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Volumn 12, Issue , 2012, Pages

A glutathione-based system for defense against carbonyl stress in Haemophilus influenzae

Author keywords

H. influenzae; Reactive aldehydes; Stress response

Indexed keywords

ALDEHYDE; BACTERIAL ENZYME; CARBON; CARBONYL DERIVATIVE; ELECTROPHILE; FORMALDEHYDE; GLUCOSE; S NITROSOGLUTATHIONE;

EID: 84864334279     PISSN: None     EISSN: 14712180     Source Type: Journal    
DOI: 10.1186/1471-2180-12-159     Document Type: Article
Times cited : (8)

References (22)
  • 2
    • 0037369926 scopus 로고    scopus 로고
    • Exogenous glutathione completes the defense against oxidative stress in Haemophilus influenzae
    • DOI 10.1128/JB.185.5.1572-1581.2003
    • Exogenous glutathione completes the defense against oxidative stress in Haemophilus influenzae. Vergauwen B, Pauwels F, Vaneechoutte M, Van Beeumen JJ, J Bact 2003 185 1572 1581 10.1128/JB.185.5.1572-1581.2003 12591874 (Pubitemid 36245959)
    • (2003) Journal of Bacteriology , vol.185 , Issue.5 , pp. 1572-1581
    • Vergauwen, B.1    Pauwels, F.2    Vaneechoutte, M.3    Van Beeumen, J.J.4
  • 3
    • 0042838106 scopus 로고    scopus 로고
    • Glutathione and catalase provide overlapping defenses for protection against respiration-generated hydrogen peroxide in Haemophilus influenzae
    • DOI 10.1128/JB.185.18.5555-5562.2003
    • Glutathione and catalase provide overlapping defenses for protection against repiration generated hydrogen peroxide in Haemophilus influenzae. Vergauwen B, Pauwels F, Van Beeumen JJ, J Bact 2003 185 5555 5562 10.1128/JB.185.18.5555-5562.2003 12949108 (Pubitemid 37082412)
    • (2003) Journal of Bacteriology , vol.185 , Issue.18 , pp. 5555-5562
    • Vergauwen, B.1    Pauwels, F.2    Van Beeumen, J.J.3
  • 4
    • 0032512416 scopus 로고    scopus 로고
    • Function of a glutathione-dependent formaldehyde dehydrogenase in Rhodobacter sphaeroides formaldehyde oxidation and assimilation
    • DOI 10.1021/bi971463t
    • Function of a glutathione-dependent formaldehyde dehydrogenase in Rhodobacter sphaeroides formaldehyde oxidation and assimilation. Barber RD, Donohue TJ, Biochem 1998 37 530 537 10.1021/bi971463t (Pubitemid 28123784)
    • (1998) Biochemistry , vol.37 , Issue.2 , pp. 530-537
    • Barber, R.D.1    Donohue, T.J.2
  • 5
    • 0036135679 scopus 로고    scopus 로고
    • Link between the membrane-bound pyridine nucleotide transhydrogenase and glutathione-dependent processes in Rhodobacter sphaeroides
    • DOI 10.1128/JB.184.2.400-409.2002
    • Link between the membrane bound pyridine nucleotide transhydrogenase and glutathione-dependent processes in Rhodobacter sphaeriodes. Hickman JW, Barber RD, Skaar EP, Donohue TJ, J Bact 2002 184 400 409 10.1128/JB.184.2.400-409.2002 11751816 (Pubitemid 34027379)
    • (2002) Journal of Bacteriology , vol.184 , Issue.2 , pp. 400-409
    • Hickman, J.W.1    Barber, R.D.2    Skaar, E.P.3    Donohue, T.J.4
  • 6
    • 9244244738 scopus 로고    scopus 로고
    • Positive and negative transcriptional regulators of glutathione-dependent formaldehyde metabolism
    • DOI 10.1128/JB.186.23.7914-7925.2004
    • Positive and negative transcriptional regulators of glutathione-dependent formaldehyde metabolism. Hickman JW, Witthuhn VC Jr, Dominguez M, Donohue TJ, J Bact 2004 186 7914 7925 10.1128/JB.186.23.7914-7925.2004 15547263 (Pubitemid 39552502)
    • (2004) Journal of Bacteriology , vol.186 , Issue.23 , pp. 7914-7925
    • Hickman, J.W.1    Witthuhn Jr., V.C.2    Dominguez, M.3    Donohue, T.J.4
  • 7
    • 58149141583 scopus 로고    scopus 로고
    • Medium- and short-chain dehydrogenase/reductase gene and protein families
