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Volumn 8, Issue 4, 2013, Pages

Nuclear Localization of the Mitochondrial Factor HIGD1A during Metabolic Stress

Author keywords

[No Author keywords available]

Indexed keywords

ETOPOSIDE; HYPOXIA INDUCIBLE FACTOR 1ALPHA; HYPOXIA INDUCIBLE GENE DOMAIN 1A PROTEIN; MITOCHONDRIAL PROTEIN; PROTEIN BAX; UNCLASSIFIED DRUG; HIG1 PROTEIN, HUMAN; PROTEIN BAK; PROTEIN BINDING; TUMOR PROTEIN;

EID: 84877001869     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0062758     Document Type: Article
Times cited : (32)

References (69)
  • 1
    • 0034464872 scopus 로고    scopus 로고
    • Hypoxia, HIF-1, and the pathophysiology of common human diseases
    • Semenza GL, Agani F, Feldser D, Iyer N, Kotch L, et al. (2000) Hypoxia, HIF-1, and the pathophysiology of common human diseases. Adv Exp Med Biol 475: 123-130.
    • (2000) Adv Exp Med Biol , vol.475 , pp. 123-130
    • Semenza, G.L.1    Agani, F.2    Feldser, D.3    Iyer, N.4    Kotch, L.5
  • 2
    • 49249090437 scopus 로고    scopus 로고
    • Anoxic cell core can promote necrotic cell death in cardiomyocytes at physiological extracellular PO2
    • Takahashi E, (2008) Anoxic cell core can promote necrotic cell death in cardiomyocytes at physiological extracellular PO2. Am J Physiol Heart Circ Physiol 294: H2507-2515.
    • (2008) Am J Physiol Heart Circ Physiol , vol.294
    • Takahashi, E.1
  • 4
    • 40949088023 scopus 로고    scopus 로고
    • Role of hypoxia-inducible factor in cell survival during myocardial ischemia-reperfusion
    • Loor G, Schumacker PT, (2008) Role of hypoxia-inducible factor in cell survival during myocardial ischemia-reperfusion. Cell Death Differ 15: 686-690.
    • (2008) Cell Death Differ , vol.15 , pp. 686-690
    • Loor, G.1    Schumacker, P.T.2
  • 5
    • 80051625243 scopus 로고    scopus 로고
    • Oxygen sensing, homeostasis, and disease
    • Semenza GL, (2011) Oxygen sensing, homeostasis, and disease. N Engl J Med 365: 537-547.
    • (2011) N Engl J Med , vol.365 , pp. 537-547
    • Semenza, G.L.1
  • 6
    • 43649093915 scopus 로고    scopus 로고
    • Oxygen sensing by metazoans: the central role of the HIF hydroxylase pathway
    • Kaelin WG Jr, Ratcliffe PJ, (2008) Oxygen sensing by metazoans: the central role of the HIF hydroxylase pathway. Mol Cell 30: 393-402.
    • (2008) Mol Cell , vol.30 , pp. 393-402
    • Kaelin Jr., W.G.1    Ratcliffe, P.J.2
  • 7
    • 0030943461 scopus 로고    scopus 로고
    • Abnormal angiogenesis and responses to glucose and oxygen deprivation in mice lacking the protein ARNT
    • Maltepe E, Schmidt JV, Baunoch D, Bradfield CA, Simon MC, (1997) Abnormal angiogenesis and responses to glucose and oxygen deprivation in mice lacking the protein ARNT. Nature 386: 403-407.
    • (1997) Nature , vol.386 , pp. 403-407
    • Maltepe, E.1    Schmidt, J.V.2    Baunoch, D.3    Bradfield, C.A.4    Simon, M.C.5
  • 8
    • 82355191512 scopus 로고    scopus 로고
    • Disruption of HIF-1alpha in hepatocytes impairs glucose metabolism in diet-induced obesity mice
    • Ochiai D, Goda N, Hishiki T, Kanai M, Senoo-Matsuda N, et al. (2011) Disruption of HIF-1alpha in hepatocytes impairs glucose metabolism in diet-induced obesity mice. Biochem Biophys Res Commun 415: 445-449.
    • (2011) Biochem Biophys Res Commun , vol.415 , pp. 445-449
    • Ochiai, D.1    Goda, N.2    Hishiki, T.3    Kanai, M.4    Senoo-Matsuda, N.5
  • 9
    • 17944375360 scopus 로고    scopus 로고
    • C. elegans EGL-9 and mammalian homologs define a family of dioxygenases that regulate HIF by prolyl hydroxylation
    • Epstein AC, Gleadle JM, McNeill LA, Hewitson KS, O'Rourke J, et al. (2001) C. elegans EGL-9 and mammalian homologs define a family of dioxygenases that regulate HIF by prolyl hydroxylation. Cell 107: 43-54.
