메뉴 건너뛰기




Volumn 18, Issue 3, 2013, Pages 309-322

Nitrosothiols in bacterial pathogens and pathogenesis

Author keywords

[No Author keywords available]

Indexed keywords

ABC TRANSPORTER; ADENOSINE TRIPHOSPHATASE; BACTERIAL PROTEIN; CELL PROTEIN; DYNAMIN II; ENDOTHELIAL NITRIC OXIDE SYNTHASE; GAMMA GLUTAMYLTRANSFERASE; GLUTATHIONE; GLUTATHIONE PEROXIDASE; GUANOSINE TRIPHOSPHATASE; HEMOGLOBIN; HOMOCYSTEINE; METHIONINE; NITRIC OXIDE; NITRIC OXIDE DONOR; NITRIC OXIDE REDUCTASE; NITROPRUSSIDE SODIUM; NITROREDUCTASE; PEROXYNITRITE; PROTEIN; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; S NITROSOGLUTATHIONE; S NITROSOPROTEIN; S NITROSOTHIOL; SURFACTANT PROTEIN D; THIOREDOXIN; THIOREDOXIN REDUCTASE; UNCLASSIFIED DRUG; XANTHINE OXIDASE;

EID: 84870719815     PISSN: 15230864     EISSN: 15577716     Source Type: Journal    
DOI: 10.1089/ars.2012.4767     Document Type: Review
Times cited : (21)

References (124)
  • 1
    • 42949125903 scopus 로고    scopus 로고
    • The preparation and purification of NO gas and the use of NO releasers: The application of NO donors and other agents of nitrosative stress in biological systems
    • Aga RG and Hughes MN. The preparation and purification of NO gas and the use of NO releasers: The application of NO donors and other agents of nitrosative stress in biological systems. Methods Enzymol 436: 35-48, 2008.
    • (2008) Methods Enzymol , vol.436 , pp. 35-48
    • Aga, R.G.1    Hughes, M.N.2
  • 2
    • 84862556342 scopus 로고    scopus 로고
    • Enzymatic mechanisms regulating protein S-nitrosylation: Implications in health and disease
    • Anand P and Stamler JS. Enzymatic mechanisms regulating protein S-nitrosylation: Implications in health and disease. J Mol Med (Berl) 90: 233-244, 2012.
    • (2012) J Mol Med (Berl) , vol.90 , pp. 233-244
    • Anand, P.1    Stamler, J.S.2
  • 3
    • 0028928312 scopus 로고
    • Chemical mechanisms underlying the vasodilator and platelet anti-aggregating properties of S-nitroso-N-acetyl-DL-penicillamine and S-nitrosoglutathione
    • Askew SC, Butler AR, Flitney FW, Kemp GD, and Megson IL. Chemical mechanisms underlying the vasodilator and platelet anti-aggregating properties of S-nitroso-N-acetyl-DL-penicillamine and S-nitrosoglutathione. Bioorg Med Chem 3: 1-9, 1995.
    • (1995) Bioorg Med Chem , vol.3 , pp. 1-9
    • Askew, S.C.1    Butler, A.R.2    Flitney, F.W.3    Kemp, G.D.4    Megson, I.L.5
  • 4
    • 84860469996 scopus 로고    scopus 로고
    • S-nitrosylation of surfactant protein D as a modulator of pulmonary inflammation
    • Atochina-Vasserman EN. S-nitrosylation of surfactant protein D as a modulator of pulmonary inflammation. Biochim Biophys Acta 1820: 763-769, 2012.
    • (2012) Biochim Biophys Acta , vol.1820 , pp. 763-769
    • Atochina-Vasserman, E.N.1
  • 5
    • 61449239078 scopus 로고    scopus 로고
    • Immune reconstitution during Pneumocystis lung infection: Disruption of surfactant component expression and function by S-nitrosylation
    • Atochina-Vasserman EN, Gow AJ, Abramova H, Guo CJ, Tomer Y, Preston AM, Beck JM, and Beers MF. Immune reconstitution during Pneumocystis lung infection: Disruption of surfactant component expression and function by S-nitrosylation. J Immunol 182: 2277-2287, 2009.
    • (2009) J Immunol , vol.182 , pp. 2277-2287
    • Atochina-Vasserman, E.N.1    Gow, A.J.2    Abramova, H.3    Guo, C.J.4    Tomer, Y.5    Preston, A.M.6    Beck, J.M.7    Beers, M.F.8
  • 7
    • 70349470951 scopus 로고    scopus 로고
    • Glutathione disulfide and S-nitrosoglutathione detoxification by Mycobacterium tuberculosis thioredoxin system
    • Attarian R, Bennie C, Bach H, and Av-Gay Y. Glutathione disulfide and S-nitrosoglutathione detoxification by Mycobacterium tuberculosis thioredoxin system. FEBS Lett 583: 3215-3220, 2009.
    • (2009) FEBS Lett , vol.583 , pp. 3215-3220
    • Attarian, R.1    Bennie, C.2    Bach, H.3    Av-Gay, Y.4
  • 8
    • 84871337611 scopus 로고    scopus 로고
    • Do globins in microaerophilic Campylobacter jejuni confer nitrosative stress tolerance under oxygen limitation?
    • Epub ahead of print] DOI: 10. 1089/ars 2012.4750
    • Avila Ramirez C, Tinajero Trejo M, Davidge K, Monk C, and Kelly DJ. Do globins in microaerophilic Campylobacter jejuni confer nitrosative stress tolerance under oxygen limitation? Antiox Redox Signal 2012 [Epub ahead of print]; DOI: 10. 1089/ars. 2012. 4750.
    • (2012) Antiox Redox Signal
    • Avila Ramirez, C.1    Tinajero Trejo, M.2    Davidge, K.3    Monk, C.4    Kelly, D.J.5
  • 9
    • 43049181499 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis Virulence Is Mediated by PtpA Dephosphorylation of Human Vacuolar Protein Sorting 33B
    • DOI 10.1016/j.chom.2008.03.008, PII S1931312808001182
    • Bach H, Papavinasasundaram KG, Wong D, Hmama Z, and Av-Gay Y. Mycobacterium tuberculosis virulence is mediated by PtpA dephosphorylation of human vacuolar protein sorting 33B. Cell Host Microbe 3: 316-322, 2008. (Pubitemid 351635998)
    • (2008) Cell Host and Microbe , vol.3 , Issue.5 , pp. 316-322
    • Bach, H.1    Papavinasasundaram, K.G.2    Wong, D.3    Hmama, Z.4    Av-Gay, Y.5
  • 12
    • 31344459536 scopus 로고    scopus 로고
    • The yjeB (nsrR) gene of Escherichia coli encodes a nitric oxide-sensitive transcriptional regulator
    • DOI 10.1128/JB.188.3.874-881.2006
    • Bodenmiller DM and Spiro S. The yjeB (nsrR) gene of Escherichia coli encodes a nitric oxide-sensitive transcriptional regulator. J Bacteriol 188: 874-881, 2006. (Pubitemid 43146402)
    • (2006) Journal of Bacteriology , vol.188 , Issue.3 , pp. 874-881
    • Bodenmiller, D.M.1    Spiro, S.2
  • 13
    • 0034640125 scopus 로고    scopus 로고
    • The crystal structure of a sulfurtransferase from Azotobacter vinelandii highlights the evolutionary relationship between the rhodanese and phosphatase enzyme families
    • Bordo D, Deriu D, Colnaghi R, Carpen A, Pagani S, and Bolognesi M. The crystal structure of a sulfurtransferase from Azotobacter vinelandii highlights the evolutionary relationship between the rhodanese and phosphatase enzyme families. J Mol Biol 298: 691-704, 2000.
