메뉴 건너뛰기




Volumn 41, Issue , 2014, Pages 4-10

The physiological role of hydrogen sulfide and beyond

Author keywords

Bound sulfane sulfur; Polysulfides; Sulfhydration; Sulfuration; TRP channels

Indexed keywords

3 MERCAPTOPYRUVATE SULFURTRANSFERASE; CALCIUM ION; CYSTEINE; DEXTRO AMINO ACID OXIDASE; ELECTROPHILE; HYDROGEN SULFIDE; SULFIDE; SULFURTRANSFERASE; TRANSIENT RECEPTOR POTENTIAL CHANNEL A1; UNCLASSIFIED DRUG; CALCIUM;

EID: 84907598996     PISSN: 10898603     EISSN: 10898611     Source Type: Journal    
DOI: 10.1016/j.niox.2014.01.002     Document Type: Review
Times cited : (252)

References (92)
  • 3
    • 0025266258 scopus 로고
    • Determination of sulfide in brain tissue and rumen fluid by ion-interaction reversed-phase high-performance liquid chromatography
    • J.C. Savage, D.H. Gould, Determination of sulfide in brain tissue and rumen fluid by ion-interaction reversed-phase high-performance liquid chromatography, J. Chromatogr. 526 (1990) 540-545.
    • (1990) J. Chromatogr. , vol.526 , pp. 540-545
    • Savage, J.C.1    Gould, D.H.2
  • 4
    • 0029876402 scopus 로고    scopus 로고
    • The possible role of hydrogen sulfide as an endogenous neuromodulator
    • K. Abe, H. Kimura, The possible role of hydrogen sulfide as an endogenous neuromodulator, J. Neurosci. 16 (1996) 1066-1071.
    • (1996) J. Neurosci. , vol.16 , pp. 1066-1071
    • Abe, K.1    Kimura, H.2
  • 5
    • 0031589557 scopus 로고    scopus 로고
    • The possible role of hydrogen sulfide as an endogenous smooth muscle relaxant in synergy with nitric oxide
    • R. Hosoki, N. Matsuki, H. Kimura, The possible role of hydrogen sulfide as an endogenous smooth muscle relaxant in synergy with nitric oxide, Biochem. Biophys. Res. Commun. 237 (1997) 527-531.
    • (1997) Biochem. Biophys. Res. Commun. , vol.237 , pp. 527-531
    • Hosoki, R.1    Matsuki, N.2    Kimura, H.3
  • 6
    • 0035503695 scopus 로고    scopus 로고
    • 2S as a novel endogenous gaseous KATP channel opener
    • W. Zhao, J. Zhang, Y. Lu, R. Wang, The vasorelaxant effect of H2S as a novel endogenous gaseous KATP channel opener, EMBO J. 20 (2001) 6008-6016.
    • (2001) EMBO J. , vol.20 , pp. 6008-6016
    • Zhao, W.1    Zhang, J.2    Lu, Y.3    Wang, R.4
  • 7
    • 0036737715 scopus 로고    scopus 로고
    • The smooth muscle relaxant effect of hydrogen sulphide in vitro: Evidence for a physiological role to control intestinal contractility
    • B. Teague, S. Asiedu, P.K. Moore, The smooth muscle relaxant effect of hydrogen sulphide in vitro: evidence for a physiological role to control intestinal contractility, Br. J. Pharmacol. 137 (2002) 139-145.
    • (2002) Br. J. Pharmacol. , vol.137 , pp. 139-145
    • Teague, B.1    Asiedu, S.2    Moore, P.K.3
  • 9
    • 84858182910 scopus 로고    scopus 로고
    • NOSH-aspirin: A novel nitric oxidehydrogen sulfide-releasing hybrid: A new class of anti-inflammatory pharmaceuticals
    • R. Kodela, M. Chattopadhyay, K. Kashfi, NOSH-aspirin: A novel nitric oxidehydrogen sulfide-releasing hybrid: A new class of anti-inflammatory pharmaceuticals, ACS Med. Chem. Lett. 3 (2012) 257-262.
    • (2012) ACS Med. Chem. Lett. , vol.3 , pp. 257-262
    • Kodela, R.1    Chattopadhyay, M.2    Kashfi, K.3
  • 12
    • 9444263079 scopus 로고    scopus 로고
    • Hydrogen sulfide protects neurons from oxidative stress
    • Y. Kimura, H. Kimura, Hydrogen sulfide protects neurons from oxidative stress, FASEB J. 18 (2004) 1165-1167.
