메뉴 건너뛰기




Volumn 68, Issue 23, 2011, Pages 3869-3883

Cytoglobin: Biochemical, functional and clinical perspective of the newest member of the globin family

Author keywords

Cancer; Cytoglobin; Fibrosis; Hypoxia; Nitric oxide dioxygenase; Oxidative stress

Indexed keywords

CYTOGLOBIN; NITRIC OXIDE; NITRIC OXIDE SYNTHASE; PEROXYNITRITE; REACTIVE NITROGEN SPECIES; REACTIVE OXYGEN METABOLITE;

EID: 82255175104     PISSN: 1420682X     EISSN: 14209071     Source Type: Journal    
DOI: 10.1007/s00018-011-0764-9     Document Type: Review
Times cited : (68)

References (131)
  • 1
    • 0032052216 scopus 로고    scopus 로고
    • Hemoglobins from bacteria to man: Evolution of different patterns of gene expression
    • Hardison R (1998) Hemoglobins from bacteria to man: evolution of different patterns of gene expression. J Exp Biol 201(Pt 8):1099-1117 (Pubitemid 28278316)
    • (1998) Journal of Experimental Biology , vol.201 , Issue.8 , pp. 1099-1117
    • Hardison, R.1
  • 2
    • 7944231804 scopus 로고    scopus 로고
    • Functional adaptation and its molecular basis in vertebrate hemoglobins, neuroglobins and cytoglobins
    • DOI 10.1016/j.resp.2004.04.018, PII S1569904804002034
    • Weber RE, Fago A (2004) Functional adaptation and its molecular basis in vertebrate hemoglobins, neuroglobins and cytoglobins. Respir Physiol Neurobiol 144(2-3):141-159. doi: 10.1016/j.resp. 2004.04.018 (Pubitemid 39535958)
    • (2004) Respiratory Physiology and Neurobiology , vol.144 , Issue.SPEC. ISS. , pp. 141-159
    • Weber, R.E.1    Fago, A.2
  • 3
    • 61549133928 scopus 로고    scopus 로고
    • Structure and function evolution in the superfamily of globins
    • doi:S1631-0691 08 00227-8
    • Wajcman H, Kiger L, Marden MC (2009) Structure and function evolution in the superfamily of globins. C R Biol 332(2-3):273-282. doi:S1631-0691 (08) 00227-8
    • (2009) C R Biol , vol.332 , Issue.2-3 , pp. 273-282
    • Wajcman, H.1    Kiger, L.2    Marden, M.C.3
  • 4
    • 0036219963 scopus 로고    scopus 로고
    • Cytoglobin: A novel globin type ubiquitously expressed in vertebrate tissues
    • Burmester T, Ebner B, Weich B, Hankeln T (2002) Cytoglobin: a novel globin type ubiquitously expressed in vertebrate tissues. Mol Biol Evol 19(4):416-421 (Pubitemid 34289416)
    • (2002) Molecular Biology and Evolution , vol.19 , Issue.4 , pp. 416-421
    • Burmester, T.1    Ebner, B.2    Weich, B.3    Hankeln, T.4
  • 5
    • 0034726874 scopus 로고    scopus 로고
    • A vertebrate globin expressed in the brain
    • doi:10.1038/35035093
    • Burmester T, Weich B, Reinhardt S, Hankeln T (2000) A vertebrate globin expressed in the brain. Nature 407(6803):520-523. doi:10.1038/35035093
    • (2000) Nature , vol.407 , Issue.6803 , pp. 520-523
    • Burmester, T.1    Weich, B.2    Reinhardt, S.3    Hankeln, T.4
  • 8
    • 0037205447 scopus 로고    scopus 로고
    • A ubiquitously expressed human hexacoordinate hemoglobin
    • DOI 10.1074/jbc.M201934200
    • Trent JT, Hargrove MS (2002) A ubiquitously expressed human hexacoordinate hemoglobin. J Bio Chem 277(22):19538-19545 (Pubitemid 34967466)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.22 , pp. 19538-19545
    • Trent III, J.T.1    Hargrove, M.S.2
  • 9
    • 10644291828 scopus 로고    scopus 로고
    • Nitric oxide dioxygenase function and mechanism of flavohemoglobin, hemoglobin, myoglobin and their associated reductases
    • DOI 10.1016/j.jinorgbio.2004.10.003, PII S016201340400296X, Heme-Diatomic Interactions, Part 1
    • Gardner PR (2005) Nitric oxide dioxygenase function and mechanism of flavohemoglobin, hemoglobin, myoglobin and their associated reductases. J Inorg Biochem 99(1):247-266. doi:S0162-0134 (04) 00296-X (Pubitemid 39646484)
    • (2005) Journal of Inorganic Biochemistry , vol.99 , Issue.1 , pp. 247-266
    • Gardner, P.R.1
  • 10
    • 61849150615 scopus 로고    scopus 로고
    • The new chemical biology of nitrite reactions with hemoglobin: R-state catalysis, oxidative denitrosylation, and nitrite reductase/anhydrase
    • doi:10.1021/ar800089j
    • Gladwin MT, Grubina R, Doyle MP (2009) The new chemical biology of nitrite reactions with hemoglobin: R-state catalysis, oxidative denitrosylation, and nitrite reductase/anhydrase. Acc Chem Res 42(1):157-167. doi:10.1021/ar800089j
    • (2009) Acc Chem Res , vol.42 , Issue.1 , pp. 157-167
    • Gladwin, M.T.1    Grubina, R.2    Doyle, M.P.3
  • 11
    • 53449085187 scopus 로고    scopus 로고
    • The functional nitrite reductase activity of the heme-globins
    • doi:blood-2008-01-115261
    • Gladwin MT, Kim-Shapiro DB (2008) The functional nitrite reductase activity of the heme-globins. Blood 112(7):2636-2647. doi:blood-2008-01-115261
    • (2008) Blood , vol.112 , Issue.7 , pp. 2636-2647
    • Gladwin, M.T.1    Kim-Shapiro, D.B.2
  • 12
    • 77955880548 scopus 로고    scopus 로고
    • The redox activity of hemoglobins: From physiologic functions to pathologic mechanisms
    • doi:10.1089/ars.2009.2974
    • Reeder BJ (2010) The redox activity of hemoglobins: from physiologic functions to pathologic mechanisms. Antioxid Redox Signal 13(7):1087-1123. doi:10.1089/ars.2009.2974
    • (2010) Antioxid Redox Signal , vol.13 , Issue.7 , pp. 1087-1123
    • Reeder, B.J.1
  • 13
    • 44049108195 scopus 로고    scopus 로고
    • Diversity of globin function: Enzymatic, transport, storage, and sensing
    • doi:R700029200
    • Vinogradov SN, Moens L (2008) Diversity of globin function: enzymatic, transport, storage, and sensing. J Biol Chem 283(14):8773-8777. doi:R700029200
    • (2008) J Biol Chem , vol.283 , Issue.14 , pp. 8773-8777
    • Vinogradov, S.N.1    Moens, L.2
  • 14
    • 0035816696 scopus 로고    scopus 로고
    • Characterization of a stellate cell activation-associated protein (STAP) with peroxidase activity found in rat hepatic stellate cells
    • Kawada N, Kristensen DB, Asahina K, Nakatani K, Minamiyama Y, Seki S, Yoshizato K (2001) Characterization of a stellate cell activation-associated protein (STAP) with peroxidase activity found in rat hepatic stellate cells. J Biol Chem 276(27):25318-25323
