메뉴 건너뛰기




Volumn 49, Issue 1, 2014, Pages 1-15

Transcriptional regulation by hypoxia inducible factors

Author keywords

Chromatin; Histones; Hydroxylation; Hypoxia response element; Mediator; P300; RNA polymerase II

Indexed keywords

CITED2 PROTEIN; CYCLIN DEPENDENT KINASE 8; E1A ASSOCIATED P300 PROTEIN; HISTONE ACETYLTRANSFERASE PCAF; HYPOXIA INDUCIBLE FACTOR; HYPOXIA INDUCIBLE FACTOR 1ALPHA; HYPOXIA INDUCIBLE FACTOR 1BETA; HYPOXIA INDUCIBLE FACTOR 2ALPHA; PONTIN PROTEIN; PROTEIN; PROTEIN SWI; PYRUVATE KINASE; PYRUVATE KINASE ISOFORM M2; REPTIN PROTEIN; RNA POLYMERASE II; SIRTUIN 6; TRANSCRIPTION FACTOR SNF; UNCLASSIFIED DRUG;

EID: 84893077858     PISSN: 10409238     EISSN: 15497798     Source Type: Journal    
DOI: 10.3109/10409238.2013.838205     Document Type: Review
Times cited : (573)

References (172)
  • 1
    • 4644318828 scopus 로고    scopus 로고
    • Differential function of the prolyl hydroxylases PHD1, PHD2, and PHD3 in the regulation of hypoxia-inducible factor
    • Appelhoff RJ. (2004). Differential function of the prolyl hydroxylases PHD1, PHD2, and PHD3 in the regulation of hypoxia-inducible factor. J Biol Chem 279:38458-65.
    • (2004) J Biol Chem , vol.279 , pp. 38458-38465
    • Appelhoff, R.J.1
  • 2
    • 33745274488 scopus 로고    scopus 로고
    • Role of ETS transcription factors in the hypoxia-inducible factor-2 target gene selection
    • Aprelikova O, Wood M, Tackett S, et al. (2006). Role of ETS transcription factors in the hypoxia-inducible factor-2 target gene selection. Cancer Res 66:5641-7.
    • (2006) Cancer Res , vol.66 , pp. 5641-5647
    • Aprelikova, O.1    Wood, M.2    Tackett, S.3
  • 3
    • 0029803552 scopus 로고    scopus 로고
    • An essential role for p300/ CBP in the cellular response to hypoxia
    • Arany Z, Huang LE, Eckner R, et al. (1996). An essential role for p300/ CBP in the cellular response to hypoxia. Proc Natl Acad Sci USA 93: 12969-73.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 12969-12973
    • Arany, Z.1    Huang, L.E.2    Eckner, R.3
  • 4
    • 27744450043 scopus 로고    scopus 로고
    • Interaction between HIF-1 alpha (ODD) and hARD1 does not induce acetylation and destabilization of HIF-1 alpha
    • Arnesen T, Kong X, Evjenth R, et al. (2005). Interaction between HIF-1 alpha (ODD) and hARD1 does not induce acetylation and destabilization of HIF-1 alpha. FEBS Lett 579:6428-32.
    • (2005) FEBS Lett , vol.579 , pp. 6428-6432
    • Arnesen, T.1    Kong, X.2    Evjenth, R.3
  • 5
    • 4744353220 scopus 로고    scopus 로고
    • Sumoylation increases HIF-1a stability and its transcriptional activity
    • Bae S-H, Jeong J-W, Park JA, et al. (2004). Sumoylation increases HIF-1a stability and its transcriptional activity. Biochem Biophys Res Commun 324:394-400.
    • (2004) Biochem Biophys Res Commun , vol.324 , pp. 394-400
    • Bae, S.-H.1    Jeong, J.-W.2    Park, J.A.3
  • 6
    • 77449109789 scopus 로고    scopus 로고
    • Target gene context influences the transcriptional requirement for the KAT3 family of CBP and p300 histone acetyltransferases
    • Bedford DC, Kasper LH, Fukuyama T, et al. (2010). Target gene context influences the transcriptional requirement for the KAT3 family of CBP and p300 histone acetyltransferases. Epigenetics : official journal of the DNA Methylation Society 5:9-15.
    • (2010) Epigenetics : Official Journal of the DNA Methylation Society , vol.5 , pp. 9-15
    • Bedford, D.C.1    Kasper, L.H.2    Fukuyama, T.3
  • 7
    • 11144232325 scopus 로고    scopus 로고
    • Recruitment of thyroid hormone receptor/retinoblastoma-interacting protein 230 by the aryl hydrocarbon receptor nuclear translocator is required for the transcriptional response to both dioxin and hypoxia
    • Beischlag TV, Taylor RT, Rose DW, et al. (2004). Recruitment of thyroid hormone receptor/retinoblastoma-interacting protein 230 by the aryl hydrocarbon receptor nuclear translocator is required for the transcriptional response to both dioxin and hypoxia. J Biol Chem 279: 54620-8.
    • (2004) J Biol Chem , vol.279 , pp. 54620-54628
    • Beischlag, T.V.1    Taylor, R.T.2    Rose, D.W.3
  • 8
    • 69049111041 scopus 로고    scopus 로고
    • An integrative genomics approach identifies Hypoxia Inducible Factor-1 (HIF-1)-target genes that form the core response to hypoxia
    • Benita Y, Kikuchi H, Smith AD, et al. (2009). An integrative genomics approach identifies Hypoxia Inducible Factor-1 (HIF-1)-target genes that form the core response to hypoxia. Nucl Acids Res 37:4587-602.
    • (2009) Nucl Acids Res , vol.37 , pp. 4587-4602
    • Benita, Y.1    Kikuchi, H.2    Smith, A.D.3
  • 9
    • 78649753203 scopus 로고    scopus 로고
    • The chaperonedependent ubiquitin ligase CHIP targets HIF-1a for degradation in the presence of methylglyoxal
    • Bento CF, Fernandes R, Ramalho J, et al. (2010). The chaperonedependent ubiquitin ligase CHIP targets HIF-1a for degradation in the presence of methylglyoxal. PLoS ONE 5:e15062.
    • (2010) PLoS ONE , vol.5
    • Bento, C.F.1    Fernandes, R.2    Ramalho, J.3
  • 10
    • 0041465022 scopus 로고    scopus 로고
    • HIF prolyl-hydroxylase 2 is the key oxygen sensor setting low steady-state levels of HIF-1 in normoxia
    • Berra E, Benizri E, Ginouvès A, et al. (2003). HIF prolyl-hydroxylase 2 is the key oxygen sensor setting low steady-state levels of HIF-1 in normoxia. EMBO J 22:4082-90.
    • (2003) EMBO J , vol.22 , pp. 4082-4090
    • Berra, E.1    Benizri, E.2    Ginouvès, A.3
  • 11
    • 34447249876 scopus 로고    scopus 로고
    • SUMOylation of hypoxiainducible factor-1a reduces its transcriptional activity
    • Berta MA, Mazure N, Hattab M, et al. (2007). SUMOylation of hypoxiainducible factor-1a reduces its transcriptional activity. Biochem Biophys Res Commun 360:646-52.
    • (2007) Biochem Biophys Res Commun , vol.360 , pp. 646-652
    • Berta, M.A.1    Mazure, N.2    Hattab, M.3
  • 12
    • 0032900610 scopus 로고    scopus 로고
    • Functional role of p35srj, a novel p300/CBP binding protein, during transactivation by HIF-1
    • Bhattacharya S, Michels CL, Leung MK, et al. (1999). Functional role of p35srj, a novel p300/CBP binding protein, during transactivation by HIF-1. Genes Dev 13:64-75.
    • (1999) Genes Dev , vol.13 , pp. 64-75
    • Bhattacharya, S.1    Michels, C.L.2    Leung, M.K.3
  • 13
    • 33747366672 scopus 로고    scopus 로고
    • Cell-specific regulation of hypoxia-inducible factor (HIF)-1a stabilization and transactivation in a graded oxygen environment
    • Bracken CP, Fedele AO, Linke S, et al. (2006). Cell-specific regulation of hypoxia-inducible factor (HIF)-1a stabilization and transactivation in a graded oxygen environment. J Biol Chem 281:22575-85.
    • (2006) J Biol Chem , vol.281 , pp. 22575-22585
    • Bracken, C.P.1    Fedele, A.O.2    Linke, S.3
  • 14
    • 0038386022 scopus 로고    scopus 로고
    • Physical and functional interactions among AP-2 transcription factors, p300/ CREB-binding protein, and CITED2
    • Bragança J, Eloranta JJ, Bamforth SD, et al. (2003). Physical and functional interactions among AP-2 transcription factors, p300/ CREB-binding protein, and CITED2. J Biol Chem 278:16021-9.
    • (2003) J Biol Chem , vol.278 , pp. 16021-16029
    • Bragança, J.1    Eloranta, J.J.2    Bamforth, S.D.3
  • 15
    • 0032581277 scopus 로고    scopus 로고
    • Role of HIF-1a in hypoxia-mediated apoptosis, cell proliferation and tumor angiogenesis
    • Carmeliet P, Dor Y, Herbert JM, et al. (1998). Role of HIF-1a in hypoxia-mediated apoptosis, cell proliferation and tumor angiogenesis. Nature 394:485-90.
    • (1998) Nature , vol.394 , pp. 485-490
    • Carmeliet, P.1    Dor, Y.2    Herbert, J.M.3
  • 16
    • 0033986948 scopus 로고    scopus 로고
    • Redox-regulated recruitment of the transcriptional coactivators CREB-binding protein and SRC-1 to hypoxia-inducible factor 1alpha
    • Carrero P, Okamoto K, Coumailleau P, et al. (2000). Redox-regulated recruitment of the transcriptional coactivators CREB-binding protein and SRC-1 to hypoxia-inducible factor 1alpha. Mol Cell Biol 20: 402-15.
    • (2000) Mol Cell Biol , vol.20 , pp. 402-415
    • Carrero, P.1    Okamoto, K.2    Coumailleau, P.3
  • 17
    • 84865773630 scopus 로고    scopus 로고
    • The acetylase/deacetylase couple CREB-binding protein/sirtuin 1 controls hypoxia-inducible factor 2 signaling
    • Chen R, Xu M, Hogg RT, et al. (2012). The acetylase/deacetylase couple CREB-binding protein/sirtuin 1 controls hypoxia-inducible factor 2 signaling. J Biol Chem 287:30800-11.
    • (2012) J Biol Chem , vol.287 , pp. 30800-30811
    • Chen, R.1    Xu, M.2    Hogg, R.T.3
  • 18
    • 33644551073 scopus 로고    scopus 로고
    • Gene expression programs in response to hypoxia: Cell type specificity and prognostic significance in human cancers
    • Chi JT, Wang Z, Nuyten D, et al. (2006). Gene expression programs in response to hypoxia: cell type specificity and prognostic significance in human cancers. PLoS Med 3:395-409.
    • (2006) PLoS Med , vol.3 , pp. 395-409
    • Chi, J.T.1    Wang, Z.2    Nuyten, D.3
  • 19
    • 34047124233 scopus 로고    scopus 로고
    • Modulation of p300 binding by posttranslational modifications of the C-terminal activation domain of hypoxia-inducible factor-1a
    • Cho H, Ahn D-R, Park H, et al. (2007). Modulation of p300 binding by posttranslational modifications of the C-terminal activation domain of hypoxia-inducible factor-1a. FEBS Lett 581:1542-8.
