030810620 scopus 로고    scopus 로고
    • Urokinase and tissue-type plasminogen activator are required for the mitogenic and chemotactic effects of bovine fibroblast growth factor and platelet-derived growth factor-BB for vascular smooth muscle cells
    • Herbert JM, Lamarche I, Carmelit P: Urokinase and tissue-type plasminogen activator are required for the mitogenic and chemotactic effects of bovine fibroblast growth factor and platelet-derived growth factor-BB for vascular smooth muscle cells. J Biol Chem 1997, 272:23585-23591.
    • (1997) J Biol Chem , vol.272 , pp. 23585-23591
    • Herbert, J.M.1    Lamarche, I.2    Carmelit, P.3
  • 12
    • 0028228649 scopus 로고
    • Urokinase-type and tissue-type plasminogen activators as growth factors of human fibroblasts
    • De Petro G, Copeta A, Barlati S: Urokinase-type and tissue-type plasminogen activators as growth factors of human fibroblasts. Exp Cell Res 1994, 213:286-294.
    • (1994) Exp Cell Res , vol.213 , pp. 286-294
    • De Petro, G.1    Copeta, A.2    Barlati, S.3
  • 13
    • 0032582802 scopus 로고    scopus 로고
    • Urokinase induces proliferation of human ovarian cancer cells: Characterization of structural elements required for growth factor function
    • Fischer K, Lutz V, Wilhelm O, Schmitt M, Graeff H, Heiss P, et al.: Urokinase induces proliferation of human ovarian cancer cells: characterization of structural elements required for growth factor function. FEBS Lett 1998, 438:101-105.
    • (1998) FEBS Lett , vol.438 , pp. 101-105
    • Fischer, K.1    Lutz, V.2    Wilhelm, O.3    Schmitt, M.4    Graeff, H.5    Heiss, P.6
  • 14
    • 0032509476 scopus 로고    scopus 로고
    • Mitogenic effects of urokinase on melanoma cells are independent of high affinity binding to the urokinase receptor
    • Koopman JL, Slomp J, De Bart ACW, Quax PHA, Verheijen JH: Mitogenic effects of urokinase on melanoma cells are independent of high affinity binding to the urokinase receptor. J Biol Chem 1998, 273:33267-33272.
    • (1998) J Biol Chem , vol.273 , pp. 33267-33272
    • Koopman, J.L.1    Slomp, J.2    De Bart, A.C.W.3    Quax, P.H.A.4    Verheijen, J.H.5
  • 15
    • 0028305433 scopus 로고
    • Induction of cell migration by pro-urokinase binding to its receptor: Possible mechanism for signal transduction in human epithelial cells
    • Busso N, Masur SK, Lazeda D, Waxman S, Ossowski L: Induction of cell migration by pro-urokinase binding to its receptor: possible mechanism for signal transduction in human epithelial cells. J Cell Biol 1994, 128:259-270.
    • (1994) J Cell Biol , vol.128 , pp. 259-270
    • Busso, N.1    Masur, S.K.2    Lazeda, D.3    Waxman, S.4    Ossowski, L.5
  • 16
    • 0028294295 scopus 로고
    • Induction of c-fos gene expression by urokinase-type plasminogen activator in human ovarian cancer cells
    • Dumler I, Petri T, Schleuning WD: Induction of c-fos gene expression by urokinase-type plasminogen activator in human ovarian cancer cells. FEBS Lett 1994, 343:103-106.
    • (1994) FEBS Lett , vol.343 , pp. 103-106
    • Dumler, I.1    Petri, T.2    Schleuning, W.D.3
  • 17
    • 0028925552 scopus 로고
    • Urokinase plasminogen activator receptor, β2-integrins, and Src-kinases within a single receptor complex of human monocytes
    • Bohuslav J, Horejsi V, Hansmann C, Stöckl J, Weidle UH, Majdic O, et al: Urokinase plasminogen activator receptor, β2-integrins, and Src-kinases within a single receptor complex of human monocytes. J Exp Med 1995, 181:1381-1390.
    • (1995) J Exp Med , vol.181 , pp. 1381-1390
    • Bohuslav, J.1    Horejsi, V.2    Hansmann, C.3    Stöckl, J.4    Weidle, U.H.5    Majdic, O.6
  • 18
    • 0029923744 scopus 로고    scopus 로고
    • Proteolytic cleavage of the urokinase receptor substitutes for the agonist-induced chemotactic effect
    • Resnati M, Guttinger M, Valcamonica S, Sidenius N, Blasi F, Fazioli F: Proteolytic cleavage of the urokinase receptor substitutes for the agonist-induced chemotactic effect. EMBO J 1996, 15:1572-1582.