    • (2001) J Biol Chem , vol.276 , Issue.27 , pp. 25318-25323
    • Kawada, N.1    Kristensen, D.B.2    Asahina, K.3    Nakatani, K.4    Minamiyama, Y.5    Seki, S.6    Yoshizato, K.7
  • 20
    • 0038333244 scopus 로고    scopus 로고
    • Characterization of the heme environmental structure of cytoglobin, a fourth globin in humans
    • DOI 10.1021/bi027067e
    • Sawai H, Kawada N, Yoshizato K, Nakajima H, Aono S, Shiro Y (2003) Characterization of the heme environmental structure of cytoglobin, a fourth globin in humans. Biochemistry 42(17):5133-5142. doi:10.1021/bi027067e (Pubitemid 36532068)
    • (2003) Biochemistry , vol.42 , Issue.17 , pp. 5133-5142
    • Sawai, H.1    Kawada, N.2    Yoshizato, K.3    Nakajima, H.4    Aono, S.5    Shiro, Y.6
  • 21
    • 46349108421 scopus 로고    scopus 로고
    • Cellular protection from oxidative DNA damage by over-expression of the novel globin cytoglobin in vitro
    • DOI 10.1093/mutage/gen013
    • Hodges NJ, Innocent N, Dhanda S, Graham M (2008) Cellular protection from oxidative DNA damage by over-expression of the novel globin cytoglobin in vitro. Mutagenesis 23(4):293-298. doi:10.1093/mutage/gen013 (Pubitemid 351918962)
    • (2008) Mutagenesis , vol.23 , Issue.4 , pp. 293-298
    • Hodges, N.J.1    Innocent, N.2    Dhanda, S.3    Graham, M.4
  • 22
    • 82255176679 scopus 로고    scopus 로고
    • Lipid binding to cytoglobin leads to a change in heme coordination: A role for cytoglobin in lipid signalling of oxidative stress
    • doi: BJ20101136
    • Reeder BJ, Svistunenko D, Wilson M (2010) Lipid binding to cytoglobin leads to a change in heme coordination: a role for cytoglobin in lipid signalling of oxidative stress. Biochem J. doi: BJ20101136
    • (2010) Biochem J
    • Reeder, B.J.1    Svistunenko, D.2    Wilson, M.3
  • 29
    • 17144420129 scopus 로고    scopus 로고
    • Functional properties of neuroglobin and cytoglobin. Insights into the ancestral physiological roles of globins
    • DOI 10.1080/15216540500037299
    • Fago A, Hundahl C, Malte H, Weber RE (2004) Functional properties of neuroglobin and cytoglobin. Insights into the ancestral physiological roles of globins. IUBMB Life 56(11-12):689-696 (Pubitemid 40515814)
    • (2004) IUBMB Life , vol.56 , Issue.11-12 , pp. 689-696
    • Fago, A.1    Hundahl, C.2    Malte, H.3    Weber, R.E.4
  • 30
    • 77956487198 scopus 로고    scopus 로고
    • Hypoxic regulation of cytoglobin and neuroglobin expression in human normal and tumor tissues
    • doi:1475-2867-10-33
    • Emara M, Turner AR, Allalunis-Turner J (2010) Hypoxic regulation of cytoglobin and neuroglobin expression in human normal and tumor tissues. Cancer Cell Int 10:33. doi:1475-2867-10-33
    • (2010) Cancer Cell Int , vol.10 , pp. 33
    • Emara, M.1    Turner, A.R.2    Allalunis-Turner, J.3
  • 31
    • 56549090632 scopus 로고    scopus 로고
    • Localization and expression pattern of cytoglobin in carbon tetrachloride-induced liver fibrosis
    • doi:S0378-4274 08 01276-9
    • Man KN, Philipsen S, Tan-Un KC (2008) Localization and expression pattern of cytoglobin in carbon tetrachloride-induced liver fibrosis. Toxicol Lett 183(1-3):36-44. doi:S0378-4274 (08) 01276-9
    • (2008) Toxicol Lett , vol.183 , Issue.1-3 , pp. 36-44
    • Man, K.N.1    Philipsen, S.2    Tan-Un, K.C.3
  • 32
    • 33750705253 scopus 로고    scopus 로고
    • Neuroglobin and cytoglobin overexpression protects human SH-SY5Y neuroblastoma cells against oxidative stress-induced cell death
    • DOI 10.1016/j.neulet.2006.09.027, PII S030439400600975X
    • Fordel E, Thijs L, Martinet W, Lenjou M, Laufs T, Van Bockstaele D, Moens L, Dewilde S (2006) Neuroglobin and cytoglobin overexpression protects human SH-SY5Y neuroblastoma cells against oxidative stress-induced cell death. Neurosci Lett 410(2):146-151 (Pubitemid 44709414)
    • (2006) Neuroscience Letters , vol.410 , Issue.2 , pp. 146-151
    • Fordel, E.1    Thijs, L.2    Martinet, W.3    Lenjou, M.4    Laufs, T.5    Van Bockstaele, D.6    Moens, L.7    Dewilde, S.8
  • 33
    • 33745264870 scopus 로고    scopus 로고
    • Hypoxia differentially regulates the expression of neuroglobin and cytoglobin in rat brain
    • DOI 10.1016/j.brainres.2006.04.063, PII S0006899306011152
    • Li RC, Lee SK, Pouranfar F, Brittian KR, Clair HB, Row BW, Wang Y, Gozal D (2006) Hypoxia differentially regulates the expression of neuroglobin and cytoglobin in rat brain. Brain Res 1096(1):173-179 (Pubitemid 43928926)
    • (2006) Brain Research , vol.1096 , Issue.1 , pp. 173-179
    • Li, R.C.1    Lee, S.K.2    Pouranfar, F.3    Brittian, K.R.4    Clair, H.B.5    Row, B.W.6    Wang, Y.7    Gozal, D.8
  • 36
    • 33846863589 scopus 로고    scopus 로고
    • Nitric oxide and peroxynitrite in health and disease
    • DOI 10.1152/physrev.00029.2006
    • Pacher P, Beckman JS, Liaudet L (2007) Nitric oxide and peroxynitrite in health and disease. Physiol Rev 87(1):315-424. doi:87/1/315 (Pubitemid 46217686)
    • (2007) Physiological Reviews , vol.87 , Issue.1 , pp. 315-424
    • Pacher, P.1    Beckman, J.S.2    Liaudet, L.3
  • 37
    • 2642546072 scopus 로고    scopus 로고
    • Interspecies comparison of neuroglobin, cytoglobin and myoglobin: Sequence evolution and candidate regulatory elements
    • DOI 10.1159/000078011
    • Wystub S, Ebner B, Fuchs C, Weich B, Burmester T, Hankeln T (2004) Interspecies comparison of neuroglobin, cytoglobin and myoglobin: sequence evolution and candidate regulatory elements. Cytogenet Genome Res 105(1):65-78 (Pubitemid 38823859)
    • (2004) Cytogenetic and Genome Research , vol.105 , Issue.1 , pp. 65-78
    • Wystub, S.1    Ebner, B.2    Fuchs, C.3    Weich, B.4    Burmester, T.5    Hankeln, T.6
  • 38
    • 33645823676 scopus 로고    scopus 로고
    • Downregulation of the cytoglobin gene, located on 17q25, in tylosis with oesophageal cancer (TOC): Evidence for trans-allele repression
    • doi:10.1093/hmg/ddl042
    • McRonald FE, Liloglou T, Xinarianos G, Hill L, Rowbottom L, Langan JE, Ellis A, Shaw JM, Field JK, Risk JM (2006) Downregulation of the cytoglobin gene, located on 17q25, in tylosis with oesophageal cancer (TOC): evidence for trans-allele repression. Hum Mol Genet 15(8):1271-1277. doi:10.1093/hmg/ddl042
