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Volumn 274, Issue 5 18-5, 1998, Pages

PDGF-induced glycosaminoglycan synthesis is mediated via phosphatidylinositol 3-kinase

Author keywords

Deoxyribonucleic acid synthesis; Fetal lung fibroblasts; Platelet derived growth factor

Indexed keywords

1 [[6 (3 METHOXYESTRA 1,3,5(10) TRIEN 17BETA YL)AMINO]HEXYL] 1H PYRROLE 2,5 DIONE; 2 (2 AMINO 3 METHOXYPHENYL)CHROMONE; 2 MORPHOLINO 8 PHENYLCHROMONE; CALPHOSTIN C; ELONGATION FACTOR; GLYCOSAMINOGLYCAN; PHOSPHATIDYLINOSITOL 3 KINASE; PHOSPHOLIPASE; WORTMANNIN;

EID: 0031863254     PISSN: 10400605     EISSN: None     Source Type: Journal    
DOI: 10.1152/ajplung.1998.274.5.l702     Document Type: Article
Times cited : (22)

References (53)
  • 1
    • 0024596794 scopus 로고
    • Calcium and GTP: Essential components in vesicular trafficking between the endoplasmic reticulum and Golgi apparatus
    • Beckers, C. J., and W. E. Balch. Calcium and GTP: essential components in vesicular trafficking between the endoplasmic reticulum and Golgi apparatus. J. Cell Biol. 108: 1245-1256, 1989.
    • (1989) J. Cell Biol. , vol.108 , pp. 1245-1256
    • Beckers, C.J.1    Balch, W.E.2
  • 4
    • 0028363216 scopus 로고
    • Differential regulation of PDGF genes in fetal rat lung fibroblasts
    • Buch, S., C. Jones, J. Liu, R. Han, A. K. Tanswell, and M. Post. Differential regulation of PDGF genes in fetal rat lung fibroblasts. Exp. Cell Res. 211: 142-149, 1994.
    • (1994) Exp. Cell Res. , vol.211 , pp. 142-149
    • Buch, S.1    Jones, C.2    Liu, J.3    Han, R.4    Tanswell, A.K.5    Post, M.6
  • 6
    • 0030002924 scopus 로고    scopus 로고
    • Fetal lung fibroblasts selectively down regulate proteoglycan synthesis in response to elevated oxygen
    • Caniggia, I., J. Liu, M. Kuliszewski, A. K. Tanswell, and M. Post. Fetal lung fibroblasts selectively down regulate proteoglycan synthesis in response to elevated oxygen. J. Biol. Chem. 271: 6625-6630, 1996.
    • (1996) J. Biol. Chem. , vol.271 , pp. 6625-6630
    • Caniggia, I.1    Liu, J.2    Kuliszewski, M.3    Tanswell, A.K.4    Post, M.5
  • 7
    • 0026787150 scopus 로고
    • Differential effect of platelet-derived growth factor on glycosaminoglycan synthesis by fetal rat lung cells
    • Lung Cell. Mol. Physiol. 7
    • Caniggia, I., and M. Post. Differential effect of platelet-derived growth factor on glycosaminoglycan synthesis by fetal rat lung cells. Am. J. Physiol. 263 (Lung Cell. Mol. Physiol. 7): L495-L500, 1992.
    • (1992) Am. J. Physiol. , vol.263
    • Caniggia, I.1    Post, M.2
  • 8
    • 0026344272 scopus 로고
    • Spatial and temporal differences in fibroblast behavior in fetal rat lung
    • Lung Cell. Mol. Physiol. 5
    • Caniggia, I., I. Tseu, N. N. Han, B. T. Smith, A. K. Tanswell, and M. Post. Spatial and temporal differences in fibroblast behavior in fetal rat lung. Am. J. Physiol. 261 (Lung Cell. Mol. Physiol. 5): L424-L433, 1991.
    • (1991) Am. J. Physiol. , vol.261
    • Caniggia, I.1    Tseu, I.2    Han, N.N.3    Smith, B.T.4    Tanswell, A.K.5    Post, M.6
  • 9
    • 0027443058 scopus 로고
    • Involvement of PKC-α in PDGF-mediated mitogenic signaling in human mesengial cells
    • Renal Fluid Electrolyte Physiol. 34
    • Choudhury, G., P. Biswas, G. Gramdaliano, and H. E. Abboud. Involvement of PKC-α in PDGF-mediated mitogenic signaling in human mesengial cells. Am. J. Physiol. 265 (Renal Fluid Electrolyte Physiol. 34): F634-F642, 1993.
