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Volumn 584, Issue 15, 2010, Pages 3340-3347

OGFOD1, a member of the 2-oxoglutarate and iron dependent dioxygenase family, functions in ischemic signaling

Author keywords

2 Oxoglutarate and iron dependent dioxygenase; Cell death; Ischemia

Indexed keywords

ADENOSINE TRIPHOSPHATASE; DIOXYGENASE; MESSENGER RNA; PROTEIN ATPAF1; PROTEIN OGFOD1; UNCLASSIFIED DRUG;

EID: 77955276499     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2010.06.015     Document Type: Article
Times cited : (25)

References (23)
  • 1
    • 0033529656 scopus 로고    scopus 로고
    • Perspectives on oxygen sensing
    • Semenza G.L. Perspectives on oxygen sensing. Cell 1999, 98:281-284.
    • (1999) Cell , vol.98 , pp. 281-284
    • Semenza, G.L.1
  • 2
    • 0034901463 scopus 로고    scopus 로고
    • Hypoxia-inducible factor 1: oxygen homeostasis and disease pathophysiology
    • Semenza G.L. Hypoxia-inducible factor 1: oxygen homeostasis and disease pathophysiology. Trends Mol. Med. 2001, 7:345-350.
    • (2001) Trends Mol. Med. , vol.7 , pp. 345-350
    • Semenza, G.L.1
  • 3
    • 0035917313 scopus 로고    scopus 로고
    • HIFalpha targeted for VHL-mediated destruction by proline hydroxylation: implications for O2 sensing
    • Ivan M., et al. HIFalpha targeted for VHL-mediated destruction by proline hydroxylation: implications for O2 sensing. Science 2001, 292:464-468.
    • (2001) Science , vol.292 , pp. 464-468
    • Ivan, M.1
  • 4
    • 0037097861 scopus 로고    scopus 로고
    • FIH-1 is an asparaginyl hydroxylase enzyme that regulates the transcriptional activity of hypoxia-inducible factor
    • Lando D., Peet D.J., Gorman J.J., Whelan D.A., Whitelaw M.L., Bruick R.K. FIH-1 is an asparaginyl hydroxylase enzyme that regulates the transcriptional activity of hypoxia-inducible factor. Genes Dev. 2002, 16:1466-1471.
    • (2002) Genes Dev. , vol.16 , pp. 1466-1471
    • Lando, D.1    Peet, D.J.2    Gorman, J.J.3    Whelan, D.A.4    Whitelaw, M.L.5    Bruick, R.K.6
  • 5
    • 0036469038 scopus 로고    scopus 로고
    • Asparagine hydroxylation of the HIF transactivation domain a hypoxic switch
    • Lando D., Peet D.J., Whelan D.A., Gorman J.J., Whitelaw M.L. Asparagine hydroxylation of the HIF transactivation domain a hypoxic switch. Science 2002, 295:858-861.
    • (2002) Science , vol.295 , pp. 858-861
    • Lando, D.1    Peet, D.J.2    Whelan, D.A.3    Gorman, J.J.4    Whitelaw, M.L.5
  • 7
    • 0035917808 scopus 로고    scopus 로고
    • Targeting of HIF-alpha to the von Hippel-Lindau ubiquitylation complex by O2-regulated prolyl hydroxylation
    • Jaakkola P., et al. Targeting of HIF-alpha to the von Hippel-Lindau ubiquitylation complex by O2-regulated prolyl hydroxylation. Science 2001, 292:468-472.
    • (2001) Science , vol.292 , pp. 468-472
    • Jaakkola, P.1
  • 8
    • 0033617296 scopus 로고    scopus 로고
    • Glucose uptake and glycolysis reduce hypoxia-induced apoptosis in cultured neonatal rat cardiac myocytes
    • Malhotra R., Brosius F.C. Glucose uptake and glycolysis reduce hypoxia-induced apoptosis in cultured neonatal rat cardiac myocytes. J. Biol. Chem. 1999, 274:12567-12575.
    • (1999) J. Biol. Chem. , vol.274 , pp. 12567-12575
    • Malhotra, R.1    Brosius, F.C.2
