메뉴 건너뛰기




Volumn 12, Issue 1, 2012, Pages 9-22

HIF1 α and HIF2 α: sibling rivalry in hypoxic tumour growth and progression

Author keywords

[No Author keywords available]

Indexed keywords

CAMPTOTHECIN; DAUNORUBICIN; DOXORUBICIN; ECHINOMYCIN; ERLOTINIB; EVEROLIMUS; GEFITINIB; HYPOXIA INDUCIBLE FACTOR 1ALPHA; HYPOXIA INDUCIBLE FACTOR 2ALPHA; IMATINIB; MAMMALIAN TARGET OF RAPAMYCIN; ONCOPROTEIN; RAPAMYCIN; RNA; TEMSIROLIMUS; TOPOTECAN; TRASTUZUMAB;

EID: 84655161946     PISSN: 1474175X     EISSN: 14741768     Source Type: Journal    
DOI: 10.1038/nrc3183     Document Type: Review
Times cited : (1435)

References (192)
  • 1
    • 0142166332 scopus 로고    scopus 로고
    • Targeting HIF-1 for cancer therapy
    • Semenza, G. L. Targeting HIF-1 for cancer therapy. Nature Rev. Cancer 3, 721-732 (2003). (Pubitemid 37328811)
    • (2003) Nature Reviews Cancer , vol.3 , Issue.10 , pp. 721-732
    • Semenza, G.L.1
  • 2
    • 57149142495 scopus 로고    scopus 로고
    • The impact of O2 availability on human cancer
    • Bertout, J. A., Patel, S. A. & Simon, M. C. The impact of O2 availability on human cancer. Nature Rev. Cancer 8, 967-975 (2008).
    • (2008) Nature Rev. Cancer , vol.8 , pp. 967-975
    • Bertout, J.A.1    Patel, S.A.2    Simon, M.C.3
  • 3
    • 40949142209 scopus 로고    scopus 로고
    • The role of hypoxia-inducible factors in tumorigenesis
    • DOI 10.1038/cdd.2008.21, PII CDD200821, The biology of Hypoxia-inducible factors
    • Rankin, E. B. & Giaccia, A. J. The role of hypoxia-inducible factors in tumorigenesis. Cell Death Differ. 15, 678-685 (2008). (Pubitemid 351405072)
    • (2008) Cell Death and Differentiation , vol.15 , Issue.4 , pp. 678-685
    • Rankin, E.B.1    Giaccia, A.J.2
  • 4
    • 43649093915 scopus 로고    scopus 로고
    • Oxygen sensing by metazoans: The central role of the HIF hydroxylase pathway
    • DOI 10.1016/j.molcel.2008.04.009, PII S109727650800292X
    • Kaelin, W. G. Jr & Ratcliffe, P. J. Oxygen sensing by metazoans: the central role of the HIF hydroxylase pathway. Mol. Cell 30, 393-402 (2008). (Pubitemid 351681994)
    • (2008) Molecular Cell , vol.30 , Issue.4 , pp. 393-402
    • Kaelin Jr., W.G.1    Ratcliffe, P.J.2
  • 5
    • 78649364332 scopus 로고    scopus 로고
    • Hypoxia-inducible factors and the response to hypoxic stress
    • Majmundar, A. J., Wong, W. J. & Simon, M. C. Hypoxia-inducible factors and the response to hypoxic stress. Mol. Cell 40, 294-309 (2010).
    • (2010) Mol. Cell , vol.40 , pp. 294-309
    • Majmundar, A.J.1    Wong, W.J.2    Simon, M.C.3
  • 6
    • 33745303045 scopus 로고    scopus 로고
    • Hypoxia signalling in cancer and approaches to enforce tumour regression
    • DOI 10.1038/nature04871, PII NATURE04871
    • Pouyssegur, J., Dayan, F. & Mazure, N. M. Hypoxia signalling in cancer and approaches to enforce tumour regression. Nature 441, 437-443 (2006). (Pubitemid 44050138)
    • (2006) Nature , vol.441 , Issue.7092 , pp. 437-443
    • Pouyssegur, J.1    Dayan, F.2    Mazure, N.M.3
  • 7
    • 0029051439 scopus 로고
    • Hypoxia-inducible factor 1 is a basic-helix-loop-helix-PAS heterodimer regulated by cellular O2 tension
    • Wang, G. L., Jiang, B.-H., Rue, E. A. & Semenza, G. L. Hypoxia-inducible factor 1 is a basic-helix-loop-helix-PAS heterodimer regulated by cellular O2 tension. Proc. Natl Acad. Sci. USA 92, 5510-5514 (1995).
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 5510-5514
    • Wang, G.L.1    Jiang, B.-H.2    Rue, E.A.3    Semenza, G.L.4
  • 8
    • 0031020884 scopus 로고    scopus 로고
    • Endothelial PAS domain protein 1 (EPAS1), a transcription factor selectively expressed in endothelial cells
    • Tian, H., McKnight, S. L. & Russell, D. W. Endothelial PAS domain protein 1 (EPAS1), a transcription factor selectively expressed in endothelial cells. Genes Dev. 11, 72-82 (1997). (Pubitemid 27043825)
    • (1997) Genes and Development , vol.11 , Issue.1 , pp. 72-82
    • Tian, H.1    McKnight, S.L.2    Russell, D.W.3
  • 9
    • 0343683375 scopus 로고    scopus 로고
    • HRF, a putative basic helix-loop-helix-PAS-domain transcription factor is closely related to hypoxia-inducible factor-lot and developmentally expressed in blood vessels
    • DOI 10.1016/S0925-4773(97)00674-6, PII S0925477397006746
    • Flamme, I. et al. HRF, a putative basic helix-loop-helix-PAS-domain transcription factor is closely related to hypoxia-inducible factor-1α and developmentally expressed in blood vessels. Mech. Dev. 63, 51-60 (1997). (Pubitemid 27214502)
    • (1997) Mechanisms of Development , vol.63 , Issue.1 , pp. 51-60
    • Flamme, I.1    Frohlich, T.2    Von Reutern, M.3    Kappel, A.4    Damert, A.5    Risau, W.6
  • 10
    • 0031000736 scopus 로고    scopus 로고
    • A novel bHLH-PAS factor with close sequence similarity to hypoxia-inducible factor 1α regulates the VEGF expression and is potentially involved in lung and vascular development
    • Ema, M. et al. A novel bHLH-PAS factor with close sequence similarity to hypoxia-inducible factor 1α regulates the VEGF expression and is potentially involved in lung and vascular development. Proc. Natl Acad. Sci. USA 94, 4273-4278 (1997).
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 4273-4278
    • Ema, M.1
  • 12
    • 0037315337 scopus 로고    scopus 로고
    • Widespread hypoxia-inducible expression of HIF-2α in distinct cell populations of different organs
    • Wiesener, M. S. et al. Widespread hypoxia-inducible expression of HIF-2α in distinct cell populations of different organs. FASEB J. 17, 271-273 (2003).
    • (2003) FASEB J. , vol.17 , pp. 271-273
    • Wiesener, M.S.1
  • 13
    • 0037031808 scopus 로고    scopus 로고
    • Inhibitory PAS domain protein (IPAS) is a hypoxia-inducible splicing variant of the hypoxia-inducible factor-3α locus
    • DOI 10.1074/jbc.C200328200
    • Makino, Y., Kanopka, A., Wilson, W. J., Tanaka, H. & Poellinger, L. Inhibitory PAS domain protein (IPAS) is a hypoxia-inducible splicing variant of the hypoxia-inducible factor-3α locus. J. Biol. Chem. 277, 32405-32408 (2002). (Pubitemid 34984738)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.36 , pp. 32405-32408
    • Makino, Y.1    Kanopka, A.2    Wilson, W.J.3    Tanaka, H.4    Poellinger, L.5
  • 14
    • 82255186546 scopus 로고    scopus 로고
    • Roles of the human hypoxia-inducible factor (HIF)-3α variants in the hypoxia response
    • Heikkila, M., Pasanen, A., Kivirikko, K. I. & Myllyharju, J. Roles of the human hypoxia-inducible factor (HIF)-3α variants in the hypoxia response. Cell. Mol. Life Sci. 68, 3885-3901 (2011).
    • (2011) Cell. Mol. Life Sci. , vol.68 , pp. 3885-3901
    • Heikkila, M.1    Pasanen, A.2    Kivirikko, K.I.3    Myllyharju, J.4
  • 15
    • 70350692093 scopus 로고    scopus 로고
    • The human HIF (hypoxia-inducible factor)-3α gene is a HIF-1 target gene and may modulate hypoxic gene induction
    • Tanaka, T., Wiesener, M., Bernhardt, W., Eckardt, K. U. & Warnecke, C. The human HIF (hypoxia-inducible factor)-3α gene is a HIF-1 target gene and may modulate hypoxic gene induction. Biochem. J. 424, 143-151 (2009).
    • (2009) Biochem. J. , vol.424 , pp. 143-151
    • Tanaka, T.1    Wiesener, M.2    Bernhardt, W.3    Eckardt, K.U.4    Warnecke, C.5
  • 17
    • 37249001223 scopus 로고    scopus 로고
    • Dominant-negative HIF-3α4 suppresses VHL-null renal cell carcinoma progression
    • Maynard, M. A. et al. Dominant-negative HIF-3α4 suppresses VHL-null renal cell carcinoma progression. Cell Cycle 6, 2810-2816 (2007). (Pubitemid 350277174)
    • (2007) Cell Cycle , vol.6 , Issue.22 , pp. 2810-2816
    • Maynard, M.A.1    Evans, A.J.2    Shi, W.3    Kim, W.Y.4    Liu, F.-F.5    Ohh, M.6
  • 18
    • 0029928689 scopus 로고    scopus 로고
    • CDNA cloning and tissue-specific expression of a novel basic helix-loop-helix/PAS factor (Arnt2) with close sequence similarity to the Aryl hydrocarbon receptor nuclear translocator (Arnt)
    • Hirose, K. et al. cDNA cloning and tissue-specific expression of a novel basic helix-loop-helix/PAS factor (Arnt2) with close sequence similarity to the Aryl hydrocarbon receptor nuclear translocator (Arnt). Mol. Cell. Biol. 16, 1706-1713 (1996).
