메뉴 건너뛰기




Volumn 413, Issue 1, 2011, Pages 1-7

Sulfur signaling: Is the agent sulfide or sulfane?

Author keywords

[No Author keywords available]

Indexed keywords

SULFUR COMPOUNDS;

EID: 79953712285     PISSN: 00032697     EISSN: 10960309     Source Type: Journal    
DOI: 10.1016/j.ab.2011.01.044     Document Type: Review
Times cited : (249)

References (77)
  • 1
    • 77749271091 scopus 로고    scopus 로고
    • Hydrogen sulfide as a gasotransmitter
    • M.M. Gadalia, S.H. Snyder, Hydrogen sulfide as a gasotransmitter, J. Neurochem. 113 (2010) 14-26.
    • (2010) J. Neurochem. , vol.113 , pp. 14-26
    • Gadalia, M.M.1    Snyder, S.H.2
  • 2
    • 77950805698 scopus 로고    scopus 로고
    • Hydrogen sulfide: The third gasotransmitter in biology and medicine
    • R. Wang, Hydrogen sulfide: the third gasotransmitter in biology and medicine, Antioxid. Redox Signal. 12 (2010) 1061-1064.
    • (2010) Antioxid. Redox Signal. , vol.12 , pp. 1061-1064
    • Wang, R.1
  • 3
    • 0024817618 scopus 로고
    • Sulphane sulphur in biological systems: A possible regulatory role
    • J.I. Toohey, Sulphane sulphur in biological systems: a possible regulatory role, Biochem. J. 264 (1989) 625-632. (Pubitemid 20023429)
    • (1989) Biochemical Journal , vol.264 , Issue.3 , pp. 625-632
    • Toohey, J.I.1
  • 4
    • 34047225116 scopus 로고    scopus 로고
    • Common themes and variations in the rhodanese superfamily
    • DOI 10.1080/15216540701206859, PII 776197113
    • R. Cipollone, P. Acsenzi, P. Visca, Common themes and variations in the rhodanese superfamily, IUBMB Life 59 (2009) 51-59. (Pubitemid 46535402)
    • (2007) IUBMB Life , vol.59 , Issue.2 , pp. 51-59
    • Cipollone, R.1    Ascenzi, P.2    Visca, P.3
  • 5
    • 33646349748 scopus 로고    scopus 로고
    • Trafficking in persulfides: Delivering sulfur in biosynthetic pathways
    • E.G. Mueller, Trafficking in persulfides: delivering sulfur in biosynthetic pathways, Nat. Chem. Biol. 2 (2006) 185-194.
    • (2006) Nat. Chem. Biol. , vol.2 , pp. 185-194
    • Mueller, E.G.1
  • 6
    • 33750083296 scopus 로고    scopus 로고
    • Enzymatic activation of sulfur for incorporation into biomolecules in prokaryotes
    • D. Kessler, Enzymatic activation of sulfur for incorporation into biomolecules in prokaryotes, FEMS Microbiol. Rev. 30 (2006) 825-840.
    • (2006) FEMS Microbiol. Rev. , vol.30 , pp. 825-840
    • Kessler, D.1
  • 7
    • 0033829523 scopus 로고    scopus 로고
    • A tribute to sulfur
    • H.A. Beinert, A tribute to sulfur, Eur. J. Biochem. 267 (2000) 5657-5664.
    • (2000) Eur. J. Biochem. , vol.267 , pp. 5657-5664
    • Beinert, H.A.1
  • 8
    • 0022550131 scopus 로고
    • Persulfide sulfur is a growth factor for cells defective in sulfur metabolism
    • J.I. Toohey, Persulfide sulfur is a growth factor for cells defective in sulfur metabolism, Biochem. Cell Biol. 64 (1986) 758-765.