    • (2000) J Mol Biol , vol.298 , pp. 691-704
    • Bordo, D.1    Deriu, D.2    Colnaghi, R.3    Carpen, A.4    Pagani, S.5    Bolognesi, M.6
  • 14
    • 79959554902 scopus 로고    scopus 로고
    • Nitrosative damage to free and zinc-bound cysteine thiols underlies nitric oxide toxicity in wild-type Borrelia burgdorferi
    • Bourret TJ, Boylan JA, Lawrence KA, and Gherardini FC. Nitrosative damage to free and zinc-bound cysteine thiols underlies nitric oxide toxicity in wild-type Borrelia burgdorferi. Mol Microbiol 81: 259-273, 2011.
    • (2011) Mol Microbiol , vol.81 , pp. 259-273
    • Bourret, T.J.1    Boylan, J.A.2    Lawrence, K.A.3    Gherardini, F.C.4
  • 15
    • 81855175401 scopus 로고    scopus 로고
    • The diversity of microbial responses to nitric oxide and agents of nitrosative stress close cousins but not identical twins
    • Bowman LA, McLean S, Poole RK, and Fukuto JM. The diversity of microbial responses to nitric oxide and agents of nitrosative stress close cousins but not identical twins. Adv Microb Physiol 59: 135-219, 2011.
    • (2011) Adv Microb Physiol , vol.59 , pp. 135-219
    • Bowman, L.A.1    McLean, S.2    Poole, R.K.3    Fukuto, J.M.4
  • 16
    • 35748969097 scopus 로고    scopus 로고
    • Nitrosative stress treatment of E. coli targets distinct set of thiol-containing proteins
    • DOI 10.1111/j.1365-2958.2007.05964.x
    • Brandes N, Rinck A, Leichert LI, and Jakob U. Nitrosative stress treatment of E. coli targets distinct set of thiolcontaining proteins. Mol Microbiol 66: 901-914, 2007. (Pubitemid 350050418)
    • (2007) Molecular Microbiology , vol.66 , Issue.4 , pp. 901-914
    • Brandes, N.1    Rinck, A.2    Leichert, L.I.3    Jakob, U.4
  • 17
    • 0346251029 scopus 로고    scopus 로고
    • Contribution of Glutathione Peroxidase to the Virulence of Streptococcus pyogenes
    • DOI 10.1128/IAI.72.1.408-413.2004
    • Brenot A, King KY, Janowiak B, Griffith O, and Caparon MG. Contribution of glutathione peroxidase to the virulence of Streptococcus pyogenes. Infect Immun 72: 408-413, 2004. (Pubitemid 38018202)
    • (2004) Infection and Immunity , vol.72 , Issue.1 , pp. 408-413
    • Brenot, A.1    King, K.Y.2    Janowiak, B.3    Griffith, O.4    Caparon, M.G.5
  • 18
    • 0037458730 scopus 로고    scopus 로고
    • The proline-rich domain of dynamin-2 is responsible for dynamin-dependent in vitro potentiation of endothelial nitric-oxide synthase activity via selective effects on reductase domain function
    • DOI 10.1074/jbc.M212546200
    • Cao S, Yao J, and Shah V. The proline-rich domain of dynamin-2 is responsible for dynamin-dependent in vitro potentiation of endothelial nitric-oxide synthase activity via selective effects on reductase domain function. J Biol Chem 278: 5894-5901, 2003. (Pubitemid 36800836)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.8 , pp. 5894-5901
    • Cao, S.1    Yao, J.2    Shah, V.3
  • 19
    • 0037258943 scopus 로고    scopus 로고
    • Role of the thioredoxin system and the thiol-peroxidases Tpx and Bcp in mediating resistance to oxidative and nitrosative stress in Helicobacter pylori
    • DOI 10.1099/mic.0.25896-0
    • Comtois SL, Gidley MD, and Kelly DJ. Role of the thioredoxin system and the thiol-peroxidases Tpx and Bcp in mediating resistance to oxidative and nitrosative stress in Helicobacter pylori. Microbiology 149: 121-129, 2003. (Pubitemid 36175683)
    • (2003) Microbiology , vol.149 , Issue.1 , pp. 121-129
    • Comtois, S.L.1    Gidley, M.D.2    Kelly, D.J.3
  • 20
    • 0042858242 scopus 로고    scopus 로고
    • Nitric oxide formation by Escherichia coli. Dependence on nitrite reductase, the no-sensing regulator Fnr, and flavohemoglobin Hmp
    • DOI 10.1074/jbc.M303282200
    • Corker H and Poole RK. Nitric oxide formation by Escherichia coli: Dependence on nitrite reductase, the NO-sensing regulator FNR, and flavohemoglobin Hmp. J Biol Chem 278: 31584-31592, 2003. (Pubitemid 37048336)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.34 , pp. 31584-31592
    • Corker, H.1    Poole, R.K.2
  • 22
    • 0036646484 scopus 로고    scopus 로고
    • NO sensing by FNR: Regulation of the Escherichia coli NO-detoxifying flavohaemoglobin, Hmp
    • DOI 10.1093/emboj/cdf339
    • Cruz-Ramos H, Crack J, Wu G, Hughes MN, Scott C, Thomson AJ, Green J, and Poole RK. NO sensing by FNR: Regulation of the Escherichia coli NO-detoxifying flavohaemoglobin, Hmp. EMBO J 21: 3235-3244, 2002. (Pubitemid 34760556)
    • (2002) EMBO Journal , vol.21 , Issue.13 , pp. 3235-3244
    • Cruz-Ramos, H.1    Crack, J.2    Wu, G.3    Hughes, M.N.4    Scott, C.5    Thomson, A.J.6    Green, J.7    Poole, R.K.8
  • 24
    • 26944499456 scopus 로고    scopus 로고
    • A non-haem iron centre in the transcription factor NorR senses nitric oxide
    • DOI 10.1038/nature03953, PII N03953
    • D'Autreaux B, Tucker NP, Dixon R, and Spiro S. A nonhaem iron centre in the transcription factor NorR senses nitric oxide. Nature 437: 769-772, 2005. (Pubitemid 41486549)
    • (2005) Nature , vol.437 , Issue.7059 , pp. 769-772
    • D'Autreaux, B.1    Tucker, N.P.2    Dixon, R.3    Spiro, S.4
  • 26
    • 32444445544 scopus 로고    scopus 로고
    • Characterization of a glutathione metabolic mutant of Mycobacterium tuberculosis and its resistance to glutathione and nitrosoglutathione
    • DOI 10.1128/JB.188.4.1364-1372.2006
    • Dayaram YK, Talaue MT, Connell ND, and Venketaraman V. Characterization of a glutathione metabolic mutant of Mycobacterium tuberculosis and its resistance to glutathione and nitrosoglutathione. J Bacteriol 188: 1364-1372, 2006. (Pubitemid 43228668)
    • (2006) Journal of Bacteriology , vol.188 , Issue.4 , pp. 1364-1372
    • Dayaram, Y.K.1    Talaue, M.T.2    Connell, N.D.3    Venketaraman, V.4
  • 28
    • 0029664555 scopus 로고    scopus 로고
    • Homocysteine antagonism of nitric oxide-related cytostasis in Salmonella typhimurium
    • Degroote MA, Testerman T, Xu YS, Stauffer G, and Fang FC. Homocysteine antagonism of nitric oxide-related cytostasis in Salmonella typhimurium. Science 272: 414-417, 1996.