  • 9
    • 0031172230 scopus 로고    scopus 로고
    • Persistent myocardial ischemia increases GLUT1 glucose transporter expression in both ischemic and non-ischemic heart regions
    • Brosius F.C., Liu Y., Nguyen N., Sun D., Bartlett J., Schwaiger M. Persistent myocardial ischemia increases GLUT1 glucose transporter expression in both ischemic and non-ischemic heart regions. J. Mol. Cell. Cardiol. 1997, 29:1675-1685.
    • (1997) J. Mol. Cell. Cardiol. , vol.29 , pp. 1675-1685
    • Brosius, F.C.1    Liu, Y.2    Nguyen, N.3    Sun, D.4    Bartlett, J.5    Schwaiger, M.6
  • 10
    • 0000481740 scopus 로고    scopus 로고
    • Vascular endothelial growth factor: direct neuroprotective effect in in vitro ischemia
    • Jin K.L., Mao X.O., Greenberg D.A. Vascular endothelial growth factor: direct neuroprotective effect in in vitro ischemia. Proc. Natl. Acad. Sci. USA 2000, 97:10242-10247.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 10242-10247
    • Jin, K.L.1    Mao, X.O.2    Greenberg, D.A.3
  • 11
    • 0041743159 scopus 로고    scopus 로고
    • VEGF-induced neuroprotection, neurogenesis, and angiogenesis after focal cerebral ischemia
    • Sun Y., Jin K., Xie L., Childs J., Mao X.O., Logvinova A., Greenberg D.A. VEGF-induced neuroprotection, neurogenesis, and angiogenesis after focal cerebral ischemia. J. Clin. Invest. 2003, 111:1843-1851.
    • (2003) J. Clin. Invest. , vol.111 , pp. 1843-1851
    • Sun, Y.1    Jin, K.2    Xie, L.3    Childs, J.4    Mao, X.O.5    Logvinova, A.6    Greenberg, D.A.7
  • 12
    • 29244485561 scopus 로고    scopus 로고
    • Hypoxia-inducible factor prolyl 4-hydroxylase inhibition. A target for neuroprotection in the central nervous system
    • Siddiq A., et al. Hypoxia-inducible factor prolyl 4-hydroxylase inhibition. A target for neuroprotection in the central nervous system. J. Biol. Chem. 2005, 280:41732-41743.
    • (2005) J. Biol. Chem. , vol.280 , pp. 41732-41743
    • Siddiq, A.1
  • 13
    • 36248945117 scopus 로고    scopus 로고
    • Prolyl hydroxylase inhibitors delay neuronal cell death caused by trophic factor deprivation
    • Lomb D.J., Straub J.A., Freeman R.S. Prolyl hydroxylase inhibitors delay neuronal cell death caused by trophic factor deprivation. J. Neurochem. 2007, 103:1897-1906.
    • (2007) J. Neurochem. , vol.103 , pp. 1897-1906
    • Lomb, D.J.1    Straub, J.A.2    Freeman, R.S.3
  • 15
    • 0035834409 scopus 로고    scopus 로고
    • A conserved family of prolyl-4-hydroxylases that modify HIF
    • Bruick R.K., McKnight S.L. A conserved family of prolyl-4-hydroxylases that modify HIF. Science 2001, 294:1337-1340.
    • (2001) Science , vol.294 , pp. 1337-1340
    • Bruick, R.K.1    McKnight, S.L.2
  • 16
    • 33745614894 scopus 로고    scopus 로고
    • Cellular oxygen sensing: crystal structure of hypoxia-inducible factor prolyl hydroxylase (PHD2)
    • McDonough M.A., et al. Cellular oxygen sensing: crystal structure of hypoxia-inducible factor prolyl hydroxylase (PHD2). Proc. Natl. Acad. Sci. USA 2006, 103:9814-9819.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 9814-9819
    • McDonough, M.A.1
  • 17
    • 0025350272 scopus 로고
    • Identification of two nuclear genes (ATP11, ATP12) required for assembly of the yeast F1-ATPase
