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Volumn 15, Issue 33, 2009, Pages 3867-3877

Kinases as upstream regulators of the HIF system: Their emerging potential as anti-cancer drug targets

Author keywords

HIF 1; Hypoxia; Kinase; MAPK pathway; Phosphorylation; PI3K PKB pathway

Indexed keywords

1,4 DIAMINO 1,4 BIS(2 AMINOPHENYLTHIO) 2,3 DICYANOBUTADIENE; 2 (2 AMINO 3 METHOXYPHENYL)CHROMONE; 2 AMINOPURINE; 2 MORPHOLINO 8 PHENYLCHROMONE; 4 (4 FLUOROPHENYL) 2 (4 METHYLSULFINYLPHENYL) 5 (4 PYRIDYL)IMIDAZOLE; 6 (4 FLUOROPHENYL) 2,3 DIHYDRO 5 (4 PYRIDYL)IMIDAZO[2,1 B]THIAZOLE; CASEIN KINASE II; COMPOUND C; CYCLIC AMP DEPENDENT PROTEIN KINASE; CYCLOHEXIMIDE; GENISTEIN; GLYCOGEN SYNTHASE KINASE 3; HYDROXYMETHYLGLUTARYL COENZYME A REDUCTASE KINASE; HYPOXIA INDUCIBLE FACTOR 1ALPHA; MAMMALIAN TARGET OF RAPAMYCIN; MITOGEN ACTIVATED PROTEIN KINASE 1; MITOGEN ACTIVATED PROTEIN KINASE 3; MITOGEN ACTIVATED PROTEIN KINASE P38; PHOSPHATIDYLINOSITOL 3 KINASE; PHOSPHOPROTEIN PHOSPHATASE INHIBITOR; PROTEIN KINASE B; PROTEIN KINASE C; PROTEIN MDM2; PROTEIN SERINE THREONINE KINASE INHIBITOR; RAPAMYCIN; STRESS ACTIVATED PROTEIN KINASE; UNCLASSIFIED DRUG; VANADATE SODIUM; WORTMANNIN;

EID: 70649088038     PISSN: 13816128     EISSN: None     Source Type: Journal    
DOI: 10.2174/138161209789649358     Document Type: Review
Times cited : (33)

References (148)
  • 1
    • 35148828429 scopus 로고    scopus 로고
    • Hypoxia-inducible factor 1 (HIF-1) pathway
    • Semenza GL. Hypoxia-inducible factor 1 (HIF-1) pathway. Sci STKE 2007; 407: cm8.
    • (2007) Sci STKE , vol.407
    • Semenza, G.L.1
  • 2
    • 0028891906 scopus 로고
    • The transcription factors ATF-1 and CREB-1 bind constitutively to the hypoxia-inducible factor-1 (HIF-1) DNA recognition site
    • Kvietikova I, Wenger RH, Marti HH, Gassmann M. The transcription factors ATF-1 and CREB-1 bind constitutively to the hypoxia-inducible factor-1 (HIF-1) DNA recognition site. Nucleic Acids Res 1995; 23: 4542-4550
    • (1995) Nucleic Acids Res , vol.23 , pp. 4542-4550
    • Kvietikova, I.1    Wenger, R.H.2    Marti, H.H.3    Gassmann, M.4
  • 3
    • 31444444162 scopus 로고    scopus 로고
    • Integration of oxygen signaling at the consensus HRE
    • Wenger RH, Stiehl DP, Camenisch G. Integration of oxygen signaling at the consensus HRE. Sci STKE 2005; 306: re12.
    • (2005) Sci STKE , vol.306
    • Wenger, R.H.1    Stiehl, D.P.2    Camenisch, G.3
  • 4
    • 0028816847 scopus 로고
    • Purification and characterization of hypoxia-inducible factor 1
    • Wang GL, Semenza GL. Purification and characterization of hypoxia-inducible factor 1. J Biol Chem 1995; 270: 1230-1237
    • (1995) J Biol Chem , vol.270 , pp. 1230-1237
    • Wang, G.L.1    Semenza, G.L.2
  • 5
    • 0032538797 scopus 로고    scopus 로고
    • Signal transduction in hypoxic cells: Inducible nuclear translocation and recruitment of the CBP/p300 coactivator by the hypoxia-inducible factor-1α
    • Kallio PJ, Okamoto K, O'Brien S, Carrero P, Makino Y, Tanaka H et al. Signal transduction in hypoxic cells: inducible nuclear translocation and recruitment of the CBP/p300 coactivator by the hypoxia-inducible factor-1alpha. EMBO J 1998; 17: 6573-6586 (Pubitemid 28521792)
    • (1998) EMBO Journal , vol.17 , Issue.22 , pp. 6573-6586
    • Kallio, P.J.1    Okamoto, K.2    O'Brien, S.3    Carrero, P.4    Makino, Y.5    Tanaka, H.6    Poellinger, L.7
  • 6
    • 0030787469 scopus 로고    scopus 로고
    • Transactivation and inhibitory domains of Hypoxia-inducible factor 1α: Modulation of transcriptional activity by oxygen tension
    • DOI 10.1074/jbc.272.31.19253
    • Jiang BH, Zheng JZ, Leung SW, Roe R, Semenza GL. Transactivation and inhibitory domains of hypoxia-inducible factor 1alpha. Modulation of transcriptional activity by oxygen tension. J Biol Chem 1997; 272: 19253-19260 (Pubitemid 27337716)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.31 , pp. 19253-19260
    • Jiang, B.-H.1    Zheng, J.Z.2    Leung, S.W.3    Roe, R.4    Semenza, G.L.5
  • 7
    • 0030937718 scopus 로고    scopus 로고
    • Activation of hypoxia-inducible factor-1; Definition of regulatory domains within the α subunit
    • DOI 10.1074/jbc.272.17.11205
    • Pugh CW, O'Rourke JF, Nagao M, Gleadle JM, Ratcliffe PJ. Activation of hypoxia-inducible factor-1; definition of regulatory domains within the alpha subunit. J Biol Chem 1997; 272: 11205-11214 (Pubitemid 27184117)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.17 , pp. 11205-11214
    • Pugh, C.W.1    O'Rourke, J.F.2    Nagao, M.3    Gleadle, J.M.4    Ratcliffe, P.J.5
  • 8
    • 0033118983 scopus 로고    scopus 로고
    • Molecular mechanisms of transcription activation by HLF and HIF1α in response to hypoxia: Their stabilization and redox signal-induced interaction with CBP/p300
    • Ema M, Hirota K, Mimura J, Abe H, Yodoi J, Sogawa K, et al. Molecular mechanisms of transcription activation by HLF and HIF1alpha in response to hypoxia: their stabilization and redox signal-induced interaction with CBP/p300. EMBO J 1999; 18: 1905-1914 (Pubitemid 29158534)
    • (1999) EMBO Journal , vol.18 , Issue.7 , pp. 1905-1914
    • Ema, M.1    Hirota, K.2    Mimura, J.3    Abe, H.4    Yodoi, J.5    Sogawa, K.6    Poellinger, L.7    Fujii-Kuriyama, Y.8
  • 13
    • 0035868277 scopus 로고    scopus 로고
    • Perivenous expression of the mRNA of the three hypoxia-inducible factor alpha-subunits, HIF1alpha, HIF2alpha and HIF3alpha, in rat liver
    • Kietzmann T, Cornesse Y, Brechtel K, Modaressi S, Jungermann K. Perivenous expression of the mRNA of the three hypoxia-inducible factor alpha-subunits, HIF1alpha, HIF2alpha and HIF3alpha, in rat liver. Biochem J 2001; 354: 531-537
    • (2001) Biochem J , vol.354 , pp. 531-537
    • Kietzmann, T.1    Cornesse, Y.2    Brechtel, K.3    Modaressi, S.4    Jungermann, K.5
  • 14
    • 0035783413 scopus 로고    scopus 로고
    • Selective cardiorespiratory and catecholaminergic areas express the hypoxia-inducible factor-1alpha (HIF-1alpha) under in vivo hypoxia in rat brainstem
    • Pascual O, Denavit-Saubie M, Dumas S, Kietzmann T, Ghilini G, Mallet J, et al. Selective cardiorespiratory and catecholaminergic areas express the hypoxia-inducible factor-1alpha (HIF-1alpha) under in vivo hypoxia in rat brainstem. Eur J Neurosci 2001; 14: 1981-1991.
