메뉴 건너뛰기




Volumn 62, Issue , 2013, Pages 26-36

Hypoxia-inducible factor prolyl hydroxylases as targets for neuroprotection by "antioxidant" metal chelators: From ferroptosis to stroke

Author keywords

Free radicals; Hypoxia inducible factors; Metal chelators; Neurodegeneration; Prolyl hydroxylases; Transcription

Indexed keywords

ANTIOXIDANT; CHELATING AGENT; DEFEROXAMINE; DIMETHYLOXALYLGLYCINE; ETHYL 3,4 DIHYDROXY BENZOIC ACID; FIBRINOLYTIC AGENT; HYPOXIA INDUCIBLE FACTOR; HYPOXIA INDUCIBLE FACTOR 1ALPHA; METAL; OXYGEN; PROCOLLAGEN PROLINE 2 OXOGLUTARATE 4 DIOXYGENASE; PROTEIN P53; TISSUE PLASMINOGEN ACTIVATOR; UBIQUITIN; UNCLASSIFIED DRUG; VON HIPPEL LINDAU PROTEIN;

EID: 84884900556     PISSN: 08915849     EISSN: 18734596     Source Type: Journal    
DOI: 10.1016/j.freeradbiomed.2013.01.026     Document Type: Review
Times cited : (123)

References (140)
  • 2
    • 0037868957 scopus 로고    scopus 로고
    • Sp1 and Sp3 are oxidative stress-inducible, antideath transcription factors in cortical neurons
    • Ryu, H.; Lee, J.; Zaman, K.; Kubilis, J.; Ferrante, R. J.; Ross, B. D.; Neve, R.; Ratan, R. R. Sp1 and Sp3 are oxidative stress-inducible, antideath transcription factors in cortical neurons. J. Neurosci. 23: 3597-3606; 2003. (Pubitemid 36958467)
    • (2003) Journal of Neuroscience , vol.23 , Issue.9 , pp. 3597-3606
    • Ryu, H.1    Lee, J.2    Zaman, K.3    Kubilis, J.4    Ferrante, R.J.5    Ross, B.D.6    Neve, R.7    Ratan, R.R.8
  • 10
    • 78650887484 scopus 로고    scopus 로고
    • The hypoxia-inducible transcription factor pathway regulates oxygen sensing in the simplest animal trichoplax adhaerens
    • Loenarz, C.; Coleman, M. L.; Boleininger, A.; Schierwater, B.; Holland, P. W.; Ratcliffe, P. J.; Schofield, C. J. The hypoxia-inducible transcription factor pathway regulates oxygen sensing in the simplest animal, Trichoplax adhaerens. EMBO Rep. 12: 63-70; 2011.
    • (2011) EMBO Rep , vol.12 , pp. 63-70
    • Loenarz, C.1    Coleman, M.L.2    Boleininger, A.3    Schierwater, B.4    Holland, P.W.5    Ratcliffe, P.J.6    Schofield, C.J.7
  • 11
    • 0027427588 scopus 로고
    • Characterization of hypoxia-inducible factor 1 and regulation of DNA binding activity by hypoxia
    • Wang, G. L.; Semenza, G. L. Characterization of hypoxia-inducible factor 1 and regulation of DNA binding activity by hypoxia. J. Biol. Chem. 268: 21513-21518; 1993. (Pubitemid 23320639)
    • (1993) Journal of Biological Chemistry , vol.268 , Issue.29 , pp. 21513-21518
    • Wang, G.L.1    Semenza, G.L.2
  • 13
    • 17144416530 scopus 로고    scopus 로고
    • Differential gene up-regulation by hypoxia-inducible factor-1alpha and hypoxia-inducible factor-2alpha in HEK293T cells
    • Wang, V.; Davis, D. A.; Haque, M.; Huang, L. E.; Yarchoan, R. Differential gene up-regulation by hypoxia-inducible factor-1alpha and hypoxia-inducible factor-2alpha in HEK293T cells. Cancer Res. 65: 3299-3306; 2005. (Pubitemid 40524614)
    • (2005) Cancer Research , vol.65 , Issue.8 , pp. 3299-3306
    • Wang, V.1    Davis, D.A.2    Haque, M.3    Huang, L.E.4    Yarchoan, R.5
  • 14
    • 0035834409 scopus 로고    scopus 로고
    • A conserved family of prolyl-4-hydroxylases that modify HIF
    • DOI 10.1126/science.1066373
    • Bruick, R. K.; McKnight, S. L. A conserved family of prolyl-4- hydroxylases that modify HIF. Science 294: 1337-1340; 2001. (Pubitemid 33063099)
    • (2001) Science , vol.294 , Issue.5545 , pp. 1337-1340
    • Bruick, R.K.1    McKnight, S.L.2
  • 17
    • 0029944965 scopus 로고    scopus 로고
    • Dimerization, DNA binding, and transactivation properties of hypoxia- inducible factor 1
    • DOI 10.1074/jbc.271.30.17771
    • Jiang, B. H.; Rue, E.; Wang, G. L.; Roe, R.; Semenza, G. L. Dimerization, DNA binding, and transactivation properties of hypoxia-inducible factor 1. J. Biol. Chem. 271: 17771-17778; 1996. (Pubitemid 26250751)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.30 , pp. 17771-17778
    • Jiang, B.-H.1    Rue, E.2    Wang, G.L.3    Roe, R.4    Semenza, G.L.5
  • 20
    • 59349098621 scopus 로고    scopus 로고
    • Inhibition of oxygen sensors as a therapeutic strategy for ischaemic and inflammatory disease
    • Fraisl, P.; Aragones, J.; Carmeliet, P. Inhibition of oxygen sensors as a therapeutic strategy for ischaemic and inflammatory disease. Nat. Rev. Drug Discovery 8: 139-152; 2009.
    • (2009) Nat. Rev. Drug Discovery , vol.8 , pp. 139-152
    • Fraisl, P.1    Aragones, J.2    Carmeliet, P.3
  • 21
    • 22544464403 scopus 로고    scopus 로고
    • Coordinate regulation of the oxygen-dependent degradation domains of hypoxia-inducible factor 1alpha
    • DOI 10.1128/MCB.25.15.6415-6426.2005
    • Chan, D. A.; Sutphin, P. D.; Yen, S. E.; Giaccia, A. J. Coordinate regulation of the oxygen-dependent degradation domains of hypoxia-inducible factor 1 alpha. Mol. Cell. Biol. 25: 6415-6426; 2005. (Pubitemid 41023218)
    • (2005) Molecular and Cellular Biology , vol.25 , Issue.15 , pp. 6415-6426
    • Chan, D.A.1    Sutphin, P.D.2    Yen, S.-E.3    Giaccia, A.J.4
  • 28
    • 59749096845 scopus 로고    scopus 로고
    • Prolyl hydroxylases as regulators of cell metabolism
    • Boulahbel, H.; Duran, R. V.; Gottlieb, E. Prolyl hydroxylases as regulators of cell metabolism. Biochem. Soc. Trans. 37: 291-294; 2009.
    • (2009) Biochem. Soc. Trans , vol.37 , pp. 291-294
    • Boulahbel, H.1    Duran, R.V.2    Gottlieb, E.3
  • 29
  • 30
    • 0043234538 scopus 로고    scopus 로고
    • Characterization of the human prolyl 4-hydroxylases that modify the hypoxia-inducible factor
    • DOI 10.1074/jbc.M304982200
    • Hirsila, M.; Koivunen, P.; Gunzler, V.; Kivirikko, K. I.; Myllyharju, J. Characterization of the human prolyl 4-hydroxylases that modify the hypoxia-inducible factor. J. Biol. Chem. 278: 30772-30780; 2003. (Pubitemid 36994584)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.33 , pp. 30772-30780
    • Hirsila, M.1    Koivunen, P.2    Gunzler, V.3    Kivirikko, K.I.4    Myllyharju, J.5
  • 31
    • 77957810983 scopus 로고    scopus 로고
    • Stabilization of hypoxia-inducible factor-1alpha protein in hypoxia occurs independently of mitochondrial reactive oxygen species production
    • Chua, Y. L.; Dufour, E.; Dassa, E. P.; Rustin, P.; Jacobs, H. T.; Taylor, C. T.; Hagen, T. Stabilization of hypoxia-inducible factor-1alpha protein in hypoxia occurs independently of mitochondrial reactive oxygen species production. J. Biol. Chem. 285: 31277-31284; 2010.