    • (1993) Am. J. Physiol. , vol.265
    • Choudhury, G.1    Biswas, P.2    Gramdaliano, G.3    Abboud, H.E.4
  • 10
  • 11
    • 0027174818 scopus 로고
    • Effects of platelet-derived growth factor isoforms on human lung fibroblast proliferation and procollagen gene expression
    • Clark, J. G., D. K. Madtes, and G. Rughu. Effects of platelet-derived growth factor isoforms on human lung fibroblast proliferation and procollagen gene expression. Exp. Lung Res. 19: 327-344, 1993.
    • (1993) Exp. Lung Res. , vol.19 , pp. 327-344
    • Clark, J.G.1    Madtes, D.K.2    Rughu, G.3
  • 12
    • 0028979563 scopus 로고
    • Phosphatidyl-3-kinase regulation of fluid phase endocytosis
    • Claque, M. J., C. Thorpe, and A. Jones. Phosphatidyl-3-kinase regulation of fluid phase endocytosis. FEBS Lett. 367: 272-274, 1995.
    • (1995) FEBS Lett. , vol.367 , pp. 272-274
    • Claque, M.J.1    Thorpe, C.2    Jones, A.3
  • 13
    • 0022163967 scopus 로고
    • Progress in unraveling pathway of Golgi traffic
    • Farquhar, M. G. Progress in unraveling pathway of Golgi traffic. Annu. Rev. Cell Biol. 1: 447-488, 1985.
    • (1985) Annu. Rev. Cell Biol. , vol.1 , pp. 447-488
    • Farquhar, M.G.1
  • 14
    • 0027531637 scopus 로고
    • SH2-containing phosphotyrosine phophatase as a target of protein-tyrosine kinases
    • Feng, G.-S., C.-C. Hui, and T. Pawson. SH2-containing phosphotyrosine phophatase as a target of protein-tyrosine kinases. Science 259: 1607-1611, 1993.
    • (1993) Science , vol.259 , pp. 1607-1611
    • Feng, G.-S.1    Hui, C.-C.2    Pawson, T.3
  • 15
    • 0026673043 scopus 로고
    • Platelet-derived growth factor-induced transcription of the vascular endothelial growth factor gene is mediated by protein kinase C
    • Finkenzeller, G., D. Marme, H. A. Weich, and H. Hug. Platelet-derived growth factor-induced transcription of the vascular endothelial growth factor gene is mediated by protein kinase C. Cancer Res. 52: 4821-4823, 1992.
    • (1992) Cancer Res. , vol.52 , pp. 4821-4823
    • Finkenzeller, G.1    Marme, D.2    Weich, H.A.3    Hug, H.4
  • 17
    • 0025078512 scopus 로고
    • The cellular functions of small GTP-binding proteins
    • Hall, A. The cellular functions of small GTP-binding proteins. Science 249: 635-640, 1990.
    • (1990) Science , vol.249 , pp. 635-640
    • Hall, A.1
  • 18
    • 0027442495 scopus 로고
    • Ontogeny of platelet-derived growth factor receptor in fetal rat lung
    • Han, R. N. N., J. Liu, A. K. Tanswell, and M. Post. Ontogeny of platelet-derived growth factor receptor in fetal rat lung. Microsc. Res. Tech. 26: 381-338, 1993.
    • (1993) Microsc. Res. Tech. , vol.26 , pp. 381-1338
    • Han, R.N.N.1    Liu, J.2    Tanswell, A.K.3    Post, M.4
  • 19
    • 0026535373 scopus 로고
    • PDGF and growth related gene in rat lung. IV. Immunolocalization during fetal development
    • Han, R. N. N., C. Mawdsley, P. Souza, A. K. Tanswell, and M. Post. PDGF and growth related gene in rat lung. IV. Immunolocalization during fetal development. Pediatr. Res. 31: 323-329, 1992.
    • (1992) Pediatr. Res. , vol.31 , pp. 323-329
    • Han, R.N.N.1    Mawdsley, C.2    Souza, P.3    Tanswell, A.K.4    Post, M.5
  • 20
    • 0025464639 scopus 로고
    • PDGF: Mechanism of action and possible in vivo function
    • Heldin, C.-H., and B. Westermark. PDGF: mechanism of action and possible in vivo function. Cell Regul. 1: 555-566, 1990.
