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Volumn 47, Issue 3, 2006, Pages 1016-1023

Neuroglobin and cytoglobin: Oxygen-binding proteins in retinal neurons

Author keywords

[No Author keywords available]

Indexed keywords

BETA TUBULIN; BINDING PROTEIN; CYTOGLOBIN; MICROTUBULE ASSOCIATED PROTEIN 2; NEUROGLOBIN; OXYGEN; VIMENTIN; CALBINDIN; CALRETININ; GLOBIN; NERVE PROTEIN; NUCLEAR PROTEIN; PROTEIN KINASE C ALPHA; RETINAL; TUBULIN;

EID: 33645403445     PISSN: 01460404     EISSN: None     Source Type: Journal    
DOI: 10.1167/iovs.05-0465     Document Type: Article
Times cited : (61)

References (71)
  • 1
    • 0025913227 scopus 로고
    • Oxygen in mammalian tissue: Methods of measurement and affinities of various reactions
    • Vanderkooi JM, Erecinska M, Silver IA. Oxygen in mammalian tissue: methods of measurement and affinities of various reactions. Am J Physiol. 1991;260:C1131-C1150.
    • (1991) Am J Physiol , vol.260
    • Vanderkooi, J.M.1    Erecinska, M.2    Silver, I.A.3
  • 2
    • 0033746173 scopus 로고    scopus 로고
    • CNS energy metabolism as related to function
    • Ames A 3rd. CNS energy metabolism as related to function. Brain Res Brain Res Rev. 2000;34:42-68.
    • (2000) Brain Res Brain Res Rev , vol.34 , pp. 42-68
    • Ames 3rd, A.1
  • 3
    • 0027078124 scopus 로고    scopus 로고
    • Ames A 3rd. Energy requirements of CNS cells as related to their function and to their vulnerability to ischemia: a commentary based on studies on retina. Can J Physiol Pharmacol. 1992;70(suppl):S158-S164.
    • Ames A 3rd. Energy requirements of CNS cells as related to their function and to their vulnerability to ischemia: a commentary based on studies on retina. Can J Physiol Pharmacol. 1992;70(suppl):S158-S164.
  • 4
    • 0037390258 scopus 로고    scopus 로고
    • Retinal oxygen: Fundamental and clinical aspects
    • Wangsa-Wirawan ND, Linsenmeier RA. Retinal oxygen: fundamental and clinical aspects. Arch Ophthalmol. 2003;121:547-557.
    • (2003) Arch Ophthalmol , vol.121 , pp. 547-557
    • Wangsa-Wirawan, N.D.1    Linsenmeier, R.A.2
  • 5
    • 0032898623 scopus 로고    scopus 로고
    • Retinal and optic nerve head ischemic disorders and atherosclerosis: Role of serotonin
    • Hayreh SS. Retinal and optic nerve head ischemic disorders and atherosclerosis: role of serotonin. Prog Retin Eye Res. 1999;18:191-221.
    • (1999) Prog Retin Eye Res , vol.18 , pp. 191-221
    • Hayreh, S.S.1
  • 6
    • 0036023927 scopus 로고    scopus 로고
    • The impact of ocular blood flow in glaucoma
    • Flammer J, Orgül S, Costa VP, et al. The impact of ocular blood flow in glaucoma. Prog Retin Eye Res. 2002;21:359-393.
    • (2002) Prog Retin Eye Res , vol.21 , pp. 359-393
    • Flammer, J.1    Orgül, S.2    Costa, V.P.3
  • 8
    • 0038824378 scopus 로고    scopus 로고
    • Vascular aspects in the pathophysiology of glaucomatous optic neuropathy
    • Chung HS, Harris A, Evans DW, et al. Vascular aspects in the pathophysiology of glaucomatous optic neuropathy. Surv Ophthalmol. 1999;43(suppl 1):S43-S50.