    • (1996) EMBO J , vol.15 , pp. 1572-1582
    • Resnati, M.1    Guttinger, M.2    Valcamonica, S.3    Sidenius, N.4    Blasi, F.5    Fazioli, F.6
  • 19
    • 0031463337 scopus 로고    scopus 로고
    • A urokinase-sensitive region of the human urokinase receptor is responsible for its chemotactic activity
    • Fazioli F, Resnati M, Sidenius N, Higashimoto Y, Appella E, Blasi F: A urokinase-sensitive region of the human urokinase receptor is responsible for its chemotactic activity. EMBO J 1997, 16:7279-7286.
    • (1997) EMBO J , vol.16 , pp. 7279-7286
    • Fazioli, F.1    Resnati, M.2    Sidenius, N.3    Higashimoto, Y.4    Appella, E.5    Blasi, F.6
  • 20
    • 0030855023 scopus 로고    scopus 로고
    • Induction in human osteoblastic cells (SaOs2 of the early response genes fos, jun, and myc by the amino-terminal fragment (ATF) of urokinase
    • Rabbani SA, Gladu J, Mazar AP, Henkin J, Golzman D: Induction in human osteoblastic cells (SaOs2) of the early response genes fos, jun, and myc by the amino-terminal fragment (ATF) of urokinase. J Cell Physiol 1997, 172:137-145.
    • (1997) J Cell Physiol , vol.172 , pp. 137-145
    • Rabbani, S.A.1    Gladu, J.2    Mazar, A.P.3    Henkin, J.4    Golzman, D.5
  • 21
    • 0032478829 scopus 로고    scopus 로고
    • Binding of urokinase-type plasminogen activator to its receptor in MCF-7 cells activates extracellular signal-regulated kinase 1 and 2 which is required for increased cellular motility
    • Nguyen DHD, Hussaini IM, Gonias SL: Binding of urokinase-type plasminogen activator to its receptor in MCF-7 cells activates extracellular signal-regulated kinase 1 and 2 which is required for increased cellular motility. J Biol Chem 1998, 273:8502-8507.
    • (1998) J Biol Chem , vol.273 , pp. 8502-8507
    • Nguyen, D.H.D.1    Hussaini, I.M.2    Gonias, S.L.3
  • 22
    • 0032540943 scopus 로고    scopus 로고
    • The urokinase-type plasminogen activator receptor mediates tyrosine phosphorylation of focal adhesion proteins and activation of mitogen-activated protein kinase in cultured endothelial cells
    • Tang H, Kerins DM, Hao Q, Inagami T, Vaughan DE: The urokinase-type plasminogen activator receptor mediates tyrosine phosphorylation of focal adhesion proteins and activation of mitogen-activated protein kinase in cultured endothelial cells. J Biol Chem 1998, 273:18268-18272.
    • (1998) J Biol Chem , vol.273 , pp. 18268-18272
    • Tang, H.1    Kerins, D.M.2    Hao, Q.3    Inagami, T.4    Vaughan, D.E.5
  • 23
    • 0031983177 scopus 로고    scopus 로고
    • The Jak/Stat pathway and urokinase receptor signaling in human aortic vascular smooth muscle cells
    • Dumler I, Weis A, Mayboroda OA, Maasch C, Jerke U, Haller H, Gulba DC: The Jak/Stat pathway and urokinase receptor signaling in human aortic vascular smooth muscle cells. J Biol Chem 1998, 273:315-321.
    • (1998) J Biol Chem , vol.273 , pp. 315-321
    • Dumler, I.1    Weis, A.2    Mayboroda, O.A.3    Maasch, C.4    Jerke, U.5    Haller, H.6    Gulba, D.C.7
  • 24
    • 0030716909 scopus 로고    scopus 로고
    • Urokinase receptor is associated with the components of the JAK1/STAT1 signaling pathway and leads to activation of this pathway upon receptor clustering in the human kidney epithelial tumour cell line TCL-598
    • Koshelnick Y, Ehart M, Hufnagl P, Heinrich PC, Binder BR: Urokinase receptor is associated with the components of the JAK1/STAT1 signaling pathway and leads to activation of this pathway upon receptor clustering in the human kidney epithelial tumour cell line TCL-598. J Biol Chem 1997, 272:28563-28567.
