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Volumn 21, Issue 2, 2007, Pages 85-95

Targeting the phosphatidylinositol 3-kinase pathway in airway smooth muscle: Rationale and promise

Author keywords

[No Author keywords available]

Indexed keywords

CHOLINERGIC RECEPTOR BLOCKING AGENT; CORTICOSTEROID; EVEROLIMUS; HAMARTIN; LEUKOTRIENE; MAMMALIAN TARGET OF RAPAMYCIN; PHOSPHATIDYLINOSITOL 3 KINASE; PHOSPHATIDYLINOSITOL 3 KINASE INHIBITOR; PHOSPHATIDYLINOSITOL 3,4,5 TRISPHOSPHATE 3 PHOSPHATASE; RAPAMYCIN; S6 KINASE; TEMSIROLIMUS; TUBERIN; WORTMANNIN;

EID: 34247182075     PISSN: 11738804     EISSN: None     Source Type: Journal    
DOI: 10.2165/00063030-200721020-00003     Document Type: Review
Times cited : (30)

References (159)
  • 3
    • 33646338189 scopus 로고    scopus 로고
    • Chronic obstructive pulmonary disease: Linking outcomes and pathobiology of disease modification
    • Rennard SI. Chronic obstructive pulmonary disease: linking outcomes and pathobiology of disease modification. Proc Am Thoracic Soc 2006; 3 (3): 276-80
    • (2006) Proc Am Thoracic Soc , vol.3 , Issue.3 , pp. 276-280
    • Rennard, S.I.1
  • 4
    • 26944489955 scopus 로고    scopus 로고
    • Exacerbations: The asthma paradox
    • Holgate ST. Exacerbations: the asthma paradox. Am J Resp Crit Care Med 2005; 172 (8): 941-3
    • (2005) Am J Resp Crit Care Med , vol.172 , Issue.8 , pp. 941-943
    • Holgate, S.T.1
  • 5
    • 0033940869 scopus 로고    scopus 로고
    • Outcome measures in asthma
    • Barnes N. Outcome measures in asthma. Thorax 2000; 55 Suppl.: 70S-74
    • (2000) Thorax , vol.55 , Issue.SUPPL.
    • Barnes, N.1
  • 6
    • 34247183129 scopus 로고    scopus 로고
    • Panettieri RA, Grunstein MM. Airway smooth muscle hyperplasia and hypertrophy. In: Barnes PJ, Grunstein MM, Leff AR, et al. editors. Asthma. Philadelphia (PA): Lippincott-Raven; 1997: 823-42
    • Panettieri RA, Grunstein MM. Airway smooth muscle hyperplasia and hypertrophy. In: Barnes PJ, Grunstein MM, Leff AR, et al. editors. Asthma. Philadelphia (PA): Lippincott-Raven; 1997: 823-42
  • 7
    • 14944346763 scopus 로고    scopus 로고
    • Airway remodeling in asthma: Therapeutic implications of mechanisms
    • Homer RJ, Elias JA. Airway remodeling in asthma: therapeutic implications of mechanisms. Physiology 2005; 20 (1): 28-35
    • (2005) Physiology , vol.20 , Issue.1 , pp. 28-35
    • Homer, R.J.1    Elias, J.A.2
  • 8
    • 0035891664 scopus 로고    scopus 로고
    • Remodeling in asthma and chronic obstructive lung disease
    • Jeffery PK. Remodeling in asthma and chronic obstructive lung disease. Am J Resp Crit Care Med 2001; 164 (10 Suppl.): 28S-38
    • (2001) Am J Resp Crit Care Med , vol.164 , Issue.10 SUPPL.
    • Jeffery, P.K.1
  • 9
    • 24944464002 scopus 로고    scopus 로고
    • Remodeling and inflammation of bronchi in asthma and chronic obstructive pulmonary disease
    • Jeffery PK. Remodeling and inflammation of bronchi in asthma and chronic obstructive pulmonary disease. Proc Am Thoracic Soc 2004; 1 (3): 176-83
    • (2004) Proc Am Thoracic Soc , vol.1 , Issue.3 , pp. 176-183
    • Jeffery, P.K.1
  • 10
    • 4644241215 scopus 로고    scopus 로고
    • Differences in airway remodeling between asthma and chronic obstructive pulmonary disease
    • Aoshiba K, Nagai A. Differences in airway remodeling between asthma and chronic obstructive pulmonary disease. Clin Rev Allergy Immunol 2004; 1: 35-43
    • (2004) Clin Rev Allergy Immunol , vol.1 , pp. 35-43
    • Aoshiba, K.1    Nagai, A.2
  • 11
    • 2142700884 scopus 로고    scopus 로고
    • Asthma: More muscle cells or more muscular cells?
    • Black JL. Asthma: more muscle cells or more muscular cells? Am J Respir Crit Care Med 2004; 169 (9): 980-1
    • (2004) Am J Respir Crit Care Med , vol.169 , Issue.9 , pp. 980-981
    • Black, J.L.1
  • 12
    • 0002543851 scopus 로고
    • The pathology of asthma, with special reference to the changes in the bronchial mucosa
    • Dunnill MS. The pathology of asthma, with special reference to the changes in the bronchial mucosa. J Clin Pathol 1960; 13: 27-33
    • (1960) J Clin Pathol , vol.13 , pp. 27-33
    • Dunnill, M.S.1
  • 13
    • 0014491275 scopus 로고
    • A comparison of the quantitative anatomy of the bronchi in normal subjects, in status asthmaticus, in chronic bronchitis, and in emphysema
    • Dunnill MS, Massarella GR, Anderson JA. A comparison of the quantitative anatomy of the bronchi in normal subjects, in status asthmaticus, in chronic bronchitis, and in emphysema. Thorax 1969; 24: 176-9
    • (1969) Thorax , vol.24 , pp. 176-179
    • Dunnill, M.S.1    Massarella, G.R.2    Anderson, J.A.3
  • 14
    • 0015535510 scopus 로고
    • Quantitative measurement of bronchial muscle in asthma
    • Hossain S. Quantitative measurement of bronchial muscle in asthma. Am Rev Resp Dis 1973; 107: 99-109
    • (1973) Am Rev Resp Dis , vol.107 , pp. 99-109
    • Hossain, S.1
  • 15
    • 0027181166 scopus 로고
    • Cellular hypertrophy and hyperplasia of airway smooth muscle underlying bronchial asthma: A 3-D morphometric study
    • Ebina M, Takahashi T, Chiba T, et al. Cellular hypertrophy and hyperplasia of airway smooth muscle underlying bronchial asthma: a 3-D morphometric study. Am Rev Resp Dis 1993; 148: 720-6
    • (1993) Am Rev Resp Dis , vol.148 , pp. 720-726
    • Ebina, M.1    Takahashi, T.2    Chiba, T.3
  • 16
    • 0035376725 scopus 로고    scopus 로고
    • Airway smooth muscle as an immunomodulatory cell: A new target for pharmacotherapy?
    • Lazaar AL, Panettieri RA. Airway smooth muscle as an immunomodulatory cell: a new target for pharmacotherapy? Curr Opin Pharmacol 2001; 1: 259-64
    • (2001) Curr Opin Pharmacol , vol.1 , pp. 259-264
    • Lazaar, A.L.1    Panettieri, R.A.2
  • 17
    • 11144358047 scopus 로고    scopus 로고
    • Hyperplasia of smooth muscle in mild to moderate asthma without changes in cell size or gene expression
    • Woodruff PG, Dolganov GM, Ferrando RE, et al. Hyperplasia of smooth muscle in mild to moderate asthma without changes in cell size or gene expression. Am J Resp Crit Care Med 2004; 169 (9): 1001-6
    • (2004) Am J Resp Crit Care Med , vol.169 , Issue.9 , pp. 1001-1006
    • Woodruff, P.G.1    Dolganov, G.M.2    Ferrando, R.E.3
  • 19
    • 0037952701 scopus 로고    scopus 로고
    • Airway structural alterations selectively associated with severe asthma
    • Benayoun L, Druilhe A, Dombret M-C, et al. Airway structural alterations selectively associated with severe asthma. Am J Resp Crit Care Med 2003; 167 (10): 1360-8
    • (2003) Am J Resp Crit Care Med , vol.167 , Issue.10 , pp. 1360-1368
    • Benayoun, L.1    Druilhe, A.2    Dombret, M.-C.3
  • 20
    • 0036907405 scopus 로고    scopus 로고
    • Airway smooth muscle: An immunomodulatory cell
    • Panettieri J, Reynold A. Airway smooth muscle: an immunomodulatory cell. J Allergy Clin Immunol 2002; 110 Suppl.: S269-74
    • (2002) J Allergy Clin Immunol , vol.110 , Issue.SUPPL.
