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Volumn 2, Issue 3, 2014, Pages

The physiology and genetics of oxidative stress in mycobacteria

Author keywords

[No Author keywords available]

Indexed keywords

ANTIOXIDANT; FREE RADICAL;

EID: 84956706134     PISSN: None     EISSN: 21650497     Source Type: Journal    
DOI: 10.1128/microbiolspec.MGM2-0019-2013     Document Type: Article
Times cited : (28)

References (223)
  • 2
    • 37349033017 scopus 로고    scopus 로고
    • Drugs versus bugs: in pursuit of the persistent predator Mycobacterium tuberculosis
    • Sacchettini JC, Rubin EJ, Freundlich JS. 2008. Drugs versus bugs: in pursuit of the persistent predator Mycobacterium tuberculosis. Nat Rev Microbiol 6:41-52.
    • (2008) Nat Rev Microbiol , vol.6 , pp. 41-52
    • Sacchettini, J.C.1    Rubin, E.J.2    Freundlich, J.S.3
  • 5
    • 0035371184 scopus 로고    scopus 로고
    • Redox environment of the cell as viewed through the redox state of the glutathione disulfide/glutathione couple
    • Schafer FQ, Buettner GR. 2001. Redox environment of the cell as viewed through the redox state of the glutathione disulfide/glutathione couple. Free Radic Biol Med 30:1191-1212.
    • (2001) Free Radic Biol Med , vol.30 , pp. 1191-1212
    • Schafer, F.Q.1    Buettner, G.R.2
  • 6
    • 58849148335 scopus 로고    scopus 로고
    • Quantifying the global cellular thiol-disulfide status
    • Hansen RE, Roth D, Winther JR. 2009. Quantifying the global cellular thiol-disulfide status. Proc Natl Acad Sci USA 106:422-427.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 422-427
    • Hansen, R.E.1    Roth, D.2    Winther, J.R.3
  • 11
    • 0031980127 scopus 로고    scopus 로고
    • NADH dehydrogenase defects confer isoniazid resistance and conditional lethality in Mycobacterium smegmatis
    • Miesel L, Weisbrod TR, Marcinkeviciene JA, Bittman R, Jacobs WR, Jr. 1998. NADH dehydrogenase defects confer isoniazid resistance and conditional lethality in Mycobacterium smegmatis. J Bacteriol 180:2459-2467.
    • (1998) J Bacteriol , vol.180 , pp. 2459-2467
    • Miesel, L.1    Weisbrod, T.R.2    Marcinkeviciene, J.A.3    Bittman, R.4    Jacobs, W.R.5
  • 12
    • 79959226734 scopus 로고    scopus 로고
    • Precise null deletion mutations of the mycothiol synthesis genes reveal their role in isoniazid and ethionamide resistance in Mycobacterium smegmatis
    • Xu X, Vilcheze C, Av-Gay Y, Gomez-Velasco A, Jacobs WR, Jr. 2011. Precise null deletion mutations of the mycothiol synthesis genes reveal their role in isoniazid and ethionamide resistance in Mycobacterium smegmatis. Antimicrob Agents Chemother 55:3133-3139.
    • (2011) Antimicrob Agents Chemother , vol.55 , pp. 3133-3139
    • Xu, X.1    Vilcheze, C.2    Av-Gay, Y.3    Gomez-Velasco, A.4    Jacobs, W.R.5
  • 13
    • 33846794822 scopus 로고    scopus 로고
    • The NOX family of ROS-generating NADPH oxidases: physiology and pathophysiology
    • Bedard K, Krause KH. 2007. The NOX family of ROS-generating NADPH oxidases: physiology and pathophysiology. Physiol Rev 87:245-313.
    • (2007) Physiol Rev , vol.87 , pp. 245-313
    • Bedard, K.1    Krause, K.H.2
  • 14
    • 0026549480 scopus 로고
    • Killing of virulent Mycobacterium tuberculosis by reactive nitrogen intermediates produced by activated murine macrophages
    • Chan J, Xing Y, Magliozzo RS, Bloom BR. 1992. Killing of virulent Mycobacterium tuberculosis by reactive nitrogen intermediates produced by activated murine macrophages. J Exp Med 175:1111-1122.
