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Volumn 54, Issue 21, 2015, Pages 3235-3249

Cysteine sulfur chemistry in transcriptional regulators at the host-bacterial pathogen interface

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIA; CHEMICAL BONDS; COVALENT BONDS; CYTOLOGY; DETOXIFICATION; MOBILE SECURITY; MOLECULES; PATHOGENS; SULFUR; TRANSCRIPTION;

EID: 84930661260     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/acs.biochem.5b00085     Document Type: Article
Times cited : (19)

References (191)
  • 1
    • 0026698060 scopus 로고
    • Oxidized redox state of glutathione in the endoplasmic-reticulum
    • Hwang, C., Sinskey, A. J., and Lodish, H. F. (1992) Oxidized redox state of glutathione in the endoplasmic-reticulum Science 257, 1496-1502
    • (1992) Science , vol.257 , pp. 1496-1502
    • Hwang, C.1    Sinskey, A.J.2    Lodish, H.F.3
  • 3
    • 84930667997 scopus 로고    scopus 로고
    • Chemical probes for molecular imaging and detection of hydrogen sulfide and reactive sulfur species in biological systems
    • Lin, V. S., Chen, W., Xian, M., and Chang, C. J. (2015) Chemical probes for molecular imaging and detection of hydrogen sulfide and reactive sulfur species in biological systems Chem. Soc. Rev. DOI: 10.1039/C4CS00298A
    • (2015) Chem. Soc. Rev.
    • Lin, V.S.1    Chen, W.2    Xian, M.3    Chang, C.J.4
  • 4
    • 84879422944 scopus 로고    scopus 로고
    • The molecular mechanisms and physiological consequences of oxidative stress: Lessons from a model bacterium
    • Imlay, J. A. (2013) The molecular mechanisms and physiological consequences of oxidative stress: Lessons from a model bacterium Nat. Rev. Microbiol. 11, 443-454
    • (2013) Nat. Rev. Microbiol. , vol.11 , pp. 443-454
    • Imlay, J.A.1
  • 5
    • 84884528066 scopus 로고    scopus 로고
    • Bacterial responses to reactive chlorine species
    • Gray, M. J., Wholey, W.-Y., and Jakob, U. (2013) Bacterial responses to reactive chlorine species Annu. Rev. Microbiol. 67, 141-160
    • (2013) Annu. Rev. Microbiol. , vol.67 , pp. 141-160
    • Gray, M.J.1    Wholey, W.-Y.2    Jakob, U.3
  • 6
    • 84861321238 scopus 로고    scopus 로고
    • Connecting the chemical and biological properties of nitric oxide
    • Toledo, J. C. and Augusto, O. (2012) Connecting the chemical and biological properties of nitric oxide Chem. Res. Toxicol. 25, 975-989
    • (2012) Chem. Res. Toxicol. , vol.25 , pp. 975-989
    • Toledo, J.C.1    Augusto, O.2
  • 7
    • 64649087275 scopus 로고    scopus 로고
    • Phagocytic leukocytes and reactive oxygen species
    • Robinson, J. (2009) Phagocytic leukocytes and reactive oxygen species Histochem. Cell Biol. 131, 465-469
    • (2009) Histochem. Cell Biol. , vol.131 , pp. 465-469
    • Robinson, J.1
  • 11
    • 33645037891 scopus 로고    scopus 로고
    • The PerR transcription factor senses H2O2 by metal-catalysed histidine oxidation
    • Lee, J. W. and Helmann, J. D. (2006) The PerR transcription factor senses H2O2 by metal-catalysed histidine oxidation Nature 440, 363-367
    • (2006) Nature , vol.440 , pp. 363-367
    • Lee, J.W.1    Helmann, J.D.2
  • 12
    • 0038352097 scopus 로고    scopus 로고
    • The role of Fe-S proteins in sensing and regulation in bacteria
    • Kiley, P. J. and Beinert, H. (2003) The role of Fe-S proteins in sensing and regulation in bacteria Curr. Opin. Microbiol. 6, 181-185
    • (2003) Curr. Opin. Microbiol. , vol.6 , pp. 181-185
    • Kiley, P.J.1    Beinert, H.2
  • 13
    • 41949137280 scopus 로고    scopus 로고
    • Crystal structure of the [2Fe-2S] oxidative-stress sensor SoxR bound to DNA
    • Watanabe, S., Kita, A., Kobayashi, K., and Miki, K. (2008) Crystal structure of the [2Fe-2S] oxidative-stress sensor SoxR bound to DNA Proc. Natl. Acad. Sci. U.S.A. 105, 4121-4126
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 4121-4126
    • Watanabe, S.1    Kita, A.2    Kobayashi, K.3    Miki, K.4
  • 14
    • 84897113579 scopus 로고    scopus 로고
    • Insights into redox sensing metalloproteins in Mycobacterium tuberculosis
    • Chim, N., Johnson, P. M., and Goulding, C. W. (2014) Insights into redox sensing metalloproteins in Mycobacterium tuberculosis J. Inorg. Biochem. 133, 118-126
    • (2014) J. Inorg. Biochem. , vol.133 , pp. 118-126
    • Chim, N.1    Johnson, P.M.2    Goulding, C.W.3
  • 15
    • 0141737064 scopus 로고    scopus 로고
    • A novel sensor of NADH/NAD+ redox poise in Streptomyces coelicolor A32
    • Brekasis, D. and Paget, M. S. (2003) A novel sensor of NADH/NAD+ redox poise in Streptomyces coelicolor A32 EMBO J. 22, 4856-4865
    • (2003) EMBO J. , vol.22 , pp. 4856-4865
    • Brekasis, D.1    Paget, M.S.2
  • 16
    • 84876088340 scopus 로고    scopus 로고
    • A rex family transcriptional repressor influences H2O2 accumulation by Enterococcus faecalis
    • Vesić, D. and Kristich, C. J. (2013) A rex family transcriptional repressor influences H2O2 accumulation by Enterococcus faecalis J. Bacteriol. 195, 1815-1824
    • (2013) J. Bacteriol. , vol.195 , pp. 1815-1824
    • Vesić, D.1    Kristich, C.J.2
  • 18
    • 84902287070 scopus 로고    scopus 로고
    • The physiological role of reversible methionine oxidation
    • Drazic, A. and Winter, J. (2014) The physiological role of reversible methionine oxidation Biochim. Biophys. Acta 1844, 1367-1382
    • (2014) Biochim. Biophys. Acta , vol.1844 , pp. 1367-1382
    • Drazic, A.1    Winter, J.2
  • 20
    • 79951906200 scopus 로고    scopus 로고
    • Thiol-based redox switches and gene regulation
    • Antelmann, H. and Helmann, J. D. (2010) Thiol-based redox switches and gene regulation Antioxid. Redox Signaling 14, 1049-1063
    • (2010) Antioxid. Redox Signaling , vol.14 , pp. 1049-1063
    • Antelmann, H.1    Helmann, J.D.2
  • 21
    • 27144496052 scopus 로고    scopus 로고
    • A mycothiol synthase mutant of Mycobacterium smegmatis produces novel thiols and has an altered thiol redox status
    • Newton, G. L., Ta, P., and Fahey, R. C. (2005) A mycothiol synthase mutant of Mycobacterium smegmatis produces novel thiols and has an altered thiol redox status J. Bacteriol. 187, 7309-7316
    • (2005) J. Bacteriol. , vol.187 , pp. 7309-7316
    • Newton, G.L.1    Ta, P.2    Fahey, R.C.3
  • 23
    • 84869105723 scopus 로고    scopus 로고
    • Streptococcus pneumoniae uses glutathione to defend against oxidative stress and metal ion toxicity
    • Potter, A. J., Trappetti, C., and Paton, J. C. (2012) Streptococcus pneumoniae uses glutathione to defend against oxidative stress and metal ion toxicity J. Bacteriol. 194, 6248-6254
    • (2012) J. Bacteriol. , vol.194 , pp. 6248-6254
    • Potter, A.J.1    Trappetti, C.2    Paton, J.C.3
  • 24
    • 84889569252 scopus 로고    scopus 로고
    • Biophysical features of bacillithiol, the glutathione surrogate of Bacillus subtilis and other firmicutes
    • Sharma, S. V., Arbach, M., Roberts, A. A., Macdonald, C. J., Groom, M., and Hamilton, C. J. (2013) Biophysical features of bacillithiol, the glutathione surrogate of Bacillus subtilis and other firmicutes ChemBioChem 14, 2160-2168
    • (2013) ChemBioChem , vol.14 , pp. 2160-2168
    • Sharma, S.V.1    Arbach, M.2    Roberts, A.A.3    MacDonald, C.J.4    Groom, M.5    Hamilton, C.J.6
  • 27
    • 84903572069 scopus 로고    scopus 로고
    • Redox regulation in Bacillus subtilis: The bacilliredoxins BrxA(YphP) and BrxB(YqiW) function in de-bacillithiolation of S -bacillithiolated OhrR and MetE
    • Gaballa, A., Chi, B. K., Roberts, A. A., Becher, D., Hamilton, C. J., Antelmann, H., and Helmann, J. D. (2014) Redox regulation in Bacillus subtilis: The bacilliredoxins BrxA(YphP) and BrxB(YqiW) function in de-bacillithiolation of S -bacillithiolated OhrR and MetE Antioxid. Redox Signaling 21, 357-367
    • (2014) Antioxid. Redox Signaling , vol.21 , pp. 357-367
    • Gaballa, A.1    Chi, B.K.2    Roberts, A.A.3    Becher, D.4    Hamilton, C.J.5    Antelmann, H.6    Helmann, J.D.7
  • 28
    • 0032489438 scopus 로고    scopus 로고
    • Coenzyme A disulfide reductase, the primary low molecular weight disulfide reductase from Staphylococcus aureus: Purification and characterization of the native enzyme
    • delCardayré, S. B., Stock, K. P., Newton, G. L., Fahey, R. C., and Davies, J. E. (1998) Coenzyme A disulfide reductase, the primary low molecular weight disulfide reductase from Staphylococcus aureus: Purification and characterization of the native enzyme J. Biol. Chem. 273, 5744-5751