    • Panettieri, J.1    Reynold, A.2
  • 21
    • 0033788441 scopus 로고    scopus 로고
    • Phosphatidylinositol kinase regulation of airway smooth muscle cell proliferation
    • Thomas CF, Limper AH. Phosphatidylinositol kinase regulation of airway smooth muscle cell proliferation. Am J Resp Cell Mol Biol 2000; 23 (4): 429-30
    • (2000) Am J Resp Cell Mol Biol , vol.23 , Issue.4 , pp. 429-430
    • Thomas, C.F.1    Limper, A.H.2
  • 22
    • 0034133112 scopus 로고    scopus 로고
    • Mitogen-activated signaling and cell cycle regulation in airway smooth muscle
    • Page K, Hershenson MB. Mitogen-activated signaling and cell cycle regulation in airway smooth muscle. Front Biosci 2000; 5: d258-67
    • (2000) Front Biosci , vol.5
    • Page, K.1    Hershenson, M.B.2
  • 23
    • 0034581626 scopus 로고    scopus 로고
    • Phosphoinositide 3-kinase: A critical signaling event in pulmonary cells
    • Condliffe AM, Cadwallader KA, Walker TR, et al. Phosphoinositide 3-kinase: a critical signaling event in pulmonary cells. Resp Res 2000; 1: 24-9
    • (2000) Resp Res , vol.1 , pp. 24-29
    • Condliffe, A.M.1    Cadwallader, K.A.2    Walker, T.R.3
  • 24
    • 4444302962 scopus 로고    scopus 로고
    • Phophatidylinositol-3 kinase/mammalian target of rapamycin/p70s6k regulates contractile protein accumulation in airway myocyte differentiation
    • Halayko AJ, Kartha S, Stelmack GL, et al. Phophatidylinositol-3 kinase/mammalian target of rapamycin/p70s6k regulates contractile protein accumulation in airway myocyte differentiation. Am J Resp Cell Molec Biol 2004; 31 (3): 266-75
    • (2004) Am J Resp Cell Molec Biol , vol.31 , Issue.3 , pp. 266-275
    • Halayko, A.J.1    Kartha, S.2    Stelmack, G.L.3
  • 25
    • 0034911881 scopus 로고    scopus 로고
    • Synthesis and function of 3-phosphorylated inositol lipids
    • Vanhaesebroeck B, Leevers SJ, Ahmadi K, et al. Synthesis and function of 3-phosphorylated inositol lipids. Ann Rev Biochem 2001; 70 (1): 535-602
    • (2001) Ann Rev Biochem , vol.70 , Issue.1 , pp. 535-602
    • Vanhaesebroeck, B.1    Leevers, S.J.2    Ahmadi, K.3
  • 26
    • 0034912744 scopus 로고    scopus 로고
    • PTEN and myotubularin: Novel phosphoinositide phosphatases
    • Maehama T, Taylor GS, Dixon JE. PTEN and myotubularin: novel phosphoinositide phosphatases. Ann Rev Biochem 2001; 70 (1): 247-79
    • (2001) Ann Rev Biochem , vol.70 , Issue.1 , pp. 247-279
    • Maehama, T.1    Taylor, G.S.2    Dixon, J.E.3
  • 27
    • 16244393685 scopus 로고    scopus 로고
    • Signalling by PI3K isoforms: Insights from gene-targeted mice
    • Vanhaesebroeck B, Ali K, Bilancio A, et al. Signalling by PI3K isoforms: insights from gene-targeted mice. Trends Biochem Sci 2005; 30 (4): 194-204
    • (2005) Trends Biochem Sci , vol.30 , Issue.4 , pp. 194-204
    • Vanhaesebroeck, B.1    Ali, K.2    Bilancio, A.3
  • 28
    • 0030612144 scopus 로고    scopus 로고
    • p110δ, a novel phosphatidylinositol 3-kinase catalytic subunit that associates with p85 and is expressed predominantly in leukocytes
    • Chantry D, Vojtek A, Kashishian A, et al. p110δ, a novel phosphatidylinositol 3-kinase catalytic subunit that associates with p85 and is expressed predominantly in leukocytes. J Biol Chem 1997; 272: 19236-41
    • (1997) J Biol Chem , vol.272 , pp. 19236-19241
    • Chantry, D.1    Vojtek, A.2    Kashishian, A.3
  • 29
    • 0029090212 scopus 로고
    • Cloning and characterization of a G protein-activated human phosphoinositide 3-kinase
    • Stoyanov B, Volonia S, Hanck T, et al. Cloning and characterization of a G protein-activated human phosphoinositide 3-kinase. Science 1995; 269: 690-3
    • (1995) Science , vol.269 , pp. 690-693
    • Stoyanov, B.1    Volonia, S.2    Hanck, T.3
  • 30
    • 0034697119 scopus 로고    scopus 로고
    • The class II phosphoinositide 3-kinase PI3K-α is concentrated in the trans-Golgi network and present in clatrin-coated vesicles
    • Domin J, Gaidarov I, Smith MEK, et al. The class II phosphoinositide 3-kinase PI3K-α is concentrated in the trans-Golgi network and present in clatrin-coated vesicles. J Biol Chem 2000; 275: 11943-50
    • (2000) J Biol Chem , vol.275 , pp. 11943-11950
    • Domin, J.1    Gaidarov, I.2    Smith, M.E.K.3
  • 31
    • 0028981018 scopus 로고
    • A human phosphatidylinositol 3-kinase complex related to the yeast Vps34p-Vps15p protein sorting system
    • Volinia S, Dhand R, Vanhaesebroeck B, et al. A human phosphatidylinositol 3-kinase complex related to the yeast Vps34p-Vps15p protein sorting system. EMBO J 1995; 14: 3339-48
    • (1995) EMBO J , vol.14 , pp. 3339-3348
    • Volinia, S.1    Dhand, R.2    Vanhaesebroeck, B.3
  • 32
    • 1342292522 scopus 로고    scopus 로고
    • Phosphoinositide 3-kinase: Diverse roles in immune cell activation
    • Deane JA, Fruman DA. Phosphoinositide 3-kinase: diverse roles in immune cell activation. Ann Rev Immunol 2004; 22 (1): 563-98
    • (2004) Ann Rev Immunol , vol.22 , Issue.1 , pp. 563-598
    • Deane, J.A.1    Fruman, D.A.2
  • 33
    • 0036007421 scopus 로고    scopus 로고
    • Regulation of cell size in growth, development and human disease
    • Kozma SC, Thomas G. Regulation of cell size in growth, development and human disease. BioEssays 2002; 24: 65-71
    • (2002) BioEssays , vol.24 , pp. 65-71
    • Kozma, S.C.1    Thomas, G.2
  • 34
    • 0035190026 scopus 로고    scopus 로고
    • Cellular function of phosphoinositide 3-kinases: Implications for development, homeostasis, and cancer
    • Katso R, Okkenhaug K, Ahmadi K, et al. Cellular function of phosphoinositide 3-kinases: implications for development, homeostasis, and cancer. Ann Rev Cell Develop Biol 2001; 17 (1): 615-75
    • (2001) Ann Rev Cell Develop Biol , vol.17 , Issue.1 , pp. 615-675
    • Katso, R.1    Okkenhaug, K.2    Ahmadi, K.3
  • 35
    • 0033574429 scopus 로고    scopus 로고
    • Proliferative defect and embryonic lethality in mice homozygous for a deletion in the p110α subunit of phosphoinositide 3-kinase
    • Bi L, Okabe I, Bernard DJ, et al. Proliferative defect and embryonic lethality in mice homozygous for a deletion in the p110α subunit of phosphoinositide 3-kinase. J Biol Chem 1999; 274: 10963-8
    • (1999) J Biol Chem , vol.274 , pp. 10963-10968
    • Bi, L.1    Okabe, I.2    Bernard, D.J.3
  • 36
    • 0033556333 scopus 로고    scopus 로고
    • Impaired B cell development and proliferation in absence of phosphoinositide 3-kinase p85α
    • Fruman DA, Snapper SB, Yballe CM, et al. Impaired B cell development and proliferation in absence of phosphoinositide 3-kinase p85α. Science 1999; 283: 393-7
    • (1999) Science , vol.283 , pp. 393-397
    • Fruman, D.A.1    Snapper, S.B.2    Yballe, C.M.3
  • 37
    • 0034213075 scopus 로고    scopus 로고
    • The conserved phosphoinositide 3-kinase pathway determines heart size in mice
    • Shioi T, Kang PM, Douglas PS, et al. The conserved phosphoinositide 3-kinase pathway determines heart size in mice. EMBO J 2000; 19: 2537-48
    • (2000) EMBO J , vol.19 , pp. 2537-2548
    • Shioi, T.1    Kang, P.M.2    Douglas, P.S.3
  • 38
    • 0034681264 scopus 로고    scopus 로고
    • The multiple roles of PTEN in tumor suppression
    • Di Cristofano A, Pandolfi PP. The multiple roles of PTEN in tumor suppression. Cell 2000; 100: 387-90
    • (2000) Cell , vol.100 , pp. 387-390
    • Di Cristofano, A.1    Pandolfi, P.P.2
  • 39
    • 0037683087 scopus 로고    scopus 로고
    • Tumor suppressors hamartin and tuberin: Intracellular signaling
    • Krymskaya VP. Tumor suppressors hamartin and tuberin: intracellular signaling. Cell Signal 2003; 15: 729-39
    • (2003) Cell Signal , vol.15 , pp. 729-739
    • Krymskaya, V.P.1
  • 40
    • 0034705207 scopus 로고    scopus 로고
    • Mutations in the tuberous sclerosis complex gene TSC2 are a cause of sporadic pulmonary lymphangioleiomyomatosis
    • Carsillo T, Astrinidis A, Henske EP. Mutations in the tuberous sclerosis complex gene TSC2 are a cause of sporadic pulmonary lymphangioleiomyomatosis. Proc Natl Acad Sci U S A 2000; 97: 6085-90
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 6085-6090
    • Carsillo, T.1    Astrinidis, A.2    Henske, E.P.3
  • 41
    • 34247243645 scopus 로고    scopus 로고
    • Moses J. LAM and other diseases characterized by smooth muscle proliferation. New York: Marcel Dekker, Inc., 1999
    • Moses J. LAM and other diseases characterized by smooth muscle proliferation. New York: Marcel Dekker, Inc., 1999
  • 43
    • 0032246307 scopus 로고    scopus 로고
    • Lymphangioleiomyomatosis
    • Sullivan EJ. Lymphangioleiomyomatosis. Chest 1998; 114: 1689-703
    • (1998) Chest , vol.114 , pp. 1689-1703
    • Sullivan, E.J.1
  • 44
    • 0037732711 scopus 로고    scopus 로고
    • Lymphangioleiomyomatosis: A complex tale of serum response factor-mediated tissue inhibitor of metalloproteinase-3 regulation
    • Krymskaya VP, Shipley JM. Lymphangioleiomyomatosis: a complex tale of serum response factor-mediated tissue inhibitor of metalloproteinase-3 regulation. Am J Resp Cell Molec Biol 2003; 28 (5): 546-50
    • (2003) Am J Resp Cell Molec Biol , vol.28 , Issue.5 , pp. 546-550
    • Krymskaya, V.P.1    Shipley, J.M.2
  • 45
    • 11244297916 scopus 로고    scopus 로고
    • Dysregulation of the TSC-mTOR pathway in human disease
    • Inoki K, Corradetti MN, Guan K-L. Dysregulation of the TSC-mTOR pathway in human disease. Nat Genet 2005; 37 (1): 19-24
    • (2005) Nat Genet , vol.37 , Issue.1 , pp. 19-24
    • Inoki, K.1    Corradetti, M.N.2    Guan, K.-L.3
  • 46
    • 12344279947 scopus 로고    scopus 로고
    • TSC1-2 tumor suppressor and regulation of mTOR signalling: Linking cell growth and proliferation?
