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Volumn 4, Issue JUL, 2013, Pages

Production of hydrogen sulfide from D-cysteine and its therapeutic potential

Author keywords

3MST; Bound sulfane sulfur; D cysteine; DAO; Hydrogen sulfide; Ischemia reperfusion injury; L cysteine

Indexed keywords

AMINO ACID OXIDASE; AMINOTRANSFERASE; ATRIAL NATRIURETIC FACTOR; CALCIUM ION; CYSTATHIONINE BETA SYNTHASE; CYSTATHIONINE GAMMA LYASE; CYSTEINE; ENDOTHELIN RECEPTOR ANTAGONIST; HYDROGEN SULFIDE; PROSTAGLANDIN; SOMATOMEDIN C; THYROXINE;

EID: 84884180984     PISSN: None     EISSN: 16642392     Source Type: Journal    
DOI: 10.3389/fendo.2013.00087     Document Type: Review
Times cited : (82)

References (64)
  • 1
    • 0024566415 scopus 로고
    • Determination of sulfide in brain tissue by gas dialysis/ion chromatography: postmortem studies and two case reports
    • Goodwin LR, Francom D, Dieken FP, Taylor JD, Warenycia MW, Reiffenstein RJ, et al. Determination of sulfide in brain tissue by gas dialysis/ion chromatography: postmortem studies and two case reports. J Anal Toxicol (1989) 13:105-9.
    • (1989) J Anal Toxicol , vol.13 , pp. 105-109
    • Goodwin, L.R.1    Francom, D.2    Dieken, F.P.3    Taylor, J.D.4    Warenycia, M.W.5    Reiffenstein, R.J.6
  • 3
    • 0025266258 scopus 로고
    • Determination of sulfide in brain tissue and rumen fluid by ion-interaction reversed-phase high-performance liquid chromatography
    • Savage JC, Gould DH. Determination of sulfide in brain tissue and rumen fluid by ion-interaction reversed-phase high-performance liquid chromatography. J Chromatogr (1990) 526:540-5.
    • (1990) J Chromatogr , vol.526 , pp. 540-545
    • Savage, J.C.1    Gould, D.H.2
  • 4
    • 57349171934 scopus 로고    scopus 로고
    • Whole tissue hydrogen sulfide concentrations are orders of magnitude lower than presently accepted values
    • Furne J, Saeed A, Levitt MD. Whole tissue hydrogen sulfide concentrations are orders of magnitude lower than presently accepted values. Am J Physiol Regul Integr Comp Physiol (2008) 295:R1479-85.
    • (2008) Am J Physiol Regul Integr Comp Physiol , vol.295
    • Furne, J.1    Saeed, A.2    Levitt, M.D.3
  • 6
    • 77952859292 scopus 로고    scopus 로고
    • A monobromobimane-based assay to measure the pharmacokinetic profile of reactive sulphide species in blood
    • Wintner EA, Deckwerth TL, Langston W, Bengtsson A, Leviten D, Hill P, et al. A monobromobimane-based assay to measure the pharmacokinetic profile of reactive sulphide species in blood. Br J Pharmacol (2010) 160:941-57.
    • (2010) Br J Pharmacol , vol.160 , pp. 941-957
    • Wintner, E.A.1    Deckwerth, T.L.2    Langston, W.3    Bengtsson, A.4    Leviten, D.5    Hill, P.6
  • 7
    • 0029876402 scopus 로고    scopus 로고
    • The possible role of hydrogen sulfide as an endogenous neuromodulator
    • Abe K, Kimura H. The possible role of hydrogen sulfide as an endogenous neuromodulator. J Neurosci (1996) 16:1066-71.
    • (1996) J Neurosci , vol.16 , pp. 1066-1071
    • Abe, K.1    Kimura, H.2
  • 8
    • 2442655642 scopus 로고    scopus 로고
    • Hydrogen sulfide induces calcium waves in astrocytes
    • Nagai Y, Tsugane M, Oka J, Kimura H. Hydrogen sulfide induces calcium waves in astrocytes. FASEB J (2004) 18:557-9.