    • (2004) FASEB J. , vol.18 , pp. 1165-1167
    • Kimura, Y.1    Kimura, H.2
  • 14
  • 15
    • 71549130783 scopus 로고    scopus 로고
    • Hydrogen sulfide increases glutathione production and suppresses oxidative stress in mitochondria
    • Y. Kimura, Y.-I. Goto, H. Kimura, Hydrogen sulfide increases glutathione production and suppresses oxidative stress in mitochondria, Antioxid. Redox. Signal. 12 (2010) 1-13.
    • (2010) Antioxid. Redox. Signal. , vol.12 , pp. 1-13
    • Kimura, Y.1    Goto, Y.-I.2    Kimura, H.3
  • 16
    • 80655128144 scopus 로고    scopus 로고
    • Hydrogen sulfide protects the retina from light-induced degeneration by the modulation of ca2+ influx
    • Y. Mikami, N. Shibuya, Y. Kimura, N. Nagahara, M. Yamada, H. Kimura, Hydrogen sulfide protects the retina from light-induced degeneration by the modulation of Ca2+ influx, J. Biol. Chem. 286 (2011) 39379-39386.
    • (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
    • 83655165310 scopus 로고    scopus 로고
    • H2s-induced sulfhydration of the phosphatase ptp1b and its role in the endoplasmic reticulum stress response
    • N. Krishnan, C. Fu, D.J. Pappin, N.K. Tonks, H2S-induced sulfhydration of the phosphatase PTP1B and its role in the endoplasmic reticulum stress response, Sci. Signal. 4 (2011) ra86.
    • (2011) Sci. Signal. , vol.4
    • Krishnan, N.1    Fu, C.2    Pappin, D.J.3    Tonks, N.K.4
  • 24
    • 77049164862 scopus 로고
    • Enzymatic desulfuratio of mercaptopyruvate to pyruvate
    • A. Meister, P.E. Fraser, S.V. Tice, Enzymatic desulfuratio of mercaptopyruvate to pyruvate, J. Biol. Chem. 260 (1954) 561-575.
    • (1954) J. Biol. Chem. , vol.260 , pp. 561-575
    • Meister, A.1    Fraser, P.E.2    Tice, S.V.3
  • 26
    • 0015235272 scopus 로고
    • Specificity and some other properties of liver serine sulphhydrase: Evidence for its identity with cystathionine β-synthase
    • A.E. Braunstein, E.V. Goryachenkowa, E.A. Tolosa, I.H. Willhardt, L.L. Yefremova, Specificity and some other properties of liver serine sulphhydrase: evidence for its identity with cystathionine β-synthase, Biochim. Biophys. Acta 242 (1971) 247-260.
    • (1971) Biochim. Biophys. Acta , vol.242 , pp. 247-260
    • Braunstein, A.E.1    Goryachenkowa, E.V.2    Tolosa, E.A.3    Willhardt, I.H.4    Yefremova, L.L.5
  • 27
    • 0020483746 scopus 로고
    • Characterization of the enzymic capacity for cysteine desulphhydration in liver and kidney of the rat
    • M.H. Stipanuk, P.W. Beck, Characterization of the enzymic capacity for cysteine desulphhydration in liver and kidney of the rat, Biochem. J. 206 (1982) 267-277.
    • (1982) Biochem. J. , vol.206 , pp. 267-277
    • Stipanuk, M.H.1    Beck, P.W.2
  • 28
    • 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
    • Y. Kaneko, Y. Kimura, H. Kimura, I. Niki, L-Cysteine inhibits insulin release from the pancreatic beta-cell: possible involvement of metabolic production of hydrogen sulfide, a novel gasotransmitter, Diabetes 55 (2006) 1391-1397.
    • (2006) Diabetes , vol.55 , pp. 1391-1397
    • Kaneko, Y.1    Kimura, Y.2    Kimura, H.3    Niki, I.4
  • 30
    • 10644254287 scopus 로고    scopus 로고
    • 2S by cystathionine beta-synthase via the condensation of cysteine and homocysteine
    • 2S by cystathionine beta-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.H.2    Kruger, W.D.3
  • 31
    • 0035893841 scopus 로고    scopus 로고
    • Characterization of NO binding to human cystathionine beta-synthase: Possible implications of the effects of CO and NO binding to the human enzyme
    • S. Taoka, R. Banerjee, Characterization of NO binding to human cystathionine beta-synthase: possible implications of the effects of CO and NO binding to the human enzyme, J. Inorg. Biochem. 87 (2001) 245-251.