    • Findlay GM, Harrington LS, Lamb RF. TSC1-2 tumor suppressor and regulation of mTOR signalling: linking cell growth and proliferation? Curr Opin Genet Develop 2005; 15 (1): 69-76
    • (2005) Curr Opin Genet Develop , vol.15 , Issue.1 , pp. 69-76
    • Findlay, G.M.1    Harrington, L.S.2    Lamb, R.F.3
  • 47
    • 27844562649 scopus 로고    scopus 로고
    • Tuberous sclerosis complex: Linking growth and energy signaling pathways with human disease
    • Astrinidis A, Henske EP. Tuberous sclerosis complex: linking growth and energy signaling pathways with human disease. Oncogene 2005; 24 (50): 7475-81
    • (2005) Oncogene , vol.24 , Issue.50 , pp. 7475-7481
    • Astrinidis, A.1    Henske, E.P.2
  • 48
    • 16544383044 scopus 로고    scopus 로고
    • The mTOR/S6K signaling pathway: The role of the TSC1/2 tumor suppressor complex and the proto-oncogene Rheb
    • Nobukini T, Thomas G. The mTOR/S6K signaling pathway: the role of the TSC1/2 tumor suppressor complex and the proto-oncogene Rheb. Novartis Foundation Symposium 2005; 262: 148-59
    • (2005) Novartis Foundation Symposium , vol.262 , pp. 148-159
    • Nobukini, T.1    Thomas, G.2
  • 49
    • 0033775869 scopus 로고    scopus 로고
    • The TSC1 tumor suppressor hamartin regulates cell adhesion through ERM proteins and the GTPase Rho
    • Lamb RF, Roy C, Diefenbach TJ, et al. The TSC1 tumor suppressor hamartin regulates cell adhesion through ERM proteins and the GTPase Rho. Nat Cell Biol 2000; 2: 281-7
    • (2000) Nat Cell Biol , vol.2 , pp. 281-287
    • Lamb, R.F.1    Roy, C.2    Diefenbach, T.J.3
  • 50
    • 11244277987 scopus 로고    scopus 로고
    • TSC2 modulates actin cytoskeleton and focal adhesion through TSC1-binding domain and the Rac1 GTPase
    • Goncharova E, Goncharov D, Noonan D, et al. TSC2 modulates actin cytoskeleton and focal adhesion through TSC1-binding domain and the Rac1 GTPase. J Cell Biol 2004; 167 (6): 1171-82
    • (2004) J Cell Biol , vol.167 , Issue.6 , pp. 1171-1182
    • Goncharova, E.1    Goncharov, D.2    Noonan, D.3
  • 51
    • 0032741978 scopus 로고    scopus 로고
    • Tsc2+/- mice develop tumors in multiple sites that express gelsolin and are influenced by genetic background
    • Onda H, Lueck A, Marks PW, et al. Tsc2+/- mice develop tumors in multiple sites that express gelsolin and are influenced by genetic background. J Clin Invest 1999; 104: 687-95
    • (1999) J Clin Invest , vol.104 , pp. 687-695
    • Onda, H.1    Lueck, A.2    Marks, P.W.3
  • 52
    • 0033559663 scopus 로고    scopus 로고
    • Renal carcinogenesis, hepatic hemangiomatosis, and embryonic lethality caused by a germ-line Tsc2 mutation in mice
    • Kobayashi E, Minowa O, Kuno J, et al. Renal carcinogenesis, hepatic hemangiomatosis, and embryonic lethality caused by a germ-line Tsc2 mutation in mice. Cancer Res 1999; 59: 1206-11
    • (1999) Cancer Res , vol.59 , pp. 1206-1211
    • Kobayashi, E.1    Minowa, O.2    Kuno, J.3
  • 53
    • 0035902509 scopus 로고    scopus 로고
    • A germ-line Tsc1 mutation causes tumor development and embryonic lethality that are similar, but not identical to, those caused by Tsc2 mutation in mice
    • Kobayashi T, Minowa O, Sugitani Y, et al. A germ-line Tsc1 mutation causes tumor development and embryonic lethality that are similar, but not identical to, those caused by Tsc2 mutation in mice. Proc Natl Acad Sci U S A 2001; 98 (15): 8762-7
    • (2001) Proc Natl Acad Sci U S A , vol.98 , Issue.15 , pp. 8762-8767
    • Kobayashi, T.1    Minowa, O.2    Sugitani, Y.3
  • 54
    • 0036501277 scopus 로고    scopus 로고
    • A mouse model of TSC1 reveals sex-dependent lethality from liver hemangiomas, and up-regulation of p70S6 kinase activity in Tsc1 null cells
    • Kwiatkowski DJ, Zhang H, Bandura JL, et al. A mouse model of TSC1 reveals sex-dependent lethality from liver hemangiomas, and up-regulation of p70S6 kinase activity in Tsc1 null cells. Hum Mol Genet 2002; 11: 525-34
    • (2002) Hum Mol Genet , vol.11 , pp. 525-534
    • Kwiatkowski, D.J.1    Zhang, H.2    Bandura, J.L.3
  • 55
    • 0037163033 scopus 로고    scopus 로고
    • Tuberin regulates p70 S6 kinase activation and ribosomal protein S6 phosphorylation: A role for the TSC2 tumor suppressor gene in pulmonary lymphangioleiomyomatosis
    • Goncharova EA, Goncharov DA, Eszterhas A, et al. Tuberin regulates p70 S6 kinase activation and ribosomal protein S6 phosphorylation: a role for the TSC2 tumor suppressor gene in pulmonary lymphangioleiomyomatosis. J Biol Chem 2002; 277: 30958-67
    • (2002) J Biol Chem , vol.277 , pp. 30958-30967
    • Goncharova, E.A.1    Goncharov, D.A.2    Eszterhas, A.3
  • 56
    • 0036712741 scopus 로고    scopus 로고
    • McManus EJ, Alessi DR. TSC1-TSC2: a complex tale of PKB-mediated S6K regulation. Nat Cell Biol 2002; 4: E214-6
    • McManus EJ, Alessi DR. TSC1-TSC2: a complex tale of PKB-mediated S6K regulation. Nat Cell Biol 2002; 4: E214-6
  • 57
    • 0036342294 scopus 로고    scopus 로고
    • Identification of the tuberous sclerosis scomplex-2 tumor suppressor gene product tuberin as a target of the phosphoinositide 3-kinase/Akt/PKB pathway
    • Manning BD, Tee AR, Longdon MN, et al. Identification of the tuberous sclerosis scomplex-2 tumor suppressor gene product tuberin as a target of the phosphoinositide 3-kinase/Akt/PKB pathway. Mol Cell 2002; 10: 151-62
    • (2002) Mol Cell , vol.10 , pp. 151-162
    • Manning, B.D.1    Tee, A.R.2    Longdon, M.N.3
  • 58
    • 0041356888 scopus 로고    scopus 로고
    • Rheb binds TSC2 and promotes S6 kinase activation in a rapamycin- and farnesylation-dependent manner
    • Castro AF, Rebhun JF, Clark GG, et al. Rheb binds TSC2 and promotes S6 kinase activation in a rapamycin- and farnesylation-dependent manner. J Biol Chem 2003; 278: 32493-6
    • (2003) J Biol Chem , vol.278 , pp. 32493-32496
    • Castro, A.F.1    Rebhun, J.F.2    Clark, G.G.3
  • 59
    • 0038433304 scopus 로고    scopus 로고
    • Insulin activation of Rheb, a mediator of mTOR/S6K/4E-BP signaling, is inhibited by TSC1 and 2
    • Garami A, Zwartruis FJT, Nobukuni T, et al. Insulin activation of Rheb, a mediator of mTOR/S6K/4E-BP signaling, is inhibited by TSC1 and 2. Mol Cell 2003; 11: 1457-66
    • (2003) Mol Cell , vol.11 , pp. 1457-1466
    • Garami, A.1    Zwartruis, F.J.T.2    Nobukuni, T.3
  • 60
    • 0043127125 scopus 로고    scopus 로고
    • Rheb GTPase is a direct target of TSC2 GAP activity and regulates mTOR signaling
    • Inoki K, Li Y, Xu T, et al. Rheb GTPase is a direct target of TSC2 GAP activity and regulates mTOR signaling. Genes Devel 2003; 17 (15): 1829-34
    • (2003) Genes Devel , vol.17 , Issue.15 , pp. 1829-1834
    • Inoki, K.1    Li, Y.2    Xu, T.3
  • 61
    • 0042701991 scopus 로고    scopus 로고
    • Tuberous sclerosis complex gene products, tuberin and hamartin, control mTOR signaling by acting as a GTPase-activating protein complex toward Rheb
    • Tee AR, Manning BD, Roux PP, et al. Tuberous sclerosis complex gene products, tuberin and hamartin, control mTOR signaling by acting as a GTPase-activating protein complex toward Rheb. Curr Biol 2003; 13 (15): 1259-68
    • (2003) Curr Biol , vol.13 , Issue.15 , pp. 1259-1268
    • Tee, A.R.1    Manning, B.D.2    Roux, P.P.3
  • 62
    • 0141733228 scopus 로고    scopus 로고
    • Inactivation of the tuberous sclerosis complex-1 and -2 gene products occurs by phosphoinositide 3-kinase (PI3K)/Akt/PKB-dependent and -independent phosphorylation of tuberin