    • (2004) FASEB J , vol.18 , pp. 557-559
    • Nagai, Y.1    Tsugane, M.2    Oka, J.3    Kimura, H.4
  • 9
    • 0031589557 scopus 로고    scopus 로고
    • The possible role of hydrogen sulfide as an endogenous smooth muscle relaxant in synergy with nitric oxide
    • Hosoki R, Matsuki N, Kimura H. The possible role of hydrogen sulfide as an endogenous smooth muscle relaxant in synergy with nitric oxide. Biochem Biophys Res Commun (1997) 237:527-31.
    • (1997) Biochem Biophys Res Commun , vol.237 , pp. 527-531
    • Hosoki, R.1    Matsuki, N.2    Kimura, H.3
  • 10
    • 0035503695 scopus 로고    scopus 로고
    • 2S as a novel endogenous gaseous KATP channel opener
    • 2S as a novel endogenous gaseous KATP channel opener. EMBO J (2001) 20:6008-16.
    • (2001) EMBO J , vol.20 , pp. 6008-6016
    • Zhao, W.1    Zhang, J.2    Lu, Y.3    Wang, R.4
  • 11
    • 29244485145 scopus 로고    scopus 로고
    • 2S in rat insulin-secreting cells and the underlying mechanisms
    • 2S in rat insulin-secreting cells and the underlying mechanisms. J Physiol (2005) 569:519-31.
    • (2005) J Physiol , vol.569 , pp. 519-531
    • Yang, W.1    Yang, G.2    Jia, X.3    Wu, L.4    Wang, R.5
  • 12
    • 33745306741 scopus 로고    scopus 로고
    • l-Cysteine inhibits insulin release from the pancreatic beta-cell: possible involvement of metabolic production of hydrogen sulfide, a novel gasotransmitter
    • Kaneko Y, Kimura Y, Kimura H, Niki I. l-Cysteine inhibits insulin release from the pancreatic beta-cell: possible involvement of metabolic production of hydrogen sulfide, a novel gasotransmitter. Diabetes (2006) 55:1391-7.
    • (2006) Diabetes , vol.55 , pp. 1391-1397
    • Kaneko, Y.1    Kimura, Y.2    Kimura, H.3    Niki, I.4
  • 14
    • 81355127489 scopus 로고    scopus 로고
    • Hydrogen sulfide as endothelium-derived hyperpolarizing factor sulfhydrates potassium channels
    • Mustafa AK, Sikka G, Gazi SK, Steppan J, Jung SM, Bhunia AK, et al. Hydrogen sulfide as endothelium-derived hyperpolarizing factor sulfhydrates potassium channels. Circ Res (2011) 109:1259-68.
    • (2011) Circ Res , vol.109 , pp. 1259-1268
    • Mustafa, A.K.1    Sikka, G.2    Gazi, S.K.3    Steppan, J.4    Jung, S.M.5    Bhunia, A.K.6
  • 15
    • 9444263079 scopus 로고    scopus 로고
    • Hydrogen sulfide protects neurons from oxidative stress
    • Kimura Y, Kimura H. Hydrogen sulfide protects neurons from oxidative stress. FASEB J (2004) 18:1165-7.
    • (2004) FASEB J , vol.18 , pp. 1165-1167
    • Kimura, Y.1    Kimura, H.2
  • 16
    • 71549130783 scopus 로고    scopus 로고
    • Hydrogen sulfide increases glutathione production and suppresses oxidative stress in mitochondria
    • Kimura Y, Goto Y, Kimura H. Hydrogen sulfide increases glutathione production and suppresses oxidative stress in mitochondria. Antioxid Redox Signal (2010) 12:1-13.
    • (2010) Antioxid Redox Signal , vol.12 , pp. 1-13
    • Kimura, Y.1    Goto, Y.2    Kimura, H.3
  • 17
    • 80655128144 scopus 로고    scopus 로고
    • Hydrogen sulfide protects the retina from light-induced degeneration by the modulation of Ca2+ influx
    • Mikami Y, Shibuya N, Kimura Y, Nagahara N, Yamada M, Kimura H. Hydrogen sulfide protects the retina from light-induced degeneration by the modulation of Ca2+ influx. J Biol Chem (2011) 286:39379-86.
