메뉴 건너뛰기




Volumn 38, Issue 1, 2004, Pages 47-57

Redox-dependent regulation of the expression of nitric oxide-inducible genes

Author keywords

Gene regulation; Nitric oxide; Reactive nitrogen species; Reactive oxygen species

Indexed keywords

CYTOCHROME C OXIDASE; GUANYLATE CYCLASE; NITRIC OXIDE; PROTEIN TYROSINE KINASE; RAS PROTEIN; REACTIVE OXYGEN METABOLITE;

EID: 3442882491     PISSN: 00268933     EISSN: None     Source Type: Journal    
DOI: 10.1023/B:MBIL.0000015139.68759.69     Document Type: Review
Times cited : (2)

References (65)
  • 1
    • 0036511547 scopus 로고    scopus 로고
    • Reactive oxygen species and gene expression regulation
    • Turpaev K.T. 2002. Reactive oxygen species and gene expression regulation. Biokhimiya. 67, 281-292.
    • (2002) Biokhimiya , vol.67 , pp. 281-292
    • Turpaev, K.T.1
  • 2
    • 85044702418 scopus 로고    scopus 로고
    • Nitric oxide: Regulation of cell metabolism not involving the cell receptor system
    • Vanin A.F. 2001. Nitric oxide: Regulation of cell metabolism not involving the cell receptor system. Biofizika. 46, 631-641.
    • (2001) Biofizika , vol.46 , pp. 631-641
    • Vanin, A.F.1
  • 4
    • 0033815334 scopus 로고    scopus 로고
    • Nitrosation and oxidation in the regulation of gene expression
    • Marshall H.E., Merchant K., Stamler J.S. 2000. Nitrosation and oxidation in the regulation of gene expression. FASEB J. 14, 1889-1900.
    • (2000) FASEB J. , vol.14 , pp. 1889-1900
    • Marshall, H.E.1    Merchant, K.2    Stamler, J.S.3
  • 5
    • 0028092958 scopus 로고
    • Nitric oxide synthases: Roles, tolls, and controls
    • Nathan C., Xie Q. 1994. Nitric oxide synthases: roles, tolls, and controls. Cell. 78, 915-918.
    • (1994) Cell , vol.78 , pp. 915-918
    • Nathan, C.1    Xie, Q.2
  • 6
    • 0033637918 scopus 로고    scopus 로고
    • Nitric oxide synthase: Models and mechanisms
    • Groves J.T., Wang C.C. 2000. Nitric oxide synthase: models and mechanisms. Curr. Opin. Chem. Biol. 4, 687-695.
    • (2000) Curr. Opin. Chem. Biol. , vol.4 , pp. 687-695
    • Groves, J.T.1    Wang, C.C.2
  • 7
    • 0037064058 scopus 로고    scopus 로고
    • Biochemistry of mitochondrial nitric-oxide synthase
    • Elfering S.L., Sarkela T.M., Giulivi C. 2002. Biochemistry of mitochondrial nitric-oxide synthase. J. Biol. Chem. 277, 38079-38086.
    • (2002) J. Biol. Chem. , vol.277 , pp. 38079-38086
    • Elfering, S.L.1    Sarkela, T.M.2    Giulivi, C.3
  • 8
    • 0027104253 scopus 로고
    • Biochemistry of nitric oxide and its redox-activated forms
    • Stamler J.S., Singel D.J., Loscalzo J. 1992. Biochemistry of nitric oxide and its redox-activated forms. Science. 258, 1898-1892.
    • (1992) Science , vol.258 , pp. 1898-11892
    • Stamler, J.S.1    Singel, D.J.2    Loscalzo, J.3
  • 11
    • 0032910873 scopus 로고    scopus 로고
    • Nitric oxide. I. Physiological chemistry of nitric oxide and its metabolites: Implications in inflammation
    • Grisham M.B., Jourd'heuil D., Wink D.A. 1999. Nitric oxide. I. Physiological chemistry of nitric oxide and its metabolites: implications in inflammation. Am. J. Physiol. 276, G315-321.