    • (1996) Science , vol.272 , pp. 414-417
    • Degroote, M.A.1    Testerman, T.2    Xu, Y.S.3    Stauffer, G.4    Fang, F.C.5
  • 29
    • 0034625165 scopus 로고    scopus 로고
    • Direct nitric oxide signal transduction via nitrosylation of iron-sulfur centers SoxR transcription activator
    • DOI 10.1073/pnas.97.10.5146
    • Ding HG and Demple B. Direct nitric oxide signal transduction via nitrosylation of iron-sulfur centers in the SoxR transcription activator. Proc Natl Acad Sci USA 97: 5146-5150, 2000. (Pubitemid 30313686)
    • (2000) Proceedings of the National Academy of Sciences of the United States of America , vol.97 , Issue.10 , pp. 5146-5150
    • Ding, H.1    Demple, B.2
  • 30
    • 78049288138 scopus 로고    scopus 로고
    • Structural profiling of endogenous S-nitrosocysteine residues reveals unique features that accommodate diverse mechanisms for protein S-nitrosylation
    • Doulias PT, Greene JL, Greco TM, Tenopoulou M, Seeholzer SH, Dunbrack RL, and Ischiropoulos H. Structural profiling of endogenous S-nitrosocysteine residues reveals unique features that accommodate diverse mechanisms for protein S-nitrosylation. Proc Natl Acad Sci USA 107: 16958-16963, 2010.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 16958-16963
    • Doulias, P.T.1    Greene, J.L.2    Greco, T.M.3    Tenopoulou, M.4    Seeholzer, S.H.5    Dunbrack, R.L.6    Ischiropoulos, H.7
  • 31
    • 77957664606 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis tyrosine phosphatase A (PtpA) activity is modulated by S-nitrosylation
    • Ecco G, Vernal J, Razzera G, Martins PA, Matiollo C, and Terenzi H. Mycobacterium tuberculosis tyrosine phosphatase A (PtpA) activity is modulated by S-nitrosylation. Chem Commun (Camb) 46: 7501-7503, 2010.
    • (2010) Chem Commun (Camb) , vol.46 , pp. 7501-7503
    • Ecco, G.1    Vernal, J.2    Razzera, G.3    Martins, P.A.4    Matiollo, C.5    Terenzi, H.6
  • 32
    • 78751684152 scopus 로고    scopus 로고
    • MexEF-oprN multidrug efflux operon of Pseudomonas aeruginosa: Regulation by the MexT activator in response to nitrosative stress and chloramphenicol
    • Fetar H, Gilmour C, Klinoski R, Daigle DM, Dean CR, and Poole K. mexEF-oprN multidrug efflux operon of Pseudomonas aeruginosa: Regulation by the MexT activator in response to nitrosative stress and chloramphenicol. Antimicrob Agents Chemother 55: 508-514, 2011.
    • (2011) Antimicrob Agents Chemother , vol.55 , pp. 508-514
    • Fetar, H.1    Gilmour, C.2    Klinoski, R.3    Daigle, D.M.4    Dean, C.R.5    Poole, K.6
  • 34
    • 15444363634 scopus 로고    scopus 로고
    • Transcriptional responses of Escherichia coli to S-nitrosoglutathione under defined chemostat conditions reveal major changes in methionine biosynthesis
    • DOI 10.1074/jbc.M410393200
    • Flatley J, Barrett J, Pullan ST, Hughes MN, Green J, and Poole RK. Transcriptional responses of Escherichia coli to Snitrosoglutathione under defined chemostat conditions reveal major changes in methionine biosynthesis. J Biol Chem 280: 10065-10072, 2005. (Pubitemid 40395858)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.11 , pp. 10065-10072
    • Flatley, J.1    Barrett, J.2    Pullan, S.T.3    Hughes, M.N.4    Green, J.5    Poolet, R.K.6
  • 35
    • 0025800573 scopus 로고
    • Mechanisms involved in mycobacterial growth-inhibition by gamma interferonactivated bone-marrow macrophages. Role of reactive nitrogen intermediates
    • Flesch IEA and Kaufmann SHE. Mechanisms involved in mycobacterial growth-inhibition by gamma interferonactivated bone-marrow macrophages. Role of reactive nitrogen intermediates. Infect Immun 59: 3213-3218, 1991.
    • (1991) Infect Immun , vol.59 , pp. 3213-3218
    • Flesch, I.E.A.1    Kaufmann, S.H.E.2
  • 38
    • 0034644756 scopus 로고    scopus 로고
    • Nitric-oxide dioxygenase activity and function of flavohemoglobins. Sensitivity to nitric oxide and carbon monoxide inhibition
    • Gardner PR, Gardner AM, Martin LA, Dou Y, Li TS, Olson JS, Zhu H, and Riggs AF. Nitric-oxide dioxygenase activity and function of flavohemoglobins. Sensitivity to nitric oxide and carbon monoxide inhibition. J Biol Chem 275: 31581-31587, 2000.
    • (2000) J Biol Chem , vol.275 , pp. 31581-31587
    • Gardner, P.R.1    Gardner, A.M.2    Martin, L.A.3    Dou, Y.4    Li, T.S.5    Olson, J.S.6    Zhu, H.7    Riggs, A.F.8
  • 40
    • 34250745705 scopus 로고    scopus 로고
    • NsrR: A key regulator circumventing Salmonella enterica serovar Typhimurium oxidative and nitrosative stress in vitro and in IFN-gamma-stimulated J774.2 macrophages
    • DOI 10.1099/mic.0.2006/003731-0
    • Gilberthorpe NJ, Lee ME, Stevanin TM, Read RC, and Poole RK. NsrR: A key regulator circumventing Salmonella enterica serovar Typhimurium oxidative and nitrosative stress in vitro and in IFN-gamma-stimulated J774. 2 macrophages. Microbiology 153: 1756-1771, 2007. (Pubitemid 46952506)
    • (2007) Microbiology , vol.153 , Issue.6 , pp. 1756-1771
    • Gilberthorpe, N.J.1    Lee, M.E.2    Stevanin, T.M.3    Read, R.C.4    Poole, R.K.5
  • 41
    • 45549109686 scopus 로고    scopus 로고
    • Nitric oxide homeostasis in Salmonella typhimurium. Roles of respiratory nitrate reductase and flavohemoglobin
    • Gilberthorpe NJ and Poole RK. Nitric oxide homeostasis in Salmonella typhimurium. Roles of respiratory nitrate reductase and flavohemoglobin. J Biol Chem 283: 11146-11154, 2008.