    • (1992) J Exp Med , vol.175 , pp. 1111-1122
    • Chan, J.1    Xing, Y.2    Magliozzo, R.S.3    Bloom, B.R.4
  • 15
    • 0028936417 scopus 로고
    • Effects of nitric oxide synthase inhibitors on murine infection with Mycobacterium tuberculosis
    • Chan J, Tanaka K, Carroll D, Flynn J, Bloom BR. 1995. Effects of nitric oxide synthase inhibitors on murine infection with Mycobacterium tuberculosis. Infect Immun 63:736-740.
    • (1995) Infect Immun , vol.63 , pp. 736-740
    • Chan, J.1    Tanaka, K.2    Carroll, D.3    Flynn, J.4    Bloom, B.R.5
  • 16
    • 0018881804 scopus 로고
    • Recent advances in epidemiological research in tuberculosis
    • Styblo K. 1980. Recent advances in epidemiological research in tuberculosis. Adv Tuberc Res 20:1-63.
    • (1980) Adv Tuberc Res , vol.20 , pp. 1-63
    • Styblo, K.1
  • 18
    • 58149107469 scopus 로고    scopus 로고
    • Impact of oxidative stress on lung diseases
    • Park HS, Kim SR, Lee YC. 2009. Impact of oxidative stress on lung diseases. Respirology 14:2-38.
    • (2009) Respirology , vol.14 , pp. 2-38
    • Park, H.S.1    Kim, S.R.2    Lee, Y.C.3
  • 19
    • 77956257800 scopus 로고    scopus 로고
    • Oxidative stress: acute and progressive lung injury
    • Ward PA. 2010. Oxidative stress: acute and progressive lung injury. Ann NY Acad Sci 1203:53-59.
    • (2010) Ann NY Acad Sci , vol.1203 , pp. 53-59
    • Ward, P.A.1
  • 20
    • 33644781601 scopus 로고    scopus 로고
    • Oxidant and antioxidant balance in the airways and airway diseases
    • Rahman I, Biswas SK, Kode A. 2006. Oxidant and antioxidant balance in the airways and airway diseases. Eur J Pharmacol 533:222-239.
    • (2006) Eur J Pharmacol , vol.533 , pp. 222-239
    • Rahman, I.1    Biswas, S.K.2    Kode, A.3
  • 21
    • 84872808481 scopus 로고    scopus 로고
    • Chronic-alcohol-abuseinduced oxidative stress in the development of acute respiratory distress syndrome
    • Liang Y, Yeligar SM, Brown LA. 2012. Chronic-alcohol-abuseinduced oxidative stress in the development of acute respiratory distress syndrome. Sci World J 2012:740308.
    • (2012) Sci World J , vol.2012
    • Liang, Y.1    Yeligar, S.M.2    Brown, L.A.3
  • 24
    • 37349010344 scopus 로고    scopus 로고
    • Non-invasive evaluation of pulmonary glutathione in the exhaled breath condensate of otherwise healthy alcoholics
    • Yeh MY, Burnham EL, Moss M, Brown LA. 2008. Non-invasive evaluation of pulmonary glutathione in the exhaled breath condensate of otherwise healthy alcoholics. Respir Med 102:248-255.
    • (2008) Respir Med , vol.102 , pp. 248-255
    • Yeh, M.Y.1    Burnham, E.L.2    Moss, M.3    Brown, L.A.4
  • 26
    • 77049229538 scopus 로고
    • The treated pulmonary lesion and its tubercle bacillus. II. The death and resurrection
    • passim
    • Vandiviere HM, Loring WE, Melvin I, Willis S. 1956. The treated pulmonary lesion and its tubercle bacillus. II. The death and resurrection. Am J Med Sci 232:30-37; passim.
    • (1956) Am J Med Sci , vol.232 , pp. 30-37
    • Vandiviere, H.M.1    Loring, W.E.2    Melvin, I.3    Willis, S.4
  • 27
    • 0029976980 scopus 로고    scopus 로고
    • An in vitro model for sequential study of shiftdown of Mycobacterium tuberculosis through two stages of nonreplicating persistence
    • Wayne LG, Hayes LG. 1996. An in vitro model for sequential study of shiftdown of Mycobacterium tuberculosis through two stages of nonreplicating persistence. Infect Immun 64:2062-2069.