    • (2001) J. Inorg. Biochem. , vol.87 , pp. 245-251
    • Taoka, S.1    Banerjee, R.2
  • 33
    • 0025362827 scopus 로고
    • Methionine metabolism in mammals
    • J.D. Finkelstein, Methionine metabolism in mammals, J. Nutr. Biochem. 1 (1990) 228-237.
    • (1990) J. Nutr. Biochem. , vol.1 , pp. 228-237
    • Finkelstein, J.D.1
  • 34
    • 3142758491 scopus 로고    scopus 로고
    • Murine cystathionine4 γ-lyase: Complete cDNA and genomic sequences, promoter activity, tissue ddistribution and developmental expression
    • I. Ishii, N. Akahoshi, X.-N. Yu, Y. Kobayashi, K. Namekata, G. Komaki, H. Kimura, Murine cystathionine4 γ-lyase: complete cDNA and genomic sequences, promoter activity, tissue ddistribution and developmental expression, Biochem. J. 381 (2004) 113-123.
    • (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    Kimura, H.7
  • 35
    • 66449109703 scopus 로고    scopus 로고
    • 2S biogenesis by human cystathionine β-lyase leads to the novel sulfur metabolites lanthionine and homnolanthionine and is responsive to the grade of hyperhomocysteinemia
    • 2S biogenesis by human cystathionine β-lyase leads to the novel sulfur metabolites lanthionine and homnolanthionine and is responsive to the grade of hyperhomocysteinemia, J. Biol. Bhem. 284 (2009) 11601-11612.
    • (2009) J. Biol. Bhem. , vol.284 , pp. 11601-11612
    • Chiku, T.1    Padovani, D.2    Zhu, W.3    Singh, S.4    Vitvitsky, V.5    Banerjee, R.6
  • 36
    • 0016215747 scopus 로고
    • Role of 3-mercaptopyruvate sulfurtransferase in the formation of the iron-sulfur chromophore of adrenal ferredoxin
    • T. Taniguchi, T. Kimura, Role of 3-mercaptopyruvate sulfurtransferase in the formation of the iron-sulfur chromophore of adrenal ferredoxin, Biochim. Biophys. Acta 364 (1974) 284-295.
    • (1974) Biochim. Biophys. Acta , vol.364 , pp. 284-295
    • Taniguchi, T.1    Kimura, T.2
  • 37
    • 0018213564 scopus 로고
    • Purification and characterization of mitochondrial cysteine aminotransferase from rat liver
    • T. Ubuka, S. Umemura, S. Yuasa, M. Kinuta, K. Watanabe, Purification and characterization of mitochondrial cysteine aminotransferase from rat liver, Physiol. Chem. Phys. 10 (1978) 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
  • 38
    • 0020686355 scopus 로고
    • Biochemistry of sulfur-containing amino acids
    • A.J.L. Cooper, Biochemistry of sulfur-containing amino acids, Annu. Rev. Biochem. 52 (1983) 187-222.
    • (1983) Annu. Rev. Biochem. , vol.52 , pp. 187-222
    • Cooper, A.J.L.1
  • 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
    • N. Nagahara, T. Ito, H. Kitamura, T. Nishino, Tissue and subcellular distribution of mercaptopyruvate sulfurtransferase in the rat: confocal laser fluorescence and immunoelectron microscopic studies combined with biochemical analysis, Histochem. Cell Biol. 110 (1998) 243-250.
    • (1998) Histochem. Cell Biol. , vol.110 , pp. 243-250
    • Nagahara, N.1    Ito, T.2    Kitamura, H.3    Nishino, T.4
  • 40
    • 0033231162 scopus 로고    scopus 로고
    • Biologic and pharmacologic regulation of mammalian glutathione synthesis
    • O.W. Griffith, Biologic and pharmacologic regulation of mammalian glutathione synthesis, Free Radic. Biol. Med. 27 (1999) 922-935.