    • (2001) Eur J Neurosci , vol.14 , pp. 1981-1991
    • Pascual, O.1    Denavit-Saubie, M.2    Dumas, S.3    Kietzmann, T.4    Ghilini, G.5    Mallet, J.6
  • 15
    • 0029123437 scopus 로고
    • Effect of altered redox states on expression and DNA-binding activity of hypoxia-inducible factor 1
    • Wang GL, Jiang BH, Semenza GL. Effect of altered redox states on expression and DNA-binding activity of hypoxia-inducible factor 1. Biochem Biophys Res Commun 1995; 212: 550-556
    • (1995) Biochem Biophys Res Commun , vol.212 , pp. 550-556
    • Wang, G.L.1    Jiang, B.H.2    Semenza, G.L.3
  • 17
    • 0035917808 scopus 로고    scopus 로고
    • Targeting of HIF-alpha to the von Hippel-Lindau ubiquitylation complex by O-2-regulated prolyl hydroxylation
    • Jaakkola P, Mole DR, Tian YM, Wilson MI, Gielbert J, Gaskell SJ, et al. Targeting of HIF-alpha to the von Hippel-Lindau ubiquitylation complex by O-2-regulated prolyl hydroxylation. Science 2001; 292: 468-472
    • (2001) Science , vol.292 , pp. 468-472
    • Jaakkola, P.1    Mole, D.R.2    Tian, Y.M.3    Wilson, M.I.4    Gielbert, J.5    Gaskell, S.J.6
  • 18
    • 0035903468 scopus 로고    scopus 로고
    • Independent function of two destruction domains in hypoxia-inducible factor-α chains activated by prolyl hydroxylation
    • DOI 10.1093/emboj/20.18.5197
    • Masson N, Willam C, Maxwell PH, Pugh CW, Ratcliffe PJ. Independent function of two destruction domains in hypoxia-inducible factor-alpha chains activated by prolyl hydroxylation. EMBO J 2001; 20: 5197-5206 (Pubitemid 32910914)
    • (2001) EMBO Journal , vol.20 , Issue.18 , pp. 5197-5206
    • Masson, N.1    Willam, C.2    Maxwell, P.H.3    Pugh, C.W.4    Ratcliffe, P.J.5
  • 19
    • 0036469038 scopus 로고    scopus 로고
    • Asparagine hydroxylation of the HIF transactivation domain: A hypoxic switch
    • DOI 10.1126/science.1068592
    • Lando D, Peet DJ, Whelan DA, Gorman JJ, Whitelaw ML. Asparagine hydroxylation of the HIF transactivation domain a hypoxic switch. Science 2002; 295: 858-861 (Pubitemid 34118367)
    • (2002) Science , vol.295 , Issue.5556 , pp. 858-861
    • Lando, D.1    Peet, D.J.2    Whelan, D.A.3    Gorman, J.J.4    Whitelaw, M.L.5
  • 20
    • 0033587146 scopus 로고    scopus 로고
    • The tumour suppressor protein VHL targets hypoxia-inducible factors for oxygen-dependent proteolysis
    • see comments
    • Maxwell PH, Wiesener MS, Chang GW, Clifford SC, Vaux EC, Cockman ME, et al. The tumour suppressor protein VHL targets hypoxia-inducible factors for oxygen-dependent proteolysis [see comments]. Nature 1999; 399: 271-275
    • (1999) Nature , vol.399 , pp. 271-275
    • Maxwell, P.H.1    Wiesener, M.S.2    Chang, G.W.3    Clifford, S.C.4    Vaux, E.C.5    Cockman, M.E.6
  • 21
    • 0037035851 scopus 로고    scopus 로고
    • Structure of an HIF-1α-pVHL complex: Hydroxyproline recognition in signaling
    • DOI 10.1126/science.1073440
    • Min JH, Yang H, Ivan M, Gertler F, Kaelin WG, Jr., Pavletich NP. Structure of an HIF-1alpha -pVHL complex: hydroxyproline recognition in signaling. Science 2002; 296: 1886-1889 (Pubitemid 34596278)
    • (2002) Science , vol.296 , Issue.5574 , pp. 1886-1889
    • Min, J.-H.1    Yang, H.2    Ivan, M.3    Gertler, F.4    Kaelin Jr., W.G.5    Pavietich, N.P.6
  • 23
    • 0034663894 scopus 로고    scopus 로고
    • Mechanism of regulation of the hypoxia-inducible factor-la by the von Hippel-Lindau tumor suppressor protein
    • Tanimoto K, Makino Y, Pereira T, Poellinger L. Mechanism of regulation of the hypoxia-inducible factor-1 alpha by the von Hippel-Lindau tumor suppressor protein. EMBO J 2000; 19: 4298-4309 (Pubitemid 30623741)
    • (2000) EMBO Journal , vol.19 , Issue.16 , pp. 4298-4309
    • Tanimoto, K.1    Makino, Y.2    Pereira, T.3    Poellinger, L.4
  • 25
    • 0345164318 scopus 로고    scopus 로고
    • The VHL tumour-suppressor gene paradigm
    • Kaelin WGJ, Maher ER. The VHL tumour-suppressor gene paradigm. Trends Genet 1998; 14: 423-426
    • (1998) Trends Genet , vol.14 , pp. 423-426
    • Kaelin, W.G.J.1    Maher, E.R.2
  • 26
    • 0033525830 scopus 로고    scopus 로고
    • Regulation of the hypoxia-inducible transcription factor 1α by the ubiquitin-proteasome pathway
    • DOI 10.1074/jbc.274.10.6519
    • Kallio PJ, Wilson WJ, O'Brien S, Makino Y, Poellinger L. Regulation of the hypoxia-inducible transcription factor 1alpha by the ubiquitin-proteasome pathway. J Biol Chem 1999; 274: 6519-6525 (Pubitemid 29111068)
    • (1999) Journal of Biological Chemistry , vol.274 , Issue.10 , pp. 6519-6525
    • Kallio, P.J.1    Wilson, W.J.2    O'Brien, S.3    Makino, Y.4    Poellinger, L.5
  • 27
    • 0030961006 scopus 로고    scopus 로고
    • Hypoxia-inducible factor 1α (HIF-1α) protein is rapidly degraded by the ubiquitin-proteasome system under normoxic conditions. Its stabilization by hypoxia depends on redox-induced changes
    • DOI 10.1074/jbc.272.36.22642
    • Salceda S, Caro J. Hypoxia-inducible factor 1alpha (HIF-1alpha) protein is rapidly degraded by the ubiquitin-proteasome system under normoxic conditions. Its stabilization by hypoxia depends on redox-induced changes. J Biol Chem 1997; 272: 22642-22647 (Pubitemid 27386079)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.36 , pp. 22642-22647
    • Salceda, S.1    Caro, J.2
  • 28
    • 0027427588 scopus 로고
    • Characterization of hypoxia-inducible factor 1 and regulation of DNA binding activity by hypoxia
    • Wang GL, Semenza GL. Characterization of hypoxia-inducible factor 1 and regulation of DNA binding activity by hypoxia. J Biol Chem 1993; 268: 21513-21518 (Pubitemid 23320639)
    • (1993) Journal of Biological Chemistry , vol.268 , Issue.29 , pp. 21513-21518
    • Wang, G.L.1    Semenza, G.L.2
  • 29
    • 0028785860 scopus 로고
    • Effect of protein kinase and phosphatase inhibitors on expression of hypoxia-inducible factor 1
    • Wang GL, Jiang BH, Semenza GL. Effect of protein kinase and phosphatase inhibitors on expression of hypoxia-inducible factor 1. Biochem Biophys Res Commun 1995; 216: 669-675
    • (1995) Biochem Biophys Res Commun , vol.216 , pp. 669-675
    • Wang, G.L.1    Jiang, B.H.2    Semenza, G.L.3
  • 30
    • 34547228831 scopus 로고    scopus 로고
    • Atypical mitogen-activated protein kinases: Structure, regulation and functions
    • DOI 10.1016/j.bbamcr.2006.11.001, PII S0167488906003703
    • Coulombe P, Meloche S. Atypical mitogen-activated protein kinases: structure, regulation and functions. Biochim Biophys Acta 2007; 1773: 1376-1387 (Pubitemid 47125971)
    • (2007) Biochimica et Biophysica Acta - Molecular Cell Research , vol.1773 , Issue.8 , pp. 1376-1387
    • Coulombe, P.1    Meloche, S.2
  • 31
    • 0031038419 scopus 로고    scopus 로고
    • Complex role of protein phosphorylation in gene activation by hypoxia
    • Salceda S, Beck I, Srinivas V, Caro J. Complex role of protein phosphorylation in gene activation by hypoxia. Kidney Int 1997; 51: 556-559 (Pubitemid 27088175)
    • (1997) Kidney International , vol.51 , Issue.2 , pp. 556-559
    • Salceda, S.1    Beck, I.2    Srinivas, V.3    Caro, J.4
  • 32
    • 0030866226 scopus 로고    scopus 로고
    • Hypoxia induces c-fos transcription via a mitogen-activated protein kinase-dependent pathway
    • DOI 10.1074/jbc.272.37.23435
    • Muller JM, Krauss B, Kaltschmidt C, Baeuerle PA, Rupec RA. Hypoxia induces c-fos transcription via a mitogen-activated protein kinase-dependent pathway. J Biol Chem 1997; 272: 23435-23439 (Pubitemid 27392486)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.37 , pp. 23435-23439
    • Muller, J.M.1    Krauss, B.2    Kaltschmidt, C.3    Baeuerle, P.A.4    Rupec, R.A.5
  • 35
    • 0032725554 scopus 로고    scopus 로고
    • P42/p44 mitogen-activated protein kinases phosphorylate hypoxia-inducible factor 1alpha (HIF-1alpha) and enhance the transcriptional activity of HIF-1
    • Richard DE, Berra E, Gothie E, Roux D, Pouyssegur J. p42/p44 mitogen-activated protein kinases phosphorylate hypoxia-inducible factor 1alpha (HIF-1alpha) and enhance the transcriptional activity of HIF-1. J Biol Chem 1999; 274: 32631-32637