    • (1990) Cell Regul. , vol.1 , pp. 555-566
    • Heldin, C.-H.1    Westermark, B.2
  • 21
    • 0025200830 scopus 로고
    • Characterization of UPS34, a gene required for vacuolar protein sorting and vacuole segregation in Saccharomyces cerevisiae
    • Herman, P. K., and S. D. Emr. Characterization of UPS34, a gene required for vacuolar protein sorting and vacuole segregation in Saccharomyces cerevisiae. Mol. Cell. Biol. 10: 6742-6754, 1990.
    • (1990) Mol. Cell. Biol. , vol.10 , pp. 6742-6754
    • Herman, P.K.1    Emr, S.D.2
  • 22
    • 0028351218 scopus 로고
    • Disruption of PDGF receptor trafficking by mutation of its PI-3-kinase binding sites
    • Joly, M., A. Kazlauskas, F. S. Fay, and S. Corvera. Disruption of PDGF receptor trafficking by mutation of its PI-3-kinase binding sites. Science 263: 684-687, 1994.
    • (1994) Science , vol.263 , pp. 684-687
    • Joly, M.1    Kazlauskas, A.2    Fay, F.S.3    Corvera, S.4
  • 23
    • 0029151540 scopus 로고
    • Phosphatidylinosital-3-kinase activity is required for early endosome fusion
    • Jones, A. T., and M. J. Claque. Phosphatidylinosital-3-kinase activity is required for early endosome fusion. Biochem. J. 311: 31-34, 1995.
    • (1995) Biochem. J. , vol.311 , pp. 31-34
    • Jones, A.T.1    Claque, M.J.2
  • 24
    • 0024434183 scopus 로고
    • Autophosphorylation of the PDGF receptor in the kinase insert region regulates interactions with cell proteins
    • Kazlauskas, A., and J. A. Cooper. Autophosphorylation of the PDGF receptor in the kinase insert region regulates interactions with cell proteins. Cell 58: 1121-1133, 1989.
    • (1989) Cell , vol.58 , pp. 1121-1133
    • Kazlauskas, A.1    Cooper, J.A.2
  • 25
    • 0026176904 scopus 로고
    • Function of the major tyrosine phosphorylation site of the PDGF receptor beta subunit
    • Kazlauskas, A., A. Kashishian, J. A. Cooper, and M. Valius. Function of the major tyrosine phosphorylation site of the PDGF receptor beta subunit. Cell Regul. 2: 413-425, 1991.
    • (1991) Cell Regul. , vol.2 , pp. 413-425
    • Kazlauskas, A.1    Kashishian, A.2    Cooper, J.A.3    Valius, M.4
  • 26
    • 0024550448 scopus 로고
    • Calphostin C (UCN-1028C), a novel microbial compound, is a highly potent and specific inhibitor of protein kinase C
    • Kobayashi, E., H. Nakano, M. Morimoto, and T. Tamaoki. Calphostin C (UCN-1028C), a novel microbial compound, is a highly potent and specific inhibitor of protein kinase C. Biochem. Biophys. Res. Commun. 159: 548-553, 1989.
    • (1989) Biochem. Biophys. Res. Commun. , vol.159 , pp. 548-553
    • Kobayashi, E.1    Nakano, H.2    Morimoto, M.3    Tamaoki, T.4
  • 27
    • 0029093670 scopus 로고
    • The chemotactic response to PDGF-BB: Evidence of a role for Ras
    • Kundra, V., B. Anand-Apte, L. A. Feig, and B. R. Zetter. The chemotactic response to PDGF-BB: evidence of a role for Ras. J. Cell Biol. 130: 725-731, 1994.
    • (1994) J. Cell Biol. , vol.130 , pp. 725-731
    • Kundra, V.1    Anand-Apte, B.2    Feig, L.A.3    Zetter, B.R.4
  • 29
    • 0027312272 scopus 로고
    • Guanine-nucleotide-releasing factor hSos 1 binds to Grb2 and links receptor tyrosine kinases to Ras signalling
    • Li, N., A. Batzer, R. Daly, V. Yajnik, E. Skolnik, P. Chardin, D. Bar-Sagi, B. Margolis, and J. Schlessinger. Guanine-nucleotide-releasing factor hSos 1 binds to Grb2 and links receptor tyrosine kinases to Ras signalling. Nature 363: 85-92, 1993.