    • (1999) Surv Ophthalmol , vol.43 , Issue.SUPPL. 1
    • Chung, H.S.1    Harris, A.2    Evans, D.W.3
  • 9
    • 0029893918 scopus 로고    scopus 로고
    • A brief history of hemoglobins: Plant, animal, protist, and bacteria
    • Hardison RC. A brief history of hemoglobins: plant, animal, protist, and bacteria. Proc Natl Acad Sci USA. 1996;93:5675-5679.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 5675-5679
    • Hardison, R.C.1
  • 11
    • 0035839641 scopus 로고    scopus 로고
    • Trent JT 3rd, Watts RA, Hargrove MS. Human neuroglobin, a hexacoordinate hemoglobin that reversibly binds oxygen. J Biol Chem. 2001;276:30106-30110.
    • Trent JT 3rd, Watts RA, Hargrove MS. Human neuroglobin, a hexacoordinate hemoglobin that reversibly binds oxygen. J Biol Chem. 2001;276:30106-30110.
  • 12
    • 0037205447 scopus 로고    scopus 로고
    • A ubiquitously expressed human hexacoordinate hemoglobin
    • Trent JT 3rd, Hargrove MS. A ubiquitously expressed human hexacoordinate hemoglobin. J Biol Chem. 2002;277:19538-19545.
    • (2002) J Biol Chem , vol.277 , pp. 19538-19545
    • Trent 3rd, J.T.1    Hargrove, M.S.2
  • 13
    • 0036219963 scopus 로고    scopus 로고
    • Cytoglobin: A novel globin type ubiquitously expressed in vertebrate tissues
    • Burmester T, Ebner B, Weich B, Hankeln T. Cytoglobin: a novel globin type ubiquitously expressed in vertebrate tissues. Mol Biol Evol. 2002;19:416-421.
    • (2002) Mol Biol Evol , vol.19 , pp. 416-421
    • Burmester, T.1    Ebner, B.2    Weich, B.3    Hankeln, T.4
  • 14
    • 0012231458 scopus 로고    scopus 로고
    • Neuroglobin and cytoglobin: Fresh blood for the vertebrate globin family
    • 2002;3:1146-1151
    • Pesce A, Bolognesi M, Bocedi A, et al. Neuroglobin and cytoglobin: fresh blood for the vertebrate globin family. EMBO Rep. 2002;3:1146-1151.
    • EMBO Rep
    • Pesce, A.1    Bolognesi, M.2    Bocedi, A.3
  • 17
    • 0037049288 scopus 로고    scopus 로고
    • Expression analysis of neuroglobin mRNA in rodent tissues
    • Reuss S, Saaler-Reinhardt S, Weich B, et al. Expression analysis of neuroglobin mRNA in rodent tissues. Neuroscience. 2002;115:645-656.
    • (2002) Neuroscience , vol.115 , pp. 645-656
    • Reuss, S.1    Saaler-Reinhardt, S.2    Weich, B.3
  • 18
    • 18444404621 scopus 로고    scopus 로고
    • Full-length cDNA cloning of human neuroglobin and tissue expression of rat neuroglobin
    • Zhang C, Wang C, Deng M, et al. Full-length cDNA cloning of human neuroglobin and tissue expression of rat neuroglobin. Biochem Biophys Res Commun. 2002;290:1411-1419.
    • (2002) Biochem Biophys Res Commun , vol.290 , pp. 1411-1419
    • Zhang, C.1    Wang, C.2    Deng, M.3
  • 19
    • 0036939854 scopus 로고    scopus 로고
    • Neuroglobin, a novel member of the globin family, is expressed in focal regions of the brain
    • Mammen PP, Shelton JM, Goetsch SC, et al. Neuroglobin, a novel member of the globin family, is expressed in focal regions of the brain. J Histochem Cytochem. 2002;50:1591-1598.
    • (2002) J Histochem Cytochem , vol.50 , pp. 1591-1598
    • Mammen, P.P.1    Shelton, J.M.2    Goetsch, S.C.3
  • 20
    • 0037707580 scopus 로고    scopus 로고
    • Localization of neuroglobin protein in the mouse brain
    • Wystub S, Laufs T, Schmidt M, et al. Localization of neuroglobin protein in the mouse brain. Neurosci Lett. 2003;346:114-116.