    • (1999) J Biol Chem , vol.274 , pp. 32631-32637
    • Richard, D.E.1    Berra, E.2    Gothie, E.3    Roux, D.4    Pouyssegur, J.5
  • 36
    • 0037515549 scopus 로고    scopus 로고
    • MAPK signaling up-regulates the activity of hypoxia-inducible factors by its effects on p300
    • DOI 10.1074/jbc.M209702200
    • Sang N, Stiehl DP, Bohensky J, Leshchinsky I, Srinivas V, Caro J. MAPK signaling up-regulates the activity of hypoxia-inducible factors by its effects on p300. J Biol Chem 2003; 278: 14013-14019 (Pubitemid 36799945)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.16 , pp. 14013-14019
    • Sang, N.1    Stiehl, D.P.2    Bohensky, J.3    Leshchinsky, I.4    Srinivas, V.5    Caro, J.6
  • 37
    • 55549107180 scopus 로고    scopus 로고
    • Atypical CRM1-dependent nuclear export signal mediates regulation of hypoxia-inducible factor-1alpha by MAPK
    • Mylonis I, Chachami G, Paraskeva E, Simos G. Atypical CRM1-dependent nuclear export signal mediates regulation of hypoxia-inducible factor-1alpha by MAPK. J Biol Chem 2008; 283: 27620-27627
    • (2008) J Biol Chem , vol.283 , pp. 27620-27627
    • Mylonis, I.1    Chachami, G.2    Paraskeva, E.3    Simos, G.4
  • 38
    • 0034282553 scopus 로고    scopus 로고
    • The Kaposi's sarcoma-associated herpes virus G protein-coupled receptor up-regulates vascular endothelial growth factor expression and secretion through mitogen-activated protein kinase and p38 pathways acting on hypoxia-inducible factor 1α
    • Sodhi A, Montaner S, Patel V, Zohar M, Bais C, Mesri EA, et al. The Kaposi's sarcoma-associated herpes virus G protein-coupled receptor up-regulates vascular endothelial growth factor expression and secretion through mitogen-activated protein kinase and p38 pathways acting on hypoxia-inducible factor 1alpha. Cancer Res 2000; 60: 4873-4880 (Pubitemid 30701503)
    • (2000) Cancer Research , vol.60 , Issue.17 , pp. 4873-4880
    • Sodhi, A.1    Montaner, S.2    Patel, V.3    Zohar, M.4    Bais, C.5    Mesri, E.A.6    Gutkind, J.S.7
  • 39
    • 0035037527 scopus 로고    scopus 로고
    • Mitogen-activated protein kinase kinase inhibitor PD98059 blocks the trans-activation but not the stabilization or DNA binding ability of Hypoxia-inducible factor-1α
    • Hur E, Chang KY, Lee E, Lee SK, Park H. Mitogen-activated protein kinase kinase inhibitor PD98059 blocks the trans-activation but not the stabilization or DNA binding ability of hypoxia-inducible factor-1alpha. Mol Pharmacol 2001; 59: 1216-1224 (Pubitemid 32381601)
    • (2001) Molecular Pharmacology , vol.59 , Issue.5 , pp. 1216-1224
    • Hur, E.1    Chang, K.Y.2    Lee, E.3    Lee, S.-K.4    Park, H.5
  • 40
    • 0037391958 scopus 로고    scopus 로고
    • Regulation of the hypoxia-dependent plasminogen activator inhibitor I expression by MAP kinases
    • Kietzmann T, Jungermann K, Gorlach A. Regulation of the hypoxia-dependent plasminogen activator inhibitor 1 expression by MAP kinases. Thromb Haemost 2003; 89: 666-673 (Pubitemid 36456964)
    • (2003) Thrombosis and Haemostasis , vol.89 , Issue.4 , pp. 666-673
    • Kietzmann, T.1    Jungermann, K.2    Gorlach, A.3
  • 41
    • 10844278331 scopus 로고    scopus 로고
    • C-Jun NH2-terminal kinase activation contributes to hypoxia-inducible factor 1alpha-dependent P-glycoprotein expression in hypoxia
    • Comerford KM, Cummins EP, Taylor CT. c-Jun NH2-terminal kinase activation contributes to hypoxia-inducible factor 1alpha-dependent P-glycoprotein expression in hypoxia. Cancer Res 2004; 64: 9057-9061
    • (2004) Cancer Res , vol.64 , pp. 9057-9061
    • Comerford, K.M.1    Cummins, E.P.2    Taylor, C.T.3
  • 42
    • 15944397647 scopus 로고    scopus 로고
    • Cytokines and the regulation of hypoxia-inducible factor (HIF)-1α
    • DOI 10.1016/j.intimp.2004.11.009
    • Haddad JJ, Harb HL. Cytokines and the regulation of hypoxia-inducible factor (HIF)-1alpha. Int Immunopharmacol 2005; 5: 461-483 (Pubitemid 40430755)
    • (2005) International Immunopharmacology , vol.5 , Issue.3 , pp. 461-483
    • Haddad, J.J.1    Harb, H.L.2
  • 43
    • 20444480218 scopus 로고    scopus 로고
    • Transcriptional regulation of plasminogen activator inhibitor-I expression by insulin-like growth factor-I via MAP kinases and hypoxia-inducible factor-I in HepG2 cells
    • DOI 10.1160/TH04-11-0761
    • Dimova EY, Moller U, Herzig S, Fink T, Zachar V, Ebbesen P, et al. Transcriptional regulation of plasminogen activator inhibitor-1 expression by insulin-like growth factor-1 via MAP kinases and hypoxia-inducible factor-1 in HepG2 cells. Thromb Haemost 2005; 93: 1176-1184 (Pubitemid 40823525)
    • (2005) Thrombosis and Haemostasis , vol.93 , Issue.6 , pp. 1176-1184
    • Dimova, E.Y.1    Moller, U.2    Herzig, S.3    Fink, T.4    Zachar, V.5    Ebbesen, P.6    Kietzmann, T.7
  • 44
    • 33746496671 scopus 로고    scopus 로고
    • Proteasomal inhibition attenuates transcriptional activity of hypoxia-inducible factor 1 (HIF-1) via specific effect on the HIF-1α C-terminal activation domain
    • DOI 10.1128/MCB.00552-06
    • Kaluz S, Kaluzova M, Stanbridge EJ. Proteasomal inhibition attenuates transcriptional activity of hypoxia-inducible factor 1 (HIF-1) via specific effect on the HIF-1alpha C-terminal activation domain. Mol Cell Biol 2006; 26: 5895-5907 (Pubitemid 44134343)
    • (2006) Molecular and Cellular Biology , vol.26 , Issue.15 , pp. 5895-5907
    • Kaluz, S.1    Kaluzova, M.2    Stanbridge, E.J.3
  • 45
    • 0035855668 scopus 로고    scopus 로고
    • Dephosphorylated hypoxia-inducible factor 1α as a mediator of p53-dependent apoptosis during hypoxia
    • DOI 10.1038/sj.onc.1204742
    • Suzuki H, Tomida A, Tsuruo T. Dephosphorylated hypoxia-inducible factor 1 alpha as a mediator of p53-dependent apoptosis during hypoxia. Oncogene 2001; 20: 5779-5788 (Pubitemid 32937947)
    • (2001) Oncogene , vol.20 , Issue.41 , pp. 5779-5788
    • Suzuki, H.1    Tomida, A.2    Tsuruo, T.3
  • 46
    • 0031754373 scopus 로고    scopus 로고
    • Mersalyl is a novel inducer of vascular endothelial growth factor gene expression and hypoxia-inducible factor 1 activity
    • Agani F, Semenza GL. Mersalyl is a novel inducer of vascular endothelial growth factor gene expression and hypoxia-inducible factor 1 activity. Mol Pharmacol 1998; 54: 749-754 (Pubitemid 28523166)
    • (1998) Molecular Pharmacology , vol.54 , Issue.5 , pp. 749-754
    • Agani, F.1    Semenza, G.L.2
  • 47
    • 0037206312 scopus 로고    scopus 로고
    • Two transactivation domains of hypoxia-inducible factor-1α regulated by the MEK-1/p42/p44 MARK pathway
    • Lee E, Yim S, Lee SK, Park H. Two transactivation domains of hypoxia-inducible factor-1alpha regulated by the MEK-1/p42/p44 MAPK pathway. Mol Cells 2002; 14: 9-15. (Pubitemid 41582973)
    • (2002) Molecules and Cells , vol.14 , Issue.1 , pp. 9-15
    • Lee, E.1    Yim, S.2    Lee, S.-K.3    Park, H.4
  • 48
    • 0037189565 scopus 로고    scopus 로고
    • The transcriptional activation function of the HIF-like factor requires phosphorylation at a conserved threonine
    • DOI 10.1074/jbc.M201307200
    • Gradin K, Takasaki C, Fujii-Kuriyama Y, Sogawa K. The transcriptional activation function of the HIF-like factor requires phosphorylation at a conserved threonine. J Biol Chem 2002; 277: 23508-23514 (Pubitemid 34952186)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.26 , pp. 23508-23514
    • Gradin, K.1    Takasaki, C.2    Fujii-Kuriyama, Y.3    Sogawa, K.4
  • 49
    • 33845403070 scopus 로고    scopus 로고
    • Identification of MAPK phosphorylation sites and their role in the localization and activity of hypoxia-inducible factor-1alpha
    • Mylonis I, Chachami G, Samiotaki M, Panayotou G, Paraskeva E, Kalousi A, et al. Identification of MAPK phosphorylation sites and their role in the localization and activity of hypoxia-inducible factor-1alpha. J Biol Chem 2006; 281: 33095-33106
    • (2006) J Biol Chem , vol.281 , pp. 33095-33106
    • Mylonis, I.1    Chachami, G.2    Samiotaki, M.3    Panayotou, G.4    Paraskeva, E.5    Kalousi, A.6
  • 51
    • 0037064010 scopus 로고    scopus 로고