    • (1993) Nature , vol.363 , pp. 85-92
    • Li, N.1    Batzer, A.2    Daly, R.3    Yajnik, V.4    Skolnik, E.5    Chardin, P.6    Bar-Sagi, D.7    Margolis, B.8    Schlessinger, J.9
  • 31
    • 0029074007 scopus 로고
    • Mechanical strain-enhanced fetal lung cell proliferation is mediated by phospholipase C and D and protein kinase C
    • Lung Cell. Mol. Physiol. 12
    • Liu, M., J. Xu., J. Liu, M. E. Kraw, A. K. Tanswell, and M. Post. Mechanical strain-enhanced fetal lung cell proliferation is mediated by phospholipase C and D and protein kinase C. Am. J. Physiol. 268 (Lung Cell. Mol. Physiol. 12): L729-L738, 1995.
    • (1995) Am. J. Physiol. , vol.268
    • Liu, M.1    Xu, J.2    Liu, J.3    Kraw, M.E.4    Tanswell, A.K.5    Post, M.6
  • 32
    • 0028280103 scopus 로고
    • Effect of U-73,122, an inhibitor of phospholipase C, on actions of parathyroid hormone in opossum kidney cells
    • Renal Fluid Electrolyte Physiol 35
    • Martin, K. J., C. L. McConkey, M. K. Jacob, E. A. Gonzalez, M. Khan, and J. Baldassare. Effect of U-73,122, an inhibitor of phospholipase C, on actions of parathyroid hormone in opossum kidney cells. Am. J. Physiol. 266 (Renal Fluid Electrolyte Physiol 35): F254-F258, 1994.
    • (1994) Am. J. Physiol. , vol.266
    • Martin, K.J.1    McConkey, C.L.2    Jacob, M.K.3    Gonzalez, E.A.4    Khan, M.5    Baldassare, J.6
  • 34
    • 0027337519 scopus 로고
    • Complexes of Ras. GTP with Raf-1 and mitogen-activated protein kinase kinase
    • Moodie, S. A., B. M. Willumsen, M. J. Weber, and A. Wolfman. Complexes of Ras. GTP with Raf-1 and mitogen-activated protein kinase kinase. Science 260: 1658-1660, 1993.
    • (1993) Science , vol.260 , pp. 1658-1660
    • Moodie, S.A.1    Willumsen, B.M.2    Weber, M.J.3    Wolfman, A.4
  • 35
    • 0024382967 scopus 로고
    • Direct activation of the serine/threonine kinase activity of raf-1 though tyrosine phosphorylation by PDGF β-receptor
    • Morrison, D. K., D. R. Kaplan, J. A. Escobedo, U. R. Rapp, T. M. Roberts, and L. T. Williams. Direct activation of the serine/threonine kinase activity of raf-1 though tyrosine phosphorylation by PDGF β-receptor. Cell 58: 649-657, 1989.
    • (1989) Cell , vol.58 , pp. 649-657
    • Morrison, D.K.1    Kaplan, D.R.2    Escobedo, J.A.3    Rapp, U.R.4    Roberts, T.M.5    Williams, L.T.6
  • 36
    • 0027219341 scopus 로고
    • Platelet-derived growth factor increases the turnover of GTP/GDP on ras in permeabilized fibroblasts
    • Naberg, E., and B. Westermark. Platelet-derived growth factor increases the turnover of GTP/GDP on ras in permeabilized fibroblasts. J. Cell Biol. 268: 18187-18194, 1993.
    • (1993) J. Cell Biol. , vol.268 , pp. 18187-18194
    • Naberg, E.1    Westermark, B.2
  • 37
    • 0029034774 scopus 로고
    • Inhibition of MAP kinase blocks the differentiation of PC-12 cells induced by nerve growth factor
    • Pang, L., T. Sawada, S. J. Decker, and A. R. Saltiel. Inhibition of MAP kinase blocks the differentiation of PC-12 cells induced by nerve growth factor. J. Biol. Chem. 270: 13585-13588, 1995.