    • (1999) Am. J. Physiol. , vol.276
    • Grisham, M.B.1    Jourd'heuil, D.2    Wink, D.A.3
  • 13
    • 0034916201 scopus 로고    scopus 로고
    • Induction of vascular endothelial growth factor by nitric oxide in cultured human articular chondrocytes
    • Turpaev K., Litvinov D., Dubovaya V., Panasyuk A., Ivanov D., Prassolov V. 2001. Induction of vascular endothelial growth factor by nitric oxide in cultured human articular chondrocytes. Biochimie. 83, 515-522.
    • (2001) Biochimie , vol.83 , pp. 515-522
    • Turpaev, K.1    Litvinov, D.2    Dubovaya, V.3    Panasyuk, A.4    Ivanov, D.5    Prassolov, V.6
  • 14
    • 0042093583 scopus 로고    scopus 로고
    • Redox modulation of NO-dependent induction of interleukin 8 in monocytic U937 cells
    • Turpaev K., Litvinov D., Justesen J. 2003. Redox modulation of NO-dependent induction of interleukin 8 in monocytic U937 cells. Cytokine. 23, 15-22.
    • (2003) Cytokine , vol.23 , pp. 15-22
    • Turpaev, K.1    Litvinov, D.2    Justesen, J.3
  • 15
    • 0035839611 scopus 로고    scopus 로고
    • Distinction between nitrosating mechanisms within human cells and aqueous solution
    • Espey M.G., Miranda K.M., Thomas D.D., Wink D.A. 2001. Distinction between nitrosating mechanisms within human cells and aqueous solution. J. Biol. Chem. 276, 30085-30091.
    • (2001) J. Biol. Chem. , vol.276 , pp. 30085-30091
    • Espey, M.G.1    Miranda, K.M.2    Thomas, D.D.3    Wink, D.A.4
  • 16
    • 0035253023 scopus 로고    scopus 로고
    • Nitric oxide and the regulation of gene expression
    • Bogdan C. 2001. Nitric oxide and the regulation of gene expression. Trends Cell. Biol. 11, 66-75.
    • (2001) Trends Cell. Biol. , vol.11 , pp. 66-75
    • Bogdan, C.1
  • 17
    • 0034123171 scopus 로고    scopus 로고
    • Interactions of oxidants with vascular signaling systems
    • Wolin M.S. 2000. Interactions of oxidants with vascular signaling systems. Arterioscler. Thromb. Vasc. Biol. 20, 1430-1442.
    • (2000) Arterioscler. Thromb. Vasc. Biol. , vol.20 , pp. 1430-1442
    • Wolin, M.S.1
  • 18
    • 0038359369 scopus 로고    scopus 로고
    • Nitric oxide induces phosphorylation of p53 and impairs nuclear export
    • Schneiderhan N., Budde A., Zhang Y., Brune B. 2003. Nitric oxide induces phosphorylation of p53 and impairs nuclear export. Oncogene. 22, 2857-2868.
    • (2003) Oncogene , vol.22 , pp. 2857-2868
    • Schneiderhan, N.1    Budde, A.2    Zhang, Y.3    Brune, B.4
  • 19
    • 0037031848 scopus 로고    scopus 로고
    • p38 kinase regulates nitric oxide-induced apoptosis of articular chondrocytes by accumulating p53 via NF-κB-dependent transcription and stabilization by serine 15 phosphorylation
    • Kim SJ., Hwang S.G., Shin D.Y., Kang S.S., Chun J.S. 2002. p38 kinase regulates nitric oxide-induced apoptosis of articular chondrocytes by accumulating p53 via NF-κB-dependent transcription and stabilization by serine 15 phosphorylation. J. Biol. Chem. 277, 33501-33508.