    • (1999) Free Radic. Biol. Med. , vol.27 , pp. 922-935
    • Griffith, O.W.1
  • 41
  • 42
    • 84860761445 scopus 로고    scopus 로고
    • Hydrogen sulfide is a signaling molecule and a cytoprotectant
    • H. Kimura, N. Shibuya, Y. Kimura, Hydrogen sulfide is a signaling molecule and a cytoprotectant, Antioxid. Redox. Sginal. 17 (2012) 45-57.
    • (2012) Antioxid. Redox. Sginal. , vol.17 , pp. 45-57
    • Kimura, H.1    Shibuya, N.2    Kimura, Y.3
  • 43
    • 77954579286 scopus 로고    scopus 로고
    • Redox biochemistry of hydrogen sulfide
    • O. Kabil, R. Banerjee, 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
  • 44
    • 33847335589 scopus 로고    scopus 로고
    • Thioredoxin-dependent enzymatic activation of mercaptopyruvate sulfurtransferase. An intersubunit disulfide bond serves as a redox switch for activation
    • N. Nagahara, T. Yoshii, Y. Abe, T. Matsumura, Thioredoxin-dependent enzymatic activation of mercaptopyruvate sulfurtransferase. An intersubunit disulfide bond serves as a redox switch for activation, J. Biol. Chem. 282 (2007) 1561-1569.
    • (2007) J. Biol. Chem. , vol.282 , pp. 1561-1569
    • Nagahara, N.1    Yoshii, T.2    Abe, Y.3    Matsumura, T.4
  • 46
    • 80054015725 scopus 로고    scopus 로고
    • Thioredoxin and dihydrolipoic acid are required for 3-mercaptopyruvate sulfurtransferase to produce hydrogen sulfide
    • Y. Mikami, N. Shibuya, Y. Kimura, N. Nagahara, Y. Ogasawara, H. Kimura, Thioredoxin and dihydrolipoic acid are required for 3-mercaptopyruvate sulfurtransferase to produce hydrogen sulfide, Biochem. J. 439 (2011) 479-485.
    • (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
  • 47
    • 0027311039 scopus 로고
    • Analysis of lipoic acid in biological samples by gas chromatography with flame photometric detection
    • H. Kataoka, N. Hirabayashi, M. Makita, Analysis of lipoic acid in biological samples by gas chromatography with flame photometric detection, J. Chromatogr. 615 (1993) 197-202.
    • (1993) J. Chromatogr. , vol.615 , pp. 197-202
    • Kataoka, H.1    Hirabayashi, N.2    Makita, M.3
  • 48
    • 48849114553 scopus 로고    scopus 로고
    • Is a-lipoic acid a scavenger of reactive oxygen species in vivo? Evidence for its initiation of stress signaling pathways that promote endogenous antioxidant capacity
    • K. Petersen-Shay, R. Moreau, E. Smith, T. Hagen, Is a-lipoic acid a scavenger of reactive oxygen species in vivo? Evidence for its initiation of stress signaling pathways that promote endogenous antioxidant capacity, IUBMB Life 60 (2008) 362-367.
    • (2008) IUBMB Life , vol.60 , pp. 362-367
    • Petersen-Shay, K.1    Moreau, R.2    Smith, E.3    Hagen, T.4
  • 49
    • 0014404185 scopus 로고
    • Thioredoxin. VI. The amino acid sequence of the protein from escherichia coli b
    • A. Holmgren, Thioredoxin. VI. The amino acid sequence of the protein from Escherichia coli B, Eur. J. Biochem. 6 (1968) 475-484.
    • (1968) Eur. J. Biochem. , vol.6 , pp. 475-484
    • Holmgren, A.1
  • 50
    • 0014139748 scopus 로고
    • The standard redox potential of cysteine-cystine form the thioldisulphide exchange reaction with glutathione and lipoic acid
    • P.C. Jocelyn, The standard redox potential of cysteine-cystine form the thioldisulphide exchange reaction with glutathione and lipoic acid, Eur. J. Biochem. 2 (1967) 327-331.
    • (1967) Eur. J. Biochem. , vol.2 , pp. 327-331
    • Jocelyn, P.C.1
  • 51
    • 0003021182 scopus 로고
    • The free-energy changes for the reduction of diphosphopyridine nucleotide and the dehydrogenation of L-malate and lglycerol 1-phosphate
    • K. Burton, T. Wilson, The free-energy changes for the reduction of diphosphopyridine nucleotide and the dehydrogenation of L-malate and Lglycerol 1-phosphate, Biochem. J. 54 (1953) 86-94.