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 1706-1713
    • Hirose, K.1
  • 19
    • 0033989154 scopus 로고    scopus 로고
    • ARNT2 acts as the dimerization partner of SIM1 for the development of the hypothalamus
    • DOI 10.1016/S0925-4773(99)00328-7, PII S0925477399003287
    • Michaud, J. L., DeRossi, C., May, N. R., Holdener, B. C. & Fan, C. ARNT2 acts as the dimerization partner of SIM1 for the development of the hypothalamus. Mech. Dev. 90, 253-261 (2000). (Pubitemid 30042930)
    • (2000) Mechanisms of Development , vol.90 , Issue.2 , pp. 253-261
    • Michaud, J.L.1    Derossi, C.2    May, N.R.3    Holdener, B.C.4    Fan, C.-M.5
  • 20
    • 0035810987 scopus 로고    scopus 로고
    • Targeted mutation of the murine arylhydrocarbon receptor nuclear translocator 2 (Arnt2) gene reveals partial redundancy with Arnt
    • DOI 10.1073/pnas.121494298
    • Keith, B., Adelman, D. M. & Simon, M. C. Targeted mutation of the murine arylhydrocarbon receptor nuclear translocator 2 (Arnt2) gene reveals partial redundancy with Arnt. Proc. Natl Acad. Sci. USA 98, 6692-6697 (2001). (Pubitemid 32538278)
    • (2001) Proceedings of the National Academy of Sciences of the United States of America , vol.98 , Issue.12 , pp. 6692-6697
    • Keith, B.1    Adelman, D.M.2    Simon, M.C.3
  • 21
    • 80054072674 scopus 로고    scopus 로고
    • SiRNA-mediated knockdown of aryl hydrocarbon receptor nuclear translocator 2 affects hypoxia-inducible factor-1 regulatory signaling and metabolism in human breast cancer cells
    • Qin, X. Y. et al. siRNA-mediated knockdown of aryl hydrocarbon receptor nuclear translocator 2 affects hypoxia-inducible factor-1 regulatory signaling and metabolism in human breast cancer cells. FEBS Lett. 585, 3310-3315 (2011).
    • (2011) FEBS Lett. , vol.585 , pp. 3310-3315
    • Qin, X.Y.1
  • 22
    • 54549113030 scopus 로고    scopus 로고
    • The von Hippel-Lindau tumour suppressor protein: O2 sensing and cancer
    • Kaelin, W. G. Jr. The von Hippel-Lindau tumour suppressor protein: O2 sensing and cancer. Nature Rev. Cancer 8, 865-873 (2008).
    • (2008) Nature Rev. Cancer , vol.8 , pp. 865-873
    • Kaelin Jr., W.G.1
  • 23
    • 0036527785 scopus 로고    scopus 로고
    • The contribution of VHL substrate binding and HIF1-α to the phenotype of VHL loss in renal cell carcinoma
    • DOI 10.1016/S1535-6108(02)00044-2
    • Maranchie, J. K. et al. The contribution of VHL substrate binding and HIF1-α to the phenotype of VHL loss in renal cell carcinoma. Cancer Cell 1, 247-255 (2002). (Pubitemid 41039149)
    • (2002) Cancer Cell , vol.1 , Issue.3 , pp. 247-255
    • Maranchie, J.K.1    Vasselli, J.R.2    Riss, J.3    Bonifacino, J.S.4    Linehan, W.M.5    Klausner, R.D.6
  • 24
    • 2342597973 scopus 로고    scopus 로고
    • Inhibition of HIF2α is sufficient to suppress pVHL-defective tumor growth
    • Kondo, K., Kim, W. Y., Lechpammer, M. & Kaelin, W. G. Jr. Inhibition of HIF2α is sufficient to suppress pVHL-defective tumor growth. PLoS Biol. 1, e83 (2003).
    • (2003) PLoS Biol. , vol.1
    • Kondo, K.1    Kim, W.Y.2    Lechpammer, M.3    Kaelin Jr., W.G.4
  • 26
    • 77955982276 scopus 로고    scopus 로고
    • HIF-2α deletion promotes Kras-driven lung tumor development
    • Mazumdar, J. et al. HIF-2α deletion promotes Kras-driven lung tumor development. Proc. Natl Acad. Sci. USA 107, 14182-14187 (2010).
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , pp. 14182-14187
    • Mazumdar, J.1
  • 27
    • 0345491599 scopus 로고    scopus 로고
    • Differential Roles of Hypoxia-Inducible Factor 1α (HIF-1α) and HIF-2α in Hypoxic Gene Regulation
    • DOI 10.1128/MCB.23.24.9361-9374.2003
    • Hu, C.J., Wang, L.Y., Chodosh, L. A., Keith, B. & Simon, M. C. Differential roles of hypoxia-inducible factor 1α (HIF-1α) and HIF-2α in hypoxic gene regulation. Mol. Biol. Cell 23, 9361-9374 (2003). (Pubitemid 37499822)
    • (2003) Molecular and Cellular Biology , vol.23 , Issue.24 , pp. 9361-9374
    • Hu, C.-J.1    Wang, L.-Y.2    Chodosh, L.A.3    Keith, B.4    Simon, M.C.5
  • 29
    • 35848938945 scopus 로고    scopus 로고
    • The N-terminal transactivation domain confers target gene specificity of hypoxia-inducible factors HIF-1α and HIF-2α
    • DOI 10.1091/mbc.E06-05-0419
    • Hu, C. J., Sataur, A., Wang, L., Chen, H. & Simon, M. C. The N-terminal transactivation domain confers target gene specificity of hypoxia-inducible factors HIF-1α and HIF-2α. Mol. Biol. Cell 18, 4528-4542 (2007). (Pubitemid 350060179)
    • (2007) Molecular Biology of the Cell , vol.18 , Issue.11 , pp. 4528-4542
    • Hu, C.-J.1    Sataur, A.2    Wang, L.3    Chen, H.4    Simon, M.C.5
  • 30
    • 34247219188 scopus 로고    scopus 로고
    • Target gene selectivity of hypoxia-inducible factor-α in renal cancer cells is conveyed by post-DNA-binding mechanisms
    • DOI 10.1038/sj.bjc.6603675, PII 6603675
    • Lau, K. W., Tian, Y. M., Raval, R. R., Ratcliffe, P. J. & Pugh, C. W. Target gene selectivity of hypoxia-inducible factor-α in renal cancer cells is conveyed by post-DNA-binding mechanisms. Br. J. Cancer 96, 1284-1292 (2007). (Pubitemid 46625064)
    • (2007) British Journal of Cancer , vol.96 , Issue.8 , pp. 1284-1292
    • Lau, K.W.1    Tian, Y.-M.2    Raval, R.R.3    Ratcliffe, P.J.4    Pugh, C.W.5
  • 31
    • 63449103705 scopus 로고    scopus 로고
    • Integrative analysis of HIF binding and transactivation reveals its role in maintaining histone methylation homeostasis
    • Xia, X. et al. Integrative analysis of HIF binding and transactivation reveals its role in maintaining histone methylation homeostasis. Proc. Natl Acad. Sci. USA 106, 4260-4265 (2009).
    • (2009) Proc. Natl Acad. Sci. USA , vol.106 , pp. 4260-4265
    • Xia, X.1
  • 32
    • 75349114759 scopus 로고    scopus 로고
    • Preferential binding of HIF-1 to transcriptionally active loci determines cell-type specific response to hypoxia
    • Xia, X. & Kung, A. L. Preferential binding of HIF-1 to transcriptionally active loci determines cell-type specific response to hypoxia. Genome Biol. 10, R113 (2009).
    • (2009) Genome Biol. , vol.10
    • Xia, X.1    Kung, A.L.2
  • 33
    • 67650531089 scopus 로고    scopus 로고
    • Genome-wide association of hypoxia-inducible factor (HIF)-1α and HIF-2α. DNA binding with expression profiling of hypoxia-inducible transcripts
    • Mole, D. R. et al. Genome-wide association of hypoxia-inducible factor (HIF)-1α and HIF-2α DNA binding with expression profiling of hypoxia-inducible transcripts. J. Biol. Chem. 284, 16767-16775 (2009).
    • (2009) J. Biol. Chem. , vol.284 , pp. 16767-16775
    • Mole, D.R.1
  • 34
    • 73549088729 scopus 로고    scopus 로고
    • Regulation of the histone demethylase JMJD1A by hypoxia-inducible factor 1α enhances hypoxic gene expression and tumor growth
    • Krieg, A. J. et al. Regulation of the histone demethylase JMJD1A by hypoxia-inducible factor 1α enhances hypoxic gene expression and tumor growth. Mol. Cell. Biol. 30, 344-353 (2010).
    • (2010) Mol. Cell. Biol. , vol.30 , pp. 344-353
    • Krieg, A.J.1
  • 35
    • 79959450883 scopus 로고    scopus 로고
    • High-resolution genome-wide mapping of HIF-binding sites by ChIP-seq
    • Schodel, J. et al. High-resolution genome-wide mapping of HIF-binding sites by ChIP-seq. Blood 117, e207-e217 (2011).