    • (2006) Hum Mol Genet , vol.15 , Issue.8 , pp. 1271-1277
    • McRonald, F.E.1    Liloglou, T.2    Xinarianos, G.3    Hill, L.4    Rowbottom, L.5    Langan, J.E.6    Ellis, A.7    Shaw, J.M.8    Field, J.K.9    Risk, J.M.10
  • 39
    • 0030460724 scopus 로고    scopus 로고
    • Hypoxia response elements in the aldolase A, enolase 1, and lactate dehydrogenase A gene promoters contain essential binding sites for hypoxia-inducible factor 1
    • Semenza GL, Jiang B-H, Leung SW, Passantino R, Concordet J-P, Maire P, Giallongo A (1996) Hypoxia response elements in the aldolase A, enolase 1, and lactate dehydrogenase A gene promoters contain essential binding sites for hypoxia-inducible factor 1. J Biol Chem 271(51):32529-32537
    • (1996) J Biol Chem , vol.271 , Issue.51 , pp. 32529-32537
    • Semenza, G.L.1    Jiang, B.-H.2    Leung, S.W.3    Passantino, R.4    Concordet, J.-P.5    Maire, P.6    Giallongo, A.7
  • 40
    • 70449527373 scopus 로고    scopus 로고
    • Hypoxia, hypoxiainducible factors (HIF), HIF hydroxylases and oxygen sensing
    • doi:10.1007/s00018-009-0147-7
    • Webb JD, Coleman ML, Pugh CW (2009) Hypoxia, hypoxiainducible factors (HIF), HIF hydroxylases and oxygen sensing. Cell Mol Life Sci 66(22):3539-3554. doi:10.1007/s00018-009-0147-7
    • (2009) Cell Mol Life Sci , vol.66 , Issue.22 , pp. 3539-3554
    • Webb, J.D.1    Coleman, M.L.2    Pugh, C.W.3
  • 41
    • 0036359548 scopus 로고    scopus 로고
    • Hypoxia - A key regulatory factor in tumour growth
    • Harris AL (2002) Hypoxia-a key regulatory factor in tumour growth. Nat Rev Cancer 2(1):38-47 (Pubitemid 37328806)
    • (2002) Nature Reviews Cancer , vol.2 , Issue.1 , pp. 38-47
    • Harris, A.L.1
  • 42
    • 34447547148 scopus 로고    scopus 로고
    • Regulation of tumor pH and the role of carbonic anhydrase 9
    • DOI 10.1007/s10555-007-9064-0, Special issue on Hypoxia and Cancer, Guest Editor: Gregg L. Semenza
    • Swietach P, Vaughan-Jones R, Harris A (2007) Regulation of tumor pH and the role of carbonic anhydrase 9. Cancer Metastasis Rev 26(2):299-310 (Pubitemid 47101667)
    • (2007) Cancer and Metastasis Reviews , vol.26 , Issue.2 , pp. 299-310
    • Swietach, P.1    Vaughan-Jones, R.D.2    Harris, A.L.3
  • 43
    • 50149097983 scopus 로고    scopus 로고
    • Hypoxia, HIF1 and glucose metabolism in the solid tumour
    • Denko NC (2008) Hypoxia, HIF1 and glucose metabolism in the solid tumour. Nat Rev Cancer 8(9):705-713
    • (2008) Nat Rev Cancer , vol.8 , Issue.9 , pp. 705-713
    • Denko, N.C.1
  • 44
    • 75149190912 scopus 로고    scopus 로고
    • Iron homeostasis and its interaction with prolyl hydroxylases
    • Mole D (2010) Iron homeostasis and its interaction with prolyl hydroxylases. Antioxid Redox Signal 12(4):445-458
    • (2010) Antioxid Redox Signal , vol.12 , Issue.4 , pp. 445-458
    • Mole, D.1
  • 45
    • 39749114978 scopus 로고    scopus 로고
    • Hypoxia and metabolism: Hypoxia, DNA repair and genetic instability
    • DOI 10.1038/nrc2344, PII NRC2344
    • Bristow RG, Hill RP (2008) Hypoxia and metabolism: hypoxia, DNA repair and genetic instability. Nat Rev Cancer 8(3):180-192 (Pubitemid 351301853)
    • (2008) Nature Reviews Cancer , vol.8 , Issue.3 , pp. 180-192
    • Bristow, R.G.1    Hill, R.P.2
  • 46
    • 0030020622 scopus 로고    scopus 로고
    • Characterization of the hypoxia-inducible protein binding site within the pyrimidinerich tract in the 3'-untranslated region of the tyrosine hydroxylase mRNA
    • Czyzyk-Krzeska MF, Beresh JE (1996) Characterization of the hypoxia-inducible protein binding site within the pyrimidinerich tract in the 3'-untranslated region of the tyrosine hydroxylase mRNA. J Biol Chem 271(6):3293-3299
    • (1996) J Biol Chem , vol.271 , Issue.6 , pp. 3293-3299
    • Czyzyk-Krzeska, M.F.1    Beresh, J.E.2
  • 49
    • 59849120420 scopus 로고    scopus 로고
    • Inflammatory cytokine production by human neutrophils involves C/EBP transcription factors
    • doi:182/1/563
    • Cloutier A, Guindi C, Larivee P, Dubois CM, Amrani A, McDonald PP (2009) Inflammatory cytokine production by human neutrophils involves C/EBP transcription factors. J Immunol 182(1):563-571. doi:182/1/563
    • (2009) J Immunol , vol.182 , Issue.1 , pp. 563-571
    • Cloutier, A.1    Guindi, C.2    Larivee, P.3    Dubois, C.M.4    Amrani, A.5    McDonald, P.P.6
  • 50
    • 51349163517 scopus 로고    scopus 로고
    • Immunology: Oxysterols hold T cells in check
    • doi:455040a
    • Glass CK, Saijo K (2008) Immunology: oxysterols hold T cells in check. Nature 455(7209):40-41. doi:455040a
    • (2008) Nature , vol.455 , Issue.7209 , pp. 40-41
    • Glass, C.K.1    Saijo, K.2
  • 51
    • 69949160564 scopus 로고    scopus 로고
    • Redox mechanisms in hepatic chronic wound healing and fibrogenesis
    • doi:1755-1536-1-5
    • Novo E, Parola M (2008) Redox mechanisms in hepatic chronic wound healing and fibrogenesis. Fibrogenesis Tissue Repair 1(1):5. doi:1755-1536-1-5
    • (2008) Fibrogenesis Tissue Repair , vol.1 , Issue.1 , pp. 5
    • Novo, E.1    Parola, M.2
  • 52
    • 35948992285 scopus 로고    scopus 로고
    • Healthy aging and longevity third international conference
    • Dwyer J, Li H, Xu D, Liu J-P (2007) Ann N Y Acad Sci 1114:36-47 (Healthy Aging and Longevity Third International Conference)
    • (2007) Ann N Y Acad Sci , vol.1114 , pp. 36-47
    • Dwyer, J.1    Li, H.2    Xu, D.3    Liu, J.-P.4
  • 53
    • 1642443906 scopus 로고    scopus 로고
    • Ets-1 Regulates TNF-α-Induced Matrix Metalloproteinase-9 and Tenascin Expression in Primary Bronchial Fibroblasts
    • Nakamura Y, Esnault S, Maeda T, Kelly EAB, Malter JS, Jarjour NN (2004) Ets-1 regulates TNF-a-induced matrix metalloproteinase-9 and tenascin expression in primary bronchial fibroblasts. J Immunol 172(3):1945-1952 (Pubitemid 38116845)
    • (2004) Journal of Immunology , vol.172 , Issue.3 , pp. 1945-1952
    • Nakamura, Y.1    Esnault, S.2    Maeda, T.3    Kelly, E.A.B.4    Malter, J.S.5    Jarjour, N.N.6
  • 56
