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Volumn 67, Issue 4, 2007, Pages 1735-1743

Suppression of the hypoxia-inducible factor-1 response in cervical carcinoma xenografts by proteasome inhibitors

Author keywords

[No Author keywords available]

Indexed keywords

BENZYLOXYCARBONYLLEUCYLLEUCYLLEUCINAL; BORTEZOMIB; CARBONATE DEHYDRATASE; CARBONIC ACID; CASPASE 3; DRUG VEHICLE; HISTONE ACETYLTRANSFERASE PCAF; HYPOXIA INDUCIBLE FACTOR 1; NITROIMIDAZOLE; PROTEASOME INHIBITOR; PROTEIN P53; VASCULOTROPIN;

EID: 33847751015     PISSN: 00085472     EISSN: None     Source Type: Journal    
DOI: 10.1158/0008-5472.CAN-06-2722     Document Type: Article
Times cited : (66)

References (50)
  • 1
    • 2942756226 scopus 로고    scopus 로고
    • The ubiquitin-proteasome pathway
    • Roos-Mattjus P, Sistonen L. The ubiquitin-proteasome pathway. Ann Med 2004;36:285-95.
    • (2004) Ann Med , vol.36 , pp. 285-295
    • Roos-Mattjus, P.1    Sistonen, L.2
  • 2
    • 2342613652 scopus 로고    scopus 로고
    • The proteasome: A suitable antineoplastic target
    • Adams J. The proteasome: a suitable antineoplastic target. Nat Rev Cancer 2004;4:349-60.
    • (2004) Nat Rev Cancer , vol.4 , pp. 349-360
    • Adams, J.1
  • 3
    • 2942708234 scopus 로고    scopus 로고
    • The role of proteasome inhibitors in solid tumors
    • Park DJ, Lenz HJ. The role of proteasome inhibitors in solid tumors. Ann Med 2004;36:296-303.
    • (2004) Ann Med , vol.36 , pp. 296-303
    • Park, D.J.1    Lenz, H.J.2
  • 4
    • 22144493866 scopus 로고    scopus 로고
    • Negative and positive regulation of HIF-1: A complex network
    • Bardos JI, Ashcroft M. Negative and positive regulation of HIF-1: a complex network. Biochim Biophys Acta 2005;1755:107-20.
    • (2005) Biochim Biophys Acta , vol.1755 , pp. 107-120
    • Bardos, J.I.1    Ashcroft, M.2
  • 5
    • 4644370374 scopus 로고    scopus 로고
    • Signalling via the hypoxia-inducible factor-1α requires multiple posttranslational modifications
    • Brahimi-Horn C, Mazure N, Pouyssegur J. Signalling via the hypoxia-inducible factor-1α requires multiple posttranslational modifications. Cell Signal 2005;17:1-9.
    • (2005) Cell Signal , vol.17 , pp. 1-9
    • Brahimi-Horn, C.1    Mazure, N.2    Pouyssegur, J.3
  • 6
    • 0036710591 scopus 로고    scopus 로고
    • Signal transduction to hypoxia-inducible factor 1
    • Semenza G. Signal transduction to hypoxia-inducible factor 1. Biochem Pharmacol 2002;64:993-8.
    • (2002) Biochem Pharmacol , vol.64 , pp. 993-998
    • Semenza, G.1
  • 7
    • 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
    • Salceda S, Caro J. 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. J Biol Chem 1997;272:22642-7.
    • (1997) J Biol Chem , vol.272 , pp. 22642-22647
    • Salceda, S.1    Caro, J.2
  • 8
    • 0033525830 scopus 로고    scopus 로고
    • Regulation of the hypoxia-inducible transcription factor 1α by the ubiquitin-proteasome pathway
    • Kallio PJ, Wilson WJ, O'Brien S, Makino Y, Poellinger L. Regulation of the hypoxia-inducible transcription factor 1α by the ubiquitin-proteasome pathway. J Biol Chem 1999;274:6519-25.