    • (2002) J. Biol. Chem. , vol.277 , pp. 33501-33508
    • Kim, S.J.1    Hwang, S.G.2    Shin, D.Y.3    Kang, S.S.4    Chun, J.S.5
  • 20
    • 0034712704 scopus 로고    scopus 로고
    • Nitric oxide modulates expression of cell cycle regulatory proteins: A cytostatic strategy for inhibition of human vascular smooth muscle cell proliferation
    • Tanner F.C., Meier P., Greutert H., Champion C., Nabel E.G., Luscher T.F. 2000. Nitric oxide modulates expression of cell cycle regulatory proteins: a cytostatic strategy for inhibition of human vascular smooth muscle cell proliferation. Circulation. 101, 1982-1989.
    • (2000) Circulation , vol.101 , pp. 1982-1989
    • Tanner, F.C.1    Meier, P.2    Greutert, H.3    Champion, C.4    Nabel, E.G.5    Luscher, T.F.6
  • 21
    • 2242421714 scopus 로고    scopus 로고
    • Nitric oxide: The role of soluble guanylate cyclase in mechanisms of its physiological effects
    • Severina I.S. 2002. Nitric oxide: The role of soluble guanylate cyclase in mechanisms of its physiological effects. Vopr. Med. Khim. 48, 4-30.
    • (2002) Vopr. Med. Khim. , vol.48 , pp. 4-30
    • Severina, I.S.1
  • 22
    • 5844284193 scopus 로고    scopus 로고
    • Spectral and kinetic studies on the activation of soluble guanylate cyclase by nitric oxide
    • Stone J.R., Marletta M.A. 1996. Spectral and kinetic studies on the activation of soluble guanylate cyclase by nitric oxide. Biochemistry. 35, 1093-1099.
    • (1996) Biochemistry , vol.35 , pp. 1093-1099
    • Stone, J.R.1    Marletta, M.A.2
  • 24
    • 0043269271 scopus 로고    scopus 로고
    • Regulation of nitric oxide-sensitive guanylyl cyclase
    • Friebe A., Koesling D. 2003. Regulation of nitric oxide-sensitive guanylyl cyclase. Circ. Res. 93, 96-105.
    • (2003) Circ. Res. , vol.93 , pp. 96-105
    • Friebe, A.1    Koesling, D.2
  • 26
    • 0036784336 scopus 로고    scopus 로고
    • Activation of the mitogen activated protein kinase extracellular signal-regulated kinase 1 and 2 by the nitric oxide-cGMP-cGMP-dependent protein kinase axis regulates the expression of matrix metalloproteinase 13 in vascular endothelial cells
    • Zaragoza C., Soria E., Lopez E., Browning D., Balbin M., Lopez-Otin C., Lamas S. 2002. Activation of the mitogen activated protein kinase extracellular signal-regulated kinase 1 and 2 by the nitric oxide-cGMP-cGMP-dependent protein kinase axis regulates the expression of matrix metalloproteinase 13 in vascular endothelial cells. Mol. Pharmacol. 62, 927-935.
    • (2002) Mol. Pharmacol. , vol.62 , pp. 927-935
    • Zaragoza, C.1    Soria, E.2    Lopez, E.3    Browning, D.4    Balbin, M.5    Lopez-Otin, C.6    Lamas, S.7
  • 27
    • 0036193378 scopus 로고    scopus 로고
    • MSK1 and MSK2 are required for the mitogen- and stress-induced phosphorylation of CREB and ATF1 in fibroblasts
    • Wiggin G.R., Soloaga A., Foster J.M., Murray-Tait V., Cohen P., Arthur J.S. 2002. MSK1 and MSK2 are required for the mitogen- and stress-induced phosphorylation of CREB and ATF1 in fibroblasts. Mol. Cell. Biol. 22, 2871-2881.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 2871-2881
    • Wiggin, G.R.1    Soloaga, A.2    Foster, J.M.3    Murray-Tait, V.4    Cohen, P.5    Arthur, J.S.6
  • 28
    • 0034649494 scopus 로고    scopus 로고
    • NO activation of fos promoter elements requires nuclear translocation of G-kinase I and CREB phosphorylation but is independent of MAP kinase activation
    • Gudi T., Casteel D.E., Vinson C., Boss G.R., Pilz R.B. 2000. NO activation of fos promoter elements requires nuclear translocation of G-kinase I and CREB phosphorylation but is independent of MAP kinase activation. Oncogene. 19, 6324-6333.