    • (1953) Biochem. J. , vol.54 , pp. 86-94
    • Burton, K.1    Wilson, T.2
  • 52
    • 0032568532 scopus 로고    scopus 로고
    • Human sulfite oxidase R160Q: Identification of the mutation in a sulfite oxidasedeficient patient and expression and characterization of the mutant enzyme
    • R.M. Garrett, J.L. Johnson, T.N. Graf, A. Feigenbaum, K.V. Rajagopalan, Human sulfite oxidase R160Q: identification of the mutation in a sulfite oxidasedeficient patient and expression and characterization of the mutant enzyme, Proc. Natl. Acad. Sci. USA 95 (1998) 6394-6398.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 6394-6398
    • Garrett, R.M.1    Johnson, J.L.2    Graf, T.N.3    Feigenbaum, A.4    Rajagopalan, K.V.5
  • 56
    • 0036716376 scopus 로고    scopus 로고
    • Calcium regulation in photoreceptors
    • D. Krizaj, D.R. Copenhagen, Calcium regulation in photoreceptors, Front. Biosci. 7 (2002) d2023-d2044.
    • (2002) Front. Biosci. , vol.7
    • Krizaj, D.1    Copenhagen, D.R.2
  • 57
    • 84930832275 scopus 로고    scopus 로고
    • A mechanism of retinal protection from light-induced degeneration by hydrogen sulfide
    • Y. Mikami, H. Kimura, A mechanism of retinal protection from light-induced degeneration by hydrogen sulfide, Commun. Integr. Biol. 5 (2) (2012) 1-3.
    • (2012) Commun. Integr. Biol. , vol.5 , Issue.2 , pp. 1-3
    • Mikami, Y.1    Kimura, H.2
  • 60
    • 68649090226 scopus 로고    scopus 로고
    • Regulation of mitochondrial dehydrogenases by calcium ions
    • R.M. Denton, Regulation of mitochondrial dehydrogenases by calcium ions, Biochim. Biophys. Acta 1787 (2009) 1309-1316.
    • (2009) Biochim. Biophys. Acta , vol.1787 , pp. 1309-1316
    • Denton, R.M.1
  • 61
    • 0029156742 scopus 로고
    • Anatomical distribution and postnatal changes in endogenous free D-aspartate and d-serine in rat brain and periphery
    • A. Hashimoto, T. Oka, T. Nishikawa, Anatomical distribution and postnatal changes in endogenous free D-aspartate and D-serine in rat brain and periphery, Eur. J. Neurosci. 7 (1995) 1657-1663.
    • (1995) Eur. J. Neurosci. , vol.7 , pp. 1657-1663
    • Hashimoto, A.1    Oka, T.2    Nishikawa, T.3
  • 62
    • 44649112394 scopus 로고    scopus 로고
    • Special delivery from mitochondria to peroxisomes
    • U. Schumann, S. Subramani, Special delivery from mitochondria to peroxisomes, Trends Cell Biol. 18 (2008) 253-256.
    • (2008) Trends Cell Biol. , vol.18 , pp. 253-256
    • Schumann, U.1    Subramani, S.2
  • 63
    • 0024076281 scopus 로고
    • Identification of peroxisomal targeting signals located at the carboxy terminus of four peroxisomal proteins
    • S.J. Gould, G.A. Keller, S. Subramani, Identification of peroxisomal targeting signals located at the carboxy terminus of four peroxisomal proteins, J. Cell Biol. 107 (1988) 897-905.
    • (1988) J. Cell Biol. , vol.107 , pp. 897-905
    • Gould, S.J.1    Keller, G.A.2    Subramani, S.3
  • 64
    • 0001062020 scopus 로고
    • Metabolism of amino-acids
    • H.A. Krebs, Metabolism of amino-acids, Biochem. J. 29 (1935) 1620-1644.
    • (1935) Biochem. J. , vol.29 , pp. 1620-1644
    • Krebs, H.A.1
  • 65
    • 0032525749 scopus 로고    scopus 로고
    • Hepatocyte-catalysed detoxification of cyanide by L- And D-cysteine
    • J. Huang, H. Niknahad, S. Khan, P.J. O'Brien, Hepatocyte-catalysed detoxification of cyanide by L- And D-cysteine, Biochem. Pharmacol. 55 (1998) 1983-1990.
