메뉴 건너뛰기




Volumn 53, Issue , 2016, Pages 22-34

Characterization of zebrafish neuroglobin and cytoglobins 1 and 2: Zebrafish cytoglobins provide insights into the transition from six-coordinate to five-coordinate globins

Author keywords

Cytoglobin; Neuroglobin; Nitrite reduction; Protein evolution; Protein lipid interaction

Indexed keywords

CYTOGLOBIN; CYTOGLOBIN 1; CYTOGLOBIN 2; HEME; LIPID; NEUROGLOBIN; NITRIC OXIDE; NITRITE; NITRITE REDUCTASE; OLEIC ACID; OXYGEN; RECOMBINANT PROTEIN; UNCLASSIFIED DRUG; GLOBIN; MESSENGER RNA; NERVE PROTEIN;

EID: 84955311200     PISSN: 10898603     EISSN: 10898611     Source Type: Journal    
DOI: 10.1016/j.niox.2015.12.004     Document Type: Article
Times cited : (40)

References (80)
  • 1
    • 84901003921 scopus 로고    scopus 로고
    • Mammalian nerve globins in search of functions
    • P. Ascenzi, S. Gustincich, and M. Marino Mammalian nerve globins in search of functions IUBMB Life 66 2014 268 276
    • (2014) IUBMB Life , vol.66 , pp. 268-276
    • Ascenzi, P.1    Gustincich, S.2    Marino, M.3
  • 2
    • 66149086544 scopus 로고    scopus 로고
    • What is the function of neuroglobin?
    • T. Burmester, and T. Hankeln What is the function of neuroglobin? J. Exp. Biol. 212 2009 1423 1428
    • (2009) J. Exp. Biol. , vol.212 , pp. 1423-1428
    • Burmester, T.1    Hankeln, T.2
  • 4
    • 84902348270 scopus 로고    scopus 로고
    • Function and evolution of vertebrate globins
    • T. Burmester, and T. Hankeln Function and evolution of vertebrate globins Acta Physiol. (Oxf) 211 2014 501 514
    • (2014) Acta Physiol. (Oxf) , vol.211 , pp. 501-514
    • Burmester, T.1    Hankeln, T.2
  • 5
    • 38849162730 scopus 로고    scopus 로고
    • The nitrate-nitrite-nitric oxide pathway in physiology and therapeutics
    • J.O. Lundberg, E. Weitzberg, and M.T. Gladwin The nitrate-nitrite-nitric oxide pathway in physiology and therapeutics Nat. Rev. Drug Discov. 7 2008 156 167
    • (2008) Nat. Rev. Drug Discov. , vol.7 , pp. 156-167
    • Lundberg, J.O.1    Weitzberg, E.2    Gladwin, M.T.3
  • 6
    • 84924029435 scopus 로고    scopus 로고
    • Hypoxia tolerance, nitric oxide, and nitrite: lessons from extreme animals
    • A. Fago, and F.B. Jensen Hypoxia tolerance, nitric oxide, and nitrite: lessons from extreme animals Physiology 30 2015 116 126
    • (2015) Physiology , vol.30 , pp. 116-126
    • Fago, A.1    Jensen, F.B.2
  • 7
    • 84899823580 scopus 로고    scopus 로고
    • The globin superfamily: functions in nitric oxide formation and decay
    • J. Tejero, and M.T. Gladwin The globin superfamily: functions in nitric oxide formation and decay Biol. Chem. 395 2014 631 639
    • (2014) Biol. Chem. , vol.395 , pp. 631-639
    • Tejero, J.1    Gladwin, M.T.2
  • 8
    • 53449085187 scopus 로고    scopus 로고
    • The functional nitrite reductase activity of the heme-globins
    • M.T. Gladwin, and D.B. Kim-Shapiro The functional nitrite reductase activity of the heme-globins Blood 112 2008 2636 2647
    • (2008) Blood , vol.112 , pp. 2636-2647
    • Gladwin, M.T.1    Kim-Shapiro, D.B.2
  • 10
    • 84922041980 scopus 로고    scopus 로고
    • Exploring the mechanisms of the reductase activity of neuroglobin by site-directed mutagenesis of the heme distal pocket
    • J. Tejero, C.E. Sparacino-Watkins, V. Ragireddy, S. Frizzell, and M.T. Gladwin Exploring the mechanisms of the reductase activity of neuroglobin by site-directed mutagenesis of the heme distal pocket Biochemistry 54 2015 722 733