    • (2010) J. Biol. Chem , vol.285 , pp. 31277-31284
    • Chua, Y.L.1    Dufour, E.2    Dassa, E.P.3    Rustin, P.4    Jacobs, H.T.5    Taylor, C.T.6    Hagen, T.7
  • 32
    • 0348134741 scopus 로고    scopus 로고
    • Redistribution of Intracellular Oxygen in Hypoxia by Nitric Oxide: Effect on HIF1alpha
    • DOI 10.1126/science.1088805
    • Hagen, T.; Taylor, C. T.; Lam, F.; Moncada, S. Redistribution of intracellular oxygen in hypoxia by nitric oxide: effect on HIF1alpha. Science 302: 1975-1978; 2003. (Pubitemid 37523507)
    • (2003) Science , vol.302 , Issue.5652 , pp. 1975-1978
    • Hagen, T.1    Taylor, C.T.2    Lam, F.3    Moncada, S.4
  • 33
    • 20344386238 scopus 로고    scopus 로고
    • Mitochondrial reactive oxygen species activation of p38 mitogen-activated protein kinase is required for hypoxia signaling
    • DOI 10.1128/MCB.25.12.4853-4862.2005
    • Emerling, B. M.; Platanias, L. C.; Black, E.; Nebreda, A. R.; Davis, R. J.; Chandel, N. S. Mitochondrial reactive oxygen species activation of p38 mitogen-activated protein kinase is required for hypoxia signaling. Mol. Cell. Biol. 25: 4853-4862; 2005. (Pubitemid 40781087)
    • (2005) Molecular and Cellular Biology , vol.25 , Issue.12 , pp. 4853-4862
    • Emerling, B.M.1    Platanias, L.C.2    Black, E.3    Nebreda, A.R.4    Davis, R.J.5    Chandel, N.S.6
  • 34
    • 0035955663 scopus 로고    scopus 로고
    • Regulation of the hypoxia-inducible factor 1alpha by the inflammatory mediators nitric oxide and tumor necrosis factor-alpha in contrast to desferroxamine and phenylarsine oxide
    • Sandau, K. B.; Zhou, J.; Kietzmann, T.; Brune, B. Regulation of the hypoxia-inducible factor 1alpha by the inflammatory mediators nitric oxide and tumor necrosis factor-alpha in contrast to desferroxamine and phenylarsine oxide. J. Biol. Chem 276: 39805-39811; 2001.
    • (2001) J. Biol. Chem , vol.276 , pp. 39805-39811
    • Sandau, K.B.1    Zhou, J.2    Kietzmann, T.3    Brune, B.4
  • 36
    • 45249124315 scopus 로고    scopus 로고
    • Role of the VHL (von Hippel-Lindau) gene in renal cancer: A multifunctional tumour suppressor
    • DOI 10.1042/BST0360472
    • Nyhan, M. J.; O'Sullivan, G. C.; McKenna, S. L. Role of the VHL (von Hippel-Lindau) gene in renal cancer: a multifunctional tumour suppressor. Bio-chem. Soc. Trans. 36: 472-478; 2008. (Pubitemid 351839358)
    • (2008) Biochemical Society Transactions , vol.36 , Issue.3 , pp. 472-478
    • Nyhan, M.J.1    O'Sullivan, G.C.2    McKenna, S.L.3
  • 37
    • 0037131189 scopus 로고    scopus 로고
    • The von Hippel-Lindau tumor suppressor stabilizes novel plant homeodomain protein Jade-1
    • DOI 10.1074/jbc.M205040200
    • Zhou, M. I.; Wang, H.; Ross, J. J.; Kuzmin, I.; Xu, C.; Cohen, H. T. The von Hippel-Lindau tumor suppressor stabilizes novel plant homeodomain protein Jade-1. J. Biol. Chem. 277: 39887-39898; 2002. (Pubitemid 35190975)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.42 , pp. 39887-39898
    • Zhou, M.I.1    Wang, H.2    Ross, J.J.3    Kuzmin, I.4    Xu, C.5    Cohen, H.T.6
  • 39
    • 0034602845 scopus 로고    scopus 로고
    • Recognition of the polyubiquitin proteolytic signal
    • Thrower, J. S.; Hoffman, L.; Rechsteiner, M.; Pickart, C. M. Recognition of the polyubiquitin proteolytic signal. EMBO J. 19: 94-102; 2000. (Pubitemid 30009229)
    • (2000) EMBO Journal , vol.19 , Issue.1 , pp. 94-102
    • Thrower, J.S.1    Hoffman, L.2    Rechsteiner, M.3    Pickart, C.M.4
  • 40
    • 0020478717 scopus 로고
    • Ubiquitin-activating enzyme: Mechanism and role in protein-ubiquitin conjugation
    • Haas, A. L.; Warms, J. V.; Hershko, A.; Rose, I. A. Ubiquitin-activating enzyme: mechanism and role in protein-ubiquitin conjugation. J. Biol. Chem. 257: 2543-2548; 1982.
    • (1982) J. Biol. Chem , vol.257 , pp. 2543-2548
    • Haas, A.L.1    Warms, J.V.2    Hershko, A.3    Rose, I.A.4
  • 41
    • 27144526164 scopus 로고    scopus 로고
    • Orchestra for assembly and fate of polyubiquitin chains
    • Kuhlbrodt, K.; Mouysset, J.; Hoppe, T. Orchestra for assembly and fate of polyubiquitin chains. Essays Biochem. 41: 1-14; 2005. (Pubitemid 41500967)
    • (2005) Essays in Biochemistry , vol.41 , pp. 1-14
    • Kuhlbrodt, K.1    Mouysset, J.2    Hoppe, T.3
  • 42
    • 0028018268 scopus 로고
    • The ubiquitin-proteasome proteolytic pathway
    • DOI 10.1016/0092-8674(94)90396-4
    • Ciechanover, A. The ubiquitin-proteasome proteolytic pathway. Cell 79: 13-21; 1994. (Pubitemid 24309509)
    • (1994) Cell , vol.79 , Issue.1 , pp. 13-21
    • Ciechanover, A.1
  • 43
    • 28444452611 scopus 로고    scopus 로고
    • ATP binding to PAN or the 26S ATPases causes association with the 20S proteasome, gate opening, and translocation of unfolded proteins
    • DOI 10.1016/j.molcel.2005.10.019, PII S1097276505017144
    • Smith, D. M.; Kafri, G.; Cheng, Y.; Ng, D.; Walz, T.; Goldberg, A. L. ATP binding to PAN or the 26S ATPases causes association with the 20S proteasome, gate opening, and translocation of unfolded proteins. Mol. Cell 20: 687-698; 2005. (Pubitemid 41740691)
    • (2005) Molecular Cell , vol.20 , Issue.5 , pp. 687-698
    • Smith, D.M.1    Kafri, G.2    Cheng, Y.3    Ng, D.4    Walz, T.5    Goldberg, A.L.6
  • 44
    • 33749069075 scopus 로고    scopus 로고
    • ATP Binding and ATP Hydrolysis Play Distinct Roles in the Function of 26S Proteasome
    • DOI 10.1016/j.molcel.2006.08.025, PII S1097276506006289
    • Liu, C. W.; Li, X.; Thompson, D.; Wooding, K.; Chang, T. L.; Tang, Z.; Yu, H.; Thomas, P. J.; DeMartino, G. N. ATP binding and ATP hydrolysis play distinct roles in the function of 26S proteasome. Mol. Cell 24: 39-50; 2006. (Pubitemid 44466684)
    • (2006) Molecular Cell , vol.24 , Issue.1 , pp. 39-50
    • Liu, C.-W.1    Li, X.2    Thompson, D.3    Wooding, K.4    Chang, T.-l.5    Tang, Z.6    Yu, H.7    Thomas, P.J.8    DeMartino, G.N.9
  • 45
    • 65649139569 scopus 로고    scopus 로고
    • The role of the ubiquitin proteasome system in ischemia and ischemic tolerance
    • Meller, R. The role of the ubiquitin proteasome system in ischemia and ischemic tolerance. Neuroscientist 15: 243-260; 2009.