    • (1996) Infect Immun , vol.64 , pp. 2062-2069
    • Wayne, L.G.1    Hayes, L.G.2
  • 28
    • 0026569136 scopus 로고
    • Reduced intracellular growth of mycobacteria in human macrophages cultivated at physiologic oxygen pressure
    • Meylan PR, Richman DD, Kornbluth RS. 1992. Reduced intracellular growth of mycobacteria in human macrophages cultivated at physiologic oxygen pressure. Am Rev Respir Dis 145:947-953.
    • (1992) Am Rev Respir Dis , vol.145 , pp. 947-953
    • Meylan, P.R.1    Richman, D.D.2    Kornbluth, R.S.3
  • 29
    • 11144250804 scopus 로고    scopus 로고
    • Tuberculosis: metabolism and respiration in the absence of growth
    • Boshoff HI, Barry CE, 3rd. 2005. Tuberculosis: metabolism and respiration in the absence of growth. Nat Rev Microbiol 3:70-80.
    • (2005) Nat Rev Microbiol , vol.3 , pp. 70-80
    • Boshoff, H.I.1    Barry, C.E.2
  • 31
    • 77949356979 scopus 로고    scopus 로고
    • The Mycobacterium tuberculosis DosR regulon assists in metabolic homeostasis and enables rapid recovery from nonrespiring dormancy
    • Leistikow RL, Morton RA, Bartek IL, Frimpong I, Wagner K, Voskuil MI. 2010. The Mycobacterium tuberculosis DosR regulon assists in metabolic homeostasis and enables rapid recovery from nonrespiring dormancy. J Bacteriol 192:1662-1670.
    • (2010) J Bacteriol , vol.192 , pp. 1662-1670
    • Leistikow, R.L.1    Morton, R.A.2    Bartek, I.L.3    Frimpong, I.4    Wagner, K.5    Voskuil, M.I.6
  • 34
    • 43049170080 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis senses host-derived carbon monoxide during macrophage infection
    • Shiloh MU, Manzanillo P, Cox JS. 2008. Mycobacterium tuberculosis senses host-derived carbon monoxide during macrophage infection. Cell Host Microbe 3:323-330.
    • (2008) Cell Host Microbe , vol.3 , pp. 323-330
    • Shiloh, M.U.1    Manzanillo, P.2    Cox, J.S.3
  • 35
    • 34147117736 scopus 로고    scopus 로고
    • DevS, a heme-containing two-component oxygen sensor of Mycobacterium tuberculosis
    • Ioanoviciu A, Yukl ET, Moenne-Loccoz P, de Montellano PR. 2007. DevS, a heme-containing two-component oxygen sensor of Mycobacterium tuberculosis. Biochemistry 46:4250-4260.
    • (2007) Biochemistry , vol.46 , pp. 4250-4260
    • Ioanoviciu, A.1    Yukl, E.T.2    Moenne-Loccoz, P.3    de Montellano, P.R.4
  • 36
  • 39
    • 0033983745 scopus 로고    scopus 로고
    • Multiple paralogous genes related to the Streptomyces coelicolor developmental regulatory gene whiB are present in Streptomyces and other actinomycetes
    • Soliveri JA, Gomez J, Bishai WR, Chater KF. 2000. Multiple paralogous genes related to the Streptomyces coelicolor developmental regulatory gene whiB are present in Streptomyces and other actinomycetes. Microbiology 146:333-343.
    • (2000) Microbiology , vol.146 , pp. 333-343
    • Soliveri, J.A.1    Gomez, J.2    Bishai, W.R.3    Chater, K.F.4
  • 40
    • 0037022605 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis WhiB3 interacts with RpoV to affect host survival but is dispensable for in vivo growth
    • Steyn AJ, Collins DM, Hondalus MK, Jacobs WR, Jr, Kawakami RP, Bloom BR. 2002. Mycobacterium tuberculosis WhiB3 interacts with RpoV to affect host survival but is dispensable for in vivo growth. Proc Natl Acad Sci USA 99:3147-3152.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 3147-3152
    • Steyn, A.J.1    Collins, D.M.2    Hondalus, M.K.3    Jacobs, W.R.4    Kawakami, R.P.5    Bloom, B.R.6
  • 41
    • 26844571035 scopus 로고    scopus 로고
    • The whcE gene of Corynebacterium glutamicum is important for survival following heat and oxidative stress
    • Kim TH, Park JS, Kim HJ, Kim Y, Kim P, Lee HS. 2005. The whcE gene of Corynebacterium glutamicum is important for survival following heat and oxidative stress. Biochem Biophys Res Commun 337:757-764.