    • (2015) Biochemistry , vol.54 , pp. 722-733
    • Tejero, J.1    Sparacino-Watkins, C.E.2    Ragireddy, V.3    Frizzell, S.4    Gladwin, M.T.5
  • 13
    • 48849090525 scopus 로고    scopus 로고
    • Reactions of ferrous neuroglobin and cytoglobin with nitrite under anaerobic conditions
    • M.G. Petersen, S. Dewilde, and A. Fago Reactions of ferrous neuroglobin and cytoglobin with nitrite under anaerobic conditions J. Inorg. Biochem. 102 2008 1777 1782
    • (2008) J. Inorg. Biochem. , vol.102 , pp. 1777-1782
    • Petersen, M.G.1    Dewilde, S.2    Fago, A.3
  • 14
    • 84867795031 scopus 로고    scopus 로고
    • Characterization of the mechanism and magnitude of cytoglobin-mediated nitrite reduction and nitric oxide generation under anaerobic conditions
    • H. Li, C. Hemann, T.M. Abdelghany, M.A. El-Mahdy, and J.L. Zweier Characterization of the mechanism and magnitude of cytoglobin-mediated nitrite reduction and nitric oxide generation under anaerobic conditions J. Biol. Chem. 287 2012 36623 36633
    • (2012) J. Biol. Chem. , vol.287 , pp. 36623-36633
    • Li, H.1    Hemann, C.2    Abdelghany, T.M.3    El-Mahdy, M.A.4    Zweier, J.L.5
  • 16
    • 79955448391 scopus 로고    scopus 로고
    • Interaction between alk1 and blood flow in the development of arteriovenous malformations
    • P. Corti, S. Young, C.Y. Chen, M.J. Patrick, E.R. Rochon, K. Pekkan, and B.L. Roman Interaction between alk1 and blood flow in the development of arteriovenous malformations Development 138 2011 1573 1582
    • (2011) Development , vol.138 , pp. 1573-1582
    • Corti, P.1    Young, S.2    Chen, C.Y.3    Patrick, M.J.4    Rochon, E.R.5    Pekkan, K.6    Roman, B.L.7
  • 18
    • 84856397079 scopus 로고    scopus 로고
    • Differential loss and retention of cytoglobin, myoglobin, and globin-E during the radiation of vertebrates
    • F.G. Hoffmann, J.C. Opazo, and J.F. Storz Differential loss and retention of cytoglobin, myoglobin, and globin-E during the radiation of vertebrates Genome Biology Evolution 3 2011 588 600
    • (2011) Genome Biology Evolution , vol.3 , pp. 588-600
    • Hoffmann, F.G.1    Opazo, J.C.2    Storz, J.F.3
  • 19
    • 78651484467 scopus 로고    scopus 로고
    • Changes of globin expression in the Japanese medaka (Oryzias latipes) in response to acute and chronic hypoxia
    • A. Wawrowski, F. Gerlach, T. Hankeln, and T. Burmester Changes of globin expression in the Japanese medaka (Oryzias latipes) in response to acute and chronic hypoxia J. Comp. Physiol. B 181 2011 199 208
    • (2011) J. Comp. Physiol. B , vol.181 , pp. 199-208
    • Wawrowski, A.1    Gerlach, F.2    Hankeln, T.3    Burmester, T.4
  • 20
    • 50549094066 scopus 로고    scopus 로고
    • Globins and hypoxia adaptation in the goldfish, Carassius auratus
    • A. Roesner, S.A. Mitz, T. Hankeln, and T. Burmester Globins and hypoxia adaptation in the goldfish, Carassius auratus FEBS J. 275 2008 3633 3643
    • (2008) FEBS J. , vol.275 , pp. 3633-3643
    • Roesner, A.1    Mitz, S.A.2    Hankeln, T.3    Burmester, T.4
  • 21
    • 33745616788 scopus 로고    scopus 로고
    • Hypoxia induces a complex response of globin expression in zebrafish (Danio rerio)
    • A. Roesner, T. Hankeln, and T. Burmester Hypoxia induces a complex response of globin expression in zebrafish (Danio rerio) J. Exp. Biol. 209 2006 2129 2137