    • (1995) J. Biol. Chem. , vol.270 , pp. 13585-13588
    • Pang, L.1    Sawada, T.2    Decker, S.J.3    Saltiel, A.R.4
  • 38
    • 0028800326 scopus 로고
    • Platelet-derived growth factor stimulates the secretion of hyaluronic acid by proliferating human vascular smooth muscle cells
    • Papakonstantinou, E., G. Karakiulakis, M. Roth, and L. H. Block. Platelet-derived growth factor stimulates the secretion of hyaluronic acid by proliferating human vascular smooth muscle cells. Proc. Natl. Acad. Sci. USA 92: 9881-9885, 1995.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 9881-9885
    • Papakonstantinou, E.1    Karakiulakis, G.2    Roth, M.3    Block, L.H.4
  • 39
    • 0026718378 scopus 로고
    • PDGF (BB homodimer), TGF-β1, and b-FGF in dermal wound healing. Neovessel and matrices formation and cessation of repair
    • Pierce, G. F., J. E. Tarpley, D. Yanagihara, T. A. Mustoe, G. M. Fox, and A. Thomasom. PDGF (BB homodimer), TGF-β1, and b-FGF in dermal wound healing. Neovessel and matrices formation and cessation of repair. Am. J. Pathol. 140: 1375-1388, 1992.
    • (1992) Am. J. Pathol. , vol.140 , pp. 1375-1388
    • Pierce, G.F.1    Tarpley, J.E.2    Yanagihara, D.3    Mustoe, T.A.4    Fox, G.M.5    Thomasom, A.6
  • 40
    • 0025963720 scopus 로고
    • PDGF and TGF-β1 selectively modulate GAG, collagen, and myofibroblasts in excisional wounds
    • Pierce, G. F., J. Vande Berg, R. Rudolph, J. E. Tarpley, and T. Mustoe. PDGF and TGF-β1 selectively modulate GAG, collagen, and myofibroblasts in excisional wounds. Am. J. Pathol. 138: 629-646, 1991.
    • (1991) Am. J. Pathol. , vol.138 , pp. 629-646
    • Pierce, G.F.1    Vande Berg, J.2    Rudolph, R.3    Tarpley, J.E.4    Mustoe, T.5
  • 41
    • 0025729730 scopus 로고
    • Role of raf-1 serine/threonine protein kinase in growth factor signal transduction
    • Rapp, U. R. Role of raf-1 serine/threonine protein kinase in growth factor signal transduction. Oncogens 6: 495-500, 1991.
    • (1991) Oncogens , vol.6 , pp. 495-500
    • Rapp, U.R.1
  • 42
    • 0027930436 scopus 로고
    • PI-3-kinase inhibitor wortmannin blocks the insulin-like effects of growth hormone in isolated rat adipocytes
    • Ridderstrale, M., and H. Tornqvist. PI-3-kinase inhibitor wortmannin blocks the insulin-like effects of growth hormone in isolated rat adipocytes. Biochem. Biophys. Res. Commun. 203: 306-310, 1994.
    • (1994) Biochem. Biophys. Res. Commun. , vol.203 , pp. 306-310
    • Ridderstrale, M.1    Tornqvist, H.2
  • 43
    • 0027222560 scopus 로고
    • PDGF and TGF-β1 differentially affect the synthesis of biglycan and decorin by monkey arterial smooth muscle cells
    • Schonherr, E., H. T. Jarvelainen, M. G. Kinsella, L. T. Sandell, and T. N. Wight. PDGF and TGF-β1 differentially affect the synthesis of biglycan and decorin by monkey arterial smooth muscle cells. Arterioscler. Thromb. 13: 1026-1036, 1993.
    • (1993) Arterioscler. Thromb. , vol.13 , pp. 1026-1036
    • Schonherr, E.1    Jarvelainen, H.T.2    Kinsella, M.G.3    Sandell, L.T.4    Wight, T.N.5
  • 45
    • 0028122081 scopus 로고
    • Antisense oligodeoxynucleotides targeting PDGF-B mRNA inhibit cell proliferation during embryonic rat lung development
    • Souza, P., L. Sedlackova, M. Kuliszewski, J. Wang, J. Liu, I. Tsue, M. Liu, A. K. Tanswell, and M. Post. Antisense oligodeoxynucleotides targeting PDGF-B mRNA inhibit cell proliferation during embryonic rat lung development. Development 120: 2163-2173, 1994.