    • (1997) J Biol Chem , vol.272 , pp. 28563-28567
    • Koshelnick, Y.1    Ehart, M.2    Hufnagl, P.3    Heinrich, P.C.4    Binder, B.R.5
  • 28
    • 0029900546 scopus 로고    scopus 로고
    • The physical association of casein kinase 2 with nucleolin
    • Li D, Dobrowolska G, Krebs EG: The physical association of casein kinase 2 with nucleolin. J Biol Chem 1996, 271:15662-15668.
    • (1996) J Biol Chem , vol.271 , pp. 15662-15668
    • Li, D.1    Dobrowolska, G.2    Krebs, E.G.3
  • 29
    • 0026705442 scopus 로고
    • Concerted activities of the RNA recognition and the glycine-rich C-terminal domains of nucleolin are required for efficient complex formation with pre-ribosomal RNA
    • Ghisolfi L, Kharrat A, Joseph G, Amalric F, Erard M: Concerted activities of the RNA recognition and the glycine-rich C-terminal domains of nucleolin are required for efficient complex formation with pre-ribosomal RNA. Bur J Biochem 1992, 209:541-548.
    • (1992) Bur J Biochem , vol.209 , pp. 541-548
    • Ghisolfi, L.1    Kharrat, A.2    Joseph, G.3    Amalric, F.4    Erard, M.5
  • 30
    • 0026740718 scopus 로고
    • Primary structure and binding activity of the hnRNP U protein: Binding RNA through RGG box
    • Kiledjian M, Dreyfuss G: Primary structure and binding activity of the hnRNP U protein: Binding RNA through RGG box. EMBO J 1992, 11:2655-2664.
    • (1992) EMBO J , vol.11 , pp. 2655-2664
    • Kiledjian, M.1    Dreyfuss, G.2
  • 31
    • 0023846071 scopus 로고
    • Mammalian heterogeneous nuclear ribonucleoprotein complex protein A1. Large-scale overproduction in Escherichia coli and cooperative binding to single-stranded nucleic acids
    • Cobianchi F, Karpel RL, Williams KR, Notario V, Wilson SH: Mammalian heterogeneous nuclear ribonucleoprotein complex protein A1. Large-scale overproduction in Escherichia coli and cooperative binding to single-stranded nucleic acids. J Biol Chem 1988, 263:1063-1071.
    • (1988) J Biol Chem , vol.263 , pp. 1063-1071
    • Cobianchi, F.1    Karpel, R.L.2    Williams, K.R.3    Notario, V.4    Wilson, S.H.5
  • 32
    • 0032563213 scopus 로고    scopus 로고
    • Nucleolin interacts with several ribosomal proteins through its RGG domain
    • Bouvet P, Diaz JJ, KIndbeiter K, Madjar JJ, Amalric F: Nucleolin interacts with several ribosomal proteins through its RGG domain. J Biol Chem 1998, 273:19025-19029.
    • (1998) J Biol Chem , vol.273 , pp. 19025-19029
    • Bouvet, P.1    Diaz, J.J.2    Kindbeiter, K.3    Madjar, J.J.4    Amalric, F.5
  • 33
    • 0027722138 scopus 로고
    • Casein kinase II in signal transduction and cell cycle regulation
    • Litchfield DW, Lüscher B: Casein kinase II in signal transduction and cell cycle regulation. Mol Cell Biochem 1993, 127/128:187-199.
    • (1993) Mol Cell Biochem , vol.127-128 , pp. 187-199
    • Litchfield, D.W.1    Lüscher, B.2
  • 34
    • 0028909420 scopus 로고
    • Protein kinase CK2: An enzyme with multiple substrates and a puzzling regulation
    • Allende JE, Allende CC: Protein kinase CK2: an enzyme with multiple substrates and a puzzling regulation. FASEB J 1995, 9:313-323.
    • (1995) FASEB J , vol.9 , pp. 313-323
    • Allende, J.E.1    Allende, C.C.2
  • 36
    • 0032544409 scopus 로고    scopus 로고
    • Phosphorylation of vitronectin by casein kinase II. Identification of the sites and their promotion of cell adhesion and spreading
    • Seger D, Gechtman Z, Shaltiel S: Phosphorylation of vitronectin by casein kinase II. Identification of the sites and their promotion of cell adhesion and spreading. J Biol Chem 1998, 273:24805-24813.