    • (2007) FEBS Lett , vol.581 , pp. 1542-1548
    • Cho, H.1    Ahn, D.-R.2    Park, H.3
  • 20
    • 40749163248 scopus 로고    scopus 로고
    • The M2 splice isoform of pyruvate kinase is important for cancer metabolism and tumour growth
    • Christofk HR, Vander Heiden MG, Harris MH, et al. (2008). The M2 splice isoform of pyruvate kinase is important for cancer metabolism and tumour growth. Nature 452:230-3.
    • (2008) Nature , vol.452 , pp. 230-233
    • Christofk, H.R.1    Vander Heiden, M.G.2    Harris, M.H.3
  • 21
    • 0035983324 scopus 로고    scopus 로고
    • Loss of HIF-2a and inhibition of VEGF impair fetal lung maturation, whereas treatment with VEGF prevents fatal respiratory distress in premature mice
    • Compernolle V, Brusselmans K, Acker T, et al. (2002). Loss of HIF-2a and inhibition of VEGF impair fetal lung maturation, whereas treatment with VEGF prevents fatal respiratory distress in premature mice. Nat Med 8:703-10.
    • (2002) Nat Med , vol.8 , pp. 703-710
    • Compernolle, V.1    Brusselmans, K.2    Acker, T.3
  • 22
    • 0033584965 scopus 로고    scopus 로고
    • EPAS1 transactivation during hypoxia requires p42/p44 MAPK
    • Conrad PW, Freeman LT, Beitner-Johnson D, et al. (1999). EPAS1 transactivation during hypoxia requires p42/p44 MAPK. J Biol Chem 274: 33709-13.
    • (1999) J Biol Chem , vol.274 , pp. 33709-33713
    • Conrad, P.W.1    Freeman, L.T.2    Beitner-Johnson, D.3
  • 23
    • 33644747418 scopus 로고    scopus 로고
    • HIF-2a regulates OCT-4: Effects of hypoxia on stem cell function, embryonic development, and tumor growth
    • Covello KL, Kehler J, Yu H, et al. (2006). HIF-2a regulates OCT-4: effects of hypoxia on stem cell function, embryonic development, and tumor growth. Genes Dev 20:557-70.
    • (2006) Genes Dev , vol.20 , pp. 557-570
    • Covello, K.L.1    Kehler, J.2    Yu, H.3
  • 24
    • 0037117486 scopus 로고    scopus 로고
    • Structural basis for Hif-1a/CBP recognition in the cellular hypoxic response
    • Dames SA, Martinez-Yamout M, De Guzman RN, et al. (2002). Structural basis for Hif-1a/CBP recognition in the cellular hypoxic response. Proc Natl Acad Sci USA 99:5271-6.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 5271-5276
    • Dames, S.A.1    Martinez-Yamout, M.2    De Guzman, R.N.3
  • 25
    • 80052277906 scopus 로고    scopus 로고
    • Control of TH17/treg balance by hypoxia-inducible factor 1
    • Dang EV, Barbi J, Yang H-Y, et al. (2011). Control of TH17/treg balance by hypoxia-inducible factor 1. Cell 146:772-84.
    • (2011) Cell , vol.146 , pp. 772-784
    • Dang, E.V.1    Barbi, J.2    Yang, H.-Y.3
  • 26
    • 33645735151 scopus 로고    scopus 로고
    • The oxygen sensor factor-inhibiting hypoxia-inducible factor-1 controls expression of distinct genes through the bifunctional transcriptional character of hypoxia-inducible factor-1a
    • Dayan F, Roux D, Brahimi-Horn MC, et al. (2006). The oxygen sensor factor-inhibiting hypoxia-inducible factor-1 controls expression of distinct genes through the bifunctional transcriptional character of hypoxia-inducible factor-1a. Cancer Res 66:3688-98.
    • (2006) Cancer Res , vol.66 , pp. 3688-3698
    • Dayan, F.1    Roux, D.2    Brahimi-Horn, M.C.3
  • 27
    • 77950628758 scopus 로고    scopus 로고
    • High glucose concentrations attenuate hypoxia-inducible factor-1a expression and signaling in nontumor cells
    • Dehne N, Hintereder G, Brüne, B. (2010). High glucose concentrations attenuate hypoxia-inducible factor-1a expression and signaling in nontumor cells. Exp Cell Res 316:1179-89.
    • (2010) Exp Cell Res , vol.316 , pp. 1179-1189
    • Dehne, N.1    Hintereder, G.2    Brüne, B.3
  • 28
    • 77954162661 scopus 로고    scopus 로고
    • Drosophila genomewide RNAi screen identifies multiple regulators of HIF-dependent transcription in hypoxia
    • Dekanty A, Romero NM, Bertolin AP, et al. (2010). Drosophila genomewide RNAi screen identifies multiple regulators of HIF-dependent transcription in hypoxia. PLoS Genet 6:e1000994.
    • (2010) PLoS Genet , vol.6
    • Dekanty, A.1    Romero, N.M.2    Bertolin, A.P.3
  • 29
    • 66749129781 scopus 로고    scopus 로고
    • Regulation of hypoxia-inducible factor 2 a signaling by the stress-responsive deacetylase sirtuin 1
    • Dioum EM, Chen R, Alexander MS, et al. (2009). Regulation of hypoxia-inducible factor 2 a signaling by the stress-responsive deacetylase sirtuin 1. Science 324:1289-93.
    • (2009) Science , vol.324 , pp. 1289-1293
    • Dioum, E.M.1    Chen, R.2    Alexander, M.S.3
  • 30
    • 0031835957 scopus 로고    scopus 로고
    • Regulation of transcription by hypoxia requires a multiprotein complex that includes hypoxia-inducible factor 1, an adjacent transcription factor, and p300/CREB binding protein
    • Ebert BL, Bunn, HF. (1998). Regulation of transcription by hypoxia requires a multiprotein complex that includes hypoxia-inducible factor 1, an adjacent transcription factor, and p300/CREB binding protein. Mol Cell Biol 18:4089-96.
    • (1998) Mol Cell Biol , vol.18 , pp. 4089-4096
    • Ebert, B.L.1    Bunn, H.F.2
  • 31
    • 0033118983 scopus 로고    scopus 로고
    • Molecular mechanisms of transcription activation by HLF and HIF1a in response to hypoxia: Their stabilization and redox signal-induced interaction with CBP/ p300
    • Ema M, Hirota K, Mimura J, et al. (1999). Molecular mechanisms of transcription activation by HLF and HIF1a in response to hypoxia: their stabilization and redox signal-induced interaction with CBP/ p300. EMBO J 18:1905-14.
    • (1999) EMBO J , vol.18 , pp. 1905-1914
    • Ema, M.1    Hirota, K.2    Mimura, J.3
  • 32
    • 0031000736 scopus 로고    scopus 로고
    • A novel bHLH-PAS factor with close sequence similarity to hypoxia-inducible factor 1alpha regulates the VEGF expression and is potentially involved in lung and vascular development
    • Ema M, Taya S, Yokotani N, et al. (1997). A novel bHLH-PAS factor with close sequence similarity to hypoxia-inducible factor 1alpha regulates the VEGF expression and is potentially involved in lung and vascular development. Proc Natl Acad Sci USA 94:4273-8.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 4273-4278
    • Ema, M.1    Taya, S.2    Yokotani, N.3
  • 33
    • 77957748627 scopus 로고    scopus 로고
    • Hypoxia in abdominal aortic aneurysm supports a role for HIF-1a and Ets-1 as drivers of matrix metalloproteinase upregulation in human aortic smooth muscle cells
    • Erdozain OJ, Pegrum S, Winrow VR, et al. (2011). Hypoxia in abdominal aortic aneurysm supports a role for HIF-1a and Ets-1 as drivers of matrix metalloproteinase upregulation in human aortic smooth muscle cells. J Vasc Res 48:163-70.
    • (2011) J Vasc Res , vol.48 , pp. 163-170
    • Erdozain, O.J.1    Pegrum, S.2    Winrow, V.R.3
  • 34
    • 33646365644 scopus 로고    scopus 로고
    • Lysyl oxidase is essential for hypoxia-induced metastasis
    • Erler JT, Bennewith KL, Nicolau M, et al. (2006). Lysyl oxidase is essential for hypoxia-induced metastasis. Nat Lett 440:1222-6.
    • (2006) Nat Lett , vol.440 , pp. 1222-1226
    • Erler, J.T.1    Bennewith, K.L.2    Nicolau, M.3
  • 35
    • 78649276218 scopus 로고    scopus 로고
    • The meaning of pausing
    • Espinosa JM. (2010). The meaning of pausing. Mol Cell 40:507-8.
    • (2010) Mol Cell , vol.40 , pp. 507-508
    • Espinosa, J.M.1
  • 36
    • 0343683375 scopus 로고    scopus 로고
    • HRF, a putative basic helix-loop-helix-PAS-domain transcription factor is closely related to hypoxia-inducible factor-1a and developmentally expressed in blood vessels
    • Flamme I, Fröhlich T, Von Reutern M, et al. (1997). HRF, a putative basic helix-loop-helix-PAS-domain transcription factor is closely related to hypoxia-inducible factor-1a and developmentally expressed in blood vessels. Mech Dev 63:51-60.
    • (1997) Mech Dev , vol.63 , pp. 51-60
    • Flamme, I.1    Fröhlich, T.2    Von Reutern, M.3
  • 37
    • 34247583794 scopus 로고    scopus 로고
    • Glycogen synthase kinase 3 phosphorylates hypoxia-inducible factor 1 and mediates its destabilization in a VHL-independent manner
    • Flügel D, Görlach A, Michiels C, et al. (2007). Glycogen synthase kinase 3 phosphorylates hypoxia-inducible factor 1 and mediates its destabilization in a VHL-independent manner. Mol Cell Biol 27: 3253-65.
    • (2007) Mol Cell Biol , vol.27 , pp. 3253-3265
    • Flügel, D.1    Görlach, A.2    Michiels, C.3
  • 38
    • 65549121943 scopus 로고    scopus 로고
    • Notch signaling: The core pathway and its posttranslational regulation
    • Fortini ME. (2009). Notch signaling: the core pathway and its posttranslational regulation. Dev Cell 16:633-47.
    • (2009) Dev Cell , vol.16 , pp. 633-647
    • Fortini, M.E.1
  • 40
    • 4344594531 scopus 로고    scopus 로고
    • CITED4 inhibits hypoxiaactivated transcription in cancer cells, and its cytoplasmic location in breast cancer is associated with elevated expression of tumor cell hypoxia-inducible factor 1a
    • Fox SB, Bragança J, Turley H, et al. (2004). CITED4 inhibits hypoxiaactivated transcription in cancer cells, and its cytoplasmic location in breast cancer is associated with elevated expression of tumor cell hypoxia-inducible factor 1a. Cancer Res 64:6075-81.
    • (2004) Cancer Res , vol.64 , pp. 6075-6081
    • Fox, S.B.1    Bragança, J.2    Turley, H.3
  • 41
    • 84856496317 scopus 로고    scopus 로고
    • The LIMD1 protein bridges an association between the prolyl hydroxylases and VHL to repress HIF-1 activity
    • Foxler DE, Bridge KS, James V, et al. (2012). The LIMD1 protein bridges an association between the prolyl hydroxylases and VHL to repress HIF-1 activity. Nat Cell Biol 14:201-8.