    • (2011) Blood , vol.117
    • Schodel, J.1
  • 37
    • 0032100732 scopus 로고    scopus 로고
    • HIF-1α is required for solid tumor formation and embryonic vascularization
    • DOI 10.1093/emboj/17.11.3005
    • Ryan, H. E., Lo, J. & Johnson, R. S. HIF-1α is required for solid tumor formation and embryonic vascularization. EMBO J. 17, 3005-3015 (1998). (Pubitemid 28254373)
    • (1998) EMBO Journal , vol.17 , Issue.11 , pp. 3005-3015
    • Ryan, H.E.1    Lo, J.2    Johnson, R.S.3
  • 38
    • 0032213236 scopus 로고    scopus 로고
    • The hypoxia-responsive transcription factor EPAS1 is essential for catecholamine homeostasis and protection against heart failure during embryonic development
    • Tian, H., Hammer, R. E., Matsumoto, A. M., Russell, D. W. & McKnight, S. L. The hypoxia-responsive transcription factor EPAS1 is essential for catecholamine homeostasis and protection against heart failure during embryonic development. Genes Dev. 12, 3320-3324 (1998). (Pubitemid 28520979)
    • (1998) Genes and Development , vol.12 , Issue.21 , pp. 3320-3324
    • Tian, H.1    Hammer, R.E.2    Matsumoto, A.M.3    Russell, D.W.4    McKnight, S.L.5
  • 43
    • 33846652552 scopus 로고    scopus 로고
    • Hypoxia-inducible factor-1α is a key regulator of metastasis in a transgenic model of cancer initiation and progression
    • DOI 10.1158/0008-5472.CAN-06-2701
    • Liao, D., Corle, C., Seagroves, T. N. & Johnson, R. S. Hypoxia-inducible factor-1α is a key regulator of metastasis in a transgenic model of cancer initiation and progression. Cancer Res. 67, 563-572 (2007). (Pubitemid 46192193)
    • (2007) Cancer Research , vol.67 , Issue.2 , pp. 563-572
    • Liao, D.1    Corle, C.2    Seagroves, T.N.3    Johnson, R.S.4
  • 45
    • 68849102685 scopus 로고    scopus 로고
    • HIF2α cooperates with RAS to promote lung tumorigenesis in mice
    • Kim, W. Y. et al. HIF2α cooperates with RAS to promote lung tumorigenesis in mice. J. Clin. Invest. 119, 2160-2170 (2009).
    • (2009) J. Clin. Invest. , vol.119 , pp. 2160-2170
    • Kim, W.Y.1
  • 46
    • 51649090078 scopus 로고    scopus 로고
    • Hypoxia-inducible factor-2 regulates vascular tumorigenesis in mice
    • Rankin, E. B. et al. Hypoxia-inducible factor-2 regulates vascular tumorigenesis in mice. Oncogene 27, 5354-5358 (2008).
    • (2008) Oncogene , vol.27 , pp. 5354-5358
    • Rankin, E.B.1
  • 47
    • 68249140395 scopus 로고    scopus 로고
    • Hypoxia-inducible factors 1 and 2 are important transcriptional effectors in primary macrophages experiencing hypoxia
    • Fang, H. Y. et al. Hypoxia-inducible factors 1 and 2 are important transcriptional effectors in primary macrophages experiencing hypoxia. Blood 114, 844-859 (2009).
    • (2009) Blood , vol.114 , pp. 844-859
    • Fang, H.Y.1
  • 48
    • 77957350018 scopus 로고    scopus 로고
    • Macrophage expression of hypoxia-inducible factor-1α suppresses T-cell function and promotes tumor progression
    • Doedens, A. L. et al. Macrophage expression of hypoxia-inducible factor-1α suppresses T-cell function and promotes tumor progression. Cancer Res. 70, 7465-7475 (2010).
    • (2010) Cancer Res. , vol.70 , pp. 7465-7475
    • Doedens, A.L.1
  • 49
    • 77649177217 scopus 로고    scopus 로고
    • Differential activation and antagonistic function of HIF-α isoforms in macrophages are essential for NO homeostasis
    • Takeda, N. et al. Differential activation and antagonistic function of HIF-α isoforms in macrophages are essential for NO homeostasis. Genes Dev. 24, 491-501 (2010).
    • (2010) Genes Dev. , vol.24 , pp. 491-501
    • Takeda, N.1
  • 50
    • 77955295091 scopus 로고    scopus 로고
    • Hypoxia-inducible factor 2α regulates macrophage function in mouse models of acute and tumor inflammation
    • Imtiyaz, H. Z. et al. Hypoxia-inducible factor 2α regulates macrophage function in mouse models of acute and tumor inflammation. J. Clin. Invest. 120, 2699-2714 (2010).
    • (2010) J. Clin. Invest. , vol.120 , pp. 2699-2714
    • Imtiyaz, H.Z.1
  • 51
    • 7944224442 scopus 로고    scopus 로고
    • Loss of HIF-1α in endothelial cells disrupts a hypoxia-driven VEGF autocrine loop necessary for tumorigenesis
    • DOI 10.1016/j.ccr.2004.09.026, PII S1535610804003022
    • Tang, N. et al. Loss of HIF-1α in endothelial cells disrupts a hypoxia-driven VEGF autocrine loop necessary for tumorigenesis. Cancer Cell 6, 485-495 (2004). (Pubitemid 39469984)
    • (2004) Cancer Cell , vol.6 , Issue.5 , pp. 485-495
    • Tang, N.1    Wang, L.2    Esko, J.3    Giordano, F.J.4    Huang, Y.5    Gerber, H.-P.6    Ferrara, N.7    Johnson, R.S.8
  • 52
    • 49649115935 scopus 로고    scopus 로고
    • Hypoxia-inducible transcription factor-2α in endothelial cells regulates tumor neovascularization through activation of ephrin A1
    • Yamashita, T. et al. Hypoxia-inducible transcription factor-2α in endothelial cells regulates tumor neovascularization through activation of ephrin A1. J. Biol. Chem. 283, 18926-18936 (2008).
    • (2008) J. Biol. Chem. , vol.283 , pp. 18926-18936
    • Yamashita, T.1
  • 53
    • 67651098992 scopus 로고    scopus 로고
    • Endothelial deletion of hypoxia-inducible factor-2α (HIF-2α) alters vascular function and tumor angiogenesis
    • Skuli, N. et al. Endothelial deletion of hypoxia-inducible factor-2α (HIF-2α) alters vascular function and tumor angiogenesis. Blood 114, 469-477 (2009).
    • (2009) Blood , vol.114 , pp. 469-477
    • Skuli, N.1
  • 54
    • 37049002653 scopus 로고    scopus 로고
    • Hypoxia up-regulates hypoxia-inducible factor-1αtranscription by involving phosphatidylinositol 3-kinase and nuclear factor κb in pulmonary artery smooth muscle cells
    • Belaiba, R. S. et al. Hypoxia up-regulates hypoxia-inducible factor-1αtranscription by involving phosphatidylinositol 3-kinase and nuclear factor κB in pulmonary artery smooth muscle cells. Mol. Biol. Cell 18, 4691-4697 (2007).
    • (2007) Mol. Biol. Cell , vol.18 , pp. 4691-4697
    • Belaiba, R.S.1
  • 55
    • 33745003285 scopus 로고    scopus 로고
    • Bacterial lipopolysaccharide induces HIF-1 activation in human monocytes via p44/42 MAPK and NF-κB
    • DOI 10.1042/BJ20051839
    • Frede, S., Stockmann, C., Freitag, P. & Fandrey, J. Bacterial lipopolysaccharide induces HIF-1 activation in human monocytes via p44/42 MAPK and NF-κB. Biochem. J. 396, 517-527 (2006). (Pubitemid 44228166)
    • (2006) Biochemical Journal , vol.396 , Issue.3 , pp. 517-527
    • Frede, S.1    Stockmann, C.2    Freitag, P.3    Fandrey, J.4
  • 56
    • 70249099576 scopus 로고    scopus 로고
    • Interdependence of hypoxic and innate immune responses
    • Nizet, V. & Johnson, R. S. Interdependence of hypoxic and innate immune responses. Nature Rev. Immunol. 9, 609-617 (2009).
    • (2009) Nature Rev. Immunol. , vol.9 , pp. 609-617
    • Nizet, V.1    Johnson, R.S.2
  • 58
    • 63249087504 scopus 로고    scopus 로고
    • SWI/SNF regulates the cellular response to hypoxia
    • Kenneth, N. S., Mudie, S., van Uden, P. & Rocha, S. SWI/SNF regulates the cellular response to hypoxia. J. Biol. Chem. 284, 4123-4131 (2009).
    • (2009) J. Biol. Chem. , vol.284 , pp. 4123-4131
    • Kenneth, N.S.1    Mudie, S.2    Van Uden, P.3    Rocha, S.4
  • 59
    • 58049216350 scopus 로고    scopus 로고
    • Differential dependence of hypoxia-inducible factors 1α and 2α on mTORC1 and mTORC2
    • Toschi, A., Lee, E., Gadir, N., Ohh, M. & Foster, D. A. Differential dependence of hypoxia-inducible factors 1α and 2α on mTORC1 and mTORC2. J. Biol. Chem. 283, 34495-34499 (2008).
    • (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
  • 60
    • 2442544693 scopus 로고    scopus 로고
    • Prolonged hypoxia differentially regulates hypoxia-inducible factor (HIF)-1α and HIF-2α expression in lung epithelial cells: Implication of natural antisense HIF-1α
    • Uchida, T. et al. Prolonged hypoxia differentially regulates hypoxia-inducible factor (HIF)-1α and HIF-2α expression in lung epithelial cells: implication of natural antisense HIF-1α. J. Biol. Chem. 279, 14871-14878 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 14871-14878
    • Uchida, T.1
  • 61
    • 34247628002 scopus 로고    scopus 로고
    • Iron-regulatory proteins limit hypoxia-inducible factor-2α expression in iron deficiency
    • DOI 10.1038/nsmb1222, PII NSMB1222
    • Sanchez, M., Galy, B., Muckenthaler, M. U. & Hentze, M. W. Iron-regulatory proteins limit hypoxia-inducible factor-2α expression in iron deficiency. Nature Struct. Mol. Biol. 14, 420-426 (2007). (Pubitemid 46685876)
    • (2007) Nature Structural and Molecular Biology , vol.14 , Issue.5 , pp. 420-426
    • Sanchez, M.1    Galy, B.2    Muckenthaler, M.U.3    Hentze, M.W.4
  • 62
    • 57849147670 scopus 로고    scopus 로고
    • Small-molecule inhibitors of HIF-2a translation link its 5'UTR iron-responsive element to oxygen sensing
    • Zimmer, M. et al. Small-molecule inhibitors of HIF-2a translation link its 5'UTR iron-responsive element to oxygen sensing. Mol. Cell 32, 838-848 (2008).
    • (2008) Mol. Cell , vol.32 , pp. 838-848
    • Zimmer, M.1
  • 63
    • 79751479288 scopus 로고    scopus 로고
    • The HIF pathway and erythrocytosis
    • Lee, F. S. & Percy, M. J. The HIF pathway and erythrocytosis. Annu. Rev. Pathol. 6, 165-192 (2011).