    • (2011) J Biol Chem , vol.286 , pp. 39379-39386
    • Mikami, Y.1    Shibuya, N.2    Kimura, Y.3    Nagahara, N.4    Yamada, M.5    Kimura, H.6
  • 18
    • 34848828558 scopus 로고    scopus 로고
    • Hydrogen sulfide attenuates myocardial ischemia-reperfusion injury by preservation of mitochondrial function
    • Elrod JW, Calvert JW, Morrison J, Doeller JE, Kraus DW, Tao L, et al. Hydrogen sulfide attenuates myocardial ischemia-reperfusion injury by preservation of mitochondrial function. Proc Natl Acad Sci U S A (2007) 104:15560-5.
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 15560-15565
    • Elrod, J.W.1    Calvert, J.W.2    Morrison, J.3    Doeller, J.E.4    Kraus, D.W.5    Tao, L.6
  • 19
    • 52649096364 scopus 로고    scopus 로고
    • Generation of endogenous hydrogen sulfide by cystathionine gamma-lyase limits renal ischemia/reperfusion injury and dysfunction
    • Tripatara P, Patel NS, Collino M, Gallicchio M, Kieswich J, Castiglia S, et al. Generation of endogenous hydrogen sulfide by cystathionine gamma-lyase limits renal ischemia/reperfusion injury and dysfunction. Lab Invest (2008) 88:1038-48.
    • (2008) Lab Invest , vol.88 , pp. 1038-1048
    • Tripatara, P.1    Patel, N.S.2    Collino, M.3    Gallicchio, M.4    Kieswich, J.5    Castiglia, S.6
  • 20
    • 0020483746 scopus 로고
    • Characterization of the enzymic capacity for cysteine desulphhydration in liver and kidney of the rat
    • Stipanuk MH, Beck PW. Characterization of the enzymic capacity for cysteine desulphhydration in liver and kidney of the rat. Biochem J (1982) 206:267-77.
    • (1982) Biochem J , vol.206 , pp. 267-277
    • Stipanuk, M.H.1    Beck, P.W.2
  • 21
    • 60749088329 scopus 로고    scopus 로고
    • 3-Mercaptopyruvate sulfurtransferase produces hydrogen sulfide and bound sulfane sulfur in the brain
    • Shibuya N, Tanaka M, Yoshida M, Ogasawara Y, Togawa T, Ishii K, et al. 3-Mercaptopyruvate sulfurtransferase produces hydrogen sulfide and bound sulfane sulfur in the brain. Antioxid Redox Signal (2009) 11:703-14.
    • (2009) Antioxid Redox Signal , vol.11 , pp. 703-714
    • Shibuya, N.1    Tanaka, M.2    Yoshida, M.3    Ogasawara, Y.4    Togawa, T.5    Ishii, K.6
  • 23
    • 80054015725 scopus 로고    scopus 로고
    • Thioredoxin and dihydrolipoic acid are required for 3-mercaptopyruvate sulfurtransferase to produce hydrogen sulfide
    • Mikami Y, Shibuya N, Kimura Y, Nagahara N, Ogasawara Y, Kimura H. Thioredoxin and dihydrolipoic acid are required for 3-mercaptopyruvate sulfurtransferase to produce hydrogen sulfide. Biochem J (2011) 439:479-85.
    • (2011) Biochem J , vol.439 , pp. 479-485
    • Mikami, Y.1    Shibuya, N.2    Kimura, Y.3    Nagahara, N.4    Ogasawara, Y.5    Kimura, H.6
  • 24
    • 0018213564 scopus 로고
    • Purification and characterization of mitochondrial cysteine aminotransferase from rat liver
    • Ubuka T, Umemura S, Yuasa S, Kinuta M, Watanabe K. Purification and characterization of mitochondrial cysteine aminotransferase from rat liver. Physiol Chem Phys (1978) 10:483-500.
    • (1978) Physiol Chem Phys , vol.10 , pp. 483-500
    • Ubuka, T.1    Umemura, S.2    Yuasa, S.3    Kinuta, M.4    Watanabe, K.5
  • 25
    • 0019984593 scopus 로고
    • Purification and characterization of cysteine aminotransferase from rat liver cytosol
    • Akagi R. Purification and characterization of cysteine aminotransferase from rat liver cytosol. Acta Med Okayama (1982) 36:187-97.