    • (2012) Nat Cell Biol , vol.14 , pp. 201-208
    • Foxler, D.E.1    Bridge, K.S.2    James, V.3
  • 42
    • 0038392752 scopus 로고    scopus 로고
    • Structural basis for negative regulation of hypoxia-inducible factor-1alpha by CITED2
    • Freedman SJ, Sun Z-YJ, Kung A. L, et al. (2003). Structural basis for negative regulation of hypoxia-inducible factor-1alpha by CITED2. Nat Struct Biol 10:504-12.
    • (2003) Nat Struct Biol , vol.10 , pp. 504-512
    • Freedman, S.J.1    Sun, Z.-Y.J.2    Kung, A.L.3
  • 43
    • 84878831596 scopus 로고    scopus 로고
    • HIF1A employs CDK8-mediator to stimulate RNAPII elongation in response to hypoxia
    • Galbraith MD, Allen MA, Bensard CL, et al. (2013). HIF1A employs CDK8-mediator to stimulate RNAPII elongation in response to hypoxia. Cell 153:1327-39.
    • (2013) Cell , vol.153 , pp. 1327-1339
    • Galbraith, M.D.1    Allen, M.A.2    Bensard, C.L.3
  • 44
    • 80055077899 scopus 로고    scopus 로고
    • HDAC4 protein regulates HIF1a protein lysine acetylation and cancer cell response to hypoxia
    • Geng H, Harvey CT, Pittsenbarger J, et al. (2011). HDAC4 protein regulates HIF1a protein lysine acetylation and cancer cell response to hypoxia. J Biol Chem 286:38095-102.
    • (2011) J Biol Chem , vol.286 , pp. 38095-38102
    • Geng, H.1    Harvey, C.T.2    Pittsenbarger, J.3
  • 45
    • 84867424393 scopus 로고    scopus 로고
    • HIF1a protein stability is increased by acetylation at lysine 709
    • Geng H, Liu Q, Xue C, et al. (2012). HIF1a protein stability is increased by acetylation at lysine 709. J Biol Chem 287:35496-505.
    • (2012) J Biol Chem , vol.287 , pp. 35496-35505
    • Geng, H.1    Liu, Q.2    Xue, C.3
  • 46
    • 47549090254 scopus 로고    scopus 로고
    • NELF-mediated stalling of Pol II can enhance gene expression by blocking promoter-proximal nucleosome assembly
    • Gilchrist DA, Nechaev S, Lee C, et al. (2008). NELF-mediated stalling of Pol II can enhance gene expression by blocking promoter-proximal nucleosome assembly. Genes Dev 22:1921-33.
    • (2008) Genes Dev , vol.22 , pp. 1921-1933
    • Gilchrist, D.A.1    Nechaev, S.2    Lee, C.3
  • 47
    • 0037189565 scopus 로고    scopus 로고
    • The transcriptional activation function of the HIF-like factor requires phosphorylation at a conserved threonine
    • Gradin K, Takasaki C, Fujii-Kuriyama Y, et al. (2002). The transcriptional activation function of the HIF-like factor requires phosphorylation at a conserved threonine. J Biol Chem 277:23508-14.
    • (2002) J Biol Chem , vol.277 , pp. 23508-23514
    • Gradin, K.1    Takasaki, C.2    Fujii-Kuriyama, Y.3
  • 48
    • 84861845402 scopus 로고    scopus 로고
    • The updated biology of hypoxia-inducible factor
    • Greer SN, Metcalf JL, Wang Y, et al. (2012). The updated biology of hypoxia-inducible factor. EMBO J 31:2448-60.
    • (2012) EMBO J , vol.31 , pp. 2448-2460
    • Greer, S.N.1    Metcalf, J.L.2    Wang, Y.3
  • 49
    • 0031733828 scopus 로고    scopus 로고
    • Molecular characterization and chromosomal localization of a third alpha-class hypoxia inducible factor subunit, HIF3a
    • Gu YZ, Moran SM, Hogenesch JB, et al. (1998). Molecular characterization and chromosomal localization of a third alpha-class hypoxia inducible factor subunit, HIF3a. Gene Expr 7:205-13.
    • (1998) Gene Expr , vol.7 , pp. 205-213
    • Gu, Y.Z.1    Moran, S.M.2    Hogenesch, J.B.3
  • 50
    • 84865241459 scopus 로고    scopus 로고
    • The Notch signalling system: Recent insights into the complexity of a conserved pathway
    • Guruharsha KG, Kankel MW, Artavanis-Tsakonas S. (2012). The Notch signalling system: recent insights into the complexity of a conserved pathway. Nat Rev Genet 13:654-66.
    • (2012) Nat Rev Genet , vol.13 , pp. 654-666
    • Guruharsha, K.G.1    Kankel, M.W.2    Artavanis-Tsakonas, S.3
  • 51
    • 27644561755 scopus 로고    scopus 로고
    • Hypoxia requires notch signaling to maintain the undifferentiated cell state
    • Gustafsson MV, Zheng X, Pereira T, et al. (2005). Hypoxia requires notch signaling to maintain the undifferentiated cell state. Dev Cell 9: 617-28.
    • (2005) Dev Cell , vol.9 , pp. 617-628
    • Gustafsson, M.V.1    Zheng, X.2    Pereira, T.3
  • 52
    • 0035812789 scopus 로고    scopus 로고
    • Expression and characterization of Hypoxia-Inducible Factor (HIF)-3a in human kidney: Suppression of HIF-mediated gene expression by HIF-3a
    • Hara S, Hamada J, Kobayashi C, et al. (2001). Expression and characterization of Hypoxia-Inducible Factor (HIF)-3a in human kidney: suppression of HIF-mediated gene expression by HIF-3a. Biochem Biophys Res Commun 287:808-13.
    • (2001) Biochem Biophys Res Commun , vol.287 , pp. 808-813
    • Hara, S.1    Hamada, J.2    Kobayashi, C.3
  • 53
    • 82255186546 scopus 로고    scopus 로고
    • Roles of the human hypoxia-inducible factor (HIF)-3a variants in the hypoxia response
    • Heikkilä M, Pasanen A, Kivirikko KI, et al. (2011). Roles of the human hypoxia-inducible factor (HIF)-3a variants in the hypoxia response. Cell Mol Life Sci 68:3885-901.
    • (2011) Cell Mol Life Sci , vol.68 , pp. 3885-3901
    • Heikkilä, M.1    Pasanen, A.2    Kivirikko, K.I.3
  • 54
    • 77449131347 scopus 로고    scopus 로고
    • Tyrosine phosphorylation inhibits PKM2 to promote the Warburg effect and tumor growth
    • doi: 10.1126/scisignal.2000431
    • Hitosugi T, Kang S, Vander Heiden MG, et al. (2009). Tyrosine phosphorylation inhibits PKM2 to promote the Warburg effect and tumor growth. Sci Signal 2:ra73. doi: 10.1126/scisignal.2000431.
    • (2009) Sci Signal , vol.2
    • Hitosugi, T.1    Kang, S.2    Vander Heiden, M.G.3
  • 55
    • 0025906014 scopus 로고
    • Cloning of a factor required for activity of the Ah (dioxin) receptor
    • Hoffman EC, Reyes H, Chu FF, et al. (1991). Cloning of a factor required for activity of the Ah (dioxin) receptor. Science 252:954-8.
    • (1991) Science , vol.252 , pp. 954-958
    • Hoffman, E.C.1    Reyes, H.2    Chu, F.F.3
  • 56
    • 0345491599 scopus 로고    scopus 로고
    • Differential roles of Hypoxia-Inducible Factor 1 (HIF-1) and HIF-2 in hypoxic gene regulation
    • Hu CH, Wang L-Y, Chodosh LA, et al. (2003). Differential roles of Hypoxia-Inducible Factor 1 (HIF-1) and HIF-2 in hypoxic gene regulation. Mol Cell Biol 23:9361-74.
    • (2003) Mol Cell Biol , vol.23 , pp. 9361-9374
    • Hu, C.H.1    Wang, L.-Y.2    Chodosh, L.A.3
  • 57
    • 35848938945 scopus 로고    scopus 로고
    • The N-terminal transactivation domain confers target gene specificity of hypoxia-inducible factors HIF-1 and HIF-2
    • Hu CJ, Sataur A, Wang L, et al. (2007). The N-terminal transactivation domain confers target gene specificity of hypoxia-inducible factors HIF-1 and HIF-2. Mol Biol Cell 18:4528-42.
    • (2007) Mol Biol Cell , vol.18 , pp. 4528-4542
    • Hu, C.J.1    Sataur, A.2    Wang, L.3
  • 58
    • 0029753008 scopus 로고    scopus 로고
    • Activation of hypoxiainducible transcription factor depends primarily upon redox-sensitive stabilization of its alpha subunit
    • Huang LE, Arany Z, Livingston DM, et al. (1996). Activation of hypoxiainducible transcription factor depends primarily upon redox-sensitive stabilization of its alpha subunit. J Biol Chem 271:32253-9.
    • (1996) J Biol Chem , vol.271 , pp. 32253-32259
    • Huang, L.E.1    Arany, Z.2    Livingston, D.M.3
  • 59
    • 0032493368 scopus 로고    scopus 로고
    • Regulation of hypoxiainducible factor 1a is mediated by an O2-dependent degradation domain via the ubiquitin-proteasome pathway
    • Huang LE, Gu J, Schau M, et al. (1998). Regulation of hypoxiainducible factor 1a is mediated by an O2-dependent degradation domain via the ubiquitin-proteasome pathway. Proc Natl Acad Sci USA 95:7987-92.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 7987-7992
    • Huang, L.E.1    Gu, J.2    Schau, M.3
  • 60
    • 84874367417 scopus 로고    scopus 로고
    • Hypoxia inducible factor 3a plays a critical role in alveolarization and distal epithelial cell differentiation during mouse lung development
    • Huang Y, Kapere Ochieng J, Kempen MB-V, et al. (2013). Hypoxia inducible factor 3a plays a critical role in alveolarization and distal epithelial cell differentiation during mouse lung development. PLoS ONE 8:e57695.
    • (2013) PLoS ONE , vol.8
    • Huang, Y.1    Kapere Ochieng, J.2    Mb-V, K.3
  • 61
    • 75349105801 scopus 로고    scopus 로고
    • Rvb1-Rvb2: Essential ATPdependent helicases for critical complexes
    • Huen J, Kakihara Y, Ugwu F, et al. (2010). Rvb1-Rvb2: essential ATPdependent helicases for critical complexes. Biochem Cell Biol 88: 29-40.
    • (2010) Biochem Cell Biol , vol.88 , pp. 29-40
    • Huen, J.1    Kakihara, Y.2    Ugwu, F.3
  • 62
    • 0035917313 scopus 로고    scopus 로고
    • HIFa targeted for VHLmediated destruction by proline hydroxylation: Implications for O2 sensing
    • Ivan M, Kondo K, Yang H, et al. (2001). HIFa targeted for VHLmediated destruction by proline hydroxylation: implications for O2 sensing. Science 292:464-8.