    • (1986) Biochem. Cell Biol. , vol.64 , pp. 758-765
    • Toohey, J.I.1
  • 9
    • 71949114140 scopus 로고    scopus 로고
    • Sulfur metabolism in AIDS: Cystamine as an anti-HIV agent
    • J.I. Toohey, Sulfur metabolism in AIDS: cystamine as an anti-HIV agent, AIDS Res. Hum. Retroviruses 25 (2009) 1057-1060.
    • (2009) AIDS Res. Hum. Retroviruses , vol.25 , pp. 1057-1060
    • Toohey, J.I.1
  • 12
    • 77954579286 scopus 로고    scopus 로고
    • The redox biochemistry of hydrogen sulfide
    • O. Kabil, R. Banerjee, The redox biochemistry of hydrogen sulfide, J. Biol. Chem. 285 (2010) 21903-21907.
    • (2010) J. Biol. Chem. , vol.285 , pp. 21903-21907
    • Kabil, O.1    Banerjee, R.2
  • 13
    • 33845553498 scopus 로고
    • Compounds containing the S=S bond
    • G.W. Kutney, K. Turnbull, Compounds containing the S=S bond, Chem. Rev. 82 (1962) 333-357.
    • (1962) Chem. Rev. , vol.82 , pp. 333-357
    • Kutney, G.W.1    Turnbull, K.2
  • 14
    • 0021116479 scopus 로고
    • Elemental sulfur: A novel inhibitor of adenylate kinase
    • J. Conner, P.J. Russell, Elemental sulfur: a novel inhibitor of adenylate kinase, Biochem. Biophys. Res. Commun. 113 (1983) 348-352.
    • (1983) Biochem. Biophys. Res. Commun. , vol.113 , pp. 348-352
    • Conner, J.1    Russell, P.J.2
  • 16
    • 0036668633 scopus 로고    scopus 로고
    • The rhodanese/Cdc25 phosphatase superfamily. Sequence-structure-function relations
    • DOI 10.1093/embo-reports/kvf150
    • D. Bordo, P. Bork, The rhodanese/Cdc25 phosphatase superfamily: sequence-structure-function relations, EMBO Rep. 3 (2002) 741-746. (Pubitemid 34966012)
    • (2002) EMBO Reports , vol.3 , Issue.8 , pp. 741-746
    • Bordo, D.1    Bork, P.2
  • 17
    • 0032508464 scopus 로고    scopus 로고
    • A model of Cdc25 phosphatase catalytic domain and Cdk-interaction surface based on the presence of a rhodanese homology domain
    • K. Hofmann, P. Bucher, A.V. Kajava, A model of Cdc25 phosphatase catalytic domain and Cdk-interaction surface based on the presence of a rhodanese homology domain, J. Mol. Biol. 282 (1998) 195-208.
    • (1998) J. Mol. Biol. , vol.282 , pp. 195-208
    • Hofmann, K.1    Bucher, P.2    Kajava, A.V.3
  • 19
    • 33645817522 scopus 로고    scopus 로고
    • Carbon monoxide and hydrogen sulfide: Gaseous messengers in cerebrovascular circulation
    • C.W. Leffler, H. Parfenova, J.H. Jagger, R. Wang, Carbon monoxide and hydrogen sulfide: gaseous messengers in cerebrovascular circulation, J. Appl. Physiol. 100 (2006) 1065-1076.
    • (2006) J. Appl. Physiol. , vol.100 , pp. 1065-1076
    • Leffler, C.W.1    Parfenova, H.2    Jagger, J.H.3    Wang, R.4
  • 20
    • 77955485967 scopus 로고    scopus 로고
    • Hydrogen sulfide, a gaseous transmitter, stimulates proliferation of interstitial cells of Cajal via phosphorylation of AKT protein kinase
    • Y. Huang, F. Li, W. Tong, A. Zhang, Y. He, T. Fu, B. Liu, Hydrogen sulfide, a gaseous transmitter, stimulates proliferation of interstitial cells of Cajal via phosphorylation of AKT protein kinase, Tohoku J. Exp. Med. 221 (2010) 125-132.