    • Insulin-like growth factor 1 induces hypoxia-inducible factor 1-mediated vascular endothelial growth factor expression, which is dependent on MAP kinase and phosphatidylinositol 3-kinase signaling in colon cancer cells
    • DOI 10.1074/jbc.M203781200
    • Fukuda R, Hirota K, Fan F, Jung YD, Ellis LM, Semenza GL. Insulin-like growth factor 1 induces hypoxia-inducible factor 1-mediated vascular endothelial growth factor expression, which is dependent on MAP kinase and phosphatidylinositol 3-kinase signaling in colon cancer cells. J Biol Chem 2002; 277: 38205-38211 (Pubitemid 35154674)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.41 , pp. 38205-38211
    • Fukuda, R.1    Hirota, K.2    Fan, F.3    Jung, Y.D.4    Ellis, L.M.5    Semenza, G.L.6
  • 52
    • 27744605175 scopus 로고    scopus 로고
    • Signal pathway of hypoxia-inducible factor-1alpha phosphorylation and its interaction with von Hippel-Lindau tumor suppressor protein during ischemia in MiaPaCa-2 pancreatic cancer cells
    • Kwon SJ, Song JJ, Lee YJ. Signal pathway of hypoxia-inducible factor-1alpha phosphorylation and its interaction with von Hippel-Lindau tumor suppressor protein during ischemia in MiaPaCa-2 pancreatic cancer cells. Clin Cancer Res 2005; 11: 7607-7613
    • (2005) Clin Cancer Res , vol.11 , pp. 7607-7613
    • Kwon, S.J.1    Song, J.J.2    Lee, Y.J.3
  • 53
    • 10844278331 scopus 로고    scopus 로고
    • C-Jun NH2-terminal kinase activation contributes to hypoxia-inducible factor 1alpha-dependent P-glycoprotein expression in hypoxia
    • Comerford KM, Cummins EP, Taylor CT. c-Jun NH2-terminal kinase activation contributes to hypoxia-inducible factor 1alpha-dependent P-glycoprotein expression in hypoxia. Cancer Res 2004; 64: 9057-9061
    • (2004) Cancer Res , vol.64 , pp. 9057-9061
    • Comerford, K.M.1    Cummins, E.P.2    Taylor, C.T.3
  • 54
    • 10844278331 scopus 로고    scopus 로고
    • C-Jun NH2-terminal kinase activation contributes to hypoxia-inducible factor 1alpha-dependent P-glycoprotein expression in hypoxia
    • Comerford KM, Cummins EP, Taylor CT. c-Jun NH2-terminal kinase activation contributes to hypoxia-inducible factor 1alpha-dependent P-glycoprotein expression in hypoxia. Cancer Res 2004; 64: 9057-9061
    • (2004) Cancer Res , vol.64 , pp. 9057-9061
    • Comerford, K.M.1    Cummins, E.P.2    Taylor, C.T.3
  • 55
    • 38149015503 scopus 로고    scopus 로고
    • PI3K/PTEN signaling in tumorigenesis and angiogenesis
    • Jiang BH, Liu LZ. PI3K/PTEN signaling in tumorigenesis and angiogenesis. Biochim Biophys Acta 2008; 1784: 150-158
    • (2008) Biochim Biophys Acta , vol.1784 , pp. 150-158
    • Jiang, B.H.1    Liu, L.Z.2
  • 56
    • 4043171462 scopus 로고    scopus 로고
    • Upstream and downstream of mTOR
    • Hay N, Sonenberg N. Upstream and downstream of mTOR. Genes Dev 2004; 18: 1926-1945
    • (2004) Genes Dev , vol.18 , pp. 1926-1945
    • Hay, N.1    Sonenberg, N.2
  • 57
    • 0037134442 scopus 로고    scopus 로고
    • Lack of evidence for the involvement of the phosphoinositide 3-kinase/Akt pathway in the activation of hypoxia-inducible factors by low oxygen tension
    • Alvarez-Tejado M, Alfranca A, Aragones J, Vara A, Landazuri MO, del Peso L. Lack of evidence for the involvement of the phosphoinositide 3-kinase/Akt pathway in the activation of hypoxia-inducible factors by low oxygen tension. J Biol Chem 2002; 277: 13508-13517
    • (2002) J Biol Chem , vol.277 , pp. 13508-13517
    • Alvarez-Tejado, M.1    Alfranca, A.2    Aragones, J.3    Vara, A.4    Landazuri, M.O.5    Del Peso, L.6
  • 58
    • 0035933726 scopus 로고    scopus 로고
    • Hypoxia induces the activation of the phosphatidylinositol 3-kinase/Akt cell survival pathway in PC12 cells. Protective role in apoptosis
    • DOI 10.1074/jbc.M011688200
    • Alvarez-Tejado M, Naranjo-Suarez S, Jimenez C, Carrera AC, Landazuri MO, del Peso L. Hypoxia induces the activation of the phosphatidylinositol 3-kinase/Akt cell survival pathway in PC12 cells: protective role in apoptosis. J Biol Chem 2001; 276: 22368-22374 (Pubitemid 37410910)
    • (2001) Journal of Biological Chemistry , vol.276 , Issue.25 , pp. 22368-22374
    • Alvarez-Tejado, M.1    Naranjo-Suarez, S.2    Jimenez, C.3    Carrera, A.C.4    Landazuri, M.O.5    Del Peso, L.6
  • 59
    • 0035107345 scopus 로고    scopus 로고
    • Hypoxia activates Akt and induces phosphorylation of GSK-3 in PC12 cells
    • Beitner-Johnson D, Rust RT, Hsieh TC, Millhorn DE. Hypoxia activates Akt and induces phosphorylation of GSK-3 in PC12 cells. Cell Signal 2001; 13: 23-27
    • (2001) Cell Signal , vol.13 , pp. 23-27
    • Beitner-Johnson, D.1    Rust, R.T.2    Hsieh, T.C.3    Millhorn, D.E.4
  • 60
    • 0035866784 scopus 로고    scopus 로고
    • Hypoxia activates a platelet-derived growth factor receptor/ phosphatidylinositol 3-kinase/Akt pathway that results in glycogen synthase kinase-3 inactivation
    • Chen EY, Mazure NM, Cooper JA, Giaccia AJ. Hypoxia activates a platelet-derived growth factor receptor/phosphatidylinositol 3-kinase/Akt pathway that results in glycogen synthase kinase-3 inactivation. Cancer Res 2001; 61: 2429-2433
    • (2001) Cancer Res , vol.61 , pp. 2429-2433
    • Chen, E.Y.1    Mazure, N.M.2    Cooper, J.A.3    Giaccia, A.J.4
  • 61
    • 0043234256 scopus 로고    scopus 로고
    • Regulation of hypoxia-inducible factor-1α protein level during hypoxic conditions by the phosphatidylinositol 3-kinase/Akt/glycogen synthase kinase 3β pathway in HepG2 cells
    • DOI 10.1074/jbc.M300763200
    • Mottet D, Dumont V, Deccache Y, Demazy C, Ninane N, Raes M, et al. Regulation of hypoxia-inducible factor-1alpha protein level during hypoxic conditions by the phosphatidylinositol 3-kinase/Akt/glycogen synthase kinase 3beta pathway in HepG2 cells. J Biol Chem 2003; 278: 31277-31285 (Pubitemid 36994645)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.33 , pp. 31277-31285
    • Mottet, D.1    Dumont, V.2    Deccache, Y.3    Demazy, C.4    Ninane, N.5    Raes, M.6    Michiels, C.7
  • 62
    • 0037177867 scopus 로고    scopus 로고
    • Phosphatidylinositol 3-kinase/Akt signaling is neither required for hypoxic stabilization of HIF-1 alpha nor sufficient for HIF-1-dependent target gene transcription
    • Arsham AM, Plas DR, Thompson CB, Simon MC. Phosphatidylinositol 3-kinase/Akt signaling is neither required for hypoxic stabilization of HIF-1 alpha nor sufficient for HIF-1-dependent target gene transcription. J Biol Chem 2002; 277: 15162-15170
    • (2002) J Biol Chem , vol.277 , pp. 15162-15170
    • Arsham, A.M.1    Plas, D.R.2    Thompson, C.B.3    Simon, M.C.4
  • 63
    • 0032484019 scopus 로고    scopus 로고
    • CREB is a regulatory target for the protein kinase Akt/PKB
    • DOI 10.1074/jbc.273.49.32377
    • Du K, Montminy M. CREB is a regulatory target for the protein kinase Akt/PKB. J Biol Chem 1998; 273: 32377-32379 (Pubitemid 28557606)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.49 , pp. 32377-32379
    • Du, K.1    Montminy, M.2
  • 67
    • 0034654174 scopus 로고    scopus 로고
    • Modulation of hypoxia-inducible factor 1α expression by the epidermal growth factor/phosphatidylinositol 3-kinase/PTEN/AKT/FRAP pathway in human prostate cancer cells: Implications for tumor angiogenesis and therapeutics
    • Zhong H, Chiles K, Feldser D, Laughner E, Hanrahan C, Georgescu MM, et al. Modulation of hypoxia-inducible factor 1 alpha expression by the epidermal growth factor/phosphatidylinositol 3-kinase/PTEN/AKT/FRAP pathway in human prostate cancer cells: Implications for tumor angiogenesis and therapeutics. CANCER RESEARCH 2000; 60: 1541-1545 (Pubitemid 30183422)
    • (2000) Cancer Research , vol.60 , Issue.6 , pp. 1541-1545
    • Zhong, H.1    Chiles, K.2    Feldser, D.3    Laughner, E.4    Hanrahan, C.5    Georgescu, M.-M.6    Simons, J.W.7    Semenza, G.L.8
  • 69
    • 0037070223 scopus 로고    scopus 로고
    • Normoxic induction of the hypoxia-inducible factor 1α by insulin and interleukin-1β involves the phosphatidylinositol 3-kinase pathway
    • DOI 10.1016/S0014-5793(02)02247-0, PII S0014579302022470