    • (1998) J. Biol. Chem. , vol.273 , pp. 5744-5751
    • Delcardayré, S.B.1    Stock, K.P.2    Newton, G.L.3    Fahey, R.C.4    Davies, J.E.5
  • 29
    • 33645895565 scopus 로고    scopus 로고
    • Diamide stress induces a metallothionein BmtA through a repressor BxmR and is modulated by Zn-inducible BmtA in the cyanobacterium Oscillatoria brevis
    • Hirose, K., Ezaki, B., Liu, T., and Nakashima, S. (2006) Diamide stress induces a metallothionein BmtA through a repressor BxmR and is modulated by Zn-inducible BmtA in the cyanobacterium Oscillatoria brevis Toxicol. Lett. 163, 250-256
    • (2006) Toxicol. Lett. , vol.163 , pp. 250-256
    • Hirose, K.1    Ezaki, B.2    Liu, T.3    Nakashima, S.4
  • 32
    • 70849126660 scopus 로고    scopus 로고
    • Solution structure of a paradigm ArsR family zinc sensor in the DNA-bound state
    • Arunkumar, A. I., Campanello, G. C., and Giedroc, D. P. (2009) Solution structure of a paradigm ArsR family zinc sensor in the DNA-bound state Proc. Natl. Acad. Sci. U.S.A. 106, 18177-18182
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 18177-18182
    • Arunkumar, A.I.1    Campanello, G.C.2    Giedroc, D.P.3
  • 33
    • 84907829274 scopus 로고    scopus 로고
    • Metal preferences and metallation
    • Foster, A. W., Osman, D., and Robinson, N. J. (2014) Metal preferences and metallation J. Biol. Chem. 289, 28095-28103
    • (2014) J. Biol. Chem. , vol.289 , pp. 28095-28103
    • Foster, A.W.1    Osman, D.2    Robinson, N.J.3
  • 34
    • 78649529306 scopus 로고    scopus 로고
    • Cysteine function governs its conservation and degeneration and restricts Its utilization on protein surfaces
    • Marino, S. M. and Gladyshev, V. N. (2010) Cysteine function governs its conservation and degeneration and restricts Its utilization on protein surfaces J. Mol. Biol. 404, 902-916
    • (2010) J. Mol. Biol. , vol.404 , pp. 902-916
    • Marino, S.M.1    Gladyshev, V.N.2
  • 35
    • 84856834259 scopus 로고    scopus 로고
    • Analysis and functional prediction of reactive cysteine residues
    • Marino, S. M. and Gladyshev, V. N. (2012) Analysis and functional prediction of reactive cysteine residues J. Biol. Chem. 287, 4419-4425
    • (2012) J. Biol. Chem. , vol.287 , pp. 4419-4425
    • Marino, S.M.1    Gladyshev, V.N.2
  • 36
    • 38649084667 scopus 로고    scopus 로고
    • Functional site profiling and electrostatic analysis of cysteines modifiable to cysteine sulfenic acid
    • Salsbury, F. R., Knutson, S. T., Poole, L. B., and Fetrow, J. S. (2008) Functional site profiling and electrostatic analysis of cysteines modifiable to cysteine sulfenic acid Protein Sci. 17, 299-312
    • (2008) Protein Sci. , vol.17 , pp. 299-312
    • Salsbury, F.R.1    Knutson, S.T.2    Poole, L.B.3    Fetrow, J.S.4
  • 37
    • 84868206533 scopus 로고    scopus 로고
    • Understanding the p K a of redox cysteines: The key role of hydrogen bonding
    • Roos, G., Foloppe, N., and Messens, J. (2012) Understanding the p K a of redox cysteines: The key role of hydrogen bonding Antioxid. Redox Signaling 18, 94-127
    • (2012) Antioxid. Redox Signaling , vol.18 , pp. 94-127
    • Roos, G.1    Foloppe, N.2    Messens, J.3
  • 38
    • 0032865515 scopus 로고    scopus 로고
    • Reactivity of biologically important thiol compounds with superoxide and hydrogen peroxide
    • Winterbourn, C. C. and Metodiewa, D. (1999) Reactivity of biologically important thiol compounds with superoxide and hydrogen peroxide Free Radical Biol. Med. 27, 322-328
    • (1999) Free Radical Biol. Med. , vol.27 , pp. 322-328
    • Winterbourn, C.C.1    Metodiewa, D.2
  • 40
    • 57549095616 scopus 로고    scopus 로고
    • Expanding the functional diversity of proteins through cysteine oxidation
    • Reddie, K. G. and Carroll, K. S. (2008) Expanding the functional diversity of proteins through cysteine oxidation Curr. Opin. Chem. Biol. 12, 746-754
    • (2008) Curr. Opin. Chem. Biol. , vol.12 , pp. 746-754
    • Reddie, K.G.1    Carroll, K.S.2
  • 41
    • 79551676040 scopus 로고    scopus 로고
    • Quantification of protein sulfenic acid modifications using isotope-coded dimedone and iododimedone
    • Seo, Y. H. and Carroll, K. S. (2011) Quantification of protein sulfenic acid modifications using isotope-coded dimedone and iododimedone Angew. Chem., Int. Ed. 50, 1342-1345
    • (2011) Angew. Chem., Int. Ed. , vol.50 , pp. 1342-1345
    • Seo, Y.H.1    Carroll, K.S.2
  • 42
    • 84886883539 scopus 로고    scopus 로고
    • In situ visualization and detection of protein sulfenylation responses in living cells through a dimedone-based fluorescent probe
    • Yin, Q., Huang, C., Zhang, C., Zhu, W., Xu, Y., Qian, X., and Yang, Y. (2013) In situ visualization and detection of protein sulfenylation responses in living cells through a dimedone-based fluorescent probe Org. Biomol. Chem. 11, 7566-7573
    • (2013) Org. Biomol. Chem. , vol.11 , pp. 7566-7573
    • Yin, Q.1    Huang, C.2    Zhang, C.3    Zhu, W.4    Xu, Y.5    Qian, X.6    Yang, Y.7
  • 43
    • 69949138465 scopus 로고    scopus 로고
    • Crystal structures of the reduced, sulfenic acid, and mixed disulfide forms of SarZ, a redox active global regulator in Staphylococcus aureus
    • Poor, C. B., Chen, P. R., Duguid, E., Rice, P. A., and He, C. (2009) Crystal structures of the reduced, sulfenic acid, and mixed disulfide forms of SarZ, a redox active global regulator in Staphylococcus aureus J. Biol. Chem. 284, 23517-23524
    • (2009) J. Biol. Chem. , vol.284 , pp. 23517-23524
    • Poor, C.B.1    Chen, P.R.2    Duguid, E.3    Rice, P.A.4    He, C.5
  • 44
    • 84873060569 scopus 로고    scopus 로고
    • Low-molecular-weight thiol-dependent antioxidant and antinitrosative defences in Salmonella pathogenesis
    • Song, M., Husain, M., Jones-Carson, J., Liu, L., Henard, C. A., and Vázquez-Torres, A. (2013) Low-molecular-weight thiol-dependent antioxidant and antinitrosative defences in Salmonella pathogenesis Mol. Microbiol. 87, 609-622
    • (2013) Mol. Microbiol. , vol.87 , pp. 609-622
    • Song, M.1    Husain, M.2    Jones-Carson, J.3    Liu, L.4    Henard, C.A.5    Vázquez-Torres, A.6
  • 45
    • 84918511722 scopus 로고    scopus 로고
    • Tuning of peroxiredoxin catalysis for various physiological roles
    • Perkins, A., Poole, L. B., and Karplus, P. A. (2014) Tuning of peroxiredoxin catalysis for various physiological roles Biochemistry 53, 7693-7705
    • (2014) Biochemistry , vol.53 , pp. 7693-7705
    • Perkins, A.1    Poole, L.B.2    Karplus, P.A.3
  • 46
    • 33745518017 scopus 로고    scopus 로고
    • Mycothiol-dependent mycobacterial response to oxidative stress
    • Ung, K. S. and Av-Gay, Y. (2006) Mycothiol-dependent mycobacterial response to oxidative stress FEBS Lett. 580, 2712-2716
    • (2006) FEBS Lett. , vol.580 , pp. 2712-2716
    • Ung, K.S.1    Av-Gay, Y.2
  • 49
    • 80052929972 scopus 로고    scopus 로고
    • S -Bacillithiolation protects against hypochlorite stress in Bacillus subtilis as revealed by transcriptomics and redox proteomics
    • Chi, B. K., Gronau, K., Mäder, U., Hessling, B., Becher, D., and Antelmann, H. (2011) S -Bacillithiolation protects against hypochlorite stress in Bacillus subtilis as revealed by transcriptomics and redox proteomics Mol. Cell. Proteomics 10, M111.009506
    • (2011) Mol. Cell. Proteomics , vol.10 , pp. 111009506
    • Chi, B.K.1    Gronau, K.2    Mäder, U.3    Hessling, B.4    Becher, D.5    Antelmann, H.6
  • 50
    • 34547399134 scopus 로고    scopus 로고
    • A complex thiolate switch regulates the Bacillus subtilis organic peroxide sensor OhrR
    • Lee, J.-W., Soonsanga, S., and Helmann, J. D. (2007) A complex thiolate switch regulates the Bacillus subtilis organic peroxide sensor OhrR Proc. Natl. Acad. Sci. U.S.A. 104, 8743-8748
    • (2007) Proc. Natl. Acad. Sci. U.S.A. , vol.104 , pp. 8743-8748
    • Lee, J.-W.1    Soonsanga, S.2    Helmann, J.D.3
  • 53
    • 84919485199 scopus 로고    scopus 로고
    • The role of macrophages in the innate immune response to Streptococcus pneumoniae and Staphylococcus aureus: Mechanisms and contrasts
    • Cole, J., Aberdein, J., Jubrail, J., and Dockrell, D. H. (2014) The role of macrophages in the innate immune response to Streptococcus pneumoniae and Staphylococcus aureus: Mechanisms and contrasts Adv. Microb. Physiol. 65, 125-202
    • (2014) Adv. Microb. Physiol. , vol.65 , pp. 125-202