    • (2000) Oncogene , vol.19 , pp. 6324-6333
    • Gudi, T.1    Casteel, D.E.2    Vinson, C.3    Boss, G.R.4    Pilz, R.B.5
  • 29
    • 0036889794 scopus 로고    scopus 로고
    • Nitric oxide inhibition of mitochondrial respiration and its role in cell death
    • Brown G.C., Borutaite V. 2002. Nitric oxide inhibition of mitochondrial respiration and its role in cell death. Free Radic. Biol. Med. 33, 1440-1450.
    • (2002) Free Radic. Biol. Med. , vol.33 , pp. 1440-1450
    • Brown, G.C.1    Borutaite, V.2
  • 30
  • 33
    • 0034731455 scopus 로고    scopus 로고
    • Poly(ADP-ribose) binds to specific domains in DNA damage checkpoint proteins
    • Pleschke J.M., Kleczkowska H.E., Strohm M., Althaus F.R. 2000. Poly(ADP-ribose) binds to specific domains in DNA damage checkpoint proteins. J. Biol. Chem. 275, 40974-40980.
    • (2000) J. Biol. Chem. , vol.275 , pp. 40974-40980
    • Pleschke, J.M.1    Kleczkowska, H.E.2    Strohm, M.3    Althaus, F.R.4
  • 34
    • 0037663696 scopus 로고    scopus 로고
    • Peroxynitrite and nitric oxide differently target the iron-sulfur cluster and amino acid residues of human iron regulatory protein 1
    • Soum E., Brazzolotto X., Goussias C., Bouton C., Moulis J.M, Mattioli T.A., Drapier J.C. 2003. Peroxynitrite and nitric oxide differently target the iron-sulfur cluster and amino acid residues of human iron regulatory protein 1. Biochemistry. 42, 7648-7654.
    • (2003) Biochemistry , vol.42 , pp. 7648-7654
    • Soum, E.1    Brazzolotto, X.2    Goussias, C.3    Bouton, C.4    Moulis, J.M.5    Mattioli, T.A.6    Drapier, J.C.7
  • 35
    • 0030197587 scopus 로고    scopus 로고
    • Modulation by nitric oxide of metalloprotein regulatory activities
    • Drapier J.C., Bouton C. 1996. Modulation by nitric oxide of metalloprotein regulatory activities. BioEssays. 18, 549-556.
    • (1996) BioEssays , vol.18 , pp. 549-556
    • Drapier, J.C.1    Bouton, C.2
  • 36
    • 0037125975 scopus 로고    scopus 로고
    • Nitrogen monoxide-mediated control of ferritin synthesis: Implications for macrophage iron homeostasis
    • Kim S., Ponka P. 2002. Nitrogen monoxide-mediated control of ferritin synthesis: implications for macrophage iron homeostasis. Proc. Natl. Acad. Sci. USA. 99, 12214-12219.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 12214-12219
    • Kim, S.1    Ponka, P.2
  • 38
    • 0033729838 scopus 로고    scopus 로고
    • Control of the eukaryotic cell cycle by MAP kinase signaling pathways
    • Wilkinson M.G., Millar J.B.A. 2000. Control of the eukaryotic cell cycle by MAP kinase signaling pathways. FASEB J. 14, 2147-2157.
    • (2000) FASEB J. , vol.14 , pp. 2147-2157
    • Wilkinson, M.G.1    Millar, J.B.A.2
  • 39
    • 0034383949 scopus 로고    scopus 로고
    • The regulation of protein function by multisite phosphorylation - A 25 year update
    • Cohen P. 2000. The regulation of protein function by multisite phosphorylation - a 25 year update. Trends Biochem. Sci. 25, 596-601.