    • 10.1007/s00018-008-8592-2 19011746
    • Medium- and short-chain dehydrogenase/reductase gene and protein families. Staab C, Hellgren M, Höög JO, Cell Mol Life Sci 2008 65 3950 3960 10.1007/s00018-008-8592-2 19011746
    • (2008) Cell Mol Life Sci , vol.65 , pp. 3950-3960
    • Staab, C.1    Hellgren, M.2    Höög, J.O.3
  • 9
    • 37549054690 scopus 로고    scopus 로고
    • Mechanistic considerations for formaldehyde-induced bronchoconstriction involving S-nitrosoglutathione reductase
    • Mechanistic considerations for formaldehyde-induced bronchoconstriction involving S-nitrosoglutathione reductase. Thompson CM, Grafstroum RC, J Tox Environl Health, Part A 2008 71 244 248
    • (2008) J Tox Environl Health, Part A , vol.71 , pp. 244-248
    • Thompson, C.M.1    Grafstroum, R.C.2
  • 10
    • 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
    • A glutathione-dependent Alcohol Dehydrogenase (AdhC) is required for defense against nitrosative stress in Haemophilus influenzae. Kidd SP, Jiang D, Jennings MP, McEwan AG, Infect Immun 2007 75 4506 4513 10.1128/IAI.00487-07 17591795 (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
  • 11
    • 0030854261 scopus 로고    scopus 로고
    • Human neutrophils employ the myeloperoxidase-hydrogen peroxide-chloride system to convert hydroxy-amino acids into glycolaldehyde, 2-hydroxypropanal, and acrolein: A mechanism for the generation of highly reactive α-hydroxy and α,β-unsaturated aldehydes by phagocytes at sites of inflammation
    • Human neutrophils employ the myeloperoxidase-hydrogen peroxide-chloride system to convert hydroxy-amino acids into glycolaldehyde, 2-hydroxypropanal, and acrolein. A mechanism for the generation of highly reactive alpha-hydroxy and alpha,beta-unsaturated aldehydes by phagocytes at sites of inflammation. Anderson MM, Hazen SL, Hsu FF, Heinecke JW, J Clin Invest 1997 99 424 432 10.1172/JCI119176 9022075 (Pubitemid 27414799)
    • (1997) Journal of Clinical Investigation , vol.99 , Issue.3 , pp. 424-432
    • Anderson, M.M.1    Hazen, S.L.2    Hsu, F.F.3    Heinecke, J.W.4
  • 12
    • 0034634553 scopus 로고    scopus 로고
    • The role of alpha, beta-dicarbonyl compounds in the toxicity of short chain sugars
    • 10.1074/jbc.M005536200 10931845
    • The role of alpha, beta-dicarbonyl compounds in the toxicity of short chain sugars. Okado-Matsumoto A, Fridovich I, J Biol Chem 2000 275 34853 34857 10.1074/jbc.M005536200 10931845
    • (2000) J Biol Chem , vol.275 , pp. 34853-34857
    • Okado-Matsumoto, A.1    Fridovich, I.2
  • 13
    • 0041919182 scopus 로고    scopus 로고
    • Chemically defined media for growth of Haemophilus influenzae strains
    • DOI 10.1128/JCM.41.9.4408-4410.2003
    • Chemically defined media for growth of Haemophilus influenzae strains. Coleman HN, Daines DA, Jarisch J, Smith AL, J Clin Micro 2003 41 4408 4410 10.1128/JCM.41.9.4408-4410.2003 (Pubitemid 37099716)
    • (2003) Journal of Clinical Microbiology , vol.41 , Issue.9 , pp. 4408-4410
    • Coleman, H.N.1    Daines, D.A.2    Jarisch, J.3    Smith, A.L.4
  • 14
    • 0038192048 scopus 로고    scopus 로고
    • Regulation of expression of the cyanide-insensitive terminal oxidase in Pseudomonas aeruginosa
    • DOI 10.1099/mic.0.26017-0
    • Regulation of expression of the cyanide-insensitive terminal oxidase in Pseudomonas aeruginosa. Cooper M, Tavankar GR, Williams HD, Microbiol 2003 149 5 1275 1284 10.1099/mic.0.26017-0 (Pubitemid 36626176)
    • (2003) Microbiology , vol.149 , Issue.5 , pp. 1275-1284
    • Cooper, M.1    Tavankar, G.R.2    Williams, H.D.3
  • 16
    • 0030823068 scopus 로고    scopus 로고