    • (1998) Biochem. Pharmacol. , vol.55 , pp. 1983-1990
    • Huang, J.1    Niknahad, H.2    Khan, S.3    O'Brien, P.J.4
  • 66
    • 0000182791 scopus 로고
    • Racemization kinetics of free and protein-bound amino acids under moderate alkaline treatment
    • R. Liardon, S. Ledermann, Racemization kinetics of free and protein-bound amino acids under moderate alkaline treatment, J. Agric. Food Chem. 34 (1986) 557-565.
    • (1986) J. Agric. Food Chem. , vol.34 , pp. 557-565
    • Liardon, R.1    Ledermann, S.2
  • 67
    • 77953888010 scopus 로고    scopus 로고
    • Origin, microbiology, nutrition and pharmacology of d-amino acids
    • M. Friedman, Origin, microbiology, nutrition and pharmacology of D-amino acids, Chem. Biodivers. 7 (2010) 1491-1530.
    • (2010) Chem. Biodivers. , vol.7 , pp. 1491-1530
    • Friedman, M.1
  • 69
    • 0028557060 scopus 로고
    • Tissue and subcellular distribution of bound and acid-labile sulfur, and the enzymic capacity for sulfide production in the rat
    • Y. Ogasawara, S. Isoda, S. Tanabe, Tissue and subcellular distribution of bound and acid-labile sulfur, and the enzymic capacity for sulfide production in the rat, Biol. Pharm. Bull. 17 (1994) 1535-1542.
    • (1994) Biol. Pharm. Bull. , vol.17 , pp. 1535-1542
    • Ogasawara, Y.1    Isoda, S.2    Tanabe, S.3
  • 70
    • 84864285556 scopus 로고    scopus 로고
    • 2S signaling through protein sulfhydration and beyond
    • 2S signaling through protein sulfhydration and beyond, Nat. Rev. Mol. Cell Biol. 13 (2012) 499-507.
    • (2012) Nat. Rev. Mol. Cell Biol. , vol.13 , pp. 499-507
    • Paul, B.D.1    Snyder, S.H.2
  • 71
    • 79953712285 scopus 로고    scopus 로고
    • Sulfur signaling: Is the agent sulfide or sulfane?
    • J.I. Toohey, Sulfur signaling: Is the agent sulfide or sulfane?, Anal Biochem. 413 (2011) 1-7.
    • (2011) Anal Biochem. , vol.413 , pp. 1-7
    • Toohey, J.I.1
  • 73
    • 77950851571 scopus 로고    scopus 로고
    • Hydrogen sulfide: From brain to gut
    • H. Kimura, Hydrogen sulfide: from brain to gut, Antioxid. Redox. Signal. 12 (2010) 1111-1123.
    • (2010) Antioxid. Redox. Signal. , vol.12 , pp. 1111-1123
    • Kimura, H.1
  • 75
    • 0027997626 scopus 로고
    • Rat hippocampal astrocytes exhibit electrogenic sodium-bicarbonate co-transport
    • E.R. O'Connor, H. Sontheimer, B.R. Ransom, Rat hippocampal astrocytes exhibit electrogenic sodium-bicarbonate co-transport, J. Neurophysiol. 72 (1994) 2580-2589.
    • (1994) J. Neurophysiol , vol.72 , pp. 2580-2589
    • O'Connor, E.R.1    Sontheimer, H.2    Ransom, B.R.3
  • 77
    • 77958095282 scopus 로고    scopus 로고
    • Rapid reaction of hydrogen sulfide with the neutrophil oxidant hypochlorous acid to generate polysulfides
    • P. Nagy, C.C. Winterbourn, Rapid reaction of hydrogen sulfide with the neutrophil oxidant hypochlorous acid to generate polysulfides, Chem. Res. Toxicol. 23 (2010) 1541-1543.
    • (2010) Chem. Res. Toxicol. , vol.23 , pp. 1541-1543
    • Nagy, P.1    Winterbourn, C.C.2
  • 78
    • 2442655642 scopus 로고    scopus 로고
    • Hydrogen sulfide induces calcium waves in astrocytes
    • Y. Nagai, M. Tsugane, J. Oka, H. Kimura, Hydrogen sulfide induces calcium waves in astrocytes, FASEB J. 18 (2004) 557-559.