    • (2003) Neurosci Lett , vol.346 , pp. 114-116
    • Wystub, S.1    Laufs, T.2    Schmidt, M.3
  • 22
    • 2642570165 scopus 로고    scopus 로고
    • Zebrafish reveals different and conserved features of vertebrate neuroglobin gene structure, expression pattern, and ligand binding
    • Fuchs C, Heib V, Kiger L, et al. Zebrafish reveals different and conserved features of vertebrate neuroglobin gene structure, expression pattern, and ligand binding. J Biol Chem. 2004;279:24116-24122.
    • (2004) J Biol Chem , vol.279 , pp. 24116-24122
    • Fuchs, C.1    Heib, V.2    Kiger, L.3
  • 23
    • 0035929255 scopus 로고    scopus 로고
    • Neuroglobins from the zebrafish Danio rerio and the pufferfish Tetraodon nigroviridis
    • Awenius C, Hankeln T, Burmester T. Neuroglobins from the zebrafish Danio rerio and the pufferfish Tetraodon nigroviridis. Biochem Biophys Res Commun. 2001;287:418-421.
    • (2001) Biochem Biophys Res Commun , vol.287 , pp. 418-421
    • Awenius, C.1    Hankeln, T.2    Burmester, T.3
  • 24
    • 0037449744 scopus 로고    scopus 로고
    • How does the eye breathe? Evidence for neuroglobin-mediated oxygen supply in the mammalian retina
    • Schmidt M, Giessl A, Laufs T, et al. How does the eye breathe? Evidence for neuroglobin-mediated oxygen supply in the mammalian retina. J Biol Chem. 2003;278:1932-1935.
    • (2003) J Biol Chem , vol.278 , pp. 1932-1935
    • Schmidt, M.1    Giessl, A.2    Laufs, T.3
  • 25
    • 3042727978 scopus 로고    scopus 로고
    • Neuroglobin: A respiratory protein of the nervous system
    • Burmester T, Hankeln T. Neuroglobin: a respiratory protein of the nervous system. News Physiol Sci. 2004;19:110-113.
    • (2004) News Physiol Sci , vol.19 , pp. 110-113
    • Burmester, T.1    Hankeln, T.2
  • 26
    • 2642546072 scopus 로고    scopus 로고
    • Interspecies comparison of neuroglobin, cytoglobin and myoglobin: Sequence evolution and candidate regulatory elements
    • Wystub S, Ebner B, Fuchs C, et al. Interspecies comparison of neuroglobin, cytoglobin and myoglobin: sequence evolution and candidate regulatory elements. Cytogenet Genome Res. 2004;105:65-78.
    • (2004) Cytogenet Genome Res , vol.105 , pp. 65-78
    • Wystub, S.1    Ebner, B.2    Fuchs, C.3
  • 27
    • 2642521269 scopus 로고    scopus 로고
    • The structure of murine neuroglobin: Novel pathways for ligand migration and binding
    • Vallone B, Nienhaus K, Brunori M, Nienhaus GU. The structure of murine neuroglobin: novel pathways for ligand migration and binding. Proteins. 2004;56:85-92.
    • (2004) Proteins , vol.56 , pp. 85-92
    • Vallone, B.1    Nienhaus, K.2    Brunori, M.3    Nienhaus, G.U.4
  • 28
    • 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
    • Herold S, Fago A, Weber RE, Dewilde S, Moens L. Reactivity studies of the Fe(III) and Fe(II)NO forms of human neuroglobin reveal a potential role against oxidative stress. J Biol Chem. 2004;279:22841-22847.
    • (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
  • 29
    • 2542460159 scopus 로고    scopus 로고
    • Structural dynamics in the active site of murine neuroglobin and its effects on ligand binding
    • Nienhaus K, Kriegl JM, Nienhaus GU. Structural dynamics in the active site of murine neuroglobin and its effects on ligand binding. J Biol Chem. 2004;279:22944-22952.