    • (1982) Acta Med Okayama , vol.36 , pp. 187-197
    • Akagi, R.1
  • 26
    • 0020686355 scopus 로고
    • Biochemistry of sulfur-containing amino acids
    • Cooper AJ. Biochemistry of sulfur-containing amino acids. Annu Rev Biochem (1983) 52:187-222.
    • (1983) Annu Rev Biochem , vol.52 , pp. 187-222
    • Cooper, A.J.1
  • 27
    • 84873470505 scopus 로고    scopus 로고
    • A novel pathway for the production of hydrogen sulfide from d-cysteine in mammalian cells
    • Shibuya N, Koike S, Tanaka M, Ishigami-Yuasa M, Kimura Y, Ogasawara Y, et al. A novel pathway for the production of hydrogen sulfide from d-cysteine in mammalian cells. Nat Commun (2013) 4::1366.
    • (2013) Nat Commun , vol.4 , pp. 1366
    • Shibuya, N.1    Koike, S.2    Tanaka, M.3    Ishigami-Yuasa, M.4    Kimura, Y.5    Ogasawara, Y.6
  • 28
    • 0024076281 scopus 로고
    • Identification of peroxisomal targeting signals located at the carboxy terminus of four peroxisomal proteins
    • Gould SJ, Keller GA, Subramani S. Identification of peroxisomal targeting signals located at the carboxy terminus of four peroxisomal proteins. J Cell Biol (1988) 107:897-905.
    • (1988) J Cell Biol , vol.107 , pp. 897-905
    • Gould, S.J.1    Keller, G.A.2    Subramani, S.3
  • 29
    • 44649112394 scopus 로고    scopus 로고
    • Special delivery from mitochondria to peroxisomes
    • Schumann U, Subramani S. Special delivery from mitochondria to peroxisomes. Trends Cell Biol (2008) 18:253-6.
    • (2008) Trends Cell Biol , vol.18 , pp. 253-256
    • Schumann, U.1    Subramani, S.2
  • 30
    • 3142758491 scopus 로고    scopus 로고
    • Murine cystathionine gamma-lyase: complete cDNA and genomic sequences, promoter activity, tissue distribution and developmental expression
    • Ishii I, Akahoshi N, Yu XN, Kobayashi Y, Namekata K, Komaki G, et al. Murine cystathionine gamma-lyase: complete cDNA and genomic sequences, promoter activity, tissue distribution and developmental expression. Biochem J (2004) 381:113-23.
    • (2004) Biochem J , vol.381 , pp. 113-123
    • Ishii, I.1    Akahoshi, N.2    Yu, X.N.3    Kobayashi, Y.4    Namekata, K.5    Komaki, G.6
  • 31
    • 70449686289 scopus 로고    scopus 로고
    • Vascular endothelium expresses 3-mercaptopyruvate sulfurtransferase and produces hydrogen sulfide
    • Shibuya N, Mikami Y, Kimura Y, Nagahara N, Kimura H. Vascular endothelium expresses 3-mercaptopyruvate sulfurtransferase and produces hydrogen sulfide. J Biochem (2009) 146:623-6.
    • (2009) J Biochem , vol.146 , pp. 623-626
    • Shibuya, N.1    Mikami, Y.2    Kimura, Y.3    Nagahara, N.4    Kimura, H.5
  • 32
    • 27744461725 scopus 로고    scopus 로고
    • Cystathionine beta-synthase, a key enzyme for homocysteine metabolism, is preferentially expressed in the radial glia/astrocyte lineage of developing mouse CNS
    • Enokido Y, Suzuki E, Iwasawa K, Namekata K, Okazawa H, Kimura H. Cystathionine beta-synthase, a key enzyme for homocysteine metabolism, is preferentially expressed in the radial glia/astrocyte lineage of developing mouse CNS. FASEB J (2005) 19:1854-6.
    • (2005) FASEB J , vol.19 , pp. 1854-1856
    • Enokido, Y.1    Suzuki, E.2    Iwasawa, K.3    Namekata, K.4    Okazawa, H.5    Kimura, H.6
  • 33
    • 33846308476 scopus 로고    scopus 로고
    • Inhibition of cystathionine-gamma-lyase leads to loss of glutathione and aggravation of mitochondrial dysfunction mediated by excitatory amino acid in the CNS
    • Diwakar L, Ravindranath V. Inhibition of cystathionine-gamma-lyase leads to loss of glutathione and aggravation of mitochondrial dysfunction mediated by excitatory amino acid in the CNS. Neurochem Int (2007) 50:418-26.