    • (1998) J Biol Chem , vol.273 , pp. 24805-24813
    • Seger, D.1    Gechtman, Z.2    Shaltiel, S.3
  • 37
    • 0029784488 scopus 로고    scopus 로고
    • Fibroblast growth factor-2 binds to the regulatory β subunit of CK2 and directly stimulates CK2 activity toward nucleolin
    • Bonnet H, Filhol O, Truchet I, Brethenou P, Cochet C, Amalric F, Bouche G: Fibroblast growth factor-2 binds to the regulatory β subunit of CK2 and directly stimulates CK2 activity toward nucleolin. J Biol Chem 1996, 271:24781-24787.
    • (1996) J Biol Chem , vol.271 , pp. 24781-24787
    • Bonnet, H.1    Filhol, O.2    Truchet, I.3    Brethenou, P.4    Cochet, C.5    Amalric, F.6    Bouche, G.7
  • 38
    • 0024966024 scopus 로고
    • Major nucleolar proteins shuttle between nucleus and cytoplasm
    • Borer RA, Lehner C, Eppenberger HM, Nigg EA: Major nucleolar proteins shuttle between nucleus and cytoplasm. Cell 1989, 56:379-390.
    • (1989) Cell , vol.56 , pp. 379-390
    • Borer, R.A.1    Lehner, C.2    Eppenberger, H.M.3    Nigg, E.A.4
  • 39
    • 0025123543 scopus 로고
    • A protein partially expressed on the surface of Hep G2 cells that binds lipoproteins specifically is nucleolin
    • Semenkovich CF, Ostlund Jr RE, Olson MO, Yang JW: A protein partially expressed on the surface of Hep G2 cells that binds lipoproteins specifically is nucleolin. Biochemistry 1990, 29:9708-9713.
    • (1990) Biochemistry , vol.29 , pp. 9708-9713
    • Semenkovich, C.F.1    Ostlund R.E., Jr.2    Olson, M.O.3    Yang, J.W.4
  • 40
    • 0028884482 scopus 로고
    • A 110-kD nuclear shuttling protein, nucleolin, binds to the neurite-promoting IKVAV site of laminin-1
    • Kibbey MC, Johnson B, Petryshyn R, Jucker M, Kleinman HK: A 110-kD nuclear shuttling protein, nucleolin, binds to the neurite-promoting IKVAV site of laminin-1. J Neurosci Res 1995, 42:314-322.
    • (1995) J Neurosci Res , vol.42 , pp. 314-322
    • Kibbey, M.C.1    Johnson, B.2    Petryshyn, R.3    Jucker, M.4    Kleinman, H.K.5
  • 41
    • 0030436735 scopus 로고    scopus 로고
    • Internalization of anti-nucleolin antibody into viable Hep-2 cells
    • Deng JS, Ballou B, Hofmeister JK: Internalization of anti-nucleolin antibody into viable Hep-2 cells. Mol Biol Rep 1996, 23:191-195.
    • (1996) Mol Biol Rep , vol.23 , pp. 191-195
    • Deng, J.S.1    Ballou, B.2    Hofmeister, J.K.3
  • 44
    • 0032499570 scopus 로고    scopus 로고
    • Effect of laminin on the nuclear localization of nucleolin in rat intestinal epithelial IEC-6 cells
    • Yu D, Schwartz MZ, Petryshyn R: Effect of laminin on the nuclear localization of nucleolin in rat intestinal epithelial IEC-6 cells. Biochem Biophys Res Commun 1998, 247:186-192.
    • (1998) Biochem Biophys Res Commun , vol.247 , pp. 186-192
    • Yu, D.1    Schwartz, M.Z.2    Petryshyn, R.3
  • 45
    • 0033610837 scopus 로고    scopus 로고
    • Cellular adhesion mediated by factor J, a complement inhibitor. Evidence for nucleolin involvement
    • Larrucea S, González-Rubio C, Cambronero R, Ballou B, Bonay P, López-Granados E, et al.: Cellular adhesion mediated by factor J, a complement inhibitor. Evidence for nucleolin involvement. J Biol Chem 1998, 273:31718-31725.