    • (2004) J Biol Chem , vol.279 , pp. 22944-22952
    • Nienhaus, K.1    Kriegl, J.M.2    Nienhaus, G.U.3
  • 30
    • 0035914459 scopus 로고    scopus 로고
    • Biochemical characterization and ligand binding properties of neuroglobin, a novel member of the globin family
    • Dewilde S, Kiger L, Burmester T, et al. Biochemical characterization and ligand binding properties of neuroglobin, a novel member of the globin family. J Biol Chem. 2001;276:38949-38955.
    • (2001) J Biol Chem , vol.276 , pp. 38949-38955
    • Dewilde, S.1    Kiger, L.2    Burmester, T.3
  • 31
    • 0035965286 scopus 로고    scopus 로고
    • The heme environment of mouse neuroglobin: Evidence for the presence of two conformations of the heme pocket
    • Couture M, Burmester T, Hankeln T, Rousseau DL. The heme environment of mouse neuroglobin: evidence for the presence of two conformations of the heme pocket. J Biol Chem. 2001;276:36377-36382.
    • (2001) J Biol Chem , vol.276 , pp. 36377-36382
    • Couture, M.1    Burmester, T.2    Hankeln, T.3    Rousseau, D.L.4
  • 32
    • 0141704224 scopus 로고    scopus 로고
    • Oxidized human neuroglobin acts as a heterotrimeric Galpha protein guanine nucleotide dissociation inhibitor
    • Wakasugi K, Nakano T, Morishima I. Oxidized human neuroglobin acts as a heterotrimeric Galpha protein guanine nucleotide dissociation inhibitor. J Biol Chem. 2003;278:36505-36512.
    • (2003) J Biol Chem , vol.278 , pp. 36505-36512
    • Wakasugi, K.1    Nakano, T.2    Morishima, I.3
  • 33
    • 0035909992 scopus 로고    scopus 로고
    • Neuroglobin is up-regulated by and protects neurons from hypoxic-ischemic injury
    • Sun Y, Jin K, Mao XO, Zhu Y, Greenberg DA. Neuroglobin is up-regulated by and protects neurons from hypoxic-ischemic injury. Proc Natl Acad Sci USA. 2001;98:15306-15311.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 15306-15311
    • Sun, Y.1    Jin, K.2    Mao, X.O.3    Zhu, Y.4    Greenberg, D.A.5
  • 34
    • 0037452987 scopus 로고    scopus 로고
    • Neuroglobin protects the brain from experimental stroke in vivo
    • Sun Y, Jin K, Peel A, et al. Neuroglobin protects the brain from experimental stroke in vivo. Proc Natl Acad Sci USA. 2003;100:3497-3500.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 3497-3500
    • Sun, Y.1    Jin, K.2    Peel, A.3
  • 35
    • 10044235333 scopus 로고    scopus 로고
    • Effect of aging on neuroglobin expression in rodent brain
    • Sun Y, Jin K, Mao XO, et al. Effect of aging on neuroglobin expression in rodent brain. Neurobiol Aging. 2005;26:275-278.
    • (2005) Neurobiol Aging , vol.26 , pp. 275-278
    • Sun, Y.1    Jin, K.2    Mao, X.O.3
  • 36
    • 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, et al. Characterization of a stellate cell activation-associated protein (STAP) with peroxidase activity found in rat hepatic stellate cells. J Biol Chem. 2001;276:25318-25323.
    • (2001) J Biol Chem , vol.276 , pp. 25318-25323
    • Kawada, N.1    Kristensen, D.B.2    Asahina, K.3
  • 37
    • 10744220623 scopus 로고    scopus 로고
    • Cytoglobin is a respiratory protein in connective tissue and neurons, which is up-regulated by hypoxia
    • Schmidt M, Gerlach F, Avivi A, et al. Cytoglobin is a respiratory protein in connective tissue and neurons, which is up-regulated by hypoxia. J Biol Chem. 2004;279:8063-8069.