    • (2007) Neurochem Int , vol.50 , pp. 418-426
    • Diwakar, L.1    Ravindranath, V.2
  • 34
    • 54949084607 scopus 로고    scopus 로고
    • 2S as a physiologic vasorelaxant: hypertension in mice with deletion of cystathionine gamma-lyase
    • 2S as a physiologic vasorelaxant: hypertension in mice with deletion of cystathionine gamma-lyase. Science (2008) 322:587-90.
    • (2008) Science , vol.322 , pp. 587-590
    • Yang, G.1    Wu, L.2    Jiang, B.3    Yang, W.4    Qi, J.5    Cao, K.6
  • 35
    • 77952194773 scopus 로고    scopus 로고
    • Familial amyotrophic lateral sclerosis is associated with a mutation in d-amino acid oxidase
    • Mitchell J, Paul P, Chen HJ, Morris A, Payling M, Falchi M, et al. Familial amyotrophic lateral sclerosis is associated with a mutation in d-amino acid oxidase. Proc Natl Acad Sci U S A (2010) 107:7556-61.
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 7556-7561
    • Mitchell, J.1    Paul, P.2    Chen, H.J.3    Morris, A.4    Payling, M.5    Falchi, M.6
  • 36
    • 0033499883 scopus 로고    scopus 로고
    • Immunocytochemical localization of d-amino acid oxidase in rat brain
    • Moreno S, Nardacci R, Cimini A, Cerù MP. Immunocytochemical localization of d-amino acid oxidase in rat brain. J Neurocytol (1999) 28:169-85.
    • (1999) J Neurocytol , vol.28 , pp. 169-185
    • Moreno, S.1    Nardacci, R.2    Cimini, A.3    Cerù, M.P.4
  • 37
    • 0023179622 scopus 로고
    • Immunoelectron microscopic localization of d-amino acid oxidase in rat kidney and liver
    • Perotti ME, Gavazzi E, Trussardo L, Malgaretti N, Curti B. Immunoelectron microscopic localization of d-amino acid oxidase in rat kidney and liver. Histochem J (1987) 19:157-69.
    • (1987) Histochem J , vol.19 , pp. 157-169
    • Perotti, M.E.1    Gavazzi, E.2    Trussardo, L.3    Malgaretti, N.4    Curti, B.5
  • 38
    • 0030722634 scopus 로고    scopus 로고
    • Characterization of homocysteine metabolism in the rat kidney
    • House JD, Brosnan ME, Brosnan JT. Characterization of homocysteine metabolism in the rat kidney. Biochem J (1997) 328:287-92.
    • (1997) Biochem J , vol.328 , pp. 287-292
    • House, J.D.1    Brosnan, M.E.2    Brosnan, J.T.3
  • 39
    • 0031666759 scopus 로고    scopus 로고
    • Tissue and subcellular distribution of mercaptopyruvate sulfurtransferase in the rat: confocal laser fluorescence and immunoelectron microscopic studies combined with biochemical analysis
    • Nagahara N, Ito T, Kitamura H, Nishino T. Tissue and subcellular distribution of mercaptopyruvate sulfurtransferase in the rat: confocal laser fluorescence and immunoelectron microscopic studies combined with biochemical analysis. Histochem Cell Biol (1998) 110:243-50.
    • (1998) Histochem Cell Biol , vol.110 , pp. 243-250
    • Nagahara, N.1    Ito, T.2    Kitamura, H.3    Nishino, T.4
  • 40
    • 84873477156 scopus 로고    scopus 로고
    • Hydrogen sulfide is produced by cystathionine γ-lyase at the steady-state low intracellular Ca2+ concentrations
    • Mikami Y, Shibuya N, Ogasawara Y, Kimura H. Hydrogen sulfide is produced by cystathionine γ-lyase at the steady-state low intracellular Ca2+ concentrations. Biochem Biophys Res Commun (2013) 431:131-5.