    • Stiehl DP, Jelkmann W, Wenger RH, Hellwig-Burgel T. Normoxic induction of the hypoxia-inducible factor 1alpha by insulin and interleukin-1beta involves the phosphatidylinositol 3-kinase pathway. FEBS Lett 2002; 512: 157-162 (Pubitemid 34164471)
    • (2002) FEBS Letters , vol.512 , Issue.1-3 , pp. 157-162
    • Stiehl, D.P.1    Jelkmann, W.2    Wenger, R.H.3    Hellwig-Burgel, T.4
  • 70
    • 34247607209 scopus 로고    scopus 로고
    • The MAPK pathway and HIF-1 are involved in the induction of the human PAI-1 gene expression by insulin in the human hepatoma cell line HepG2
    • DOI 10.1196/annals.1378.039, Signal Transduction Pathways, Part A: Apoptotic and Extracellular Signalling
    • Dimova EY, Kietzmann T. The MAPK pathway and HIF-1 are involved in the induction of the human PAI-1 gene expression by insulin in the human hepatoma cell line HepG2. Ann N Y Acad Sci 2006; 1090: 355-367 (Pubitemid 47092141)
    • (2006) Annals of the New York Academy of Sciences , vol.1090 , pp. 355-367
    • Dimova, E.Y.1    Kietzmann, T.2
  • 72
    • 0029881595 scopus 로고    scopus 로고
    • Assignment of the human FKBP12-rapamycin-associated protein (FRAP) gene to chromosome 1p36 by fluorescence in situ hybridization
    • DOI 10.1006/geno.1996.0206
    • Moore PA, Rosen CA, Carter KC. Assignment of the human FKBP12-rapamycin-associated protein (FRAP) gene to chromosome 1p36 by fluorescence in situ hybridization. Genomics 1996; 33: 331-332 (Pubitemid 26132137)
    • (1996) Genomics , vol.33 , Issue.2 , pp. 331-332
    • Moore, P.A.1    Rosen, C.A.2    Carter, K.C.3
  • 73
    • 33745918631 scopus 로고    scopus 로고
    • Curcumin inhibits the mammalian target of rapamycin-mediated signaling pathways in cancer cells
    • DOI 10.1002/ijc.21932
    • Beevers CS, Li F, Liu L, Huang S. Curcumin inhibits the mammalian target of rapamycin-mediated signaling pathways in cancer cells. Int J Cancer 2006; 119: 757-764 (Pubitemid 44051438)
    • (2006) International Journal of Cancer , vol.119 , Issue.4 , pp. 757-764
    • Beevers, C.S.1    Li, F.2    Liu, L.3    Huang, S.4
  • 74
    • 62749096589 scopus 로고    scopus 로고
    • Mammalian target of rapamycin complex 1: Signalling inputs, substrates and feedback mechanisms
    • Dunlop EA, Tee AR. Mammalian target of rapamycin complex 1: signalling inputs, substrates and feedback mechanisms. Cell Signal 2009; 21: 827-835
    • (2009) Cell Signal , vol.21 , pp. 827-835
    • Dunlop, E.A.1    Tee, A.R.2
  • 75
    • 11244297916 scopus 로고    scopus 로고
    • Dysregulation of the TSC-mTOR pathway in human disease
    • DOI 10.1038/ng1494
    • Inoki K, Corradetti MN, Guan KL. Dysregulation of the TSC-mTOR pathway in human disease. Nat Genet 2005; 37: 19-24. (Pubitemid 40070934)
    • (2005) Nature Genetics , vol.37 , Issue.1 , pp. 19-24
    • Inoki, K.1    Corradetti, M.N.2    Guan, K.-L.3
  • 76
    • 32044465506 scopus 로고    scopus 로고
    • TOR signaling in growth and metabolism
    • Wullschleger S, Loewith R, Hall MN. TOR signaling in growth and metabolism. Cell 2006; 124: 471-484
    • (2006) Cell , vol.124 , pp. 471-484
    • Wullschleger, S.1    Loewith, R.2    Hall, M.N.3
  • 77
    • 4644239244 scopus 로고    scopus 로고
    • Mammalian target of rapamycin inhibition
    • Dutcher JP. Mammalian target of rapamycin inhibition. Clin Cancer Res 2004; 10: 6382S-7S.
    • (2004) Clin Cancer Res , vol.10
    • Dutcher, J.P.1
  • 78
    • 0037178786 scopus 로고    scopus 로고
    • MTOR interacts with raptor to form a nutrient-sensitive complex that signals to the cell growth machinery
    • DOI 10.1016/S0092-8674(02)00808-5
    • Kim DH, Sarbassov DD, Ali SM, King JE, Latek RR, Erdjument-Bromage H, et al. mTOR interacts with raptor to form a nutrient-sensitive complex that signals to the cell growth machinery. Cell 2002; 110: 163-175 (Pubitemid 34876545)
    • (2002) Cell , vol.110 , Issue.2 , pp. 163-175
    • Kim, D.-H.1    Sarbassov, D.D.2    Ali, S.M.3    King, J.E.4    Latek, R.R.5    Erdjument-Bromage, H.6    Tempst, P.7    Sabatini, D.M.8
  • 79
    • 0037623417 scopus 로고    scopus 로고
    • GβL, a positive regulator of the rapamycin-sensitive pathway required for the nutrient-sensitive interaction between raptor and mTOR
    • DOI 10.1016/S1097-2765(03)00114-X
    • Kim DH, Sarbassov DD, Ali SM, Latek RR, Guntur KV, Erdjument-Bromage H, et al. GbetaL, a positive regulator of the rapamycin-sensitive pathway required for the nutrient-sensitive interaction between raptor and mTOR. Mol Cell 2003; 11: 895-904. (Pubitemid 36566312)
    • (2003) Molecular Cell , vol.11 , Issue.4 , pp. 895-904
    • Kim, D.-H.1    Sarbassov, D.D.2    Ali, S.M.3    Latek, R.R.4    Guntur, K.V.P.5    Erdjument-Bromage, H.6    Tempst, P.7    Sabatini, D.M.8
  • 80
    • 34547099855 scopus 로고    scopus 로고
    • PRAS40 regulates mTORC1 kinase activity by functioning as a direct inhibitor of substrate binding
    • DOI 10.1074/jbc.M702376200
    • Wang L, Harris TE, Roth RA, Lawrence JC, Jr. PRAS40 regulates mTORC1 kinase activity by functioning as a direct inhibitor of substrate binding. J Biol Chem 2007; 282: 20036-20044 (Pubitemid 47100127)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.27 , pp. 20036-20044
    • Wang, L.1    Harris, T.E.2    Roth, R.A.3    Lawrence Jr., J.C.4
  • 81
    • 3342895823 scopus 로고    scopus 로고
    • Rictor, a novel binding partner of mTOR, defines a rapamycin-insensitive and raptor-independent pathway that regulates the cytoskeleton
    • DOI 10.1016/j.cub.2004.06.054, PII S0960982204004713
    • Sarbassov DD, Ali SM, Kim DH, Guertin DA, Latek RR, Erdjument-Bromage H, et al. Rictor, a novel binding partner of mTOR, defines a rapamycin-insensitive and raptor-independent pathway that regulates the cytoskeleton. Curr Biol 2004; 14: 1296-1302 (Pubitemid 38991819)
    • (2004) Current Biology , vol.14 , Issue.14 , pp. 1296-1302
    • Dos D, S.1    Ali, S.M.2    Kim, D.-H.3    Guertin, D.A.4    Latek, R.R.5    Erdjument-Bromage, H.6    Tempst, P.7    Sabatini, D.M.8
  • 82
    • 33748471980 scopus 로고    scopus 로고
    • MSin1 Is Necessary for Akt/PKB Phosphorylation, and Its Isoforms Define Three Distinct mTORC2s
    • DOI 10.1016/j.cub.2006.08.001, PII S0960982206019749
    • Frias MA, Thoreen CC, Jaffe JD, Schroder W, Sculley T, Carr SA, et al. mSin1 is necessary for Akt/PKB phosphorylation, and its isoforms define three distinct mTORC2s. Curr Biol 2006; 16: 1865-1870 (Pubitemid 44354144)
    • (2006) Current Biology , vol.16 , Issue.18 , pp. 1865-1870
    • Frias, M.A.1    Thoreen, C.C.2    Jaffe, J.D.3    Schroder, W.4    Sculley, T.5    Carr, S.A.6    Sabatini, D.M.7
  • 83
    • 0035012605 scopus 로고    scopus 로고
    • HER2 (neu) signaling increases the rate of hypoxia-inducible factor 1α (HIF-1α) synthesis: Novel mechanism for HIF-1-mediated vascular endothelial growth factor expression
    • DOI 10.1128/MCB.21.12.3995-4004.2001
    • Laughner E, Taghavi P, Chiles K, Mahon PC, Semenza GL. HER2 (neu) signaling increases the rate of hypoxia-inducible factor 1alpha (HIF-1alpha) synthesis: novel mechanism for HIF-1-mediated vascular endothelial growth factor expression. Mol Cell Biol 2001; 21: 3995-4004. (Pubitemid 32476461)
    • (2001) Molecular and Cellular Biology , vol.21 , Issue.12 , pp. 3995-4004
    • Laughner, E.1    Taghavi, P.2    Chiles, K.3    Mahon, P.C.4    Semenza, G.L.5
  • 84
    • 60249099640 scopus 로고    scopus 로고
    • Okadaic acid promotes angiogenesis via activation of hypoxia-inducible factor-1
    • Kim YS, Ahn KH, Kim SY, Jeong JW. Okadaic acid promotes angiogenesis via activation of hypoxia-inducible factor-1. Cancer Lett 2009; 276: 102-108
    • (2009) Cancer Lett , vol.276 , pp. 102-108
    • Kim, Y.S.1    Ahn, K.H.2    Kim, S.Y.3    Jeong, J.W.4
  • 85
    • 58049216350 scopus 로고    scopus 로고
    • Differential dependence of hypoxia-inducible factors 1 alpha and 2 alpha on mTORC1 and mTORC2
    • Toschi A, Lee E, Gadir N, Ohh M, Foster DA. Differential dependence of hypoxia-inducible factors 1 alpha and 2 alpha on mTORC1 and mTORC2. J Biol Chem 2008; 283: 34495-34499
    • (2008) J Biol Chem , vol.283 , pp. 34495-34499
    • Toschi, A.1    Lee, E.2    Gadir, N.3    Ohh, M.4    Foster, D.A.5
  • 86