    • (2008) J Biol Chem , vol.283 , pp. 11146-11154
    • Gilberthorpe, N.J.1    Poole, R.K.2
  • 42
    • 0033972395 scopus 로고    scopus 로고
    • A peptide permease mutant of Mycobacterium bovis BCG resistant to the toxic peptides glutathione and S-nitrosoglutathione
    • DOI 10.1128/IAI.68.2.429-436.2000
    • Green RM, Seth A, and Connell ND. A peptide permease mutant of Mycobacterium bovis BCG resistant to the toxic peptides glutathione and S-nitrosoglutathione. Infect Immun 68: 429-436, 2000. (Pubitemid 30056490)
    • (2000) Infection and Immunity , vol.68 , Issue.2 , pp. 429-436
    • Green, R.M.1    Seth, A.2    Connell, N.D.3
  • 44
    • 70249096979 scopus 로고    scopus 로고
    • Endogenous nitric oxide protects bacteria against a wide spectrum of antibiotics
    • Gusarov I, Shatalin K, Starodubtseva M, and Nudler E. Endogenous nitric oxide protects bacteria against a wide spectrum of antibiotics. Science 325: 1380-1384, 2009.
    • (2009) Science , vol.325 , pp. 1380-1384
    • Gusarov, I.1    Shatalin, K.2    Starodubtseva, M.3    Nudler, E.4
  • 48
    • 0030572708 scopus 로고    scopus 로고
    • Nitrosative stress: Activation of the transcription factor OxyR
    • DOI 10.1016/S0092-8674(00)80147-6
    • Hausladen A, Privalle CT, Keng T, DeAngelo J, and Stamler JS. Nitrosative stress: Activation of the transcription factor OxyR. Cell 86: 719-729, 1996. (Pubitemid 26303441)
    • (1996) Cell , vol.86 , Issue.5 , pp. 719-729
    • Hausladen, A.1    Privalle, C.T.2    Keng, T.3    DeAngelo, J.4    Stamler, J.S.5
  • 49
    • 0030945376 scopus 로고    scopus 로고
    • S-nitrosoglutathione as a substrate for gamma-glutamyl transpeptidase
    • Hogg N, Singh RJ, Konorev E, Joseph J, and Kalyanaraman B. S-nitrosoglutathione as a substrate for gamma-glutamyl transpeptidase. Biochem J 323: 477-481, 1997.
    • (1997) Biochem J , vol.323 , pp. 477-481
    • Hogg, N.1    Singh, R.J.2    Konorev, E.3    Joseph, J.4    Kalyanaraman, B.5
  • 50
    • 0030296758 scopus 로고    scopus 로고
    • Seleno compounds and glutathione peroxidase catalyzed decomposition of S-nitrosothiols
    • DOI 10.1006/bbrc.1996.1620
    • Hou Y, Guo Z, Li J, and Wang PG. Seleno compounds and glutathione peroxidase catalyzed decomposition of Snitrosothiols. Biochem Biophys Res Commun 228: 88-93, 1996. (Pubitemid 26390634)
    • (1996) Biochemical and Biophysical Research Communications , vol.228 , Issue.1 , pp. 88-93
    • Hou, Y.1    Guo, Z.2    Li, J.3    Wang, P.G.4
  • 51
    • 26244433294 scopus 로고    scopus 로고
    • Transcriptional response of Candida albicans to nitric oxide and the role of the YHB1 gene in nitrosative stress and virulence
    • DOI 10.1091/mbc.E05-05-0435
    • Hromatka BS, Noble SM, and Johnson AD. Transcriptional response of Candida albicans to nitric oxide and the role of the YHB1 gene in nitrosative stress and virulence. Mol Biol Cell 16: 4814-4826, 2005. (Pubitemid 41416462)
    • (2005) Molecular Biology of the Cell , vol.16 , Issue.10 , pp. 4814-4826
    • Hromatka, B.S.1    Noble, S.M.2    Johnson, A.D.3
  • 52
    • 33746070773 scopus 로고    scopus 로고
    • An ascorbate-dependent artifact that interferes with the interpretation of the biotin switch assay
    • DOI 10.1016/j.freeradbiomed.2006.03.006, PII S0891584906001687
    • Huang B and Chen C. An ascorbate-dependent artifact that interferes with the interpretation of the biotin switch assay. Free Radic Biol Med 41: 562-567, 2006. (Pubitemid 44080503)
    • (2006) Free Radical Biology and Medicine , vol.41 , Issue.4 , pp. 562-567
    • Huang, B.1    Chen, C.2
  • 54
    • 0035849715 scopus 로고    scopus 로고
    • The biotin switch method for the detection of S-nitrosylated proteins
    • Jaffrey SR and Snyder SH. The biotin switch method for the detection of S-nitrosylated proteins. Sci STKE 2001: pl1, 2001.
    • (2001) Sci STKE 2001
    • Jaffrey, S.R.1    Snyder, S.H.2
  • 55
    • 41949119905 scopus 로고    scopus 로고
    • Determination of the Escherichia coli S-nitrosoglutathione response network using integrated biochemical and systems analysis
    • Jarboe LR, Hyduke DR, Tran LM, Chou KJY, and Liao JC. Determination of the Escherichia coli S-nitrosoglutathione response network using integrated biochemical and systems analysis. J Biol Chem 283: 5148-5157, 2008.
    • (2008) J Biol Chem , vol.283 , pp. 5148-5157
    • Jarboe, L.R.1    Hyduke, D.R.2    Tran, L.M.3    Kjy, C.4    Liao, J.C.5
  • 56
    • 0023687623 scopus 로고
    • Mechanism for nitrosation of 2, 3-diaminonaphthalene by Escherichia coli: Enzymatic production of NO followed by O2-dependent chemical nitrosation
    • Ji XB and Hollocher TC. Mechanism for nitrosation of 2, 3-diaminonaphthalene by Escherichia coli: Enzymatic production of NO followed by O2-dependent chemical nitrosation. Appl Environ Microbiol 54: 1791-1794, 1988.
    • (1988) Appl Environ Microbiol , vol.54 , pp. 1791-1794
    • Ji, X.B.1    Hollocher, T.C.2
  • 58
    • 84855211491 scopus 로고    scopus 로고
    • Inhibitory effect of sulphated polysaccharide porphyran on nitric oxide production in lipopolysaccharide-stimulated RAW264. 7 macrophages
    • Jiang Z, Hama Y, Yamaguchi K, and Oda T. Inhibitory effect of sulphated polysaccharide porphyran on nitric oxide production in lipopolysaccharide- stimulated RAW264. 7 macrophages. J Biochem 151: 65-74, 2012.
    • (2012) J Biochem , vol.151 , pp. 65-74
    • Jiang, Z.1    Hama, Y.2    Yamaguchi, K.3    Oda, T.4
  • 59
    • 33847350668 scopus 로고    scopus 로고
    • Nitric oxide promotes endothelial cell survival signaling through S-nitrosylation and activation of dynamin-2
    • DOI 10.1242/jcs.03361
    • Kang-Decker N, Cao S, Chatterjee S, Yao J, Egan LJ, Semela D, Mukhopadhyay D, and Shah V. Nitric oxide promotes endothelial cell survival signaling through S-nitrosylation and activation of dynamin-2. J Cell Sci 120: 492-501, 2007. (Pubitemid 46332512)
    • (2007) Journal of Cell Science , vol.120 , Issue.3 , pp. 492-501
    • Kang-Decker, N.1    Cao, S.2    Chatterjee, S.3    Yao, J.4    Egan, L.J.5    Semela, D.6    Mukhopadhyay, D.7    Shah, V.8
  • 60
    • 33847219039 scopus 로고    scopus 로고
    • Does S-methyl methanethiosulfonate trap the thiol-disulfide state of proteins?