    • (2005) Biochem Biophys Res Commun , vol.337 , pp. 757-764
    • Kim, T.H.1    Park, J.S.2    Kim, H.J.3    Kim, Y.4    Kim, P.5    Lee, H.S.6
  • 43
    • 84864050604 scopus 로고    scopus 로고
    • Gene expression of Mycobacterium tuberculosis putative transcription factors whiB1-7 in redox environments
    • Larsson C, Luna B, Ammerman NC, Maiga M, Agarwal N, Bishai WR. 2012. Gene expression of Mycobacterium tuberculosis putative transcription factors whiB1-7 in redox environments. PLoS One 7: e37516.
    • (2012) PLoS One , vol.7
    • Larsson, C.1    Luna, B.2    Ammerman, N.C.3    Maiga, M.4    Agarwal, N.5    Bishai, W.R.6
  • 44
    • 70149116303 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis WhiB3 maintains redox homeostasis by regulating virulence lipid anabolism to modulate macrophage response
    • Singh A, Crossman DK, Mai D, Guidry L, Voskuil MI, Renfrow MB, Steyn AJ. 2009. Mycobacterium tuberculosis WhiB3 maintains redox homeostasis by regulating virulence lipid anabolism to modulate macrophage response. PLoS Pathog 5:e1000545.
    • (2009) PLoS Pathog , vol.5
    • Singh, A.1    Crossman, D.K.2    Mai, D.3    Guidry, L.4    Voskuil, M.I.5    Renfrow, M.B.6    Steyn, A.J.7
  • 46
    • 0041827138 scopus 로고    scopus 로고
    • The effects of reactive nitrogen intermediates on gene expression in Mycobacterium tuberculosis
    • Ohno H, Zhu G, Mohan VP, Chu D, Kohno S, Jacobs WR, Jr, Chan J. 2003. The effects of reactive nitrogen intermediates on gene expression in Mycobacterium tuberculosis. Cell Microbiol 5:637-648.
    • (2003) Cell Microbiol , vol.5 , pp. 637-648
    • Ohno, H.1    Zhu, G.2    Mohan, V.P.3    Chu, D.4    Kohno, S.5    Jacobs, W.R.6    Chan, J.7
  • 47
    • 3042838120 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis gene expression during adaptation to stationary phase and lowoxygen dormancy
    • Voskuil MI, Visconti KC, Schoolnik GK. 2004. Mycobacterium tuberculosis gene expression during adaptation to stationary phase and lowoxygen dormancy. Tuberculosis (Edinb) 84:218-227.
    • (2004) Tuberculosis (Edinb) , vol.84 , pp. 218-227
    • Voskuil, M.I.1    Visconti, K.C.2    Schoolnik, G.K.3
  • 48
    • 0036270739 scopus 로고    scopus 로고
    • Evaluation of a nutrient starvation model of Mycobacterium tuberculosis persistence by gene and protein expression profiling
    • Betts JC, Lukey PT, Robb LC, McAdam RA, Duncan K. 2002. Evaluation of a nutrient starvation model of Mycobacterium tuberculosis persistence by gene and protein expression profiling. Mol Microbiol 43: 717-731.
    • (2002) Mol Microbiol , vol.43 , pp. 717-731
    • Betts, J.C.1    Lukey, P.T.2    Robb, L.C.3    McAdam, R.A.4    Duncan, K.5
  • 49
    • 43049182981 scopus 로고    scopus 로고
    • The enduring hypoxic response of Mycobacterium tuberculosis
    • Rustad TR, Harrell MI, Liao R, Sherman DR. 2008. The enduring hypoxic response of Mycobacterium tuberculosis. PLoS One 3:e1502.
    • (2008) PLoS One , vol.3
    • Rustad, T.R.1    Harrell, M.I.2    Liao, R.3    Sherman, D.R.4
  • 53
    • 84868146046 scopus 로고    scopus 로고
    • WhiB7, a transcriptional activator that coordinates physiology with intrinsic drug resistance in Mycobacterium tuberculosis
    • Burian J, Ramon-Garcia S, Howes CG, Thompson CJ. 2012. WhiB7, a transcriptional activator that coordinates physiology with intrinsic drug resistance in Mycobacterium tuberculosis. Expert Rev Anti Infect Ther 10: 1037-1047.