    • 0042031047 scopus 로고    scopus 로고
    • A novel hypoxia-inducible factor-independent hypoxic response regulating mammalian target of rapamycin and its targets
    • Arsham AM, Howell JJ, Simon MC. A novel hypoxia-inducible factor-independent hypoxic response regulating mammalian target of rapamycin and its targets. J Biol Chem 2003; 278: 29655-29660
    • (2003) J Biol Chem , vol.278 , pp. 29655-29660
    • Arsham, A.M.1    Howell, J.J.2    Simon, M.C.3
  • 88
    • 0038141979 scopus 로고    scopus 로고
    • Rheb is a direct target of the tuberous sclerosis tumour suppressor proteins
    • DOI 10.1038/ncb999
    • Zhang Y, Gao X, Saucedo LJ, Ru B, Edgar BA, Pan D. Rheb is a direct target of the tuberous sclerosis tumour suppressor proteins. Nat Cell Biol 2003; 5: 578-581 (Pubitemid 36781094)
    • (2003) Nature Cell Biology , vol.5 , Issue.6 , pp. 578-581
    • Zhang, Y.1    Gao, X.2    Saucedo, L.J.3    Ru, B.4    Edgar, B.A.5    Pan, D.6
  • 90
    • 0043127125 scopus 로고    scopus 로고
    • Rheb GTpase is a direct target of TSC2 GAP activity and regulates mTOR signaling
    • DOI 10.1101/gad.1110003
    • Inoki K, Li Y, Xu T, Guan KL. Rheb GTPase is a direct target of TSC2 GAP activity and regulates mTOR signaling. Genes Dev 2003; 17: 1829-1834 (Pubitemid 36944560)
    • (2003) Genes and Development , vol.17 , Issue.15 , pp. 1829-1834
    • Inoki, K.1    Li, Y.2    Xu, T.3    Guan, K.-L.4
  • 91
    • 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
    • DOI 10.1016/S0960-9822(03)00506-2
    • Tee AR, Manning BD, Roux PP, Cantley LC, Blenis J. 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: 1259-1268 (Pubitemid 36953298)
    • (2003) Current Biology , vol.13 , Issue.15 , pp. 1259-1268
    • Tee, A.R.1    Manning, B.D.2    Roux, P.P.3    Cantley, L.C.4    Blenis, J.5
  • 92
    • 34547134517 scopus 로고    scopus 로고
    • Hypoxia-inducible factor 1alpha is regulated by the mammalian target of rapamycin (mTOR) via an mTOR signaling motif
    • Land SC, Tee AR. Hypoxia-inducible factor 1alpha is regulated by the mammalian target of rapamycin (mTOR) via an mTOR signaling motif. J Biol Chem 2007; 282: 20534-20543
    • (2007) J Biol Chem , vol.282 , pp. 20534-20543
    • Land, S.C.1    Tee, A.R.2
  • 94
    • 0028207001 scopus 로고
    • Rapamycin selectively represses translation of the "polypyrimidine tract" mRNA family
    • Jefferies HB, Reinhard C, Kozma SC, Thomas G. Rapamycin selectively represses translation of the "polypyrimidine tract" mRNA family. Proc Natl Acad Sci USA 1994; 91: 4441-4445
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 4441-4445
    • Jefferies, H.B.1    Reinhard, C.2    Kozma, S.C.3    Thomas, G.4
  • 95
    • 54049088213 scopus 로고    scopus 로고
    • Induction of HIF-1alpha expression by intermittent hypoxia: Involvement of NADPH oxidase, Ca2+ signaling, prolyl hydroxylases, and mTOR
    • Yuan G, Nanduri J, Khan S, Semenza GL, Prabhakar NR. Induction of HIF-1alpha expression by intermittent hypoxia: involvement of NADPH oxidase, Ca2+ signaling, prolyl hydroxylases, and mTOR. J Cell Physiol 2008; 217: 674-685
    • (2008) J Cell Physiol , vol.217 , pp. 674-685
    • Yuan, G.1    Nanduri, J.2    Khan, S.3    Semenza, G.L.4    Prabhakar, N.R.5
  • 96
    • 58649097037 scopus 로고    scopus 로고
    • Mutual regulation of hypoxia-inducible factor and mammalian target of rapamycin as a function of oxygen availability
    • Knaup KX, Jozefowski K, Schmidt R, Bernhardt WM, Weidemann A, Juergensen JS, et al. Mutual regulation of hypoxia-inducible factor and mammalian target of rapamycin as a function of oxygen availability. Mol Cancer Res 2009; 7: 88-98.
    • (2009) Mol Cancer Res , vol.7 , pp. 88-98
    • Knaup, K.X.1    Jozefowski, K.2    Schmidt, R.3    Bernhardt, W.M.4    Weidemann, A.5    Juergensen, J.S.6
  • 97
    • 0036789574 scopus 로고    scopus 로고
    • Regulation of hypoxia-inducible factor 1alpha expression and function by the mammalian target of rapamycin
    • Hudson CC, Liu M, Chiang GG, Otterness DM, Loomis DC, Kaper F, et al. Regulation of hypoxia-inducible factor 1alpha expression and function by the mammalian target of rapamycin. Mol Cell Biol 2002; 22: 7004-7014
    • (2002) Mol Cell Biol , vol.22 , pp. 7004-7014
    • Hudson, C.C.1    Liu, M.2    Chiang, G.G.3    Otterness, D.M.4    Loomis, D.C.5    Kaper, F.6
  • 98
    • 58149157656 scopus 로고    scopus 로고
    • Activation of HIF-1alpha in exponentially growing cells via hypoxic stimulation is independent of the Akt/mTOR pathway
    • Dayan F, Bilton RL, Laferriere J, Trottier E, Roux D, Pouyssegur J, et al. Activation of HIF-1alpha in exponentially growing cells via hypoxic stimulation is independent of the Akt/mTOR pathway. J Cell Physiol 2009; 218: 167-174
    • (2009) J Cell Physiol , vol.218 , pp. 167-174
    • Dayan, F.1    Bilton, R.L.2    Laferriere, J.3    Trottier, E.4    Roux, D.5    Pouyssegur, J.6
  • 99
    • 0019026208 scopus 로고
    • Glycogen synthase kinase-3 from rabbit skeletal muscle. Separation from cyclic-AMP-dependent protein inase and phosphorylase kinase
    • Embi N, Rylatt DB, Cohen P. Glycogen synthase kinase-3 from rabbit skeletal muscle. Separation from cyclic-AMP-dependent protein inase and phosphorylase kinase. Eur J Biochem 1980; 107: 519-527
    • (1980) Eur J Biochem , vol.107 , pp. 519-527
    • Embi, N.1    Rylatt, D.B.2    Cohen, P.3
  • 100
    • 0035477020 scopus 로고    scopus 로고
    • GSK3 takes centre stage more than 20 years after its discovery
    • DOI 10.1042/0264-6021:3590001
    • Frame S, Cohen P. GSK3 takes centre stage more than 20 years after its discovery. Biochem J 2001; 359: 1-16. (Pubitemid 32939202)
    • (2001) Biochemical Journal , vol.359 , Issue.1 , pp. 1-16
    • Frame, S.1    Cohen, P.2
  • 101
    • 0037383322 scopus 로고    scopus 로고
    • GSK-3: Tricks of the trade for a multi-tasking kinase
    • Doble BW, Woodgett JR. GSK-3: tricks of the trade for a multi-tasking kinase. J Cell Sci 2003; 116: 1175-1186
    • (2003) J Cell Sci , vol.116 , pp. 1175-1186
    • Doble, B.W.1    Woodgett, J.R.2
  • 102
    • 0025286104 scopus 로고
    • Molecular cloning and expression of glycogen synthase kinase-3/Factor a
    • Woodgett JR. Molecular cloning and expression of glycogen synthase kinase-3/factor A. EMBO J 1990; 9: 2431-2438 (Pubitemid 20218338)
    • (1990) EMBO Journal , vol.9 , Issue.8 , pp. 2431-2438
    • Woodgett, J.R.1
  • 103
    • 0026353474 scopus 로고
    • CDNA cloning and properties of glycogen synthase kinase-3
    • Woodgett JR. cDNA cloning and properties of glycogen synthase kinase-3. Methods Enzymol 1991; 200: 564-577
    • (1991) Methods Enzymol , vol.200 , pp. 564-577
    • Woodgett, J.R.1
  • 104
    • 65649100104 scopus 로고    scopus 로고
    • Unique and overlapping functions of GSK-3 isoforms in cell differentiation and proliferation and cardiovascular development
    • Force T, Woodgett JR. Unique and overlapping functions of GSK-3 isoforms in cell differentiation and proliferation and cardiovascular development. J Biol Chem 2009; 284: 9643-9647
    • (2009) J Biol Chem , vol.284 , pp. 9643-9647
    • Force, T.1    Woodgett, J.R.2
  • 105
    • 0032486258 scopus 로고    scopus 로고
    • The activation of glycogen synthase by insulin switches from kinase inhibition to phosphatase activation during adipogenesis in 3T3-L1 cells
    • Brady MJ, Bourbonais FJ, Saltiel AR. The activation of glycogen synthase by insulin switches from kinase inhibition to phosphatase activation during adipogenesis in 3T3-L1 cells. J Biol Chem 1998; 273: 14063-14066
    • (1998) J Biol Chem , vol.273 , pp. 14063-14066
    • Brady, M.J.1    Bourbonais, F.J.2    Saltiel, A.R.3
  • 106
    • 0035846952 scopus 로고    scopus 로고
    • Regulation of glycogen synthesis by amino acids in cultured human muscle cells
    • DOI 10.1074/jbc.M004812200
    • Armstrong JL, Bonavaud SM, Toole BJ, Yeaman SJ. Regulation of glycogen synthesis by amino acids in cultured human muscle cells. J Biol Chem 2001; 276: 952-956 (Pubitemid 32096514)
    • (2001) Journal of Biological Chemistry , vol.276 , Issue.2 , pp. 952-956