    • (2011) Annu. Rev. Pathol. , vol.6 , pp. 165-192
    • Lee, F.S.1    Percy, M.J.2
  • 64
    • 66449124596 scopus 로고    scopus 로고
    • HIF-2α, but not HIF-1α, promotes iron absorption in mice
    • Mastrogiannaki, M. et al. HIF-2α, but not HIF-1α, promotes iron absorption in mice. J. Clin. Invest. 119, 1159-1166 (2009).
    • (2009) J. Clin. Invest. , vol.119 , pp. 1159-1166
    • Mastrogiannaki, M.1
  • 67
    • 12344331744 scopus 로고    scopus 로고
    • HIF-2α expression in human fetal paraganglia and neuroblastoma: Relation to sympathetic differentiation, glucose deficiency, and hypoxia
    • DOI 10.1016/j.yexcr.2004.10.003, PII S0014482704005865
    • Nilsson, H. et al. HIF-2α expression in human fetal paraganglia and neuroblastoma: relation to sympathetic differentiation, glucose deficiency, and hypoxia. Exp. Cell Res. 303, 447-456 (2005). (Pubitemid 40126276)
    • (2005) Experimental Cell Research , vol.303 , Issue.2 , pp. 447-456
    • Nilsson, H.1    Jogi, A.2    Beckman, S.3    Harris, A.L.4    Poellinger, L.5    Pahlman, S.6
  • 69
    • 65749106405 scopus 로고    scopus 로고
    • Hypoxia-inducible factors regulate tumorigenic capacity of glioma stem cells
    • Li, Z. et al. Hypoxia-inducible factors regulate tumorigenic capacity of glioma stem cells. Cancer Cell 15, 501-513 (2009).
    • (2009) Cancer Cell , vol.15 , pp. 501-513
    • Li, Z.1
  • 70
    • 57349136768 scopus 로고    scopus 로고
    • Hypoxia-associated factor, a novel E3-ubiquitin ligase, binds and ubiquitinates hypoxia-inducible factor 1α, leading to its oxygen-independent degradation
    • Koh, M. Y., Darnay, B. G. & Powis, G. Hypoxia-associated factor, a novel E3-ubiquitin ligase, binds and ubiquitinates hypoxia-inducible factor 1α, leading to its oxygen-independent degradation. Mol. Cell. Biol. 28, 7081-7095 (2008).
    • (2008) Mol. Cell. Biol. , vol.28 , pp. 7081-7095
    • Koh, M.Y.1    Darnay, B.G.2    Powis, G.3
  • 71
    • 79957440998 scopus 로고    scopus 로고
    • The hypoxia-associated factor switches cells from HIF-1α-to HIF-2α-dependent signaling promoting stem cell characteristics, aggressive tumor growth and invasion
    • Koh, M. Y., Lemos, R. Jr, Liu, X. & Powis, G. The hypoxia-associated factor switches cells from HIF-1α-to HIF-2α-dependent signaling promoting stem cell characteristics, aggressive tumor growth and invasion. Cancer Res. 71, 4015-4027 (2011).
    • (2011) Cancer Res. , vol.71 , pp. 4015-4027
    • Koh, M.Y.1    Lemos Jr., R.2    Liu, X.3    Powis, G.4
  • 72
    • 77950473770 scopus 로고    scopus 로고
    • Hsp70 and CHIP selectively mediate ubiquitination and degradation of hypoxia-inducible factor (HIF)-1α but Not HIF-2α
    • Luo, W. et al. Hsp70 and CHIP selectively mediate ubiquitination and degradation of hypoxia-inducible factor (HIF)-1α but Not HIF-2α. J. Biol. Chem. 285, 3651-3663 (2010).
    • (2010) J. Biol. Chem. , vol.285 , pp. 3651-3663
    • Luo, W.1
  • 73
    • 77953954331 scopus 로고    scopus 로고
    • The role of HIF prolyl hydroxylases in tumour growth
    • Jokilehto, T. & Jaakkola, P. M. The role of HIF prolyl hydroxylases in tumour growth. J. Cell. Mol. Med. 14, 758-770 (2010).
    • (2010) J. Cell. Mol. Med. , vol.14 , pp. 758-770
    • Jokilehto, T.1    Jaakkola, P.M.2
  • 74
    • 77954175077 scopus 로고    scopus 로고
    • PHD2 in tumour angiogenesis
    • Chan, D. A. & Giaccia, A. J. PHD2 in tumour angiogenesis. Br. J. Cancer 103, 1-5 (2010).
    • (2010) Br. J. Cancer , vol.103 , pp. 1-5
    • Chan, D.A.1    Giaccia, A.J.2
  • 75
    • 70350389957 scopus 로고    scopus 로고
    • FIH-dependent asparaginyl hydroxylation of ankyrin repeat domain-containing proteins
    • Cockman, M. E., Webb, J. D. & Ratcliffe, P. J. FIH-dependent asparaginyl hydroxylation of ankyrin repeat domain-containing proteins. Ann. NY Acad. Sci. 1177, 9-18 (2009).
    • (2009) Ann. NY Acad. Sci. , vol.1177 , pp. 9-18
    • Cockman, M.E.1    Webb, J.D.2    Ratcliffe, P.J.3
  • 76
    • 4644318828 scopus 로고    scopus 로고
    • Differential function of the prolyl hydroxylases, PHD1, PHD2 and PHD3 in the regulation of hypoxia-inducible factor
    • Appelhoff, R. J. et al. Differential function of the prolyl hydroxylases, PHD1, PHD2 and PHD3 in the regulation of hypoxia-inducible factor. J. Biol. Chem. 279, 38458-38465 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 38458-38465
    • Appelhoff, R.J.1
  • 77
    • 33747366672 scopus 로고    scopus 로고
    • Cell-specific regulation of hypoxia-inducible factor (HIF)-1α and HIF-2α stabilization and transactivation in a graded oxygen environment
    • Bracken, C. P. et al. Cell-specific regulation of hypoxia-inducible factor (HIF)-1α and HIF-2α stabilization and transactivation in a graded oxygen environment. J. Biol. Chem. 281, 22575-22585 (2006).
    • (2006) J. Biol. Chem. , vol.281 , pp. 22575-22585
    • Bracken, C.P.1
  • 78
    • 77955284188 scopus 로고    scopus 로고
    • The asparaginyl hydroxylase factor inhibiting HIF-1α is an essential regulator of metabolism
    • Zhang, N. et al. The asparaginyl hydroxylase factor inhibiting HIF-1α is an essential regulator of metabolism. Cell Metab. 11, 364-378 (2010).
    • (2010) Cell Metab. , vol.11 , pp. 364-378
    • Zhang, N.1
  • 79
    • 0032725554 scopus 로고    scopus 로고
    • P42/p44 mitogen-activated protein kinases phosphorylate hypoxia-inducible factor 1α (HIF-1α) and enhance the transcriptional activity of HIF-1
    • Richard, D. E., Berra, E., Gothie, E., Roux., D. & Pouyssegur, J. p42/p44 mitogen-activated protein kinases phosphorylate hypoxia-inducible factor 1α (HIF-1α) and enhance the transcriptional activity of HIF-1. J. Biol. Chem. 274, 32631-32637 (1999). (Pubitemid 129535289)
    • (1999) Journal of Biological Chemistry , vol.274 , Issue.46 , pp. 32631-32637
    • Richard, D.E.1    Berra, E.2    Gothie, E.3    Roux, D.4    Pouyssegur, J.5
  • 81
    • 33750202279 scopus 로고    scopus 로고
    • The phosphorylation status of PAS-B distinguishes HIF-1α from HIF-2α in NBS1 repression
    • DOI 10.1038/sj.emboj.7601369, PII 7601369
    • To, K. K., Sedelnikova, O. A., Samons, M., Bonner, W. M. & Huang, L. E. The phosphorylation status of PAS-B distinguishes HIF-1α from HIF-2α in NBS1 repression. EMBO J. 25, 4784-4794 (2006). (Pubitemid 44607024)
    • (2006) EMBO Journal , vol.25 , Issue.20 , pp. 4784-4794
    • To, K.K.-W.1    Sedelnikova, O.A.2    Samons, M.3    Bonner, W.M.4    Huang, L.E.5
  • 83
    • 77956912534 scopus 로고    scopus 로고
    • Casein kinase 1 regulates human hypoxia-inducible factor HIF-1
    • Kalousi, A. et al. Casein kinase 1 regulates human hypoxia-inducible factor HIF-1. J. Cell Sci. 123, 2976-2986 (2010).
    • (2010) J. Cell Sci. , vol.123 , pp. 2976-2986
    • Kalousi, A.1
  • 84
    • 78649231611 scopus 로고    scopus 로고
    • MTORC1 signaling under hypoxic conditions is controlled by ATM-dependent phosphorylation of HIF-1α
    • Cam, H., Easton, J. B., High, A. & Houghton, P. J. mTORC1 signaling under hypoxic conditions is controlled by ATM-dependent phosphorylation of HIF-1α. Mol. Cell 40, 509-520 (2010).
    • (2010) Mol. Cell , vol.40 , pp. 509-520
    • Cam, H.1    Easton, J.B.2    High, A.3    Houghton, P.J.4
  • 85
    • 67949102053 scopus 로고    scopus 로고
    • Recent progress in the biology and physiology of sirtuins
    • Finkel, T., Deng, C. X. & Mostoslavsky, R. Recent progress in the biology and physiology of sirtuins. Nature 460, 587-591 (2009).
    • (2009) Nature , vol.460 , pp. 587-591
    • Finkel, T.1    Deng, C.X.2    Mostoslavsky, R.3
  • 86
    • 66749129781 scopus 로고    scopus 로고
    • Regulation of hypoxia-inducible factor 2α signaling by the stress-responsive deacetylase sirtuin 1
    • Dioum, E. M. et al. Regulation of hypoxia-inducible factor 2α signaling by the stress-responsive deacetylase sirtuin 1. Science 324, 1289-1293 (2009).
    • (2009) Science , vol.324 , pp. 1289-1293
    • Dioum, E.M.1
  • 87
    • 77955499804 scopus 로고    scopus 로고
    • Sirtuin 1 modulates cellular responses to hypoxia by deacetylating hypoxia-inducible factor 1α
    • Lim, J. H. et al. Sirtuin 1 modulates cellular responses to hypoxia by deacetylating hypoxia-inducible factor 1α. Mol. Cell 38, 864-878 (2010).