    • (2004) J Biol Chem , vol.279 , pp. 8063-8069
    • Schmidt, M.1    Gerlach, F.2    Avivi, A.3
  • 38
    • 85047691361 scopus 로고    scopus 로고
    • Cytoglobin/STAP, its unique localization in splanchnic fibroblast-like cells and function in organ fibrogenesis
    • Nakatani K, Okuyama H, Shimahara Y, et al. Cytoglobin/STAP, its unique localization in splanchnic fibroblast-like cells and function in organ fibrogenesis. Lab Invest. 2004;84:91-101.
    • (2004) Lab Invest , vol.84 , pp. 91-101
    • Nakatani, K.1    Okuyama, H.2    Shimahara, Y.3
  • 39
    • 12344316097 scopus 로고    scopus 로고
    • Divergent distribution of cytoglobin and neuroglobin in the murine eye
    • Schmidt M, Laufs T, Reuss S, Hankeln T, Burmester T. Divergent distribution of cytoglobin and neuroglobin in the murine eye. Neurosci Lett. 2005;374:207-211.
    • (2005) Neurosci Lett , vol.374 , pp. 207-211
    • Schmidt, M.1    Laufs, T.2    Reuss, S.3    Hankeln, T.4    Burmester, T.5
  • 40
    • 2442584665 scopus 로고    scopus 로고
    • Association of human neuroglobin with cystatin C, a cysteine proteinase inhibitor
    • Wakasugi K, Nakano T, Morishima I. Association of human neuroglobin with cystatin C, a cysteine proteinase inhibitor. Biochemistry. 2004;43:5119-5125.
    • (2004) Biochemistry , vol.43 , pp. 5119-5125
    • Wakasugi, K.1    Nakano, T.2    Morishima, I.3
  • 41
    • 20844446668 scopus 로고    scopus 로고
    • Neuroglobin, nitric oxide, and oxygen: Functional pathways and conformational changes
    • Brunori M, Giuffrè A, Nienhaus K, et al. Neuroglobin, nitric oxide, and oxygen: functional pathways and conformational changes. Proc Natl Acad Sci USA. 2005;102:8483-8488.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 8483-8488
    • Brunori, M.1    Giuffrè, A.2    Nienhaus, K.3
  • 42
    • 2642671098 scopus 로고    scopus 로고
    • Transient, high levels of SNAP-25 expression in cholinergic amacrine cells during postnatal development of the mammalian retina
    • West Greenlee MH, Finley SK, Wilson MC, Jacobson CD, Sakaguchi DS. Transient, high levels of SNAP-25 expression in cholinergic amacrine cells during postnatal development of the mammalian retina. J Comp Neurol. 1998;394:374-385.
    • (1998) J Comp Neurol , vol.394 , pp. 374-385
    • West Greenlee, M.H.1    Finley, S.K.2    Wilson, M.C.3    Jacobson, C.D.4    Sakaguchi, D.S.5
  • 44
    • 0036293752 scopus 로고    scopus 로고
    • Spectral profiling of autofluorescence associated with lipofuscin, Bruch's membrane, and sub-RPE deposits in normal and AMD eyes
    • Marmorstein AD, Marmorstein LY, Sakaguchi H, Hollyfield JG. Spectral profiling of autofluorescence associated with lipofuscin, Bruch's membrane, and sub-RPE deposits in normal and AMD eyes. Invest Ophthalmol Vis Sci. 2002;43:2435-2441.
    • (2002) Invest Ophthalmol Vis Sci , vol.43 , pp. 2435-2441
    • Marmorstein, A.D.1    Marmorstein, L.Y.2    Sakaguchi, H.3    Hollyfield, J.G.4
  • 46
    • 0026738411 scopus 로고
    • Morphological types of ganglion cells in the dog and wolf retina
    • Peichl L. Morphological types of ganglion cells in the dog and wolf retina. J Comp Neurol. 1992;324:590-602.