    • (2009) Neuroscientist , vol.15 , pp. 243-260
    • Meller, R.1
  • 50
    • 0032725554 scopus 로고    scopus 로고
    • P42/P44 mitogen-activated protein kinases phosphorylate hypoxia-inducible factor 1alpha (HIF-1alpha) and enhance the transcriptional activity of HIF-1
    • Richard, D. E.; Berra, E.; Gothie, E.; Roux, D.; Pouyssegur, J. p42/p44 mitogen-activated protein kinases phosphorylate hypoxia-inducible factor 1alpha (HIF-1alpha) and enhance the transcriptional activity of HIF-1. J. Biol. Chem. 274: 32631-32637; 1999. (Pubitemid 129535289)
    • (1999) Journal of Biological Chemistry , vol.274 , Issue.46 , pp. 32631-32637
    • Richard, D.E.1    Berra, E.2    Gothie, E.3    Roux, D.4    Pouyssegur, J.5
  • 52
    • 34547134517 scopus 로고    scopus 로고
    • Hypoxia-inducible factor 1alpha is regulated by the mammalian target of rapamycin (mTOR) via an mTOR signaling motif
    • DOI 10.1074/jbc.M611782200
    • Land, S. C.; Tee, A. R. Hypoxia-inducible factor 1alpha is regulated by the mammalian target of rapamycin (mTOR) via an mTOR signaling motif. J. Biol. Chem 282: 20534-20543; 2007. (Pubitemid 47100043)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.28 , pp. 20534-20543
    • Land, S.C.1    Tee, A.R.2
  • 53
    • 0042564792 scopus 로고    scopus 로고
    • S-nitrosation of Cys-800 of HIF-1alpha protein activates its interaction with p300 and stimulates its transcriptional activity
    • DOI 10.1016/S0014-5793(03)00807-X
    • Yasinska, I. M.; Sumbayev, V. V. S-nitrosation of Cys-800 of HIF-1alpha protein activates its interaction with p300 and stimulates its transcriptional activity. FEBS Lett 549: 105-109; 2003. (Pubitemid 36959853)
    • (2003) FEBS Letters , vol.549 , Issue.1-3 , pp. 105-109
    • Yasinska, I.M.1    Sumbayev, V.V.2
  • 54
    • 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.; O'Brien, S.; Tanaka, H.; Poellinger, L. Redox-regulated recruitment of the transcriptional coactivators CREB-binding protein and SRC-1 to hypoxia-inducible factor 1alpha. Mol. Cell. Biol. 20: 402-415; 2000. (Pubitemid 30002581)
    • (2000) Molecular and Cellular Biology , vol.20 , Issue.1 , pp. 402-415
    • Carrero, P.1    Okamoto, K.2    Coumailleau, P.3    O'Brien, S.A.4    Tanaka, H.5    Poellinger, L.6
  • 55
    • 0034681378 scopus 로고    scopus 로고
    • A redox mechanism controls differential DNA binding activities of hypoxia-inducible factor (HIF) 1alpha and the HIF-like factor
    • DOI 10.1074/jbc.275.7.4618
    • Lando, D.; Pongratz, I.; Poellinger, L.; Whitelaw, M. L. A redox mechanism controls differential DNA binding activities of hypoxia-inducible factor (HIF) 1alpha and the HIF-like factor. J. Biol. Chem. 275: 4618-4627; 2000. (Pubitemid 30108846)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.7 , pp. 4618-4627
    • Lando, D.1    Pongratz, I.2    Poellinger, L.3    Whitelaw, M.L.4
  • 56
    • 33846254999 scopus 로고    scopus 로고
    • 2-Independent and HSP90 Inhibitor-Induced Degradation of HIF-1alpha
    • DOI 10.1016/j.molcel.2007.01.001, PII S1097276507000020
    • Liu, Y. V.; Baek, J. H.; Zhang, H.; Diez, R.; Cole, R. N.; Semenza, G. L. RACK1 competes with HSP90 for binding to HIF-1alpha and is required for O2-independent and HSP90 inhibitor-induced degradation of HIF-1alpha. Mol. Cell 25: 207-217; 2007. (Pubitemid 46109612)
    • (2007) Molecular Cell , vol.25 , Issue.2 , pp. 207-217
    • Liu, Y.V.1    Baek, J.H.2    Zhang, H.3    Diez, R.4    Cole, R.N.5    Semenza, G.L.6
  • 57
    • 37549028456 scopus 로고    scopus 로고
    • Calcineurin promotes hypoxia-inducible factor 1alpha expression by dephosphorylating RACK1 and blocking RACK1 dimerization
    • Liu, Y. V.; Hubbi, M. E.; Pan, F.; McDonald, K. R.; Mansharamani, M.; Cole, R. N.; Liu, J. O.; Semenza, G. L. Calcineurin promotes hypoxia-inducible factor 1alpha expression by dephosphorylating RACK1 and blocking RACK1 dimerization. J. Biol. Chem. 282: 37064-37073; 2007.
    • (2007) J. Biol. Chem , vol.282 , pp. 37064-37073
    • Liu, Y.V.1    Hubbi, M.E.2    Pan, F.3    McDonald, K.R.4    Mansharamani, M.5    Cole, R.N.6    Liu, J.O.7    Semenza, G.L.8
  • 58
    • 34247583794 scopus 로고    scopus 로고
    • Glycogen synthase kinase 3 phosphorylates hypoxia-inducible factor 1alpha and mediates its destabilization in a VHL-independent manner
    • DOI 10.1128/MCB.00015-07
    • Flugel, D.; Gorlach, A.; Michiels, C.; Kietzmann, T. Glycogen synthase kinase 3 phosphorylates hypoxia-inducible factor 1alpha and mediates its desta-bilization in a VHL-independent manner. Mol. Cell. Biol 27: 3253-3265; 2007. (Pubitemid 46685205)
    • (2007) Molecular and Cellular Biology , vol.27 , Issue.9 , pp. 3253-3265
    • Flugel, D.1    Gorlach, A.2    Michiels, C.3    Kietzmann, T.4
  • 59
    • 84856604061 scopus 로고    scopus 로고
    • Gsk-3beta regulates cell growth migration and angiogenesis via fbw7 and usp28-dependent degradation of hif-1alpha
    • Flugel, D.; Gorlach, A.; Kietzmann, T. GSK-3beta regulates cell growth, migration, and angiogenesis via Fbw7 and USP28-dependent degradation of HIF-1alpha. Blood 119: 1292-1301; 2012.
    • (2012) Blood , vol.119 , pp. 1292-1301
    • Flugel, D.1    Gorlach, A.2    Kietzmann, T.3
  • 60
    • 84865429409 scopus 로고    scopus 로고
    • Passing the baton: The HIF switch
    • Koh, M. Y.; Powis, G. Passing the baton: the HIF switch. Trends Biochem. Sci. 37: 364-372; 2012.