    • (2001) Science , vol.292 , pp. 464-468
    • Ivan, M.1    Kondo, K.2    Yang, H.3
  • 63
    • 15444342958 scopus 로고    scopus 로고
    • Cellular and developmental control of O2 homeostasis by hypoxia-inducible factor 1a
    • Iyer NV, Kotch LE, Agani F, et al. (1998a). Cellular and developmental control of O2 homeostasis by hypoxia-inducible factor 1a. Genes Dev 12:149-62.
    • (1998) Genes Dev , vol.12 , pp. 149-162
    • Iyer, N.V.1    Kotch, L.E.2    Agani, F.3
  • 64
    • 0032167784 scopus 로고    scopus 로고
    • The human hypoxiainducible factor 1a gene: HIF1A structure and evolutionary conservation
    • Iyer NV, Leung SW, Semenza GL. (1998b). The human hypoxiainducible factor 1a gene: HIF1A structure and evolutionary conservation. Genomics 52:159-65.
    • (1998) Genomics , vol.52 , pp. 159-165
    • Iyer, N.V.1    Leung, S.W.2    Semenza, G.L.3
  • 65
    • 0035917808 scopus 로고    scopus 로고
    • Targeting of HIF-a to the von Hippel-Lindau ubiquitylation complex by O2-regulated prolyl hydroxylation
    • Jaakkola P, Mole DR, Tian YM, et al. (2001). Targeting of HIF-a to the von Hippel-Lindau ubiquitylation complex by O2-regulated prolyl hydroxylation. Science 292:468-72.
    • (2001) Science , vol.292 , pp. 468-472
    • Jaakkola, P.1    Mole, D.R.2    Tian, Y.M.3
  • 66
    • 18744375998 scopus 로고    scopus 로고
    • Regulation and destabilization of HIF-1a by ARD1-mediated acetylation
    • Jeong J-W, Bae M-K, Ahn M-Y, et al. (2002). Regulation and destabilization of HIF-1a by ARD1-mediated acetylation. Cell 111: 709-20.
    • (2002) Cell , vol.111 , pp. 709-720
    • Jeong, J.-W.1    Bae, M.-K.2    Ahn, M.-Y.3
  • 67
    • 0030787469 scopus 로고    scopus 로고
    • Transactivation and inhibitory domains of hypoxia-inducible factor 1a: Modulation of transcriptional activity by oxygen tension
    • Jiang BH, Zheng JZ, Leung SW, et al. (1997). Transactivation and inhibitory domains of hypoxia-inducible factor 1a: modulation of transcriptional activity by oxygen tension. J Biol Chem 272:19253-60.
    • (1997) J Biol Chem , vol.272 , pp. 19253-19260
    • Jiang, B.H.1    Zheng, J.Z.2    Leung, S.W.3
  • 68
    • 0029944965 scopus 로고    scopus 로고
    • Dimerization, DNA binding, and transactivation properties of hypoxia-inducible factor 1
    • Jiang BH, Rue E, Wang GL, et al. (1996). Dimerization, DNA binding, and transactivation properties of hypoxia-inducible factor 1. J Biol Chem 271:17771-8.
    • (1996) J Biol Chem , vol.271 , pp. 17771-17778
    • Jiang, B.H.1    Rue, E.2    Wang, G.L.3
  • 69
    • 77956912534 scopus 로고    scopus 로고
    • Casein kinase 1 regulates human hypoxia-inducible factor HIF-1
    • Kalousi A, Mylonis I, Politou AS, et al. (2010). Casein kinase 1 regulates human hypoxia-inducible factor HIF-1. J Cell Sci 123:2976-86.
    • (2010) J Cell Sci , vol.123 , pp. 2976-2986
    • Kalousi, A.1    Mylonis, I.2    Politou, A.S.3
  • 70
    • 27844514169 scopus 로고    scopus 로고
    • Two transactivation mechanisms cooperate for the bulk of HIF-1-responsive gene expression
    • Kasper LH, Boussouar F, Boyd K, et al. (2005). Two transactivation mechanisms cooperate for the bulk of HIF-1-responsive gene expression. EMBO J 24:3846-58.
    • (2005) EMBO J , vol.24 , pp. 3846-3858
    • Kasper, L.H.1    Boussouar, F.2    Boyd, K.3
  • 71
    • 34247527730 scopus 로고    scopus 로고
    • Hypoxia-inducible factors, stem cells, and cancer
    • Keith B, Simon MC. (2007). Hypoxia-inducible factors, stem cells, and cancer. Cell 129:465-472.
    • (2007) Cell , vol.129 , pp. 465-472
    • Keith, B.1    Simon, M.C.2
  • 72
    • 63249087504 scopus 로고    scopus 로고
    • SWI/SNF regulates the cellular response to hypoxia
    • Kenneth NS, Mudie S, Van Uden P, et al. (2009). SWI/SNF regulates the cellular response to hypoxia. J Biol Chem 284:4123-31.
    • (2009) J Biol Chem , vol.284 , pp. 4123-4131
    • Kenneth, N.S.1    Mudie, S.2    Van Uden, P.3
  • 73
    • 9644257219 scopus 로고    scopus 로고
    • Role of the coiled-coil coactivator (CoCoA) in aryl hydrocarbon receptor-mediated transcription
    • Kim JH, Stallcup MR. (2004). Role of the coiled-coil coactivator (CoCoA) in aryl hydrocarbon receptor-mediated transcription. J Biol Chem 279:49842-8.
    • (2004) J Biol Chem , vol.279 , pp. 49842-49848
    • Kim, J.H.1    Stallcup, M.R.2
  • 74
    • 0033975850 scopus 로고    scopus 로고
    • Hypoxia response element of the human vascular endothelial growth factor gene mediates transcriptional regulation by nitric oxide: Control of hypoxia-inducible factor-1 activity by nitric oxide
    • Kimura H, Weisz A, Kurashima Y, et al. (1999). Hypoxia response element of the human vascular endothelial growth factor gene mediates transcriptional regulation by nitric oxide: control of hypoxia-inducible factor-1 activity by nitric oxide. Blood 95:189-97.
    • (1999) Blood , vol.95 , pp. 189-197
    • Kimura, H.1    Weisz, A.2    Kurashima, Y.3
  • 75
    • 0035910429 scopus 로고    scopus 로고
    • Identification of hypoxiainducible factor 1 ancillary sequence and its function in vascular endothelial growth factor gene induction by hypoxia and nitric oxide
    • Kimura H, Weisz A, Ogura T, et al. (2001). Identification of hypoxiainducible factor 1 ancillary sequence and its function in vascular endothelial growth factor gene induction by hypoxia and nitric oxide. J Biol Chem 276:2292-8.
    • (2001) J Biol Chem , vol.276 , pp. 2292-2298
    • Kimura, H.1    Weisz, A.2    Ogura, T.3
  • 76
    • 13844294211 scopus 로고    scopus 로고
    • The casein kinase 1 family: Participation in multiple cellular processes in eukaryotes
    • Knippschild U, Gocht A, Wolff S, et al. (2005). The casein kinase 1 family: participation in multiple cellular processes in eukaryotes. Cell Signal 17:675-89.
    • (2005) Cell Signal , vol.17 , pp. 675-689
    • Knippschild, U.1    Gocht, A.2    Wolff, S.3
  • 77
    • 57349136768 scopus 로고    scopus 로고
    • Hypoxia-associated factor, a novel E3-ubiquitin ligase, binds and ubiquitinates hypoxia-inducible factor 1a, leading to its oxygen-independent degradation
    • Koh MY, Darnay BG, Powis, G. (2008a). Hypoxia-associated factor, a novel E3-ubiquitin ligase, binds and ubiquitinates hypoxia-inducible factor 1a, leading to its oxygen-independent degradation. Mol Cell Biol 28:7081-95.
    • (2008) Mol Cell Biol , vol.28 , pp. 7081-7095
    • Koh, M.Y.1    Darnay, B.G.2    Powis, G.3
  • 79
    • 79957440998 scopus 로고    scopus 로고
    • The hypoxia-associated factor switches cells from HIF-1- to HIF-2-dependent signaling promoting stem cell characteristics, aggressive tumor growth and invasion
    • Koh MY, Lemos R, Liu X, et al. (2011). The hypoxia-associated factor switches cells from HIF-1- to HIF-2-dependent signaling promoting stem cell characteristics, aggressive tumor growth and invasion. Cancer Res 71:4015-27.
    • (2011) Cancer Res , vol.71 , pp. 4015-4027
    • Koh, M.Y.1    Lemos, R.2    Liu, X.3
  • 80
    • 84865429409 scopus 로고    scopus 로고
    • Passing the baton: The HIF switch
    • Koh MY, Powis, G. (2012). Passing the baton: the HIF switch. Trends Biochem Sci 37:364-72.
    • (2012) Trends Biochem Sci , vol.37 , pp. 364-372
    • Koh, M.Y.1    Powis, G.2
  • 81
    • 1642315195 scopus 로고    scopus 로고
    • Catalytic properties of the asparaginyl hydroxylase (FIH) in the oxygen sensing pathway are distinct from those of its prolyl 4-hydroxylases
    • Koivunen PMH, Günzler V, et al. (2004). Catalytic properties of the asparaginyl hydroxylase (FIH) in the oxygen sensing pathway are distinct from those of its prolyl 4-hydroxylases. J Biol Chem 279: 9899-904.
    • (2004) J Biol Chem , vol.279 , pp. 9899-9904
    • Koivunen, P.M.H.1    Günzler, V.2
  • 82
    • 35648930417 scopus 로고    scopus 로고
    • An endoplasmic reticulum transmembrane prolyl 4-hydroxylase is induced by hypoxia and acts on hypoxia-inducible factor alpha
    • Koivunen P, Tiainen P, Hyvarinen J, et al. (2007). An endoplasmic reticulum transmembrane prolyl 4-hydroxylase is induced by hypoxia and acts on hypoxia-inducible factor alpha. J Biol Chem 282: 30544-52.
    • (2007) J Biol Chem , vol.282 , pp. 30544-30552
    • Koivunen, P.1    Tiainen, P.2    Hyvarinen, J.3
  • 83
    • 84863223765 scopus 로고    scopus 로고
    • HIF2a-Sp1 interaction mediates a deacetylation-dependent FVII-gene activation under hypoxic conditions in ovarian cancer cells
    • Koizume S, Ito S, Miyagi E, et al. (2012). HIF2a-Sp1 interaction mediates a deacetylation-dependent FVII-gene activation under hypoxic conditions in ovarian cancer cells. Nucl Acids Res 40:5389-401.
    • (2012) Nucl Acids Res , vol.40 , pp. 5389-5401
    • Koizume, S.1    Ito, S.2    Miyagi, E.3
  • 84
    • 84856628731 scopus 로고    scopus 로고
    • Dietary obesity-associated Hif1a activation in adipocytes restricts fatty acid oxidation and energy expenditure via suppression of the Sirt2-NAD+ system
    • Krishnan J, Danzer C, Simka T, et al. (2012). Dietary obesity-associated Hif1a activation in adipocytes restricts fatty acid oxidation and energy expenditure via suppression of the Sirt2-NAD+ system. Genes Dev 26:259-70.
    • (2012) Genes Dev , vol.26 , pp. 259-270
    • Krishnan, J.1    Danzer, C.2    Simka, T.3
  • 85
    • 9144250328 scopus 로고    scopus 로고
    • Disruption of dimerization and substrate phosphorylation inhibit factor inhibiting hypoxia-inducible factor (FIH) activity
    • Lancaster DE, McNeill LA, McDonough MA, et al. (2004). Disruption of dimerization and substrate phosphorylation inhibit factor inhibiting hypoxia-inducible factor (FIH) activity. Biochem J 383:429-37.