    • 77952526531 scopus 로고    scopus 로고
    • Epoetin-d reduces oxidative stress in primary human renal tubular cells
    • doi:10.1155/2010/395785
    • De Beuf A, Hou XH, D'Haese PC, Verhulst A (2010) Epoetin-d reduces oxidative stress in primary human renal tubular cells. J Biomed Biotechnol 2010:395785. doi:10.1155/2010/395785
    • (2010) J Biomed Biotechnol , vol.2010 , pp. 395785
    • De Beuf, A.1    Hou, X.H.2    D'Haese, P.C.3    Verhulst, A.4
  • 57
    • 7244245630 scopus 로고    scopus 로고
    • Allosteric regulation and temperature dependence of oxygen binding in human neuroglobin and cytoglobin
    • Fago A, Hundahl C, Dewilde S, Gilany K, Moens L, Weber RE (2004) Allosteric regulation and temperature dependence of oxygen binding in human neuroglobin and cytoglobin. J Biol Chem 279(43):44417-44426
    • (2004) J Biol Chem , vol.279 , Issue.43 , pp. 44417-44426
    • Fago, A.1    Hundahl, C.2    Dewilde, S.3    Gilany, K.4    Moens, L.5    Weber, R.E.6
  • 58
    • 77954894512 scopus 로고    scopus 로고
    • Nitric-oxide dioxygenase function of human cytoglobin with cellular reductants and in rat hepatocytes
    • doi:M110.132340
    • Gardner AM, Cook MR, Gardner PR (2010) Nitric-oxide dioxygenase function of human cytoglobin with cellular reductants and in rat hepatocytes. J Biol Chem 285(31):23850-23857. doi:M110.132340
    • (2010) J Biol Chem , vol.285 , Issue.31 , pp. 23850-23857
    • Gardner, A.M.1    Cook, M.R.2    Gardner, P.R.3
  • 59
    • 67649763457 scopus 로고    scopus 로고
    • Cytoglobin is expressed in the vasculature and regulates cell respiration and proliferation via nitric oxide dioxygenation
    • Halligan KE, Jourd'heuil FL, Jourd'heuil D (2009) Cytoglobin is expressed in the vasculature and regulates cell respiration and proliferation via nitric oxide dioxygenation. J Biol Chem 284(13):8539-8547
    • (2009) J Biol Chem , vol.284 , Issue.13 , pp. 8539-8547
    • Halligan, K.E.1    Jourd'heuil, F.L.2    Jourd'heuil, D.3
  • 61
    • 44349180793 scopus 로고    scopus 로고
    • NO dioxygenase activity in hemoglobins in ubiquitous in vitro, but limited by reduction in vivo
    • Smagghe BJ, Trent James T, III Hargrove, Mark S (2008) NO dioxygenase activity in hemoglobins in ubiquitous in vitro, but limited by reduction in vivo. PLoS One 3(4):e2039
    • (2008) PLoS One , vol.3 , Issue.4
    • Smagghe, B.J.1    Trent James, T.2    Hargrove, I.3    Mark, S.4
  • 63
    • 10444280038 scopus 로고    scopus 로고
    • Structure-function studies on nitric oxide synthases
    • DOI 10.1016/j.jinorgbio.2004.10.016, PII S0162013404003216, Heme-Diatomic Interactions, Part 1
    • Li H, Poulos TL (2005) Structure-function studies on nitric oxide synthases. J Inorg Biochem 99(1):293-305. doi: S0162-0134 (04) 00321-6 (Pubitemid 39642983)
    • (2005) Journal of Inorganic Biochemistry , vol.99 , Issue.1 , pp. 293-305
    • Li, H.1    Poulos, T.L.2
  • 64
    • 77953752629 scopus 로고    scopus 로고
    • What part of NO don't you understand? Some answers to the cardinal questions in nitric oxide biology
    • doi:R110.101618
    • Hill BG, Dranka BP, Bailey SM, Lancaster JR Jr, Darley-Usmar VM (2010) What part of NO don't you understand? Some answers to the cardinal questions in nitric oxide biology. J Biol Chem 285(26):19699-19704. doi:R110.101618
    • (2010) J Biol Chem , vol.285 , Issue.26 , pp. 19699-19704
    • Hill, B.G.1    Dranka, B.P.2    Bailey, S.M.3    Lancaster Jr., J.R.4    Darley-Usmar, V.M.5
  • 65
    • 33847307112 scopus 로고    scopus 로고
    • Nitric oxide modulates oxygen sensing by hypoxia-inducible factor 1-dependent induction of prolyl hydroxylase 2
    • DOI 10.1074/jbc.M607065200
    • Berchner-Pfannschmidt U, Yamac H, Trinidad B, Fandrey J (2007) Nitric oxide modulates oxygen sensing by hypoxiainducible factor 1-dependent induction of prolyl hydroxylase 2. J Biol Chem 282(3):1788-1796. doi:M607065200 (Pubitemid 47076719)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.3 , pp. 1788-1796
    • Berchner-Pfannschmidt, U.1    Yamac, H.2    Trinidad, B.3    Fandrey, J.4
  • 66
    • 0033975850 scopus 로고    scopus 로고
    • Hypoxia response element of the human vascular endothelial growth factor gene mediates transcriptional regulation by nitric oxide: Control of hypoxia- inducible factor-1 activity by nitric oxide
    • Kimura H, Weisz A, Kurashima Y, Hashimoto K, Ogura T, D'Acquisto F, Addeo R, Makuuchi M, Esumi H (2000) Hypoxia response element of the human vascular endothelial growth factor gene mediates transcriptional regulation by nitric oxide: control of hypoxia-inducible factor-1 activity by nitric oxide. Blood 95(1):189-197 (Pubitemid 30017242)
    • (2000) Blood , vol.95 , Issue.1 , pp. 189-197
    • Kimura, H.1    Weisz, A.2    Kurashima, Y.3    Hashimoto, K.4    Ogura, T.5    D'Acquisto, F.6    Addeo, R.7    Makuuchi, M.8    Esumi, H.9
  • 67
    • 0042469448 scopus 로고    scopus 로고
    • Nitric oxide impairs normoxic degradation of HIF-1α by inhibition of prolyl hydroxylases
    • DOI 10.1091/mbc.E02-12-0791
    • Metzen E, Zhou J, Jelkmann W, Fandrey J, Brune B (2003) Nitric oxide impairs normoxic degradation of HIF-1alpha by inhibition of prolyl hydroxylases. Mol Biol Cell 14(8):3470-3481. doi:10.1091/mbc. E02-12-0791E02-12-0791 (Pubitemid 37013142)
    • (2003) Molecular Biology of the Cell , vol.14 , Issue.8 , pp. 3470-3481
    • Metzen, E.1    Zhou, J.2    Jelkmann, W.3    Fandrey, J.4    Brune, B.5
  • 68
    • 36348953730 scopus 로고    scopus 로고
    • Nitric oxide and mitochondrial signaling: From physiology to pathophysiology
    • DOI 10.1161/ATVBAHA.107.151167
    • Erusalimsky JD, Moncada S (2007) Nitric oxide and mitochondrial signaling: from physiology to pathophysiology. Arterioscler Thromb Vasc Biol 27(12):2524-2531. doi: ATVBAHA.107.151167 (Pubitemid 350158901)
    • (2007) Arteriosclerosis, Thrombosis, and Vascular Biology , vol.27 , Issue.12 , pp. 2524-2531
    • Erusalimsky, J.D.1    Moncada, S.2
  • 69
    • 34250861281 scopus 로고    scopus 로고
    • Cytoglobin up-regulated by hydrogen peroxide plays a protective role in oxidative stress