    • (2012) Trends Biochem. Sci , vol.37 , pp. 364-372
    • Koh, M.Y.1    Powis, G.2
  • 62
    • 37049002653 scopus 로고    scopus 로고
    • Hypoxia up-regulates hypoxia-inducible factor-1alpha transcription by involving phosphatidylinositol 3-kinase and nuclear factor kappaB in pulmonary artery smooth muscle cells
    • DOI 10.1091/mbc.E07-04-0391
    • Belaiba, R. S.; Bonello, S.; Zahringer, C.; Schmidt, S.; Hess, J.; Kietzmann, T.; Gorlach, A. Hypoxia up-regulates hypoxia-inducible factor-1alpha transcription by involving phosphatidylinositol 3-kinase and nuclear factor kappaB in pulmonary artery smooth muscle cells. Mol. Biol. Cell. 18: 4691-4697; 2007. (Pubitemid 350246672)
    • (2007) Molecular Biology of the Cell , vol.18 , Issue.12 , pp. 4691-4697
    • BelAiba, R.S.1    Bonello, S.2    Zahringer, C.3    Schmidt, S.4    Hess, J.5    Kietzmann, T.6    Gorlach, A.7
  • 63
    • 0028268629 scopus 로고
    • Hypoxia causes the activation of nuclear factor kappaB through the phosphorylation of IkappaBalpha on tyrosine residues
    • Koong, A. C.; Chen, E. Y.; Giaccia, A. J. Hypoxia causes the activation of nuclear factor kappa B through the phosphorylation of I kappa B alpha on tyrosine residues. Cancer Res 54: 1425-1430; 1994. (Pubitemid 24106401)
    • (1994) Cancer Research , vol.54 , Issue.6 , pp. 1425-1430
    • Koong, A.C.1    Chen, E.Y.2    Giaccia, A.J.3
  • 65
    • 1642453685 scopus 로고    scopus 로고
    • Nitric Oxide Induces Hypoxia-inducible Factor 1 Activation That Is Dependent on MAPK and Phosphatidylinositol 3-Kinase Signaling
    • DOI 10.1074/jbc.M308197200
    • Kasuno, K.; Takabuchi, S.; Fukuda, K.; Kizaka-Kondoh, S.; Yodoi, J.; Adachi, T.; Semenza, G. L.; Hirota, K. Nitric oxide induces hypoxia-inducible factor 1 activation that is dependent on MAPK and phosphatidylinositol 3-kinase signaling. J. Biol. Chem. 279: 2550-2558; 2004. (Pubitemid 38114240)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.4 , pp. 2550-2558
    • Kasuno, K.1    Takabuchi, S.2    Fukuda, K.3    Kizaka-Kondoh, S.4    Yodoi, J.5    Adachi, T.6    Semenza, G.L.7    Hirota, K.8
  • 68
    • 0142166332 scopus 로고    scopus 로고
    • Targeting HIF-1 for cancer therapy
    • Semenza, G. L. Targeting HIF-1 for cancer therapy. Nat. Rev. Cancer 3: 721-732; 2003. (Pubitemid 37328811)
    • (2003) Nature Reviews Cancer , vol.3 , Issue.10 , pp. 721-732
    • Semenza, G.L.1
  • 72
    • 0021740750 scopus 로고
    • Inhibition of autoimmune neuropathological process by treatment with an iron-chelating agent
    • DOI 10.1084/jem.160.5.1532
    • Bowern, N.; Ramshaw, I. A.; Clark, I. A.; Doherty, P. C. Inhibition of autoimmune neuropathological process by treatment with an iron-chelating agent. J. Exp. Med. 160: 1532-1543; 1984. (Pubitemid 15220781)
    • (1984) Journal of Experimental Medicine , vol.160 , Issue.5 , pp. 1532-1543
    • Bowern, N.1    Ramshaw, I.A.2    Clark, I.A.3    Doherty, P.C.4
  • 73
    • 3042654997 scopus 로고    scopus 로고
    • Does cellular iron dysregulation play a causative role in Parkinson's disease?
    • DOI 10.1016/j.arr.2004.01.003, PII S1568163704000145
    • Kaur, D.; Andersen, J. Does cellular iron dysregulation play a causative role in Parkinson's disease? Ageing Res. Rev 3: 327-343; 2004. (Pubitemid 38844698)
    • (2004) Ageing Research Reviews , vol.3 , Issue.3 , pp. 327-343
    • Kaur, D.1    Andersen, J.2
  • 74
    • 0033571939 scopus 로고    scopus 로고
    • Protection from oxidative stress-induced apoptosis in cortical neuronal cultures by iron chelators is associated with enhanced DNA binding of hypoxia-inducible factor-1 and ATF-1/CREB and increased expression of glycolytic enzymes, p21(waf1/cip1), and erythropoietin
    • Zaman, K.; Ryu, H.; Hall, D.; O'Donovan, K.; Lin, K. I.; Miller, M. P.; Marquis, J. C.; Baraban, J. M.; Semenza, G. L.; Ratan, R. R. Protection from oxidative stress-induced apoptosis in cortical neuronal cultures by iron chelators is associated with enhanced DNA binding of hypoxia-inducible factor-1 and ATF-1/CREB and increased expression of glycolytic enzymes, p21(waf1/cip1), and erythropoietin. J. Neurosci. 19: 9821-9830; 1999. (Pubitemid 30226655)
    • (1999) Journal of Neuroscience , vol.19 , Issue.22 , pp. 9821-9830
    • Zaman, K.1    Ryu, H.2    Hall, D.3    O'Donovan, K.4    Lin, K.-I.5    Miller, M.P.6    Marquis, J.C.7    Baraban, J.M.8    Semenza, G.L.9    Ratan, R.R.10
  • 75
    • 79958748164 scopus 로고    scopus 로고
    • Adaptation to moderate hypoxia protects cortical neurons against ischemia-reperfusion injury and excitotoxicity independently of HIF-1a
    • Li, D.; Bai, T.; Brorson, J. R. Adaptation to moderate hypoxia protects cortical neurons against ischemia-reperfusion injury and excitotoxicity independently of HIF-1a. Exp. Neurol 230: 302-310; 2011.
    • (2011) Exp. Neurol , vol.230 , pp. 302-310
    • Li, D.1    Bai, T.2    Brorson, J.R.3
  • 76
    • 36248945117 scopus 로고    scopus 로고
    • Prolyl hydroxylase inhibitors delay neuronal cell death caused by trophic factor deprivation
    • DOI 10.1111/j.1471-4159.2007.04873.x
    • Lomb, D. J.; Straub, J. A.; Freeman, R. S. Prolyl hydroxylase inhibitors delay neuronal cell death caused by trophic factor deprivation. J. Neurochem. 103: 1897-1906; 2007. (Pubitemid 350130097)
    • (2007) Journal of Neurochemistry , vol.103 , Issue.5 , pp. 1897-1906
    • Lomb, D.J.1    Straub, J.A.2    Freeman, R.S.3
  • 77
    • 75149154666 scopus 로고    scopus 로고
    • HIF prolyl hydroxylase inhibitors prevent neuronal death induced by mitochondrial toxins: Therapeutic implications for Huntington's disease and Alzheimer's disease
    • Niatsetskaya, Z.; Basso, M.; Speer, R. E.; McConoughey, S. J.; Coppola, G.; Ma, T. C.; Ratan, R. R. HIF prolyl hydroxylase inhibitors prevent neuronal death induced by mitochondrial toxins: therapeutic implications for Huntington's disease and Alzheimer's disease. Antioxid. Redox Signaling 12: 435-443; 2010.
    • (2010) Antioxid. Redox Signaling , vol.12 , pp. 435-443
    • Niatsetskaya, Z.1    Basso, M.2    Speer, R.E.3    McConoughey, S.J.4    Coppola, G.5    Ma, T.C.6    Ratan, R.R.7
  • 79
    • 70350365391 scopus 로고    scopus 로고
    • Inhibition of prolyl hydroxylase protects against 1-methyl-4-phenyl-1,2, 36-tetrahydropyridine-induced neurotoxicity model for the potential involvement of the hypoxia-inducible factor pathway in Parkinson disease
    • Lee, D. W.; Rajagopalan, S.; Siddiq, A.; Gwiazda, R.; Yang, L.; Beal, M. F.; Ratan, R. R.; Andersen, J. K. Inhibition of prolyl hydroxylase protects against 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine-induced neurotoxicity: model for the potential involvement of the hypoxia-inducible factor pathway in Parkinson disease. J. Biol. Chem. 284: 29065-29076; 2009.