    • (2006) J. Exp. Biol. , vol.209 , pp. 2129-2137
    • Roesner, A.1    Hankeln, T.2    Burmester, T.3
  • 22
    • 84888297068 scopus 로고    scopus 로고
    • Environmental acidification triggers oxidative stress and enhances globin expression in zebrafish gills
    • J. Tiedke, C. Cubuk, and T. Burmester Environmental acidification triggers oxidative stress and enhances globin expression in zebrafish gills Biochem. Biophys. Res. Commun. 441 2013 624 629
    • (2013) Biochem. Biophys. Res. Commun. , vol.441 , pp. 624-629
    • Tiedke, J.1    Cubuk, C.2    Burmester, T.3
  • 24
    • 84923540356 scopus 로고    scopus 로고
    • Molecular characterization, phylogenetic analysis and expression profiling of myoglobin and cytoglobin genes in response to heat stress in channel catfish Ictalurus punctatus
    • J.B. Feng, S.K. Liu, R.J. Wang, J.R. Zhang, X.L. Wang, L. Kaltenboeck, J.L. Li, and Z.J. Liu Molecular characterization, phylogenetic analysis and expression profiling of myoglobin and cytoglobin genes in response to heat stress in channel catfish Ictalurus punctatus Journal Fish Biology 86 2015 592 604
    • (2015) Journal Fish Biology , vol.86 , pp. 592-604
    • Feng, J.B.1    Liu, S.K.2    Wang, R.J.3    Zhang, J.R.4    Wang, X.L.5    Kaltenboeck, L.6    Li, J.L.7    Liu, Z.J.8
  • 27
    • 43249104256 scopus 로고    scopus 로고
    • Zebrafish neuroglobin is a cell-membrane-penetrating globin
    • S. Watanabe, and K. Wakasugi Zebrafish neuroglobin is a cell-membrane-penetrating globin Biochemistry 47 2008 5266 5270
    • (2008) Biochemistry , vol.47 , pp. 5266-5270
    • Watanabe, S.1    Wakasugi, K.2
  • 28
    • 84867830765 scopus 로고    scopus 로고
    • Widespread occurrence of N-terminal acylation in animal globins and possible origin of respiratory globins from a membrane-bound ancestor
    • M. Blank, and T. Burmester Widespread occurrence of N-terminal acylation in animal globins and possible origin of respiratory globins from a membrane-bound ancestor Mol. Biol. Evol. 29 2012 3553 3561
    • (2012) Mol. Biol. Evol. , vol.29 , pp. 3553-3561
    • Blank, M.1    Burmester, T.2
  • 31
    • 79952144810 scopus 로고    scopus 로고
    • Lipid binding to cytoglobin leads to a change in haem co-ordination: a role for cytoglobin in lipid signalling of oxidative stress
    • B.J. Reeder, D.A. Svistunenko, and M.T. Wilson Lipid binding to cytoglobin leads to a change in haem co-ordination: a role for cytoglobin in lipid signalling of oxidative stress Biochem. J. 434 2011 483 492
    • (2011) Biochem. J. , vol.434 , pp. 483-492
    • Reeder, B.J.1    Svistunenko, D.A.2    Wilson, M.T.3
  • 37
    • 7244245630 scopus 로고    scopus 로고
    • Allosteric regulation and temperature dependence of oxygen binding in human neuroglobin and cytoglobin. Molecular mechanisms and physiological significance
    • A. Fago, C. Hundahl, S. Dewilde, K. Gilany, L. Moens, and R.E. Weber Allosteric regulation and temperature dependence of oxygen binding in human neuroglobin and cytoglobin. Molecular mechanisms and physiological significance J. Biol. Chem. 279 2004 44417 44426
    • (2004) J. Biol. Chem. , vol.279 , pp. 44417-44426
    • Fago, A.1    Hundahl, C.2    Dewilde, S.3    Gilany, K.4    Moens, L.5    Weber, R.E.6
  • 38
    • 0019807744 scopus 로고
    • Kinetics and mechanism of the oxidation of human deoxyhemoglobin by nitrites