    • DOI 10.1007/s11064-007-9317-x
    • Li D, Chen X, Li W-J, Yang Y-H, Wang J-Z, Yu A (2007) Cytoglobin up-regulated by hydrogen peroxide plays a protective role in oxidative stress. Neurochem Res 32(8):1375-1380 (Pubitemid 46988199)
    • (2007) Neurochemical Research , vol.32 , Issue.8 , pp. 1375-1380
    • Li, D.1    Chen, X.Q.2    Li, W.-J.3    Yang, Y.-H.4    Wang, J.-Z.5    Yu, A.C.H.6
  • 70
    • 70349087001 scopus 로고    scopus 로고
    • Cell cycle arrest induced by hydrogen peroxide is associated with modulation of oxidative stress related genes in breast cancer cells
    • doi:10.3181/0903-rm-98
    • Chua P-J, Yip GW-C, Bay B-H (2009) Cell cycle arrest induced by hydrogen peroxide is associated with modulation of oxidative stress related genes in breast cancer cells. Exp Biol Med 234(9):1086-1094. doi:10.3181/0903-rm-98
    • (2009) Exp Biol Med , vol.234 , Issue.9 , pp. 1086-1094
    • Chua, P.-J.1    Yip, G.W.-C.2    Bay, B.-H.3
  • 71
    • 33846968462 scopus 로고    scopus 로고
    • Neuroglobin and cytoglobin expression in mice
    • Fordel E, Thijs L, Moens L, Dewilde S (2007) Neuroglobin and cytoglobin expression in mice. FEBS J 274(5):1312-1317
    • (2007) FEBS J , vol.274 , Issue.5 , pp. 1312-1317
    • Fordel, E.1    Thijs, L.2    Moens, L.3    Dewilde, S.4
  • 75
    • 34447518537 scopus 로고    scopus 로고
    • Anoxia or oxygen and glucose deprivation in SH-SY5Y cells: A step closer to the unraveling of neuroglobin and cytoglobin functions
    • DOI 10.1016/j.gene.2007.03.022, PII S0378111907002211
    • Fordel E, Thijs L, Martinet W, Schrijvers D, Moens L, Dewilde S (2007) Anoxia or oxygen and glucose deprivation in SH-SY5Y cells: a step closer to the unraveling of neuroglobin and cytoglobin functions. Gene 398(1-2):114-122 (Pubitemid 47068903)
    • (2007) Gene , vol.398 , Issue.1-2 SPEC. ISS. , pp. 114-122
    • Fordel, E.1    Thijs, L.2    Martinet, W.3    Schrijvers, D.4    Moens, L.5    Dewilde, S.6
  • 76
    • 48849090525 scopus 로고    scopus 로고
    • Reactions of ferrous neuroglobin and cytoglobin with nitrite under anaerobic conditions
    • Petersen MG, Dewilde S, Fago A (2008) Reactions of ferrous neuroglobin and cytoglobin with nitrite under anaerobic conditions. J Inorg Biochem 102(9):1777-1782
    • (2008) J Inorg Biochem , vol.102 , Issue.9 , pp. 1777-1782
    • Petersen, M.G.1    Dewilde, S.2    Fago, A.3
  • 77
    • 0034644756 scopus 로고    scopus 로고
    • Nitric-oxide dioxygenase activity and function of flavohemoglobins sensitivity to nitric oxide and carbon monoxide inhibition
    • doi:10.1074/jbc. M004141200
    • Gardner PR, Gardner AM, Martin LA, Dou Y, Li T, Olson JS, Zhu H, Riggs AF (2000) Nitric-oxide dioxygenase activity and function of flavohemoglobins sensitivity to nitric oxide and carbon monoxide inhibition. J Biol Chem 275(41):31581-31587. doi:10.1074/jbc. M004141200
    • (2000) J Biol Chem , vol.275 , Issue.41 , pp. 31581-31587
    • Gardner, P.R.1    Gardner, A.M.2    Martin, L.A.3    Dou, Y.4    Li, T.5    Olson, J.S.6    Zhu, H.7    Riggs, A.F.8
  • 78
    • 38549159026 scopus 로고    scopus 로고
    • Cellular and molecular mechanisms of fibrosis
    • DOI 10.1002/path.2277
    • Wynn TA (2008) Cellular and molecular mechanisms of fibrosis. J Pathol 214(2):199-210. doi:10.1002/path.2277 (Pubitemid 351160157)
    • (2008) Journal of Pathology , vol.214 , Issue.2 , pp. 199-210
    • Wynn, T.A.1
  • 79
    • 66149156949 scopus 로고    scopus 로고
    • Inhibition of transforming growth factor-b signaling by halofuginone as a modality for pancreas fibrosis prevention
    • doi: 10.1097/MPA.0b013e3181967670
    • Zion O, Genin O, Kawada N, Yoshizato K, Roffe S, Nagler A, Iovanna JL, Halevy O, Pines M (2009) Inhibition of transforming growth factor-b signaling by halofuginone as a modality for pancreas fibrosis prevention. Pancreas 38(4):427-435. doi: 10.1097/MPA.0b013e3181967670
    • (2009) Pancreas , vol.38 , Issue.4 , pp. 427-435
    • Zion, O.1    Genin, O.2    Kawada, N.3    Yoshizato, K.4    Roffe, S.5    Nagler, A.6    Iovanna, J.L.7    Halevy, O.8    Pines, M.9
  • 82
    • 34250810263 scopus 로고    scopus 로고
    • Effect of nitric oxide and peroxynitrite on type I collagen synthesis in normal and scleroderma dermal fibroblasts
    • DOI 10.1016/j.freeradbiomed.2007.04.017, PII S0891584907002845
    • Dooley A, Gao B, Shi-Wen X, Abraham DJ, Black CM, Jacobs M, Bruckdorfer KR (2007) Effect of nitric oxide and peroxynitrite on type I collagen synthesis in normal and scleroderma dermal fibroblasts. Free Radic Biol Med 43(2):253-264. doi: S0891-5849 (07) 00284-5 (Pubitemid 46977167)
    • (2007) Free Radical Biology and Medicine , vol.43 , Issue.2 , pp. 253-264
    • Dooley, A.1    Gao, B.2    Shi-Wen, X.3    Abraham, D.J.4    Black, C.M.5    Jacobs, M.6    Bruckdorfer, K.R.7
  • 83
    • 54549111991 scopus 로고    scopus 로고
    • Oxidative and nitrosative stress and fibrogenic response
    • doi:S1089-3261 08 00076-7 viii
    • Urtasun R, Conde de la Rosa L, Nieto N (2008) Oxidative and nitrosative stress and fibrogenic response. Clin Liver Dis 12(4):769-790. doi:S1089-3261 (08) 00076-7 viii
    • (2008) Clin Liver Dis , vol.12 , Issue.4 , pp. 769-790
    • Urtasun, R.1    Conde De La Rosa, L.2    Nieto, N.3
  • 84
    • 34250620498 scopus 로고    scopus 로고
    • Using nitric oxide to treat tendinopathy
    • DOI 10.1136/bjsm.2006.034447
    • Murrell GA (2007) Using nitric oxide to treat tendinopathy. Br J Sports Med 41(4):227-231. doi:bjsm.2006.034447 (Pubitemid 350143333)
    • (2007) British Journal of Sports Medicine , vol.41 , Issue.4 , pp. 227-231
    • Murrell, G.A.C.1
  • 85
    • 0036227477 scopus 로고    scopus 로고
    • Role of nitric oxide in wound repair
    • DOI 10.1016/S0002-9610(02)00815-2, PII S0002961002008152
    • Witte MB, Barbul A (2002) Role of nitric oxide in wound repair. Am J Surg 183(4):406-412. doi:S0002961002008152 (Pubitemid 34442505)
    • (2002) American Journal of Surgery , vol.183 , Issue.4 , pp. 406-412
    • Witte, M.B.1    Barbul, A.2
  • 86
    • 53849121922 scopus 로고    scopus 로고