    • (1999) J Biol Chem , vol.274 , pp. 6519-6525
    • Kallio, P.J.1    Wilson, W.J.2    O'Brien, S.3    Makino, Y.4    Poellinger, L.5
  • 9
    • 23044431754 scopus 로고    scopus 로고
    • A phase II trial with pharmacodynamic endpoints of the proteasome inhibitor bortezomib in patients with metastatic colorectal cancer
    • Mackay H, Hedley D, Major P, et al. A phase II trial with pharmacodynamic endpoints of the proteasome inhibitor bortezomib in patients with metastatic colorectal cancer. Clin Cancer Res 2005;11:5526-33.
    • (2005) Clin Cancer Res , vol.11 , pp. 5526-5533
    • Mackay, H.1    Hedley, D.2    Major, P.3
  • 10
    • 33645080666 scopus 로고    scopus 로고
    • Normoxic stabilization of hypoxia-inducible factor-1α by modulation of the labile iron pool in differentiating U937 macrophages: Effect of natural resistance-associated macrophage protein 1
    • Knowles HJ, Mole DR, Ratcliffe PJ, Harris AL. Normoxic stabilization of hypoxia-inducible factor-1α by modulation of the labile iron pool in differentiating U937 macrophages: effect of natural resistance-associated macrophage protein 1. Cancer Res 2006;66:2600-7.
    • (2006) Cancer Res , vol.66 , pp. 2600-2607
    • Knowles, H.J.1    Mole, D.R.2    Ratcliffe, P.J.3    Harris, A.L.4
  • 11
    • 3342955379 scopus 로고    scopus 로고
    • Novel mechanism of action for hydralazine: Induction of hypoxia-inducible factor-1α, vascular endothelial growth factor, and angiogenesis by inhibition of prolyl hydroxylases
    • Knowles HJ, Tian YM, Mole DR, Harris AL. Novel mechanism of action for hydralazine: induction of hypoxia-inducible factor-1α, vascular endothelial growth factor, and angiogenesis by inhibition of prolyl hydroxylases. Circ Res 2004;95:162-9.
    • (2004) Circ Res , vol.95 , pp. 162-169
    • Knowles, H.J.1    Tian, Y.M.2    Mole, D.R.3    Harris, A.L.4
  • 12
    • 0035887489 scopus 로고    scopus 로고
    • Hypoxia-inducible factor-1α is an intrinsic marker for hypoxia in cervical cancer xenografts
    • Vukovic V, Haugland HK, Nicklee T, Morrison AJ, Hedley DW. Hypoxia-inducible factor-1α is an intrinsic marker for hypoxia in cervical cancer xenografts. Cancer Res 2001;61:7394-8.
    • (2001) Cancer Res , vol.61 , pp. 7394-7398
    • Vukovic, V.1    Haugland, H.K.2    Nicklee, T.3    Morrison, A.J.4    Hedley, D.W.5
  • 13
    • 18844378923 scopus 로고    scopus 로고
    • Activation of hypoxia-induced transcription in normoxia
    • Hagg M, Wennstrom S. Activation of hypoxia-induced transcription in normoxia. Exp Cell Res 2005;306:180-91.
    • (2005) Exp Cell Res , vol.306 , pp. 180-191
    • Hagg, M.1    Wennstrom, S.2
  • 14
    • 2942731503 scopus 로고    scopus 로고
    • Siah2 regulates stability of prolyl-hydroxylases, controls HIF1α abundance, and modulates physiological responses to hypoxia
    • Nakayama K, Frew IJ, Hagensen M, et al. Siah2 regulates stability of prolyl-hydroxylases, controls HIF1α abundance, and modulates physiological responses to hypoxia. Cell 2004;117:941-52.
    • (2004) Cell , vol.117 , pp. 941-952
    • Nakayama, K.1    Frew, I.J.2    Hagensen, M.3
  • 15
    • 0037386143 scopus 로고    scopus 로고
    • Intracellular localisation of human HIF-1 α hydroxylases: Implications for oxygen sensing
    • Metzen E, Berchner-Pfannschmidt U, Stengel P, et al. Intracellular localisation of human HIF-1 α hydroxylases: implications for oxygen sensing. J Cell Sci 2003;116:1319-26.
    • (2003) J Cell Sci , vol.116 , pp. 1319-1326
    • Metzen, E.1    Berchner-Pfannschmidt, U.2    Stengel, P.3
  • 16
    • 0035887011 scopus 로고    scopus 로고
    • FIH-1: A novel protein that interacts with HIF-1α and VHL to mediate repression of HIF-1 transcriptional activity
    • Mahon PC, Hirota K, Semenza GL. FIH-1: a novel protein that interacts with HIF-1α and VHL to mediate repression of HIF-1 transcriptional activity. Genes Dev 2001;15:2675-86.