    • Induction of glutathione-dependent formaldehyde dehydrogenase activity in Escherichia coli and Hemophilus influenza
    • Induction of glutathione-dependent formaldehyde dehydrogenase activity in Escherichia coli and Haemophilus influenzae. Gutheil WG, Kasimoglu E, Nicholson PC, Biochem Biophysl Res Comm 1997 238 693 696 10.1016/S0006-291X(00)90000-7 (Pubitemid 27472635)
    • (1997) Biochemical and Biophysical Research Communications , vol.238 , Issue.3 , pp. 693-696
    • Gutheil, W.G.1    Kasimoglu, E.2    Nicholson, P.C.3
  • 17
    • 0032694683 scopus 로고    scopus 로고
    • The myeloperoxidase system of human phagocytes generates N(ε)- (carboxymethyl)lysine on proteins: A mechanism for producing advanced glycation end products at sites of inflammation
    • The myeloperoxidase system of human phagocytes generates N-(carboxymethyl)lysine on proteins: a mechanism for producing advanced glycation end products at sites of inflammation. Anderson MM, Requena JR, Crowley JR, Thorpe SR, Heinecke JW, J Clin Invest 1999 104 103 113 10.1172/JCI3042 10393704 (Pubitemid 29534350)
    • (1999) Journal of Clinical Investigation , vol.104 , Issue.1 , pp. 103-113
    • Anderson, M.M.1    Requena, J.R.2    Crowley, J.R.3    Thorpe, S.R.4    Heinecke, J.W.5
  • 18
    • 0033580813 scopus 로고    scopus 로고
    • Systems properties of the Haemophilus influenzae Rd metabolic genotype
    • DOI 10.1074/jbc.274.25.17410
    • Systems Properties of the Haemophilus influenzae Rd Metabolic Genotype. Edwards JS, Palsson BO, J Biol Chem 1999 274 17410 17416 10.1074/jbc.274.25. 17410 10364169 (Pubitemid 29283246)
    • (1999) Journal of Biological Chemistry , vol.274 , Issue.25 , pp. 17410-17416
    • Edwards, J.S.1    Palsson, B.O.2
  • 20
    • 60349101109 scopus 로고    scopus 로고
    • Genome-wide responses to carbonyl electrophiles in Bacillus subtilis: Control of the thiol-dependent formaldehyde dehydrogenase AdhA and cysteine proteinase YraA by the MerR-family regulator YraB (AdhR)
    • 10.1111/j.1365-2958.2008.06568.x
    • Genome-wide responses to carbonyl electrophiles in Bacillus subtilis: control of the thiol-dependent formaldehyde dehydrogenase AdhA and cysteine proteinase YraA by the MerR-family regulator YraB (AdhR). Huyen NTT, Eiamphungporn W, Mader U, Liebeke M, Lalk M, Hecker M, Helmann JD, Antelmann H, Mol Micro 2009 71 876 894 10.1111/j.1365-2958.2008.06568.x
    • (2009) Mol Micro , vol.71 , pp. 876-894
    • Huyen, N.T.T.1    Eiamphungporn, W.2    Mader, U.3    Liebeke, M.4    Lalk, M.5    Hecker, M.6    Helmann, J.D.7    Antelmann, H.8
  • 21
    • 39149119282 scopus 로고    scopus 로고
    • A pneumococcal MerR-like regulator and S-nitrosoglutathione reductase are required for systemic virulence
    • DOI 10.1086/523107
    • A pneumococcal MerR-like regulator and S-nitrosoglutathione reductase are required for systemic virulence. Stroeher UH, Kidd SP, Stafford SL, Jennings MP, Paton JC, McEwan AG, J Infect Dis 2007 196 1820 1826 10.1086/523107 18190263 (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
  • 22
    • 25144450560 scopus 로고    scopus 로고
    • NmIR of Neisseria gonorrhoeae: A novel redox responsive transcription factor from the MerR family
    • DOI 10.1111/j.1365-2958.2005.04773.x
    • NmlR of Neisseria gonorrhoeae: a novel redox responsive transcription factor from the MerR family. Kidd SP, Potter AJ, Apicella MA, Jennings MP, McEwan AG, Mol Micro 2005 57 1676 1689 10.1111/j.1365-2958.2005.04773.x (Pubitemid 41337395)
    • (2005) Molecular Microbiology , vol.57 , Issue.6 , pp. 1676-1689
    • Kidd, S.P.1    Potter, A.J.2    Apicella, M.A.3    Jennings, M.P.4    McEwan, A.G.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.