    • Karala AR and Ruddock LW. Does S-methyl methanethiosulfonate trap the thiol-disulfide state of proteins? Antioxid Redox Signal 9: 527-531, 2007.
    • (2007) Antioxid Redox Signal , vol.9 , pp. 527-531
    • Karala, A.R.1    Ruddock, L.W.2
  • 62
    • 34548515549 scopus 로고    scopus 로고
    • Glutathione-dependent alcohol dehydrogenase AdhC is required for defense against nitrosative stress in Haemophilus influenzae
    • DOI 10.1128/IAI.00487-07
    • Kidd SP, Jiang D, Jennings MP, and McEwan AG. Glutathione-dependent alcohol dehydrogenase AdhC is required for defense against nitrosative stress in Haemophilus influenzae. Infect Immun 75: 4506-4513, 2007. (Pubitemid 47378110)
    • (2007) Infection and Immunity , vol.75 , Issue.9 , pp. 4506-4513
    • Kidd, S.P.1    Jiang, D.2    Jennings, M.P.3    McEwan, A.G.4
  • 65
    • 75149137411 scopus 로고    scopus 로고
    • Bacterial nitric oxide detoxification prevents host cell S-nitrosothiol formation: A novel mechanism of bacterial pathogenesis
    • Laver JR, Stevanin TM, Messenger SL, Lunn AD, Lee ME, Moir JW, Poole RK, and Read RC. Bacterial nitric oxide detoxification prevents host cell S-nitrosothiol formation: A novel mechanism of bacterial pathogenesis. FASEB J 24: 286-295, 2010.
    • (2010) FASEB J , vol.24 , pp. 286-295
    • Laver, J.R.1    Stevanin, T.M.2    Messenger, S.L.3    Lunn, A.D.4    Lee, M.E.5    Moir, J.W.6    Poole, R.K.7    Read, R.C.8
  • 66
    • 42949108214 scopus 로고    scopus 로고
    • Chemiluminescence quantification of NO and its derivatives in liquid samples
    • Laver JR, Stevanin TM, and Read RC. Chemiluminescence quantification of NO and its derivatives in liquid samples. Methods Enzymol 436: 113-127, 2008.
    • (2008) Methods Enzymol , vol.436 , pp. 113-127
    • Laver, J.R.1    Stevanin, T.M.2    Read, R.C.3
  • 68
    • 0035932413 scopus 로고    scopus 로고
    • A metabolic enzyme for S-nitrosothiol conserved from bacteria to humans
    • DOI 10.1038/35068596
    • Liu LM, Hausladen A, Zeng M, Que L, Heitman J, and Stamler JS. A metabolic enzyme for S-nitrosothiol conserved from bacteria to humans. Nature 410: 490-494, 2001. (Pubitemid 32240051)
    • (2001) Nature , vol.410 , Issue.6827 , pp. 490-494
    • Liu, L.1    Hausladen, A.2    Zeng, M.3    Que, L.4    Heitman, J.5    Stamler, J.S.6
  • 69
    • 34548502206 scopus 로고    scopus 로고
    • Structural and functional properties of a single domain hemoglobin from the food-borne pathogen Campylobactor jejuni
    • DOI 10.1074/jbc.M704415200
    • Lu C, Mukai M, Lin Y, Wu G, Poole RK, and Yeh S-R. Structural and functional properties of a single-domain hemoglobin from the food-borne pathogen Campylobacter jejuni. J Biol Chem 282: 25917-25928, 2007. (Pubitemid 47372797)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.35 , pp. 25917-25928
    • Lu, C.1    Mukai, M.2    Lin, Y.3    Wu, G.4    Poole, R.K.5    Yeh, S.-R.6
  • 70
    • 34249785140 scopus 로고    scopus 로고
    • Structural and functional properties of a truncated hemoglobin from a food-borne pathogen Campylobacter jejuni
    • DOI 10.1074/jbc.M609397200
    • Lu CY, Egawa T, Wainwright LM, Poole RK, and Yeh S-R. Structural and functional properties of a truncated hemoglobin from a food-borne pathogen Campylobacter jejuni. J Biol Chem 282: 13627-13636, 2007. (Pubitemid 47100515)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.18 , pp. 13627-13636
    • Lu, C.1    Egawa, T.2    Wainwright, L.M.3    Poole, R.K.4    Yeh, S.-R.5
  • 71
    • 34250738347 scopus 로고    scopus 로고
    • Signalling by NO-induced protein S-nitrosylation and S-glutathionylation: Convergences and divergences
    • DOI 10.1016/j.cardiores.2007.03.016, PII S0008636307001411
    • Martinez-Ruiz A and Lamas S. Signalling by NO-induced protein S-nitrosylation and S-glutathionylation: Convergences and divergences. Cardiovasc Res 75: 220-228, 2007. (Pubitemid 46970703)
    • (2007) Cardiovascular Research , vol.75 , Issue.2 , pp. 220-228
    • Martinez-Ruiz, A.1    Lamas, S.2
  • 72
    • 77954228805 scopus 로고    scopus 로고
    • Peroxynitrite toxicity in Escherichia coli K12 elicits expression of oxidative stress responses and protein nitration and nitrosylation
    • McLean S, Bowman LAH, Sanguinetti G, Read RC, and Poole RK. Peroxynitrite toxicity in Escherichia coli K12 elicits expression of oxidative stress responses and protein nitration and nitrosylation. J Biol Chem 285: 20724-20731, 2010.
    • (2010) J Biol Chem , vol.285 , pp. 20724-20731
    • McLean, S.1    Lah, B.2    Sanguinetti, G.3    Read, R.C.4    Poole, R.K.5
  • 73
    • 0031844664 scopus 로고    scopus 로고
    • A novel mechanism for upregulation of the Escherichia coil K-12 hmp (flavohaemoglobin) gene by the 'NO releaser', S-nitrosoglutathione: Nitrosation of homocysteine and modulation of MetR binding to the glyA-hmp intergenic region
    • DOI 10.1046/j.1365-2958.1998.01000.x
    • Membrillo-Hernandez J, Coopamah MD, Channa A, Hughes MN, and Poole RK. A novel mechanism for upregulation of the Escherichia coli K-12hmp (flavohaemoglobin) gene by the 'NO releaser', S-nitrosoglutathione: nitrosation of homocysteine and modulation of MetR binding to the glyA-hmp intergenic region. Mol Microbiol 29: 1101-1112, 1998. (Pubitemid 28389449)
    • (1998) Molecular Microbiology , vol.29 , Issue.4 , pp. 1101-1112
    • Membrillo-Hernandez, J.1    Coopamah, M.D.2    Channa, A.3    Hughes, M.N.4    Poole, R.K.5
  • 74
    • 0030846053 scopus 로고    scopus 로고
    • A reassessment of the genetic determinants, the effect of growth conditions and the availability of an electron donor on the nitrosating activity of Escherichia coli K-12
    • Metheringham R and Cole JA. A reassessment of the genetic determinants, the effect of growth conditions and the availability of an electron donor on the nitrosating activity of Escherichia coli K-12. Microbiology 143: 2647-2656, 1997. (Pubitemid 27389950)
    • (1997) Microbiology , vol.143 , Issue.8 , pp. 2647-2656
    • Metheringham, R.1    Cole, J.A.2
  • 75
    • 57649129414 scopus 로고    scopus 로고
    • Oxygen-and NssR-dependent globin expression and enhanced iron acquisition in the response of Campylobacter to nitrosative stress
    • Monk CE, Pearson BM, Mulholland F, Smith HK, and Poole RK. Oxygen-and NssR-dependent globin expression and enhanced iron acquisition in the response of Campylobacter to nitrosative stress. J Biol Chem 283: 28413-28425, 2008.