    • (2001) Cell , vol.107 , pp. 43-54
    • Epstein, A.C.1    Gleadle, J.M.2    McNeill, L.A.3    Hewitson, K.S.4    O'Rourke, J.5
  • 10
    • 0035917313 scopus 로고    scopus 로고
    • HIFalpha targeted for VHL-mediated destruction by proline hydroxylation: implications for O2 sensing
    • Ivan M, Kondo K, Yang H, Kim W, Valiando J, et al. (2001) HIFalpha targeted for VHL-mediated destruction by proline hydroxylation: implications for O2 sensing. Science 292: 464-468.
    • (2001) Science , vol.292 , pp. 464-468
    • Ivan, M.1    Kondo, K.2    Yang, H.3    Kim, W.4    Valiando, J.5
  • 11
    • 0035834409 scopus 로고    scopus 로고
    • A conserved family of prolyl-4-hydroxylases that modify HIF
    • Bruick RK, McKnight SL, (2001) A conserved family of prolyl-4-hydroxylases that modify HIF. Science 294: 1337-1340.
    • (2001) Science , vol.294 , pp. 1337-1340
    • Bruick, R.K.1    McKnight, S.L.2
  • 13
    • 81555202624 scopus 로고    scopus 로고
    • Oxygen, a Key Factor Regulating Cell Behavior during Neurogenesis and Cerebral Diseases
    • Zhang K, Zhu L, Fan M, (2011) Oxygen, a Key Factor Regulating Cell Behavior during Neurogenesis and Cerebral Diseases. Front Mol Neurosci 4: 5.
    • (2011) Front Mol Neurosci , vol.4 , pp. 5
    • Zhang, K.1    Zhu, L.2    Fan, M.3
  • 15
    • 71649094085 scopus 로고    scopus 로고
    • The role of hypoxia in development of the Mammalian embryo
    • Dunwoodie SL, (2009) The role of hypoxia in development of the Mammalian embryo. Dev Cell 17: 755-773.
    • (2009) Dev Cell , vol.17 , pp. 755-773
    • Dunwoodie, S.L.1
  • 16
    • 61949143204 scopus 로고    scopus 로고
    • Oxygen in health and disease: regulation of oxygen homeostasis-clinical implications
    • Maltepe E, Saugstad OD, (2009) Oxygen in health and disease: regulation of oxygen homeostasis-clinical implications. Pediatr Res 65: 261-268.
    • (2009) Pediatr Res , vol.65 , pp. 261-268
    • Maltepe, E.1    Saugstad, O.D.2
  • 18
    • 57049172037 scopus 로고    scopus 로고
    • Bnip3 functions as a mitochondrial sensor of oxidative stress during myocardial ischemia and reperfusion
    • Kubli DA, Quinsay MN, Huang C, Lee Y, Gustafsson AB, (2008) Bnip3 functions as a mitochondrial sensor of oxidative stress during myocardial ischemia and reperfusion. Am J Physiol Heart Circ Physiol 295: H2025-2031.
    • (2008) Am J Physiol Heart Circ Physiol , vol.295
    • Kubli, D.A.1    Quinsay, M.N.2    Huang, C.3    Lee, Y.4    Gustafsson, A.B.5
  • 19
    • 17144416875 scopus 로고    scopus 로고
    • Anoxia is necessary for tumor cell toxicity caused by a low-oxygen environment
    • Papandreou I, Krishna C, Kaper F, Cai D, Giaccia AJ, et al. (2005) Anoxia is necessary for tumor cell toxicity caused by a low-oxygen environment. Cancer Res 65: 3171-3178.
    • (2005) Cancer Res , vol.65 , pp. 3171-3178
    • Papandreou, I.1    Krishna, C.2    Kaper, F.3    Cai, D.4    Giaccia, A.J.5
  • 20
    • 33846094145 scopus 로고    scopus 로고
    • Selective silencing of the hypoxia-inducible factor 1 target gene BNIP3 by histone deacetylation and methylation in colorectal cancer
    • Bacon AL, Fox S, Turley H, Harris AL, (2007) Selective silencing of the hypoxia-inducible factor 1 target gene BNIP3 by histone deacetylation and methylation in colorectal cancer. Oncogene 26: 132-141.