    • M.P. Doyle, R.A. Pickering, T.M. DeWeert, J.W. Hoekstra, and D. Pater Kinetics and mechanism of the oxidation of human deoxyhemoglobin by nitrites J. Biol. Chem. 256 1981 12393 12398
    • (1981) J. Biol. Chem. , vol.256 , pp. 12393-12398
    • Doyle, M.P.1    Pickering, R.A.2    Deweert, T.M.3    Hoekstra, J.W.4    Pater, D.5
  • 41
    • 33845674111 scopus 로고    scopus 로고
    • Influence of the protein matrix on intramolecular histidine ligation in ferric and ferrous hexacoordinate hemoglobins
    • P. Halder, J.T. Trent 3rd, and M.S. Hargrove Influence of the protein matrix on intramolecular histidine ligation in ferric and ferrous hexacoordinate hemoglobins Proteins 66 2007 172 182
    • (2007) Proteins , vol.66 , pp. 172-182
    • Halder, P.1    Trent, J.T.2    Hargrove, M.S.3
  • 43
    • 0031552067 scopus 로고    scopus 로고
    • Biphasic nature in the autoxidation reaction of human oxyhemoglobin
    • M. Tsuruga, and K. Shikama Biphasic nature in the autoxidation reaction of human oxyhemoglobin Biochim. Biophys. Acta 1337 1997 96 104
    • (1997) Biochim. Biophys. Acta , vol.1337 , pp. 96-104
    • Tsuruga, M.1    Shikama, K.2
  • 44
    • 0024495355 scopus 로고
    • Effects of buried ionizable amino acids on the reduction potential of recombinant myoglobin
    • R. Varadarajan, T.E. Zewert, H.B. Gray, and S.G. Boxer Effects of buried ionizable amino acids on the reduction potential of recombinant myoglobin Science 243 1989 69 72
    • (1989) Science , vol.243 , pp. 69-72
    • Varadarajan, R.1    Zewert, T.E.2    Gray, H.B.3    Boxer, S.G.4
  • 45
    • 0037177797 scopus 로고    scopus 로고
    • Heme redox properties of S-nitrosated hemoglobin A0 and hemoglobin S: implications for interactions of nitric oxide with normal and sickle red blood cells
    • C. Bonaventura, C.H. Taboy, P.S. Low, R.D. Stevens, C. Lafon, and A.L. Crumbliss Heme redox properties of S-nitrosated hemoglobin A0 and hemoglobin S: implications for interactions of nitric oxide with normal and sickle red blood cells J. Biol. Chem. 277 2002 14557 14563
    • (2002) J. Biol. Chem. , vol.277 , pp. 14557-14563
    • Bonaventura, C.1    Taboy, C.H.2    Low, P.S.3    Stevens, R.D.4    Lafon, C.5    Crumbliss, A.L.6
  • 46
    • 84918591432 scopus 로고    scopus 로고
    • Cytoglobin ligand binding regulated by changing haem-co-ordination in response to intramolecular disulfide bond formation and lipid interaction
    • P. Beckerson, M.T. Wilson, D.A. Svistunenko, and B.J. Reeder Cytoglobin ligand binding regulated by changing haem-co-ordination in response to intramolecular disulfide bond formation and lipid interaction Biochem. J. 465 2015 127 137
    • (2015) Biochem. J. , vol.465 , pp. 127-137
    • Beckerson, P.1    Wilson, M.T.2    Svistunenko, D.A.3    Reeder, B.J.4
  • 47
    • 53949097152 scopus 로고    scopus 로고
    • Interaction of fatty acid with myoglobin
    • R. Sriram, U. Kreutzer, L. Shih, and T. Jue Interaction of fatty acid with myoglobin FEBS Lett. 582 2008 3643 3649
    • (2008) FEBS Lett. , vol.582 , pp. 3643-3649
    • Sriram, R.1    Kreutzer, U.2    Shih, L.3    Jue, T.4
  • 48
    • 0038629108 scopus 로고    scopus 로고
    • Interaction with membrane lipids and heme ligand binding properties of Escherichia coli flavohemoglobin
    • A. Bonamore, A. Farina, M. Gattoni, M.E. Schinina, A. Bellelli, and A. Boffi Interaction with membrane lipids and heme ligand binding properties of Escherichia coli flavohemoglobin Biochemistry 42 2003 5792 5801