    • (2012) Expert Rev Anti Infect Ther , vol.10 , pp. 1037-1047
    • Burian, J.1    Ramon-Garcia, S.2    Howes, C.G.3    Thompson, C.J.4
  • 54
    • 0033582933 scopus 로고    scopus 로고
    • Bridge over troubled waters: sensing stress by disulfide bond formation
    • Aslund F, Beckwith J. 1999. Bridge over troubled waters: sensing stress by disulfide bond formation. Cell 96:751-753.
    • (1999) Cell , vol.96 , pp. 751-753
    • Aslund, F.1    Beckwith, J.2
  • 55
    • 84859645414 scopus 로고    scopus 로고
    • The response of Mycobacterium tuberculosis to reactive oxygen and nitrogen species
    • Voskuil MI, Bartek IL, Visconti K, Schoolnik GK. 2011. The response of Mycobacterium tuberculosis to reactive oxygen and nitrogen species. Front Microbiol 2:105.
    • (2011) Front Microbiol , vol.2 , pp. 105
    • Voskuil, M.I.1    Bartek, I.L.2    Visconti, K.3    Schoolnik, G.K.4
  • 56
    • 77952046005 scopus 로고    scopus 로고
    • The SigF regulon in Mycobacterium smegmatis reveals roles in adaptation to stationary phase, heat, and oxidative stress
    • Humpel A, Gebhard S, Cook GM, Berney M. 2010. The SigF regulon in Mycobacterium smegmatis reveals roles in adaptation to stationary phase, heat, and oxidative stress. J Bacteriol 192:2491-2502.
    • (2010) J Bacteriol , vol.192 , pp. 2491-2502
    • Humpel, A.1    Gebhard, S.2    Cook, G.M.3    Berney, M.4
  • 57
    • 26444518218 scopus 로고    scopus 로고
    • The Mycobacterium tuberculosis extracytoplasmic-function sigma factor SigL regulates polyketide synthases and secreted or membrane proteins and is required for virulence
    • Hahn MY, Raman S, Anaya M, Husson RN. 2005. The Mycobacterium tuberculosis extracytoplasmic-function sigma factor SigL regulates polyketide synthases and secreted or membrane proteins and is required for virulence. J Bacteriol 187:7062-7071.
    • (2005) J Bacteriol , vol.187 , pp. 7062-7071
    • Hahn, M.Y.1    Raman, S.2    Anaya, M.3    Husson, R.N.4
  • 58
    • 77950517981 scopus 로고    scopus 로고
    • Structural and biochemical bases for the redox sensitivity of Mycobacterium tuberculosis RslA
    • Thakur KG, Praveena T, Gopal B. 2010. Structural and biochemical bases for the redox sensitivity of Mycobacterium tuberculosis RslA. J Mol Biol 397:1199-1208.
    • (2010) J Mol Biol , vol.397 , pp. 1199-1208
    • Thakur, K.G.1    Praveena, T.2    Gopal, B.3
  • 59
    • 0242521392 scopus 로고    scopus 로고
    • RshA, an anti-sigma factor that regulates the activity of the mycobacterial stress response sigma factor SigH
    • Song T, Dove SL, Lee KH, Husson RN. 2003. RshA, an anti-sigma factor that regulates the activity of the mycobacterial stress response sigma factor SigH. Mol Microbiol 50:949-959.
    • (2003) Mol Microbiol , vol.50 , pp. 949-959
    • Song, T.1    Dove, S.L.2    Lee, K.H.3    Husson, R.N.4
  • 60
    • 75149132523 scopus 로고    scopus 로고
    • RseA, the SigE specific anti-sigma factor of Mycobacterium tuberculosis, is inactivated by phosphorylation-dependent ClpC1P2 proteolysis
    • Barik S, Sureka K, Mukherjee P, Basu J, Kundu M. 2010. RseA, the SigE specific anti-sigma factor of Mycobacterium tuberculosis, is inactivated by phosphorylation-dependent ClpC1P2 proteolysis. Mol Microbiol 75:592-606.
    • (2010) Mol Microbiol , vol.75 , pp. 592-606
    • Barik, S.1    Sureka, K.2    Mukherjee, P.3    Basu, J.4    Kundu, M.5
  • 61
    • 0141645618 scopus 로고    scopus 로고
    • The role of zinc in the disulphide stress-regulated anti-sigma factor RsrA from Streptomyces coelicolor
    • Li W, Bottrill AR, Bibb MJ, Buttner MJ, Paget MS, Kleanthous C. 2003. The role of zinc in the disulphide stress-regulated anti-sigma factor RsrA from Streptomyces coelicolor. J Mol Biol 333:461-472.