    • (2007) Oncogene , vol.26 , pp. 132-141
    • Bacon, A.L.1    Fox, S.2    Turley, H.3    Harris, A.L.4
  • 21
    • 0030025773 scopus 로고    scopus 로고
    • Hypoxia-mediated selection of cells with diminished apoptotic potential in solid tumours
    • Graeber TG, Osmanian C, Jacks T, Housman DE, Koch CJ, et al. (1996) Hypoxia-mediated selection of cells with diminished apoptotic potential in solid tumours. Nature 379: 88-91.
    • (1996) Nature , vol.379 , pp. 88-91
    • Graeber, T.G.1    Osmanian, C.2    Jacks, T.3    Housman, D.E.4    Koch, C.J.5
  • 22
    • 3442888541 scopus 로고    scopus 로고
    • Silencing of the hypoxia-inducible cell death protein BNIP3 in pancreatic cancer
    • Okami J, Simeone DM, Logsdon CD, (2004) Silencing of the hypoxia-inducible cell death protein BNIP3 in pancreatic cancer. Cancer Res 64: 5338-5346.
    • (2004) Cancer Res , vol.64 , pp. 5338-5346
    • Okami, J.1    Simeone, D.M.2    Logsdon, C.D.3
  • 23
    • 77951901715 scopus 로고    scopus 로고
    • Cell death in the pathogenesis of heart disease: mechanisms and significance
    • Whelan RS, Kaplinskiy V, Kitsis RN, (2010) Cell death in the pathogenesis of heart disease: mechanisms and significance. Annu Rev Physiol 72: 19-44.
    • (2010) Annu Rev Physiol , vol.72 , pp. 19-44
    • Whelan, R.S.1    Kaplinskiy, V.2    Kitsis, R.N.3
  • 25
    • 0033258120 scopus 로고    scopus 로고
    • Bcl-2 proteins: regulators of apoptosis or of mitochondrial homeostasis?
    • Vander Heiden MG, Thompson CB, (1999) Bcl-2 proteins: regulators of apoptosis or of mitochondrial homeostasis? Nat Cell Biol 1: E209-216.
    • (1999) Nat Cell Biol , vol.1
    • Vander Heiden, M.G.1    Thompson, C.B.2
  • 26
    • 33750619845 scopus 로고    scopus 로고
    • How do Bax and Bak lead to permeabilization of the outer mitochondrial membrane?
    • Antignani A, Youle RJ, (2006) How do Bax and Bak lead to permeabilization of the outer mitochondrial membrane? Curr Opin Cell Biol 18: 685-689.
    • (2006) Curr Opin Cell Biol , vol.18 , pp. 685-689
    • Antignani, A.1    Youle, R.J.2
  • 28
    • 57649171241 scopus 로고    scopus 로고
    • Human glyceraldehyde-3-phosphate dehydrogenase plays a direct role in reactivating oxidized forms of the DNA repair enzyme APE1
    • Azam S, Jouvet N, Jilani A, Vongsamphanh R, Yang X, et al. (2008) Human glyceraldehyde-3-phosphate dehydrogenase plays a direct role in reactivating oxidized forms of the DNA repair enzyme APE1. J Biol Chem 283: 30632-30641.
    • (2008) J Biol Chem , vol.283 , pp. 30632-30641
    • Azam, S.1    Jouvet, N.2    Jilani, A.3    Vongsamphanh, R.4    Yang, X.5
  • 29
    • 65249176434 scopus 로고    scopus 로고
    • BNIP3 (Bcl-2 19 kDa interacting protein) acts as transcriptional repressor of apoptosis-inducing factor expression preventing cell death in human malignant gliomas
    • Burton TR, Eisenstat DD, Gibson SB, (2009) BNIP3 (Bcl-2 19 kDa interacting protein) acts as transcriptional repressor of apoptosis-inducing factor expression preventing cell death in human malignant gliomas. J Neurosci 29: 4189-4199.
    • (2009) J Neurosci , vol.29 , pp. 4189-4199
    • Burton, T.R.1    Eisenstat, D.D.2    Gibson, S.B.3
  • 30
    • 33644870946 scopus 로고    scopus 로고
    • The pro-cell death Bcl-2 family member, BNIP3, is localized to the nucleus of human glial cells: Implications for glioblastoma multiforme tumor cell survival under hypoxia
    • Burton TR, Henson ES, Baijal P, Eisenstat DD, Gibson SB, (2006) The pro-cell death Bcl-2 family member, BNIP3, is localized to the nucleus of human glial cells: Implications for glioblastoma multiforme tumor cell survival under hypoxia. Int J Cancer 118: 1660-1669.