    • Tee AR, Anjum R, Blenis J. Inactivation of the tuberous sclerosis complex-1 and -2 gene products occurs by phosphoinositide 3-kinase (PI3K)/Akt/PKB-dependent and -independent phosphorylation of tuberin. J Biol Chem 2003; 278: 37288-96
    • (2003) J Biol Chem , vol.278 , pp. 37288-37296
    • Tee, A.R.1    Anjum, R.2    Blenis, J.3
  • 63
    • 18044381192 scopus 로고    scopus 로고
    • Rheb binds and regulates the mTOR kinase
    • Long X, Lin Y, Ortiz-Vega S, et al. Rheb binds and regulates the mTOR kinase. Curr Biol 2005; 15 (8): 702-13
    • (2005) Curr Biol , vol.15 , Issue.8 , pp. 702-713
    • Long, X.1    Lin, Y.2    Ortiz-Vega, S.3
  • 64
    • 21244456553 scopus 로고    scopus 로고
    • Rheb binding to mammalian target of rapamycin (mTOR) is regulated by amino acid sufficiency
    • Long X, Ortiz-Vega S, Lin Y, et al. Rheb binding to mammalian target of rapamycin (mTOR) is regulated by amino acid sufficiency. J Biol Chem 2005; 280 (25): 23433-6
    • (2005) J Biol Chem , vol.280 , Issue.25 , pp. 23433-23436
    • Long, X.1    Ortiz-Vega, S.2    Lin, Y.3
  • 65
    • 0442323560 scopus 로고    scopus 로고
    • Tuberous sclerosis complex: From Drosophila to human disease
    • Pan D, Dong J, Zhang Y, et al. Tuberous sclerosis complex: from Drosophila to human disease. Trends Cell Biol 2004; 14 (2): 78-85
    • (2004) Trends Cell Biol , vol.14 , Issue.2 , pp. 78-85
    • Pan, D.1    Dong, J.2    Zhang, Y.3
  • 66
    • 14844363721 scopus 로고    scopus 로고
    • Signaling by target of rapamycin proteins in cell growth control
    • Inoki K, Ouyang H, Li Y, et al. Signaling by target of rapamycin proteins in cell growth control. Microbiol Mol Biol Rev 2005; 69 (1): 79-100
    • (2005) Microbiol Mol Biol Rev , vol.69 , Issue.1 , pp. 79-100
    • Inoki, K.1    Ouyang, H.2    Li, Y.3
  • 67
    • 0034644525 scopus 로고    scopus 로고
    • Schmelzle T, Hall MN. TOR, a central controller of cell growth. Cell 2000; 103: 253-62
    • Schmelzle T, Hall MN. TOR, a central controller of cell growth. Cell 2000; 103: 253-62
  • 69
    • 0031453135 scopus 로고    scopus 로고
    • The mammalian target of rapamycin phosphorylates sites having a (Ser/Thr)-pro motif and is activated by antibodies to a region near its COOH terminus
    • Brunn GJ, Fadden P, Haystead TAJ, et al. The mammalian target of rapamycin phosphorylates sites having a (Ser/Thr)-pro motif and is activated by antibodies to a region near its COOH terminus. J Biol Chem 1997; 272 (51): 32547-50
    • (1997) J Biol Chem , vol.272 , Issue.51 , pp. 32547-32550
    • Brunn, G.J.1    Fadden, P.2    Haystead, T.A.J.3
  • 70
    • 0036753494 scopus 로고    scopus 로고
    • Two TOR complexes, only one of which is rapamycin sensitive, have distinct roles in cell growth control
    • Loewith R, Jacinto E, Wullschleger S, et al. Two TOR complexes, only one of which is rapamycin sensitive, have distinct roles in cell growth control. Mol Cell 2002; 10 (3): 457-68
    • (2002) Mol Cell , vol.10 , Issue.3 , pp. 457-468
    • Loewith, R.1    Jacinto, E.2    Wullschleger, S.3
  • 71
    • 3342895823 scopus 로고    scopus 로고
    • Sarbassov DD, Siraj MA, Kim D-H. Rictor, a novel binding partner of mTOR, defines a rapamycin-insensitive and raptor-independent pathway that regulates the cytoskeleton. Curr Biol 2004; 14 (14): 1296-302
    • Sarbassov DD, Siraj MA, Kim D-H. Rictor, a novel binding partner of mTOR, defines a rapamycin-insensitive and raptor-independent pathway that regulates the cytoskeleton. Curr Biol 2004; 14 (14): 1296-302
  • 72
    • 7944235758 scopus 로고    scopus 로고
    • Mammalian TOR complex 2 controls the actin cytoskeleton and is rapamycin insensitive
    • Jacinto E, Loewith R, Schmidt A, et al. Mammalian TOR complex 2 controls the actin cytoskeleton and is rapamycin insensitive. Nat Cell Biol 2004; 6 (11): 1122-8
    • (2004) Nat Cell Biol , vol.6 , Issue.11 , pp. 1122-1128
    • Jacinto, E.1    Loewith, R.2    Schmidt, A.3
  • 73
    • 13844312400 scopus 로고    scopus 로고
    • Phosphorylation and regulation of Akt/PKB/PKB by the Rictor-mTOR complex
    • Sarbassov DD, Guertin DA, Ali SM, et al. Phosphorylation and regulation of Akt/PKB/PKB by the Rictor-mTOR complex. Science 2005; 307 (5712): 1098-101
    • (2005) Science , vol.307 , Issue.5712 , pp. 1098-1101
    • Sarbassov, D.D.1    Guertin, D.A.2    Ali, S.M.3
  • 74
    • 33646485688 scopus 로고    scopus 로고
    • TSC1/TSC2 and Rheb have different effects on TORC1 and TORC2 activity
    • Yang Q, Inoki K, Kim E, et al. TSC1/TSC2 and Rheb have different effects on TORC1 and TORC2 activity. Proc Natl Acad Sci U S A 2006; 103 (18): 6811-6
    • (2006) Proc Natl Acad Sci U S A , vol.103 , Issue.18 , pp. 6811-6816
    • Yang, Q.1    Inoki, K.2    Kim, E.3
  • 75
    • 0025806666 scopus 로고
    • Inhibition of human T-cell activation by FK 506, rapamycin, and cyclosporine A
    • Sigal NH, Lin CS, Siekierka JJ. Inhibition of human T-cell activation by FK 506, rapamycin, and cyclosporine A. Transplant Proc 1991; 23: 1-5
    • (1991) Transplant Proc , vol.23 , pp. 1-5
    • Sigal, N.H.1    Lin, C.S.2    Siekierka, J.J.3
  • 76
    • 0026659046 scopus 로고
    • Rapamycin-FKBP specifically blocks growth-dependent activation of and signaling by the 70 kd S6 protein kinases
    • Chung J, Kuo CJ, Crabtree GR, et al. Rapamycin-FKBP specifically blocks growth-dependent activation of and signaling by the 70 kd S6 protein kinases. Cell 1992; 69: 1227-36
    • (1992) Cell , vol.69 , pp. 1227-1236
    • Chung, J.1    Kuo, C.J.2    Crabtree, G.R.3
  • 77
    • 0026721092 scopus 로고
    • Rapamycin selectively inhibits interleukin-2 activation of p70 S6 kinase
    • Kuo CJ, Chung J, Fiorentino DF, et al. Rapamycin selectively inhibits interleukin-2 activation of p70 S6 kinase. Nature 1992; 358: 70-3
    • (1992) Nature , vol.358 , pp. 70-73
    • Kuo, C.J.1    Chung, J.2    Fiorentino, D.F.3
  • 78
    • 0026759874 scopus 로고
    • Rapamycin-induced inhibition of the 70-kilodalton S6 protein kinase
    • Price DJ, Grove JR, Calvo V, et al. Rapamycin-induced inhibition of the 70-kilodalton S6 protein kinase. Science 1992; 257: 973-7
    • (1992) Science , vol.257 , pp. 973-977
    • Price, D.J.1    Grove, J.R.2    Calvo, V.3
  • 79
    • 0032539664 scopus 로고    scopus 로고
    • RAFT1 phosphorylation of the translational regulators p70 S6 kinase and 4E-BP1
    • Burnett PE, Barrow RK, Cohen NA, et al. RAFT1 phosphorylation of the translational regulators p70 S6 kinase and 4E-BP1. Proc Natl Acad Sci U S A 1998; 95: 1432-7
    • (1998) Proc Natl Acad Sci U S A , vol.95 , pp. 1432-1437
    • Burnett, P.E.1    Barrow, R.K.2    Cohen, N.A.3
  • 80
    • 0030881836 scopus 로고    scopus 로고
    • Phosphorylation of the translational repressor PHAS-I by mammalian target of rapamycin
    • Brunn GJ, Hudson CC, Sekulic A, et al. Phosphorylation of the translational repressor PHAS-I by mammalian target of rapamycin. Science 1997; 277: 99-101
    • (1997) Science , vol.277 , pp. 99-101
    • Brunn, G.J.1    Hudson, C.C.2    Sekulic, A.3
  • 81
    • 0031919552 scopus 로고    scopus 로고
    • Insulin signal transduction through protein kinase cascades
    • Avruch J. Insulin signal transduction through protein kinase cascades. Mol Cell Biochem 1998; 182: 31-48
    • (1998) Mol Cell Biochem , vol.182 , pp. 31-48
    • Avruch, J.1
  • 82
    • 5044229348 scopus 로고    scopus 로고
    • Molecular mechanisms of translational control
    • Gebauer F, Hentze MW. Molecular mechanisms of translational control. Nat Rev Mol Cell Biol 2004; 5: 827-35
    • (2004) Nat Rev Mol Cell Biol , vol.5 , pp. 827-835
    • Gebauer, F.1    Hentze, M.W.2