    • (2004) Biochem J , vol.383 , pp. 429-437
    • Lancaster, D.E.1    McNeill, L.A.2    McDonough, M.A.3
  • 87
    • 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. (2002a). FIH-1 is an asparaginyl hydroxylase enzyme that regulates the transcriptional activity of hypoxia-inducible factor. Genes Dev 16:1466-71.
    • (2002) Genes Dev , vol.16 , pp. 1466-1471
    • Lando, D.1    Peet, D.J.2    Gorman, J.J.3
  • 88
    • 0036469038 scopus 로고    scopus 로고
    • Asparagine hydroxylation of the HIF transactivation domain: A hypoxic switch
    • Lando D, Peet DJ, Whelan DA, et al. (2002b). Asparagine hydroxylation of the HIF transactivation domain: a hypoxic switch. Sci Signal 295: 858-61.
    • (2002) Sci Signal , vol.295 , pp. 858-861
    • Lando, D.1    Peet, D.J.2    Whelan, D.A.3
  • 89
    • 34247219188 scopus 로고    scopus 로고
    • Target gene selectivity of hypoxia-inducible factor-alpha in renal cancer cells is conveyed by post-DNA-binding mechanisms
    • Lau KW, Tian YM, Raval RR, et al. (2007). Target gene selectivity of hypoxia-inducible factor-alpha in renal cancer cells is conveyed by post-DNA-binding mechanisms. Br J Cancer 96:1284-92.
    • (2007) Br J Cancer , vol.96 , pp. 1284-1292
    • Lau, K.W.1    Tian, Y.M.2    Raval, R.R.3
  • 90
    • 0035012605 scopus 로고    scopus 로고
    • HER2 (neu) Signaling increases the rate of hypoxia-inducible factor 1a (HIF-1a) synthesis: Novel mechanism for hif-1-mediated vascular endothelial growth factor expression
    • Laughner E, Taghavi P, Chiles K, et al. (2001). HER2 (neu) Signaling increases the rate of hypoxia-inducible factor 1a (HIF-1a) synthesis: novel mechanism for hif-1-mediated vascular endothelial growth factor expression. Mol Cell Biol 21:3995-4004.
    • (2001) Mol Cell Biol , vol.21 , pp. 3995-4004
    • Laughner, E.1    Taghavi, P.2    Chiles, K.3
  • 91
    • 80051978418 scopus 로고    scopus 로고
    • Hypoxia-induced methylation of a pontin chromatin remodeling factor
    • Lee JS, Kim Y, Bhin J, et al. (2011). Hypoxia-induced methylation of a pontin chromatin remodeling factor. Proc Natl Acad Sci USA 108: 13510-15.
    • (2011) Proc Natl Acad Sci USA , vol.108 , pp. 13510-13515
    • Lee, J.S.1    Kim, Y.2    Bhin, J.3
  • 92
    • 77954265666 scopus 로고    scopus 로고
    • Negative regulation of hypoxic responses via induced Reptin methylation
    • Lee JS, Kim Y, Kim IS, et al. (2010). Negative regulation of hypoxic responses via induced Reptin methylation. Mol Cell 39:71-85.
    • (2010) Mol Cell , vol.39 , pp. 71-85
    • Lee, J.S.1    Kim, Y.2    Kim, I.S.3
  • 93
    • 70450223507 scopus 로고    scopus 로고
    • Generating specificity and diversity in the transcriptional response to hypoxia
    • Lendahl U, Lee KL, Yang H, et al. (2009). Generating specificity and diversity in the transcriptional response to hypoxia. Nat Rev Genet 10: 821-32.
    • (2009) Nat Rev Genet , vol.10 , pp. 821-832
    • Lendahl, U.1    Lee, K.L.2    Yang, H.3
  • 94
    • 77955499804 scopus 로고    scopus 로고
    • Sirtuin 1 modulates cellular responses to hypoxia by deacetylating hypoxia-inducible factor 1a
    • Lim J-H, Lee Y-M, Chun Y-S, et al. (2010). Sirtuin 1 modulates cellular responses to hypoxia by deacetylating hypoxia-inducible factor 1a. Mol Cell 38:864-78.
    • (2010) Mol Cell , vol.38 , pp. 864-878
    • Lim, J.-H.1    Lee, Y.-M.2    Chun, Y.-S.3
  • 95
    • 33846254999 scopus 로고    scopus 로고
    • RACK1 competes with HSP90 for binding to HIF-1a and is required for O2-independent and HSP90 inhibitor-induced degradation of HIF-1a
    • Liu YV, Baek JH, Zhang H, et al. (2007). RACK1 competes with HSP90 for binding to HIF-1a and is required for O2-independent and HSP90 inhibitor-induced degradation of HIF-1a. Mol Cell 25:207-17.
    • (2007) Mol Cell , vol.25 , pp. 207-217
    • Liu, Y.V.1    Baek, J.H.2    Zhang, H.3
  • 96
    • 0037189542 scopus 로고    scopus 로고
    • Hypoxia-inducible factor 1 activation by aerobic glycolysis implicates the Warburg effect in carcinogenesis
    • Lu H, Forbes RA, Verma A. (2002). Hypoxia-inducible factor 1 activation by aerobic glycolysis implicates the Warburg effect in carcinogenesis. J Biol Chem 277:23111-15.
    • (2002) J Biol Chem , vol.277 , pp. 23111-23115
    • Lu, H.1    Forbes, R.A.2    Verma, A.3
  • 97
    • 29644442625 scopus 로고    scopus 로고
    • Reversible inactivation of HIF-1 prolyl hydroxylases allows cell metabolism to control basal HIF-1
    • Lu H, Dalgard CL, Mohyeldin A, et al. (2005). Reversible inactivation of HIF-1 prolyl hydroxylases allows cell metabolism to control basal HIF-1. J Biol Chem 280:41928-39.
    • (2005) J Biol Chem , vol.280 , pp. 41928-41939
    • Lu, H.1    Dalgard, C.L.2    Mohyeldin, A.3
  • 98
    • 79957567239 scopus 로고    scopus 로고
    • Pyruvate kinase M2 is a PHD3- stimulated coactivator for hypoxia-inducible factor 1
    • Luo W, Hu H, Chang R, et al. (2011). Pyruvate kinase M2 is a PHD3- stimulated coactivator for hypoxia-inducible factor 1. Cell 145: 732-44.
    • (2011) Cell , vol.145 , pp. 732-744
    • Luo, W.1    Hu, H.2    Chang, R.3
  • 99
    • 77950473770 scopus 로고    scopus 로고
    • Hsp70 and CHIP selectively mediate ubiquitination and degradation of hypoxia-inducible factor (HIF)-1 but Not HIF-2
    • Luo W, Zhong J, Chang R, et al. (2010). Hsp70 and CHIP selectively mediate ubiquitination and degradation of hypoxia-inducible factor (HIF)-1 but Not HIF-2. J Biol Chem 285:3651-63.
    • (2010) J Biol Chem , vol.285 , pp. 3651-3663
    • Luo, W.1    Zhong, J.2    Chang, R.3
  • 100
    • 0035887011 scopus 로고    scopus 로고
    • FIH-1: A novel protein that interacts with HIF-1alpha and VHL to mediate repression of HIF-1 transcriptional activity
    • Mahon PC, Hirota K, Semenza GL. (2001). FIH-1: a novel protein that interacts with HIF-1alpha and VHL to mediate repression of HIF-1 transcriptional activity. Genes Dev 15:2675-86.
    • (2001) Genes Dev , vol.15 , pp. 2675-2686
    • Mahon, P.C.1    Hirota, K.2    Semenza, G.L.3
  • 101
    • 78649364332 scopus 로고    scopus 로고
    • Hypoxia-inducible factors and the response to hypoxic stress
    • Majmundar AJ, Wong WJ, Simon MC. (2010). Hypoxia-inducible factors and the response to hypoxic stress. Mol Cell 40:294-309.
    • (2010) Mol Cell , vol.40 , pp. 294-309
    • Majmundar, A.J.1    Wong, W.J.2    Simon, M.C.3
  • 102
    • 0035969508 scopus 로고    scopus 로고
    • Inhibitory PAS domain protein is a negative regulator of hypoxia-inducible gene expression
    • Makino Y, Cao R, Svensson K, et al. (2001). Inhibitory PAS domain protein is a negative regulator of hypoxia-inducible gene expression. Nature 414:550-4.
    • (2001) Nature , vol.414 , pp. 550-554
    • Makino, Y.1    Cao, R.2    Svensson, K.3
  • 103
    • 0037031808 scopus 로고    scopus 로고
    • Inhibitory PAS domain protein (IPAS) is a hypoxia-inducible splicing variant of the hypoxiainducible factor-3a locus
    • Makino Y, Kanopka A, Wilson WJ, et al. (2002). Inhibitory PAS domain protein (IPAS) is a hypoxia-inducible splicing variant of the hypoxiainducible factor-3a locus. J Biol Chem 277:32405-8.
    • (2002) J Biol Chem , vol.277 , pp. 32405-32408
    • Makino, Y.1    Kanopka, A.2    Wilson, W.J.3
  • 104
    • 0035903468 scopus 로고    scopus 로고
    • Independent function of two destruction domains in hypoxia-inducible factor - A chains activated by prolyl hydroxylation
    • Masson N, Willam C, Maxwell PH, et al. (2001). Independent function of two destruction domains in hypoxia-inducible factor-a chains activated by prolyl hydroxylation. EMBO J 20:5197-206.
    • (2001) EMBO J , vol.20 , pp. 5197-5206
    • Masson, N.1    Willam, C.2    Maxwell, P.H.3
  • 105
    • 24644484730 scopus 로고    scopus 로고
    • Human HIF-3a4 is a dominant-negative regulator of HIF-1 and is down-regulated in renal cell carcinoma
    • Maynard MA, Evans AJ, Hosomi T, et al. (2005). Human HIF-3a4 is a dominant-negative regulator of HIF-1 and is down-regulated in renal cell carcinoma. FASEB J 19:1396-406.
    • (2005) FASEB J , vol.19 , pp. 1396-1406
    • Maynard, M.A.1    Evans, A.J.2    Hosomi, T.3
  • 106
    • 0037837724 scopus 로고    scopus 로고
    • Multiple splice variants of the human HIF-3a locus are targets of the von Hippel-Lindau E3 ubiquitin ligase complex
    • Maynard MA, Qi H, Chung J, et al. (2003). Multiple splice variants of the human HIF-3a locus are targets of the von Hippel-Lindau E3 ubiquitin ligase complex. J Biol Chem 278:11032-40.
    • (2003) J Biol Chem , vol.278 , pp. 11032-11040
    • Maynard, M.A.1    Qi, H.2    Chung, J.3
  • 107
  • 108
    • 0033981845 scopus 로고    scopus 로고
    • ERK activation upon hypoxia: Involvement in HIF-1 activation
    • Minet E, Arnould T, Michel G, et al. (2000). ERK activation upon hypoxia: involvement in HIF-1 activation. FEBS Lett 468:53-8.