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 596-601
    • Cohen, P.1
  • 40
    • 0032444348 scopus 로고    scopus 로고
    • Inducible and constitutive transcription factors in the mammalian nervous system: Control of gene expression by Jun, Fos and Krox, and CREB/ATF proteins
    • Herdegen, T., Leah, J.D. 1998. Inducible and constitutive transcription factors in the mammalian nervous system: control of gene expression by Jun, Fos and Krox, and CREB/ATF proteins. Brain Res. Rev. 28, 370-490.
    • (1998) Brain Res. Rev. , vol.28 , pp. 370-490
    • Herdegen, T.1    Leah, J.D.2
  • 41
    • 0034816062 scopus 로고    scopus 로고
    • Mitogen-activated protein kinase p38 controls the expression and posttranslational modification of tristetraprolin, a regulator of tumor necrosis factor alpha mRNA stability
    • Mahtani K.R., Brook M., Dean J.L., Sully G., Saklatvala J., Clark A.R. 2001. Mitogen-activated protein kinase p38 controls the expression and posttranslational modification of tristetraprolin, a regulator of tumor necrosis factor alpha mRNA stability. Mol. Cell. Biol. 21, 6461-6469.
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 6461-6469
    • Mahtani, K.R.1    Brook, M.2    Dean, J.L.3    Sully, G.4    Saklatvala, J.5    Clark, A.R.6
  • 42
    • 0034907223 scopus 로고    scopus 로고
    • Parallel and independent regulation of interleukin-3 mRNA turnover by phosphatidylinositol 3-kinase and p38 mitogen-activated protein kinase
    • Ming X.F., Stoecklin G., Lu M., Looser R., Moroni C. 2001. Parallel and independent regulation of interleukin-3 mRNA turnover by phosphatidylinositol 3-kinase and p38 mitogen-activated protein kinase. Mol. Cell. Biol. 21, 5778-5789.
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 5778-5789
    • Ming, X.F.1    Stoecklin, G.2    Lu, M.3    Looser, R.4    Moroni, C.5
  • 43
    • 0141960214 scopus 로고    scopus 로고
    • p38 mitogen-activated protein kinase stabilises mRNAs that contain cyclooxygenase-2 and tumour necrosis factor AU-rich elements by inhibiting deadenylation
    • Dean J.L., Sarsfield S.J., Tsounakou E., Saklatvala J. 2003. p38 mitogen-activated protein kinase stabilises mRNAs that contain cyclooxygenase-2 and tumour necrosis factor AU-rich elements by inhibiting deadenylation. J. Biol. Chem. 278, 39470-39476.
    • (2003) J. Biol. Chem. , vol.278 , pp. 39470-39476
    • Dean, J.L.1    Sarsfield, S.J.2    Tsounakou, E.3    Saklatvala, J.4
  • 44
    • 0003979231 scopus 로고    scopus 로고
    • Functions of the p53 gene: A choice between life and death
    • Chumakov P.M. 2000. Functions of the p53 gene: A choice between life and death. Biokhimiya. 65, 34-47.
    • (2000) Biokhimiya , vol.65 , pp. 34-47
    • Chumakov, P.M.1
  • 45
    • 0033572746 scopus 로고    scopus 로고
    • Serine 15 phosphorylation stimulates p53 transactivation but does not directly influence interaction with HDM2
    • Dumaz N., Meek D.W. 1999. Serine 15 phosphorylation stimulates p53 transactivation but does not directly influence interaction with HDM2. EMBO J. 18, 7002-7010.
    • (1999) EMBO J. , vol.18 , pp. 7002-7010
    • Dumaz, N.1    Meek, D.W.2
  • 46
    • 0041553609 scopus 로고    scopus 로고
    • Kinases of the Src family: The structure and functions
    • Tatosyan A.G., Mizenina O.A. 2000. Kinases of the Src family: The structure and functions. Biokhimiya. 65, 57-67.