    • Cole, J.1    Aberdein, J.2    Jubrail, J.3    Dockrell, D.H.4
  • 54
    • 84875442814 scopus 로고    scopus 로고
    • Neutrophil recruitment and function in health and inflammation
    • Kolaczkowska, E. and Kubes, P. (2013) Neutrophil recruitment and function in health and inflammation Nat. Rev. Immunol. 13, 159-175
    • (2013) Nat. Rev. Immunol. , vol.13 , pp. 159-175
    • Kolaczkowska, E.1    Kubes, P.2
  • 55
    • 84918842939 scopus 로고    scopus 로고
    • Nitric oxide synthase: Non-canonical expression patterns
    • Mattila, J. T. and Thomas, A. C. (2014) Nitric oxide synthase: Non-canonical expression patterns Front. Immunol. 5, 478
    • (2014) Front. Immunol. , vol.5 , pp. 478
    • Mattila, J.T.1    Thomas, A.C.2
  • 57
    • 18244390487 scopus 로고    scopus 로고
    • Myeloperoxidase: Friend and foe
    • Klebanoff, S. J. (2005) Myeloperoxidase: Friend and foe J. Leukocyte Biol. 77, 598-625
    • (2005) J. Leukocyte Biol. , vol.77 , pp. 598-625
    • Klebanoff, S.J.1
  • 58
    • 84872476329 scopus 로고    scopus 로고
    • Redox reactions and microbial killing in the neutrophil phagosome
    • Winterbourn, C. C. and Kettle, A. J. (2013) Redox reactions and microbial killing in the neutrophil phagosome Antioxid. Redox Signaling 18, 642-660
    • (2013) Antioxid. Redox Signaling , vol.18 , pp. 642-660
    • Winterbourn, C.C.1    Kettle, A.J.2
  • 59
    • 84877723813 scopus 로고    scopus 로고
    • Bacterial-derived uracil as a modulator of mucosal immunity and gut-microbe homeostasis in Drosophila
    • Lee, K.-A., Kim, S.-H., Kim, E.-K., Ha, E.-M., You, H., Kim, B., Kim, M.-J., Kwon, Y., Ryu, J.-H., and Lee, W.-J. (2013) Bacterial-derived uracil as a modulator of mucosal immunity and gut-microbe homeostasis in Drosophila Cell 153, 797-811
    • (2013) Cell , vol.153 , pp. 797-811
    • Lee, K.-A.1    Kim, S.-H.2    Kim, E.-K.3    Ha, E.-M.4    You, H.5    Kim, B.6    Kim, M.-J.7    Kwon, Y.8    Ryu, J.-H.9    Lee, W.-J.10
  • 60
    • 0028814066 scopus 로고
    • Purification and characterization of a mesohalic catalase from the halophilic bacterium Halobacterium halobium
    • Brownpeterson, N. J. and Salin, M. L. (1995) Purification and characterization of a mesohalic catalase from the halophilic bacterium Halobacterium halobium J. Bacteriol. 177, 378-384
    • (1995) J. Bacteriol. , vol.177 , pp. 378-384
    • Brownpeterson, N.J.1    Salin, M.L.2
  • 61
    • 0026045587 scopus 로고
    • Superoxide sensitivity of the Escherichia coli aconitase
    • Gardner, P. R. and Fridovich, I. (1991) Superoxide sensitivity of the Escherichia coli aconitase J. Biol. Chem. 266, 19328-19333
    • (1991) J. Biol. Chem. , vol.266 , pp. 19328-19333
    • Gardner, P.R.1    Fridovich, I.2
  • 62
    • 0016827580 scopus 로고
    • Estimation of life times and diffusion distances of radicals involved in X-ray-induced DNA strand breaks or killing of mammalian-cells
    • Roots, R. and Okada, S. (1975) Estimation of life times and diffusion distances of radicals involved in X-ray-induced DNA strand breaks or killing of mammalian-cells Radiat. Res. 64, 306-320
    • (1975) Radiat. Res. , vol.64 , pp. 306-320
    • Roots, R.1    Okada, S.2
  • 63
    • 84884179149 scopus 로고    scopus 로고
    • Causes and consequences of cysteine S -glutathionylation
    • Grek, C. L., Zhang, J., Manevich, Y., Townsend, D. M., and Tew, K. D. (2013) Causes and consequences of cysteine S -glutathionylation J. Biol. Chem. 288, 26497-26504
    • (2013) J. Biol. Chem. , vol.288 , pp. 26497-26504
    • Grek, C.L.1    Zhang, J.2    Manevich, Y.3    Townsend, D.M.4    Tew, K.D.5
  • 64
    • 0030465238 scopus 로고    scopus 로고
    • Superoxide accelerates DNA damage by elevating free-iron levels
    • Keyer, K. and Imlay, J. A. (1996) Superoxide accelerates DNA damage by elevating free-iron levels Proc. Natl. Acad. Sci. U.S.A. 93, 13635-13640
    • (1996) Proc. Natl. Acad. Sci. U.S.A. , vol.93 , pp. 13635-13640
    • Keyer, K.1    Imlay, J.A.2
  • 65
    • 0032544035 scopus 로고    scopus 로고
    • DNA strand breaking by the hydroxyl radical is governed by the accessible surface areas of the hydrogen atoms of the DNA backbone
    • Balasubramanian, B., Pogozelski, W. K., and Tullius, T. D. (1998) DNA strand breaking by the hydroxyl radical is governed by the accessible surface areas of the hydrogen atoms of the DNA backbone Proc. Natl. Acad. Sci. U.S.A. 95, 9738-9743
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 9738-9743
    • Balasubramanian, B.1    Pogozelski, W.K.2    Tullius, T.D.3
  • 66
    • 0038799736 scopus 로고    scopus 로고
    • Oxidative DNA damage: Mechanisms, mutation, and disease
    • Cooke, M. S., Evans, M. D., Dizdaroglu, M., and Lunec, J. (2003) Oxidative DNA damage: Mechanisms, mutation, and disease FASEB J. 17, 1195-1214
    • (2003) FASEB J. , vol.17 , pp. 1195-1214
    • Cooke, M.S.1    Evans, M.D.2    Dizdaroglu, M.3    Lunec, J.4
  • 67
    • 0028973482 scopus 로고
    • Requirement for generation of H2O2 for platelet-derived growth-factor signal-transduction
    • Sundaresan, M., Yu, Z. X., Ferrans, V. J., Irani, K., and Finkel, T. (1995) Requirement for generation of H2O2 for platelet-derived growth-factor signal-transduction Science 270, 296-299
    • (1995) Science , vol.270 , pp. 296-299
    • Sundaresan, M.1    Yu, Z.X.2    Ferrans, V.J.3    Irani, K.4    Finkel, T.5
  • 68
    • 0029964556 scopus 로고    scopus 로고
    • Identification of the primary metal ion-activation sites of the diphtheria tox repressor by X-ray crystallography and site-directed mutational analysis
    • Ding, X., Zeng, H., Schiering, N., Ringe, D., and Murphy, J. R. (1996) Identification of the primary metal ion-activation sites of the diphtheria tox repressor by X-ray crystallography and site-directed mutational analysis Nat. Struct. Biol. 3, 382-387
    • (1996) Nat. Struct. Biol. , vol.3 , pp. 382-387
    • Ding, X.1    Zeng, H.2    Schiering, N.3    Ringe, D.4    Murphy, J.R.5
  • 69
    • 79951789722 scopus 로고    scopus 로고
    • The SoxRS response of Escherichia coli is directly activated by redox-cycling drugs rather than by superoxide
    • Gu, M. and Imlay, J. A. (2011) The SoxRS response of Escherichia coli is directly activated by redox-cycling drugs rather than by superoxide Mol. Microbiol. 79, 1136-1150
    • (2011) Mol. Microbiol. , vol.79 , pp. 1136-1150
    • Gu, M.1    Imlay, J.A.2
  • 70
    • 79953716809 scopus 로고    scopus 로고
    • The soxRS response of Escherichia coli can be induced in the absence of oxidative stress and oxygen by modulation of NADPH content
    • Krapp, A. R., Humbert, M. V., and Carrillo, N. (2011) The soxRS response of Escherichia coli can be induced in the absence of oxidative stress and oxygen by modulation of NADPH content Microbiology 157, 957-965
    • (2011) Microbiology , vol.157 , pp. 957-965
    • Krapp, A.R.1    Humbert, M.V.2    Carrillo, N.3
  • 72
    • 0037215627 scopus 로고    scopus 로고
    • The global transcriptional response of Bacillus subtilis to peroxide stress is coordinated by three transcription factors
    • Helmann, J. D., Wu, M. F., Gaballa, A., Kobel, P. A., Morshedi, M. M., Fawcett, P., and Paddon, C. (2003) The global transcriptional response of Bacillus subtilis to peroxide stress is coordinated by three transcription factors J. Bacteriol. 185, 243-253
    • (2003) J. Bacteriol. , vol.185 , pp. 243-253
    • Helmann, J.D.1    Wu, M.F.2    Gaballa, A.3    Kobel, P.A.4    Morshedi, M.M.5    Fawcett, P.6    Paddon, C.7
  • 74
    • 50649117912 scopus 로고    scopus 로고
    • Cellular defenses against superoxide and hydrogen peroxide
    • Imlay, J. A. (2008) Cellular defenses against superoxide and hydrogen peroxide Annu. Rev. Biochem. 77, 755-776
    • (2008) Annu. Rev. Biochem. , vol.77 , pp. 755-776
    • Imlay, J.A.1
  • 75
    • 84868603203 scopus 로고    scopus 로고
    • Peroxide-sensing transcriptional regulators in bacteria
    • Dubbs, J. M. and Mongkolsuk, S. (2012) Peroxide-sensing transcriptional regulators in bacteria J. Bacteriol. 194, 5495-5503
    • (2012) J. Bacteriol. , vol.194 , pp. 5495-5503
    • Dubbs, J.M.1    Mongkolsuk, S.2
  • 76
    • 0023505509 scopus 로고
    • Endothelium-derived relaxing factor produced and released from artery and vein is nitric oxide
    • Ignarro, L. J., Buga, G. M., Wood, K. S., Byrns, R. E., and Chaudhuri, G. (1987) Endothelium-derived relaxing factor produced and released from artery and vein is nitric oxide Proc. Natl. Acad. Sci. U.S.A. 84, 9265-9269