    • (2003) Biochemistry , vol.42 , pp. 5792-5801
    • Bonamore, A.1    Farina, A.2    Gattoni, M.3    Schinina, M.E.4    Bellelli, A.5    Boffi, A.6
  • 49
    • 32944462917 scopus 로고    scopus 로고
    • The amphibian globin gene repertoire as revealed by the Xenopus genome
    • C. Fuchs, T. Burmester, and T. Hankeln The amphibian globin gene repertoire as revealed by the Xenopus genome Cytogenet Genome Res. 112 2006 296 306
    • (2006) Cytogenet Genome Res. , vol.112 , pp. 296-306
    • Fuchs, C.1    Burmester, T.2    Hankeln, T.3
  • 50
    • 85005992320 scopus 로고    scopus 로고
    • More than hemoglobin - the unexpected diversity of globins in vertebrate red blood cells
    • M. Gotting, and M. Nikinmaa More than hemoglobin - the unexpected diversity of globins in vertebrate red blood cells Physiol. Rep. 3 2015 e12284
    • (2015) Physiol. Rep. , vol.3 , pp. e12284
    • Gotting, M.1    Nikinmaa, M.2
  • 52
    • 79960662890 scopus 로고    scopus 로고
    • Oxygen supply from the bird's eye perspective: globin E is a respiratory protein in the chicken retina
    • M. Blank, L. Kiger, A. Thielebein, F. Gerlach, T. Hankeln, M.C. Marden, and T. Burmester Oxygen supply from the bird's eye perspective: globin E is a respiratory protein in the chicken retina J. Biol. Chem. 286 2011 26507 26515
    • (2011) J. Biol. Chem. , vol.286 , pp. 26507-26515
    • Blank, M.1    Kiger, L.2    Thielebein, A.3    Gerlach, F.4    Hankeln, T.5    Marden, M.C.6    Burmester, T.7
  • 53
    • 44049108195 scopus 로고    scopus 로고
    • Diversity of globin function: enzymatic, transport, storage, and sensing
    • S.N. Vinogradov, and L. Moens Diversity of globin function: enzymatic, transport, storage, and sensing J. Biol. Chem. 283 2008 8773 8777
    • (2008) J. Biol. Chem. , vol.283 , pp. 8773-8777
    • Vinogradov, S.N.1    Moens, L.2
  • 54
    • 84863513471 scopus 로고    scopus 로고
    • Nitrite reductase activity of nonsymbiotic hemoglobins from Arabidopsis thaliana
    • M. Tiso, J. Tejero, C. Kenney, S. Frizzell, and M.T. Gladwin Nitrite reductase activity of nonsymbiotic hemoglobins from Arabidopsis thaliana Biochemistry 51 2012 5285 5292
    • (2012) Biochemistry , vol.51 , pp. 5285-5292
    • Tiso, M.1    Tejero, J.2    Kenney, C.3    Frizzell, S.4    Gladwin, M.T.5
  • 55
    • 79955859483 scopus 로고    scopus 로고
    • Plant and cyanobacterial hemoglobins reduce nitrite to nitric oxide under anoxic conditions
    • R. Sturms, A.A. DiSpirito, and M.S. Hargrove Plant and cyanobacterial hemoglobins reduce nitrite to nitric oxide under anoxic conditions Biochemistry 50 2011 3873 3878
    • (2011) Biochemistry , vol.50 , pp. 3873-3878
    • Sturms, R.1    Dispirito, A.A.2    Hargrove, M.S.3
  • 56
    • 0004377199 scopus 로고
    • Potentiometric determination of the ionization constant of nitrous acid in aqueous sodium perchlorate solutions at 25°C
    • P. Lumme, and J. Tummavuori Potentiometric determination of the ionization constant of nitrous acid in aqueous sodium perchlorate solutions at 25°C Acta Chem. Scand. 19 1965 617 621
    • (1965) Acta Chem. Scand. , vol.19 , pp. 617-621
    • Lumme, P.1    Tummavuori, J.2
  • 58
    • 84890460548 scopus 로고    scopus 로고
    • Identification of proximal and distal axial ligands in Leishmania major pseudoperoxidase
    • R. Saha, M. Bose, S. Sen Santara, J. Roy, and S. Adak Identification of proximal and distal axial ligands in Leishmania major pseudoperoxidase Biochemistry 52 2013 8878 8887