    • (2010) Mol. Cell , vol.38 , pp. 864-878
    • Lim, J.H.1
  • 88
    • 79954609893 scopus 로고    scopus 로고
    • Hypoxia increases sirtuin 1 expression in a hypoxia-inducible factor-dependent manner
    • Chen, R., Dioum, E. M., Hogg, R. T., Gerard, R. D. & Garcia, J. A. Hypoxia increases sirtuin 1 expression in a hypoxia-inducible factor-dependent manner. J. Biol. Chem. 286, 13869-13878 (2011).
    • (2011) J. Biol. Chem. , vol.286 , pp. 13869-13878
    • Chen, R.1    Dioum, E.M.2    Hogg, R.T.3    Gerard, R.D.4    Garcia, J.A.5
  • 89
    • 77955727321 scopus 로고    scopus 로고
    • AKT-ing via microRNA
    • Sayed, D. & Abdellatif, M. AKT-ing via microRNA. Cell Cycle 9, 3213-3217 (2010).
    • (2010) Cell Cycle , vol.9 , pp. 3213-3217
    • Sayed, D.1    Abdellatif, M.2
  • 90
    • 74549142287 scopus 로고    scopus 로고
    • The histone deacetylase Sirt6 regulates glucose homeostasis via Hif1α
    • Zhong, L. et al. The histone deacetylase Sirt6 regulates glucose homeostasis via Hif1α. Cell 140, 280-293 (2010).
    • (2010) Cell , vol.140 , pp. 280-293
    • Zhong, L.1
  • 91
    • 79958041601 scopus 로고    scopus 로고
    • The SirT3 divining rod points to oxidative stress
    • Bell, E. L. & Guarente, L. The SirT3 divining rod points to oxidative stress. Mol. Cell 42, 561-568 (2011).
    • (2011) Mol. Cell , vol.42 , pp. 561-568
    • Bell, E.L.1    Guarente, L.2
  • 93
    • 24144447915 scopus 로고    scopus 로고
    • Cytochrome C is required for cellular oxygen sensing and hypoxic HIF activation
    • Mansfield, K. D. et al. Cytochrome C is required for cellular oxygen sensing and hypoxic HIF activation. Cell Metab. 1, 393-399 (2005).
    • (2005) Cell Metab. , vol.1 , pp. 393-399
    • Mansfield, K.D.1
  • 95
    • 79959819034 scopus 로고    scopus 로고
    • SirT3 suppresses hypoxia inducible factor 1α and tumor growth by inhibiting mitochondrial ROS production
    • Bell, E. L., Emerling, B. M., Ricoult, S. J. & Guarente, L. SirT3 suppresses hypoxia inducible factor 1α and tumor growth by inhibiting mitochondrial ROS production. Oncogene 30, 2986-2996 (2011).
    • (2011) Oncogene , vol.30 , pp. 2986-2996
    • Bell, E.L.1    Emerling, B.M.2    Ricoult, S.J.3    Guarente, L.4
  • 96
    • 79952501323 scopus 로고    scopus 로고
    • SIRT3 opposes reprogramming of cancer cell metabolism through HIF1α destabilization
    • Finley, L. W. et al. SIRT3 opposes reprogramming of cancer cell metabolism through HIF1α destabilization. Cancer Cell 19, 416-428 (2011).
    • (2011) Cancer Cell , vol.19 , pp. 416-428
    • Finley, L.W.1
  • 97
    • 18744375998 scopus 로고    scopus 로고
    • Regulation and destabilization of HIF-1α by ARD1-mediated acetylation
    • Jeong, J. W. et al. Regulation and destabilization of HIF-1α by ARD1-mediated acetylation. Cell 111, 709-720 (2002).
    • (2002) Cell , vol.111 , pp. 709-720
    • Jeong, J.W.1
  • 98
    • 33645322383 scopus 로고    scopus 로고
    • Metastasis-associated protein 1 enhances stability of hypoxia-inducible factor-1α protein by recruiting histone deacetylase 1
    • Yoo, Y. G., Kong, G. & Lee, M. O. Metastasis-associated protein 1 enhances stability of hypoxia-inducible factor-1α protein by recruiting histone deacetylase 1. EMBO J. 25, 1231-1241 (2006).
    • (2006) EMBO J. , vol.25 , pp. 1231-1241
    • Yoo, Y.G.1    Kong, G.2    Lee, M.O.3
  • 100
    • 35548935098 scopus 로고    scopus 로고
    • SUMO-Specific protease 1 is essential for stabilization of HIF1α during hypoxia
    • DOI 10.1016/j.cell.2007.08.045, PII S0092867407011439
    • Cheng, J., Kang, X., Zhang, S. & Yeh, E. T. SUMO-specific protease 1 is essential for stabilization of HIF1α during hypoxia. Cell 131, 584-595 (2007). (Pubitemid 350007694)
    • (2007) Cell , vol.131 , Issue.3 , pp. 584-595
    • Cheng, J.1    Kang, X.2    Zhang, S.3    Yeh, E.T.H.4
  • 101
    • 77951211689 scopus 로고    scopus 로고
    • RNF4 and VHL regulate the proteasomal degradation of SUMO-conjugated Hypoxia-Inducible Factor-2α
    • van Hagen, M., Overmeer, R. M., Abolvardi, S. S. & Vertegaal, A. C. RNF4 and VHL regulate the proteasomal degradation of SUMO-conjugated Hypoxia-Inducible Factor-2α. Nucleic Acids Res. 38, 1922-1931 (2010).
    • (2010) Nucleic Acids Res. , vol.38 , pp. 1922-1931
    • Van Hagen, M.1    Overmeer, R.M.2    Abolvardi, S.S.3    Vertegaal, A.C.4
  • 102
    • 4744353220 scopus 로고    scopus 로고
    • Sumoylation increases HIF-1α stability and its transcriptional activity
    • Bae, S. H. et al. Sumoylation increases HIF-1α stability and its transcriptional activity. Biochem. Biophys. Res. Commun. 324, 394-400 (2004).
    • (2004) Biochem. Biophys. Res. Commun. , vol.324 , pp. 394-400
    • Bae, S.H.1
  • 104
    • 70349213234 scopus 로고    scopus 로고
    • SENP3 is responsible for HIF-1 transactivation under mild oxidative stress via p300 de-SUMOylation
    • Huang, C. et al. SENP3 is responsible for HIF-1 transactivation under mild oxidative stress via p300 de-SUMOylation. EMBO J. 28, 2748-2762 (2009).
    • (2009) EMBO J. , vol.28 , pp. 2748-2762
    • Huang, C.1
  • 106
    • 79953170581 scopus 로고    scopus 로고
    • Hypoxia-inducible factor α subunit stabilization by NEDD8 conjugation is reactive oxygen species-dependent
    • Ryu, J. H. et al. Hypoxia-inducible factor α subunit stabilization by NEDD8 conjugation is reactive oxygen species-dependent. J. Biol. Chem. 286, 6963-6970 (2011).
    • (2011) J. Biol. Chem. , vol.286 , pp. 6963-6970
    • Ryu, J.H.1
  • 110
    • 34047156190 scopus 로고    scopus 로고
    • HIF-2α Promotes Hypoxic Cell Proliferation by Enhancing c-Myc Transcriptional Activity
    • DOI 10.1016/j.ccr.2007.02.006, PII S1535610807000591
    • Gordan, J. D., Bertout, J. A., Hu, C. J., Diehl, J. A. & Simon, M. C. HIF-2α promotes hypoxic cell proliferation by enhancing c-myc transcriptional activity. Cancer Cell 11, 335-347 (2007). (Pubitemid 46518312)
    • (2007) Cancer Cell , vol.11 , Issue.4 , pp. 335-347
    • Gordan, J.D.1    Bertout, J.A.2    Hu, C.-J.3    Diehl, J.A.4    Simon, M.C.5
  • 111
    • 31144478127 scopus 로고    scopus 로고
    • Mxi1 is induced by hypoxia in a HIF-1-dependent manner and protects cells from c-Myc-induced apoptosis
    • Corn, P. G. et al. Mxi1 is induced by hypoxia in a HIF-1-dependent manner and protects cells from c-Myc-induced apoptosis. Cancer Biol. Ther. 4, 1285-1294 (2005).
    • (2005) Cancer Biol. Ther. , vol.4 , pp. 1285-1294
    • Corn, P.G.1
  • 112
    • 34247614521 scopus 로고    scopus 로고
    • HIF-1 inhibits mitochondrial biogenesis and cellular respiration in VHL-Deficient renal cell carcinoma by repression of C-MYC activity
    • DOI 10.1016/j.ccr.2007.04.001, PII S1535610807001158
    • Zhang, H. et al. HIF-1 inhibits mitochondrial biogenesis and cellular respiration in VHL-deficient renal cell carcinoma by repression of C-MYC activity. Cancer Cell 11, 407-420 (2007). (Pubitemid 46670080)
    • (2007) Cancer Cell , vol.11 , Issue.5 , pp. 407-420
    • Zhang, H.1    Gao, P.2    Fukuda, R.3    Kumar, G.4    Krishnamachary, B.5    Zeller, K.I.6    Dang, ChiV.7    Semenza, G.L.8
  • 113
    • 56849096837 scopus 로고    scopus 로고
    • HIF-α effects on c-Myc distinguish two subtypes of sporadic VHL-deficient clear cell renal carcinoma
    • Gordan, J. D. et al. HIF-α effects on c-Myc distinguish two subtypes of sporadic VHL-deficient clear cell renal carcinoma. Cancer Cell 14, 435-446 (2008).
    • (2008) Cancer Cell , vol.14 , pp. 435-446
    • Gordan, J.D.1
  • 114
    • 35649014840 scopus 로고    scopus 로고
    • Hypoxia-inducible factor 1 and dysregulated c-Myc cooperatively induce vascular endothelial growth factor and metabolic switches hexokinase 2 and pyruvate dehydrogenase kinase 1
    • DOI 10.1128/MCB.00440-07
    • Kim, J. W., Gao, P., Liu, Y. C., Semenza, G. L. & Dang, C. V. Hypoxia-inducible factor 1 and dysregulated c-Myc cooperatively induce vascular endothelial growth factor and metabolic switches hexokinase 2 and pyruvate dehydrogenase kinase 1. Mol. Cell. Biol. 27, 7381-7393 (2007). (Pubitemid 350033646)
    • (2007) Molecular and Cellular Biology , vol.27 , Issue.21 , pp. 7381-7393
    • Kim, J.-W.1    Gao, P.2    Liu, Y.-C.3    Semenza, G.L.4    Dang, C.V.5
  • 115
    • 78650403118 scopus 로고    scopus 로고
    • Combinatorial regulation of neuroblastoma tumor progression by N-Myc and hypoxia inducible factor HIF-1α
    • Qing, G. et al. Combinatorial regulation of neuroblastoma tumor progression by N-Myc and hypoxia inducible factor HIF-1α. Cancer Res. 70, 10351-10361 (2010).