    • (1987) Proc. Natl. Acad. Sci. U.S.A. , vol.84 , pp. 9265-9269
    • Ignarro, L.J.1    Buga, G.M.2    Wood, K.S.3    Byrns, R.E.4    Chaudhuri, G.5
  • 77
    • 0028015989 scopus 로고
    • Reaction kinetics for nitrosation of cysteine and glutathione in aerobic nitric oxide solutions at neutral pH. Insights into the fate and physiological effects of intermediates generated in the NO/O2 reaction
    • Wink, D. A., Nims, R. W., Darbyshire, J. F., Christodoulou, D., Hanbauer, I., Cox, G. W., Laval, F., Laval, J., and Cook, J. A. (1994) Reaction kinetics for nitrosation of cysteine and glutathione in aerobic nitric oxide solutions at neutral pH. Insights into the fate and physiological effects of intermediates generated in the NO/O2 reaction Chem. Res. Toxicol. 7, 519-525
    • (1994) Chem. Res. Toxicol. , vol.7 , pp. 519-525
    • Wink, D.A.1    Nims, R.W.2    Darbyshire, J.F.3    Christodoulou, D.4    Hanbauer, I.5    Cox, G.W.6    Laval, F.7    Laval, J.8    Cook, J.A.9
  • 78
    • 33749005136 scopus 로고    scopus 로고
    • Nitroxidative, nitrosative, and nitrative stress: Kinetic predictions of reactive nitrogen species chemistry under biological conditions
    • Lancaster, J. R. (2006) Nitroxidative, nitrosative, and nitrative stress: Kinetic predictions of reactive nitrogen species chemistry under biological conditions Chem. Res. Toxicol. 19, 1160-1174
    • (2006) Chem. Res. Toxicol. , vol.19 , pp. 1160-1174
    • Lancaster, J.R.1
  • 81
    • 84874588530 scopus 로고    scopus 로고
    • Beyond H2S and NO interplay: Hydrogen sulfide and nitroprusside react directly to give nitroxyl (HNO). A new pharmacological source of HNO
    • Filipovic, M. R., Eberhardt, M., Prokopovic, V., Mijuskovic, A., Orescanin-Dusic, Z., Reeh, P., and Ivanovic-Burmazovic, I. (2013) Beyond H2S and NO interplay: Hydrogen sulfide and nitroprusside react directly to give nitroxyl (HNO). A new pharmacological source of HNO J. Med. Chem. 56, 1499-1508
    • (2013) J. Med. Chem. , vol.56 , pp. 1499-1508
    • Filipovic, M.R.1    Eberhardt, M.2    Prokopovic, V.3    Mijuskovic, A.4    Orescanin-Dusic, Z.5    Reeh, P.6    Ivanovic-Burmazovic, I.7
  • 83
    • 0032554614 scopus 로고    scopus 로고
    • Reaction between S -nitrosothiols and thiols: Generation of nitroxyl (HNO) and subsequent chemistry
    • Wong, P. S. Y., Hyun, J., Fukuto, J. M., Shirota, F. N., DeMaster, E. G., Shoeman, D. W., and Nagasawa, H. T. (1998) Reaction between S -nitrosothiols and thiols: Generation of nitroxyl (HNO) and subsequent chemistry Biochemistry 37, 5362-5371
    • (1998) Biochemistry , vol.37 , pp. 5362-5371
    • Wong, P.S.Y.1    Hyun, J.2    Fukuto, J.M.3    Shirota, F.N.4    Demaster, E.G.5    Shoeman, D.W.6    Nagasawa, H.T.7
  • 85
    • 84919475251 scopus 로고    scopus 로고
    • Nitroxyl (HNO) reacts with molecular oxygen and forms peroxynitrite at physiological pH: Biological implications
    • Smulik, R., Debski, D., Zielonka, J., Michaowski, B., Adamus, J., Marcinek, A., Kalyanaraman, B., and Sikora, A. (2014) Nitroxyl (HNO) reacts with molecular oxygen and forms peroxynitrite at physiological pH: Biological implications J. Biol. Chem. 289, 35570-35581
    • (2014) J. Biol. Chem. , vol.289 , pp. 35570-35581
    • Smulik, R.1    Debski, D.2    Zielonka, J.3    Michaowski, B.4    Adamus, J.5    Marcinek, A.6    Kalyanaraman, B.7    Sikora, A.8
  • 87
    • 84876524887 scopus 로고    scopus 로고
    • Mechanism of [4Fe-4S](Cys)4 cluster nitrosylation is conserved among NO-responsive regulators
    • Crack, J. C., Stapleton, M. R., Green, J., Thomson, A. J., and Le Brun, N. E. (2013) Mechanism of [4Fe-4S](Cys)4 cluster nitrosylation is conserved among NO-responsive regulators J. Biol. Chem. 288, 11492-11502
    • (2013) J. Biol. Chem. , vol.288 , pp. 11492-11502
    • Crack, J.C.1    Stapleton, M.R.2    Green, J.3    Thomson, A.J.4    Le Brun, N.E.5
  • 88
    • 25144450560 scopus 로고    scopus 로고
    • NmlR of Neisseria gonorrhoeae: A novel redox responsive transcription factor from the MerR family
    • Kidd, S. P., Potter, A. J., Apicella, M. A., Jennings, M. P., and McEwan, A. G. (2005) NmlR of Neisseria gonorrhoeae: A novel redox responsive transcription factor from the MerR family Mol. Microbiol. 57, 1676-1689
    • (2005) Mol. Microbiol. , vol.57 , pp. 1676-1689
    • Kidd, S.P.1    Potter, A.J.2    Apicella, M.A.3    Jennings, M.P.4    McEwan, A.G.5
  • 89
    • 39149119282 scopus 로고    scopus 로고
    • A pneumococcal MerR-like regulator and S -nitrosoglutathione reductase are required for systemic virulence
    • Stroeher, U. H., Kidd, S. P., Stafford, S. L., Jennings, M. P., Paton, J. C., and McEwan, A. G. (2007) A pneumococcal MerR-like regulator and S -nitrosoglutathione reductase are required for systemic virulence J. Infect. Dis. 196, 1820-1826
    • (2007) J. Infect. Dis. , vol.196 , 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
  • 91
    • 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)
    • Thi Thu Huyen, N., Eiamphungporn, W., Mader, U., Liebeke, M., Lalk, M., Hecker, M., Helmann, J. D., and Antelmann, H. (2008) 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) Mol. Microbiol. 4, 876-894
    • (2008) Mol. Microbiol. , vol.4 , pp. 876-894
    • Thi Thu Huyen, N.1    Eiamphungporn, W.2    Mader, U.3    Liebeke, M.4    Lalk, M.5    Hecker, M.6    Helmann, J.D.7    Antelmann, H.8
  • 92
    • 77955299893 scopus 로고    scopus 로고
    • The MerR/NmlR Family Transcription Factor of Streptococcus pneumoniae Responds to Carbonyl Stress and Modulates Hydrogen Peroxide Production
    • Potter, A. J., Kidd, S. P., McEwan, A. G., and Paton, J. C. (2010) The MerR/NmlR Family Transcription Factor of Streptococcus pneumoniae Responds to Carbonyl Stress and Modulates Hydrogen Peroxide Production J. Bacteriol. 192, 4063-4066
    • (2010) J. Bacteriol. , vol.192 , pp. 4063-4066
    • Potter, A.J.1    Kidd, S.P.2    McEwan, A.G.3    Paton, J.C.4
  • 97
    • 84864393985 scopus 로고    scopus 로고
    • The electrophile responsive proteome: Integrating proteomics and lipidomics with cellular function
    • Higdon, A. N., Landar, A., Barnes, S., and Darley-Usmar, V. M. (2012) The electrophile responsive proteome: Integrating proteomics and lipidomics with cellular function Antioxid. Redox Signaling 17, 1580-1589
    • (2012) Antioxid. Redox Signaling , vol.17 , pp. 1580-1589
    • Higdon, A.N.1    Landar, A.2    Barnes, S.3    Darley-Usmar, V.M.4
  • 98
    • 84904663716 scopus 로고    scopus 로고
    • Molecular mechanisms of aldehyde toxicity: A chemical perspective
    • LoPachin, R. M. and Gavin, T. (2014) Molecular mechanisms of aldehyde toxicity: A chemical perspective Chem. Res. Toxicol. 27, 1081-1091
    • (2014) Chem. Res. Toxicol. , vol.27 , pp. 1081-1091
    • Lopachin, R.M.1    Gavin, T.2
  • 99
    • 84877654728 scopus 로고    scopus 로고
    • ROS-mediated lipid peroxidation and RES-activated signaling
    • Farmer, E. E. and Mueller, M. J. (2013) ROS-mediated lipid peroxidation and RES-activated signaling Annu. Rev. Plant Biol. 64, 429-450
    • (2013) Annu. Rev. Plant Biol. , vol.64 , pp. 429-450
    • Farmer, E.E.1    Mueller, M.J.2
  • 100
    • 36248990256 scopus 로고    scopus 로고
    • Characterization and quantification of reversible redox sites in humic substances
    • Ratasuk, N. and Nanny, M. A. (2007) Characterization and quantification of reversible redox sites in humic substances Environ. Sci. Technol. 41, 7844-7850
    • (2007) Environ. Sci. Technol. , vol.41 , pp. 7844-7850
    • Ratasuk, N.1    Nanny, M.A.2
  • 101
    • 0022495225 scopus 로고
    • Quinones in biology: Functions in electron transfer and oxygen activation
    • Nohl, H., Jordan, W., and Youngman, R. J. (1986) Quinones in biology: Functions in electron transfer and oxygen activation Adv. Free Radical Biol. Med. 2, 211-279
    • (1986) Adv. Free Radical Biol. Med. , vol.2 , pp. 211-279
    • Nohl, H.1    Jordan, W.2    Youngman, R.J.3
  • 102
    • 77951225834 scopus 로고    scopus 로고
    • A new structure-based classification of sulfide:quinone oxidoreductases
    • Marcia, M., Ermler, U., Peng, G., and Michel, H. (2010) A new structure-based classification of sulfide:quinone oxidoreductases Proteins 78, 1073-1083
    • (2010) Proteins , vol.78 , pp. 1073-1083
    • Marcia, M.1    Ermler, U.2    Peng, G.3    Michel, H.4