    • (2004) FASEB J. , vol.18 , pp. 557-559
    • Nagai, Y.1    Tsugane, M.2    Oka, J.3    Kimura, H.4
  • 79
    • 84878758877 scopus 로고    scopus 로고
    • Polysulfides induce calcium waves in rat hippocampal astrocytes
    • ISSN: 1347-8613
    • Y. Nagai, M. Tsugane, J. Oka, H. Kimura, Polysulfides induce calcium waves in rat hippocampal astrocytes. J. Pharmacol. Sci. 100 (Suppl. I) (2006) 200, ISSN: 1347-8613.
    • (2006) J. Pharmacol. Sci. , vol.100 , Issue.SUPPL. 1 , pp. 200
    • Nagai, Y.1    Tsugane, M.2    Oka, J.3    Kimura, H.4
  • 84
    • 0024623852 scopus 로고
    • Selective modulation of NMDA responses by reduction and oxidation
    • E. Aizenman, D.A. Lipton, R.H. Loring, Selective modulation of NMDA responses by reduction and oxidation, Neuron 2 (1989) 1257-1263.
    • (1989) Neuron , vol.2 , pp. 1257-1263
    • Aizenman, E.1    Lipton, D.A.2    Loring, R.H.3
  • 86
    • 84555172978 scopus 로고    scopus 로고
    • TRPA1 channels regulate astrocyte resting calcium and inhibitory synapse efficacy through GAT-3
    • E. Shigetomi, X. Tong, K.Y. Kwan, D.P. Corey, B.S. Khakh, TRPA1 channels regulate astrocyte resting calcium and inhibitory synapse efficacy through GAT-3, Nat. Neurosci. 15 (2012) 70-80.
    • (2012) Nat. Neurosci. , vol.15 , pp. 70-80
    • Shigetomi, E.1    Tong, X.2    Kwan, K.Y.3    Corey, D.P.4    Khakh, B.S.5
  • 87
    • 84878867774 scopus 로고    scopus 로고
    • TRPA1 channels are regulators of astrocyte basal calcium levels and long-term potentiation via constitutive d-serine release
    • E. Shigetomi, O. Jackson-Weaver, R.T. Huckstepp, T.J. O'Dell, B.S. Khakh, TRPA1 channels are regulators of astrocyte basal calcium levels and long-term potentiation via constitutive D-serine release, J. Neurosci. 33 (2013) 10143- 10153.
    • (2013) J. Neurosci. , vol.33 , pp. 10143-10153
    • Shigetomi, E.1    Jackson-Weaver, O.2    Huckstepp, R.T.3    O'Dell, T.J.4    Khakh, B.S.5
  • 88
    • 0026325942 scopus 로고
    • Tests of the roles of two diffusible substances in long-term potentiation: Evidence for nitric oxide as a possible early retrograde messenger
    • T.J. O'Dell, R.D. Hawkins, E.R. Kandel, O. Arancio, Tests of the roles of two diffusible substances in long-term potentiation: evidence for nitric oxide as a possible early retrograde messenger, Proc. Natl. Acad. Sci. USA 88 (1991) 11285-11289.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 11285-11289
    • O'Dell, T.J.1    Hawkins, R.D.2    Kandel, E.R.3    Arancio, O.4
  • 90
    • 0027296209 scopus 로고
    • Reversal of long-term potentiation by inhibitors of heme oxygenase
    • C.F. Stevens, Y. Wang, Reversal of long-term potentiation by inhibitors of heme oxygenase, Nature 364 (1993) 147-149.
    • (1993) Nature , vol.364 , pp. 147-149
    • Stevens, C.F.1    Wang, Y.2
  • 91
    • 0027267817 scopus 로고
    • Nitric oxide and carbon monoxide produce activity-dependent long-term synaptic enhancement in hippocampus
    • M. Zhuo, S.A. Small, E.R. Kandel, R.D. Hawkins, Nitric oxide and carbon monoxide produce activity-dependent long-term synaptic enhancement in hippocampus, Science 260 (1993) 1946-1950.
    • (1993) Science , vol.260 , pp. 1946-1950
    • Zhuo, M.1    Small, S.A.2    Kandel, E.R.3    Hawkins, R.D.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.