    • (2001) Genes Dev , vol.15 , pp. 2675-2686
    • Mahon, P.C.1    Hirota, K.2    Semenza, G.L.3
  • 17
    • 18444368709 scopus 로고    scopus 로고
    • Structural basis for the recognition of hydroxyproline in HIF-1α by pVHL
    • Hon WC, Wilson MI, Harlos K, et al. Structural basis for the recognition of hydroxyproline in HIF-1α by pVHL. Nature 2002;417:975-8.
    • (2002) Nature , vol.417 , pp. 975-978
    • Hon, W.C.1    Wilson, M.I.2    Harlos, K.3
  • 18
    • 0037035851 scopus 로고    scopus 로고
    • Structure of an HIF-1α-pVHL complex: Hydroxyproline recognition in signaling
    • Min JH, Yang H, Ivan M, Gertler F, Kaelin WG, Jr., Pavletich NP. Structure of an HIF-1α-pVHL complex: hydroxyproline recognition in signaling. Science 2002;296:1886-9.
    • (2002) Science , vol.296 , pp. 1886-1889
    • Min, J.H.1    Yang, H.2    Ivan, M.3    Gertler, F.4    Kaelin Jr., W.G.5    Pavletich, N.P.6
  • 19
    • 23444447955 scopus 로고    scopus 로고
    • Effect of desferrioxamine and metals on the hydroxylases in the oxygen sensing pathway
    • Hirsila M, Koivunen P, Xu L, Seeley T, Kivirikko KI, Myllyharju JI. Effect of desferrioxamine and metals on the hydroxylases in the oxygen sensing pathway. FASEB J 2005;19:1308-10.
    • (2005) FASEB J , vol.19 , pp. 1308-1310
    • Hirsila, M.1    Koivunen, P.2    Xu, L.3    Seeley, T.4    Kivirikko, K.I.5    Myllyharju, J.I.6
  • 21
    • 0033954247 scopus 로고    scopus 로고
    • Regulation of tumor angiogenesis by p53-induced degradation of hypoxia-inducible factor 1α
    • Ravi R, Mookerjee B, Bhujwalla ZM, et al. Regulation of tumor angiogenesis by p53-induced degradation of hypoxia-inducible factor 1α. Genes Dev 2000;14:34-44.
    • (2000) Genes Dev , vol.14 , pp. 34-44
    • Ravi, R.1    Mookerjee, B.2    Bhujwalla, Z.M.3
  • 22
    • 2642574174 scopus 로고    scopus 로고
    • p300 relieves p53-evoked transcriptional repression of hypoxia-inducible factor-1 (HIF-1)
    • Schmid T, Zhou J, Kohl R, Brune B. p300 relieves p53-evoked transcriptional repression of hypoxia-inducible factor-1 (HIF-1). Biochem J 2004;380:289-95.
    • (2004) Biochem J , vol.380 , pp. 289-295
    • Schmid, T.1    Zhou, J.2    Kohl, R.3    Brune, B.4
  • 24
    • 33645243818 scopus 로고    scopus 로고
    • Proteasome inhibitor MG132 sensitizes HPV-positive human cervical cancer cells to rhTRAIL-induced apoptosis
    • Hougardy BM, Maduro JH, van der Zee AG, et al. Proteasome inhibitor MG132 sensitizes HPV-positive human cervical cancer cells to rhTRAIL-induced apoptosis. Int J Cancer 2006;118:1892-900.
    • (2006) Int J Cancer , vol.118 , pp. 1892-1900
    • Hougardy, B.M.1    Maduro, J.H.2    van der Zee, A.G.3
  • 25
    • 0037209627 scopus 로고    scopus 로고
    • p53 and MDM2 are regulated by PI-3-kinases on multiple levels under stress induced by UV radiation and proteasome dysfunction
    • Latonen L, Kurki S, Pitkanen K, Laiho M. p53 and MDM2 are regulated by PI-3-kinases on multiple levels under stress induced by UV radiation and proteasome dysfunction. Cell Signal 2003;15:95-102.