    • (2013) Biochemistry , vol.52 , pp. 8878-8887
    • Saha, R.1    Bose, M.2    Sen Santara, S.3    Roy, J.4    Adak, S.5
  • 61
    • 79958113005 scopus 로고    scopus 로고
    • The evolutionary functions of cardiac NOS/NO in vertebrates tracked by fish and amphibian paradigms
    • S. Imbrogno, B. Tota, and A. Gattuso The evolutionary functions of cardiac NOS/NO in vertebrates tracked by fish and amphibian paradigms Nitric Oxide 25 2011 1 10
    • (2011) Nitric Oxide , vol.25 , pp. 1-10
    • Imbrogno, S.1    Tota, B.2    Gattuso, A.3
  • 62
    • 35848936310 scopus 로고    scopus 로고
    • Nitric oxide formation from nitrite in zebrafish
    • F.B. Jensen Nitric oxide formation from nitrite in zebrafish J. Exp. Biol. 210 2007 3387 3394
    • (2007) J. Exp. Biol. , vol.210 , pp. 3387-3394
    • Jensen, F.B.1
  • 63
    • 78149335620 scopus 로고    scopus 로고
    • Nitric oxide metabolites in goldfish under normoxic and hypoxic conditions
    • M.N. Hansen, and F.B. Jensen Nitric oxide metabolites in goldfish under normoxic and hypoxic conditions J. Exp. Biol. 213 2010 3593 3602
    • (2010) J. Exp. Biol. , vol.213 , pp. 3593-3602
    • Hansen, M.N.1    Jensen, F.B.2
  • 64
    • 84857576701 scopus 로고    scopus 로고
    • Dramatic increase of nitrite levels in hearts of anoxia-exposed crucian carp supporting a role in cardioprotection
    • G.K. Sandvik, G.E. Nilsson, and F.B. Jensen Dramatic increase of nitrite levels in hearts of anoxia-exposed crucian carp supporting a role in cardioprotection Am. J. Physiol. Regul. Integr. Comp. Physiol. 302 2012 R468 R477
    • (2012) Am. J. Physiol. Regul. Integr. Comp. Physiol. , vol.302 , pp. R468-R477
    • Sandvik, G.K.1    Nilsson, G.E.2    Jensen, F.B.3
  • 69
    • 84964253278 scopus 로고    scopus 로고
    • Coupling of disulfide bond and distal histidine dissociation in human ferrous cytoglobin regulates ligand binding
    • P. Beckerson, B.J. Reeder, and M.T. Wilson Coupling of disulfide bond and distal histidine dissociation in human ferrous cytoglobin regulates ligand binding FEBS Lett. 589 2015 507 512
    • (2015) FEBS Lett. , vol.589 , pp. 507-512
    • Beckerson, P.1    Reeder, B.J.2    Wilson, M.T.3
  • 70
    • 0037449744 scopus 로고    scopus 로고
    • How does the eye breathe? Evidence for neuroglobin-mediated oxygen supply in the mammalian retina
    • M. Schmidt, A. Giessl, T. Laufs, T. Hankeln, U. Wolfrum, and T. Burmester How does the eye breathe? Evidence for neuroglobin-mediated oxygen supply in the mammalian retina J. Biol. Chem. 278 2003 1932 1935
    • (2003) J. Biol. Chem. , vol.278 , pp. 1932-1935
    • Schmidt, M.1    Giessl, A.2    Laufs, T.3    Hankeln, T.4    Wolfrum, U.5    Burmester, T.6
  • 71
    • 2542447171 scopus 로고    scopus 로고
    • Reactivity studies of the Fe(III) and Fe(II)NO forms of human neuroglobin reveal a potential role against oxidative stress
    • S. Herold, A. Fago, R.E. Weber, S. Dewilde, and L. Moens Reactivity studies of the Fe(III) and Fe(II)NO forms of human neuroglobin reveal a potential role against oxidative stress J. Biol. Chem. 279 2004 22841 22847
    • (2004) J. Biol. Chem. , vol.279 , pp. 22841-22847
    • Herold, S.1    Fago, A.2    Weber, R.E.3    Dewilde, S.4    Moens, L.5
  • 74
    • 34250861281 scopus 로고    scopus 로고
    • Cytoglobin up-regulated by hydrogen peroxide plays a protective role in oxidative stress