    • Ackerman S.H., Tzagoloff A. Identification of two nuclear genes (ATP11, ATP12) required for assembly of the yeast F1-ATPase. Proc. Natl. Acad. Sci. USA 1990, 87:4986-4990.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 4986-4990
    • Ackerman, S.H.1    Tzagoloff, A.2
  • 18
    • 0032965775 scopus 로고    scopus 로고
    • The Drosophila gene 2A5 complements the defect in mitochondrial F1-ATPase assembly in yeast lacking the molecular chaperone Atp11p
    • Wang Z.G., Schmid K.J., Ackerman S.H. The Drosophila gene 2A5 complements the defect in mitochondrial F1-ATPase assembly in yeast lacking the molecular chaperone Atp11p. FEBS Lett. 1999, 452:305-308.
    • (1999) FEBS Lett. , vol.452 , pp. 305-308
    • Wang, Z.G.1    Schmid, K.J.2    Ackerman, S.H.3
  • 19
    • 44349091967 scopus 로고    scopus 로고
    • Oxygen-regulated degradation of fission yeast SREBP by Ofd1, a prolyl hydroxylase family member
    • Hughes B.T., Espenshade P.J. Oxygen-regulated degradation of fission yeast SREBP by Ofd1, a prolyl hydroxylase family member. EMBO J. 2008, 27:1491-1501.
    • (2008) EMBO J. , vol.27 , pp. 1491-1501
    • Hughes, B.T.1    Espenshade, P.J.2
  • 20
    • 58749108297 scopus 로고    scopus 로고
    • Oxygen-dependent binding of Nro1 to the prolyl hydroxylase Ofd1 regulates SREBP degradation in yeast
    • Lee C.Y., Stewart E.V., Hughes B.T., Espenshade P.J. Oxygen-dependent binding of Nro1 to the prolyl hydroxylase Ofd1 regulates SREBP degradation in yeast. EMBO J. 2009, 28:135-143.
    • (2009) EMBO J. , vol.28 , pp. 135-143
    • Lee, C.Y.1    Stewart, E.V.2    Hughes, B.T.3    Espenshade, P.J.4
  • 21
    • 39349105090 scopus 로고    scopus 로고
    • Expanding chemical biology of 2-oxoglutarate oxygenases
    • Loenarz C., Schofield C.J. Expanding chemical biology of 2-oxoglutarate oxygenases. Nat. Chem. Biol. 2008, 4:152-156.
    • (2008) Nat. Chem. Biol. , vol.4 , pp. 152-156
    • Loenarz, C.1    Schofield, C.J.2
  • 22
    • 33745806590 scopus 로고    scopus 로고
    • Tpa1p is part of an mRNP complex that influences translation termination, mRNA deadenylation, and mRNA turnover in Saccharomyces cerevisiae
    • Keeling K.M., Salas-Marco J., Osherovich L.Z., Bedwell D.M. Tpa1p is part of an mRNP complex that influences translation termination, mRNA deadenylation, and mRNA turnover in Saccharomyces cerevisiae. Mol. Cell. Biol. 2006, 26:5237-5248.
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 5237-5248
    • Keeling, K.M.1    Salas-Marco, J.2    Osherovich, L.Z.3    Bedwell, D.M.4
  • 23
    • 0034657420 scopus 로고    scopus 로고
    • The something about silencing protein, Sas3, is the catalytic subunit of NuA3, a yTAF(II)30-containing HAT complex that interacts with the Spt16 subunit of the yeast CP (Cdc68/Pob3)-FACT complex
    • John S., Howe L., Tafrov S.T., Grant P.A., Sternglanz R., Workman J.L. The something about silencing protein, Sas3, is the catalytic subunit of NuA3, a yTAF(II)30-containing HAT complex that interacts with the Spt16 subunit of the yeast CP (Cdc68/Pob3)-FACT complex. Genes Dev. 2000, 14:1196-1208.
    • (2000) Genes Dev. , vol.14 , pp. 1196-1208
    • John, S.1    Howe, L.2    Tafrov, S.T.3    Grant, P.A.4    Sternglanz, R.5    Workman, J.L.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.