  • 103
    • 0026040838 scopus 로고
    • Molecular mechanisms of quinone cytotoxicity
    • O'Brien, P. J. (1991) Molecular mechanisms of quinone cytotoxicity Chem.-Biol. Interact. 80, 1-41
    • (1991) Chem.-Biol. Interact. , vol.80 , pp. 1-41
    • O'Brien, P.J.1
  • 104
    • 0037373455 scopus 로고    scopus 로고
    • Endogenous generation of reactive oxidants and electrophiles and their reactions with DNA and protein
    • Marnett, L. J., Riggins, J. N., and West, J. D. (2003) Endogenous generation of reactive oxidants and electrophiles and their reactions with DNA and protein J. Clin. Invest. 111, 583-593
    • (2003) J. Clin. Invest. , vol.111 , pp. 583-593
    • Marnett, L.J.1    Riggins, J.N.2    West, J.D.3
  • 105
    • 38849183395 scopus 로고    scopus 로고
    • Regulation of quinone detoxification by the thiol stress sensing DUF24/MarR-like repressor, YodB in Bacillus subtilis
    • Leelakriangsak, M., Huyen, N. T. T., Töwe, S., Van Duy, N., Becher, D., Hecker, M., Antelmann, H., and Zuber, P. (2008) Regulation of quinone detoxification by the thiol stress sensing DUF24/MarR-like repressor, YodB in Bacillus subtilis Mol. Microbiol. 67, 1108-1124
    • (2008) Mol. Microbiol. , vol.67 , pp. 1108-1124
    • Leelakriangsak, M.1    Huyen, N.T.T.2    Töwe, S.3    Van Duy, N.4    Becher, D.5    Hecker, M.6    Antelmann, H.7    Zuber, P.8
  • 106
    • 34548677758 scopus 로고    scopus 로고
    • The MarR-type repressor MhqR (YkvE) regulates multiple dioxygenases/glyoxalases and an azoreductase which confer resistance to 2-methylhydroquinone and catechol in Bacillus subtilis
    • Töwe, S., Leelakriangsak, M., Kobayashi, K., Van Duy, N., Hecker, M., Zuber, P., and Antelmann, H. (2007) The MarR-type repressor MhqR (YkvE) regulates multiple dioxygenases/glyoxalases and an azoreductase which confer resistance to 2-methylhydroquinone and catechol in Bacillus subtilis Mol. Microbiol. 66, 40-54
    • (2007) Mol. Microbiol. , vol.66 , pp. 40-54
    • Töwe, S.1    Leelakriangsak, M.2    Kobayashi, K.3    Van Duy, N.4    Hecker, M.5    Zuber, P.6    Antelmann, H.7
  • 108
    • 0018386333 scopus 로고
    • Myeloperoxidase, hydrogen peroxide, chloride antimicrobial system: Nitrogen-chlorine derivatives of bacterial components in bactericidal action against Escherichia coli
    • Thomas, E. L. (1979) Myeloperoxidase, hydrogen peroxide, chloride antimicrobial system: Nitrogen-chlorine derivatives of bacterial components in bactericidal action against Escherichia coli Infect. Immun. 23, 522-531
    • (1979) Infect. Immun. , vol.23 , pp. 522-531
    • Thomas, E.L.1
  • 110
    • 84887458268 scopus 로고    scopus 로고
    • The RclR protein is a reactive chlorine-specific transcription factor in Escherichia coli
    • Parker, B. W., Schwessinger, E. A., Jakob, U., and Gray, M. J. (2013) The RclR protein is a reactive chlorine-specific transcription factor in Escherichia coli J. Biol. Chem. 288, 32574-32584
    • (2013) J. Biol. Chem. , vol.288 , pp. 32574-32584
    • Parker, B.W.1    Schwessinger, E.A.2    Jakob, U.3    Gray, M.J.4
  • 111
    • 77954579286 scopus 로고    scopus 로고
    • Redox biochemistry of hydrogen sulfide
    • Kabil, O. and Banerjee, R. (2010) Redox biochemistry of hydrogen sulfide J. Biol. Chem. 285, 21903-21907
    • (2010) J. Biol. Chem. , vol.285 , pp. 21903-21907
    • Kabil, O.1    Banerjee, R.2
  • 112
    • 84881191992 scopus 로고    scopus 로고
    • Hydrogen sulfide chemical biology: Pathophysiological roles and detection
    • Kolluru, G. K., Shen, X., Bir, S. C., and Kevil, C. G. (2013) Hydrogen sulfide chemical biology: Pathophysiological roles and detection Nitric Oxide 35, 5-20
    • (2013) Nitric Oxide , vol.35 , pp. 5-20
    • Kolluru, G.K.1    Shen, X.2    Bir, S.C.3    Kevil, C.G.4
  • 113
    • 84864285556 scopus 로고    scopus 로고
    • H2S signalling through protein sulfhydration and beyond
    • Paul, B. D. and Snyder, S. H. (2012) H2S signalling through protein sulfhydration and beyond Nat. Rev. Mol. Cell Biol. 13, 499-507
    • (2012) Nat. Rev. Mol. Cell Biol. , vol.13 , pp. 499-507
    • Paul, B.D.1    Snyder, S.H.2
  • 114
    • 84862803226 scopus 로고    scopus 로고
    • Identification and characterization of a bacterial hydrosulphide ion channel
    • Czyzewski, B. K. and Wang, D.-N. (2012) Identification and characterization of a bacterial hydrosulphide ion channel Nature 483, 494-497
    • (2012) Nature , vol.483 , pp. 494-497
    • Czyzewski, B.K.1    Wang, D.-N.2
  • 115
    • 79953712285 scopus 로고    scopus 로고
    • Sulfur signaling: Is the agent sulfide or sulfane?
    • Toohey, J. I. (2011) Sulfur signaling: Is the agent sulfide or sulfane? Anal. Biochem. 413, 1-7
    • (2011) Anal. Biochem. , vol.413 , pp. 1-7
    • Toohey, J.I.1
  • 116
  • 117
    • 84921918209 scopus 로고    scopus 로고
    • S -Glutathionylation enhances human cystathionine β-synthase activity under oxidative stress conditions
    • Niu, W.-N., Yadav, P. K., Adamec, J., and Banerjee, R. (2014) S -Glutathionylation enhances human cystathionine β-synthase activity under oxidative stress conditions Antioxid. Redox Signaling 22, 350-361
    • (2014) Antioxid. Redox Signaling , vol.22 , pp. 350-361
    • Niu, W.-N.1    Yadav, P.K.2    Adamec, J.3    Banerjee, R.4
  • 118
    • 84880050232 scopus 로고    scopus 로고
    • Structure and kinetic analysis of H2S production by human mercaptopyruvate sulfurtransferase
    • Yadav, P. K., Yamada, K., Chiku, T., Koutmos, M., and Banerjee, R. (2013) Structure and kinetic analysis of H2S production by human mercaptopyruvate sulfurtransferase J. Biol. Chem. 288, 20002-20013
    • (2013) J. Biol. Chem. , vol.288 , pp. 20002-20013
    • Yadav, P.K.1    Yamada, K.2    Chiku, T.3    Koutmos, M.4    Banerjee, R.5
  • 119
    • 81555205640 scopus 로고    scopus 로고
    • H2S: A universal defense against antibiotics in bacteria
    • Shatalin, K., Shatalina, E., Mironov, A., and Nudler, E. (2011) H2S: A universal defense against antibiotics in bacteria Science 334, 986-990
    • (2011) Science , vol.334 , pp. 986-990
    • Shatalin, K.1    Shatalina, E.2    Mironov, A.3    Nudler, E.4
  • 122
    • 84908391944 scopus 로고    scopus 로고
    • Organization of the human mitochondrial hydrogen sulfide oxidation pathway
    • Libiad, M., Yadav, P. K., Vitvitsky, V., Martinov, M., and Banerjee, R. (2014) Organization of the human mitochondrial hydrogen sulfide oxidation pathway J. Biol. Chem. 289, 30901-30910
    • (2014) J. Biol. Chem. , vol.289 , pp. 30901-30910
    • Libiad, M.1    Yadav, P.K.2    Vitvitsky, V.3    Martinov, M.4    Banerjee, R.5
  • 123
    • 84905281134 scopus 로고    scopus 로고
    • Understanding hydrogen sulfide storage: Probing conditions for sulfide release from hydrodisulfides
    • Bailey, T. S., Zakharov, L. N., and Pluth, M. D. (2014) Understanding hydrogen sulfide storage: Probing conditions for sulfide release from hydrodisulfides J. Am. Chem. Soc. 136, 10573-10576
    • (2014) J. Am. Chem. Soc. , vol.136 , pp. 10573-10576
    • Bailey, T.S.1    Zakharov, L.N.2    Pluth, M.D.3
  • 124
    • 84915735116 scopus 로고    scopus 로고
    • The CsoR-like sulfurtransferase repressor (CstR) is a persulfide sensor in Staphylococcus aureus
    • Luebke, J. L., Shen, J., Bruce, K. E., Kehl-Fie, T. E., Peng, H., Skaar, E. P., and Giedroc, D. P. (2014) The CsoR-like sulfurtransferase repressor (CstR) is a persulfide sensor in Staphylococcus aureus Mol. Microbiol. 6, 1343-1360
    • (2014) Mol. Microbiol. , vol.6 , pp. 1343-1360
    • Luebke, J.L.1    Shen, J.2    Bruce, K.E.3    Kehl-Fie, T.E.4    Peng, H.5    Skaar, E.P.6    Giedroc, D.P.7
  • 126
    • 83655165310 scopus 로고    scopus 로고
    • H2S-induced sulfhydration of the phosphatase PTP1B and its role in the endoplasmic reticulum stress response
    • Krishnan, N., Fu, C., Pappin, D. J., and Tonks, N. K. (2011) H2S-induced sulfhydration of the phosphatase PTP1B and its role in the endoplasmic reticulum stress response Sci. Signaling 4, ra86
    • (2011) Sci. Signaling , vol.4 , pp. 86
    • Krishnan, N.1    Fu, C.2    Pappin, D.J.3    Tonks, N.K.4
  • 127
    • 84862909327 scopus 로고    scopus 로고
    • Hydrogen sulfide-linked sulfhydration of NF-B mediates its anti-apoptotic actions
    • Sen, N., Paul, B. D., Gadalla, M. M., Mustafa, A. K., Sen, T., Xu, R., Kim, S., and Snyder, S. H. (2012) Hydrogen sulfide-linked sulfhydration of NF-B mediates its anti-apoptotic actions Mol. Cell 45, 13-24