    • (2009) J Biol Chem , vol.284 , pp. 29065-29076
    • Lee, D.W.1    Rajagopalan, S.2    Siddiq, A.3    Gwiazda, R.4    Yang, L.5    Beal, M.F.6    Ratan, R.R.7    Andersen, J.K.8
  • 83
    • 0028246870 scopus 로고
    • Macromolecular synthesis inhibitors prevent oxidative stress-induced apoptosis in embryonic cortical neurons by shunting cysteine from protein synthesis to glutathione
    • Ratan, R. R.; Murphy, T. H.; Baraban, J. M. Macromolecular synthesis inhibitors prevent oxidative stress-induced apoptosis in embryonic cortical neurons by shunting cysteine from protein synthesis to glutathione. J. Neurosci 14: 4385-4392; 1994. (Pubitemid 24200560)
    • (1994) Journal of Neuroscience , vol.14 , Issue.7 , pp. 4385-4392
    • Ratan, R.R.1    Murphy, T.H.2    Baraban, J.M.3
  • 84
    • 67650481882 scopus 로고    scopus 로고
    • Selective inhibition of hypoxia-inducible factor (HIF) prolyl-hydroxylase 1 mediates neuroprotection against normoxic oxidative death via HIF- and CREB-independent pathways
    • Siddiq, A.; Aminova, L. R.; Troy, C. M.; Suh, K.; Messer, Z.; Semenza, G. L.; Ratan, R. R. Selective inhibition of hypoxia-inducible factor (HIF) prolyl-hydroxylase 1 mediates neuroprotection against normoxic oxidative death via HIF- and CREB-independent pathways. J. Neurosci. 29: 8828-8838; 2009.
    • (2009) J. Neurosci , vol.29 , pp. 8828-8838
    • Siddiq, A.1    Aminova, L.R.2    Troy, C.M.3    Suh, K.4    Messer, Z.5    Semenza, G.L.6    Ratan, R.R.7
  • 87
    • 37549064016 scopus 로고    scopus 로고
    • Cerebral metabolic adaptation and ketone metabolism after brain injury
    • Prins, M. L. Cerebral metabolic adaptation and ketone metabolism after brain injury. J. Cereb. Blood Flow Metab. 28: 1-16; 2008.
    • (2008) J. Cereb. Blood Flow Metab , vol.28 , pp. 1-16
    • Prins, M.L.1
  • 88
    • 34247151286 scopus 로고    scopus 로고
    • Ketone bodies metabolism during ischemic and reperfusion brain injuries following bilateral occlusion of common carotid arteries in rats
    • DOI 10.1590/S0102-86502007000200009
    • Faria, M. H.; Muniz, L. R.; Vasconcelos, P. R. Ketone bodies metabolism during ischemic and reperfusion brain injuries following bilateral occlusion of common carotid arteries in rats. Acta Cir. Bras 22: 125-129; 2007. (Pubitemid 46597122)
    • (2007) Acta Cirurgica Brasileira , vol.22 , Issue.2 , pp. 125-129
    • Faria, M.H.G.1    Muniz, L.R.F.2    De Vasconcelos, P.R.L.3
  • 89
    • 61849100014 scopus 로고    scopus 로고
    • Fructose-1,6-bisphosphate and fructose-2,6-bisphosphate do not influence brain carbohydrate or high-energy phosphate metabolism in a rat model of forebrain ischemia
    • Hofer, R. E.; Wagner, S. R. t.; Pasternak, J. J.; Albrecht 2nd R. F.; Gallagher, W. J.; Lanier, W. L. Fructose-1,6-bisphosphate and fructose-2,6-bisphosphate do not influence brain carbohydrate or high-energy phosphate metabolism in a rat model of forebrain ischemia. J. Neurosurg. Anesthesiol. 21: 31-39; 2009.
    • (2009) J. Neurosurg. Anesthesiol , vol.21 , pp. 31-39
    • Hofer, R.E.1    Wagner, S.R.T.2    Pasternak, J.J.3    Albrecht, I.I.R.F.4    Gallagher, W.J.5    Lanier, W.L.6
  • 90
    • 80055006684 scopus 로고    scopus 로고
    • Emerging mechanisms of disrupted cellular signaling in brain ischemia
    • Tymianski, M. Emerging mechanisms of disrupted cellular signaling in brain ischemia. Nat. Neurosci. 14: 1369-1373; 2011.
    • (2011) Nat. Neurosci , vol.14 , pp. 1369-1373
    • Tymianski, M.1
  • 91
    • 42749094007 scopus 로고    scopus 로고
    • Beyond NMDA and AMPA glutamate receptors: Emerging mechanisms for ionic imbalance and cell death in stroke
    • Besancon, E.; Guo, S.; Lok, J.; Tymianski, M.; Lo, E. H. Beyond NMDA and AMPA glutamate receptors: emerging mechanisms for ionic imbalance and cell death in stroke. Trends Pharmacol. Sci. 29: 268-275; 2008.
    • (2008) Trends Pharmacol. Sci , vol.29 , pp. 268-275
    • Besancon, E.1    Guo, S.2    Lok, J.3    Tymianski, M.4    Lo, E.H.5
  • 92
    • 79960141471 scopus 로고    scopus 로고
    • The immunology of stroke: From mechanisms to translation
    • Iadecola, C.; Anrather, J. The immunology of stroke: from mechanisms to translation. Nat. Med 17: 796-808; 2011.
    • (2011) Nat. Med , vol.17 , pp. 796-808
    • Iadecola, C.1    Anrather, J.2
  • 94
    • 18744389551 scopus 로고    scopus 로고
    • Hypoxic Preconditioning Protects against Ischemic Brain Injury
    • DOI 10.1602/neurorx.1.1.26, PII S1545534306700050
    • Sharp, F. R.; Ran, R.; Lu, A.; Tang, Y.; Strauss, K. I.; Glass, T.; Ardizzone, T.; Bernaudin, M. Hypoxic preconditioning protects against ischemic brain injury. NeuroRx 1: 26-35; 2004. (Pubitemid 46613775)
    • (2004) NeuroRx , vol.1 , Issue.1 , pp. 26-35
    • Sharp, F.R.1    Ran, R.2    Lu, A.3    Tang, Y.4    Strauss, K.I.5    Glass, T.6    Ardizzone, T.7    Bernaudin, M.8
  • 95
    • 7644229277 scopus 로고    scopus 로고
    • Translation of ischemic preconditioning to the patient: Prolyl hydroxylase inhibition and hypoxia inducible factor-1 as novel targets for stroke therapy
    • DOI 10.1161/01.STR.0000143216.85349.9e
    • Ratan, R. R.; Siddiq, A.; Aminova, L.; Lange, P. S.; Langley, B.; Ayoub, I.; Gensert, J.; Chavez, J. Translation of ischemic preconditioning to the patient: prolyl hydroxylase inhibition and hypoxia inducible factor-1 as novel targets for stroke therapy. Stroke 35: 2687-2689; 2004. (Pubitemid 39458369)
    • (2004) Stroke , vol.35 , Issue.SUPPL. 1 , pp. 2687-2689
    • Ratan, R.R.1    Siddiq, A.2    Aminova, L.3    Lange, P.S.4    Langley, B.5    Ayoub, I.6    Gensert, J.7    Chavez, J.8
  • 97
    • 0037109768 scopus 로고    scopus 로고
    • Activation of hypoxia-inducible factor-1 in the rat cerebral cortex after transient global ischemia: Potential role of insulin-like growth factor-1
    • Chavez, J. C.; LaManna, J. C. Activation of hypoxia-inducible factor-1 in the rat cerebral cortex after transient global ischemia: potential role of insulinlike growth factor-1. J. Neurosci 22: 8922-8931; 2002. (Pubitemid 35379062)
    • (2002) Journal of Neuroscience , vol.22 , Issue.20 , pp. 8922-8931
    • Chavez, J.C.1    LaManna, J.C.2
  • 98
    • 34250021865 scopus 로고    scopus 로고
    • Neuron-specific inactivation of the hypoxia inducible factor 1alpha increases brain injury in a mouse model of transient focal cerebral ischemia
    • DOI 10.1523/JNEUROSCI.0449-07.2007
    • Baranova, O.; Miranda, L. F.; Pichiule, P.; Dragatsis, I.; Johnson, R. S.; Chavez, J. C. Neuron-specific inactivation of the hypoxia inducible factor 1 alpha increases brain injury in a mouse model of transient focal cerebral ischemia. J. Neurosci. 27: 6320-6332; 2007. (Pubitemid 46890035)
    • (2007) Journal of Neuroscience , vol.27 , Issue.23 , pp. 6320-6332
    • Baranova, O.1    Miranda, L.F.2    Pichiule, P.3    Dragatsis, I.4    Johnson, R.S.5    Chavez, J.C.6
  • 99
    • 77955094939 scopus 로고    scopus 로고
    • Neuroprotection of deferoxamine on rotenone-induced injury via accumulation of HIF-1 alpha and induction of autophagy in SH-SY5Y cells
    • Wu, Y.; Li, X.; Xie, W.; Jankovic, J.; Le, W.; Pan, T. Neuroprotection of deferoxamine on rotenone-induced injury via accumulation of HIF-1 alpha and induction of autophagy in SH-SY5Y cells. Neurochem. Int. 57: 198-205; 2010.