    • (1994) Development , vol.120 , pp. 2163-2173
    • Souza, P.1    Sedlackova, L.2    Kuliszewski, M.3    Wang, J.4    Liu, J.5    Tsue, I.6    Liu, M.7    Tanswell, A.K.8    Post, M.9
  • 46
    • 0029038223 scopus 로고
    • Stimulation of hyaluronic biosynthesis by platelet-derived growth factor-BB and transforming growth factor-β1 involves activation of protein kinase C
    • Suzuki, M., T. Asplund, H. Yamashita, C.-H. Heldin, and P. Heldin. Stimulation of hyaluronic biosynthesis by platelet-derived growth factor-BB and transforming growth factor-β1 involves activation of protein kinase C. Biochem. J. 307: 817-821, 1995.
    • (1995) Biochem. J. , vol.307 , pp. 817-821
    • Suzuki, M.1    Asplund, T.2    Yamashita, H.3    Heldin, C.-H.4    Heldin, P.5
  • 47
    • 0028321727 scopus 로고
    • Wortmannin binds specifically to 1-phosphatidylinositol 3-kinase while inhibiting guanine nucleotide-binding protein-coupled receptor signaling in neutrophil leukocytes
    • Thelen, M., M. P. Wymann, and H. Langen. Wortmannin binds specifically to 1-phosphatidylinositol 3-kinase while inhibiting guanine nucleotide-binding protein-coupled receptor signaling in neutrophil leukocytes. Proc. Natl. Acad. Sci. USA 91: 4960-4964, 1994.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 4960-4964
    • Thelen, M.1    Wymann, M.P.2    Langen, H.3
  • 48
    • 0027211693 scopus 로고
    • Phospholipase C-γ1 and phosphatidylinositol 3 kinase are the downstream mediators of the PDGF receptor's mitogenic signal
    • Valius, M., and A. Kazlauskas. Phospholipase C-γ1 and phosphatidylinositol 3 kinase are the downstream mediators of the PDGF receptor's mitogenic signal. Cell 73: 321-334, 1993.
    • (1993) Cell , vol.73 , pp. 321-334
    • Valius, M.1    Kazlauskas, A.2
  • 50
    • 0028170210 scopus 로고
    • A specific inhibitor of phosphatidylinosital-3-kinase, 2-(4-morpholinyl)-8-phenyl-4H-1-benzopyran-4-one (LY294002)
    • Vlahos, C. J., W. F. Matter, K. Hui, and R. F. Brown. A specific inhibitor of phosphatidylinosital-3-kinase, 2-(4-morpholinyl)-8-phenyl-4H-1-benzopyran-4-one (LY294002). J. Biol. Chem. 269: 5241-5248, 1994.
    • (1994) J. Biol. Chem. , vol.269 , pp. 5241-5248
    • Vlahos, C.J.1    Matter, W.F.2    Hui, K.3    Brown, R.F.4
  • 51
    • 0027250250 scopus 로고
    • Mammalian Ras interacts directly with the serine/threonine kinase Raf
    • Vojtek, A. B., S. M. Hollenberg, and J. A. Cooper. Mammalian Ras interacts directly with the serine/threonine kinase Raf. Cell 74: 205-214, 1993.
    • (1993) Cell , vol.74 , pp. 205-214
    • Vojtek, A.B.1    Hollenberg, S.M.2    Cooper, J.A.3
  • 52
    • 0026639464 scopus 로고
    • Hydrolysis of GTP by Sec4 protein plays an important role in vascular transport and is stimulated by a GTPase-activating protein in Saccharomyces cerevisiae
    • Walworth, N. C., P. Brennwald, A. K. Kabcenell, M. Garetl, and P. Novick. Hydrolysis of GTP by Sec4 protein plays an important role in vascular transport and is stimulated by a GTPase-activating protein in Saccharomyces cerevisiae. Mol. Cell. Biol. 12: 2017-2028, 1992.
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 2017-2028
    • Walworth, N.C.1    Brennwald, P.2    Kabcenell, A.K.3    Garetl, M.4    Novick, P.5
  • 53
    • 0021828496 scopus 로고
    • Association of phosphatidylinositol kinase activity with polyoma middle-T competent for transformation
    • Whitman, M. C., D. R. Kaplan, B. Schaffhausen, and L. Cantley. Association of phosphatidylinositol kinase activity with polyoma middle-T competent for transformation. Nature 315: 239-242, 1985.
    • (1985) Nature , vol.315 , pp. 239-242
    • Whitman, M.C.1    Kaplan, D.R.2    Schaffhausen, B.3    Cantley, L.4


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