    • Armstrong, J.L.1    Bonavaud, S.M.2    Toole, B.J.3    Yeaman, S.J.4
  • 107
  • 109
    • 0028176021 scopus 로고
    • Glycogen synthase kinase-3beta is a dual specificity kinase differentially regulated by tyrosine and serine/threonine phosphorylation
    • Wang QM, Fiol CJ, DePaoli-Roach AA, Roach PJ. Glycogen synthase kinase-3 beta is a dual specificity kinase differentially regulated by tyrosine and serine/threonine phosphorylation. J Biol Chem 1994; 269: 14566-14574 (Pubitemid 2087919)
    • (1994) Journal of Biological Chemistry , vol.269 , Issue.20 , pp. 14566-14574
    • Wang, Q.M.1    Fiol, C.J.2    Depaoli-Roach, A.A.3    Roach, P.J.4
  • 110
    • 1642494586 scopus 로고    scopus 로고
    • Further evidence that the tyrosine phosphorylation of glycogen synthase kinase-3 (GSK3) in mammalian cells is an autophosphorylation event
    • DOI 10.1042/BJ20031259
    • Cole A, Frame S, Cohen P. Further evidence that the tyrosine phosphorylation of glycogen synthase kinase-3 (GSK3) in mammalian cells is an autophosphorylation event. Biochem J 2004; 377: 249-255 (Pubitemid 38114452)
    • (2004) Biochemical Journal , vol.377 , Issue.1 , pp. 249-255
    • Cole, A.1    Frame, S.2    Cohen, P.3
  • 111
    • 34247583794 scopus 로고    scopus 로고
    • Glycogen synthase kinase 3 phosphorylates hypoxia-inducible factor 1α and mediates its destabilization in a VHL-independent manner
    • DOI 10.1128/MCB.00015-07
    • Flugel D, Gorlach A, Michiels C, Kietzmann T. Glycogen synthase kinase 3 phosphorylates hypoxia-inducible factor 1alpha and mediates its destabilization in a VHL-independent manner. Mol Cell Biol 2007; 27: 3253-3265 (Pubitemid 46685205)
    • (2007) Molecular and Cellular Biology , vol.27 , Issue.9 , pp. 3253-3265
    • Flugel, D.1    Gorlach, A.2    Michiels, C.3    Kietzmann, T.4
  • 112
    • 13244257028 scopus 로고    scopus 로고
    • Hypoxia activates glycogen synthase kinase-3 in mouse brain in vivo: Protection by mood stabilizers and imipramine
    • DOI 10.1016/j.biopsych.2004.10.039, PII S000632230401162X
    • Roh MS, Eom TY, Zmijewska AA, De Sarno P, Roth KA, Jope RS. Hypoxia activates glycogen synthase kinase-3 in mouse brain in vivo: protection by mood stabilizers and imipramine. Biol Psychiatry 2005; 57: 278-286 (Pubitemid 40187372)
    • (2005) Biological Psychiatry , vol.57 , Issue.3 , pp. 278-286
    • Roh, M.-S.1    Eom, T.-Y.2    Zmijewska, A.A.3    De Sarno, P.4    Roth, K.A.5    Jope, R.S.6
  • 113
    • 0035860246 scopus 로고    scopus 로고
    • MAPK and akt Act cooperatively but independently on hypoxia inducible factor-1α in rasV12 upregulation of VEGF
    • DOI 10.1006/bbrc.2001.5532
    • Sodhi A, Montaner S, Miyazaki H, Gutkind JS. MAPK and Akt act cooperatively but independently on hypoxia inducible factor-1alpha in rasV12 upregulation of VEGF. Biochem Biophys Res Commun 2001; 287: 292-300. (Pubitemid 32912498)
    • (2001) Biochemical and Biophysical Research Communications , vol.287 , Issue.1 , pp. 292-300
    • Sodhi, A.1    Montaner, S.2    Miyazaki, H.3    Gutkind, J.S.4
  • 114
    • 0030800922 scopus 로고    scopus 로고
    • Mdm2: Keeping p53 under control
    • Piette J, Neel H, Marechal V. Mdm2: keeping p53 under control. Oncogene 1997; 15: 1001-1010
    • (1997) Oncogene , vol.15 , pp. 1001-1010
    • Piette, J.1    Neel, H.2    Marechal, V.3
  • 115
    • 0037075898 scopus 로고    scopus 로고
    • Activation of the p53 tumor suppressor protein
    • DOI 10.1016/S0304-419X(02)00035-5, PII S0304419X02000355
    • Vousden KH. Activation of the p53 tumor suppressor protein. Biochim Biophys Acta 2002; 1602: 47-59. (Pubitemid 34311899)
    • (2002) Biochimica et Biophysica Acta - Reviews on Cancer , vol.1602 , Issue.1 , pp. 47-59
    • Vousden, K.H.1
  • 116
    • 60649090420 scopus 로고    scopus 로고
    • p53 and MDM2: Antagonists or partners in crime?
    • Eischen CM, Lozano G. p53 and MDM2: antagonists or partners in crime? Cancer Cell 2009; 15: 161-162
    • (2009) Cancer Cell , vol.15 , pp. 161-162
    • Eischen, C.M.1    Lozano, G.2
  • 117
    • 0033572417 scopus 로고    scopus 로고
    • Hypoxia induces p53 accumulation through MDM2 downregulation and inhibition of E6-mediated degradation
    • Alarcon R, Koumenis C, Geyer RK, Maki CG, Giaccia AJ. Hypoxia induces p53 accumulation through MDM2 downregulation and inhibition of E6-mediated degradation. Cancer Res 1999; 59: 6046-6051
    • (1999) Cancer Res , vol.59 , pp. 6046-6051
    • Alarcon, R.1    Koumenis, C.2    Geyer, R.K.3    Maki, C.G.4    Giaccia, A.J.5
  • 120
    • 0032535077 scopus 로고    scopus 로고
    • Up-regulation of hypoxia-inducible factor-1alpha is not sufficient for hypoxic/anoxic p53 induction
    • Wenger RH, Camenisch G, Desbaillets I, Chilov D, Gassmann M. Up-regulation of hypoxia-inducible factor-1alpha is not sufficient for hypoxic/anoxic p53 induction. Cancer Res 1998; 58: 5678-5680
    • (1998) Cancer Res , vol.58 , pp. 5678-5680
    • Wenger, R.H.1    Camenisch, G.2    Desbaillets, I.3    Chilov, D.4    Gassmann, M.5
  • 123
    • 0038529602 scopus 로고    scopus 로고
    • Direct interactions between HIF-1α and Mdm2 modulate p53 function
    • DOI 10.1074/jbc.C200694200
    • Chen D, Li M, Luo J, Gu W. Direct interactions between HIF-1 alpha and Mdm2 modulate p53 function. J Biol Chem 2003; 278: 13595-13598 (Pubitemid 36799889)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.16 , pp. 13595-13598
    • Chen, D.1    Li, M.2    Luo, J.3    Gu, W.4
  • 124
    • 0033954247 scopus 로고    scopus 로고
    • Regulation of tumor angiogenesis by p53-induced degradation of hypoxia-inducible factor 1alpha
    • Ravi R, Mookerjee B, Bhujwalla ZM, Sutter CH, Artemov D, Zeng Q, et al. Regulation of tumor angiogenesis by p53-induced degradation of hypoxia-inducible factor 1alpha. Genes Dev 2000; 14: 34-44.
    • (2000) Genes Dev , vol.14 , pp. 34-44
    • Ravi, R.1    Mookerjee, B.2    Bhujwalla, Z.M.3    Sutter, C.H.4    Artemov, D.5    Zeng, Q.6
  • 125
    • 12144288115 scopus 로고    scopus 로고
    • Growth Factor-Mediated Induction of HDM2 Positively Regulates Hypoxia-Inducible Factor 1α Expression
    • DOI 10.1128/MCB.24.7.2905-2914.2004
    • Bardos JI, Chau NM, Ashcroft M. Growth factor-mediated induction of HDM2 positively regulates hypoxia-inducible factor 1alpha expression. Mol Cell Biol 2004; 24: 2905-2914 (Pubitemid 38381279)
    • (2004) Molecular and Cellular Biology , vol.24 , Issue.7 , pp. 2905-2914
    • Bardos, J.I.1    Chau, N.-M.2    Ashcroft, M.3
  • 127
    • 0035949588 scopus 로고    scopus 로고
    • A phosphatidylinositol 3-kinase/Akt pathway promotes translocation of Mdm2 from the cytoplasm to the nucleus
    • Mayo LD, Donner DB. A phosphatidylinositol 3-kinase/Akt pathway promotes translocation of Mdm2 from the cytoplasm to the nucleus. Proc Natl Acad Sci USA 2001; 98: 11598-11603
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 11598-11603
    • Mayo, L.D.1    Donner, D.B.2
  • 128
    • 0035736487 scopus 로고    scopus 로고
    • HER-2/neu induces p53 ubiquitination via Akt-mediated MDM2 phosphorylation
    • DOI 10.1038/ncb1101-973
    • Zhou BP, Liao Y, Xia W, Zou Y, Spohn B, Hung MC. HER-2/neu induces p53 ubiquitination via Akt-mediated MDM2 phosphorylation. Nat Cell Biol 2001; 3: 973-982 (Pubitemid 34428742)
    • (2001) Nature Cell Biology , vol.3 , Issue.11 , pp. 973-982
    • Zhou, B.P.1    Liao, Y.2    Xia, W.3    Zou, Y.4    Spohn, B.5    Hung, M.-C.6
  • 130
    • 33745225026 scopus 로고    scopus 로고
    • AMP-activated protein kinase - Development of the energy sensor concept
    • DOI 10.1113/jphysiol.2006.108944
    • Hardie DG, Hawley SA, Scott JW. AMP-activated protein kinase - development of the energy sensor concept. J Physiol 2006; 574: 7-15. (Pubitemid 43905792)
    • (2006) Journal of Physiology , vol.574 , Issue.1 , pp. 7-15
    • Hardie, D.G.1    Hawley, S.A.2    Scott, J.W.3
  • 131
    • 50049091255 scopus 로고    scopus 로고
    • AMPK: A key regulator of energy balance in the single cell and the whole organism
    • Lond
    • Hardie DG. AMPK: a key regulator of energy balance in the single cell and the whole organism. Int J Obes (Lond) 2008; 32 : 7-12.