    • (2010) Tohoku J. Exp. Med. , vol.221 , pp. 125-132
    • Huang, Y.1    Li, F.2    Tong, W.3    Zhang, A.4    He, Y.5    Fu, T.6    Liu, B.7
  • 21
    • 34548379105 scopus 로고    scopus 로고
    • The novel proangiogenic effect of hydrogen sulfide is dependent on Akt phosphorylation
    • W.J. Cai, M.J. Wang, P.K. Moore, H.M. Jin, T. Yao, Y.C. Zhu, The novel proangiogenic effect of hydrogen sulfide is dependent on Akt phosphorylation, Cardiovasc. Res. 76 (2007) 29-40.
    • (2007) Cardiovasc. Res. , vol.76 , pp. 29-40
    • Cai, W.J.1    Wang, M.J.2    Moore, P.K.3    Jin, H.M.4    Yao, T.5    Zhu, Y.C.6
  • 23
    • 0037927972 scopus 로고    scopus 로고
    • Hydrogen sulfide induces serum-independent cell cycle entry in nontransformed rat intestinal epithelial cells
    • B. Deplancke, H.R. Gaskins, Hydrogen sulfide induces serum-independent cell cycle entry in nontransformed rat intestinal epithelial cells, FASEB J. 17 (2003) 1310-1339.
    • (2003) FASEB J. , vol.17 , pp. 1310-1339
    • Deplancke, B.1    Gaskins, H.R.2
  • 24
    • 57349171934 scopus 로고    scopus 로고
    • Whole tissue hydrogen sulfide concentrations are orders of magnitude lower than presently accepted values
    • J. Furne, A. Saeed, D. Levitt, Whole tissue hydrogen sulfide concentrations are orders of magnitude lower than presently accepted values, Am. J. Physiol. Regul. Integr. Comp. Physiol. 295 (2008) R1479-R1485.
    • (2008) Am. J. Physiol. Regul. Integr. Comp. Physiol. , vol.295
    • Furne, J.1    Saeed, A.2    Levitt, D.3
  • 26
    • 67649265267 scopus 로고    scopus 로고
    • Is hydrogen sulfide a circulating "gasotransmitter" in vertebrate blood?
    • K.R. Olson, Is hydrogen sulfide a circulating "gasotransmitter" in vertebrate blood?, Biochim Biophys. Acta 1787 (2009) 845-863.
    • (2009) Biochim Biophys. Acta , vol.1787 , pp. 845-863
    • Olson, K.R.1
  • 27
    • 38049130259 scopus 로고    scopus 로고
    • Nephroprotective effect of cystathionine is due to its diverse action on the kidney and Ehrlich ascites tumor cells
    • I. Kwiecien, M. Sokolowska, L. Wlodek, Nephroprotective effect of cystathionine is due to its diverse action on the kidney and Ehrlich ascites tumor cells, Pharmacol. Rep. 59 (2007) 553-564.
    • (2007) Pharmacol. Rep. , vol.59 , pp. 553-564
    • Kwiecien, I.1    Sokolowska, M.2    Wlodek, L.3
  • 28
    • 39049099900 scopus 로고    scopus 로고
    • N-acetyl-L-cysteine as a source of sulfane sulfur in astrocytoma and astrocyte cultures: Correlations with cell proliferation
    • DOI 10.1007/s00726-007-0471-2
    • H. Jurkowska, M. Wrobel, N-Acetyl-L-cysteine as a source of sulfane sulfur in astrocytoma and astrocyte cultures: correlation with cell proliferation, Amino Acids 34 (2008) 231-237. (Pubitemid 351238261)
    • (2008) Amino Acids , vol.34 , Issue.2 , pp. 231-237
    • Jurkowska, H.1    Wrobel, M.2
  • 29
    • 0024582137 scopus 로고
    • A sensitive gas chromatographic method for determination of protein-bound sulfur
    • U. Hannestad, S. Margheri, B. Sörbo, A sensitive gas chromatographic method for determination of protein-bound sulfur, Anal. Biochem. 178 (1989) 394-398.