    • (2010) Cancer Res. , vol.70 , pp. 10351-10361
    • Qing, G.1
  • 116
    • 57049177125 scopus 로고    scopus 로고
    • Kidney cancer: Now available in a new flavor
    • Kaelin, W. G. Jr. Kidney cancer: now available in a new flavor. Cancer Cell 14, 423-424 (2008).
    • (2008) Cancer Cell , vol.14 , pp. 423-424
    • Kaelin Jr., W.G.1
  • 117
    • 65349103899 scopus 로고    scopus 로고
    • Blinded by the light: The growing complexity of p53
    • Vousden, K. H. & Prives, C. Blinded by the light: the growing complexity of p53. Cell 137, 413-431 (2009).
    • (2009) Cell , vol.137 , pp. 413-431
    • Vousden, K.H.1    Prives, C.2
  • 118
    • 33646757232 scopus 로고    scopus 로고
    • The complexity of p53 stabilization and activation
    • Lavin, M. F. & Gueven, N. The complexity of p53 stabilization and activation. Cell Death Differ. 13, 941-950 (2006).
    • (2006) Cell Death Differ. , vol.13 , pp. 941-950
    • Lavin, M.F.1    Gueven, N.2
  • 119
    • 3042779529 scopus 로고    scopus 로고
    • P53 cannot be induced by hypoxia alone but responds to the hypoxic microenvironment
    • DOI 10.1038/sj.onc.1207657
    • Pan, Y., Oprysko, P. R., Asham, A. M., Koch, C. J. & Simon, M. C. p53 cannot be induced by hypoxia alone but responds to the hypoxic microenvironment. Oncogene 23, 4975-4983 (2004). (Pubitemid 38938730)
    • (2004) Oncogene , vol.23 , Issue.29 , pp. 4975-4983
    • Pan, Y.1    Oprysko, P.R.2    Asham, A.M.3    Koch, C.J.4    Simon, M.C.5
  • 120
    • 0032568150 scopus 로고    scopus 로고
    • Stabilization of wild-type p53 by hypoxia-inducible factor 1α
    • An, W. G. et al. Stabilization of wild-type p53 by hypoxia-inducible factor 1α. Nature 392, 405-408 (1998).
    • (1998) Nature , vol.392 , pp. 405-408
    • An, W.G.1
  • 121
    • 11344292626 scopus 로고    scopus 로고
    • Binding of natively unfolded HIF-1α ODD domain to p53
    • DOI 10.1016/j.molcel.2004.11.019, PII S1097276504007105
    • Sanchez-Puig, N., Veprintsev, D. B. & Fersht, A. R. Binding of natively unfolded HIF-1α ODD domain to p53. Mol. Cell 17, 11-21 (2005). (Pubitemid 40075361)
    • (2005) Molecular Cell , vol.17 , Issue.1 , pp. 11-21
    • Sanchez-Puig, N.1    Veprintsev, D.B.2    Fersht, A.R.3
  • 122
    • 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-1α and Mdm2 modulate p53 function. J. Biol. Chem. 278, 13595-13598 (2003). (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
  • 125
    • 70149106164 scopus 로고    scopus 로고
    • HIF2α inhibition promotes p53 pathway activity, tumor cell death, and radiation responses
    • Bertout, J. A. et al. HIF2α inhibition promotes p53 pathway activity, tumor cell death, and radiation responses. Proc. Natl Acad. Sci. USA 106, 14391-14396 (2009).
    • (2009) Proc. Natl Acad. Sci. USA , vol.106 , pp. 14391-14396
    • Bertout, J.A.1
  • 126
    • 71549151624 scopus 로고    scopus 로고
    • Suppression of hypoxia-inducible factor 2α restores p53 activity via Hdm2 and reverses chemoresistance of renal carcinoma cells
    • Roberts, A. M. et al. Suppression of hypoxia-inducible factor 2α restores p53 activity via Hdm2 and reverses chemoresistance of renal carcinoma cells. Cancer Res. 69, 9056-9064 (2009).
    • (2009) Cancer Res. , vol.69 , pp. 9056-9064
    • Roberts, A.M.1
  • 127
    • 78649348967 scopus 로고    scopus 로고
    • Regulation of the mTOR complex 1 pathway by nutrients, growth factors, and stress
    • Sengupta, S., Peterson, T. R. & Sabatini, D. M. Regulation of the mTOR complex 1 pathway by nutrients, growth factors, and stress. Mol. Cell 40, 310-322 (2010).
    • (2010) Mol. Cell , vol.40 , pp. 310-322
    • Sengupta, S.1    Peterson, T.R.2    Sabatini, D.M.3
  • 128
    • 72949083368 scopus 로고    scopus 로고
    • Common corruption of the mTOR signaling network in human tumors
    • Menon, S. & Manning, B. D. Common corruption of the mTOR signaling network in human tumors. Oncogene 27 (Suppl. 2), S43-S51 (2008).
    • (2008) Oncogene , vol.27 , Issue.SUPPL. 2
    • Menon, S.1    Manning, B.D.2
  • 129
    • 32444433450 scopus 로고    scopus 로고
    • Hypoxia-induced energy stress regulates mRNA translation and cell growth
    • DOI 10.1016/j.molcel.2006.01.010, PII S1097276506000116
    • Liu, L. et al. Hypoxia-induced energy stress regulates mRNA translation and cell growth. Mol. Cell 21, 521-531 (2006). (Pubitemid 43228007)
    • (2006) Molecular Cell , vol.21 , Issue.4 , pp. 521-531
    • Liu, L.1    Cash, T.P.2    Jones, R.G.3    Keith, B.4    Thompson, C.B.5    Simon, M.C.6
  • 131
    • 38349056675 scopus 로고    scopus 로고
    • Hypoxia regulates TSC1/2-mTOR signaling and tumor suppression through REDD1-mediated 14-3-3 shuttling
    • DeYoung, M. P., Horak, P., Sofer, A., Sgroi, D. & Ellisen, L. W. Hypoxia regulates TSC1/2-mTOR signaling and tumor suppression through REDD1-mediated 14-3-3 shuttling. Genes Dev. 22, 239-251 (2008).
    • (2008) Genes Dev. , vol.22 , pp. 239-251
    • Deyoung, M.P.1    Horak, P.2    Sofer, A.3    Sgroi, D.4    Ellisen, L.W.5
  • 133
    • 23744454765 scopus 로고    scopus 로고
    • Identification of FIP200 interaction with the TSC1-TSC2 complex and its role in regulation of cell size control
    • DOI 10.1083/jcb.200411106
    • Gan, B., Melkoumian, Z. K., Wu, X., Guan, K. L. & Guan, J. L. Identification of FIP200 interaction with the TSC1-TSC2 complex and its role in regulation of cell size control. J. Cell Biol. 170, 379-389 (2005). (Pubitemid 41126938)
    • (2005) Journal of Cell Biology , vol.170 , Issue.3 , pp. 379-389
    • Gan, B.1    Melkoumian, Z.K.2    Wu, X.3    Guan, K.-L.4    Guan, J.-L.5
  • 134
    • 33750592447 scopus 로고    scopus 로고
    • Neuromuscular abundance of RB1CC1 contributes to the non-proliferating enlarged cell phenotype through both RB1 maintenance and TSC1 degradation
    • Chano, T. et al. Neuromuscular abundance of RB1CC1 contributes to the non-proliferating enlarged cell phenotype through both RB1 maintenance and TSC1 degradation. Int. J. Mol. Med. 18, 425-432 (2006).
    • (2006) Int. J. Mol. Med. , vol.18 , pp. 425-432
    • Chano, T.1
  • 135
    • 75149174239 scopus 로고    scopus 로고
    • Mutation analysis of hypoxia-inducible factors HIF1A and HIF2A in renal cell carcinoma
    • Morris, M. R. et al. Mutation analysis of hypoxia-inducible factors HIF1A and HIF2A in renal cell carcinoma. Anticancer Res. 29, 4337-4343 (2009).
    • (2009) Anticancer Res. , vol.29 , pp. 4337-4343
    • Morris, M.R.1
  • 136
    • 75149188170 scopus 로고    scopus 로고
    • Systematic sequencing of renal carcinoma reveals inactivation of histone modifying genes
    • Dalgliesh, G. L. et al. Systematic sequencing of renal carcinoma reveals inactivation of histone modifying genes. Nature 463, 360-363 (2010).
    • (2010) Nature , vol.463 , pp. 360-363
    • Dalgliesh, G.L.1
  • 137
    • 66349100709 scopus 로고    scopus 로고
    • Patterns of gene expression and copy-number alterations in von-hippel lindau disease-associated and sporadic clear cell carcinoma of the kidney
    • Beroukhim, R. et al. Patterns of gene expression and copy-number alterations in von-hippel lindau disease-associated and sporadic clear cell carcinoma of the kidney. Cancer Res. 69, 4674-4681 (2009).
    • (2009) Cancer Res. , vol.69 , pp. 4674-4681
    • Beroukhim, R.1
  • 138
    • 78651257523 scopus 로고    scopus 로고
    • Genome-wide association study of renal cell carcinoma identifies two susceptibility loci on 2p21 and 11q13.3
    • Purdue, M. P. et al. Genome-wide association study of renal cell carcinoma identifies two susceptibility loci on 2p21 and 11q13.3. Nature Genet. 43, 60-65 (2010).
    • (2010) Nature Genet. , vol.43 , pp. 60-65
    • Purdue, M.P.1
  • 139
    • 76349095132 scopus 로고    scopus 로고
    • Defining the role of hypoxia-inducible factor 1 in cancer biology and therapeutics
    • Semenza, G. L. Defining the role of hypoxia-inducible factor 1 in cancer biology and therapeutics. Oncogene 29, 625-634 (2010).