    • (2008) Int J Obes , vol.32 , pp. 7-12
    • Hardie, D.G.1
  • 132
    • 0141960109 scopus 로고    scopus 로고
    • AMP-activated protein kinase activity is critical for hypoxia-inducible factor-1 transcriptional activity and its target gene expression under hypoxic conditions in DU145 cells
    • Lee M, Hwang JT, Lee HJ, Jung SN, Kang I, Chi SG, et al. AMP-activated protein kinase activity is critical for hypoxia-inducible factor-1 transcriptional activity and its target gene expression under hypoxic conditions in DU145 cells. J Biol Chem 2003; 278: 39653-39661
    • (2003) J Biol Chem , vol.278 , pp. 39653-39661
    • Lee, M.1    Hwang, J.T.2    Lee, H.J.3    Jung, S.N.4    Kang, I.5    Chi, S.G.6
  • 133
    • 10344221004 scopus 로고    scopus 로고
    • AMP-activated protein kinase activity is required for vanadate-induced hypoxia-inducible factor 1α expression in DU145 cells
    • DOI 10.1093/carcin/bgh253
    • Hwang JT, Lee M, Jung SN, Lee HJ, Kang I, Kim SS, et al. AMP-activated protein kinase activity is required for vanadate-induced hypoxia-inducible factor 1alpha expression in DU145 cells. Carcinogenesis 2004; 25: 2497-2507 (Pubitemid 39625192)
    • (2004) Carcinogenesis , vol.25 , Issue.12 , pp. 2497-2507
    • Hwang, J.-T.1    Lee, M.2    Jung, S.-N.3    Lee, H.-J.4    Kang, I.5    Kim, S.-S.6    Ha, J.7
  • 134
    • 41849094797 scopus 로고    scopus 로고
    • Reactive oxygen species stabilize hypoxia-inducible factor-1 alpha protein and stimulate transcriptional activity via AMP-activated protein kinase in DU145 human prostate cancer cells
    • Jung SN, Yang WK, Kim J, Kim HS, Kim EJ, Yun H, et al. Reactive oxygen species stabilize hypoxia-inducible factor-1 alpha protein and stimulate transcriptional activity via AMP-activated protein kinase in DU145 human prostate cancer cells. Carcinogenesis 2008; 29: 713-721
    • (2008) Carcinogenesis , vol.29 , pp. 713-721
    • Jung, S.N.1    Yang, W.K.2    Kim, J.3    Kim, H.S.4    Kim, E.J.5    Yun, H.6
  • 135
    • 33745840203 scopus 로고    scopus 로고
    • 5′-AMP-activated protein kinase (AMPK) is induced by low-oxygen and glucose deprivation conditions found in solid-tumor microenvironments
    • Laderoute KR, Amin K, Calaoagan JM, Knapp M, Le T, Orduna J, et al. 5′-AMP-activated protein kinase (AMPK) is induced by low-oxygen and glucose deprivation conditions found in solid-tumor microenvironments. Mol Cell Biol 2006; 26: 5336-5347
    • (2006) Mol Cell Biol , vol.26 , pp. 5336-5347
    • Laderoute, K.R.1    Amin, K.2    Calaoagan, J.M.3    Knapp, M.4    Le, T.5    Orduna, J.6
  • 136
  • 137
    • 36549014136 scopus 로고    scopus 로고
    • Compound C inhibits hypoxic activation of HIF-1 independent of AMPK
    • Emerling BM, Viollet B, Tormos KV, Chandel NS. Compound C inhibits hypoxic activation of HIF-1 independent of AMPK. FEBS Lett 2007; 581: 5727-5731
    • (2007) FEBS Lett , vol.581 , pp. 5727-5731
    • Emerling, B.M.1    Viollet, B.2    Tormos, K.V.3    Chandel, N.S.4
  • 138
    • 0032879917 scopus 로고    scopus 로고
    • Globozoospermia in mice lacking the casein kinase ii α catalytic subunit
    • DOI 10.1038/12729
    • Xu X, Toselli PA, Russell LD, Seldin DC. Globozoospermia in mice lacking the casein kinase II alpha' catalytic subunit. Nat Genet 1999; 23: 118-121 (Pubitemid 29418801)
    • (1999) Nature Genetics , vol.23 , Issue.1 , pp. 118-121
    • Xu, X.1    Toselli, P.A.2    Russell, L.D.3    Seldin, D.C.4
  • 139
    • 0037334895 scopus 로고    scopus 로고
    • One-thousand-and-one substrates of protein kinase CK2?
    • Meggio F, Pinna LA. One-thousand-and-one substrates of protein kinase CK2? FASEB J 2003; 17: 349-368
    • (2003) FASEB J , vol.17 , pp. 349-368
    • Meggio, F.1    Pinna, L.A.2
  • 140
    • 0037269847 scopus 로고    scopus 로고
    • Protein kinase CK2: Structure, regulation and role in cellular decisions of life and death
    • Litchfield DW. Protein kinase CK2: structure, regulation and role in cellular decisions of life and death. Biochem J 2003; 369: 1-15.
    • (2003) Biochem J , vol.369 , pp. 1-15
    • Litchfield, D.W.1
  • 142
    • 27744470520 scopus 로고    scopus 로고
    • Role for casein kinase 2 in the regulation of HIF-1 activity
    • Mottet D, Ruys SP, Demazy C, Raes M, Michiels C. Role for casein kinase 2 in the regulation of HIF-1 activity. Int J Cancer 2005; 117: 764-774
    • (2005) Int J Cancer , vol.117 , pp. 764-774
    • Mottet, D.1    Ruys, S.P.2    Demazy, C.3    Raes, M.4    Michiels, C.5
  • 143
    • 33748767112 scopus 로고    scopus 로고
    • Casein kinase 2 inhibition decreases hypoxia-inducible factor-1 activity under hypoxia through elevated p53 protein level
    • Hubert A, Paris S, Piret JP, Ninane N, Raes M, Michiels C. Casein kinase 2 inhibition decreases hypoxia-inducible factor-1 activity under hypoxia through elevated p53 protein level. J Cell Sci 2006; 119: 3351-3362
    • (2006) J Cell Sci , vol.119 , pp. 3351-3362
    • Hubert, A.1    Paris, S.2    Piret, J.P.3    Ninane, N.4    Raes, M.5    Michiels, C.6
  • 144
    • 0026408833 scopus 로고
    • Regulation of the human enkephalin promoter by two isoforms of the catalytic subunit of cyclic adenosine 3′,5′-monophosphate-dependent protein kinase
    • Huggenvik JI, Collard MW, Stofko RE, Seasholtz AF, Uhler MD. Regulation of the human enkephalin promoter by two isoforms of the catalytic subunit of cyclic adenosine 3′,5′-monophosphate-dependent protein kinase. Mol Endocrinol 1991; 5: 921-930
    • (1991) Mol Endocrinol , vol.5 , pp. 921-930
    • Huggenvik, J.I.1    Collard, M.W.2    Stofko, R.E.3    Seasholtz, A.F.4    Uhler, M.D.5
  • 145
    • 0028228544 scopus 로고
    • Protein kinase a acts at multiple points to inhibit Xenopus oocyte maturation
    • Matten W, Daar I, Vande Woude GF. Protein kinase A acts at multiple points to inhibit Xenopus oocyte maturation. Mol Cell Biol 1994; 14: 4419-4426 (Pubitemid 24196790)
    • (1994) Molecular and Cellular Biology , vol.14 , Issue.7 , pp. 4419-4426
    • Matten, W.1    Daar, I.2    Vande Woude, G.F.3
  • 146
    • 34848884803 scopus 로고    scopus 로고
    • Intermittent hypoxia changes HIF-1α phosphorylation pattern in endothelial cells: Unravelling of a new PKA-dependent regulation of HIF-1α
    • DOI 10.1016/j.bbamcr.2007.06.002, PII S0167488907001486
    • Toffoli S, Feron O, Raes M, Michiels C. Intermittent hypoxia changes HIF-1alpha phosphorylation pattern in endothelial cells: unravelling of a new PKA-dependent regulation of HIF-1alpha. Biochim Biophys Acta 2007; 1773: 1558-1571 (Pubitemid 47498610)
    • (2007) Biochimica et Biophysica Acta - Molecular Cell Research , vol.1773 , Issue.10 , pp. 1558-1571
    • Toffoli, S.1    Feron, O.2    Raes, M.3    Michiels, C.4
  • 147
    • 0032104245 scopus 로고    scopus 로고
    • The extended protein kinase C superfamily
    • Mellor H, Parker PJ. The extended protein kinase C superfamily. Biochem J 1998; 332: 281-292
    • (1998) Biochem J , vol.332 , pp. 281-292
    • Mellor, H.1    Parker, P.J.2
  • 148
    • 1642556829 scopus 로고    scopus 로고
    • Protein Kinase C ζ Transactivates Hypoxia-Inducible Factor α by Promoting Its Association with p300 in Renal Cancer
    • DOI 10.1158/0008-5472.CAN-03-2706
    • Datta K, Li J, Bhattacharya R, Gasparian L, Wang E, Mukhopadhyay D. Protein kinase C zeta transactivates hypoxia-inducible factor alpha by promoting its association with p300 in renal cancer. Cancer Res 2004; 64: 456-462 (Pubitemid 38120882)
    • (2004) Cancer Research , vol.64 , Issue.2 , pp. 456-462
    • Datta, K.1    Li, J.2    Bhattacharya, R.3    Gasparian, L.4    Wang, E.5    Mukhopadhyay, D.6


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