    • (1989) Anal. Biochem. , vol.178 , pp. 394-398
    • Hannestad, U.1    Margheri, S.2    Sörbo, B.3
  • 30
    • 27744467308 scopus 로고    scopus 로고
    • Molecular targeting by homocysteine: A mechanism for vascular pathogenesis
    • D.W. Jacobsen, O. Catanescu, P.M. diBello, J.C. Barbato, Molecular targeting by homocysteine: a mechanism for vascular pathogenesis, Clin. Chem. Lab. Med. 43 (2008) 1076-1083.
    • (2008) Clin. Chem. Lab. Med. , vol.43 , pp. 1076-1083
    • Jacobsen, D.W.1    Catanescu, O.2    DiBello, P.M.3    Barbato, J.C.4
  • 32
    • 75449151090 scopus 로고
    • Cystinuria: Metabolism of the disulfide of cysteine and homocysteine
    • G.W. Frimpter, Cystinuria: metabolism of the disulfide of cysteine and homocysteine, J. Clin. Invest. 42 (1963) 1956-1964.
    • (1963) J. Clin. Invest. , vol.42 , pp. 1956-1964
    • Frimpter, G.W.1
  • 33
    • 0018651563 scopus 로고
    • Sulphur containing amino acids in chronic renal failure with particular reference to homocystine and cysteine-homocysteine mixed disulphide
    • D.E. Wilcken, V.J. Gupta, Sulfur-containing amino acids in chronic renal failure with particular reference to homocystine and cysteine-homocysteine mixed disulfide, Eur. J. Clin. Invest. 9 (1979) 301-307. (Pubitemid 10137119)
    • (1979) European Journal of Clinical Investigation , vol.9 , Issue.4 , pp. 301-307
    • Wilcken, D.E.L.1    Gupta, V.J.2
  • 34
    • 0018126120 scopus 로고
    • The detection of cysteine-homocysteine mixed disulphide in plasma of normal fasting man
    • V.J. Gupta, D.E. Wilcken, Detection of cysteine-homocysteine mixed disulfide in plasma of normal fasting man, Eur. J. Clin. Invest. 8 (1978) 205-207. (Pubitemid 9015536)
    • (1978) European Journal of Clinical Investigation , vol.8 , Issue.4 , pp. 205-207
    • Gupta, V.J.1    Wilcken, D.E.L.2
  • 35
    • 79953681677 scopus 로고
    • γ-Cystathionase (Neurospora)
    • M. Flavin, C. Slaughter, γ-Cystathionase (Neurospora), Methods Enzymol. 5 (1962) 433-439.
    • (1962) Methods Enzymol. , vol.5 , pp. 433-439
    • Flavin, M.1    Slaughter, C.2
  • 38
    • 0037457908 scopus 로고    scopus 로고
    • Kinetics of the yeast cystathionine β-synthase forward and reverse reactions: Continuous assays and the equilibrium constant for the reaction
    • DOI 10.1021/bi026681n
    • S.M. Aitken, J.F. Kirsch, Kinetics of yeast cystathionine β-synthase forward and reverse reactions: continuous assays and the equilibrium constant for the reaction, Biochemistry 42 (2003) 571-578. (Pubitemid 36105777)
    • (2003) Biochemistry , vol.42 , Issue.2 , pp. 571-578
    • Aitken, S.M.1    Kirsch, J.F.2
  • 39
    • 58749087051 scopus 로고    scopus 로고
    • Kinetic characterization of recombinant human cystathionine β-synthase purified from E. coli
    • M.S. Belew, F.I. Quazi, W.G. Willmor, S.M. Aitken, Kinetic characterization of recombinant human cystathionine β-synthase purified from E. coli, Protein Expr. Purif. 64 (2008) 139-145.