    • (2006) Int J Cancer , vol.118 , pp. 1660-1669
    • Burton, T.R.1    Henson, E.S.2    Baijal, P.3    Eisenstat, D.D.4    Gibson, S.B.5
  • 31
    • 32344448727 scopus 로고    scopus 로고
    • Nuclear translocation and overexpression of GAPDH by the hyper-pressure in retinal ganglion cell
    • Kim CI, Lee SH, Seong GJ, Kim YH, Lee MY, (2006) Nuclear translocation and overexpression of GAPDH by the hyper-pressure in retinal ganglion cell. Biochem Biophys Res Commun 341: 1237-1243.
    • (2006) Biochem Biophys Res Commun , vol.341 , pp. 1237-1243
    • Kim, C.I.1    Lee, S.H.2    Seong, G.J.3    Kim, Y.H.4    Lee, M.Y.5
  • 32
    • 0037131519 scopus 로고    scopus 로고
    • Dueling activities of AIF in cell death versus survival: DNA binding and redox activity
    • Lipton SA, Bossy-Wetzel E, (2002) Dueling activities of AIF in cell death versus survival: DNA binding and redox activity. Cell 111: 147-150.
    • (2002) Cell , vol.111 , pp. 147-150
    • Lipton, S.A.1    Bossy-Wetzel, E.2
  • 33
    • 0027214981 scopus 로고
    • Glycolytic enzymes as DNA binding proteins
    • Ronai Z, (1993) Glycolytic enzymes as DNA binding proteins. Int J Biochem 25: 1073-1076.
    • (1993) Int J Biochem , vol.25 , pp. 1073-1076
    • Ronai, Z.1
  • 34
    • 0030868934 scopus 로고    scopus 로고
    • Glyceraldehyde-3-phosphate dehydrogenase: nuclear translocation participates in neuronal and nonneuronal cell death
    • Sawa A, Khan AA, Hester LD, Snyder SH, (1997) Glyceraldehyde-3-phosphate dehydrogenase: nuclear translocation participates in neuronal and nonneuronal cell death. Proc Natl Acad Sci U S A 94: 11669-11674.
    • (1997) Proc Natl Acad Sci U S A , vol.94 , pp. 11669-11674
    • Sawa, A.1    Khan, A.A.2    Hester, L.D.3    Snyder, S.H.4
  • 35
    • 1242314873 scopus 로고    scopus 로고
    • Nuclear localization of the hypoxia-regulated pro-apoptotic protein BNIP3 after global brain ischemia in the rat hippocampus
    • Schmidt-Kastner R, Aguirre-Chen C, Kietzmann T, Saul I, Busto R, et al. (2004) Nuclear localization of the hypoxia-regulated pro-apoptotic protein BNIP3 after global brain ischemia in the rat hippocampus. Brain Res 1001: 133-142.
    • (2004) Brain Res , vol.1001 , pp. 133-142
    • Schmidt-Kastner, R.1    Aguirre-Chen, C.2    Kietzmann, T.3    Saul, I.4    Busto, R.5
  • 36
    • 77952396366 scopus 로고    scopus 로고
    • Nuclear translocation of mitochondrial cytochrome c, lysosomal cathepsins B and D, and three other death-promoting proteins within the first 60 minutes of generalized seizures
    • Zhao S, Aviles ER Jr, Fujikawa DG, (2010) Nuclear translocation of mitochondrial cytochrome c, lysosomal cathepsins B and D, and three other death-promoting proteins within the first 60 minutes of generalized seizures. J Neurosci Res 88: 1727-1737.
    • (2010) J Neurosci Res , vol.88 , pp. 1727-1737
    • Zhao, S.1    Aviles Jr., E.R.2    Fujikawa, D.G.3
  • 37
    • 0033970086 scopus 로고    scopus 로고
    • Epigenetic regulation of gene expression in cervical cancer cells by the tumor microenvironment
    • Denko N, Schindler C, Koong A, Laderoute K, Green C, et al. (2000) Epigenetic regulation of gene expression in cervical cancer cells by the tumor microenvironment. Clin Cancer Res 6: 480-487.
    • (2000) Clin Cancer Res , vol.6 , pp. 480-487
    • Denko, N.1    Schindler, C.2    Koong, A.3    Laderoute, K.4    Green, C.5
  • 38
    • 0036807952 scopus 로고    scopus 로고
    • cDNA microarray analysis of changes in gene expression induced by neuronal hypoxia in vitro
    • Jin K, Mao XO, Eshoo MW, del Rio G, Rao R, et al. (2002) cDNA microarray analysis of changes in gene expression induced by neuronal hypoxia in vitro. Neurochem Res 27: 1105-1112.