  • 83
    • 2342545519 scopus 로고    scopus 로고
    • Target of rapamycin (TOR): An integrator of nutrient and growth factor signals and coordinator of cell growth and cell cycle progression
    • Fingar DC, Blenis J. Target of rapamycin (TOR): an integrator of nutrient and growth factor signals and coordinator of cell growth and cell cycle progression. Oncogene 2004; 23: 3151-71
    • (2004) Oncogene , vol.23 , pp. 3151-3171
    • Fingar, D.C.1    Blenis, J.2
  • 84
    • 0032514924 scopus 로고    scopus 로고
    • Molecular cloning and characterization of a novel p70 S6 kinase, p70 S6 kinase β containing proline-rich region
    • Gout I, Minami T, Hara K, et al. Molecular cloning and characterization of a novel p70 S6 kinase, p70 S6 kinase β containing proline-rich region. J Biol Chem 1998; 273: 30061-4
    • (1998) J Biol Chem , vol.273 , pp. 30061-30064
    • Gout, I.1    Minami, T.2    Hara, K.3
  • 85
    • 0242432371 scopus 로고    scopus 로고
    • Cyclin dependent kinases and cell cycle control
    • Nurse P. Cyclin dependent kinases and cell cycle control. Biosci Rep 2002; 22: 487-99
    • (2002) Biosci Rep , vol.22 , pp. 487-499
    • Nurse, P.1
  • 86
    • 0016793098 scopus 로고
    • Genetic control of cell size at cell division in yeast
    • Nurse P. Genetic control of cell size at cell division in yeast. Nature 1975; 256: 547-51
    • (1975) Nature , vol.256 , pp. 547-551
    • Nurse, P.1
  • 87
    • 0017581306 scopus 로고
    • Coordination of growth with cell division in the yeast Sacchromyces cerevisiae
    • Johnston GC, Pringle JR, Hartwell LH. Coordination of growth with cell division in the yeast Sacchromyces cerevisiae. Exp Cell Res 1977; 105: 79-98
    • (1977) Exp Cell Res , vol.105 , pp. 79-98
    • Johnston, G.C.1    Pringle, J.R.2    Hartwell, L.H.3
  • 88
    • 0032568795 scopus 로고    scopus 로고
    • Coordination of growth and cell division in the Drosophila wing
    • Neufeld TP, de la Cruz AFA, Johnston LA, et al. Coordination of growth and cell division in the Drosophila wing. Cell 1998; 93 (7): 1183-93
    • (1998) Cell , vol.93 , Issue.7 , pp. 1183-1193
    • Neufeld, T.P.1    de la Cruz, A.F.A.2    Johnston, L.A.3
  • 89
    • 0030807904 scopus 로고    scopus 로고
    • Cell cycle progression, growth and patterning in imaginal discs despite inhibition of cell division after inactivation of Drosophila Cdc2 kinase
    • Weigmann K, Cohen S, Lehner C. Cell cycle progression, growth and patterning in imaginal discs despite inhibition of cell division after inactivation of Drosophila Cdc2 kinase. Development 1997; 124 (18): 3555-63
    • (1997) Development , vol.124 , Issue.18 , pp. 3555-3563
    • Weigmann, K.1    Cohen, S.2    Lehner, C.3
  • 90
    • 0032843917 scopus 로고    scopus 로고
    • Drosophila S6 kinase: A regulator of cell size
    • Montagne J, Stewart MJ, Stocker H, et al. Drosophila S6 kinase: a regulator of cell size. Science 1999; 285: 2126-9
    • (1999) Science , vol.285 , pp. 2126-2129
    • Montagne, J.1    Stewart, M.J.2    Stocker, H.3
  • 91
    • 11144356304 scopus 로고    scopus 로고
    • S6K1-/-/S6K2-/- mice exhibit perinatal lethality and rapamycin-sensitive 5′-terminal oligopyrimidine mRNA translation and reveal a mitogen-activated protein kinase-dependent s6 kinase pathway
    • Pende M, Um SH, Mieulet V, et al. S6K1-/-/S6K2-/- mice exhibit perinatal lethality and rapamycin-sensitive 5′-terminal oligopyrimidine mRNA translation and reveal a mitogen-activated protein kinase-dependent s6 kinase pathway. Mol Cell Biol 2004; 24 (8): 3112-24
    • (2004) Mol Cell Biol , vol.24 , Issue.8 , pp. 3112-3124
    • Pende, M.1    Um, S.H.2    Mieulet, V.3
  • 92
    • 20044392290 scopus 로고    scopus 로고
    • Atrophy of S6K1-/- skeletal muscle cells reveals distinct mTOR effectors for cell cycle and size control
    • Ohanna M, Sobering AK, Lapointe T, et al. Atrophy of S6K1-/- skeletal muscle cells reveals distinct mTOR effectors for cell cycle and size control. Nat Cell Biol 2005; 7 (3): 286-94
    • (2005) Nat Cell Biol , vol.7 , Issue.3 , pp. 286-294
    • Ohanna, M.1    Sobering, A.K.2    Lapointe, T.3
  • 93
    • 27644491911 scopus 로고    scopus 로고
    • Cooperative regulation of p70s6 kinase by receptor tyrosine kinases and G protein-coupled receptors augments airway smooth muscle growth
    • Billington CK, Kong KC, Bhattacharyya R, et al. Cooperative regulation of p70s6 kinase by receptor tyrosine kinases and G protein-coupled receptors augments airway smooth muscle growth. Biochemistry 2005; 44 (44): 14595-605
    • (2005) Biochemistry , vol.44 , Issue.44 , pp. 14595-14605
    • Billington, C.K.1    Kong, K.C.2    Bhattacharyya, R.3
  • 94
    • 25444440319 scopus 로고    scopus 로고
    • Signaling and regulation of G protein-coupled receptors in airway smooth muscle
    • Billington CK, Penn RB. Signaling and regulation of G protein-coupled receptors in airway smooth muscle. Resp Res 2003; 4 (2): 1-23
    • (2003) Resp Res , vol.4 , Issue.2 , pp. 1-23
    • Billington, C.K.1    Penn, R.B.2
  • 95
    • 0033604577 scopus 로고    scopus 로고
    • Signaling by distinct classes of phosphoinositide 3-kinases
    • Vanhaesebroeck B, Waterfield MD. Signaling by distinct classes of phosphoinositide 3-kinases. Exp Cell Res 1999; 253: 239-54
    • (1999) Exp Cell Res , vol.253 , pp. 239-254
    • Vanhaesebroeck, B.1    Waterfield, M.D.2
  • 96
    • 0032549177 scopus 로고    scopus 로고
    • Gβγ stimulates phosphoinositide 3-kinase-γ by direct interaction with two domains of catalytic p110 subunit
    • Leopoldt D, Hanck T, Exner T, et al. Gβγ stimulates phosphoinositide 3-kinase-γ by direct interaction with two domains of catalytic p110 subunit. J Biol Chem 1998; 273: 7024-9
    • (1998) J Biol Chem , vol.273 , pp. 7024-7029
    • Leopoldt, D.1    Hanck, T.2    Exner, T.3
  • 97
    • 0031037296 scopus 로고    scopus 로고
    • Linkage of G protein-coupled receptors to the MAPK signaling pathway through PI 3-kinase γ
    • Lopez-Ilasaca M, Crespo P, Pellici PG, et al. Linkage of G protein-coupled receptors to the MAPK signaling pathway through PI 3-kinase γ. Science 1997; 275: 394-7
    • (1997) Science , vol.275 , pp. 394-397
    • Lopez-Ilasaca, M.1    Crespo, P.2    Pellici, P.G.3
  • 98
    • 0034635259 scopus 로고    scopus 로고
    • Signals to move cells
    • Dekker LV, Segal AW. Signals to move cells. Science 2000; 287: 982-5
    • (2000) Science , vol.287 , pp. 982-985
    • Dekker, L.V.1    Segal, A.W.2
  • 99
    • 0032810950 scopus 로고    scopus 로고
    • Phosphatidylinositol 3-kinase mediates mitogen-induced human airway smooth muscle cell proliferation
    • Krymskaya VP, Penn RB, Orsini MJ, et al. Phosphatidylinositol 3-kinase mediates mitogen-induced human airway smooth muscle cell proliferation. Am J Physiol 1999; 277: L65-78
    • (1999) Am J Physiol , vol.277
    • Krymskaya, V.P.1    Penn, R.B.2    Orsini, M.J.3
  • 100
    • 0032997708 scopus 로고    scopus 로고
    • EGF activates ErbB2 and stimulates phosphatidylinositol 3-kinase in human airway smooth muscle cells
    • Krymskaya VP, Hoffman R, Eszterhas A, et al. EGF activates ErbB2 and stimulates phosphatidylinositol 3-kinase in human airway smooth muscle cells. Am J Physiol 1999; 276: L246-55
    • (1999) Am J Physiol , vol.276
    • Krymskaya, V.P.1    Hoffman, R.2    Eszterhas, A.3
  • 101
    • 0032886631 scopus 로고    scopus 로고
    • MAPK superfamily activation in human airway smooth muscle cell: Mitogenesis requires prolonged p42/p44 activation