    • (2003) Cell Signal , vol.15 , pp. 95-102
    • Latonen, L.1    Kurki, S.2    Pitkanen, K.3    Laiho, M.4
  • 26
    • 28444478320 scopus 로고    scopus 로고
    • Hypoxia down-regulates DNA double strand break repair gene expression in prostate cancer cells
    • Meng AX, Jalali F, Cuddihy A, et al. Hypoxia down-regulates DNA double strand break repair gene expression in prostate cancer cells. Radiother Oncol 2005;76:168-76.
    • (2005) Radiother Oncol , vol.76 , pp. 168-176
    • Meng, A.X.1    Jalali, F.2    Cuddihy, A.3
  • 27
    • 0142166332 scopus 로고    scopus 로고
    • Targeting HIF-1 for cancer therapy
    • Semenza G. Targeting HIF-1 for cancer therapy. Nat Rev Cancer 2003;3:721-32.
    • (2003) Nat Rev Cancer , vol.3 , pp. 721-732
    • Semenza, G.1
  • 28
    • 12344329398 scopus 로고    scopus 로고
    • When hypoxia signalling meets the ubiquitin-proteasomal pathway, new targets for cancer therapy
    • Brahimi-Horn C, Pouyssegur J. When hypoxia signalling meets the ubiquitin-proteasomal pathway, new targets for cancer therapy. Crit Rev Oncol Hematol 2005;53:115-23.
    • (2005) Crit Rev Oncol Hematol , vol.53 , pp. 115-123
    • Brahimi-Horn, C.1    Pouyssegur, J.2
  • 29
    • 0034902354 scopus 로고    scopus 로고
    • Novel proteasome inhibitor PS-341 inhibits activation of nuclear factor-κB, cell survival, tumor growth, and angiogenesis in squamous cell carcinoma
    • Sunwoo JB, Chen Z, Dong G, et al. Novel proteasome inhibitor PS-341 inhibits activation of nuclear factor-κB, cell survival, tumor growth, and angiogenesis in squamous cell carcinoma. Clin Cancer Res 2001;7:1419-28.
    • (2001) Clin Cancer Res , vol.7 , pp. 1419-1428
    • Sunwoo, J.B.1    Chen, Z.2    Dong, G.3
  • 30
    • 0012433771 scopus 로고    scopus 로고
    • Effects of the proteasome inhibitor PS-341 on apoptosis and angiogenesis in orthotopic human pancreatic tumor xenografts
    • Nawrocki ST, Bruns CJ, Harbison MT, et al. Effects of the proteasome inhibitor PS-341 on apoptosis and angiogenesis in orthotopic human pancreatic tumor xenografts. Mol Cancer Ther 2002;1:1243-53.
    • (2002) Mol Cancer Ther , vol.1 , pp. 1243-1253
    • Nawrocki, S.T.1    Bruns, C.J.2    Harbison, M.T.3
  • 31
    • 0642349188 scopus 로고    scopus 로고
    • Differential effects of the proteasome inhibitor bortezomib on apoptosis and angiogenesis in human prostate tumor xenografts
    • Williams S, Pettaway C, Song R, Papandreou C, Logothetis C, McConkey DJ. Differential effects of the proteasome inhibitor bortezomib on apoptosis and angiogenesis in human prostate tumor xenografts. Mol Cancer Ther 2003;2:835-43.
    • (2003) Mol Cancer Ther , vol.2 , pp. 835-843
    • Williams, S.1    Pettaway, C.2    Song, R.3    Papandreou, C.4    Logothetis, C.5    McConkey, D.J.6
  • 32
    • 0035834409 scopus 로고    scopus 로고
    • A conserved family of prolyl-4-hydroxylases that modify HIF
    • Bruick RK, McKnight SL. A conserved family of prolyl-4-hydroxylases that modify HIF. Science 2001;294:1337-40.
    • (2001) Science , vol.294 , pp. 1337-1340
    • Bruick, R.K.1    McKnight, S.L.2
  • 33
    • 17944375360 scopus 로고    scopus 로고
    • Epstein AC, Gleadle JM, McNeill LA, et al. C. elegans EGL-9 and mammalian homologs define a family of dioxygenases that regulate HIF by prolyl hydroxylation. Cell 2001;107:43-54.