    • (2010) Oncogene , vol.29 , pp. 625-634
    • Semenza, G.L.1
  • 141
    • 70449580319 scopus 로고    scopus 로고
    • Acriflavine inhibits HIF-1 dimerization, tumor growth, and vascularization
    • Lee, K. et al. Acriflavine inhibits HIF-1 dimerization, tumor growth, and vascularization. Proc. Natl Acad. Sci. USA 106, 17910-17915 (2009).
    • (2009) Proc. Natl Acad. Sci. USA , vol.106 , pp. 17910-17915
    • Lee, K.1
  • 144
    • 33644780111 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors induce VHL and ubiquitin-independent proteasomal degradation of hypoxia-inducible factor 1α
    • DOI 10.1128/MCB.26.6.2019-2028.2006
    • Kong, X. et al. Histone deacetylase inhibitors induce VHL and ubiquitin-independent proteasomal degradation of hypoxia-inducible factor 1α. Mol. Cell. Biol. 26, 2019-2028 (2006). (Pubitemid 43346906)
    • (2006) Molecular and Cellular Biology , vol.26 , Issue.6 , pp. 2019-2028
    • Kong, X.1    Lin, Z.2    Liang, D.3    Fath, D.4    Sang, N.5    Caro, J.6
  • 145
    • 33749006252 scopus 로고    scopus 로고
    • Class II histone deacetylases are associated with VHL-independent regulation of hypoxia-inducible factor 1α
    • DOI 10.1158/0008-5472.CAN-05-4598
    • Qian, D. Z. et al. Class II histone deacetylases are associated with VHL-independent regulation of hypoxia-inducible factor 1α. Cancer Res. 66, 8814-8821 (2006). (Pubitemid 44449199)
    • (2006) Cancer Research , vol.66 , Issue.17 , pp. 8814-8821
    • Qian, D.Z.1    Kachhap, S.K.2    Collis, S.J.3    Verheul, H.M.W.4    Carducci, M.A.5    Atadja, P.6    Pili, R.7
  • 146
    • 0037119415 scopus 로고    scopus 로고
    • Hsp90 regulates a von Hippel Lindau-independent hypoxia-inducible factor-1α-degradative pathway
    • Isaacs, J. S. et al. Hsp90 regulates a von Hippel Lindau-independent hypoxia-inducible factor-1α-degradative pathway. J. Biol. Chem. 277, 29936-29944 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 29936-29944
    • Isaacs, J.S.1
  • 147
    • 0036569704 scopus 로고    scopus 로고
    • Geldanamycin induces degradation of hypoxia-inducible factor 1α protein via the proteosome pathway in prostate cancer cells
    • Mabjeesh, N. J. et al. Geldanamycin induces degradation of hypoxia-inducible factor 1α protein via the proteosome pathway in prostate cancer cells. Cancer Res. 62, 2478-2482 (2002). (Pubitemid 34462721)
    • (2002) Cancer Research , vol.62 , Issue.9 , pp. 2478-2482
    • Mabjeesh, N.J.1    Post, D.E.2    Willard, M.T.3    Kaur, B.4    Van Meir, E.G.5    Simons, J.W.6    Zhong, H.7
  • 148
    • 2342611976 scopus 로고    scopus 로고
    • Radiation activates HIF-1 to regulate vascular radiosensitivity in tumors: Role of reoxygenation, free radicals, and stress granules
    • DOI 10.1016/S1535-6108(04)00115-1, PII S1535610804001151
    • Moeller, B. J., Cao, Y., Li, C. Y. & Dewhirst, M. W. Radiation activates HIF-1 to regulate vascular radiosensitivity in tumors: role of reoxygenation, free radicals, and stress granules. Cancer Cell 5, 429-441 (2004). (Pubitemid 38610245)
    • (2004) Cancer Cell , vol.5 , Issue.5 , pp. 429-441
    • Moeller, B.J.1    Cao, Y.2    Li, C.Y.3    Dewhirst, M.W.4
  • 149
    • 0037097861 scopus 로고    scopus 로고
    • FIH-1 is an asparaginyl hydroxylase enzyme that regulates the transcriptional activity of hypoxia-inducible factor
    • DOI 10.1101/gad.991402
    • Lando, D. et al. FIH-1 is an asparaginyl hydroxylase enzyme that regulates the transcriptional activity of hypoxia-inducible factor. Genes Dev. 16, 1466-1471 (2002). (Pubitemid 34686328)
    • (2002) Genes and Development , vol.16 , Issue.12 , pp. 1466-1471
    • Lando, D.1    Peet, D.J.2    Gorman, J.J.3    Whelan, D.A.4    Whitelaw, M.L.5    Bruick, R.K.6
  • 150
    • 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
    • DOI 10.1101/gad.924501
    • Mahon, P. C., Hirota, K. & Semenza, G. L. FIH-1: a novel protein that interacts with HIF-1α and VHL to mediate repression of HIF-1 transcriptional activity. Genes Dev. 15, 2675-2686 (2001). (Pubitemid 32988878)
    • (2001) Genes and Development , vol.15 , Issue.20 , pp. 2675-2686
    • Mahon, P.C.1    Hirota, K.2    Semenza, G.L.3
  • 152
    • 41149115123 scopus 로고    scopus 로고
    • The role of oxygen availability in embryonic development and stem cell function
    • DOI 10.1038/nrm2354, PII NRM2354
    • Simon, M. C. & Keith, B. The role of oxygen availability in embryonic development and stem cell function. Nature Rev. Mol. Cell Biol. 9, 285-296 (2008). (Pubitemid 351430845)
    • (2008) Nature Reviews Molecular Cell Biology , vol.9 , Issue.4 , pp. 285-296
    • Simon, M.C.1    Keith, B.2
  • 153
    • 77957584397 scopus 로고    scopus 로고
    • O2 regulates stem cells through Wnt/β-catenin signalling
    • Mazumdar, J. et al. O2 regulates stem cells through Wnt/β-catenin signalling. Nature Cell Biol. 12, 1007-1013 (2010).
    • (2010) Nature Cell Biol. , vol.12 , pp. 1007-1013
    • Mazumdar, J.1
  • 154
    • 33947217823 scopus 로고    scopus 로고
    • Interaction between β-catenin and HIF-1 promotes cellular adaptation to hypoxia
    • DOI 10.1038/ncb1534, PII NCB1534
    • Kaidi, A., Williams, A. C. & Paraskeva, C. Interaction between β-catenin and HIF-1 promotes cellular adaptation to hypoxia. Nature Cell Biol. 9, 210-217 (2007). (Pubitemid 46420864)
    • (2007) Nature Cell Biology , vol.9 , Issue.2 , pp. 210-217
    • Kaidi, A.1    Williams, A.C.2    Paraskeva, C.3
  • 156
    • 66149108432 scopus 로고    scopus 로고
    • Heterozygosity for hypoxia inducible factor 1α decreases the incidence of thymic lymphomas in a p53 mutant mouse model
    • Bertout, J. A. et al. Heterozygosity for hypoxia inducible factor 1α decreases the incidence of thymic lymphomas in a p53 mutant mouse model. Cancer Res. 69, 3213-3220 (2009).
    • (2009) Cancer Res. , vol.69 , pp. 3213-3220
    • Bertout, J.A.1
  • 157
    • 70349753257 scopus 로고    scopus 로고
    • HIF-2α maintains an undifferentiated state in neural crest-like human neuroblastoma tumor-initiating cells
    • Pietras, A. et al. HIF-2α maintains an undifferentiated state in neural crest-like human neuroblastoma tumor-initiating cells. Proc. Natl Acad. Sci. USA 106, 16805-16810 (2009).
    • (2009) Proc. Natl Acad. Sci. USA , vol.106 , pp. 16805-16810
    • Pietras, A.1
  • 159
    • 34648821254 scopus 로고    scopus 로고
    • Making a tumour's bed: Glioblastoma stem cells and the vascular niche
    • DOI 10.1038/nrc2246, PII NRC2246
    • Gilbertson, R. J. & Rich, J. N. Making a tumour's bed: glioblastoma stem cells and the vascular niche. Nature Rev. Cancer 7, 733-736 (2007). (Pubitemid 47463683)
    • (2007) Nature Reviews Cancer , vol.7 , Issue.10 , pp. 733-736
    • Gilbertson, R.J.1    Rich, J.N.2
  • 160
    • 76049100577 scopus 로고    scopus 로고
    • HIF-1: Upstream and downstream of cancer metabolism
    • Semenza, G. L. HIF-1: upstream and downstream of cancer metabolism. Curr. Opin. Genet. Dev. 20, 51-56 (2010).
    • (2010) Curr. Opin. Genet. Dev. , vol.20 , pp. 51-56
    • Semenza, G.L.1
  • 165
    • 56449095636 scopus 로고    scopus 로고
    • Hypoxia-inducible factor-2α correlates to distant recurrence and poor outcome in invasive breast cancer
    • Helczynska, K. et al. Hypoxia-inducible factor-2α correlates to distant recurrence and poor outcome in invasive breast cancer. Cancer Res. 68, 9212-9220 (2008).
    • (2008) Cancer Res. , vol.68 , pp. 9212-9220
    • Helczynska, K.1
  • 166
    • 0034282518 scopus 로고    scopus 로고
    • Overexpression of hypoxia-inducible factor 1α is a marker for an unfavorable prognosis in early-stage invasive cervical cancer
    • Birner, P. et al. Overexpression of hypoxia-inducible factor 1α is a marker for an unfavorable prognosis in early-stage invasive cervical cancer. Cancer Res. 60, 4693-4696 (2000).