    • (2002) Neurochem Res , vol.27 , pp. 1105-1112
    • Jin, K.1    Mao, X.O.2    Eshoo, M.W.3    del Rio, G.4    Rao, R.5
  • 39
    • 0038756487 scopus 로고    scopus 로고
    • The involvement of hypoxia-inducible transcription factor-1-dependent pathway in nickel carcinogenesis
    • Salnikow K, Davidson T, Zhang Q, Chen LC, Su W, et al. (2003) The involvement of hypoxia-inducible transcription factor-1-dependent pathway in nickel carcinogenesis. Cancer Res 63: 3524-3530.
    • (2003) Cancer Res , vol.63 , pp. 3524-3530
    • Salnikow, K.1    Davidson, T.2    Zhang, Q.3    Chen, L.C.4    Su, W.5
  • 40
    • 33746078851 scopus 로고    scopus 로고
    • Pancreatic beta cells lack a low glucose and O2-inducible mitochondrial protein that augments cell survival
    • Wang J, Cao Y, Chen Y, Chen Y, Gardner P, et al. (2006) Pancreatic beta cells lack a low glucose and O2-inducible mitochondrial protein that augments cell survival. Proc Natl Acad Sci U S A 103: 10636-10641.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 10636-10641
    • Wang, J.1    Cao, Y.2    Chen, Y.3    Chen, Y.4    Gardner, P.5
  • 41
    • 84861761931 scopus 로고    scopus 로고
    • HIG1, a novel regulator of mitochondrial gamma-secretase, maintains normal mitochondrial function
    • Hayashi H, Nakagami H, Takeichi M, Shimamura M, Koibuchi N, et al. (2012) HIG1, a novel regulator of mitochondrial gamma-secretase, maintains normal mitochondrial function. Faseb J 26: 2306-2317.
    • (2012) Faseb J , vol.26 , pp. 2306-2317
    • Hayashi, H.1    Nakagami, H.2    Takeichi, M.3    Shimamura, M.4    Koibuchi, N.5
  • 42
    • 84863348671 scopus 로고    scopus 로고
    • beta-Cells with relative low HIMP1 overexpression levels in a transgenic mouse line enhance basal insulin production and hypoxia/hypoglycemia tolerance
    • Zhang X, Degenstein L, Cao Y, Stein J, Osei K, et al. (2012) beta-Cells with relative low HIMP1 overexpression levels in a transgenic mouse line enhance basal insulin production and hypoxia/hypoglycemia tolerance. PLoS One 7: e34126.
    • (2012) PLoS One , vol.7
    • Zhang, X.1    Degenstein, L.2    Cao, Y.3    Stein, J.4    Osei, K.5
  • 43
    • 82555164967 scopus 로고    scopus 로고
    • The survival effect of mitochondrial Higd-1a is associated with suppression of cytochrome C release and prevention of caspase activation
    • An HJ, Shin H, Jo SG, Kim YJ, Lee JO, et al. (2011) The survival effect of mitochondrial Higd-1a is associated with suppression of cytochrome C release and prevention of caspase activation. Biochim Biophys Acta 1813: 2088-2098.
    • (2011) Biochim Biophys Acta , vol.1813 , pp. 2088-2098
    • An, H.J.1    Shin, H.2    Jo, S.G.3    Kim, Y.J.4    Lee, J.O.5
  • 44
    • 23044479387 scopus 로고    scopus 로고
    • Characterization of hypoxia induced gene 1: expression during rat central nervous system maturation and evidence of antisense RNA expression
    • Bedo G, Vargas M, Ferreiro MJ, Chalar C, Agrati D, (2005) Characterization of hypoxia induced gene 1: expression during rat central nervous system maturation and evidence of antisense RNA expression. Int J Dev Biol 49: 431-436.
    • (2005) Int J Dev Biol , vol.49 , pp. 431-436
    • Bedo, G.1    Vargas, M.2    Ferreiro, M.J.3    Chalar, C.4    Agrati, D.5
  • 45
    • 84874300929 scopus 로고    scopus 로고
    • ECM-Dependent HIF Induction Directs Trophoblast Stem Cell Fate via LIMK1-Mediated Cytoskeletal Rearrangement
    • Choi HJ, Sanders TA, Tormos KV, Ameri K, Tsai JD, et al. (2013) ECM-Dependent HIF Induction Directs Trophoblast Stem Cell Fate via LIMK1-Mediated Cytoskeletal Rearrangement. PLoS One 8: e56949.