    • (2000) FEBS Lett , vol.468 , pp. 53-58
    • Minet, E.1    Arnould, T.2    Michel, G.3
  • 109
    • 67650531089 scopus 로고    scopus 로고
    • Genome-wide association of hypoxia-inducible factor (HIF)-1a and HIF-2a DNA binding with expression profiling of hypoxia-inducible transcripts
    • Mole DR, Blancher C, Copley RR, et al. (2009). Genome-wide association of hypoxia-inducible factor (HIF)-1a and HIF-2a DNA binding with expression profiling of hypoxia-inducible transcripts. J Biol Chem 284:16767-75.
    • (2009) J Biol Chem , vol.284 , pp. 16767-16775
    • Mole, D.R.1    Blancher, C.2    Copley, R.R.3
  • 110
    • 0043234256 scopus 로고    scopus 로고
    • Regulation of hypoxiainducible factor-1a protein level during hypoxic conditions by the phosphatidylinositol 3-kinase/Akt/glycogen synthase kinase 3b pathway in HepG2 cells
    • Mottet D, Dumont V, Deccache Y, et al. (2003). Regulation of hypoxiainducible factor-1a protein level during hypoxic conditions by the phosphatidylinositol 3-kinase/Akt/glycogen synthase kinase 3b pathway in HepG2 cells. J Biol Chem 278:31277-85.
    • (2003) J Biol Chem , vol.278 , pp. 31277-31285
    • Mottet, D.1    Dumont, V.2    Deccache, Y.3
  • 111
    • 33645236747 scopus 로고    scopus 로고
    • Purified recombinant hARD1 does not catalyse acetylation of Lys532 of HIF-1a fragments in vitro
    • Murray-Rust TA, Oldham NJ, Hewitson KS, et al. (2006). Purified recombinant hARD1 does not catalyse acetylation of Lys532 of HIF-1a fragments in vitro. FEBS Lett 580:1911-18.
    • (2006) FEBS Lett , vol.580 , pp. 1911-1918
    • Murray-Rust, T.A.1    Oldham, N.J.2    Hewitson, K.S.3
  • 112
    • 33845403070 scopus 로고    scopus 로고
    • Identification of MAPK phosphorylation sites and their role in the localization and activity of hypoxia-inducible factor-1a
    • Mylonis I, Chachami G, Samiotaki M, et al. (2006). Identification of MAPK phosphorylation sites and their role in the localization and activity of hypoxia-inducible factor-1a. J Biol Chem 281:33095-106.
    • (2006) J Biol Chem , vol.281 , pp. 33095-33106
    • Mylonis, I.1    Chachami, G.2    Samiotaki, M.3
  • 113
    • 84878542447 scopus 로고    scopus 로고
    • Deciphering the emerging role of SUMO conjugation in the hypoxia-signaling cascade
    • Núñez-O'Mara A, Berra E. (2013). Deciphering the emerging role of SUMO conjugation in the hypoxia-signaling cascade. Biol Chem 394: 459-69.
    • (2013) Biol Chem , vol.394 , pp. 459-469
    • Núñez-O'Mara, A.1    Berra, E.2
  • 114
    • 0033593219 scopus 로고    scopus 로고
    • Oxygen-regulated and transactivating domains in endothelial PAS protein 1: Comparison with hypoxia-inducible factor-1a
    • O'Rourke JF, Tian Y-M, Ratcliffe PJ, et al. (1999). Oxygen-regulated and transactivating domains in endothelial PAS protein 1: comparison with hypoxia-inducible factor-1a. J Biol Chem 274:2060-71.
    • (1999) J Biol Chem , vol.274 , pp. 2060-2071
    • O'rourke, J.F.1    Tian, Y.-M.2    Ratcliffe, P.J.3
  • 115
    • 0033776536 scopus 로고    scopus 로고
    • Ubiquitination of hypoxiainducible factor requires direct binding to the b-domain of the von Hippel-Lindau protein
    • Ohh M, Kaelin WG, Park CW, et al. (2000). Ubiquitination of hypoxiainducible factor requires direct binding to the b-domain of the von Hippel-Lindau protein. Nat Cell Biol 2:423-7.
    • (2000) Nat Cell Biol , vol.2 , pp. 423-427
    • Ohh, M.1    Kaelin, W.G.2    Park, C.W.3
  • 116
    • 84866070606 scopus 로고    scopus 로고
    • Hypoxic induction of the regulator of G-protein signalling 4 gene is mediated by the hypoxia-inducible factor pathway
    • Olechnowicz SWZ, Fedele AO, Peet DJ. (2012). Hypoxic induction of the regulator of G-protein signalling 4 gene is mediated by the hypoxia-inducible factor pathway. PLoS ONE 7:e44564.
    • (2012) PLoS ONE , vol.7
    • Olechnowicz, S.W.Z.1    Fedele, A.O.2    Peet, D.J.3
  • 117
    • 77952300971 scopus 로고    scopus 로고
    • Genome-wide identification of hypoxia-inducible factor binding sites and target genes by a probabilistic model integrating transcription-profiling data and in silico binding site prediction
    • Ortiz-Barahona A, Villar D, Pescador N, et al. (2010). Genome-wide identification of hypoxia-inducible factor binding sites and target genes by a probabilistic model integrating transcription-profiling data and in silico binding site prediction. Nucl Acids Res 38:2332-45.
    • (2010) Nucl Acids Res , vol.38 , pp. 2332-2345
    • Ortiz-Barahona, A.1    Villar, D.2    Pescador, N.3
  • 118
    • 79956370722 scopus 로고    scopus 로고
    • Coactivators necessary for transcriptional output of the hypoxia inducible factor, HIF, are directly recruited by ARNT PAS-B
    • Partch CL, Gardner KH. (2011). Coactivators necessary for transcriptional output of the hypoxia inducible factor, HIF, are directly recruited by ARNT PAS-B. Proc Natl Acad Sci USA 108:7739-44.
    • (2011) Proc Natl Acad Sci USA , vol.108 , pp. 7739-7744
    • Partch, C.L.1    Gardner, K.H.2
  • 119
    • 77955692247 scopus 로고    scopus 로고
    • Hypoxia-inducible factor (HIF)-3a is subject to extensive alternative splicing in human tissues and cancer cells and is regulated by HIF-1 but not HIF-2
    • Pasanen A, Heikkilä M, Rautavuoma K, et al. (2010). Hypoxia-inducible factor (HIF)-3a is subject to extensive alternative splicing in human tissues and cancer cells and is regulated by HIF-1 but not HIF-2. Int J Biochem Cell Biol 42:1189-200.
    • (2010) Int J Biochem Cell Biol , vol.42 , pp. 1189-1200
    • Pasanen, A.1    Heikkilä, M.2    Rautavuoma, K.3
  • 120
    • 84879438510 scopus 로고    scopus 로고
    • Enhanceosomes as integrators of hypoxia inducible factor (HIF) and other transcription factors in the hypoxic transcriptional response
    • Pawlus MR, Hu CJ. (2013). Enhanceosomes as integrators of hypoxia inducible factor (HIF) and other transcription factors in the hypoxic transcriptional response. Cell Signal 25:1895-903.
    • (2013) Cell Signal , vol.25 , pp. 1895-1903
    • Pawlus, M.R.1    Hu, C.J.2
  • 121
    • 84897990837 scopus 로고    scopus 로고
    • STAT3 and HIF1a cooperatively activate HIF1 target genes in MDA-MB-231 and RCC4 cells
    • Pawlus MR, Wang L, Hu CJ. (2013). STAT3 and HIF1a cooperatively activate HIF1 target genes in MDA-MB-231 and RCC4 cells. Oncogene 32:4595-610.
    • (2013) Oncogene , vol.32 , pp. 4595-4610
    • Pawlus, M.R.1    Wang, L.2    Hu, C.J.3
  • 122
    • 84868702904 scopus 로고    scopus 로고
    • Upstream stimulatory factor 2 and hypoxia-inducible factor 2a (HIF2a) cooperatively activate HIF2 target genes during hypoxia
    • Pawlus MR, Wang L, Ware K, et al. (2012). Upstream stimulatory factor 2 and hypoxia-inducible factor 2a (HIF2a) cooperatively activate HIF2 target genes during hypoxia. Mol Cell Biol 32:4595-610.
    • (2012) Mol Cell Biol , vol.32 , pp. 4595-4610
    • Pawlus, M.R.1    Wang, L.2    Ware, K.3
  • 123
    • 13944252559 scopus 로고    scopus 로고
    • Identification of membrane type-1 matrix metalloproteinase as a target of hypoxiainducible factor-2a in von Hippel-Lindau renal cell carcinoma
    • Petrella BL, Lohi J, Brinckerhoff CE. (2005). Identification of membrane type-1 matrix metalloproteinase as a target of hypoxiainducible factor-2a in von Hippel-Lindau renal cell carcinoma. Oncogene 24:1043-52.
    • (2005) Oncogene , vol.24 , pp. 1043-1052
    • Petrella, B.L.1    Lohi, J.2    Brinckerhoff, C.E.3
  • 124
    • 77951920690 scopus 로고    scopus 로고
    • C-Myc regulates transcriptional pause release
    • Rahl PB, Lin CY, Seila AC, et al. (2010). c-Myc regulates transcriptional pause release. Cell 141:432-45.
    • (2010) Cell , vol.141 , pp. 432-445
    • Rahl, P.B.1    Lin, C.Y.2    Seila, A.C.3
  • 125
    • 0032725554 scopus 로고    scopus 로고
    • P42/p44 mitogen-activated protein kinases phosphorylate hypoxia-inducible factor 1a (HIF-1a) and enhance the transcriptional activity of HIF-1
    • Richard DE, Berra E, Gothié E. (1999). p42/p44 mitogen-activated protein kinases phosphorylate hypoxia-inducible factor 1a (HIF-1a) and enhance the transcriptional activity of HIF-1. J Biol Chem 274: 32631-7.
    • (1999) J Biol Chem , vol.274 , pp. 32631-32637
    • Richard, D.E.1    Berra, E.2    Gothié, E.3
  • 126
    • 77449159578 scopus 로고    scopus 로고
    • Complex regulation of the transactivation function of hypoxia-inducible factor-1a by direct interaction with two distinct domains of the CREB-binding protein/p300
    • Ruas JL, Berchner-Pfannschmidt U, Malik S, et al. (2010). Complex regulation of the transactivation function of hypoxia-inducible factor-1a by direct interaction with two distinct domains of the CREB-binding protein/p300. J Biol Chem 285:2601-9.
    • (2010) J Biol Chem , vol.285 , pp. 2601-2609
    • Ruas, J.L.1    Berchner-Pfannschmidt, U.2    Malik, S.3
  • 127
    • 0037064141 scopus 로고    scopus 로고
    • Functional analysis of hypoxiainducible factor-1a-mediated transactivation: Identification of amino acid residues critical for transcriptional activation and/or interaction with CREB-binding protein
    • Ruas JL, Poellinger L, Pereira T. (2002). Functional analysis of hypoxiainducible factor-1a-mediated transactivation: identification of amino acid residues critical for transcriptional activation and/or interaction with CREB-binding protein. J Biol Chem 277:38723-30.
    • (2002) J Biol Chem , vol.277 , pp. 38723-38730
    • Ruas, J.L.1    Poellinger, L.2    Pereira, T.3
  • 128
    • 14044257943 scopus 로고    scopus 로고
    • Role of CBP in regulating HIF-1-mediated activation of transcription
    • Ruas JL, Poellinger L, Pereira T. (2005). Role of CBP in regulating HIF-1-mediated activation of transcription. J Cell Sci 118:301-11.