    • (2008) Protein Expr. Purif. , vol.64 , pp. 139-145
    • Belew, M.S.1    Quazi, F.I.2    Willmor, W.G.3    Aitken, S.M.4
  • 40
    • 10644254287 scopus 로고    scopus 로고
    • 2S by cystathionine β-synthase via the condensation of cysteine and homocysteine
    • 2S by cystathionine β-synthase via the condensation of cysteine and homocysteine, J. Biol. Chem. 279 (2004) 52082-52086.
    • (2004) J. Biol. Chem. , vol.279 , pp. 52082-52086
    • Chen, X.1    Jhee, K.2    Kruger, W.3
  • 42
    • 0015531079 scopus 로고
    • Cleavage of cystine by cystathionase
    • M.T. Costa, A.M. Wolf, D. Giarnieri, Cleavage of cystine by cystathionase, Enzymologia 43 (1972) 271-279.
    • (1972) Enzymologia , vol.43 , pp. 271-279
    • Costa, M.T.1    Wolf, A.M.2    Giarnieri, D.3
  • 43
    • 0019577528 scopus 로고
    • The mechanism of the L-cystine cleavage reaction catalyzed by rat liver γ-cystathionase
    • Y. Yamanishi, S. Tuboi, The mechanism of the L-cystine cleavage reaction catalyzed by rat liver γ-cystathionase, J. Biochem. 89 (1981) 1913-1921.
    • (1981) J. Biochem. , vol.89 , pp. 1913-1921
    • Yamanishi, Y.1    Tuboi, S.2
  • 44
    • 0023664452 scopus 로고
    • A cystine-dependent inactivator of tyrosine aminotransferase co-purifies with γ-cystathionase (cysteine desulfhydrase)
    • J.L. Hargrove, R.D. Wichman, A cystine-dependent inactivator of tyrosine aminotransferase co-purifies with γ-cystathionase (cysteine desulfhydrase), J. Biol. Chem. 262 (1987) 7351-7357.
    • (1987) J. Biol. Chem. , vol.262 , pp. 7351-7357
    • Hargrove, J.L.1    Wichman, R.D.2
  • 45
    • 0018704158 scopus 로고
    • On the nature of the activating enzyme of the inactive form of δ-aminolevulinate synthetase in Rhodopseudomonas spheroides
    • I. Inoue, H. Oyama, S. Tuboi, On the nature of the activating enzyme of the inactive form of δ-aminolevulinate synthase in Rhodopseudomonas spheroids, J. Biochem. 86 (1979) 477-482. (Pubitemid 10251091)
    • (1979) Journal of Biochemistry , vol.86 , Issue.2 , pp. 477-482
    • Inoue, I.1    Oyama, H.2    Tuboi, S.3
  • 46
    • 0023108924 scopus 로고
    • Red blood cell rhodanese: Its possible role in modulating δ-aminolaevulinate synthase activity in mammals
    • E. Vasquez, A.M. Buzaleh, E. Wider, A.M. Battle, Red blood cell rhodanese: its possible role in modulating δ-aminolaevulinate synthase activity in mammals, Int. J. Biochem. 19 (1987) 217-219.
    • (1987) Int. J. Biochem. , vol.19 , pp. 217-219
    • Vasquez, E.1    Buzaleh, A.M.2    Wider, E.3    Battle, A.M.4
  • 47
    • 0019248821 scopus 로고
    • Porphyrin biosynthesis in the soybean callus tissue system. XVIII: Levels of succinyl CoA synthetase, cystathionase, rhodanese, aminolevulinate synthetase, and aminolevulinate dehydratase in clones of different age
    • E. Vasquez, E. Wider de Xifra, A.M. Batlle, Porphyrin biosynthesis in the soybean callus tissue system. XVIII: Levels of succinyl CoA synthetase, cystathionase, rhodanese, aminolevulinate synthetase, and aminolevulinate dehydratase in clones of different age, Int. J. Biochem. 12 (1980) 721-724.