    • HIF-1 and ventilatory acclimatization to chronic hypoxia
    • Powell FL, Fu Z (2008) HIF-1 and ventilatory acclimatization to chronic hypoxia. Respir Physiol Neurobiol 164(1-2):282-287
    • (2008) Respir Physiol Neurobiol , vol.164 , Issue.1-2 , pp. 282-287
    • Powell, F.L.1    Fu, Z.2
  • 87
    • 2642522806 scopus 로고    scopus 로고
    • Cytoglobin expression is upregulated in all tissues upon hypoxia: An in vitro and in vivo study by quantitative real-time PCR
    • DOI 10.1016/j.bbrc.2004.05.010, PII S0006291X04009660
    • Fordel E, Geuens E, Dewilde S, Rottiers P, Carmeliet P, Grooten J, Moens L (2004) Cytoglobin expression is upregulated in all tissues upon hypoxia: an in vitro and in vivo study by quantitative real-time PCR. Biochem Biophys Res Commun 319(2):342-348 (Pubitemid 38725952)
    • (2004) Biochemical and Biophysical Research Communications , vol.319 , Issue.2 , pp. 342-348
    • Fordel, E.1    Geuens, E.2    Dewilde, S.3    Rottiers, P.4    Carmeliet, P.5    Grooten, J.6    Moens, L.7
  • 88
    • 58249102180 scopus 로고    scopus 로고
    • Regulation and role of neuroglobin and cytoglobin under hypoxia
    • Burmester T, Gerlach F, Hankeln T (2007) Regulation and role of neuroglobin and cytoglobin under hypoxia. Adv Exp Med Biol 618:169-180
    • (2007) Adv Exp Med Biol , vol.618 , pp. 169-180
    • Burmester, T.1    Gerlach, F.2    Hankeln, T.3
  • 90
    • 27844563659 scopus 로고    scopus 로고
    • Protection from ischemic cell death by the induction of cytoglobin
    • DOI 10.1016/j.transproceed.2005.10.001, PII S0041134505011516
    • Stagner JI, Parthasarathy SN, Wyler K, Parthasarathy RN (2005) Protection from ischemic cell death by the induction of cytoglobin. Transplant Proc 37(8):3452-3453 (Pubitemid 41659918)
    • (2005) Transplantation Proceedings , vol.37 , Issue.8 , pp. 3452-3453
    • Stagner, J.I.1    Parthasarathy, S.N.2    Wyler, K.3    Parthasarathy, R.N.4
  • 91
    • 71249164310 scopus 로고    scopus 로고
    • Oxygen-sensing under the influence of nitric oxide
    • doi:S0898-6568 09 00321-0
    • Berchner-Pfannschmidt U, Tug S, Kirsch M, Fandrey J (2010) Oxygen-sensing under the influence of nitric oxide. Cell Signal 22(3):349-356. doi:S0898-6568 (09) 00321-0
    • (2010) Cell Signal , vol.22 , Issue.3 , pp. 349-356
    • Berchner-Pfannschmidt, U.1    Tug, S.2    Kirsch, M.3    Fandrey, J.4
  • 92
    • 57649116076 scopus 로고    scopus 로고
    • Nuclear oxygen sensing: Induction of endogenous prolyl-hydroxylase 2 activity by hypoxia and nitric oxide
    • doi:M804390200
    • Berchner-Pfannschmidt U, Tug S, Trinidad B, Oehme F, Yamac H, Wotzlaw C, Flamme I, Fandrey J (2008) Nuclear oxygen sensing: induction of endogenous prolyl-hydroxylase 2 activity by hypoxia and nitric oxide. J Biol Chem 283(46):31745-31753. doi:M804390200
    • (2008) J Biol Chem , vol.283 , Issue.46 , pp. 31745-31753
    • Berchner-Pfannschmidt, U.1    Tug, S.2    Trinidad, B.3    Oehme, F.4    Yamac, H.5    Wotzlaw, C.6    Flamme, I.7    Fandrey, J.8
  • 93
    • 0033605676 scopus 로고    scopus 로고
    • Inhibition of hypoxia-inducible factor 1 activation by carbon monoxide and nitric oxide: Implications for oxygen sensing and signaling
    • DOI 10.1074/jbc.274.13.9038
    • Huang LE, Willmore WG, Gu J, Goldberg MA, Bunn HF (1999) Inhibition of hypoxia-inducible factor 1 activation by carbon monoxide and nitric oxide Implications for oxygen sensing and signaling. J Biol Chem 274(13):9038-9044 (Pubitemid 29164709)
    • (1999) Journal of Biological Chemistry , vol.274 , Issue.13 , pp. 9038-9044
    • Huang, L.E.1    Willmore, W.G.2    Gu, J.3    Goldberg, M.A.4    Bunn, H.F.5
  • 95
    • 77952067882 scopus 로고    scopus 로고
    • Anoxic nitric oxide cycling in plants: Participating reactions and possible mechanisms
    • doi:PPL1314
    • Igamberdiev AU, Bykova NV, Shah JK, Hill RD (2010) Anoxic nitric oxide cycling in plants: participating reactions and possible mechanisms. Physiol Plant 138(4):393-404. doi:PPL1314
    • (2010) Physiol Plant , vol.138 , Issue.4 , pp. 393-404
    • Igamberdiev, A.U.1    Bykova, N.V.2    Shah, J.K.3    Hill, R.D.4
  • 96
    • 33747596652 scopus 로고    scopus 로고
    • Oxygen sensing by mitochondria at complex III: The paradox of increased reactive oxygen species during hypoxia
    • DOI 10.1113/expphysiol.2006.033506
    • Guzy RD, Schumacker PT (2006) Oxygen sensing by mitochondria at complex III: the paradox of increased reactive oxygen species during hypoxia. Exp Physiol 91(5):807-819 (Pubitemid 44266577)
    • (2006) Experimental Physiology , vol.91 , Issue.5 , pp. 807-819
    • Guzy, R.D.1    Schumacker, P.T.2
  • 97
    • 44349140101 scopus 로고    scopus 로고
    • Hypoxia-inducible factor signaling in the development of tissue fibrosis
    • Higgins DF, Kimuro, Kuniko, Iwano, Masayuki, Hasse, Volker H (2008) Hypoxia-inducible factor signaling in the development of tissue fibrosis. Cell Cycle 7(9):1128-1132 (Pubitemid 351749261)
    • (2008) Cell Cycle , vol.7 , Issue.9 , pp. 1128-1132
    • Higgins, D.F.1    Kimura, K.2    Iwano, M.3    Haase, V.H.4
  • 98
    • 37549071817 scopus 로고    scopus 로고
    • Oxidative stress and antioxidants in the pathogenesis of pulmonary fibrosis: A potential role for Nrf2
    • Walters DM, Cho HY, Kleeberger SR (2008) Oxidative stress and antioxidants in the pathogenesis of pulmonary fibrosis: a potential role for Nrf2. Antioxid Redox Signal 10(2):321-332
    • (2008) Antioxid Redox Signal , vol.10 , Issue.2 , pp. 321-332
    • Walters, D.M.1    Cho, H.Y.2    Kleeberger, S.R.3
  • 99
    • 0033053458 scopus 로고    scopus 로고
    • 1 induces the expression of α1(I) procollagen mRNA by a hydrogen peroxide-C/EBPβ-dependent mechanism in rat hepatic stellate cells
    • García-Trevijano ER, Iraburu MJ, Fontana L, Domínguez- Rosales JA, Auster A, Covarrubias-Pinedo A, Rojkind M (1999) Transforming growth factor-b induces the expression of al1(i) procollagen mRNA by a hydrogen peroxide-C/EBPbetadependent mechanism in rat hepatic stellate cells. Hepatology 29 (3):960-970 (Pubitemid 29109616)
    • (1999) Hepatology , vol.29 , Issue.3 , pp. 960-970