    • (2010) Neurochem. Int , vol.57 , pp. 198-205
    • Wu, Y.1    Li, X.2    Xie, W.3    Jankovic, J.4    Le, W.5    Pan, T.6
  • 100
    • 49349109477 scopus 로고    scopus 로고
    • HIF-1alpha inhibition ameliorates neonatal brain injury in a rat pup hypoxic-ischemic model
    • Chen, W.; Jadhav, V.; Tang, J.; Zhang, J. H. HIF-1alpha inhibition ameliorates neonatal brain injury in a rat pup hypoxic-ischemic model. Neurobiol. Dis. 31: 433-441; 2008.
    • (2008) Neurobiol. Dis , vol.31 , pp. 433-441
    • Chen, W.1    Jadhav, V.2    Tang, J.3    Zhang, J.H.4
  • 101
    • 79951689572 scopus 로고    scopus 로고
    • Hypoxia-inducible factor-1alpha contributes to brain edema after stroke by regulating aquaporins and glycerol distribution in brain
    • Higashida, T.; Peng, C.; Li, J.; Dornbos 3rd D.; Teng, K.; Li, X.; Kinni, H.; Guthikonda, M.; Ding, Y. Hypoxia-inducible factor-1alpha contributes to brain edema after stroke by regulating aquaporins and glycerol distribution in brain. Curr. Neurovasc. Res. 8: 44-51; 2011.
    • (2011) Curr. Neurovasc. Res , vol.8 , pp. 44-51
    • Higashida, T.1    Peng, C.2    Li, J.3    Dornbos III, D.4    Teng, K.5    Li, X.6    Kinni, H.7    Guthikonda, M.8    Ding, Y.9
  • 102
    • 79954594089 scopus 로고    scopus 로고
    • Selective inhibition of early - But not late - Expressed HIF-1alpha is neuroprotective in rats after focal ischemic brain damage
    • Yeh, S. H.; Ou, L. C.; Gean, P. W.; Hung, J. J.; Chang, W. C. Selective inhibition of early - but not late - expressed HIF-1alpha is neuroprotective in rats after focal ischemic brain damage. Brain Pathol. 21: 249-262; 2011.
    • (2011) Brain Pathol , vol.21 , pp. 249-262
    • Yeh, S.H.1    Ou, L.C.2    Gean, P.W.3    Hung, J.J.4    Chang, W.C.5
  • 103
    • 13544251744 scopus 로고    scopus 로고
    • Prosurvival and prodeath effects of hypoxia-inducible factor-1alpha stabilization in a murine hippocampal cell line
    • DOI 10.1074/jbc.M409223200
    • Aminova, L. R.; Chavez, J. C.; Lee, J.; Ryu, H.; Kung, A.; Lamanna, J. C.; Ratan, R. R. Prosurvival and prodeath effects of hypoxia-inducible factor-1alpha stabilization in a murine hippocampal cell line. J. Biol. Chem. 280: 3996-4003; 2005. (Pubitemid 40223869)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.5 , pp. 3996-4003
    • Aminova, L.R.1    Chavez, J.C.2    Lee, J.3    Ryu, H.4    Kung, A.5    LaManna, J.C.6    Ratan, R.R.7
  • 104
    • 59449100497 scopus 로고    scopus 로고
    • Specific inhibition of hypoxia inducible factor 1 exaggerates cell injury induced by in vitro ischemia through deteriorating cellular redox environment
    • Guo, S.; Miyake, M.; Liu, K. J.; Shi, H. Specific inhibition of hypoxia inducible factor 1 exaggerates cell injury induced by in vitro ischemia through deteriorating cellular redox environment. J. Neurochem 108: 1309-1321; 2009.
    • (2009) J. Neurochem , vol.108 , pp. 1309-1321
    • Guo, S.1    Miyake, M.2    Liu, K.J.3    Shi, H.4
  • 105
    • 39749188133 scopus 로고    scopus 로고
    • The good, the bad, and the cell type-specific roles of hypoxia inducible factor-1alpha in neurons and astrocytes
    • DOI 10.1523/JNEUROSCI.5323-07.2008
    • Vangeison, G.; Carr, D.; Federoff, H. J.; Rempe, D. A. The good, the bad, and the cell type-specific roles of hypoxia inducible factor-1 alpha in neurons and astrocytes. J. Neurosci. 28: 1988-1993; 2008. (Pubitemid 351302661)
    • (2008) Journal of Neuroscience , vol.28 , Issue.8 , pp. 1988-1993
    • Vangeison, G.1    Carr, D.2    Federoff, H.J.3    Rempe, D.A.4
  • 106
    • 54549089738 scopus 로고    scopus 로고
    • Hypoxia signalling through mTOR and the unfolded protein response in cancer
    • Wouters, B. G.; Koritzinsky, M. Hypoxia signalling through mTOR and the unfolded protein response in cancer. Nat. Rev. Cancer 8: 851-864; 2008.
    • (2008) Nat. Rev. Cancer , vol.8 , pp. 851-864
    • Wouters, B.G.1    Koritzinsky, M.2
  • 107
    • 77954177298 scopus 로고    scopus 로고
    • Glucose is necessary for stabilization of hypoxia-inducible factor-1alpha under hypoxia: Contribution of the pentose phosphate pathway to this stabilization
    • Osada-Oka, M.; Hashiba, Y.; Akiba, S.; Imaoka, S.; Sato, T. Glucose is necessary for stabilization of hypoxia-inducible factor-1alpha under hypoxia: contribution of the pentose phosphate pathway to this stabilization. FEBS Lett 584: 3073-3079; 2010.
    • (2010) FEBS Lett , vol.584 , pp. 3073-3079
    • Osada-Oka, M.1    Hashiba, Y.2    Akiba, S.3    Imaoka, S.4    Sato, T.5
  • 109
    • 79953170581 scopus 로고    scopus 로고
    • Hypoxia-inducible factor alpha subunit stabilization by NEDD8 conjugation is reactive oxygen species-dependent
    • Ryu, J. H.; Li, S. H.; Park, H. S.; Park, J. W.; Lee, B.; Chun, Y. S. Hypoxia-inducible factor alpha subunit stabilization by NEDD8 conjugation is reactive oxygen species-dependent. J. Biol. Chem. 286: 6963-6970; 2011.