    • (2013) PLoS One , vol.8
    • Choi, H.J.1    Sanders, T.A.2    Tormos, K.V.3    Ameri, K.4    Tsai, J.D.5
  • 46
    • 79957459076 scopus 로고    scopus 로고
    • Apoptosis-inducing factor: structure, function, and redox regulation
    • Sevrioukova IF, (2011) Apoptosis-inducing factor: structure, function, and redox regulation. Antioxid Redox Signal 14: 2545-2579.
    • (2011) Antioxid Redox Signal , vol.14 , pp. 2545-2579
    • Sevrioukova, I.F.1
  • 48
    • 77952298503 scopus 로고    scopus 로고
    • Mitochondrial regulation of cell death: processing of apoptosis-inducing factor (AIF)
    • Norberg E, Orrenius S, Zhivotovsky B, (2010) Mitochondrial regulation of cell death: processing of apoptosis-inducing factor (AIF). Biochem Biophys Res Commun 396: 95-100.
    • (2010) Biochem Biophys Res Commun , vol.396 , pp. 95-100
    • Norberg, E.1    Orrenius, S.2    Zhivotovsky, B.3
  • 49
    • 2542601328 scopus 로고    scopus 로고
    • Hypoxia inducible carbonic anhydrase IX, marker of tumour hypoxia, survival pathway and therapy target
    • Potter C, Harris AL, (2004) Hypoxia inducible carbonic anhydrase IX, marker of tumour hypoxia, survival pathway and therapy target. Cell Cycle 3: 164-167.
    • (2004) Cell Cycle , vol.3 , pp. 164-167
    • Potter, C.1    Harris, A.L.2
  • 50
    • 84862909128 scopus 로고    scopus 로고
    • Myocardial improvement with human embryonic stem cell-derived cardiomyocytes enriched by p38MAPK inhibition
    • Yeghiazarians Y, Gaur M, Zhang Y, Sievers RE, Ritner C, et al. (2012) Myocardial improvement with human embryonic stem cell-derived cardiomyocytes enriched by p38MAPK inhibition. Cytotherapy 14: 223-231.
    • (2012) Cytotherapy , vol.14 , pp. 223-231
    • Yeghiazarians, Y.1    Gaur, M.2    Zhang, Y.3    Sievers, R.E.4    Ritner, C.5
  • 51
    • 76349103272 scopus 로고    scopus 로고
    • Circulating tumour cells demonstrate an altered response to hypoxia and an aggressive phenotype
    • Ameri K, Luong R, Zhang H, Powell AA, Montgomery KD, et al. (2010) Circulating tumour cells demonstrate an altered response to hypoxia and an aggressive phenotype. Br J Cancer 102: 561-569.
    • (2010) Br J Cancer , vol.102 , pp. 561-569
    • Ameri, K.1    Luong, R.2    Zhang, H.3    Powell, A.A.4    Montgomery, K.D.5
  • 52
    • 84859385707 scopus 로고    scopus 로고
    • Hypoxia-induced autophagy promotes tumor cell survival and adaptation to antiangiogenic treatment in glioblastoma
    • Hu YL, DeLay M, Jahangiri A, Molinaro AM, Rose SD, et al. (2012) Hypoxia-induced autophagy promotes tumor cell survival and adaptation to antiangiogenic treatment in glioblastoma. Cancer Res 72: 1773-1783.
    • (2012) Cancer Res , vol.72 , pp. 1773-1783
    • Hu, Y.L.1    DeLay, M.2    Jahangiri, A.3    Molinaro, A.M.4    Rose, S.D.5
  • 53
    • 84861762712 scopus 로고    scopus 로고
    • Carbonic Anhydrase IX Promotes Tumor Growth and Necrosis In Vivo and Inhibition Enhances Anti-VEGF Therapy
    • McIntyre A, Patiar S, Wigfield S, Li JL, Ledaki I, et al. (2012) Carbonic Anhydrase IX Promotes Tumor Growth and Necrosis In Vivo and Inhibition Enhances Anti-VEGF Therapy. Clin Cancer Res 18: 3100-3111.
    • (2012) Clin Cancer Res , vol.18 , pp. 3100-3111
    • McIntyre, A.1    Patiar, S.2    Wigfield, S.3    Li, J.L.4    Ledaki, I.5
  • 54
    • 21344437729 scopus 로고    scopus 로고
    • Vascular targeting and antiangiogenesis agents induce drug resistance effector GRP78 within the tumor microenvironment
    • Dong D, Ko B, Baumeister P, Swenson S, Costa F, et al. (2005) Vascular targeting and antiangiogenesis agents induce drug resistance effector GRP78 within the tumor microenvironment. Cancer Res 65: 5785-5791.