    • Garcia-Trevijano, E.R.1    Iraburu, M.J.2    Fontana, L.3    Dominguez-Rosales, J.A.4    Auster, A.5    Covarrubias-Pinedo, A.6    Rojkind, M.7
  • 100
    • 33747834381 scopus 로고    scopus 로고
    • P53-mediated apoptosis, neuroglobin overexpression, and globin deposits in a patient with hereditary ferritinopathy
    • DOI 10.1097/01.jnen.0000228200.27539.19, PII 0000507220060700000009
    • Powers JM (2006) p53-mediated apoptosis, neuroglobin overexpression, and globin deposits in a patient with hereditary ferritinopathy. J Neuropathol Exp Neurol 65(7):716-721. doi: 10.1097/01.jnen. 0000228200.27539.19 (Pubitemid 44297262)
    • (2006) Journal of Neuropathology and Experimental Neurology , vol.65 , Issue.7 , pp. 716-721
    • Powers, J.M.1
  • 102
    • 33344455657 scopus 로고    scopus 로고
    • Promoter methylation of P16, RARβ, E-cadherin, cyclin A1 and cytoglobin in oral cancer: Quantitative evaluation using pyrosequencing
    • DOI 10.1038/sj.bjc.6602972
    • Shaw RJ, Liloglou T, Rogers SN, Brown JS, Vaughan ED, Lowe D, Field JK, Risk JM (2006) Promoter methylation of P16, RARb, E-cadherin, cyclin A1 and cytoglobin in oral cancer: quantitative evaluation using pyrosequencing. Br J Cancer 94(4):561-568 (Pubitemid 43289761)
    • (2006) British Journal of Cancer , vol.94 , Issue.4 , pp. 561-568
    • Shaw, R.J.1    Liloglou, T.2    Rogers, S.N.3    Brown, J.S.4    Vaughan, E.D.5    Lowe, D.6    Field, J.K.7    Risk, J.M.8
  • 103
    • 33745244805 scopus 로고    scopus 로고
    • Frequent genetic and epigenetic abnormalities contribute to the deregulation of cytoglobin in non-small cell lung cancer
    • DOI 10.1093/hmg/ddl128
    • Xinarianos G, McRonald FE, Risk JM, Bowers NL, Nikolaidis G, Field JK, Liloglou T (2006) Frequent genetic and epigenetic abnormalities contribute to the deregulation of cytoglobin in non-small cell lung cancer. Hum Mol Genet 15(13):2038-2044. doi:10.1093/hmg/ddl128 (Pubitemid 43923394)
    • (2006) Human Molecular Genetics , vol.15 , Issue.13 , pp. 2038-2044
    • Xinarianos, G.1    McRonald, F.E.2    Risk, J.M.3    Bowers, N.L.4    Nikolaidis, G.5    Field, J.K.6    Liloglou, T.7
  • 104
    • 38949099722 scopus 로고    scopus 로고
    • Oxygen and blood flow: Players in the pathogenesis of glaucoma
    • Mozaffarieh M, Grieshaber Matthias C, Flammer Josef (2008) Oxygen and blood flow: players in the pathogenesisof glaucoma. Mol Vis 14:224-233 (Pubitemid 351223391)
    • (2008) Molecular Vision , vol.14 , pp. 224-233
    • Mozaffarieh, M.1    Grieshaber, M.C.2    Flammer, J.3
  • 105
    • 77954632584 scopus 로고    scopus 로고
    • Hyaline astrocytic inclusions in pediatric epilepsy: Report of two cases
    • doi:7715
    • Adam J, Polivka M, Kaci R, Godfraind C, Gray F (2010) Hyaline astrocytic inclusions in pediatric epilepsy: report of two cases. Clin Neuropathol 29(4):246-253. doi:7715
    • (2010) Clin Neuropathol , vol.29 , Issue.4 , pp. 246-253
    • Adam, J.1    Polivka, M.2    Kaci, R.3    Godfraind, C.4    Gray, F.5
  • 106
    • 8544253949 scopus 로고    scopus 로고
    • Mitochondrial dysfunction and oxidative stress: Cause and consequence of epileptic seizures
    • DOI 10.1016/j.freeradbiomed.2004.08.021, PII S0891584904006823
    • Patel M (2004) Mitochondrial dysfunction and oxidative stress: cause and consequence of epileptic seizures. Free Radic Biol Med 37(12):1951-1962 (Pubitemid 39491316)
    • (2004) Free Radical Biology and Medicine , vol.37 , Issue.12 , pp. 1951-1962
    • Patel, M.1
  • 107
    • 77950642047 scopus 로고    scopus 로고
    • Mitochondrial dysfunction and oxidative stress in seizure-induced neuronal cell death
    • doi:10196099/1913
    • Chuang YC (2010) Mitochondrial dysfunction and oxidative stress in seizure-induced neuronal cell death. Acta Neurol Taiwan 19(1):3-15. doi:10196099/1913
    • (2010) Acta Neurol Taiwan , vol.19 , Issue.1 , pp. 3-15
    • Chuang, Y.C.1
  • 109
    • 47349109305 scopus 로고    scopus 로고
    • Molecular mechanism of hepatic stellate cell activation and antifibrotic therapeutic strategies
    • DOI 10.1007/s00535-008-2180-y
    • Li JT, Liao ZX, Ping J, Xu D, Wang H (2008) Molecular mechanism of hepatic stellate cell activation and antifibrotic therapeutic strategies. J Gastroenterol 43(6):419-428. doi: 10.1007/s00535-008-2180-y (Pubitemid 351997878)
    • (2008) Journal of Gastroenterology , vol.43 , Issue.6 , pp. 419-428
    • Li, J.-T.1    Liao, Z.-X.2    Ping, J.3    Xu, D.4    Wang, H.5
  • 110
    • 77649168237 scopus 로고    scopus 로고
    • Distinct proteomic features of two fibrogenic liver cell populations: Hepatic stellate cells and portal myofibroblasts
    • Bosselut N, Housset C, Marcelo P, Rey C, Burmester T, Vinh J, Vaubourdolle M, Cadoret A, Baudin B (2010) Distinct proteomic features of two fibrogenic liver cell populations: hepatic stellate cells and portal myofibroblasts. Proteomics 10(5):1017-1028
    • (2010) Proteomics , vol.10 , Issue.5 , pp. 1017-1028
    • Bosselut, N.1    Housset, C.2    Marcelo, P.3    Rey, C.4    Burmester, T.5    Vinh, J.6    Vaubourdolle, M.7    Cadoret, A.8    Baudin, B.9
  • 112
    • 0029132167 scopus 로고
    • Reversible binding and inhibition of catalase by nitric oxide
    • Brown GC (1995) Reversible binding and inhibition of catalase by nitric oxide. Eur J Biochem 232(1):188-191
    • (1995) Eur J Biochem , vol.232 , Issue.1 , pp. 188-191
    • Brown, G.C.1
  • 113
    • 0029918676 scopus 로고    scopus 로고
    • The chemistry and tumoricidal activity of nitric oxide/hydrogen peroxide and the implications to cell resistance/susceptibility
    • DOI 10.1074/jbc.271.11.6144
    • Farias-Eisner R, Chaudhuri G, Aeberhard E, Fukuto JM (1996) The chemistry and tumoricidal activity of nitric oxide/hydrogen peroxide and the implications to cell resistance/susceptibility. J Biol Chem 271(11):6144-6151 (Pubitemid 26095420)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.11 , pp. 6144-6151
    • Farias-Eisner, R.1    Chaudhuri, G.2    Aeberhard, E.3    Fukuto, J.M.4
  • 115
    • 34247351198 scopus 로고    scopus 로고