    • (2011) J. Biol. Chem , vol.286 , pp. 6963-6970
    • Ryu, J.H.1    Li, S.H.2    Park, H.S.3    Park, J.W.4    Lee, B.5    Chun, Y.S.6
  • 110
    • 84879603441 scopus 로고    scopus 로고
    • In vitro ischemia suppresses hypoxic induction of hypoxia inducible factor-1a by inhibitionofsynthesis and not enhanced degradation
    • in press
    • Karuppagounder, S.S.; Basso, M.; Sleiman, S.F.; Ma, T.C.; Speer, R.E.; Smirnova, N.A.; Gazaryan, I.G.; Ratan, R.R. In vitro ischemia suppresses hypoxic induction of hypoxia inducible factor-1a by inhibitionofsynthesis and not enhanced degradation. J. Neurosci. Res., http://dx.doi.org/10.1002/jnr.23204, in press.
    • J. Neurosci. Res
    • Karuppagounder, S.S.1    Basso, M.2    Sleiman, S.F.3    Ma, T.C.4    Speer, R.E.5    Smirnova, N.A.6    Gazaryan, I.G.7    Ratan, R.R.8
  • 115
    • 77957810983 scopus 로고    scopus 로고
    • Stabilization of hypoxia-inducible factor-1alpha protein in hypoxia occurs independently of mitochondrial reactive oxygen species production
    • Chua, Y. L.; Dufour, E.; Dassa, E. P.; Rustin, P.; Jacobs, H. T.; Taylor, C. T.; Hagen, T. Stabilization of hypoxia-inducible factor-1alpha protein in hypoxia occurs independently of mitochondrial reactive oxygen species production. J. Biol. Chem. 285: 31277-31284; 2010.
    • (2010) J. Biol. Chem , vol.285 , pp. 31277-31284
    • Chua, Y.L.1    Dufour, E.2    Dassa, E.P.3    Rustin, P.4    Jacobs, H.T.5    Taylor, C.T.6    Hagen, T.7
  • 117
    • 79953190404 scopus 로고    scopus 로고
    • Use of the ODD-luciferase transgene for the non-invasive imaging of spontaneous tumors in mice
    • Goldman, S. J.; Chen, E.; Taylor, R.; Zhang, S.; Petrosky, W.; Reiss, M.; Jin, S. Use of the ODD-luciferase transgene for the non-invasive imaging of spontaneous tumors in mice. PLoS One 6:e18269; 2011.
    • (2011) PLoS One , vol.6
    • Goldman, S.J.1    Chen, E.2    Taylor, R.3    Zhang, S.4    Petrosky, W.5    Reiss, M.6    Jin, S.7
  • 118
    • 84863483418 scopus 로고    scopus 로고
    • Hypoxia-inducible factor prolyl hydro-xylase inhibition: Robust new target or another big bust for stroke therapeutics? J
    • Karuppagounder, S. S.; Ratan, R. R. Hypoxia-inducible factor prolyl hydro-xylase inhibition: robust new target or another big bust for stroke therapeutics? J. Cereb. Blood Flow Metab 32: 1347-1361; 2012.
    • (2012) Cereb. Blood Flow Metab , vol.32 , pp. 1347-1361
    • Karuppagounder, S.S.1    Ratan, R.R.2
  • 121
    • 44349181985 scopus 로고    scopus 로고
    • Desferoxamine preconditioning protects against cerebral ischemia in rats by inducing expressions of hypoxia inducible factor 1alpha and erythropoietin
    • DOI 10.1007/s12264-008-0089-3
    • Li, Y. X.; Ding, S. J.; Xiao, L.; Guo, W.; Zhan, Q. Desferoxamine preconditioning protects against cerebral ischemia in rats by inducing expressions of hypoxia inducible factor 1 alpha and erythropoietin. Neurosci. Bull 24: 89-95; 2008. (Pubitemid 351738284)
    • (2008) Neuroscience Bulletin , vol.24 , Issue.2 , pp. 89-95
    • Li, Y.-X.1    Ding, S.-J.2    Xiao, L.3    Guo, W.4    Zhan, Q.5
  • 122
    • 84866519432 scopus 로고    scopus 로고
    • A screen for inducers of p21(waf1/cip1) identifies HIF prolyl hydroxylase inhibitors as neuroprotective agents with antitumor properties
    • Ma, T. C.; Langley, B.; Ko, B.; Wei, N.; Gazaryan, I. G.; Zareen, N.; Yamashiro, D. J.; Willis, D. E.; Ratan, R. R. A screen for inducers of p21(waf1/cip1) identifies HIF prolyl hydroxylase inhibitors as neuroprotective agents with antitumor properties. Neurobiol. Dis. 49C: 13-21; 2012.
    • (2012) Neurobiol. Dis , vol.49 C , pp. 13-21
    • Ma, T.C.1    Langley, B.2    Ko, B.3    Wei, N.4    Gazaryan, I.G.5    Zareen, N.6    Yamashiro, D.J.7    Willis, D.E.8    Ratan, R.R.9
  • 123
    • 15844427058 scopus 로고    scopus 로고
    • Hemoglobin potentiates excitotoxic injury in cortical cell culture
    • Regan, R. F.; Panter, S. S. Hemoglobin potentiates excitotoxic injury in cortical cell culture. J. Neurotrauma 13: 223-231; 1996. (Pubitemid 26142615)
    • (1996) Journal of Neurotrauma , vol.13 , Issue.4 , pp. 223-231
    • Regan, R.F.1    Scott Panter, S.2
  • 124
    • 0035981020 scopus 로고    scopus 로고
    • Multiple pathways of neuroprotection against oxidative stress and excitotoxic injury in immature primary hippocampal neurons
    • DOI 10.1016/S0165-3806(01)00302-9, PII S0165380601003029
    • Almli, L. M.; Hamrick, S. E.; Koshy, A. A.; Tauber, M. G.; Ferriero, D. M. Multiple pathways of neuroprotection against oxidative stress and excito-toxic injury in immature primary hippocampal neurons. Brain Res. Dev. Brain Res. 132: 121-129; 2001. (Pubitemid 34024954)
    • (2001) Developmental Brain Research , vol.132 , Issue.2 , pp. 121-129
    • Almli, L.M.1    Hamrick, S.E.G.2    Koshy, A.A.3    Tauber, M.G.4    Ferriero, D.M.5
  • 125
    • 0029972440 scopus 로고    scopus 로고
    • Cell cycle blockers mimosine, ciclopirox, and deferoxamine prevent the death of PC12 cells and postmitotic sympathetic neurons after removal of trophic support
    • Farinelli, S. E.; Greene, L. A. Cell cycle blockers mimosine, ciclopirox, and deferoxamine prevent the death of PC12 cells and postmitotic sympathetic neurons after removal of trophic support. J. Neurosci 16: 1150-1162; 1996. (Pubitemid 26140872)
    • (1996) Journal of Neuroscience , vol.16 , Issue.3 , pp. 1150-1162
    • Farinelli, S.E.1    Greene, L.A.2
  • 126
    • 0033839757 scopus 로고    scopus 로고
    • Role of hypoxia-inducible factor-1 in hypoxia-induced ischemic tolerance in neonatal rat brain
    • Bergeron, M.; Gidday, J. M.; Yu, A. Y.; Semenza, G. L.; Ferriero, D. M.; Sharp, F. R. Role of hypoxia-inducible factor-1 in hypoxia-induced ischemic tolerance in neonatal rat brain. Ann. Neurol. 48: 285-296; 2000.