    • (2005) Cancer Res , vol.65 , pp. 5785-5791
    • Dong, D.1    Ko, B.2    Baumeister, P.3    Swenson, S.4    Costa, F.5
  • 55
    • 0034117177 scopus 로고    scopus 로고
    • Mitochondrio-nuclear translocation of AIF in apoptosis and necrosis
    • Daugas E, Susin SA, Zamzami N, Ferri KF, Irinopoulou T, et al. (2000) Mitochondrio-nuclear translocation of AIF in apoptosis and necrosis. FASEB J 14: 729-739.
    • (2000) FASEB J , vol.14 , pp. 729-739
    • Daugas, E.1    Susin, S.A.2    Zamzami, N.3    Ferri, K.F.4    Irinopoulou, T.5
  • 56
    • 0032524656 scopus 로고    scopus 로고
    • Adenovirus E1B-19K/BCL-2 interacting protein BNIP3 contains a BH3 domain and a mitochondrial targeting sequence
    • Yasuda M, Theodorakis P, Subramanian T, Chinnadurai G, (1998) Adenovirus E1B-19K/BCL-2 interacting protein BNIP3 contains a BH3 domain and a mitochondrial targeting sequence. J Biol Chem 273: 12415-12421.
    • (1998) J Biol Chem , vol.273 , pp. 12415-12421
    • Yasuda, M.1    Theodorakis, P.2    Subramanian, T.3    Chinnadurai, G.4
  • 57
    • 0031455410 scopus 로고    scopus 로고
    • The E1B 19K/Bcl-2-binding protein Nip3 is a dimeric mitochondrial protein that activates apoptosis
    • Chen G, Ray R, Dubik D, Shi L, Cizeau J, et al. (1997) The E1B 19K/Bcl-2-binding protein Nip3 is a dimeric mitochondrial protein that activates apoptosis. J Exp Med 186: 1975-1983.
    • (1997) J Exp Med , vol.186 , pp. 1975-1983
    • Chen, G.1    Ray, R.2    Dubik, D.3    Shi, L.4    Cizeau, J.5
  • 58
    • 0034255036 scopus 로고    scopus 로고
    • Expression of the gene encoding the proapoptotic Nip3 protein is induced by hypoxia
    • Bruick RK, (2000) Expression of the gene encoding the proapoptotic Nip3 protein is induced by hypoxia. Proc Natl Acad Sci U S A 97: 9082-9087.
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 9082-9087
    • Bruick, R.K.1
  • 59
    • 67549101188 scopus 로고    scopus 로고
    • Role of BNIP3 and NIX in cell death, autophagy, and mitophagy
    • Zhang J, Ney PA, (2009) Role of BNIP3 and NIX in cell death, autophagy, and mitophagy. Cell Death Differ 16: 939-946.
    • (2009) Cell Death Differ , vol.16 , pp. 939-946
    • Zhang, J.1    Ney, P.A.2
  • 60
    • 62849105988 scopus 로고    scopus 로고
    • The role of Bcl-2 family member BNIP3 in cell death and disease: NIPping at the heels of cell death
    • Burton TR, Gibson SB, (2009) The role of Bcl-2 family member BNIP3 in cell death and disease: NIPping at the heels of cell death. Cell Death Differ 16: 515-523.
    • (2009) Cell Death Differ , vol.16 , pp. 515-523
    • Burton, T.R.1    Gibson, S.B.2
  • 61
    • 58149390639 scopus 로고    scopus 로고
    • Induction of autophagy in malignant rhabdoid tumor cells by the histone deacetylase inhibitor FK228 through AIF translocation
    • Watanabe M, Adachi S, Matsubara H, Imai T, Yui Y, et al. (2009) Induction of autophagy in malignant rhabdoid tumor cells by the histone deacetylase inhibitor FK228 through AIF translocation. Int J Cancer 124: 55-67.
    • (2009) Int J Cancer , vol.124 , pp. 55-67
    • Watanabe, M.1    Adachi, S.2    Matsubara, H.3    Imai, T.4    Yui, Y.5
  • 62
    • 55249086973 scopus 로고    scopus 로고
    • Histone 2B (H2B) expression is confined to a proper NAD+/NADH redox status
    • Dai RP, Yu FX, Goh SR, Chng HW, Tan YL, et al. (2008) Histone 2B (H2B) expression is confined to a proper NAD+/NADH redox status. J Biol Chem 283: 26894-26901.