    • (2012) Mol. Cell , vol.45 , pp. 13-24
    • Sen, N.1    Paul, B.D.2    Gadalla, M.M.3    Mustafa, A.K.4    Sen, T.5    Xu, R.6    Kim, S.7    Snyder, S.H.8
  • 128
    • 79960423857 scopus 로고    scopus 로고
    • Plant pathogenic bacteria utilize biofilm growth-associated repressor (BigR), a novel winged-helix redox switch, to control hydrogen sulfide detoxification under hypoxia
    • Guimaraes, B. G., Barbosa, R. L., Soprano, A. S., Campos, B. M., de Souza, T. A., Tonoli, C. C. C., Leme, A. F. P., Murakami, M. T., and Benedetti, C. E. (2011) Plant pathogenic bacteria utilize biofilm growth-associated repressor (BigR), a novel winged-helix redox switch, to control hydrogen sulfide detoxification under hypoxia J. Biol. Chem. 286, 26148-26157
    • (2011) J. Biol. Chem. , vol.286 , pp. 26148-26157
    • Guimaraes, B.G.1    Barbosa, R.L.2    Soprano, A.S.3    Campos, B.M.4    De Souza, T.A.5    Tonoli, C.C.C.6    Leme, A.F.P.7    Murakami, M.T.8    Benedetti, C.E.9
  • 129
    • 31344443334 scopus 로고    scopus 로고
    • Ligand-responsive transcriptional regulation by members of the MarR family of winged helix proteins
    • Wilkinson, S. P. and Grove, A. (2006) Ligand-responsive transcriptional regulation by members of the MarR family of winged helix proteins Curr. Issues Mol. Biol. 8, 51-62
    • (2006) Curr. Issues Mol. Biol. , vol.8 , pp. 51-62
    • Wilkinson, S.P.1    Grove, A.2
  • 130
    • 0037500300 scopus 로고    scopus 로고
    • Organic hydroperoxide resistance gene encodes a thiol-dependent peroxidase
    • Cussiol, J. R. R., Alves, S. V., Antonio de Oliveira, M., and Netto, L. E. S. (2003) Organic hydroperoxide resistance gene encodes a thiol-dependent peroxidase J. Biol. Chem. 278, 11570-11578
    • (2003) J. Biol. Chem. , vol.278 , pp. 11570-11578
    • Cussiol, J.R.R.1    Alves, S.V.2    Antonio De Oliveira, M.3    Netto, L.E.S.4
  • 131
    • 0034971954 scopus 로고    scopus 로고
    • OhrR is a repressor of ohrA, a key organic hydroperoxide resistance determinant in Bacillus subtilis
    • Fuangthong, M., Atichartpongkul, S., Mongkolsuk, S., and Helmann, J. D. (2001) OhrR is a repressor of ohrA, a key organic hydroperoxide resistance determinant in Bacillus subtilis J. Bacteriol. 183, 4134-4141
    • (2001) J. Bacteriol. , vol.183 , pp. 4134-4141
    • Fuangthong, M.1    Atichartpongkul, S.2    Mongkolsuk, S.3    Helmann, J.D.4
  • 132
    • 0036032183 scopus 로고    scopus 로고
    • OhrR, a transcription repressor that senses and responds to changes in organic peroxide levels in Xanthomonas campestris pv phaseoli
    • Panmanee, W., Vattanaviboon, P., Eiamphungporn, W., Whangsuk, W., Sallabhan, R., and Mongkolsuk, S. (2002) OhrR, a transcription repressor that senses and responds to changes in organic peroxide levels in Xanthomonas campestris pv. phaseoli Mol. Microbiol. 45, 1647-1654
    • (2002) Mol. Microbiol. , vol.45 , pp. 1647-1654
    • Panmanee, W.1    Vattanaviboon, P.2    Eiamphungporn, W.3    Whangsuk, W.4    Sallabhan, R.5    Mongkolsuk, S.6
  • 133
    • 0035142748 scopus 로고    scopus 로고
    • Identification and characterization of gsp65, an organic hydroperoxide resistance (ohr) gene encoding a general stress protein in Enterococcus faecalis
    • Rincé, A., Giard, J.-C., Pichereau, V., Flahaut, S., and Auffray, Y. (2001) Identification and characterization of gsp65, an organic hydroperoxide resistance (ohr) gene encoding a general stress protein in Enterococcus faecalis J. Bacteriol. 183, 1482-1488
    • (2001) J. Bacteriol. , vol.183 , pp. 1482-1488
    • Rincé, A.1    Giard, J.-C.2    Pichereau, V.3    Flahaut, S.4    Auffray, Y.5
  • 134
    • 33750230997 scopus 로고    scopus 로고
    • An oxidation-sensing mechanism is used by the global regulator MgrA in Staphylococcus aureus
    • Chen, P. R., Bae, T., Williams, W. A., Duguid, E. M., Rice, P. A., Schneewind, O., and He, C. (2006) An oxidation-sensing mechanism is used by the global regulator MgrA in Staphylococcus aureus Nat. Chem. Biol. 2, 591-595
    • (2006) Nat. Chem. Biol. , vol.2 , pp. 591-595
    • Chen, P.R.1    Bae, T.2    Williams, W.A.3    Duguid, E.M.4    Rice, P.A.5    Schneewind, O.6    He, C.7
  • 135
    • 2942588414 scopus 로고    scopus 로고
    • The structure of the organic hydroperoxide resistance protein from Deinococcus radiodurans: Do conformational changes facilitate recycling of the redox disulfide?
    • Meunier-Jamin, C., Kapp, U., Leonard, G. A., and McSweeney, S. (2004) The structure of the organic hydroperoxide resistance protein from Deinococcus radiodurans: Do conformational changes facilitate recycling of the redox disulfide? J. Biol. Chem. 279, 25830-25837
    • (2004) J. Biol. Chem. , vol.279 , pp. 25830-25837
    • Meunier-Jamin, C.1    Kapp, U.2    Leonard, G.A.3    McSweeney, S.4
  • 136
    • 0035157997 scopus 로고    scopus 로고
    • Genetic and physiological characterization of ohr, encoding a protein involved in organic hydroperoxide resistance in Pseudomonas aeruginosa
    • Ochsner, U. A., Hassett, D. J., and Vasil, M. L. (2001) Genetic and physiological characterization of ohr, encoding a protein involved in organic hydroperoxide resistance in Pseudomonas aeruginosa J. Bacteriol. 183, 773-778
    • (2001) J. Bacteriol. , vol.183 , pp. 773-778
    • Ochsner, U.A.1    Hassett, D.J.2    Vasil, M.L.3
  • 137
    • 31344471227 scopus 로고    scopus 로고
    • OhrR and ohr are the primary sensor/regulator and protective genes against organic hydroperoxide stress in Agrobacterium tumefaciens
    • Chuchue, T., Tanboon, W., Prapagdee, B., Dubbs, J. M., Vattanaviboon, P., and Mongkolsuk, S. (2006) ohrR and ohr are the primary sensor/regulator and protective genes against organic hydroperoxide stress in Agrobacterium tumefaciens J. Bacteriol. 188, 842-851
    • (2006) J. Bacteriol. , vol.188 , pp. 842-851
    • Chuchue, T.1    Tanboon, W.2    Prapagdee, B.3    Dubbs, J.M.4    Vattanaviboon, P.5    Mongkolsuk, S.6
  • 138
    • 36248933266 scopus 로고    scopus 로고
    • Structural mechanism of organic hydroperoxide induction of the transcription regulator OhrR
    • Newberry, K. J., Fuangthong, M., Panmanee, W., Mongkolsuk, S., and Brennan, R. G. (2007) Structural mechanism of organic hydroperoxide induction of the transcription regulator OhrR Mol. Cell 28, 652-664
    • (2007) Mol. Cell , vol.28 , pp. 652-664
    • Newberry, K.J.1    Fuangthong, M.2    Panmanee, W.3    Mongkolsuk, S.4    Brennan, R.G.5
  • 139
    • 0037076330 scopus 로고    scopus 로고
    • The OhrR repressor senses organic hydroperoxides by reversible formation of a cysteine-sulfenic acid derivative
    • Fuangthong, M. and Helmann, J. D. (2002) The OhrR repressor senses organic hydroperoxides by reversible formation of a cysteine-sulfenic acid derivative Proc. Natl. Acad. Sci. U.S.A. 99, 6690-6695
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 6690-6695
    • Fuangthong, M.1    Helmann, J.D.2
  • 140
    • 33644755944 scopus 로고    scopus 로고
    • Transcription profiling of the mgrA regulon in Staphylococcus aureus
    • Luong, T. T., Dunman, P. M., Murphy, E., Projan, S. J., and Lee, C. Y. (2006) Transcription profiling of the mgrA regulon in Staphylococcus aureus J. Bacteriol. 188, 1899-1910
    • (2006) J. Bacteriol. , vol.188 , pp. 1899-1910
    • Luong, T.T.1    Dunman, P.M.2    Murphy, E.3    Projan, S.J.4    Lee, C.Y.5
  • 142
    • 33751364085 scopus 로고    scopus 로고
    • Novel DNA binding protein SarZ contributes to virulence in Staphylococcus aureus
    • Kaito, C., Morishita, D., Matsumoto, Y., Kurokawa, K., and Sekimizu, K. (2006) Novel DNA binding protein SarZ contributes to virulence in Staphylococcus aureus Mol. Microbiol. 62, 1601-1617
    • (2006) Mol. Microbiol. , vol.62 , pp. 1601-1617
    • Kaito, C.1    Morishita, D.2    Matsumoto, Y.3    Kurokawa, K.4    Sekimizu, K.5
  • 143
    • 0038715856 scopus 로고    scopus 로고
    • Mgr, a novel global regulator in Staphylococcus aureus
    • Luong, T. T., Newell, S. W., and Lee, C. Y. (2003) mgr, a novel global regulator in Staphylococcus aureus J. Bacteriol. 185, 3703-3710
    • (2003) J. Bacteriol. , vol.185 , pp. 3703-3710
    • Luong, T.T.1    Newell, S.W.2    Lee, C.Y.3
  • 145
    • 84860330756 scopus 로고    scopus 로고
    • Reduced aeration affects the expression of the NorB efflux pump of Staphylococcus aureus by posttranslational modification of MgrA