    • (2008) J Biol Chem , vol.283 , pp. 28413-28425
    • Monk, C.E.1    Pearson, B.M.2    Mulholland, F.3    Smith, H.K.4    Poole, R.K.5
  • 76
    • 0028953920 scopus 로고
    • Isolation and identification of a glutathione peroxidase homolog gene, gpxA, present in Neisseria meningitidis but absent in Neisseria gonorrhoeae
    • Moore TD and Sparling PF. Isolation and identification of a glutathione peroxidase homolog gene, gpxA, present in Neisseria meningitidis but absent in Neisseria gonorrhoeae. Infect Immun 63: 1603-1607, 1995.
    • (1995) Infect Immun , vol.63 , pp. 1603-1607
    • Moore, T.D.1    Sparling, P.F.2
  • 77
    • 0019868175 scopus 로고
    • Inhibition of Bacillus cereus spore outgrowth by covalent modification of a sulfhydryl group by nitrosothiol and iodoacetate
    • Morris SL and Hansen JN. Inhibition of bacillus-cereus spore outgrowth by covalent modification of a sulfhydryl-group by nitrosothiol and iodoacetate. J Bacteriol 148: 465-471, 1981. (Pubitemid 12218747)
    • (1981) Journal of Bacteriology , vol.148 , Issue.2 , pp. 465-471
    • Morris, S.L.1    Hansen, J.N.2
  • 79
    • 0029764601 scopus 로고    scopus 로고
    • S-nitrosoglutathione is cleaved by the thioredoxin system with liberation of glutathione and redox regulating nitric oxide
    • DOI 10.1074/jbc.271.32.19180
    • Nikitovic D and Holmgren A. S-nitrosoglutathione is cleaved by the thioredoxin system with liberation of glutathione and redox regulating nitric oxide. J Biol Chem 271: 19180-19185, 1996. (Pubitemid 26271582)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.32 , pp. 19180-19185
    • Nikitovic, D.1    Holmgren, A.2
  • 80
    • 0036049852 scopus 로고    scopus 로고
    • Nitric oxide scavenging and detoxification by the Mycobacterium tuberculosis haemoglobin, HbN in Escherichia coli
    • DOI 10.1046/j.1365-2958.2002.03095.x
    • Pathania R, Navani NK, Gardner AM, Gardner PR, and Dikshit KL. Nitric oxide scavenging and detoxification by the Mycobacterium tuberculosis haemoglobin, HbN in Escherichia coli. Mol Microbiol 45: 1303-1314, 2002. (Pubitemid 35015354)
    • (2002) Molecular Microbiology , vol.45 , Issue.5 , pp. 1303-1314
    • Pathania, R.1    Navani, N.K.2    Gardner, A.M.3    Gardner, P.R.4    Dikshit, K.L.5
  • 81
    • 0035252076 scopus 로고    scopus 로고
    • Export by red blood cells of nitric oxide bioactivity
    • DOI 10.1038/35054560
    • Pawloski JR, Hess DT, and Stamler JS. Export by red blood cells of nitric oxide bioactivity. Nature 409: 622-626, 2001. (Pubitemid 32154814)
    • (2001) Nature , vol.409 , Issue.6820 , pp. 622-626
    • Pawloski, J.R.1    Hes, D.T.2    Stamler, J.S.3
  • 82
    • 0024954192 scopus 로고
    • 2-Oxo acid dehydrogenase multienzyme complexes: domains, dynamics, and design
    • DOI 10.1111/j.1749-6632.1989.tb14983.x
    • Perham RN and Packman LC. 2-Oxo acid dehydrogenase multienzyme complexes: Domains, dynamics, and design. Ann NY Acad Sci 573: 1-20, 1989. (Pubitemid 20175641)
    • (1989) Annals of the New York Academy of Sciences , vol.573 , pp. 1-20
    • Perham, R.N.1    Packman, L.C.2
  • 83
    • 0014126240 scopus 로고
    • Alpha-keto acid dehydrogenase complexes. 8. Comparison of dihydrolipoyl dehydrogenases from pyruvate and alpha-ketoglutarate dehydrogenase complexes of Escherichia coli
    • Pettit FH and Reed LJ. Alpha-keto acid dehydrogenase complexes. 8. Comparison of dihydrolipoyl dehydrogenases from pyruvate and alpha-ketoglutarate dehydrogenase complexes of Escherichia coli. Proc Natl Acad Sci USA 58: 1126-1130, 1967.
    • (1967) Proc Natl Acad Sci USA , vol.58 , pp. 1126-1130
    • Pettit, F.H.1    Reed, L.J.2
  • 84
    • 0029086053 scopus 로고
    • Opsonic activities of surfactant proteins A and D in phagocytosis of gram-negative bacteria by alveolar macrophages
    • Pikaar JC, Voorhout WF, van Golde LM, Verhoef J, Van Strijp JA, and van Iwaarden JF. Opsonic activities of surfactant proteins A and D in phagocytosis of gram-negative bacteria by alveolar macrophages. J Infect Dis 172: 481-489, 1995.
    • (1995) J Infect Dis , vol.172 , pp. 481-489
    • Pikaar, J.C.1    Voorhout, W.F.2    Van Golde, L.M.3    Verhoef, J.4    Van Strijp, J.A.5    Van Iwaarden, J.F.6
  • 85
    • 0037189546 scopus 로고    scopus 로고
    • Respiratory detoxification of nitric oxide by the cytochrome c nitrite reductase of Escherichia coli
    • DOI 10.1074/jbc.M200731200
    • Poock SR, Leach ER, Moir JWB, Cole JA, and Richardson DJ. Respiratory detoxification of nitric oxide by the cytochrome c nitrite reductase of Escherichia coli. J Biol Chem 277: 23664-23669, 2002. (Pubitemid 34952205)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.26 , pp. 23664-23669
    • Poock, S.R.1    Leach, E.R.2    Moir, J.W.B.3    Cole, J.A.4    Richardson, D.J.5
  • 86
    • 14644387541 scopus 로고    scopus 로고
    • Nitric oxide and nitrosative stress tolerance in bacteria
    • DOI 10.1042/BST0330176
    • Poole RK. Nitric oxide and nitrosative stress tolerance in bacteria. Biochem Soc Trans 33: 176-180, 2005. (Pubitemid 40313794)
    • (2005) Biochemical Society Transactions , vol.33 , Issue.1 , pp. 176-180
    • Poole, R.K.1
  • 87
    • 0029831326 scopus 로고    scopus 로고
    • Nitric oxide, nitrite, and Fnr regulation of hmp (flavohemoglobin) gene expression in Escherichia coli K-12
    • Poole RK, Anjum MF, Membrillo-Hernández J, Kim SO, Hughes MN, and Stewart V. Nitric oxide, nitrite, and Fnr regulation of hmp (flavohemoglobin) gene expression in Escherichia coli K-12. J Bacteriol 178: 5487-5492, 1996. (Pubitemid 26304384)
    • (1996) Journal of Bacteriology , vol.178 , Issue.18 , pp. 5487-5492
    • Poole, R.K.1    Anjum, M.F.2    Membrillo-Hernandez, J.3    Kim, S.O.4    Hughes, M.N.5    Stewart, V.6
  • 88
    • 0034072208 scopus 로고    scopus 로고
    • New functions for the ancient globin family: Bacterial responses to nitric oxide and nitrosative stress
    • DOI 10.1046/j.1365-2958.2000.01889.x
    • Poole RK and Hughes MN. New functions for the ancient globin family: Bacterial responses to nitric oxide and nitrosative stress. Mol Microbiol 36: 775-783, 2000. (Pubitemid 30326524)
    • (2000) Molecular Microbiology , vol.36 , Issue.4 , pp. 775-783
    • Poole, R.K.1    Hughes, M.N.2
  • 89
    • 58849087683 scopus 로고    scopus 로고
    • Thioredoxin reductase is essential for protection of Neisseria gonorrhoeae against killing by nitric oxide and for bacterial growth during interaction with cervical epithelial cells
    • Potter AJ, Kidd SP, Edwards JL, Falsetta ML, Apicella MA, Jennings MP, and McEwan AG. Thioredoxin reductase is essential for protection of Neisseria gonorrhoeae against killing by nitric oxide and for bacterial growth during interaction with cervical epithelial cells. J Infect Dis 199: 227-235, 2009.