    • (2000) Ann. Neurol , vol.48 , pp. 285-296
    • Bergeron, M.1    Gidday, J.M.2    Yu, A.Y.3    Semenza, G.L.4    Ferriero, D.M.5    Sharp, F.R.6
  • 127
    • 24744444711 scopus 로고    scopus 로고
    • Hypoxia-inducible factor 1alpha and erythropoietin upregulation with deferoxamine salvage after neonatal stroke
    • DOI 10.1016/j.expneurol.2005.06.001, PII S0014488605001901
    • Mu, D.; Chang, Y. S.; Vexler, Z. S.; Ferriero, D. M. Hypoxia-inducible factor 1a and erythropoietin upregulation with deferoxamine salvage after neonatal stroke. Exp. Neurol. 195: 407-415; 2005. (Pubitemid 41297792)
    • (2005) Experimental Neurology , vol.195 , Issue.2 , pp. 407-415
    • Mu, D.1    Yun, S.C.2    Vexler, Z.S.3    Ferriero, D.M.4
  • 130
    • 79957948980 scopus 로고    scopus 로고
    • Prophylactic neuroprotection against stroke: Low-dose, prolonged treatment with deferoxamine or deferasirox establishes prolonged neuroprotection independent of HIF-1 function
    • Zhao, Y.; Rempe, D. A. Prophylactic neuroprotection against stroke: low-dose, prolonged treatment with deferoxamine or deferasirox establishes prolonged neuroprotection independent of HIF-1 function. J. Cereb. Blood Flow Metab 31: 1412-1423; 2010.
    • (2010) J. Cereb. Blood Flow Metab , vol.31 , pp. 1412-1423
    • Zhao, Y.1    Rempe, D.A.2
  • 131
    • 77949917152 scopus 로고    scopus 로고
    • Preconditioning protects against oxidative injury involving hypoxia-inducible factor-1 and vascular endothe-lial growth factor in cultured astrocytes
    • Chu, P. W.; Beart, P. M.; Jones, N. M. Preconditioning protects against oxidative injury involving hypoxia-inducible factor-1 and vascular endothe-lial growth factor in cultured astrocytes. Eur. J. Pharmacol. 633: 24-32; 2010.
    • (2010) Eur. J. Pharmacol , vol.633 , pp. 24-32
    • Chu, P.W.1    Beart, P.M.2    Jones, N.M.3
  • 132
    • 84855786346 scopus 로고    scopus 로고
    • Inhibition of prolyl hydroxylases by dimethyloxaloylglycine after stroke reduces ischemic brain injury and requires hypoxia inducible factor-1a
    • Ogle, M. E.; Gu, X.; Espinera, A. R.; Wei, L. Inhibition of prolyl hydroxylases by dimethyloxaloylglycine after stroke reduces ischemic brain injury and requires hypoxia inducible factor-1a. Neurobiol. Dis. 45: 733-742; 2012.
    • (2012) Neurobiol. Dis , vol.45 , pp. 733-742
    • Ogle, M.E.1    Gu, X.2    Espinera, A.R.3    Wei, L.4
  • 133
    • 34248586304 scopus 로고    scopus 로고
    • Novel neuroprotective neurotrophic NAP analogs targeting metal toxicity and oxidative stress: Potential candidates for the control of neurodegenerative diseases
    • Zheng, H.; Blat, D.; Fridkin, M. Novel neuroprotective neurotrophic NAP analogs targeting metal toxicity and oxidative stress: potential candidates for the control of neurodegenerative diseases. J. Neural Transm. Suppl. 71: 163-172; 2006. (Pubitemid 351412118)
    • (2006) Journal of Neural Transmission, Supplement , Issue.71 , pp. 163-172
    • Zheng, H.1    Blat, D.2    Fridkin, M.3
  • 134
    • 1842608744 scopus 로고    scopus 로고
    • Ironing iron out in Parkinson's disease and other neurodegenerative diseases with iron chelators: A lesson from 6-hydroxydopamine and iron chelators, desferal and VK-28
    • DOI 10.1196/annals.1306.025
    • Youdim, M. B.; Stephenson, G.; Ben Shachar, D. Ironing iron out in Parkinson's disease and other neurodegenerative diseases with iron chela-tors: a lesson from 6-hydroxydopamine and iron chelators, desferal and VK-28. Ann. N. Y. Acad. Sci 1012: 306-325; 2004. (Pubitemid 38453534)
    • (2004) Annals of the New York Academy of Sciences , vol.1012 , pp. 306-325
    • Youdim, M.B.H.1    Stephenson, G.2    Shachar, D.B.3
  • 135
    • 84862294186 scopus 로고    scopus 로고
    • A possible novel anti-inflammatory mechanism for the pharmacological prolyl hydroxylase inhibitor 3,4-dihydroxybenzoate: Implications for use as a therapeutic for Parkinson's disease
    • Chinta, S. J.; Rajagopalan, S.; Ganesan, A.; Andersen, J. K. A possible novel anti-inflammatory mechanism for the pharmacological prolyl hydroxylase inhibitor 3,4-dihydroxybenzoate: implications for use as a therapeutic for Parkinson's disease. Parkinsons Dis 2012: 364684; 2012.
    • (2012) Parkinsons Dis , vol.2012 , pp. 364684
    • Chinta, S.J.1    Rajagopalan, S.2    Ganesan, A.3    Andersen, J.K.4
  • 136
    • 84869080922 scopus 로고    scopus 로고
    • Intranasal deferoxamine reverses iron-induced memory deficits and inhibits amyloi-dogenic APP processing in a transgenic mouse model of Alzheimer's disease
    • Guo, C.; Wang, T.; Zheng, W.; Shan, Z. Y.; Teng, W. P.; Wang, Z. Y. Intranasal deferoxamine reverses iron-induced memory deficits and inhibits amyloi-dogenic APP processing in a transgenic mouse model of Alzheimer's disease. Neurobiol. Aging 34: 562-575; 2013.
    • (2013) Neurobiol. Aging , vol.34 , pp. 562-575
    • Guo, C.1    Wang, T.2    Zheng, W.3    Shan, Z.Y.4    Teng, W.P.5    Wang, Z.Y.6
  • 138
    • 18144374584 scopus 로고    scopus 로고
    • Induction of hypoxia inducible factor-1 attenuates metabolic insults induced by 3-nitropropionic acid in rat c6 glioma cells
    • Yang, Y. T.; Ju, T. C.; Yang, D. I. Induction of hypoxia inducible factor-1 attenuates metabolic insults induced by 3-nitropropionic acid in rat C6 glioma cells. J. Neurochem 93: 513-525; 2005.
    • (2005) J. Neurochem , vol.93 , pp. 513-525
    • Yang, Y.T.1    Ju, T.C.2    Yang, D.I.3
  • 139
    • 0033054177 scopus 로고    scopus 로고
    • The Friedreich's ataxia mutation confers cellular sensitivity to oxidant stress which is rescued by chelators of iron and calcium and inhibitors of apoptosis
    • Wong, A.; Yang, J.; Cavadini, P.; Gellera, C.; Lonnerdal, B.; Taroni, F.; Cortopassi, G. The Friedreich's ataxia mutation confers cellular sensitivity to oxidant stress which is rescued by chelators of iron and calcium and inhibitors of apoptosis. Hum. Mol. Genet 8: 425-430; 1999. (Pubitemid 29097330)
    • (1999) Human Molecular Genetics , vol.8 , Issue.3 , pp. 425-430
    • Wong, A.1    Yang, J.2    Cavadini, P.3    Gellera, C.4    Lonnerdal, B.5    Taroni, F.6    Cortopassi, G.7
  • 140
    • 47249127786 scopus 로고    scopus 로고
    • Iron-dependent regulation of frataxin expression: Implications for treatment of Friedreich ataxia
    • Li, K.; Besse, E. K.; Ha, D.; Kovtunovych, G.; Rouault, T. A. Iron-dependent regulation of frataxin expression: implications for treatment of Friedreich ataxia. Hum. Mol. Genet 17: 2265-2273; 2008.)
    • (2008) Hum. Mol. Genet , vol.17 , pp. 2265-2273
    • Li, K.1    Besse, E.K.2    Ha, D.3    Kovtunovych, G.4    Rouault, T.A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.