    • (1980) Int. J. Biochem. , vol.12 , pp. 721-724
    • Vasquez, E.1    Wider De Xifra, E.2    Batlle, A.M.3
  • 48
    • 33645963484 scopus 로고    scopus 로고
    • The mercaptopyruvate pathway in cysteine catabolism: A physiological role and related disease of the multifunctional 3-mercaptopyruvate sulfur transferase
    • N. Nagahara, N. Sawada, The mercaptopyruvate pathway in cysteine catabolism: a physiological role and related disease of the multifunctional 3-mercaptopyruvate sulfur transferase, Curr. Med. Chem. 13 (2006) 1219-1230.
    • (2006) Curr. Med. Chem. , vol.13 , pp. 1219-1230
    • Nagahara, N.1    Sawada, N.2
  • 49
    • 77049164862 scopus 로고
    • Enzymatic desulfuration of β-mercaptopyruvate to pyruvate
    • A. Meister, P.E. Fraser, S.V. Tice, Enzymatic desulfuration of β-mercaptopyruvate to pyruvate, J. Biol. Chem. 206 (1954) 561-575.
    • (1954) J. Biol. Chem. , vol.206 , pp. 561-575
    • Meister, A.1    Fraser, P.E.2    Tice, S.V.3
  • 50
    • 79953715220 scopus 로고    scopus 로고
    • Dealing with methionine/homocysteine sulfur: Cysteine metabolism to taurine and inorganic sulfur
    • M.H. Stipanuk, I. Ueki, Dealing with methionine/homocysteine sulfur: cysteine metabolism to taurine and inorganic sulfur, J. Inherit. Metab. Dis. 34 (2011) 17-32.
    • (2011) J. Inherit. Metab. Dis. , vol.34 , pp. 17-32
    • Stipanuk, M.H.1    Ueki, I.2
  • 51
    • 32944464498 scopus 로고    scopus 로고
    • Cysteine S-conjugate β-lyases
    • A.J.L. Cooper, J.T. Pinto, Cysteine S-conjugate β-lyases, Amino Acids 30 (2006) 1-15.
    • (2006) Amino Acids , vol.30 , pp. 1-15
    • Cooper, A.J.L.1    Pinto, J.T.2
  • 53
    • 13844276140 scopus 로고    scopus 로고
    • Aminotransferase, L-amino acid oxidase, and β-lyase reactions involving L-cysteine S-conjugates found in allium extracts: Relevance to biological activity?
    • A.J.L. Cooper, J.T. Pinto, Aminotransferase, L-amino acid oxidase, and β-lyase reactions involving L-cysteine S-conjugates found in allium extracts: relevance to biological activity?, Biochem Pharmacol. 69 (2005) 209-220.
    • (2005) Biochem Pharmacol. , vol.69 , pp. 209-220
    • Cooper, A.J.L.1    Pinto, J.T.2
  • 54
    • 0037209757 scopus 로고    scopus 로고
    • Bacterial cysteine desulfurases: Their function and mechanisms
    • DOI 10.1007/s00253-002-1107-4
    • H. Mihari, N. Esaki, Bacterial cysteine desulfurases: their functions and mechanisms, Appl. Microbiol. Biotechnol. 60 (2002) 12-23. (Pubitemid 35217625)
    • (2003) Applied Microbiology and Biotechnology , vol.60 , Issue.1-2 , pp. 12-23
    • Mihara, H.1    Esaki, N.2
  • 55
    • 79960395086 scopus 로고    scopus 로고
    • Latest news about the sulfurtransferase protein family of higher plants
    • doi:10: 1007/s00726-010-0478-6
    • J. Papenbrock, S. Guretzki, M. Henne, Latest news about the sulfurtransferase protein family of higher plants, Amino Acids. doi:10: 1007/s00726-010-0478-6.