    • Epstein AC, Gleadle JM, McNeill LA, et al. C. elegans EGL-9 and mammalian homologs define a family of dioxygenases that regulate HIF by prolyl hydroxylation. Cell 2001;107:43-54.
  • 34
    • 0043234538 scopus 로고    scopus 로고
    • Characterization of the human prolyl 4-hydroxylases that modify the hypoxia-inducible factor
    • Hirsila M, Koivunen P, Gunzler V, Kivirikko KI, Myllyharju J. Characterization of the human prolyl 4-hydroxylases that modify the hypoxia-inducible factor. J Biol Chem 2003;278:30772-80.
    • (2003) J Biol Chem , vol.278 , pp. 30772-30780
    • Hirsila, M.1    Koivunen, P.2    Gunzler, V.3    Kivirikko, K.I.4    Myllyharju, J.5
  • 35
    • 0037362890 scopus 로고    scopus 로고
    • HIF hydroxylation and the mammalian oxygen-sensing pathway
    • Safran M, Kaelin WG, Jr. HIF hydroxylation and the mammalian oxygen-sensing pathway. J Clin Invest 2003;111:779-83.
    • (2003) J Clin Invest , vol.111 , pp. 779-783
    • Safran, M.1    Kaelin Jr., W.G.2
  • 37
    • 4944223879 scopus 로고    scopus 로고
    • Determination and comparison of specific activity of the HIF-prolyl hydroxylases
    • Tuckerman JR, Zhao Y, Hewitson KS, et al. Determination and comparison of specific activity of the HIF-prolyl hydroxylases. FEBS Lett 2004;576:145-50.
    • (2004) FEBS Lett , vol.576 , pp. 145-150
    • Tuckerman, J.R.1    Zhao, Y.2    Hewitson, K.S.3
  • 38
    • 4344645563 scopus 로고    scopus 로고
    • Hypoxia-inducible factor-1 (HIF-1) promotes its degradation by induction of HIF-α-prolyl-4-hydroxylases
    • Marxsen JH, Stengel P, Doege K, et al. Hypoxia-inducible factor-1 (HIF-1) promotes its degradation by induction of HIF-α-prolyl-4-hydroxylases. Biochem J 2004;381:761-7.
    • (2004) Biochem J , vol.381 , pp. 761-767
    • Marxsen, J.H.1    Stengel, P.2    Doege, K.3
  • 39
    • 0037131271 scopus 로고    scopus 로고
    • Role of prolyl hydroxylation in oncogenically stabilized hypoxia-inducible factor-1α
    • Chan DA, Sutphin PD, Denko NC, Giaccia AJ. Role of prolyl hydroxylation in oncogenically stabilized hypoxia-inducible factor-1α. J Biol Chem 2002;277:40112-7.
    • (2002) J Biol Chem , vol.277 , pp. 40112-40117
    • Chan, D.A.1    Sutphin, P.D.2    Denko, N.C.3    Giaccia, A.J.4
  • 40
    • 4644318828 scopus 로고    scopus 로고
    • Differential function of the prolyl hydroxylases PHD1, PHD2, and PHD3 in the regulation of hypoxia-inducible factor
    • Appelhoff RJ, Tian YM, Raval RR, et al. Differential function of the prolyl hydroxylases PHD1, PHD2, and PHD3 in the regulation of hypoxia-inducible factor. J Biol Chem 2004;279:38458-65.
    • (2004) J Biol Chem , vol.279 , pp. 38458-38465
    • Appelhoff, R.J.1    Tian, Y.M.2    Raval, R.R.3
  • 41
    • 0041465022 scopus 로고    scopus 로고
    • HIF prolyl-hydroxylase 2 is the key oxygen sensor setting low steady-state levels of HIF-1α in normoxia
    • Berra E, Benizri E, Ginouves A, Volmat V, Roux D, Pouyssegur J. HIF prolyl-hydroxylase 2 is the key oxygen sensor setting low steady-state levels of HIF-1α in normoxia. EMBO J 2003;22:4082-90.