    • Truong-Bolduc, Q. C., Hsing, L. C., Villet, R., Bolduc, G. R., Estabrooks, Z., Taguezem, G. F., and Hooper, D. C. (2012) Reduced aeration affects the expression of the NorB efflux pump of Staphylococcus aureus by posttranslational modification of MgrA J. Bacteriol. 194, 1823-1834
    • (2012) J. Bacteriol. , vol.194 , pp. 1823-1834
    • Truong-Bolduc, Q.C.1    Hsing, L.C.2    Villet, R.3    Bolduc, G.R.4    Estabrooks, Z.5    Taguezem, G.F.6    Hooper, D.C.7
  • 146
    • 55549098541 scopus 로고    scopus 로고
    • Posttranslational modification influences the effects of MgrA on norA expression in Staphylococcus aureus
    • Truong-Bolduc, Q. C., Ding, Y., and Hooper, D. C. (2008) Posttranslational modification influences the effects of MgrA on norA expression in Staphylococcus aureus J. Bacteriol. 190, 7375-7381
    • (2008) J. Bacteriol. , vol.190 , pp. 7375-7381
    • Truong-Bolduc, Q.C.1    Ding, Y.2    Hooper, D.C.3
  • 148
    • 84921498354 scopus 로고    scopus 로고
    • Ser/Thr phosphorylation as a regulatory mechanism in bacteria
    • Dworkin, J. (2015) Ser/Thr phosphorylation as a regulatory mechanism in bacteria Curr. Opin. Microbiol. 24, 47-52
    • (2015) Curr. Opin. Microbiol. , vol.24 , pp. 47-52
    • Dworkin, J.1
  • 149
    • 0027494050 scopus 로고
    • Multiple antibiotic resistance in Pseudomonas aeruginosa: Evidence for involvement of an efflux operon
    • Poole, K., Krebes, K., McNally, C., and Neshat, S. (1993) Multiple antibiotic resistance in Pseudomonas aeruginosa: Evidence for involvement of an efflux operon J. Bacteriol. 175, 7363-7372
    • (1993) J. Bacteriol. , vol.175 , pp. 7363-7372
    • Poole, K.1    Krebes, K.2    McNally, C.3    Neshat, S.4
  • 150
    • 0028067837 scopus 로고
    • Role of efflux pump(s) in intrinsic resistance of Pseudomonas aeruginosa: Resistance to tetracycline, chloramphenicol, and norfloxacin
    • Li, X. Z., Livermore, D. M., and Nikaido, H. (1994) Role of efflux pump(s) in intrinsic resistance of Pseudomonas aeruginosa: Resistance to tetracycline, chloramphenicol, and norfloxacin Antimicrob. Agents Chemother. 38, 1732-1741
    • (1994) Antimicrob. Agents Chemother. , vol.38 , pp. 1732-1741
    • Li, X.Z.1    Livermore, D.M.2    Nikaido, H.3
  • 151
    • 0029129966 scopus 로고
    • Role of MexA-MexB-OprM in antibiotic efflux in Pseudomonas aeruginosa
    • Li, X. Z., Nikaido, H., and Poole, K. (1995) Role of MexA-MexB-OprM in antibiotic efflux in Pseudomonas aeruginosa Antimicrob. Agents Chemother. 39, 1948-1953
    • (1995) Antimicrob. Agents Chemother. , vol.39 , pp. 1948-1953
    • Li, X.Z.1    Nikaido, H.2    Poole, K.3
  • 152
    • 0029815432 scopus 로고    scopus 로고
    • Expression of the multidrug resistance operon mexA-mexB-oprM in Pseudomonas aeruginosa: MexR encodes a regulator of operon expression
    • Poole, K., Tetro, K., Zhao, Q., Neshat, S., Heinrichs, D. E., and Bianco, N. (1996) Expression of the multidrug resistance operon mexA-mexB-oprM in Pseudomonas aeruginosa: mexR encodes a regulator of operon expression Antimicrob. Agents Chemother. 40, 2021-2028
    • (1996) Antimicrob. Agents Chemother. , vol.40 , pp. 2021-2028
    • Poole, K.1    Tetro, K.2    Zhao, Q.3    Neshat, S.4    Heinrichs, D.E.5    Bianco, N.6
  • 153
    • 0037047395 scopus 로고    scopus 로고
    • Crystal structure of the MexR repressor of the mexRAB-oprM multidrug efflux operon of Pseudomonas aeruginosa
    • Lim, D., Poole, K., and Strynadka, N. C. (2002) Crystal structure of the MexR repressor of the mexRAB-oprM multidrug efflux operon of Pseudomonas aeruginosa J. Biol. Chem. 277, 29253-29259
    • (2002) J. Biol. Chem. , vol.277 , pp. 29253-29259
    • Lim, D.1    Poole, K.2    Strynadka, N.C.3
  • 154
    • 0032513362 scopus 로고    scopus 로고
    • Activation of the OxyR transcription factor by reversible disulfide bond formation
    • Zheng, M., Åslund, F., and Storz, G. (1998) Activation of the OxyR transcription factor by reversible disulfide bond formation Science 279, 1718-1722
    • (1998) Science , vol.279 , pp. 1718-1722
    • Zheng, M.1    Åslund, F.2    Storz, G.3
  • 155
    • 34548213103 scopus 로고    scopus 로고
    • A common mechanism of cellular death induced by bactericidal antibiotics
    • Kohanski, M. A., Dwyer, D. J., Hayete, B., Lawrence, C. A., and Collins, J. J. (2007) A common mechanism of cellular death induced by bactericidal antibiotics Cell 130, 797-810
    • (2007) Cell , vol.130 , pp. 797-810
    • Kohanski, M.A.1    Dwyer, D.J.2    Hayete, B.3    Lawrence, C.A.4    Collins, J.J.5
  • 159
    • 61449121100 scopus 로고    scopus 로고
    • Pneumococcal histidine triad proteins are regulated by the Zn2+-dependent repressor AdcR and inhibit complement deposition through the recruitment of complement factor H
    • Ogunniyi, A. D., Grabowicz, M., Mahdi, L. K., Cook, J., Gordon, D. L., Sadlon, T. A., and Paton, J. C. (2008) Pneumococcal histidine triad proteins are regulated by the Zn2+-dependent repressor AdcR and inhibit complement deposition through the recruitment of complement factor H FASEB J. 3, 731-738
    • (2008) FASEB J. , vol.3 , pp. 731-738
    • Ogunniyi, A.D.1    Grabowicz, M.2    Mahdi, L.K.3    Cook, J.4    Gordon, D.L.5    Sadlon, T.A.6    Paton, J.C.7
  • 160
    • 84857861036 scopus 로고    scopus 로고
    • Metal site occupancy and allosteric switching in bacterial metal sensor proteins
    • Guerra, A. J. and Giedroc, D. P. (2012) Metal site occupancy and allosteric switching in bacterial metal sensor proteins Arch. Biochem. Biophys. 519, 210-222
    • (2012) Arch. Biochem. Biophys. , vol.519 , pp. 210-222
    • Guerra, A.J.1    Giedroc, D.P.2
  • 161
    • 0032994431 scopus 로고    scopus 로고
    • Regulation of the OxyR transcription factor by hydrogen peroxide and the cellular thiol-disulfide status
    • Åslund, F., Zheng, M., Beckwith, J., and Storz, G. (1999) Regulation of the OxyR transcription factor by hydrogen peroxide and the cellular thiol-disulfide status Proc. Natl. Acad. Sci. U.S.A. 96, 6161-6165
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 6161-6165
    • Åslund, F.1    Zheng, M.2    Beckwith, J.3    Storz, G.4
  • 162
  • 163
    • 84860176878 scopus 로고    scopus 로고
    • Endogenous protein S-nitrosylation in E coli: Regulation by OxyR
    • Seth, D., Hausladen, A., Wang, Y.-J., and Stamler, J. S. (2012) Endogenous protein S -nitrosylation in E. coli: Regulation by OxyR Science 336, 470-473
    • (2012) Science , vol.336 , pp. 470-473
    • Seth, D.1    Hausladen, A.2    Wang, Y.-J.3    Stamler, J.S.4
  • 165
    • 22544482619 scopus 로고    scopus 로고
    • Avicinylation (thioesterification): A protein modification that can regulate the response to oxidative and nitrosative stress
    • Haridas, V., Kim, S.-O., Nishimura, G., Hausladen, A., Stamler, J. S., and Gutterman, J. U. (2005) Avicinylation (thioesterification): A protein modification that can regulate the response to oxidative and nitrosative stress Proc. Natl. Acad. Sci. U.S.A. 102, 10088-10093
    • (2005) Proc. Natl. Acad. Sci. U.S.A. , vol.102 , pp. 10088-10093
    • Haridas, V.1    Kim, S.-O.2    Nishimura, G.3    Hausladen, A.4    Stamler, J.S.5    Gutterman, J.U.6
  • 166
    • 45449113598 scopus 로고    scopus 로고
    • A novel OxyR sensor and regulator of hydrogen peroxide stress with one cysteine residue in Deinococcus radiodurans
    • Chen, H., Xu, G., Zhao, Y., Tian, B., Lu, H., Yu, X., Xu, Z., Ying, N., Hu, S., and Hua, Y. (2008) A novel OxyR sensor and regulator of hydrogen peroxide stress with one cysteine residue in Deinococcus radiodurans PLoS One 3, e1602
    • (2008) PLoS One , vol.3 , pp. 1602
    • Chen, H.1    Xu, G.2    Zhao, Y.3    Tian, B.4    Lu, H.5    Yu, X.6    Xu, Z.7    Ying, N.8    Hu, S.9    Hua, Y.10
  • 167
    • 84865648246 scopus 로고    scopus 로고
    • Redox active thiol sensors of oxidative and nitrosative stress
    • Vazquez-Torres, A. (2012) Redox active thiol sensors of oxidative and nitrosative stress Antioxid. Redox Signaling 17, 1201-1214
    • (2012) Antioxid. Redox Signaling , vol.17 , pp. 1201-1214
    • Vazquez-Torres, A.1
  • 168
    • 84862285306 scopus 로고    scopus 로고
    • Staphylococcus aureus CymR is a new thiol-based oxidation-sensing regulator of stress resistance and oxidative response
    • Ji, Q., Zhang, L., Sun, F., Deng, X., Liang, H., Bae, T., and He, C. (2012) Staphylococcus aureus CymR is a new thiol-based oxidation-sensing regulator of stress resistance and oxidative response J. Biol. Chem. 287, 21102-21109