    • (2005) J Cell Sci , vol.118 , pp. 301-311
    • Ruas, J.L.1    Poellinger, L.2    Pereira, T.3
  • 129
    • 0032100732 scopus 로고    scopus 로고
    • HIF-1a is required for solid tumor formation and embryonic vascularization
    • Ryan HE, Lo J, Johnson RS. (1998). HIF-1a is required for solid tumor formation and embryonic vascularization. EMBO J 17: 3005-15.
    • (1998) EMBO J , vol.17 , pp. 3005-3015
    • Ryan, H.E.1    Lo, J.2    Johnson, R.S.3
  • 130
    • 0343278978 scopus 로고    scopus 로고
    • Isolation and characterization of AINT: A novel ARNT interacting protein expressed during murine embryonic development
    • Sadek CM, Jalaguier S, Feeney EP, et al. (2000). Isolation and characterization of AINT: a novel ARNT interacting protein expressed during murine embryonic development. Mech Dev 97:13-26.
    • (2000) Mech Dev , vol.97 , pp. 13-26
    • Sadek, C.M.1    Jalaguier, S.2    Feeney, E.P.3
  • 131
    • 44049090235 scopus 로고    scopus 로고
    • Notch signaling mediates hypoxia-induced tumor cell migration and invasion
    • Sahlgren C, Gustafsson MV, Jin S, et al. (2008). Notch signaling mediates hypoxia-induced tumor cell migration and invasion. Proc Natl Acad Sci USA 105:6392-7.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 6392-6397
    • Sahlgren, C.1    Gustafsson, M.V.2    Jin, S.3
  • 132
    • 49649090182 scopus 로고    scopus 로고
    • Regulation of hypoxia-inducible genes by ETS1 transcription factor
    • Salnikow K, Aprelikova O, Ivanov S, et al. (2008). Regulation of hypoxia-inducible genes by ETS1 transcription factor. Carcinogenesis 29:1493-9.
    • (2008) Carcinogenesis , vol.29 , pp. 1493-1499
    • Salnikow, K.1    Aprelikova, O.2    Ivanov, S.3
  • 133
    • 4644260710 scopus 로고    scopus 로고
    • Depletion of intracellular ascorbate by the carcinogenic metals nickel and cobalt results in the induction of hypoxic stress
    • Salnikow K, Donald SP, Bruick RK, et al. (2004). Depletion of intracellular ascorbate by the carcinogenic metals nickel and cobalt results in the induction of hypoxic stress. J Biol Chem 279: 40337-44.
    • (2004) J Biol Chem , vol.279 , pp. 40337-40344
    • Salnikow, K.1    Donald, S.P.2    Bruick, R.K.3
  • 134
    • 84882239297 scopus 로고    scopus 로고
    • Pan-genomic binding of hypoxia-inducible transcription factors
    • Schödel J, Mole DR, Ratcliffe PJ. (2013). Pan-genomic binding of hypoxia-inducible transcription factors. Biol Chem 394:507-17.
    • (2013) Biol Chem , vol.394 , pp. 507-517
    • Schödel, J.1    Mole, D.R.2    Ratcliffe, P.J.3
  • 135
    • 79959450883 scopus 로고    scopus 로고
    • Highresolution genome-wide mapping of HIF-binding sites by ChIP-seq
    • Schödel J, Oikonomopoulos S, Ragoussis J, et al. (2011). Highresolution genome-wide mapping of HIF-binding sites by ChIP-seq. Blood 117:e207-17.
    • (2011) Blood , vol.117
    • Schödel, J.1    Oikonomopoulos, S.2    Ragoussis, J.3
  • 136
    • 0041440036 scopus 로고    scopus 로고
    • The HIF family member EPAS1/HIF-2a is required for normal hematopoiesis in mice
    • Scortegagna M, Morris MA, Oktay Y, et al. (2003). The HIF family member EPAS1/HIF-2a is required for normal hematopoiesis in mice. Blood 102:1634-40.
    • (2003) Blood , vol.102 , pp. 1634-1640
    • Scortegagna, M.1    Morris, M.A.2    Oktay, Y.3
  • 137
    • 84856739946 scopus 로고    scopus 로고
    • Hypoxia-inducible factors in physiology and medicine
    • Semenza GL. (2012a). Hypoxia-inducible factors in physiology and medicine. Cell 148:399-408.
    • (2012) Cell , vol.148 , pp. 399-408
    • Semenza, G.L.1
  • 138
    • 84859445000 scopus 로고    scopus 로고
    • Hypoxia-inducible factors: Mediators of cancer progression and targets for cancer therapy
    • Semenza GL. (2012b). Hypoxia-inducible factors: mediators of cancer progression and targets for cancer therapy. Trends Pharmacol Sci 33: 207-14.
    • (2012) Trends Pharmacol Sci , vol.33 , pp. 207-214
    • Semenza, G.L.1
  • 139
    • 0026468180 scopus 로고
    • A nuclear factor induced by hypoxia via de novo protein synthesis binds to the human erythropoietin gene enhancer at a site required for transcriptional activation
    • Semenza GL, Wang GL. (1992). A nuclear factor induced by hypoxia via de novo protein synthesis binds to the human erythropoietin gene enhancer at a site required for transcriptional activation. Mol Cell Biol 12:5447-54.
    • (1992) Mol Cell Biol , vol.12 , pp. 5447-5454
    • Semenza, G.L.1    Wang, G.L.2
  • 140
    • 3343013829 scopus 로고    scopus 로고
    • Endothelial PAS domain protein 1 gene promotes angiogenesis through the transactivation of both vascular endothelial growth factor and its receptor, Flt-1
    • Takeda N, Maemura K, Imai Y, et al. (2004). Endothelial PAS domain protein 1 gene promotes angiogenesis through the transactivation of both vascular endothelial growth factor and its receptor, Flt-1. Circ Res 95:146-53.
    • (2004) Circ Res , vol.95 , pp. 146-153
    • Takeda, N.1    Maemura, K.2    Imai, Y.3
  • 141
    • 7944224442 scopus 로고    scopus 로고
    • Loss of HIF-1a in endothelial cells disrupts a hypoxia-driven VEGF autocrine loop necessary for tumorigenesis
    • Tang N, Wang L, Esko J, et al. (2004). Loss of HIF-1a in endothelial cells disrupts a hypoxia-driven VEGF autocrine loop necessary for tumorigenesis. Cancer Cell 6:485-95.
    • (2004) Cancer Cell , vol.6 , pp. 485-495
    • Tang, N.1    Wang, L.2    Esko, J.3
  • 142
    • 0034663894 scopus 로고    scopus 로고
    • Mechanism of regulation of the hypoxia-inducible factor-1a by the von Hippel- Lindau tumor suppressor protein
    • Tanimoto K, Makino Y, Pereira T, et al. (2000). Mechanism of regulation of the hypoxia-inducible factor-1a by the von Hippel- Lindau tumor suppressor protein. EMBO J 19:4298-309.
    • (2000) EMBO J , vol.19 , pp. 4298-4309
    • Tanimoto, K.1    Makino, Y.2    Pereira, T.3
  • 143
    • 0032213236 scopus 로고    scopus 로고
    • The hypoxiaresponsive transcription factor EPAS1 is essential for catecholamine homeostasis and protection against heart failure during embryonic development
    • Tian H, Hammer RE, Matsumoto AM, et al. (1998). The hypoxiaresponsive transcription factor EPAS1 is essential for catecholamine homeostasis and protection against heart failure during embryonic development. Genes Dev 12:3320-4.
    • (1998) Genes Dev , vol.12 , pp. 3320-3324
    • Tian, H.1    Hammer, R.E.2    Matsumoto, A.M.3
  • 144
    • 0031020884 scopus 로고    scopus 로고
    • Endothelial PAS domain protein 1 (EPAS1), a transcription factor selectively expressed in endothelial cells
    • Tian H, Mcknight SL, Russell DW. (1997). Endothelial PAS domain protein 1 (EPAS1), a transcription factor selectively expressed in endothelial cells. Genes Dev 11:72-82.
    • (1997) Genes Dev , vol.11 , pp. 72-82
    • Tian, H.1    McKnight, S.L.2    Russell, D.W.3
  • 145
    • 2642518857 scopus 로고    scopus 로고
    • Identification of the CREB-binding protein/p300-interacting protein CITED2 as a peroxisome proliferator-activated receptor alpha coregulator
    • Tien ES, Davis JW, Vanden Heuvel JP. (2004). Identification of the CREB-binding protein/p300-interacting protein CITED2 as a peroxisome proliferator-activated receptor alpha coregulator. J Biol Chem 279:24053-63.
    • (2004) J Biol Chem , vol.279 , pp. 24053-24063
    • Tien, E.S.1    Davis, J.W.2    Vanden Heuvel, J.P.3
  • 146
    • 34848884803 scopus 로고    scopus 로고
    • Intermittent hypoxia changes HIF-1a phosphorylation pattern in endothelial cells: Unravelling of a new PKA-dependent regulation of HIF-1a
    • Toffoli S, Feron O, Raes M, et al. (2007). Intermittent hypoxia changes HIF-1a phosphorylation pattern in endothelial cells: unravelling of a new PKA-dependent regulation of HIF-1a. BBA-Mol Cell Res 1773: 1558-71.
    • (2007) BBA-Mol Cell Res , vol.1773 , pp. 1558-1571
    • Toffoli, S.1    Feron, O.2    Raes, M.3
  • 147
    • 84870941135 scopus 로고    scopus 로고
    • Hypoxia-regulated target genes implicated in tumor metastasis
    • doi:10.1186/1423-0127-19- 102
    • Tsai Y-P, Wu K-J. (2012). Hypoxia-regulated target genes implicated in tumor metastasis. J Biomed Sci 19:102. doi:10.1186/1423-0127-19- 102.
    • (2012) J Biomed Sci , vol.19 , pp. 102
    • Tsai, Y.-P.1    Wu, K.-J.2
  • 148
    • 84866658759 scopus 로고    scopus 로고
    • Cooperativity of stress-responsive transcription factors in core hypoxia- inducible factor binding regions
    • Villar D, Ortiz-Barahona A, Gómez-Maldonado L, et al. (2012). Cooperativity of stress-responsive transcription factors in core hypoxia- inducible factor binding regions. PLoS ONE 7:e45708.
    • (2012) PLoS ONE , vol.7
    • Villar, D.1    Ortiz-Barahona, A.2    Gómez-Maldonado, L.3
  • 149
    • 8744302175 scopus 로고    scopus 로고
    • Roles of Brahma and Brahma/SWI2-related gene 1 in hypoxic induction of the erythropoietin gene
    • Wang F, Zhang R, Beischlag TV, et al. (2004a). Roles of Brahma and Brahma/SWI2-related gene 1 in hypoxic induction of the erythropoietin gene. J Biol Chem 279:46733-41.
    • (2004) J Biol Chem , vol.279 , pp. 46733-46741
    • Wang, F.1    Zhang, R.2    Beischlag, T.V.3
  • 150
    • 1842640322 scopus 로고    scopus 로고
    • Role of mediator in transcriptional activation by the aryl hydrocarbon receptor
    • Wang S, Ge K, Roeder RG, et al. (2004b). Role of mediator in transcriptional activation by the aryl hydrocarbon receptor. J Biol Chem 279:13593-600.