    • (1998) J Biol Chem , vol.273 , pp. 31718-31725
    • Larrucea, S.1    González-Rubio, C.2    Cambronero, R.3    Ballou, B.4    Bonay, P.5    López-Granados, E.6
  • 46
    • 0030887616 scopus 로고    scopus 로고
    • Nucleolin is one component of the B cell-specific transcription factor and switch region binding protein, LR1
    • Hanakahi LA, Dempsey LA, Li MJ, Maizels N: Nucleolin is one component of the B cell-specific transcription factor and switch region binding protein, LR1. Proc Natl Acad Sci USA 1997, 94:3605-3610.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 3605-3610
    • Hanakahi, L.A.1    Dempsey, L.A.2    Li, M.J.3    Maizels, N.4
  • 47
    • 0027506444 scopus 로고
    • Interaction of urokinase-type plasminogen activator (u-PA) with its cellular receptor (u-PAR) induces phosphorylation on tyrosine of a 38 kDa protein
    • Dumler I, Petri T, Schleuning WD: Interaction of urokinase-type plasminogen activator (u-PA) with its cellular receptor (u-PAR) induces phosphorylation on tyrosine of a 38 kDa protein. FEBS Lett 1993, 322:37-40.
    • (1993) FEBS Lett , vol.322 , pp. 37-40
    • Dumler, I.1    Petri, T.2    Schleuning, W.D.3
  • 48
    • 0029854465 scopus 로고    scopus 로고
    • Identification of human myocardial proteins separated by two-dimensional electrophoresis using an effective sample preparation for mass spectrometry
    • Otto A, Thiede B, Müller EC, Scheler C, Wittmann-Liebold B, Jungblut P: Identification of human myocardial proteins separated by two-dimensional electrophoresis using an effective sample preparation for mass spectrometry. Electrophoresis 1996, 17:1643-1650.
    • (1996) Electrophoresis , vol.17 , pp. 1643-1650
    • Otto, A.1    Thiede, B.2    Müller, E.C.3    Scheler, C.4    Wittmann-Liebold, B.5    Jungblut, P.6
  • 49
    • 0000217562 scopus 로고
    • Electrospray and taylor-cone theory, dole's beam of macromolecules at least?
    • Wilm MS, Mann M: Electrospray and taylor-cone theory, dole's beam of macromolecules at least? Int J Mass Spectro Ion Process 1994, 136:167-180.
    • (1994) Int J Mass Spectro Ion Process , vol.136 , pp. 167-180
    • Wilm, M.S.1    Mann, M.2
  • 50
    • 0030026070 scopus 로고    scopus 로고
    • Femtomole sequencing of proteins from polyacrylamide gels by nano-electrospray mass spectrometry
    • Wilm M, Schevchenko A, Houthaeve T, Breit S, Schweigerer L, Fotsis T, Mann M: Femtomole sequencing of proteins from polyacrylamide gels by nano-electrospray mass spectrometry. Nature 1996, 379:466-469.
    • (1996) Nature , vol.379 , pp. 466-469
    • Wilm, M.1    Schevchenko, A.2    Houthaeve, T.3    Breit, S.4    Schweigerer, L.5    Fotsis, T.6    Mann, M.7
  • 51
    • 0028963216 scopus 로고
    • Differentiation of vascular smooth muscle cells and the regulation of protein kinase C-α
    • Haller H, Lindschau C, Quass P, Distler A, Luft FC: Differentiation of vascular smooth muscle cells and the regulation of protein kinase C-α Circ Res 1995, 76:21-29.
    • (1995) Circ Res , vol.76 , pp. 21-29
    • Haller, H.1    Lindschau, C.2    Quass, P.3    Distler, A.4    Luft, F.C.5
  • 52
    • 0028919891 scopus 로고    scopus 로고
    • High glucose concentrations and protein kinase C isoforms in vascular smooth muscle cells
    • Haller H, Bauer E, Quass P, Behrend M, Lindschau C, Distler A, Luft FC: High glucose concentrations and protein kinase C isoforms in vascular smooth muscle cells. Kidney Int 1996, 47:1057-1067.
    • (1996) Kidney Int , vol.47 , pp. 1057-1067
    • Haller, H.1    Bauer, E.2    Quass, P.3    Behrend, M.4    Lindschau, C.5    Distler, A.6    Luft, F.C.7


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