    • Amino Acids
    • Papenbrock, J.1    Guretzki, S.2    Henne, M.3
  • 56
    • 19644366036 scopus 로고    scopus 로고
    • Molybdenum cofactor biosynthesis in humans: Identification of a persulfide group in the rhodanese-like domain of MOCS3 by mass spectrometry
    • DOI 10.1021/bi0503448
    • A. Matthies, M. Nimtz, S. Leimkuhler, Molybdenum cofactor synthesis in humans: identification of a persulfide group in the rhodanese-like domain of MOCS3 by mass spectrometry, Biochemistry 44 (2005) 7912-7920. (Pubitemid 40740775)
    • (2005) Biochemistry , vol.44 , Issue.21 , pp. 7912-7920
    • Matthies, A.1    Nimtz, M.2    Leimkuhler, S.3
  • 57
    • 33744956665 scopus 로고    scopus 로고
    • Roles of the mammalian cytosolic cysteine desulfurase, ISCS, and scaffold protein, ISCU, in iron-sulfur cluster assembly
    • DOI 10.1074/jbc.M600582200
    • K. Li, W. Tong, R.M. Hughes, T.A. Rouault, Roles of the mammalian cytosolic cysteine desulfurase, ISCS, and scaffold protein, ISCU, in iron-sulfur cluster assembly, J. Biol. Chem. 281 (2006) 12344-12351. (Pubitemid 43855319)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.18 , pp. 12344-12351
    • Li, K.1    Tong, W.-H.2    Hughes, R.M.3    Rouault, T.A.4
  • 60
    • 0035371184 scopus 로고    scopus 로고
    • Redox environment of the cell as viewed through the redox state of the glutathione disulfide/glutathione couple
    • DOI 10.1016/S0891-5849(01)00480-4, PII S0891584901004804
    • F.Q. Schafer, G.R. Buettner, Redox environment of the cell as viewed through the redox state of the glutathione disulfide/glutathione couple, Free Radic. Biol. Med. 30 (2001) 1191-1212. (Pubitemid 32463931)
    • (2001) Free Radical Biology and Medicine , vol.30 , Issue.11 , pp. 1191-1212
    • Schafer, F.Q.1    Buettner, G.R.2
  • 62
    • 0031047873 scopus 로고    scopus 로고
    • Modification of liver cytosol enzyme activities promoted in vitro by reduced sulfur species generated from cystine and γ-cystathionase
    • Y. Ogasawara, T. Suzuki, K. Ishii, S. Tanabe, Modification of liver cytosol enzyme activities promoted in vitro by reduced sulfur species generated from cystine and γ-cystathionase, Biochim. Biophys. Acta 1334 (1997) 33-43.
    • (1997) Biochim. Biophys. Acta , vol.1334 , pp. 33-43
    • Ogasawara, Y.1    Suzuki, T.2    Ishii, K.3    Tanabe, S.4
  • 65
    • 76749156792 scopus 로고    scopus 로고
    • Characterization of a covalent polysulfane bridge in copper-zinc superoxide dismutase
    • Z. You, X. Cao, A.B. Taylor, P.J. Hart, R.L. Levine, Characterization of a covalent polysulfane bridge in copper-zinc superoxide dismutase, Biochemistry 49 (2010) 1191-1198.
    • (2010) Biochemistry , vol.49 , pp. 1191-1198
    • You, Z.1    Cao, X.2    Taylor, A.B.3    Hart, P.J.4    Levine, R.L.5
  • 66
    • 1042276724 scopus 로고    scopus 로고
    • Solution Structure of the 30 kDa Polysulfide-Sulfur Transferase Homodimer from Wolinella succinogenes
    • DOI 10.1021/bi0356597
    • Y.J. Lin, F. Dancea, F. Lohr, O. Klimmek, S. Pfeiffer-Marek, M. Nilges, H. Wienk, A. Kroger, H. Ruterjans, Solution structure of the 30 kDa polysulfide-sulfur transferase homodimer from Wolinella succinogenes, Biochemistry 43 (2004) 1418-1424. (Pubitemid 38200546)
    • (2004) Biochemistry , vol.43 , Issue.6 , pp. 1418-1424
    • Lin, Y.-J.1    Dancea, F.2    Lohr, F.3    Klimmek, O.4    Pfeiffer-Marek, S.5    Nilges, M.6    Wienk, H.7    Kroger, A.8    Ruterjans, H.9
  • 69
    • 0345051150 scopus 로고
    • The oxidation of cystamine and other sulfur-diamines by diamine oxidase preparations
    • D. Cavallini, D. de Marco, B. Mondovi, The oxidation of cystamine and other sulfur-diamines by diamine oxidase preparations, Experientia 12 (1956) 377-379.