    • Orsini MJ, Krymskaya VP, Eszterhas AJ, et al. MAPK superfamily activation in human airway smooth muscle cell: mitogenesis requires prolonged p42/p44 activation. Am J Physiol 1999; 277: L479-88
    • (1999) Am J Physiol , vol.277
    • Orsini, M.J.1    Krymskaya, V.P.2    Eszterhas, A.J.3
  • 102
    • 0033257938 scopus 로고    scopus 로고
    • Activation of K-p21ras and N-p21ras, but not H-p21ras, is necessary for mitogen-induced human airway smooth-muscle proliferation
    • Ammit AJ, Kane SA, Panettieri RA. Activation of K-p21ras and N-p21ras, but not H-p21ras, is necessary for mitogen-induced human airway smooth-muscle proliferation. Am J Resp Cell Molec Biol 1999; 21: 719-27
    • (1999) Am J Resp Cell Molec Biol , vol.21 , pp. 719-727
    • Ammit, A.J.1    Kane, S.A.2    Panettieri, R.A.3
  • 103
    • 0029785079 scopus 로고    scopus 로고
    • A regulatory role for cAMP in phosphatidylinositol 3-kinase/p70 ribosomal S6 kinase-mediated DNA synthesis in platelet-derived-growth-factor-stimulated bovine airway smooth-muscle cells
    • Scott PH, Belham CM, Al-Hafidh J, et al. A regulatory role for cAMP in phosphatidylinositol 3-kinase/p70 ribosomal S6 kinase-mediated DNA synthesis in platelet-derived-growth-factor-stimulated bovine airway smooth-muscle cells. Biochem J 1996; 318: 965-71
    • (1996) Biochem J , vol.318 , pp. 965-971
    • Scott, P.H.1    Belham, C.M.2    Al-Hafidh, J.3
  • 104
    • 0033787918 scopus 로고    scopus 로고
    • Mechanisms of proliferation synergy by receptor tyrosine kinase and G protein-coupled receptor activation in human airway smooth muscle
    • Krymskaya VP, Orsini MJ, Eszterhas AJ, et al. Mechanisms of proliferation synergy by receptor tyrosine kinase and G protein-coupled receptor activation in human airway smooth muscle. Am J Resp Cell Molec Biol 2000; 23 (4): 546-54
    • (2000) Am J Resp Cell Molec Biol , vol.23 , Issue.4 , pp. 546-554
    • Krymskaya, V.P.1    Orsini, M.J.2    Eszterhas, A.J.3
  • 105
    • 0033618344 scopus 로고    scopus 로고
    • 1 expression in airway smooth muscle cells
    • 1 expression in airway smooth muscle cells. J Biol Chem 1999; 274: 22065-71
    • (1999) J Biol Chem , vol.274 , pp. 22065-22071
    • Page, K.1    Li, J.2    Hodge, J.A.3
  • 106
    • 0033791846 scopus 로고    scopus 로고
    • Regulation of cyclin D1 expression and DNA synthesis by phosphatidylinositol 3-kinase in airway smooth muscle cells
    • Page K, Li J, Wang Y, et al. Regulation of cyclin D1 expression and DNA synthesis by phosphatidylinositol 3-kinase in airway smooth muscle cells. Am J Resp Cell Molec Biol 2000; 23 (4): 436-43
    • (2000) Am J Resp Cell Molec Biol , vol.23 , Issue.4 , pp. 436-443
    • Page, K.1    Li, J.2    Wang, Y.3
  • 107
    • 14644426493 scopus 로고    scopus 로고
    • Src is necessary and sufficient for human airway smooth muscle cell proliferation and migration
    • Krymskaya VP, Goncharova EA, Ammit AJ, et al. Src is necessary and sufficient for human airway smooth muscle cell proliferation and migration. FASEB J 2005; 19: 428-30
    • (2005) FASEB J , vol.19 , pp. 428-430
    • Krymskaya, V.P.1    Goncharova, E.A.2    Ammit, A.J.3
  • 108
    • 0035041349 scopus 로고    scopus 로고
    • Activation of class IA phosphatidylinositol 3-kinase stimulates DNA synthesis in human airway smooth muscle cells
    • Krymskaya VP, Ammit AJ, Hoffman RK, et al. Activation of class IA phosphatidylinositol 3-kinase stimulates DNA synthesis in human airway smooth muscle cells. Am J Physiol 2001; 280: L1009-18
    • (2001) Am J Physiol , vol.280
    • Krymskaya, V.P.1    Ammit, A.J.2    Hoffman, R.K.3
  • 109
    • 0028584245 scopus 로고
    • The phosphatidylinositol 3-kinase α is required for DNA synthesis induced by some, but not all, growth factors
    • Roche S, Koegl M, Courtneidge SA. The phosphatidylinositol 3-kinase α is required for DNA synthesis induced by some, but not all, growth factors. Proc Natl Acad Sci U S A 1994; 91: 9185-9
    • (1994) Proc Natl Acad Sci U S A , vol.91 , pp. 9185-9189
    • Roche, S.1    Koegl, M.2    Courtneidge, S.A.3
  • 110
    • 0027211693 scopus 로고
    • Phospholipase C-γ1 and phosphatidylinositol 3 kinase are the downstream mediators of the PDGF receptor's mitogenic signal
    • Valius M, Kazlauskas A. Phospholipase C-γ1 and phosphatidylinositol 3 kinase are the downstream mediators of the PDGF receptor's mitogenic signal. Cell 1993; 73: 321-34
    • (1993) Cell , vol.73 , pp. 321-334
    • Valius, M.1    Kazlauskas, A.2
  • 111
    • 0031035636 scopus 로고    scopus 로고
    • Specific activation of p85-p110 phosphatidylinositol 3′-kinase stimulates DNA synthesis by ras- and p70 S6 kinase-dependent pathways
    • McIlroy J, Chen D, Wjasow C, et al. Specific activation of p85-p110 phosphatidylinositol 3′-kinase stimulates DNA synthesis by ras- and p70 S6 kinase-dependent pathways. Mol Cell Biol 1997; 17: 248-55
    • (1997) Mol Cell Biol , vol.17 , pp. 248-255
    • McIlroy, J.1    Chen, D.2    Wjasow, C.3
  • 112
    • 0031708412 scopus 로고    scopus 로고
    • Activation of phosphatidyli-nositol 3-kinase is sufficient for cell cycle entry and promotes cellular changes characteristic of oncogenic transformation
    • Klippel A, Escobedo MA, Wachowicz MS, et al. Activation of phosphatidyli-nositol 3-kinase is sufficient for cell cycle entry and promotes cellular changes characteristic of oncogenic transformation. Mol Cell Biol 1998; 18: 5699-711
    • (1998) Mol Cell Biol , vol.18 , pp. 5699-5711
    • Klippel, A.1    Escobedo, M.A.2    Wachowicz, M.S.3
  • 113
    • 0028935995 scopus 로고
    • Dissociation of phosphatidylinositol 3-kinase activity and mitogenic inhibition in vascular smooth muscle cells
    • Weiss RH, Apostolids A. Dissociation of phosphatidylinositol 3-kinase activity and mitogenic inhibition in vascular smooth muscle cells. Cell Signal 1995; 7: 113-22
    • (1995) Cell Signal , vol.7 , pp. 113-122
    • Weiss, R.H.1    Apostolids, A.2
  • 114
    • 0030858836 scopus 로고    scopus 로고
    • Angiotensin II activates phosphatidylinositol 3-kinase in vascular smooth muscle cells
    • Saward L, Zahradka P. Angiotensin II activates phosphatidylinositol 3-kinase in vascular smooth muscle cells. Circ Res 1997; 81: 249-57
    • (1997) Circ Res , vol.81 , pp. 249-257
    • Saward, L.1    Zahradka, P.2
  • 115
    • 0032571084 scopus 로고    scopus 로고
    • Phosphatidylinositol 3-kinase inhibitors block aortic smooth muscle cell proliferation in mid-late G1 phase: Effect on cyclin-dependent kinase 2 and the inhibitory protein p27KIP1
    • Bacqueville D, Casagrande F, Perret B, et al. Phosphatidylinositol 3-kinase inhibitors block aortic smooth muscle cell proliferation in mid-late G1 phase: effect on cyclin-dependent kinase 2 and the inhibitory protein p27KIP1. Biochem Biophys Res Commun 1998; 244: 630-6
    • (1998) Biochem Biophys Res Commun , vol.244 , pp. 630-636
    • Bacqueville, D.1    Casagrande, F.2    Perret, B.3
  • 116
    • 0029664629 scopus 로고    scopus 로고
    • Hu ZW, Shi XY, Hoffman BB. ?1 Adrenergic receptors activate phosphatidylinositol 3-kinase in human vascular muscle cells. J Biol Chem 1996; 271: 8977-82
    • Hu ZW, Shi XY, Hoffman BB. ?1 Adrenergic receptors activate phosphatidylinositol 3-kinase in human vascular muscle cells. J Biol Chem 1996; 271: 8977-82
  • 117
    • 0030982219 scopus 로고    scopus 로고
    • Angiotensin II stimulates mitogen-activated protein kinases and protein synthesis by a Ras-independent pathway in vascular smooth muscle cells