    • Nitric oxide increases toxicity of hydrogen peroxide against rat liver endothelial cells and hepatocytes by inhibition of hydrogen peroxide degradation
    • DOI 10.1152/ajpcell.00366.2006
    • Rauen U, Li T, Ioannidis I, de Groot H (2007) Nitric oxide increases toxicity of hydrogen peroxide against rat liver endothelial cells and hepatocytes by inhibition of hydrogen peroxide degradation. Am J Physiol Cell Physiol 292(4):C1440-C1449. doi:00366.2006 (Pubitemid 46631745)
    • (2007) American Journal of Physiology - Cell Physiology , vol.292 , Issue.4
    • Rauen, U.1    Li, T.2    Ioannidis, I.3    De Groot, H.4
  • 117
    • 0342944465 scopus 로고    scopus 로고
    • Endogenous nitric oxide is responsible for the early loss of P450 in cultured rat hepatocytes
    • DOI 10.1016/S0014-5793(98)01283-6, PII S0014579398012836
    • Lopez-Garcia MP (1998) Endogenous nitric oxide is responsible for the early loss of P450 in cultured rat hepatocytes. FEBS Lett 438(3):145-149. doi:S0014-5793 (98) 01283-6 (Pubitemid 28529263)
    • (1998) FEBS Letters , vol.438 , Issue.3 , pp. 145-149
    • Lopez-Garcia, M.P.1
  • 119
    • 13544252462 scopus 로고    scopus 로고
    • Palmoplantar keratodermas
    • DOI 10.1016/j.clindermatol.2004.09.005
    • Itin PH, Fistarol, Susanna K (2005) Palmoplantar keratodermas. Clin Dermatol 23(1):15-22 (Pubitemid 40222771)
    • (2005) Clinics in Dermatology , vol.23 , Issue.1 , pp. 15-22
    • Itin, P.H.1    Fistarol, S.K.2
  • 121
    • 2942729612 scopus 로고    scopus 로고
    • Novel microsatellite markers and single nucleotide polymorphisms refine the tylosis with oesophageal cancer (TOC) minimal region on 17q25 to 42.5 kb: Sequencing does not identify the causative gene
    • DOI 10.1007/s00439-004-1100-3
    • Langan J, Cole C, Huckle E, Byrne S, McRonald F, Rowbottom L, Ellis A, Shaw J, Leigh I, Kelsell D, Dunham I, Field J, Risk J (2004) Novel microsatellite markers and single nucleotide polymorphisms refine the tylosis with oesophageal cancer (TOC) minimal region on 17q25 to 42.5 kb: sequencing does not identify the causative gene. Hum Genet 114(6):534-540 (Pubitemid 39010850)
    • (2004) Human Genetics , vol.114 , Issue.6 , pp. 534-540
    • Langan, J.E.1    Cole, C.G.2    Huckle, E.J.3    Byrne, S.4    McRonald, F.E.5    Rowbottom, L.6    Ellis, A.7    Shaw, J.M.8    Leigh, I.M.9    Kelsell, D.P.10    Dunham, I.11    Field, J.K.12    Risk, J.M.13
  • 122
    • 21744443762 scopus 로고    scopus 로고
    • Loss of heterozygosity and transcriptome analyses of a 1.2 Mb candidate ovarian cancer tumor suppressor locus region at 17q25.1-q25.2
    • DOI 10.1002/mc.20096
    • Presneau N, Dewar K, Forgetta V, Provencher D, Mes-Masson A-M, Tonin PN (2005) Loss of heterozygosity and transcriptome analyses of a 1.2 Mb candidate ovarian cancer tumor suppressor locus region at 17q25.1-q25.2. Mol Carcinog 43(3):141-154 (Pubitemid 40944239)
    • (2005) Molecular Carcinogenesis , vol.43 , Issue.3 , pp. 141-154
    • Presneau, N.1    Dewar, K.2    Forgetta, V.3    Provencher, D.4    Mes-Masson, A.-M.5    Tonin, P.N.6
  • 125
    • 0034538299 scopus 로고    scopus 로고
    • Epigenetic gene deregulation in cancer
    • DOI 10.1054/bjoc.2000.1549
    • Malik K, Brown KW (2000) Epigenetic gene deregulation in cancer. Br J Cancer 83(12):1583-1588 (Pubitemid 32001697)
    • (2000) British Journal of Cancer , vol.83 , Issue.12 , pp. 1583-1588
    • Malik, K.1    Brown, K.W.2
  • 126
    • 77950023207 scopus 로고    scopus 로고
    • Oxidative stress and oxidative damage in carcinogenesis
    • doi:10.1177/0192623309356453
    • Klaunig JE, Kamendulis LM, Hocevar BA (2010) Oxidative stress and oxidative damage in carcinogenesis. Toxicol Pathol 38(1):96-109. doi:10.1177/0192623309356453
    • (2010) Toxicol Pathol , vol.38 , Issue.1 , pp. 96-109
    • Klaunig, J.E.1    Kamendulis, L.M.2    Hocevar, B.A.3
  • 127
    • 67650364193 scopus 로고    scopus 로고
    • Induced nitric oxide synthase as a major player in the oncogenic transformation of inflamed tissue
    • doi: 10.1007/978-1-60327-530-9-8
    • Yang GY, Taboada S, Liao J (2009) Induced nitric oxide synthase as a major player in the oncogenic transformation of inflamed tissue. Methods Mol Biol 512:119-156. doi: 10.1007/978-1-60327-530-9-8
    • (2009) Methods Mol Biol , vol.512 , pp. 119-156
    • Yang, G.Y.1    Taboada, S.2    Liao, J.3
  • 128
    • 50949115026 scopus 로고    scopus 로고
    • Myofibroblastin pulmonary and brain metastases of alveolar soft-part sarcoma: A novel target for treatment?
    • Genin O, Rechavi G, Nagler A, Ben-Itzhak O, Nazemi KJ, Pines M (2008) Myofibroblastin pulmonary and brain metastases of alveolar soft-part sarcoma: a novel target for treatment? Neoplasia 10(9):940-948
    • (2008) Neoplasia , vol.10 , Issue.9 , pp. 940-948
    • Genin, O.1    Rechavi, G.2    Nagler, A.3    Ben-Itzhak, O.4    Nazemi, K.J.5    Pines, M.6
  • 129
    • 67650071137 scopus 로고    scopus 로고
    • Targeting cancer cells by ROS-mediated mechanisms: A radical therapeutic approach?
    • Trachootham D, Alexandre J, Huang P (2009) Targeting cancer cells by ROS-mediated mechanisms: a radical therapeutic approach? Nat Rev Drug Discov 8(7):579-591
    • (2009) Nat Rev Drug Discov , vol.8 , Issue.7 , pp. 579-591
    • Trachootham, D.1    Alexandre, J.2    Huang, P.3
  • 130
    • 0242499448 scopus 로고    scopus 로고
    • Cytostatic and apoptotic actions of TGF-β in homeostasis and cancer
    • Siegel PM, Massague J (2003) Cytostatic and apoptotic actions of TGF-b in homeostasis and cancer. Nat Rev Cancer 3(11):807-820 (Pubitemid 37376979)
    • (2003) Nature Reviews Cancer , vol.3 , Issue.11 , pp. 807-820
    • Siegel, P.M.1    Massague, J.2
  • 131
    • 54749127408 scopus 로고    scopus 로고
    • Cytoglobin: A novel potential gene medicine for fibrosis and cancer therapy
    • Lv Y, Wang Qizhao, Diao Yong, Xu Ruian (2008) Cytoglobin: a novel potential gene medicine for fibrosis and cancer therapy. Curr Gene Ther 8(4):287-294
    • (2008) Curr Gene Ther , vol.8 , Issue.4 , pp. 287-294
    • Lv, Y.1    Qizhao, W.2    Yong, D.3    Ruian, X.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.