    • (1992) J Comp Neurol , vol.324 , pp. 590-602
    • Peichl, L.1
  • 47
    • 0031761698 scopus 로고    scopus 로고
    • Immunocytochemical localization of calretinin containing neurons in retina from rabbit, cat, and dog
    • Jeon MH, Jeon CJ. Immunocytochemical localization of calretinin containing neurons in retina from rabbit, cat, and dog. Neurosci Res. 1998;32:75-84.
    • (1998) Neurosci Res , vol.32 , pp. 75-84
    • Jeon, M.H.1    Jeon, C.J.2
  • 48
    • 0016632671 scopus 로고
    • The functional significance of the haemoglobin in a marine nematode, Enoplus brevis (Bastian)
    • Atkinson HJ. The functional significance of the haemoglobin in a marine nematode, Enoplus brevis (Bastian). J Exp Biol. 1975;62:1-9.
    • (1975) J Exp Biol , vol.62 , pp. 1-9
    • Atkinson, H.J.1
  • 49
    • 0005401134 scopus 로고
    • Hemoglobin-containing cells of Neodasys (Gastrotricha, Chaetonotida). II. Respiratory significance
    • Colacino JM, Kraus DW. Hemoglobin-containing cells of Neodasys (Gastrotricha, Chaetonotida). II. Respiratory significance. Comp Biochem Physiol A Physiol. 1984;79:363-369.
    • (1984) Comp Biochem Physiol A Physiol , vol.79 , pp. 363-369
    • Colacino, J.M.1    Kraus, D.W.2
  • 50
    • 0001978749 scopus 로고
    • Functions of cytoplasmic hemoglobins and myohemerythrin
    • Wittenberg JB. Functions of cytoplasmic hemoglobins and myohemerythrin. Adv Comp Environ Physiol. 1992;13:59-85.
    • (1992) Adv Comp Environ Physiol , vol.13 , pp. 59-85
    • Wittenberg, J.B.1
  • 51
    • 77957209359 scopus 로고
    • Functions of invertebrate hemoglobins with special reference to adaptations to environmental hypoxia
    • Weber RE. Functions of invertebrate hemoglobins with special reference to adaptations to environmental hypoxia. Am Zool. 1980;20:79-101.
    • (1980) Am Zool , vol.20 , pp. 79-101
    • Weber, R.E.1
  • 52
    • 0025132256 scopus 로고
    • Simultaneous measurement of the rates of heat dissipation and oxygen consumption in marine invertebrates having and lacking hemoglobin
    • Doeller JE, Kraus DW, Colacino JM. Simultaneous measurement of the rates of heat dissipation and oxygen consumption in marine invertebrates having and lacking hemoglobin. Comp Biochem Physiol A Physiol. 1990;97:107-114.
    • (1990) Comp Biochem Physiol A Physiol , vol.97 , pp. 107-114
    • Doeller, J.E.1    Kraus, D.W.2    Colacino, J.M.3
  • 53
    • 0022552863 scopus 로고
    • Extended oxygen delivery from the nerve hemoglobin of Tellina alternata (Bivalvia)
    • Kraus DW, Colacino JM. Extended oxygen delivery from the nerve hemoglobin of Tellina alternata (Bivalvia). Science. 1986;232:90-92.
    • (1986) Science , vol.232 , pp. 90-92
    • Kraus, D.W.1    Colacino, J.M.2
  • 54
    • 0006142654 scopus 로고
    • A physiological comparison of bivalve mollusc cerebro-visceral connectives with and without neurohemoglobin. III. Oxygen demand
    • Kraus DW, Doeller JE. A physiological comparison of bivalve mollusc cerebro-visceral connectives with and without neurohemoglobin. III. Oxygen demand. Biol Bull. 1988;174:346-354.