    • (2009) J Infect Dis , vol.199 , pp. 227-235
    • Potter, A.J.1    Kidd, S.P.2    Edwards, J.L.3    Falsetta, M.L.4    Apicella, M.A.5    Jennings, M.P.6    McEwan, A.G.7
  • 90
    • 33847741834 scopus 로고    scopus 로고
    • Evidence for distinctive mechanisms of S-nitrosoglutathione metabolism by AdhC in two closely related species, Neisseria gonorrhoeae and Neisseria meningitidis
    • DOI 10.1128/IAI.01634-06
    • Potter AJ, Kidd SP, Jennings MP, and McEwan AG. Evidence for distinctive mechanisms of S-nitrosoglutathione metabolism by AdhC in two closely related species, Neisseria gonorrhoeae and Neisseria meningitidis. Infect Immun 75: 1534-1536, 2007. (Pubitemid 46385850)
    • (2007) Infection and Immunity , vol.75 , Issue.3 , pp. 1534-1536
    • Potter, A.J.1    Kidd, S.P.2    Jennings, M.P.3    McEwan, A.G.4
  • 91
    • 33947420458 scopus 로고    scopus 로고
    • Nitric oxide in chemostat-cultured Escherichia coli is sensed by Fnr and other global regulators: Unaltered methionine biosynthesis indicates lack of S nitrosation
    • DOI 10.1128/JB.01354-06
    • Pullan ST, Gidley MD, Jones RA, Barrett J, Stevanin TA, Read RC, Green J, and Poole RK. Nitric oxide in chemostatcultured Escherichia coli is sensed by Fnr and other global regulators: Unaltered methionine biosynthesis indicates lack of S-nitrosation. J Bacteriol 189: 1845-1855, 2007. (Pubitemid 46446147)
    • (2007) Journal of Bacteriology , vol.189 , Issue.5 , pp. 1845-1855
    • Pullan, S.T.1    Gidley, M.D.2    Jones, R.A.3    Barrett, J.4    Stevanin, T.M.5    Read, R.C.6    Green, J.7    Poole, R.K.8
  • 92
    • 79955704725 scopus 로고    scopus 로고
    • Identification of S-nitrosylation of proteins of Helicobacter pylori in response to nitric oxide stress
    • Qu W, Zhou Y, Sun Y, Fang M, Yu H, Li W, Liu Z, Zeng J, Chen C, Gao C, and Jia J. Identification of S-nitrosylation of proteins of Helicobacter pylori in response to nitric oxide stress. J Microbiol 49: 251-256, 2011.
    • (2011) J Microbiol , vol.49 , pp. 251-256
    • Qu, W.1    Zhou, Y.2    Sun, Y.3    Fang, M.4    Yu, H.5    Li, W.6    Liu, Z.7    Zeng, J.8    Chen, C.9    Gao, C.10    Jia, J.11
  • 94
    • 0023742156 scopus 로고
    • Bacterial catalysis of nitrosation: Involvement of the nar operon of Escherichia coli
    • Ralt D, Wishnok JS, Fitts R, and Tannenbaum SR. Bacterial catalysis of nitrosation: Involvement of the nar operon of Escherichia coli. J Bacteriol 170: 359-364, 1988.
    • (1988) J Bacteriol , vol.170 , pp. 359-364
    • Ralt, D.1    Wishnok, J.S.2    Fitts, R.3    Tannenbaum, S.R.4
  • 96
    • 78751702376 scopus 로고    scopus 로고
    • Vesicle scission: Dynamin
    • Ramachandran R. Vesicle scission: Dynamin. Semin Cell Dev Biol 22: 10-17, 2011.
    • (2011) Semin Cell Dev Biol , vol.22 , pp. 10-17
    • Ramachandran, R.1
  • 99
    • 41149096672 scopus 로고    scopus 로고
    • A nitric oxide-inducible lactate dehydrogenase enables Saphylococcus aureus to resist innate immunity
    • DOI 10.1126/science.1155207
    • Richardson AR, Libby SJ, and Fang FC. A nitric oxideinducible lactate dehydrogenase enables Staphylococcus aureus to resist innate immunity. Science 319: 1672-1676, 2008. (Pubitemid 351432506)
    • (2008) Science , vol.319 , Issue.5870 , pp. 1672-1676
    • Richardson, A.R.1    Libby, S.J.2    Fang, F.C.3
  • 101
    • 34247893903 scopus 로고    scopus 로고
    • Mechanisms of adaptation to nitrosative stress in Bacillus subtilis
    • DOI 10.1128/JB.01782-06
    • Rogstam A, Larsson JT, Kjelgaard P, and von Wachenfeldt C. Mechanisms of adaptation to nitrosative stress in Bacillus subtilis. J Bacteriol 189: 3063-3071, 2007. (Pubitemid 46697395)
    • (2007) Journal of Bacteriology , vol.189 , Issue.8 , pp. 3063-3071
    • Rogstam, A.1    Larsson, J.T.2    Kjelgaard, P.3    Von Wachenfeldt, C.4
  • 102
  • 103
    • 34247183551 scopus 로고    scopus 로고
    • Enteric glia regulate intestinal barrier function and inflammation via release of s-nitrosoglutathione
    • DOI 10.1053/j.gastro.2007.01.051, PII S0016508507001904
    • Savidge TC, Newman P, Pothoulakis C, Ruhl A, Neunlist M, Bourreille A, Hurst R, and Sofroniew MV. Enteric glia regulate intestinal barrier function and inflammation via release of S-nitrosoglutathione. Gastroenterology 132: 1344-1358, 2007. (Pubitemid 46656255)
    • (2007) Gastroenterology , vol.132 , Issue.4 , pp. 1344-1358
    • Savidge, T.C.1    Newman, P.2    Pothoulakis, C.3    Ruhl, A.4    Neunlist, M.5    Bourreille, A.6    Hurst, R.7    Sofroniew, M.V.8
  • 105
    • 84860176878 scopus 로고    scopus 로고
    • Endogenous protein S-nitrosylation in E. coli: Regulation by OxyR
    • Seth D, Hausladen A, Wang Y, and Stamler JS. Endogenous protein S-nitrosylation in E. coli: Regulation by OxyR. Science 336: 470-473, 2012.