    • (2012) J. Biol. Chem. , vol.287 , pp. 21102-21109
    • Ji, Q.1    Zhang, L.2    Sun, F.3    Deng, X.4    Liang, H.5    Bae, T.6    He, C.7
  • 169
    • 79960598587 scopus 로고    scopus 로고
    • Insights into the Rrf2 repressor family: The structure of CymR, the global cysteine regulator of Bacillus subtilis
    • Shepard, W., Soutourina, O., Courtois, E., England, P., Haouz, A., and Martin-Verstraete, I. (2011) Insights into the Rrf2 repressor family: The structure of CymR, the global cysteine regulator of Bacillus subtilis FEBS J. 278, 2689-2701
    • (2011) FEBS J. , vol.278 , pp. 2689-2701
    • Shepard, W.1    Soutourina, O.2    Courtois, E.3    England, P.4    Haouz, A.5    Martin-Verstraete, I.6
  • 172
    • 84891810747 scopus 로고    scopus 로고
    • Insights into protein allostery in the CsoR/RcnR family of transcriptional repressors
    • Higgins, K. A. and Giedroc, D. (2014) Insights into protein allostery in the CsoR/RcnR family of transcriptional repressors Chem. Lett. 43, 20-25
    • (2014) Chem. Lett. , vol.43 , pp. 20-25
    • Higgins, K.A.1    Giedroc, D.2
  • 173
    • 4944228604 scopus 로고    scopus 로고
    • Global transcriptional effects of a suppressor tRNA and the inactivation of the regulator frmR
    • Herring, C. D. and Blattner, F. R. (2004) Global transcriptional effects of a suppressor tRNA and the inactivation of the regulator frmR J. Bacteriol. 186, 6714-6720
    • (2004) J. Bacteriol. , vol.186 , pp. 6714-6720
    • Herring, C.D.1    Blattner, F.R.2
  • 174
    • 77956131582 scopus 로고    scopus 로고
    • The redox-sensing regulator YodB senses quinones and diamide via a thiol-disulfide switch in Bacillus subtilis
    • Chi, B. K., Albrecht, D., Gronau, K., Becher, D., Hecker, M., and Antelmann, H. (2010) The redox-sensing regulator YodB senses quinones and diamide via a thiol-disulfide switch in Bacillus subtilis Proteomics 10, 3155-3164
    • (2010) Proteomics , vol.10 , pp. 3155-3164
    • Chi, B.K.1    Albrecht, D.2    Gronau, K.3    Becher, D.4    Hecker, M.5    Antelmann, H.6
  • 175
    • 0037565104 scopus 로고    scopus 로고
    • The SmtB/ArsR family of metalloregulatory transcriptional repressors: Structural insights into prokaryotic metal resistance
    • Busenlehner, L. S., Pennella, M. A., and Giedroc, D. P. (2003) The SmtB/ArsR family of metalloregulatory transcriptional repressors: Structural insights into prokaryotic metal resistance FEMS Microbiol. Rev. 27, 131-143
    • (2003) FEMS Microbiol. Rev. , vol.27 , pp. 131-143
    • Busenlehner, L.S.1    Pennella, M.A.2    Giedroc, D.P.3
  • 176
  • 178
    • 84879776406 scopus 로고    scopus 로고
    • Persulfide reactivity in the detection of protein S -sulfhydration
    • Pan, J. and Carroll, K. S. (2013) Persulfide reactivity in the detection of protein S -sulfhydration ACS Chem. Biol. 8, 1110-1116
    • (2013) ACS Chem. Biol. , vol.8 , pp. 1110-1116
    • Pan, J.1    Carroll, K.S.2
  • 179
    • 70350044409 scopus 로고    scopus 로고
    • Crystal structure and catalytic properties of Bacillus anthracis CoADR-RHD: Implications for flavin-linked sulfur trafficking
    • Wallen, J. R., Mallett, T. C., Boles, W., Parsonage, D., Furdui, C. M., Karplus, P. A., and Claiborne, A. (2009) Crystal structure and catalytic properties of Bacillus anthracis CoADR-RHD: Implications for flavin-linked sulfur trafficking Biochemistry 48, 9650-9667
    • (2009) Biochemistry , vol.48 , pp. 9650-9667
    • Wallen, J.R.1    Mallett, T.C.2    Boles, W.3    Parsonage, D.4    Furdui, C.M.5    Karplus, P.A.6    Claiborne, A.7
  • 180
    • 34548504554 scopus 로고    scopus 로고
    • BigR, a transcriptional repressor from plant-associated bacteria, regulates an operon implicated in biofilm growth
    • Barbosa, R. L. and Benedetti, C. E. (2007) BigR, a transcriptional repressor from plant-associated bacteria, regulates an operon implicated in biofilm growth J. Bacteriol. 189, 6185-6194
    • (2007) J. Bacteriol. , vol.189 , pp. 6185-6194
    • Barbosa, R.L.1    Benedetti, C.E.2
  • 181
    • 79953892242 scopus 로고    scopus 로고
    • Control of copper resistance and inorganic sulfur metabolism by paralogous regulators in Staphylococcus aureus
    • Grossoehme, N. E., Kehl-Fie, T. E., Ma, Z., Adams, K. W., Cowart, D. M., Scott, R. A., Skaar, E. P., and Giedroc, D. P. (2011) Control of copper resistance and inorganic sulfur metabolism by paralogous regulators in Staphylococcus aureus J. Biol. Chem. 286, 13522-13531
    • (2011) J. Biol. Chem. , vol.286 , pp. 13522-13531
    • Grossoehme, N.E.1    Kehl-Fie, T.E.2    Ma, Z.3    Adams, K.W.4    Cowart, D.M.5    Scott, R.A.6    Skaar, E.P.7    Giedroc, D.P.8
  • 182
    • 84927725427 scopus 로고    scopus 로고
    • Conformational analysis and chemical reactivity of the multidomain sulfurtransferase, Staphylococcus aureus CstA
    • Higgins, K. A., Hui, P., Luebke, J. L., Chang, F.-M. J., and Giedroc, D. P. (2015) Conformational analysis and chemical reactivity of the multidomain sulfurtransferase, Staphylococcus aureus CstA Biochemistry 54, 2385-2398
    • (2015) Biochemistry , vol.54 , pp. 2385-2398
    • Higgins, K.A.1    Hui, P.2    Luebke, J.L.3    Chang, F.-M.J.4    Giedroc, D.P.5
  • 184
    • 84879565056 scopus 로고    scopus 로고
    • Selenite and tellurite form mixed seleno- and tellurotrisulfides with CstR from Staphylococcus aureus
    • Luebke, J. L., Arnold, R. J., and Giedroc, D. P. (2013) Selenite and tellurite form mixed seleno- and tellurotrisulfides with CstR from Staphylococcus aureus Metallomics 5, 335-342
    • (2013) Metallomics , vol.5 , pp. 335-342
    • Luebke, J.L.1    Arnold, R.J.2    Giedroc, D.P.3
  • 185
    • 84924045221 scopus 로고    scopus 로고
    • Mass spectrometry in studies of protein thiol chemistry and signaling: Opportunities and caveats
    • Devarie Baez, N. O., Reisz, J. A., and Furdui, C. M. (2015) Mass spectrometry in studies of protein thiol chemistry and signaling: Opportunities and caveats Free Radical Biol. Med. 80, 191-211
    • (2015) Free Radical Biol. Med. , vol.80 , pp. 191-211
    • Devarie Baez, N.O.1    Reisz, J.A.2    Furdui, C.M.3
  • 186
    • 84888599347 scopus 로고    scopus 로고
    • Chemical biology approaches to study protein cysteine sulfenylation
    • Pan, J. and Carroll, K. S. (2013) Chemical biology approaches to study protein cysteine sulfenylation Biopolymers 101, 165-172
    • (2013) Biopolymers , vol.101 , pp. 165-172
    • Pan, J.1    Carroll, K.S.2
  • 187
    • 12244293660 scopus 로고    scopus 로고
    • S -Nitroso proteome of Mycobacterium tuberculosis: Enzymes of intermediary metabolism and antioxidant defense
    • Rhee, K. Y., Erdjument-Bromage, H., Tempst, P., and Nathan, C. F. (2005) S -Nitroso proteome of Mycobacterium tuberculosis: Enzymes of intermediary metabolism and antioxidant defense Proc. Natl. Acad. Sci. U.S.A. 102, 467-472
    • (2005) Proc. Natl. Acad. Sci. U.S.A. , vol.102 , pp. 467-472
    • Rhee, K.Y.1    Erdjument-Bromage, H.2    Tempst, P.3    Nathan, C.F.4
  • 188
    • 42549107897 scopus 로고    scopus 로고
    • Oxidant-dependent switching between reversible and sacrificial oxidation pathways for Bacillus subtilis OhrR
    • Soonsanga, S., Lee, J.-W., and Helmann, J. D. (2008) Oxidant-dependent switching between reversible and sacrificial oxidation pathways for Bacillus subtilis OhrR Mol. Microbiol. 68, 978-986
    • (2008) Mol. Microbiol. , vol.68 , pp. 978-986
    • Soonsanga, S.1    Lee, J.-W.2    Helmann, J.D.3
  • 190
    • 0141492988 scopus 로고    scopus 로고
    • Thiol-based regulatory switches
    • Paget, M. S. and Buttner, M. J. (2003) Thiol-based regulatory switches Annu. Rev. Genet. 37, 91-121
    • (2003) Annu. Rev. Genet. , vol.37 , pp. 91-121
    • Paget, M.S.1    Buttner, M.J.2
  • 191
    • 77956229209 scopus 로고    scopus 로고
    • Structural insight into the oxidation-sensing mechanism of the antibiotic resistance of regulator MexR
    • Chen, H., Yi, C., Zhang, J., Zhang, W., Ge, Z., Yang, C. G., and He, C. (2010) Structural insight into the oxidation-sensing mechanism of the antibiotic resistance of regulator MexR EMBO Rep. 11, 685-690
    • (2010) EMBO Rep. , vol.11 , pp. 685-690
    • Chen, H.1    Yi, C.2    Zhang, J.3    Zhang, W.4    Ge, Z.5    Yang, C.G.6    He, C.7


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