    • (2000) Biokhimiya , vol.65 , pp. 57-67
    • Tatosyan, A.G.1    Mizenina, O.A.2
  • 48
    • 0036268389 scopus 로고    scopus 로고
    • Role of nitric oxide in myocardial preconditioning
    • Dawn B., Bolli R. 2002. Role of nitric oxide in myocardial preconditioning. Ann. NY Acad. Sci. 962, 18-41.
    • (2002) Ann. NY Acad. Sci. , vol.962 , pp. 18-41
    • Dawn, B.1    Bolli, R.2
  • 50
    • 0034668178 scopus 로고    scopus 로고
    • Inhibitors of Ras signal transduction as antitumor agents
    • Garbay C., Liu W.Q., Vidal M., Roques B.P. 2000. Inhibitors of Ras signal transduction as antitumor agents. Biochem. Pharmacol. 60, 1165-1169.
    • (2000) Biochem. Pharmacol. , vol.60 , pp. 1165-1169
    • Garbay, C.1    Liu, W.Q.2    Vidal, M.3    Roques, B.P.4
  • 51
    • 0034283837 scopus 로고    scopus 로고
    • The Rel / NF-κB family: Friend and foe
    • Perkins N.D. 2000. The Rel / NF-κB family: friend and foe. Trends Biochem. Sci. 25, 434-440.
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 434-440
    • Perkins, N.D.1
  • 52
    • 0036009115 scopus 로고    scopus 로고
    • NF-κB at the crossroads of life and death
    • Karin M., Lin A. 2002. NF-κB at the crossroads of life and death. Nature Immunol. 3, 221-227.
    • (2002) Nature Immunol. , vol.3 , pp. 221-227
    • Karin, M.1    Lin, A.2
  • 53
    • 0034190367 scopus 로고    scopus 로고
    • Recent advances towards understanding redox mechanisms in the activation of nuclear factor κB
    • Janssen-Heininger Y.M., Poynter M.E., Baeuerle P.A. 2000. Recent advances towards understanding redox mechanisms in the activation of nuclear factor κB. Free Rad. Biol. Med. 28, 1317-1327.
    • (2000) Free Rad. Biol. Med. , vol.28 , pp. 1317-1327
    • Janssen-Heininger, Y.M.1    Poynter, M.E.2    Baeuerle, P.A.3
  • 54
    • 0037406703 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of IκB kinase α/β by protein kinase C-dependent c-Src activation is involved in TNFα-induced cyclooxygenase-2 expression
    • Huang W.C., Chen J.J., Inoue H., Chen C.C. 2003. Tyrosine phosphorylation of IκB kinase α/β by protein kinase C-dependent c-Src activation is involved in TNFα-induced cyclooxygenase-2 expression. J. Immunol. 170, 4767-4775.
    • (2003) J. Immunol. , vol.170 , pp. 4767-4775
    • Huang, W.C.1    Chen, J.J.2    Inoue, H.3    Chen, C.C.4
  • 56
    • 0037297175 scopus 로고    scopus 로고
    • Regulation of vascular endothelial growth factor synthesis by nitric oxide: Facts and controversies
    • Dulak J., Jozkowicz A. 2003. Regulation of vascular endothelial growth factor synthesis by nitric oxide: facts and controversies. Antioxid. Redox. Signal. 5, 123-132.
    • (2003) Antioxid. Redox. Signal. , vol.5 , pp. 123-132
    • Dulak, J.1    Jozkowicz, A.2
  • 57
    • 0036710591 scopus 로고    scopus 로고
    • Signal transduction to hypoxia-inducible factor 1
    • Semenza G. 2002. Signal transduction to hypoxia-inducible factor 1. Biochem. Pharmacol. 64, 993-998.
    • (2002) Biochem. Pharmacol. , vol.64 , pp. 993-998
    • Semenza, G.1
  • 58
    • 0141643358 scopus 로고    scopus 로고
    • Hypoxia up regulates prolyl hydroxylase. A feedback mechanism that limits HIF-1 responses during reoxygenation
    • D'Angelo G., Duplan E., Boyer N., Vigne P., Frelin C. 2003. Hypoxia up regulates prolyl hydroxylase. A feedback mechanism that limits HIF-1 responses during reoxygenation. J. Biol. Chem. 278, 38183-38187.