    • D. Li, X.Q. Chen, W.J. Li, Y.H. Yang, J.Z. Wang, and A.C. Yu Cytoglobin up-regulated by hydrogen peroxide plays a protective role in oxidative stress Neurochem. Res. 32 2007 1375 1380
    • (2007) Neurochem. Res. , vol.32 , 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.6
  • 75
    • 77954894512 scopus 로고    scopus 로고
    • Nitric-oxide dioxygenase function of human cytoglobin with cellular reductants and in rat hepatocytes
    • A.M. Gardner, M.R. Cook, and P.R. Gardner Nitric-oxide dioxygenase function of human cytoglobin with cellular reductants and in rat hepatocytes J. Biol. Chem. 285 2010 23850 23857
    • (2010) J. Biol. Chem. , vol.285 , pp. 23850-23857
    • Gardner, A.M.1    Cook, M.R.2    Gardner, P.R.3
  • 76
    • 67649763457 scopus 로고    scopus 로고
    • Cytoglobin is expressed in the vasculature and regulates cell respiration and proliferation via nitric oxide dioxygenation
    • K.E. Halligan, F.L. Jourd'heuil, and D. Jourd'heuil Cytoglobin is expressed in the vasculature and regulates cell respiration and proliferation via nitric oxide dioxygenation J. Biol. Chem. 284 2009 8539 8547
    • (2009) J. Biol. Chem. , vol.284 , pp. 8539-8547
    • Halligan, K.E.1    Jourd'heuil, F.L.2    Jourd'heuil, D.3
  • 77
    • 84862845350 scopus 로고    scopus 로고
    • Characterization of the function of cytoglobin as an oxygen-dependent regulator of nitric oxide concentration
    • X. Liu, D. Follmer, J.R. Zweier, X. Huang, C. Hemann, K. Liu, L.J. Druhan, and J.L. Zweier Characterization of the function of cytoglobin as an oxygen-dependent regulator of nitric oxide concentration Biochemistry 51 2012 5072 5082
    • (2012) Biochemistry , vol.51 , pp. 5072-5082
    • Liu, X.1    Follmer, D.2    Zweier, J.R.3    Huang, X.4    Hemann, C.5    Liu, K.6    Druhan, L.J.7    Zweier, J.L.8
  • 78
    • 84880332674 scopus 로고    scopus 로고
    • Differences in oxygen-dependent nitric oxide metabolism by cytoglobin and myoglobin account for their differing functional roles
    • X. Liu, J. Tong, J.R. Zweier, D. Follmer, C. Hemann, R.S. Ismail, and J.L. Zweier Differences in oxygen-dependent nitric oxide metabolism by cytoglobin and myoglobin account for their differing functional roles FEBS J. 280 2013 3621 3631
    • (2013) FEBS J. , vol.280 , pp. 3621-3631
    • Liu, X.1    Tong, J.2    Zweier, J.R.3    Follmer, D.4    Hemann, C.5    Ismail, R.S.6    Zweier, J.L.7
  • 79
    • 40849119676 scopus 로고    scopus 로고
    • Neuroprotective function of human neuroglobin is correlated with its guanine nucleotide dissociation inhibitor activity
    • S. Watanabe, and K. Wakasugi Neuroprotective function of human neuroglobin is correlated with its guanine nucleotide dissociation inhibitor activity Biochem. Biophys. Res. Commun. 369 2008 695 700
    • (2008) Biochem. Biophys. Res. Commun. , vol.369 , pp. 695-700
    • Watanabe, S.1    Wakasugi, K.2
  • 80
    • 77951666767 scopus 로고    scopus 로고
    • Neuroglobin protects nerve cells from apoptosis by inhibiting the intrinsic pathway of cell death
    • S. Raychaudhuri, J. Skommer, K. Henty, N. Birch, and T. Brittain Neuroglobin protects nerve cells from apoptosis by inhibiting the intrinsic pathway of cell death Apoptosis 15 2010 401 411
    • (2010) Apoptosis , vol.15 , pp. 401-411
    • Raychaudhuri, S.1    Skommer, J.2    Henty, K.3    Birch, N.4    Brittain, T.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.