    • (1988) Biol Bull , vol.174 , pp. 346-354
    • Kraus, D.W.1    Doeller, J.E.2
  • 55
    • 0005482218 scopus 로고
    • A physiological comparison of bivalve mollusc cerebro-visceral connectives with and without neurohemoglobin. I. Ultrastructural and electrophysiological characteristics
    • Kraus DW, Doeller JE, Smith PR. A physiological comparison of bivalve mollusc cerebro-visceral connectives with and without neurohemoglobin. I. Ultrastructural and electrophysiological characteristics. Biol Bull. 1988;174:54-66.
    • (1988) Biol Bull , vol.174 , pp. 54-66
    • Kraus, D.W.1    Doeller, J.E.2    Smith, P.R.3
  • 56
    • 0032479053 scopus 로고    scopus 로고
    • The mini-hemoglobins in neural and body wall tissue of the nemertean worm, Cerebratulus lacteus
    • Vandergon TL, Riggs CK, Gorr TA, Colacino JM, Riggs AF. The mini-hemoglobins in neural and body wall tissue of the nemertean worm, Cerebratulus lacteus. J Biol Chem. 1998;273:16998-17011.
    • (1998) J Biol Chem , vol.273 , pp. 16998-17011
    • Vandergon, T.L.1    Riggs, C.K.2    Gorr, T.A.3    Colacino, J.M.4    Riggs, A.F.5
  • 57
    • 0041733060 scopus 로고    scopus 로고
    • A globin in the nucleus!
    • Geuens E, Brouns I, Flamez D, et al. A globin in the nucleus! J Biol Chem. 2003;278:30417-30420.
    • (2003) J Biol Chem , vol.278 , pp. 30417-30420
    • Geuens, E.1    Brouns, I.2    Flamez, D.3
  • 58
    • 2942594491 scopus 로고    scopus 로고
    • Neuron-specific expression of neuroglobin in mammals
    • Laufs TL, Wystub S, Reuss S, et al. Neuron-specific expression of neuroglobin in mammals. Neurosci Lett. 2004;362:83-86.
    • (2004) Neurosci Lett , vol.362 , pp. 83-86
    • Laufs, T.L.1    Wystub, S.2    Reuss, S.3
  • 59
    • 18244386984 scopus 로고    scopus 로고
    • Presence of neuroglobin in cultured astrocytes
    • Chen XQ, Qin LY, Zhang CG, et al. Presence of neuroglobin in cultured astrocytes. Glia. 2005;50:182-186.
    • (2005) Glia , vol.50 , pp. 182-186
    • Chen, X.Q.1    Qin, L.Y.2    Zhang, C.G.3
  • 60
    • 0036786923 scopus 로고    scopus 로고
    • Hemin induces neuroglobin expression in neural cells
    • Zhu Y, Sun Y, Jin K, Greenberg DA. Hemin induces neuroglobin expression in neural cells. Blood. 2002;100:2494-2498.
    • (2002) Blood , vol.100 , pp. 2494-2498
    • Zhu, Y.1    Sun, Y.2    Jin, K.3    Greenberg, D.A.4
  • 61
    • 0026731933 scopus 로고
    • Topography of ganglion cells in the dog and wolf retina
    • Peichl L. Topography of ganglion cells in the dog and wolf retina. J Comp Neurol. 1992;324:603-620.
    • (1992) J Comp Neurol , vol.324 , pp. 603-620
    • Peichl, L.1
  • 62
    • 0019436983 scopus 로고
    • Ganglionic cell distribution in the central area of the beagle dog retina
    • Krinke A, Schnider K, Lundbeck E, Krinke G. Ganglionic cell distribution in the central area of the beagle dog retina. Anat Histol Embryol. 1981;10:26-35.
    • (1981) Anat Histol Embryol , vol.10 , pp. 26-35
    • Krinke, A.1    Schnider, K.2    Lundbeck, E.3    Krinke, G.4
  • 63
    • 17144420129 scopus 로고    scopus 로고
    • Functional properties of neuroglobin and cytoglobin: Insights into the ancestral physiological roles of globins
    • Fago A, Hundahl C, Malte H, Weber RE. Functional properties of neuroglobin and cytoglobin: insights into the ancestral physiological roles of globins. IUBMB Life. 2004;56:689-696.