    • (2013) Biochem Biophys Res Commun , vol.431 , pp. 131-135
    • Mikami, Y.1    Shibuya, N.2    Ogasawara, Y.3    Kimura, H.4
  • 41
    • 0034193197 scopus 로고    scopus 로고
    • Regulation of mitochondrial metabolism by ER Ca2+ release: an intimate connection
    • Rutter GA, Rizzuto R. Regulation of mitochondrial metabolism by ER Ca2+ release: an intimate connection. Trends Biochem Sci (2000) 25:215-21.
    • (2000) Trends Biochem Sci , vol.25 , pp. 215-221
    • Rutter, G.A.1    Rizzuto, R.2
  • 43
    • 24944504370 scopus 로고    scopus 로고
    • Sensitive determination of d-amino acids in mammals and the effect of d-amino-acid oxidase activity on their amounts
    • Hamase K, Konno R, Morikawa A, Zaitsu K. Sensitive determination of d-amino acids in mammals and the effect of d-amino-acid oxidase activity on their amounts. Biol Pharm Bull (2005) 28:1578-84.
    • (2005) Biol Pharm Bull , vol.28 , pp. 1578-1584
    • Hamase, K.1    Konno, R.2    Morikawa, A.3    Zaitsu, K.4
  • 46
    • 84868154864 scopus 로고    scopus 로고
    • Alteration of intrinsic amounts of d-serine in the mice lacking serine racemase and d-amino acid oxidase
    • Miyoshi Y, Konno R, Sasabe J, Ueno K, Tojo Y, Mita M, et al. Alteration of intrinsic amounts of d-serine in the mice lacking serine racemase and d-amino acid oxidase. Amino Acids (2012) 43:1919-31.
    • (2012) Amino Acids , vol.43 , pp. 1919-1931
    • Miyoshi, Y.1    Konno, R.2    Sasabe, J.3    Ueno, K.4    Tojo, Y.5    Mita, M.6
  • 47
    • 77649248890 scopus 로고    scopus 로고
    • Aspartate racemase, generating neuronal d-aspartate, regulates adult neurogenesis
    • Kim PM, Duan X, Huang AS, Liu CY, Ming GL, Song H, et al. Aspartate racemase, generating neuronal d-aspartate, regulates adult neurogenesis. Proc Natl Acad Sci U S A (2010) 107:3175-9.
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 3175-3179
    • Kim, P.M.1    Duan, X.2    Huang, A.S.3    Liu, C.Y.4    Ming, G.L.5    Song, H.6
  • 48
    • 0000182791 scopus 로고
    • Racemization kinetics of free and protein-bound amino acids under moderate alkaline treatment
    • Liardon R, Ledermann S. Racemization kinetics of free and protein-bound amino acids under moderate alkaline treatment. J Agric Food Chem (1986) 34:557-65.
    • (1986) J Agric Food Chem , vol.34 , pp. 557-565
    • Liardon, R.1    Ledermann, S.2
  • 49
    • 77953888010 scopus 로고    scopus 로고
    • Origin, microbiology, nutrition, and pharmacology of d-amino acids
    • Friedman M. Origin, microbiology, nutrition, and pharmacology of d-amino acids. Chem Biodivers (2010) 7:1491-530.
    • (2010) Chem Biodivers , vol.7 , pp. 1491-1530
    • Friedman, M.1
  • 51
    • 0034737775 scopus 로고    scopus 로고
    • Identification and characterization of a Na+-independent neutral amino acid transporter that associates with the 4F2 heavy chain and exhibits substrate selectivity for small neutral d- and l-amino acids
    • Fukasawa Y, Segawa H, Kim JY, Chairoungdua A, Kim DK, Matsuo H, et al. Identification and characterization of a Na+-independent neutral amino acid transporter that associates with the 4F2 heavy chain and exhibits substrate selectivity for small neutral d- and l-amino acids. J Biol Chem (2000) 275:9690-8.
    • (2000) J Biol Chem , vol.275 , pp. 9690-9698
    • Fukasawa, Y.1    Segawa, H.2    Kim, J.Y.3    Chairoungdua, A.4    Kim, D.K.5    Matsuo, H.6
  • 52
    • 0034653957 scopus 로고    scopus 로고
    • Cerebellum as a target for toxic substances
    • Fonnum F, Lock EA. Cerebellum as a target for toxic substances. Toxicol Lett (2000) 112-113:9-16.