    • (2003) EMBO J , vol.22 , pp. 4082-4090
    • Berra, E.1    Benizri, E.2    Ginouves, A.3    Volmat, V.4    Roux, D.5    Pouyssegur, J.6
  • 42
    • 0141643358 scopus 로고    scopus 로고
    • Hypoxia up-regulates prolyl hydroxylase activity: A feedback mechanism that limits HIF-1 responses during reoxygenation
    • D'Angelo G, Duplan E, Boyer N, Vigne P, Frelin C. Hypoxia up-regulates prolyl hydroxylase activity: a feedback mechanism that limits HIF-1 responses during reoxygenation. J Biol Chem 2003;278:38183-7.
    • (2003) J Biol Chem , vol.278 , pp. 38183-38187
    • D'Angelo, G.1    Duplan, E.2    Boyer, N.3    Vigne, P.4    Frelin, C.5
  • 43
    • 4644237401 scopus 로고    scopus 로고
    • Regulation of HIF prolyl hydroxylases by hypoxia-inducible factors
    • Aprelikova O, Chandramouli GV, Wood M, et al. Regulation of HIF prolyl hydroxylases by hypoxia-inducible factors. J Cell Biochem 2004;92:491-501.
    • (2004) J Cell Biochem , vol.92 , pp. 491-501
    • Aprelikova, O.1    Chandramouli, G.V.2    Wood, M.3
  • 44
    • 13944276440 scopus 로고    scopus 로고
    • OS-9 interacts with hypoxia-inducible factor 1α and prolyl hydroxylases to promote oxygen-dependent degradation of HIF-1α
    • Baek JH, Mahon PC, Oh J, et al. OS-9 interacts with hypoxia-inducible factor 1α and prolyl hydroxylases to promote oxygen-dependent degradation of HIF-1α. Mol Cell 2005;17:503-12.
    • (2005) Mol Cell , vol.17 , pp. 503-512
    • Baek, J.H.1    Mahon, P.C.2    Oh, J.3
  • 45
    • 21244492413 scopus 로고    scopus 로고
    • Activation of HIF-prolyl hydroxylases by R59949, an inhibitor of the diacylglycerol kinase
    • Temes E, Martin-Puig S, Acosta-Iborra B, et al. Activation of HIF-prolyl hydroxylases by R59949, an inhibitor of the diacylglycerol kinase. J Biol Chem 2005;280:24238-44.
    • (2005) J Biol Chem , vol.280 , pp. 24238-24244
    • Temes, E.1    Martin-Puig, S.2    Acosta-Iborra, B.3
  • 46
    • 0037097861 scopus 로고    scopus 로고
    • FIH-1 is an asparaginyl hydroxylase enzyme that regulates the transcriptional activity of hypoxia-inducible factor
    • Lando D, Peet DJ, Gorman JJ, et al. FIH-1 is an asparaginyl hydroxylase enzyme that regulates the transcriptional activity of hypoxia-inducible factor. Genes Dev 2002;16:1466-71.
    • (2002) Genes Dev , vol.16 , pp. 1466-1471
    • Lando, D.1    Peet, D.J.2    Gorman, J.J.3
  • 47
    • 18744375998 scopus 로고    scopus 로고
    • Regulation and destabilization of HIF-1α by ARD1-mediated acetylation
    • Jeong JW, Bae MK, Ahn MY, et al. Regulation and destabilization of HIF-1α by ARD1-mediated acetylation. Cell 2002;111:709-20.
    • (2002) Cell , vol.111 , pp. 709-720
    • Jeong, J.W.1    Bae, M.K.2    Ahn, M.Y.3
  • 49
    • 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, et al. Molecular mechanisms of transcription activation by HLF and HIF1α in response to hypoxia: their stabilization and redox signal-induced interaction with CBP/p300. EMBO J 1999;18:1905-14.
    • (1999) EMBO J , vol.18 , pp. 1905-1914
    • Ema, M.1    Hirota, K.2    Mimura, J.3
  • 50
    • 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
    • Kaluz S, Kaluzova M, Stanbridge EJ. Proteasomal inhibition attenuates transcriptional activity of hypoxia-inducible factor 1 (HIF-1) via specific effect on the HIF-1α C-terminal activation domain. Mol Cell Biol 2006;26:5895-907.
    • (2006) Mol Cell Biol , vol.26 , pp. 5895-5907
    • Kaluz, S.1    Kaluzova, M.2    Stanbridge, E.J.3


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