    • (2003) J Mol Biol , vol.333 , pp. 461-472
    • Li, W.1    Bottrill, A.R.2    Bibb, M.J.3    Buttner, M.J.4    Paget, M.S.5    Kleanthous, C.6
  • 62
    • 0035116721 scopus 로고    scopus 로고
    • Mutational analysis of RsrA, a zinc-binding anti-sigma factor with a thiol-disulphide redox switch
    • Paget MS, Bae JB, Hahn MY, Li W, Kleanthous C, Roe JH, Buttner MJ. 2001. Mutational analysis of RsrA, a zinc-binding anti-sigma factor with a thiol-disulphide redox switch. Mol Microbiol 39:1036-1047.
    • (2001) Mol Microbiol , vol.39 , pp. 1036-1047
    • Paget, M.S.1    Bae, J.B.2    Hahn, M.Y.3    Li, W.4    Kleanthous, C.5    Roe, J.H.6    Buttner, M.J.7
  • 64
    • 20444419421 scopus 로고    scopus 로고
    • Genome-wide requirements for Mycobacterium tuberculosis adaptation and survival in macrophages
    • Rengarajan J, Bloom BR, Rubin EJ. 2005. Genome-wide requirements for Mycobacterium tuberculosis adaptation and survival in macrophages. Proc Natl Acad Sci USA 102:8327-8332.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 8327-8332
    • Rengarajan, J.1    Bloom, B.R.2    Rubin, E.J.3
  • 66
    • 0025852089 scopus 로고
    • Lipoarabinomannan, a possible virulence factor involved in persistence of Mycobacterium tuberculosis within macrophages
    • Chan J, Fan XD, Hunter SW, Brennan PJ, Bloom BR. 1991. Lipoarabinomannan, a possible virulence factor involved in persistence of Mycobacterium tuberculosis within macrophages. Infect Immun 59: 1755-1761.
    • (1991) Infect Immun , vol.59 , pp. 1755-1761
    • Chan, J.1    Fan, X.D.2    Hunter, S.W.3    Brennan, P.J.4    Bloom, B.R.5
  • 67
    • 0023858089 scopus 로고
    • Inhibition of macrophage priming by sulfatide from Mycobacterium tuberculosis
    • Pabst MJ, Gross JM, Brozna JP, Goren MB. 1988. Inhibition of macrophage priming by sulfatide from Mycobacterium tuberculosis. J Immunol 140:634-640.
    • (1988) J Immunol , vol.140 , pp. 634-640
    • Pabst, M.J.1    Gross, J.M.2    Brozna, J.P.3    Goren, M.B.4
  • 74
    • 0025965210 scopus 로고
    • Genetic analysis of superoxide dismutase, the 23 kilodalton antigen of Mycobacterium tuberculosis
    • Zhang Y, Lathigra R, Garbe T, Catty D, Young D. 1991. Genetic analysis of superoxide dismutase, the 23 kilodalton antigen of Mycobacterium tuberculosis. Mol Microbiol 5:381-391.
    • (1991) Mol Microbiol , vol.5 , pp. 381-391
    • Zhang, Y.1    Lathigra, R.2    Garbe, T.3    Catty, D.4    Young, D.5
  • 75
    • 0033548095 scopus 로고    scopus 로고
    • Export of recombinant Mycobacterium tuberculosis superoxide dismutase is dependent upon both information in the protein and mycobacterial export machinery. A model for studying export of leaderless proteins by pathogenic mycobacteria
    • Harth G, Horwitz MA. 1999. Export of recombinant Mycobacterium tuberculosis superoxide dismutase is dependent upon both information in the protein and mycobacterial export machinery. A model for studying export of leaderless proteins by pathogenic mycobacteria. J Biol Chem 274:4281-4292.
    • (1999) J Biol Chem , vol.274 , pp. 4281-4292
    • Harth, G.1    Horwitz, M.A.2
  • 76
    • 0037673252 scopus 로고    scopus 로고
    • SecA2 functions in the secretion of superoxide dismutase A and in the virulence of Mycobacterium tuberculosis
    • Braunstein M, Espinosa BJ, Chan J, Belisle JT, Jacobs WR, Jr. 2003. SecA2 functions in the secretion of superoxide dismutase A and in the virulence of Mycobacterium tuberculosis. Mol Microbiol 48:453-464.