    • (2000) Toxicol Lett , vol.112-113 , pp. 9-16
    • Fonnum, F.1    Lock, E.A.2
  • 53
    • 69549111063 scopus 로고    scopus 로고
    • Increase in cerebellar neurotrophin-3 and oxidative stress markers in autism
    • Sajdel-Sulkowska EM, Xu M, Koibuchi N. Increase in cerebellar neurotrophin-3 and oxidative stress markers in autism. Cerebellum (2009) 8:366-72.
    • (2009) Cerebellum , vol.8 , pp. 366-372
    • Sajdel-Sulkowska, E.M.1    Xu, M.2    Koibuchi, N.3
  • 56
    • 0032991586 scopus 로고    scopus 로고
    • Multicenter clinical trial of recombinant human insulin-like growth factor I in patients with acute renal failure
    • Hirschberg R, Kopple J, Lipsett P, Benjamin E, Minei J, Albertson T, et al. Multicenter clinical trial of recombinant human insulin-like growth factor I in patients with acute renal failure. Kidney Int (1999) 55:2423-32.
    • (1999) Kidney Int , vol.55 , pp. 2423-2432
    • Hirschberg, R.1    Kopple, J.2    Lipsett, P.3    Benjamin, E.4    Minei, J.5    Albertson, T.6
  • 58
    • 0034115616 scopus 로고    scopus 로고
    • Exacerbation of radiocontrast nephrotoxicity by endothelin receptor antagonism
    • Wang A, Holcslaw T, Bashore TM, Freed MI, Miller D, Rudnick MR, et al. Exacerbation of radiocontrast nephrotoxicity by endothelin receptor antagonism. Kidney Int (2000) 57:1675-80.
    • (2000) Kidney Int , vol.57 , pp. 1675-1680
    • Wang, A.1    Holcslaw, T.2    Bashore, T.M.3    Freed, M.I.4    Miller, D.5    Rudnick, M.R.6
  • 59
    • 0040559883 scopus 로고    scopus 로고
    • Quality control mechanisms during translation
    • Ibba M, Söll D. Quality control mechanisms during translation. Science (1999) 286:1893-7.
    • (1999) Science , vol.286 , pp. 1893-1897
    • Ibba, M.1    Söll, D.2
  • 60
    • 0017848886 scopus 로고
    • Rat liver cysteine dioxygenase (cysteine oxidase). Further purification, characterization, and analysis of the activation and inactivation
    • Yamaguchi K, Hosokawa Y, Kohashi N, Kori Y, Sakakibara S, Ueda I. Rat liver cysteine dioxygenase (cysteine oxidase). Further purification, characterization, and analysis of the activation and inactivation. J Biochem (1978) 83:479-91.
    • (1978) J Biochem , vol.83 , pp. 479-491
    • Yamaguchi, K.1    Hosokawa, Y.2    Kohashi, N.3    Kori, Y.4    Sakakibara, S.5    Ueda, I.6
  • 61
    • 0025299455 scopus 로고
    • l-cysteine, a bicarbonate-sensitive endogenous excitotoxin
    • Olney JW, Zorumski C, Price MT, Labruyere J. l-cysteine, a bicarbonate-sensitive endogenous excitotoxin. Science (1990) 248:596-9.
    • (1990) Science , vol.248 , pp. 596-599
    • Olney, J.W.1    Zorumski, C.2    Price, M.T.3    Labruyere, J.4
  • 63
    • 0024598233 scopus 로고
    • Is a certain amount of cysteine prerequisite to produce brain damage in neonatal rats?
    • Misra CH. Is a certain amount of cysteine prerequisite to produce brain damage in neonatal rats? Neurochem Res (1989) 14:253-7.
    • (1989) Neurochem Res , vol.14 , pp. 253-257
    • Misra, C.H.1
  • 64
    • 84878363435 scopus 로고    scopus 로고
    • Pressor response to l-cysteine injected into the cisterna magna of conscious rats involves recruitment of hypothalamic vasopressinergic neurons
    • Takemoto Y. Pressor response to l-cysteine injected into the cisterna magna of conscious rats involves recruitment of hypothalamic vasopressinergic neurons. Amino Acids (2012) 44:1053-60.
    • (2012) Amino Acids , vol.44 , pp. 1053-1060
    • Takemoto, Y.1


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