    • (2012) Science , vol.336 , pp. 470-473
    • Seth, D.1    Hausladen, A.2    Wang, Y.3    Stamler, J.S.4
  • 106
    • 0032984248 scopus 로고    scopus 로고
    • Phenotype of mice and macrophages deficient in both phagocyte oxidase and inducible nitric oxide synthase
    • DOI 10.1016/S1074-7613(00)80004-7
    • Shiloh MU, MacMicking JD, Nicholson S, Brause JE, Potter S, Marino M, Fang F, Dinauer M, and Nathan C. Phenotype of mice and macrophages deficient in both phagocyte oxidase and inducible nitric oxide synthase. Immunity 10: 29-38, 1999. (Pubitemid 29077381)
    • (1999) Immunity , vol.10 , Issue.1 , pp. 29-38
    • Shiloh, M.U.1    MacMicking, J.D.2    Nicholson, S.3    Brause, J.E.4    Potter, S.5    Marino, M.6    Fang, F.7    Dinauer, M.8    Nathan, C.9
  • 108
    • 33846892483 scopus 로고    scopus 로고
    • Regulators of bacterial responses to nitric oxide
    • DOI 10.1111/j.1574-6976.2006.00061.x
    • Spiro S. Regulators of bacterial responses to nitric oxide. FEMS Microbiol Rev 31: 193-211, 2007. (Pubitemid 46227144)
    • (2007) FEMS Microbiology Reviews , vol.31 , Issue.2 , pp. 193-211
    • Spiro, S.1
  • 109
    • 0036070723 scopus 로고    scopus 로고
    • Flavohemoglobin Hmp protects Salmonella enterica serovar typhimurium from nitric oxide-related killing by human macrophages
    • DOI 10.1128/IAI.70.8.4399-4405.2002
    • Stevanin TM, Poole RK, Demoncheaux EAG, and Read RC. Flavohemoglobin Hmp protects Salmonella enterica serovar Typhimurium from nitric oxide-related killing by human macrophages. Infect Immun 70: 4399-4405, 2002. (Pubitemid 34790950)
    • (2002) Infection and Immunity , vol.70 , Issue.8 , pp. 4399-4405
    • Stevanin, T.M.1    Poole, R.K.2    Demoncheaux, E.A.G.3    Read, R.C.4
  • 111
    • 39149119282 scopus 로고    scopus 로고
    • A pneumococcal MerR-like regulator and S-nitrosoglutathione reductase are required for systemic virulence
    • DOI 10.1086/523107
    • Stroeher UH, Kidd SP, Stafford SL, Jennings MP, Paton JC, and McEwan AG. A pneumococcal MerR-like regulator and S-nitrosoglutathione reductase are required for systemic virulence. J Infect Dis 196: 1820-1826, 2007. (Pubitemid 351411943)
    • (2007) Journal of Infectious Diseases , vol.196 , Issue.12 , pp. 1820-1826
    • Stroeher, U.H.1    Kidd, S.P.2    Stafford, S.L.3    Jennings, M.P.4    Paton, J.C.5    McEwan, A.G.6
  • 112
    • 65549146791 scopus 로고    scopus 로고
    • A novel nitroreductase of Staphylococcus aureus with Snitrosoglutathione reductase activity
    • Tavares AFN, Nobre LS, Melo AMP, and Saraiva LM. A novel nitroreductase of Staphylococcus aureus with Snitrosoglutathione reductase activity. J Bacteriol 191: 3403-3406, 2009.
    • (2009) J Bacteriol , vol.191 , pp. 3403-3406
    • Tavares, A.F.N.1    Nobre, L.S.2    Melo, A.M.P.3    Saraiva, L.M.4
  • 114
    • 0034679577 scopus 로고    scopus 로고
    • Antimicrobial actions of the NADPH phagocyte oxidase and inducible nitric oxide synthase in experimental salmonellosis. I. Effects on microbial killing by activated peritoneal macrophages in vitro
    • DOI 10.1084/jem.192.2.227
    • Vazquez-Torres A, Jones-Carson J, Mastroeni P, Ischiropoulos H, and Fang FC. Antimicrobial actions of the NADPH phagocyte oxidase and inducible nitric oxide synthase in experimental salmonellosis. I. Effects on microbial killing by activated peritoneal macrophages in vitro. J Exp Med 192: 227-236, 2000. (Pubitemid 30470305)
    • (2000) Journal of Experimental Medicine , vol.192 , Issue.2 , pp. 227-236
    • Vazquez-Torres, A.1    Jones-Carson, J.2    Mastroeni, P.3    Ischiropoulos, H.4    Fang, F.C.5
  • 116
    • 79958173727 scopus 로고    scopus 로고
    • The Moraxella catarrhalis nitric oxide reductase is essential for nitric oxide detoxification
    • Wang W, Kinkel T, Martens-Habbena W, Stahl DA, Fang FC, and Hansen EJ. The Moraxella catarrhalis nitric oxide reductase is essential for nitric oxide detoxification. J Bacteriol 193: 2804-2813, 2011.
    • (2011) J Bacteriol , vol.193 , pp. 2804-2813
    • Wang, W.1    Kinkel, T.2    Martens-Habbena, W.3    Stahl, D.A.4    Fang, F.C.5    Hansen, E.J.6
  • 117
    • 78651285263 scopus 로고    scopus 로고
    • Dynamin2-and endothelial nitric oxide synthase-regulated invasion of bladder epithelial cells by uropathogenic Escherichia coli
    • Wang Z, Humphrey C, Frilot N, Wang G, Nie Z, Moniri NH, and Daaka Y. Dynamin2-and endothelial nitric oxide synthase-regulated invasion of bladder epithelial cells by uropathogenic Escherichia coli. J Cell Biol 192: 101-110, 2011.
    • (2011) J Cell Biol , vol.192 , pp. 101-110
    • Wang, Z.1    Humphrey, C.2    Frilot, N.3    Wang, G.4    Nie, Z.5    Moniri, N.H.6    Daaka, Y.7
  • 119
    • 0017734449 scopus 로고
    • Distribution of xanthine oxidase and xanthine dehydrogenase specificity types among bacteria
    • Woolfolk CA and Downard JS. Distribution of xanthine oxidase and xanthine dehydrogenase specificity types among bacteria. J Bacteriol 130: 1175-1191, 1977. (Pubitemid 8124010)
    • (1977) Journal of Bacteriology , vol.130 , Issue.3 , pp. 1175-1191
    • Woolfolk, C.A.1    Downard, J.S.2
  • 123
    • 0032939206 scopus 로고    scopus 로고
    • Cell-surface protein disulfide isomerase catalyzes transnitrosation and regulates intracellular transfer of nitric oxide
    • Zai A, Rudd MA, Scribner AW, and Loscalzo J. Cell-surface protein disulfide isomerase catalyzes transnitrosation and regulates intracellular transfer of nitric oxide. J Clin Invest 103: 393-399, 1999. (Pubitemid 29069989)
    • (1999) Journal of Clinical Investigation , vol.103 , Issue.3 , pp. 393-399
    • Zai, A.1    Rudd, M.A.2    Scribner, A.W.3    Loscalzo, J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.