    • (1956) Experientia , vol.12 , pp. 377-379
    • Cavallini, D.1    De Marco, D.2    Mondovi, B.3
  • 70
    • 33644835000 scopus 로고    scopus 로고
    • Clarifying the real bioactive constituents of garlic
    • H. Amagase, Clarifying the real bioactive constituents of garlic, J. Nutr. 136 (2006) 716S-725S.
    • (2006) J. Nutr. , vol.136
    • Amagase, H.1
  • 71
    • 0343957429 scopus 로고
    • The mechanism of sulfur lability in cysteine and its derivatives Some thioethers readily split by alakali
    • B.H. Nicolet, The mechanism of sulfur lability in cysteine and its derivatives Some thioethers readily split by alakali, J. Am. Chem. Soc. 53 (1931) 3066-3072.
    • (1931) J. Am. Chem. Soc. , vol.53 , pp. 3066-3072
    • Nicolet, B.H.1
  • 72
    • 33644842783 scopus 로고    scopus 로고
    • Significance of garlic and its consituents in cancer and cardiovascular disease
    • R.S. Rivlin, M. Budoff, H. Amagase, Significance of garlic and its consituents in cancer and cardiovascular disease, J. Nutr. 136 (2006) 712S.
    • (2006) J. Nutr. , vol.136
    • Rivlin, R.S.1    Budoff, M.2    Amagase, H.3
  • 73
    • 70349295182 scopus 로고    scopus 로고
    • Aged garlic extract supplemented with B vitamins, folic acid, and L-arginine retards the progression of subclinical atheroscerlosis; a randomized clinical trial
    • M.J. Budoff, N. Ahmadi, K.M. Gui, S.T. Liu, F.R. Flores, J. Tiano, J. Takasu, E. Miller, S. Tsimikas, Aged garlic extract supplemented with B vitamins, folic acid, and L-arginine retards the progression of subclinical atheroscerlosis; a randomized clinical trial, Prev. Med. 49 (2009) 101-107.
    • (2009) Prev. Med. , vol.49 , pp. 101-107
    • Budoff, M.J.1    Ahmadi, N.2    Gui, K.M.3    Liu, S.T.4    Flores, F.R.5    Tiano, J.6    Takasu, J.7    Miller, E.8    Tsimikas, S.9
  • 74
    • 70349918058 scopus 로고    scopus 로고
    • Effect of aged garlic extract on wound healing: A new frontier in wound management
    • Ejaz, I. Chekarova, J.W. Cho, S.Y. Lee, S. Ashraf, C.W. Lin, Effect of aged garlic extract on wound healing: a new frontier in wound management, Drug Chem. Toxicol. 32 (2009) 191-203.
    • (2009) Drug Chem. Toxicol. , vol.32 , pp. 191-203
    • Ejaz, I.1    Chekarova2    Cho, J.W.3    Lee, S.Y.4    Ashraf, S.5    Lin, C.W.6
  • 77
    • 79251606051 scopus 로고    scopus 로고
    • Hydrogen sulfide-mediated cardioprotection: Mechanisms and therapeutic potential
    • M. Lavu, S. Bhushan, D.J. Lefer, Hydrogen sulfide-mediated cardioprotection: mechanisms and therapeutic potential, Clin. Sci. 120 (2010) 219-229.
    • (2010) Clin. Sci. , vol.120 , pp. 219-229
    • Lavu, M.1    Bhushan, S.2    Lefer, D.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.