    • (2003) J. Biol. Chem. , vol.278 , pp. 38183-38187
    • D'Angelo, G.1    Duplan, E.2    Boyer, N.3    Vigne, P.4    Frelin, C.5
  • 59
    • 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. 2002. FIH-1 is an asparaginyl hydroxylase enzyme that regulates the transcriptional activity of hypoxia-inducible factor. Genes Dev. 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
  • 60
    • 0035955663 scopus 로고    scopus 로고
    • Regulation of the hypoxia-inducible factor 1α by the inflammatory mediators nitric oxide and tumor necrosis factor-α in contrast to desferroxamine and phenylarsine oxide
    • Sandau K.B., Zhou J., Kietzmann T., Brune B. 2001. Regulation of the hypoxia-inducible factor 1α by the inflammatory mediators nitric oxide and tumor necrosis factor-α in contrast to desferroxamine and phenylarsine oxide. J. Biol. Chem. 276, 39805-39811.
    • (2001) J. Biol. Chem. , vol.276 , pp. 39805-39811
    • Sandau, K.B.1    Zhou, J.2    Kietzmann, T.3    Brune, B.4
  • 61
    • 0042469448 scopus 로고    scopus 로고
    • Nitric oxide impairs normoxic degradation of HIF-1α by inhibition of prolyl hydroxylases
    • Metzen E., Zhou J., Jelkmann W., Fandrey J., Brune B. 2003. Nitric oxide impairs normoxic degradation of HIF-1α by inhibition of prolyl hydroxylases. Mol. Biol. Cell. 14, 3470-3481.
    • (2003) Mol. Biol. Cell. , vol.14 , pp. 3470-3481
    • Metzen, E.1    Zhou, J.2    Jelkmann, W.3    Fandrey, J.4    Brune, B.5
  • 62
    • 0037472651 scopus 로고    scopus 로고
    • HIF-1α protein as a target for S-nitrosation
    • Sumbayev V.V., Budde A., Zhou J., Brune B. 2003. HIF-1α protein as a target for S-nitrosation. FEBS Lett. 535, 106-112.
    • (2003) FEBS Lett. , vol.535 , pp. 106-112
    • Sumbayev, V.V.1    Budde, A.2    Zhou, J.3    Brune, B.4
  • 63
    • 0028964043 scopus 로고
    • Hydroxyl radical production in the brain after CO hypoxia in rats
    • Piantadosi C.A., Tatro L., Zhang J. 1995. Hydroxyl radical production in the brain after CO hypoxia in rats. Free Radic. Biol. Med. 18, 603-609.
    • (1995) Free Radic. Biol. Med. , vol.18 , pp. 603-609
    • Piantadosi, C.A.1    Tatro, L.2    Zhang, J.3
  • 64
    • 0037278475 scopus 로고    scopus 로고
    • Protein kinases and the hypoxia-inducible factor-1, two switches in angiogenesis
    • Mazure N.M., Brahimi-Horn M.C., Pouyssegur J. 2003. Protein kinases and the hypoxia-inducible factor-1, two switches in angiogenesis. Curr. Pharm. 9, 531-541.
    • (2003) Curr. Pharm. , vol.9 , pp. 531-541
    • Mazure, N.M.1    Brahimi-Horn, M.C.2    Pouyssegur, J.3
  • 65
    • 0042564792 scopus 로고    scopus 로고
    • S-nitrosation of Cys-800 of HIF-1α protein activates its interaction with p300 and stimulates its transcriptional activity
    • Yasinska I.M., Sumbayev V.V. 2003. S-nitrosation of Cys-800 of HIF-1α protein activates its interaction with p300 and stimulates its transcriptional activity. FEBS Lett. 549, 105-109.
    • (2003) FEBS Lett. , vol.549 , pp. 105-109
    • Yasinska, I.M.1    Sumbayev, V.V.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.