    • Takahashi T, Kawahara Y, Okuda M, et al. Angiotensin II stimulates mitogen-activated protein kinases and protein synthesis by a Ras-independent pathway in vascular smooth muscle cells. J Biol Chem 1997; 272: 16018-22
    • (1997) J Biol Chem , vol.272 , pp. 16018-16022
    • Takahashi, T.1    Kawahara, Y.2    Okuda, M.3
  • 118
    • 0030575539 scopus 로고    scopus 로고
    • Phosphoinositide 3-kinase and the regulation of cell growth
    • Carpenter CL, Cantley LC. Phosphoinositide 3-kinase and the regulation of cell growth. Biochim Biophys Acta 1996; 1288: M11-6
    • (1996) Biochim Biophys Acta , vol.1288
    • Carpenter, C.L.1    Cantley, L.C.2
  • 119
    • 0029356279 scopus 로고
    • α-Thrombin increases cytosolic calcium and induces human airway smooth muscle cell proliferation
    • Panettieri RA, Hall IP, Maki CS, et al. α-Thrombin increases cytosolic calcium and induces human airway smooth muscle cell proliferation. Am J Resp Cell Molec Biol 1995; 13: 205-16
    • (1995) Am J Resp Cell Molec Biol , vol.13 , pp. 205-216
    • Panettieri, R.A.1    Hall, I.P.2    Maki, C.S.3
  • 120
    • 0031439247 scopus 로고    scopus 로고
    • Cellular functions regulated by Src family kinases
    • Thomas SM, Brugge JS. Cellular functions regulated by Src family kinases. Ann Rev Cell Develop Biol 1997; 13: 513-609
    • (1997) Ann Rev Cell Develop Biol , vol.13 , pp. 513-609
    • Thomas, S.M.1    Brugge, J.S.2
  • 121
    • 0029896163 scopus 로고    scopus 로고
    • Regulation, substrates and functions of Src
    • Brown MT, Cooper JA. Regulation, substrates and functions of Src. Biochim Biophys Acta 1996; 1287: 121-49
    • (1996) Biochim Biophys Acta , vol.1287 , pp. 121-149
    • Brown, M.T.1    Cooper, J.A.2
  • 122
    • 0036290485 scopus 로고    scopus 로고
    • Inhibitors of the tyrosine kinase signaling cascade attenuated thrombin-induced guinea pig airway smooth muscle cell proliferation
    • Tsang F, Hwa Choo H, Dawe GS, et al. Inhibitors of the tyrosine kinase signaling cascade attenuated thrombin-induced guinea pig airway smooth muscle cell proliferation. Biochem Biophys Res Commun 2002; 293 (1): 72-8
    • (2002) Biochem Biophys Res Commun , vol.293 , Issue.1 , pp. 72-78
    • Tsang, F.1    Hwa Choo, H.2    Dawe, G.S.3
  • 123
    • 0042704808 scopus 로고    scopus 로고
    • The critical role of c-Src and the Shc/Grb2/ERK2 signaling pathway in angiotensin II-dependent VSMC proliferation
    • Sayeski PP, Ali MS. The critical role of c-Src and the Shc/Grb2/ERK2 signaling pathway in angiotensin II-dependent VSMC proliferation. Exp Cell Res 2003; 287 (2): 339-49
    • (2003) Exp Cell Res , vol.287 , Issue.2 , pp. 339-349
    • Sayeski, P.P.1    Ali, M.S.2
  • 124
    • 0033613938 scopus 로고    scopus 로고
    • β-Arrestin-dependent formation of β2 adrenergic receptor-Src protein kinase complexes
    • Luttrell LM, Ferguson SSG, Daaka Y, et al. β-Arrestin-dependent formation of β2 adrenergic receptor-Src protein kinase complexes. Science 1999; 283: 655-61
    • (1999) Science , vol.283 , pp. 655-661
    • Luttrell, L.M.1    Ferguson, S.S.G.2    Daaka, Y.3
  • 125
    • 0035398487 scopus 로고    scopus 로고
    • G-protein-coupled receptors and signaling networks: Emerging paradigms
    • Marinissen MJ, Gutkind JS. G-protein-coupled receptors and signaling networks: emerging paradigms. Trends Pharmacol Sci 2001; 22 (7): 368-76
    • (2001) Trends Pharmacol Sci , vol.22 , Issue.7 , pp. 368-376
    • Marinissen, M.J.1    Gutkind, J.S.2
  • 126
    • 0027374488 scopus 로고
    • Inhibition of histamine secretion by wortmannin through the blockade of phosphatidylinositol 3-kinase in RBL-2H3 cells
    • Yano H, Nakanashi S, Kimura K, et al. Inhibition of histamine secretion by wortmannin through the blockade of phosphatidylinositol 3-kinase in RBL-2H3 cells. J Biol Chem 1993; 268: 25846-56
    • (1993) J Biol Chem , vol.268 , pp. 25846-25856
    • Yano, H.1    Nakanashi, S.2    Kimura, K.3
  • 127
    • 0025860067 scopus 로고
    • Demethoxyviridin and wortmannin block phospholipase C and D activation in human neutrophil
    • Bonser RW, Thompson NT, Randall RW, et al. Demethoxyviridin and wortmannin block phospholipase C and D activation in human neutrophil. Br J Pharmacol 1991; 103: 1237-41
    • (1991) Br J Pharmacol , vol.103 , pp. 1237-1241
    • Bonser, R.W.1    Thompson, N.T.2    Randall, R.W.3
  • 128
    • 0027968536 scopus 로고
    • Wortmannin inhibits serum-induced activation of phosphoinositide 3-kinase and proliferation of CHRF-288 cells
    • Vemuri GS, Rittenhouse SE. Wortmannin inhibits serum-induced activation of phosphoinositide 3-kinase and proliferation of CHRF-288 cells. Biochem Biophys Res Commun 1994; 202: 1619-23
    • (1994) Biochem Biophys Res Commun , vol.202 , pp. 1619-1623
    • Vemuri, G.S.1    Rittenhouse, S.E.2
  • 129
    • 0028486018 scopus 로고
    • Phosphatidylinositol 3-kinase
    • Kapeller R, Cantley LC. Phosphatidylinositol 3-kinase. BioEssays 1994; 16: 565-76
    • (1994) BioEssays , vol.16 , pp. 565-576
    • Kapeller, R.1    Cantley, L.C.2
  • 130
    • 0028918408 scopus 로고
    • Ras-dependent induction of cellular responses by constitutively active phosphatidylinositol-3 kinase
    • Hu Q, Klippel A, Muslin AJ, et al. Ras-dependent induction of cellular responses by constitutively active phosphatidylinositol-3 kinase. Science 1995; 268: 100-2
    • (1995) Science , vol.268 , pp. 100-102
    • Hu, Q.1    Klippel, A.2    Muslin, A.J.3
  • 131
    • 0029943605 scopus 로고    scopus 로고
    • Membrane localization of phospha-tidylinositol 3-kinase is sufficient to activate multiple signal-transducing kinase pathways
    • Klippel A, Reinhard C, Kavanaugh WM, et al. Membrane localization of phospha-tidylinositol 3-kinase is sufficient to activate multiple signal-transducing kinase pathways. Mol Cell Biol 1996; 16: 4117-27
    • (1996) Mol Cell Biol , vol.16 , pp. 4117-4127
    • Klippel, A.1    Reinhard, C.2    Kavanaugh, W.M.3
  • 132
    • 0028178928 scopus 로고
    • S6k activation mediated by phosphatidylinositol-3-OH kinase
    • S6k activation mediated by phosphatidylinositol-3-OH kinase. Nature 1994; 370: 71-5
    • (1994) Nature , vol.370 , pp. 71-75
    • Chung, J.1    Grammer, T.C.2    Lemon, K.P.3
  • 134
    • 0028908804 scopus 로고
    • Activation of pp70/85 S6 kinases in interleukin-2-responsive lymphoid cells is mediated by phosphatidylinositol 3-kinase and inhibited by cyclic AMP
    • Monfar M, Lemon KP, Grammer TC, et al. Activation of pp70/85 S6 kinases in interleukin-2-responsive lymphoid cells is mediated by phosphatidylinositol 3-kinase and inhibited by cyclic AMP. Mol Cell Biol 1995; 15: 326-37
    • (1995) Mol Cell Biol , vol.15 , pp. 326-337
    • Monfar, M.1    Lemon, K.P.2    Grammer, T.C.3
  • 137
    • 0032518467 scopus 로고    scopus 로고
    • 3-Phosphoinositide-dependent protein kinase 1 (PDK1) phosphorylates and activates the p70 S6 kinase in vivo and in vitro
    • Alessi DR, Kozlowski MT, Weng Q, et al. 3-Phosphoinositide-dependent protein kinase 1 (PDK1) phosphorylates and activates the p70 S6 kinase in vivo and in vitro. Curr Biol 1997; 8: 69-81
    • (1997) Curr Biol , vol.8 , pp. 69-81
    • Alessi, D.R.1    Kozlowski, M.T.2    Weng, Q.3
  • 138
    • 33745218112 scopus 로고    scopus 로고
    • Muscarinic receptor signaling in the pathophysiology of asthma and COPD
    • Gosens R, Zaagsma J, Meurs H, et al. Muscarinic receptor signaling in the pathophysiology of asthma and COPD. Resp Res 2006; 9: 73
    • (2006) Resp Res , vol.9 , pp. 73
    • Gosens, R.1    Zaagsma, J.2    Meurs, H.3
  • 139
    • 27644589238 scopus 로고    scopus 로고