    • (2004) J Biol Chem , vol.279 , pp. 13593-13600
    • Wang, S.1    Ge, K.2    Roeder, R.G.3
  • 151
    • 77956322192 scopus 로고    scopus 로고
    • Roles of coactivators in hypoxic induction of the erythropoietin gene
    • Wang F, Zhang R, Wu X, et al. (2010a). Roles of coactivators in hypoxic induction of the erythropoietin gene. PLoS ONE 5:e10002.
    • (2010) PLoS ONE , vol.5
    • Wang, F.1    Zhang, R.2    Wu, X.3
  • 152
    • 0029051439 scopus 로고
    • Hypoxia-inducible factor 1 is a basic-helix-loop-helix-PAS heterodimer regulated by cellular O2 tension
    • Wang GL, Jiang BH, Rue EA, et al. (1995). Hypoxia-inducible factor 1 is a basic-helix-loop-helix-PAS heterodimer regulated by cellular O2 tension. Proc Natl Acad Sci USA 92:5510-14.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 5510-5514
    • Wang, G.L.1    Jiang, B.H.2    Rue, E.A.3
  • 153
    • 0027427588 scopus 로고
    • Characterization of hypoxia-inducible factor 1 and regulation of DNA binding activity by hypoxia
    • Wang GL, Semenza GL. (1993a). Characterization of hypoxia-inducible factor 1 and regulation of DNA binding activity by hypoxia. J Biol Chem 268:21513-18.
    • (1993) J Biol Chem , vol.268 , pp. 21513-21518
    • Wang, G.L.1    Semenza, G.L.2
  • 154
    • 0027210562 scopus 로고
    • General involvement of hypoxiainducible factor 1 in transcriptional response to hypoxia
    • Wang GL, Semenza GL. (1993b). General involvement of hypoxiainducible factor 1 in transcriptional response to hypoxia. Proc Natl Acad Sci USA 90:4304-8.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 4304-4308
    • Wang, G.L.1    Semenza, G.L.2
  • 155
    • 0028816847 scopus 로고
    • Purification and characterization of hypoxia-inducible factor 1
    • Wang GL, Semenza GL. (1995). Purification and characterization of hypoxia-inducible factor 1. J Biol Chem 270:1230-7.
    • (1995) J Biol Chem , vol.270 , pp. 1230-1237
    • Wang, G.L.1    Semenza, G.L.2
  • 156
    • 33845674064 scopus 로고    scopus 로고
    • Transcriptional regulation of APH-1A and increased gamma-secretase cleavage of APP and Notch by HIF-1 and hypoxia
    • Wang R, Zhang YW, Zhang X, et al. (2006). Transcriptional regulation of APH-1A and increased gamma-secretase cleavage of APP and Notch by HIF-1 and hypoxia. FASEB J 20:1275-7.
    • (2006) FASEB J , vol.20 , pp. 1275-1277
    • Wang, R.1    Zhang, Y.W.2    Zhang, X.3
  • 157
    • 77949689094 scopus 로고    scopus 로고
    • Characterization of the activation of protein tyrosine phosphatase, receptor-type, Z polypeptide 1 (PTPRZ1) by hypoxia inducible factor-2 alpha
    • doi:10.1371/journal.pone.0009641
    • Wang V, Davis DA, Veeranna RP, et al. (2010b). Characterization of the activation of protein tyrosine phosphatase, receptor-type, Z polypeptide 1 (PTPRZ1) by hypoxia inducible factor-2 alpha. PLoS ONE. 5: e9641. doi:10.1371/journal.pone.0009641.
    • (2010) PLoS ONE. , vol.5
    • Wang, V.1    Davis, D.A.2    Veeranna, R.P.3
  • 158
    • 44749093281 scopus 로고    scopus 로고
    • The specific contribution of hypoxia-inducible factor-2a to hypoxic gene expression in vitro is limited and modulated by cell type-specific and exogenous factors
    • Warnecke C, Weidemann A, Volke M, et al. (2008). The specific contribution of hypoxia-inducible factor-2a to hypoxic gene expression in vitro is limited and modulated by cell type-specific and exogenous factors. Exp Cell Res 314:2016-27.
    • (2008) Exp Cell Res , vol.314 , pp. 2016-2027
    • Warnecke, C.1    Weidemann, A.2    Volke, M.3
  • 159
    • 31444444162 scopus 로고    scopus 로고
    • Integration of oxygen signaling at the consensus HRE
    • Wenger RH, Stiehl DP, Camenisch G. (2005). Integration of oxygen signaling at the consensus HRE. Sci STKE 306:re12.
    • (2005) Sci STKE , vol.306
    • Wenger, R.H.1    Stiehl, D.P.2    Camenisch, G.3
  • 160
    • 80053645045 scopus 로고    scopus 로고
    • Hypoxia-inducible factor 1 is a master regulator of breast cancer metastatic niche formation
    • Wong CC-L, Gilkes DM, Zhang H, et al. (2011). Hypoxia-inducible factor 1 is a master regulator of breast cancer metastatic niche formation. Proc Natl Acad Sci USA 108:16369-74.
    • (2011) Proc Natl Acad Sci USA , vol.108 , pp. 16369-16374
    • Cc-L, W.1    Gilkes, D.M.2    Zhang, H.3
  • 161
    • 53249088036 scopus 로고    scopus 로고
    • PCAF is an HIF-1a cofactor that regulates p53 transcriptional activity in hypoxia
    • Xenaki G, Ontikatze T, Rajendran R, et al. (2008). PCAF is an HIF-1a cofactor that regulates p53 transcriptional activity in hypoxia. Oncogene 27:5785-96.
    • (2008) Oncogene , vol.27 , pp. 5785-5796
    • Xenaki, G.1    Ontikatze, T.2    Rajendran, R.3
  • 162
    • 75349114759 scopus 로고    scopus 로고
    • Preferential binding of HIF-1 to transcriptionally active loci determines cell-type specific response to hypoxia
    • Xia X, Kung AL. (2009). Preferential binding of HIF-1 to transcriptionally active loci determines cell-type specific response to hypoxia. Genome Biol 10:R113.
    • (2009) Genome Biol , vol.10
    • Xia, X.1    Kung, A.L.2
  • 163
    • 78649814934 scopus 로고    scopus 로고
    • Plk3 functions as an essential component of the hypoxia regulatory pathway by direct phosphorylation of HIF-1
    • Xu D, Yao Y, Lu L, et al. (2010). Plk3 functions as an essential component of the hypoxia regulatory pathway by direct phosphorylation of HIF-1. J Biol Chem 285:38944-50.
    • (2010) J Biol Chem , vol.285 , pp. 38944-38950
    • Xu, D.1    Yao, Y.2    Lu, L.3
  • 164
    • 38949147367 scopus 로고    scopus 로고
    • Abnormal heart development and lung remodeling in mice lacking the hypoxiainducible factor-related basic helix-loop-helix PAS protein NEPAS
    • Yamashita T, Ohneda O, Nagano M, et al. (2008). Abnormal heart development and lung remodeling in mice lacking the hypoxiainducible factor-related basic helix-loop-helix PAS protein NEPAS. Mol Cell Biol 28:1285-97.
    • (2008) Mol Cell Biol , vol.28 , pp. 1285-1297
    • Yamashita, T.1    Ohneda, O.2    Nagano, M.3
  • 165
    • 40249113328 scopus 로고    scopus 로고
    • Direct regulation of TWIST by HIF-1a promotes metastasis
    • Yang MH, Wu MZ, Chiou SH, et al. (2008). Direct regulation of TWIST by HIF-1a promotes metastasis. Nat Cell Biol 10:295-305.
    • (2008) Nat Cell Biol , vol.10 , pp. 295-305
    • Yang, M.H.1    Wu, M.Z.2    Chiou, S.H.3
  • 166
    • 82555170271 scopus 로고    scopus 로고
    • Nuclear PKM2 regulates b-catenin transactivation upon EGFR activation
    • Yang W, Xia Y, Ji H, et al. (2011). Nuclear PKM2 regulates b-catenin transactivation upon EGFR activation. Nature 480:118-22.
    • (2011) Nature , vol.480 , pp. 118-122
    • Yang, W.1    Xia, Y.2    Ji, H.3
  • 167
    • 0042564792 scopus 로고    scopus 로고
    • S-nitrosation of Cys-800 of HIF-1a protein activates its interaction with p300 and stimulates its transcriptional activity
    • Yasinska IM, Sumbayev VV. (2003). S-nitrosation of Cys-800 of HIF-1a protein activates its interaction with p300 and stimulates its transcriptional activity. FEBS Lett 549:105-09.
    • (2003) FEBS Lett , vol.549 , pp. 105-109
    • Yasinska, I.M.1    Sumbayev, V.V.2
  • 168
    • 80053371042 scopus 로고    scopus 로고
    • CITED2 controls the hypoxic signaling by snatching p300 from the two distinct activation domains of HIF-1a
    • Yoon H, Lim J-H, Cho C-H, et al. (2011). CITED2 controls the hypoxic signaling by snatching p300 from the two distinct activation domains of HIF-1a. Biochim Biophys Acta 1813:2008-16.
    • (2011) Biochim Biophys Acta , vol.1813 , pp. 2008-2016
    • Yoon, H.1    Lim, J.-H.2    Cho, C.-H.3
  • 169
    • 4644275138 scopus 로고    scopus 로고
    • HIF-1: The knowns and unknowns of hypoxia sensing
    • Zagórska A, Dulak J. (2004). HIF-1: the knowns and unknowns of hypoxia sensing. Acta Biochimica Polonica 51:563-85.
    • (2004) Acta Biochimica Polonica , vol.51 , pp. 563-585
    • Zagórska, A.1    Dulak, J.2
  • 170
    • 42149117769 scopus 로고    scopus 로고
    • Interaction with factor inhibiting HIF-1 defines an additional mode of cross-coupling between the Notch and hypoxia signaling pathways
    • Zheng X, Linke S, Dias JM, et al. (2008). Interaction with factor inhibiting HIF-1 defines an additional mode of cross-coupling between the Notch and hypoxia signaling pathways. Proc Natl Acad Sci USA 105:3368-73.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 3368-3373
    • Zheng, X.1    Linke, S.2    Dias, J.M.3
  • 171
    • 74549142287 scopus 로고    scopus 로고
    • The histone deacetylase Sirt6 regulates glucose homeostasis via Hif1a
    • Zhong L, D'Urso A, Toiber D, et al. (2010). The histone deacetylase Sirt6 regulates glucose homeostasis via Hif1a. Cell 140:280-93.
    • (2010) Cell , vol.140 , pp. 280-293
    • Zhong, L.1    D'urso, A.2    Toiber, D.3
  • 172
    • 6944236323 scopus 로고    scopus 로고
    • Ref-1/Ape is critical for formation of the hypoxia-inducible transcriptional complex on the hypoxic response element of the rat pulmonary artery endothelial cell VEGF gene
    • Ziel KA, Campbell CC, Wilson GL, et al. (2004). Ref-1/Ape is critical for formation of the hypoxia-inducible transcriptional complex on the hypoxic response element of the rat pulmonary artery endothelial cell VEGF gene. FASEB J 18:986-8.
    • (2004) FASEB J , vol.18 , pp. 986-988
    • Ziel, K.A.1    Campbell, C.C.2    Wilson, G.L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.