    • (2004) IUBMB Life , vol.56 , pp. 689-696
    • Fago, A.1    Hundahl, C.2    Malte, H.3    Weber, R.E.4
  • 64
    • 29744432405 scopus 로고    scopus 로고
    • Possible neuroprotective mechanism of human neuroglobin
    • Wakasugi K, Kitatsuji C, Morishima I. Possible neuroprotective mechanism of human neuroglobin. Ann NY Acad Sci. 2005;1053:220-230.
    • (2005) Ann NY Acad Sci , vol.1053 , pp. 220-230
    • Wakasugi, K.1    Kitatsuji, C.2    Morishima, I.3
  • 65
    • 0030911508 scopus 로고    scopus 로고
    • A comparison of retinal and choroidal hemodynamics in patients with primary open-angle glaucoma and normal-pressure glaucoma
    • Duijm HF, van den Berg TJ, Greve EL. A comparison of retinal and choroidal hemodynamics in patients with primary open-angle glaucoma and normal-pressure glaucoma. Am J Ophthalmol. 1997;123:644-656.
    • (1997) Am J Ophthalmol , vol.123 , pp. 644-656
    • Duijm, H.F.1    van den Berg, T.J.2    Greve, E.L.3
  • 66
    • 0032800220 scopus 로고    scopus 로고
    • Color Doppler imaging of the retrobulbar circulation in glaucoma
    • Rankin SJ. Color Doppler imaging of the retrobulbar circulation in glaucoma. Surv Ophthalmol. 1999;43(suppl 1):S176-S182.
    • (1999) Surv Ophthalmol , vol.43 , Issue.SUPPL. 1
    • Rankin, S.J.1
  • 67
    • 0032807090 scopus 로고    scopus 로고
    • Introductory comments on blood flow autoregulation in the optic nerve head and vascular risk factors in glaucoma
    • Anderson DR. Introductory comments on blood flow autoregulation in the optic nerve head and vascular risk factors in glaucoma. Surv Ophthalmol. 1999;43(suppl 1):S5-S9.
    • (1999) Surv Ophthalmol , vol.43 , Issue.SUPPL. 1
    • Anderson, D.R.1
  • 68
    • 4444275866 scopus 로고    scopus 로고
    • Hypoxia-inducible factor 1alpha in the glaucomatous retina and optic nerve head
    • Tezel G, Wax MB. Hypoxia-inducible factor 1alpha in the glaucomatous retina and optic nerve head. Arch Ophthalmol. 2004;122:1348-1356.
    • (2004) Arch Ophthalmol , vol.122 , pp. 1348-1356
    • Tezel, G.1    Wax, M.B.2
  • 69
    • 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
    • Fordel E, Geuens E, Dewilde S, et al. 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. 2004;319:342-348.
    • (2004) Biochem Biophys Res Commun , vol.319 , pp. 342-348
    • Fordel, E.1    Geuens, E.2    Dewilde, S.3
  • 70
    • 0018841366 scopus 로고
    • Central retinal artery occlusion and retinal tolerance time
    • Hayreh SS, Kolder HE, Weingeist TA. Central retinal artery occlusion and retinal tolerance time. Ophthalmology. 1980;87:75-78.
    • (1980) Ophthalmology , vol.87 , pp. 75-78
    • Hayreh, S.S.1    Kolder, H.E.2    Weingeist, T.A.3
  • 71
    • 0842287983 scopus 로고    scopus 로고
    • Central retinal artery occlusion: Retinal survival time
    • Hayreh SS, Zimmerman MB, Kimura A, Sanon A. Central retinal artery occlusion: retinal survival time. Exp Eye Res. 2004;78:723-736.
    • (2004) Exp Eye Res , vol.78 , pp. 723-736
    • Hayreh, S.S.1    Zimmerman, M.B.2    Kimura, A.3    Sanon, A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.