    • (2008) J Biol Chem , vol.283 , pp. 26894-26901
    • Dai, R.P.1    Yu, F.X.2    Goh, S.R.3    Chng, H.W.4    Tan, Y.L.5
  • 63
    • 0027198854 scopus 로고
    • Cell cycle regulation of the glyceraldehyde-3-phosphate dehydrogenase/uracil DNA glycosylase gene in normal human cells
    • Mansur NR, Meyer-Siegler K, Wurzer JC, Sirover MA, (1993) Cell cycle regulation of the glyceraldehyde-3-phosphate dehydrogenase/uracil DNA glycosylase gene in normal human cells. Nucleic Acids Res 21: 993-998.
    • (1993) Nucleic Acids Res , vol.21 , pp. 993-998
    • Mansur, N.R.1    Meyer-Siegler, K.2    Wurzer, J.C.3    Sirover, M.A.4
  • 64
    • 80051935829 scopus 로고    scopus 로고
    • The 90-kDa heat-shock protein (Hsp90)-binding immunophilin FKBP51 is a mitochondrial protein that translocates to the nucleus to protect cells against oxidative stress
    • Gallo LI, Lagadari M, Piwien-Pilipuk G, Galigniana MD, (2011) The 90-kDa heat-shock protein (Hsp90)-binding immunophilin FKBP51 is a mitochondrial protein that translocates to the nucleus to protect cells against oxidative stress. J Biol Chem 286: 30152-30160.
    • (2011) J Biol Chem , vol.286 , pp. 30152-30160
    • Gallo, L.I.1    Lagadari, M.2    Piwien-Pilipuk, G.3    Galigniana, M.D.4
  • 65
    • 13844298651 scopus 로고    scopus 로고
    • Apoptosis-inducing factor is a key factor in neuronal cell death propagated by BAX-dependent and BAX-independent mechanisms
    • Cheung EC, Melanson-Drapeau L, Cregan SP, Vanderluit JL, Ferguson KL, et al. (2005) Apoptosis-inducing factor is a key factor in neuronal cell death propagated by BAX-dependent and BAX-independent mechanisms. J Neurosci 25: 1324-1334.
    • (2005) J Neurosci , vol.25 , pp. 1324-1334
    • Cheung, E.C.1    Melanson-Drapeau, L.2    Cregan, S.P.3    Vanderluit, J.L.4    Ferguson, K.L.5
  • 66
    • 0038788826 scopus 로고    scopus 로고
    • Hypoxia-induced gene expression occurs solely through the action of hypoxia-inducible factor 1alpha (HIF-1alpha): role of cytoplasmic trapping of HIF-2alpha
    • Park SK, Dadak AM, Haase VH, Fontana L, Giaccia AJ, et al. (2003) Hypoxia-induced gene expression occurs solely through the action of hypoxia-inducible factor 1alpha (HIF-1alpha): role of cytoplasmic trapping of HIF-2alpha. Mol Cell Biol 23: 4959-4971.
    • (2003) Mol Cell Biol , vol.23 , pp. 4959-4971
    • Park, S.K.1    Dadak, A.M.2    Haase, V.H.3    Fontana, L.4    Giaccia, A.J.5
  • 67
    • 0034788744 scopus 로고    scopus 로고
    • Design of the linkers which effectively separate domains of a bifunctional fusion protein
    • Arai R, Ueda H, Kitayama A, Kamiya N, Nagamune T, (2001) Design of the linkers which effectively separate domains of a bifunctional fusion protein. Protein Eng 14: 529-532.
    • (2001) Protein Eng , vol.14 , pp. 529-532
    • Arai, R.1    Ueda, H.2    Kitayama, A.3    Kamiya, N.4    Nagamune, T.5
  • 68
    • 65449154892 scopus 로고    scopus 로고
    • Generation of transgene-free induced pluripotent mouse stem cells by the piggyBac transposon
    • Yusa K, Rad R, Takeda J, Bradley A, (2009) Generation of transgene-free induced pluripotent mouse stem cells by the piggyBac transposon. Nat Methods 6: 363-369.
    • (2009) Nat Methods , vol.6 , pp. 363-369
    • Yusa, K.1    Rad, R.2    Takeda, J.3    Bradley, A.4
  • 69
    • 84861145421 scopus 로고    scopus 로고
    • Microarray analysis verifies two distinct phenotypes of glioblastomas resistant to antiangiogenic therapy
    • DeLay M, Jahangiri A, Carbonell WS, Hu YL, Tsao S, et al. (2012) Microarray analysis verifies two distinct phenotypes of glioblastomas resistant to antiangiogenic therapy. Clin Cancer Res 18: 2930-2942.
    • (2012) Clin Cancer Res , vol.18 , pp. 2930-2942
    • DeLay, M.1    Jahangiri, A.2    Carbonell, W.S.3    Hu, Y.L.4    Tsao, S.5


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