    • (2000) Cancer Res. , vol.60 , pp. 4693-4696
    • Birner, P.1
  • 167
    • 43149084780 scopus 로고    scopus 로고
    • Prognostic significance of HIF-2α expression on tumor infiltrating macrophages in patients with uterine cervical cancer undergoing radiotherapy
    • DOI 10.2152/jmi.55.78
    • Kawanaka, T. et al. Prognostic significance of HIF-2α expression on tumor infiltrating macrophages in patients with uterine cervical cancer undergoing radiotherapy. J. Med. Invest. 55, 78-86 (2008). (Pubitemid 351643597)
    • (2008) Journal of Medical Investigation , vol.55 , Issue.1-2 , pp. 78-86
    • Kawanaka, T.1    Kubo, A.2    Ikushima, H.3    Sano, T.4    Takegawa, Y.5    Nishitani, H.6
  • 168
    • 11144222884 scopus 로고    scopus 로고
    • Prognostic impact of hypoxia-inducible factors 1α and 2α in colorectal cancer patients: Correlation with tumor angiogenesis and cyclooxygenase-2 expression
    • DOI 10.1158/1078-0432.CCR-0946-03
    • Yoshimura, H. et al. Prognostic impact of hypoxia-inducible factors 1α and 2α in colorectal cancer patients: correlation with tumor angiogenesis and cyclooxygenase-2 expression. Clin. Cancer Res. 10, 8554-8560 (2004). (Pubitemid 40053424)
    • (2004) Clinical Cancer Research , vol.10 , Issue.24 , pp. 8554-8560
    • Yoshimura, H.1    Dhar, D.K.2    Kohno, H.3    Kubota, H.4    Fujii, T.5    Ueda, S.6    Kinugasa, S.7    Tachibana, M.8    Nagasue, N.9
  • 171
    • 33846001692 scopus 로고    scopus 로고
    • Relationship of hypoxia-inducible factor 1α and p21WAF1/CIP1 expression to cell apoptosis and clinical outcome in patients with gastric cancer
    • Mizokami, K., Kakeji, Y., Oda, S. & Maehara, Y. Relationship of hypoxia-inducible factor 1α and p21WAF1/CIP1 expression to cell apoptosis and clinical outcome in patients with gastric cancer. World J. Surg. Oncol. 4, 94 (2006).
    • (2006) World J. Surg. Oncol. , vol.4 , pp. 94
    • Mizokami, K.1    Kakeji, Y.2    Oda, S.3    Maehara, Y.4
  • 172
    • 0142175222 scopus 로고    scopus 로고
    • Hypoxia-inducible factor-1α expression and angiogenesis in gastrointestinal stromal tumor of the stomach
    • Takahashi, R. et al. Hypoxia-inducible factor-1α expression and angiogenesis in gastrointestinal stromal tumor of the stomach. Oncol. Rep. 10, 797-802 (2003).
    • (2003) Oncol. Rep. , vol.10 , pp. 797-802
    • Takahashi, R.1
  • 174
    • 33747176556 scopus 로고    scopus 로고
    • The relation between hypoxia-inducible factor (HIF)=1α and HIF-2α expression with anemia and outcome in surgically treated head and neck cancer
    • DOI 10.1002/cncr.21983
    • Winter, S. C. et al. The relation between hypoxia-inducible factor (HIF)-1α and HIF-2α expression with anemia and outcome in surgically treated head and neck cancer. Cancer 107, 757-766 (2006). (Pubitemid 44232668)
    • (2006) Cancer , vol.107 , Issue.4 , pp. 757-766
    • Winter, S.C.1    Shah, K.A.2    Han, C.3    Campo, L.4    Turley, H.5    Leek, R.6    Corbridge, R.J.7    Cox, G.J.8    Harris, A.L.9
  • 178
    • 78651231169 scopus 로고    scopus 로고
    • Correlations of hypoxia-inducible factor-1α/hypoxia-inducible factor-2α expression with angiogenesis factors expression and prognosis in non-small cell lung cancer
    • Wu, X. H., Qian, C. & Yuan, K. Correlations of hypoxia-inducible factor-1α/hypoxia-inducible factor-2α expression with angiogenesis factors expression and prognosis in non-small cell lung cancer. Chin. Med. J. 124, 11-18 (2011).
    • (2011) Chin. Med. J. , vol.124 , pp. 11-18
    • Wu, X.H.1    Qian, C.2    Yuan, K.3
  • 179
    • 0142120661 scopus 로고    scopus 로고
    • Hypoxia-inducible factors 1α and 2α are related to vascular endothelial growth factor expression and a poorer prognosis in nodular malignant melanomas of the skin
    • DOI 10.1097/00008390-200310000-00008
    • Giatromanolaki, A. et al. Hypoxia-inducible factors 1α and 2α are related to vascular endothelial growth factor expression and a poorer prognosis in nodular malignant melanomas of the skin. Melanoma Res. 13, 493-501 (2003). (Pubitemid 37266952)
    • (2003) Melanoma Research , vol.13 , Issue.5 , pp. 493-501
    • Giatromanolaki, A.1    Sivridis, E.2    Kouskoukis, C.3    Gatter, K.C.4    Harris, A.L.5    Koukourakis, M.I.6
  • 180
    • 73149112785 scopus 로고    scopus 로고
    • HIF-1α and HIF-2α are differentially regulated in vivo in neuroblastoma: High HIF-1α correlates negatively to advanced clinical stage and tumor vascularization
    • Noguera, R. et al. HIF-1α and HIF-2α are differentially regulated in vivo in neuroblastoma: high HIF-1α correlates negatively to advanced clinical stage and tumor vascularization. Clin. Cancer Res. 15, 7130-7136 (2009).
    • (2009) Clin. Cancer Res. , vol.15 , pp. 7130-7136
    • Noguera, R.1
  • 181
    • 62349084794 scopus 로고    scopus 로고
    • Prognostic significance of Hypoxia-Inducible Factor 1α (HIF-1α) expression in serous ovarian cancer: An immunohistochemical study
    • Daponte, A. et al. Prognostic significance of Hypoxia-Inducible Factor 1α (HIF-1α) expression in serous ovarian cancer: an immunohistochemical study. BMC Cancer 8, 335 (2008).
    • (2008) BMC Cancer , vol.8 , pp. 335
    • Daponte, A.1
  • 182
    • 34547838192 scopus 로고    scopus 로고
    • Expression of hypoxia-inducible factor 1α, hypoxia-inducible factor 2α, and von Hippel-Lindau protein in epithelial ovarian neoplasms and allelic loss of von Hippel-Lindau gene: Nuclear expression of hypoxia-inducible factor 1α is an independent prognostic factor in ovarian carcinoma
    • DOI 10.1016/j.humpath.2007.02.010, PII S0046817707000998
    • Osada, R. et al. Expression of hypoxia-inducible factor 1α, hypoxia-inducible factor 2α, and von Hippel-Lindau protein in epithelial ovarian neoplasms and allelic loss of von Hippel-Lindau gene: nuclear expression of hypoxia-inducible factor 1α is an independent prognostic factor in ovarian carcinoma. Hum. Pathol. 38, 1310-1320 (2007). (Pubitemid 47247486)
    • (2007) Human Pathology , vol.38 , Issue.9 , pp. 1310-1320
    • Osada, R.1    Horiuchi, A.2    Kikuchi, N.3    Yoshida, J.4    Hayashi, A.5    Ota, M.6    Katsuyama, Y.7    Mellilo, G.8    Konishi, I.9
  • 183
    • 34447266708 scopus 로고    scopus 로고
    • Expression of hypoxia-inducible factor-1α and associated proteins in pancreatic ductal adenocarcinoma and their impact on prognosis
    • Sun, H. C. et al. Expression of hypoxia-inducible factor-1α and associated proteins in pancreatic ductal adenocarcinoma and their impact on prognosis. Int. J. Oncol. 30, 1359-1367 (2007).
    • (2007) Int. J. Oncol. , vol.30 , pp. 1359-1367
    • Sun, H.C.1
  • 185
    • 66449130218 scopus 로고    scopus 로고
    • Endothelial NOS, estrogen receptor β, and HIFs cooperate in the activation of a prognostic transcriptional pattern in aggressive human prostate cancer
    • Nanni, S. et al. Endothelial NOS, estrogen receptor β, and HIFs cooperate in the activation of a prognostic transcriptional pattern in aggressive human prostate cancer. J. Clin. Invest. 119, 1093-1108 (2009).
    • (2009) J. Clin. Invest. , vol.119 , pp. 1093-1108
    • Nanni, S.1
  • 186
    • 12944266844 scopus 로고    scopus 로고
    • The expression of hypoxia-inducible factor 1α is a favorable independent prognostic factor in renal cell carcinoma
    • Lidgren, A. et al. The expression of hypoxia-inducible factor 1α is a favorable independent prognostic factor in renal cell carcinoma. Clin. Cancer Res. 11, 1129-1135 (2005). (Pubitemid 40175762)
    • (2005) Clinical Cancer Research , vol.11 , Issue.3 , pp. 1129-1135
    • Lidgren, A.1    Hedberg, Y.2    Grankvist, K.3    Rasmuson, T.4    Vasko, J.5    Ljungberg, B.6
  • 187
    • 37549043546 scopus 로고    scopus 로고
    • Hypoxia-inducible factor 1α in clear cell renal cell carcinoma
    • Klatte, T. et al. Hypoxia-inducible factor 1α in clear cell renal cell carcinoma. Clin. Cancer Res. 13, 7388-7393 (2007).
    • (2007) Clin. Cancer Res. , vol.13 , pp. 7388-7393
    • Klatte, T.1
  • 188
    • 77958177671 scopus 로고    scopus 로고
    • Hepatic HIF-2 regulates erythropoietic responses to hypoxia in renal anemia
    • Kapitsinou, P. P. et al. Hepatic HIF-2 regulates erythropoietic responses to hypoxia in renal anemia. Blood 116, 3039-3048 (2010).
    • (2010) Blood , vol.116 , pp. 3039-3048
    • Kapitsinou, P.P.1
  • 192
    • 0036528246 scopus 로고    scopus 로고
    • Inhibition of HIF is necessary for tumor suppression by the von Hippel-Lindau protein
    • DOI 10.1016/S1535-6108(02)00043-0
    • Kondo, K., Klco, J., Nakamura, E., Lechpammer, M. & Kaelin, W. G. Jr. Inhibition of HIF is necessary for tumor suppression by the von Hippel-Lindau protein. Cancer Cell 1, 237-246 (2002). (Pubitemid 41039148)
    • (2002) Cancer Cell , vol.1 , Issue.3 , pp. 237-246
    • Kondo, K.1    Klco, J.2    Nakamura, E.3    Lechpammer, M.4    Kaelin Jr., W.G.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.