    • Phosphodiesterase-4: Selective and dual-specificity inhibitors for the therapy of chronic obstructive pulmonary disease
    • Giembycz MA. Phosphodiesterase-4: selective and dual-specificity inhibitors for the therapy of chronic obstructive pulmonary disease. Proc Am Thoracic Soc 2005; 2 (4): 326-33
    • (2005) Proc Am Thoracic Soc , vol.2 , Issue.4 , pp. 326-333
    • Giembycz, M.A.1
  • 140
    • 4444330207 scopus 로고    scopus 로고
    • The potential of PDE4 inhibitors in respiratory disease
    • Spina D. The potential of PDE4 inhibitors in respiratory disease. Curr Drug Targets Inflam Allergy 2004; 3: 231-6
    • (2004) Curr Drug Targets Inflam Allergy , vol.3 , pp. 231-236
    • Spina, D.1
  • 141
    • 2542575493 scopus 로고    scopus 로고
    • PDE4 inhibitors in COPD: A more selective approach to treatment
    • Vignola AM. PDE4 inhibitors in COPD: a more selective approach to treatment. Resp Med 2004; 98 (6): 495-503
    • (2004) Resp Med , vol.98 , Issue.6 , pp. 495-503
    • Vignola, A.M.1
  • 142
    • 18144429417 scopus 로고    scopus 로고
    • Effects of ciclesonide and fluticasone propionate on allergen-induced airway inflammation and remodeling features
    • Leung SY, Eynott P, Nath P, et al. Effects of ciclesonide and fluticasone propionate on allergen-induced airway inflammation and remodeling features. J Allergy Clin Immunol 2005; 115 (5): 989-96
    • (2005) J Allergy Clin Immunol , vol.115 , Issue.5 , pp. 989-996
    • Leung, S.Y.1    Eynott, P.2    Nath, P.3
  • 143
    • 33645280326 scopus 로고    scopus 로고
    • Reversal of allergen-induced airway remodeling by CysLT1 receptor blockade
    • Henderson WR Jr, Chiang GKS, Tien Y-T, et al. Reversal of allergen-induced airway remodeling by CysLT1 receptor blockade. Am J Resp Crit Care Med 2006; 173 (7): 718-28
    • (2006) Am J Resp Crit Care Med , vol.173 , Issue.7 , pp. 718-728
    • Henderson Jr, W.R.1    Chiang, G.K.S.2    Tien, Y.-T.3
  • 144
    • 0034932164 scopus 로고    scopus 로고
    • Airway wall remodelling and hyperresponsiveness: Modelling remodelling in vitro and in vivo
    • Stewart AG. Airway wall remodelling and hyperresponsiveness: modelling remodelling in vitro and in vivo. Pulmon Pharmacol Ther 2001; 14 (3): 255-65
    • (2001) Pulmon Pharmacol Ther , vol.14 , Issue.3 , pp. 255-265
    • Stewart, A.G.1
  • 145
    • 33644504507 scopus 로고    scopus 로고
    • Difficult asthma
    • Strek ME. Difficult asthma. Proc Am Thoracic Soc 2006; 3 (1): 116-23
    • (2006) Proc Am Thoracic Soc , vol.3 , Issue.1 , pp. 116-123
    • Strek, M.E.1
  • 146
    • 0037162039 scopus 로고    scopus 로고
    • Lysophosphatidic acid in airway function and disease
    • Toews ML, Ediger TL, Romberger DJ, et al. Lysophosphatidic acid in airway function and disease. Biochim Biophys Acta 2002; 1582 (1-3): 240-50
    • (2002) Biochim Biophys Acta , vol.1582 , Issue.1-3 , pp. 240-250
    • Toews, M.L.1    Ediger, T.L.2    Romberger, D.J.3
  • 147
    • 32044466838 scopus 로고    scopus 로고
    • Exploiting the PI3K/AKT/PKB pathway for cancer drug discovery
    • Hennessy BT, Smith DL, Ram PT, et al. Exploiting the PI3K/AKT/PKB pathway for cancer drug discovery. Nat Rev Drug Discov 2005; 4 (12): 988-1004
    • (2005) Nat Rev Drug Discov , vol.4 , Issue.12 , pp. 988-1004
    • Hennessy, B.T.1    Smith, D.L.2    Ram, P.T.3
  • 148
    • 33646687962 scopus 로고    scopus 로고
    • Using isoform-specific inhibitors to target lipid kinases
    • Simon JA. Using isoform-specific inhibitors to target lipid kinases. Cell 2006; 125 (4): 647-9
    • (2006) Cell , vol.125 , Issue.4 , pp. 647-649
    • Simon, J.A.1
  • 149
    • 28844448182 scopus 로고    scopus 로고
    • Oncogenic PI3K deregulates transcription and translation
    • Bader AG, Kang S, Zhao L, et al. Oncogenic PI3K deregulates transcription and translation. Nat Rev Cancer 2005; 5 (12): 921-9
    • (2005) Nat Rev Cancer , vol.5 , Issue.12 , pp. 921-929
    • Bader, A.G.1    Kang, S.2    Zhao, L.3
  • 150
    • 0036632368 scopus 로고    scopus 로고
    • The phosphatidylinositol 3-kinase-Akt/PKB pathway in human cancer
    • Vivanco I, Sawyers CL. The phosphatidylinositol 3-kinase-Akt/PKB pathway in human cancer. Nat Rev Cancer 2002; 2: 489-501
    • (2002) Nat Rev Cancer , vol.2 , pp. 489-501
    • Vivanco, I.1    Sawyers, C.L.2
  • 151
    • 33646383684 scopus 로고    scopus 로고
    • A pharmacological map of the PI3-K family defines a role for p110α in insulin signaling
    • Knight ZA, Gonzalez B, Feldman ME, et al. A pharmacological map of the PI3-K family defines a role for p110α in insulin signaling. Cell 2006; 125 (4): 733-47
    • (2006) Cell , vol.125 , Issue.4 , pp. 733-747
    • Knight, Z.A.1    Gonzalez, B.2    Feldman, M.E.3
  • 152
    • 33744990592 scopus 로고    scopus 로고
    • Critical role for the p110α phosphoinositide-3-OH kinase in growth and metabolic regulation
    • Foukas LC, Claret M, Pearce W, et al. Critical role for the p110α phosphoinositide-3-OH kinase in growth and metabolic regulation. Nature 2006; 441 (7091): 366-70
    • (2006) Nature , vol.441 , Issue.7091 , pp. 366-370
    • Foukas, L.C.1    Claret, M.2    Pearce, W.3
  • 153
    • 33646382364 scopus 로고    scopus 로고
    • A dual PI3 kinase/mTOR inhibitor reveals emergent efficacy in glioma
    • Fan Q-W, Knight ZA, Goldenberg DD, et al. A dual PI3 kinase/mTOR inhibitor reveals emergent efficacy in glioma. Cancer Cell 2006; 9 (5): 341-9
    • (2006) Cancer Cell , vol.9 , Issue.5 , pp. 341-349
    • Fan, Q.-W.1    Knight, Z.A.2    Goldenberg, D.D.3
  • 155
    • 24744449495 scopus 로고    scopus 로고
    • PI3Kγ inhibition blocks glomerulo-nephritis and extends lifespan in a mouse model of systemic lupus
    • Barber DF, Bartolome A, Hernandez C, et al. PI3Kγ inhibition blocks glomerulo-nephritis and extends lifespan in a mouse model of systemic lupus. Nat Med 2005; 11 (9): 933-5
    • (2005) Nat Med , vol.11 , Issue.9 , pp. 933-935
    • Barber, D.F.1    Bartolome, A.2    Hernandez, C.3
  • 156
    • 24744448647 scopus 로고    scopus 로고
    • Modulating autoimmunity: Pick your PI3 kinase
    • Ohashi PS, Woodgett JR. Modulating autoimmunity: pick your PI3 kinase. Nat Med 2005; 11 (9): 924-5
    • (2005) Nat Med , vol.11 , Issue.9 , pp. 924-925
    • Ohashi, P.S.1    Woodgett, J.R.2
  • 157
    • 0036909260 scopus 로고    scopus 로고
    • Protein tyrosine kinases: Autoregulation and small-molecule inhibition
    • Hubbard SR. Protein tyrosine kinases: autoregulation and small-molecule inhibition. Curr Opin Struct Biol 2002; 12 (6): 735-41
    • (2002) Curr Opin Struct Biol , vol.12 , Issue.6 , pp. 735-741
    • Hubbard, S.R.1
  • 158
    • 2342559981 scopus 로고    scopus 로고
    • The TOR pathway: A target for cancer therapy
    • Bjornsti M-A, Houghton PJ. The TOR pathway: a target for cancer therapy. Nat Rev Cancer 2004; 4 (5): 335-48
    • (2004) Nat Rev Cancer , vol.4 , Issue.5 , pp. 335-348
    • Bjornsti, M.-A.1    Houghton, P.J.2
  • 159
    • 24344471377 scopus 로고    scopus 로고
    • 4E-Binding protein phosphorylation and eukaryotic initiation factor-4E release are required for airway smooth muscle hypertrophy
    • Zhou L, Goldsmith AM, Bentley JK, et al. 4E-Binding protein phosphorylation and eukaryotic initiation factor-4E release are required for airway smooth muscle hypertrophy. Am J Resp Cell Molec Biol 2005; 33 (2): 195-202
    • (2005) Am J Resp Cell Molec Biol , vol.33 , Issue.2 , pp. 195-202
    • Zhou, L.1    Goldsmith, A.M.2    Bentley, J.K.3


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