    • (2003) Mol Microbiol , vol.48 , pp. 453-464
    • Braunstein, M.1    Espinosa, B.J.2    Chan, J.3    Belisle, J.T.4    Jacobs, W.R.5
  • 77
    • 0348049821 scopus 로고    scopus 로고
    • Role of prokaryotic Cu, Zn superoxide dismutase in pathogenesis
    • Battistoni A. 2003. Role of prokaryotic Cu, Zn superoxide dismutase in pathogenesis. Biochem Soc Trans 31:1326-1329.
    • (2003) Biochem Soc Trans , vol.31 , pp. 1326-1329
    • Battistoni, A.1
  • 78
    • 0032515092 scopus 로고    scopus 로고
    • Identification and subcellular localization of a novel Cu, Zn superoxide dismutase of Mycobacterium tuberculosis
    • Wu CH, Tsai-Wu JJ, Huang YT, Lin CY, Lioua GG, Lee FJ. 1998. Identification and subcellular localization of a novel Cu, Zn superoxide dismutase of Mycobacterium tuberculosis. FEBS Lett 439:192-196.
    • (1998) FEBS Lett , vol.439 , pp. 192-196
    • Wu, C.H.1    Tsai-Wu, J.J.2    Huang, Y.T.3    Lin, C.Y.4    Lioua, G.G.5    Lee, F.J.6
  • 79
    • 0034917354 scopus 로고    scopus 로고
    • Cu, Zn superoxide dismutase of Mycobacterium tuberculosis contributes to survival in activated macrophages that are generating an oxidative burst
    • Piddington DL, Fang FC, Laessig T, Cooper AM, Orme IM, Buchmeier NA. 2001. Cu, Zn superoxide dismutase of Mycobacterium tuberculosis contributes to survival in activated macrophages that are generating an oxidative burst. Infect Immun 69:4980-4987.
    • (2001) Infect Immun , vol.69 , pp. 4980-4987
    • Piddington, D.L.1    Fang, F.C.2    Laessig, T.3    Cooper, A.M.4    Orme, I.M.5    Buchmeier, N.A.6
  • 80
    • 0018639058 scopus 로고
    • Purification and characterization of hydroperoxidase II of Escherichia coli B
    • Claiborne A, Malinowski DP, Fridovich I. 1979. Purification and characterization of hydroperoxidase II of Escherichia coli B. J Biol Chem 254:11664-11668.
    • (1979) J Biol Chem , vol.254 , pp. 11664-11668
    • Claiborne, A.1    Malinowski, D.P.2    Fridovich, I.3
  • 81
    • 0016251335 scopus 로고
    • Isolation and characterization of catalase produced by Mycobacterium tuberculosis
    • Diaz GA, Wayne LG. 1974. Isolation and characterization of catalase produced by Mycobacterium tuberculosis. Am Rev Respir Dis 110:312-319.
    • (1974) Am Rev Respir Dis , vol.110 , pp. 312-319
    • Diaz, G.A.1    Wayne, L.G.2
  • 83
    • 0031957229 scopus 로고    scopus 로고
    • Expression of katG in Mycobacterium tuberculosis is associated with its growth and persistence in mice and guinea pigs
    • Li Z, Kelley C, Collins F, Rouse D, Morris S. 1998. Expression of katG in Mycobacterium tuberculosis is associated with its growth and persistence in mice and guinea pigs. J Infect Dis 177:1030-1035.
    • (1998) J Infect Dis , vol.177 , pp. 1030-1035
    • Li, Z.1    Kelley, C.2    Collins, F.3    Rouse, D.4    Morris, S.5
  • 84
    • 0030893650 scopus 로고    scopus 로고
    • Detection of resistance to isoniazid, rifampin, and streptomycin in clinical isolates of Mycobacterium tuberculosis by molecular methods
    • Nachamkin I, Kang C, Weinstein MP. 1997. Detection of resistance to isoniazid, rifampin, and streptomycin in clinical isolates of Mycobacterium tuberculosis by molecular methods. Clin Infect Dis 24:894-900.
    • (1997) Clin Infect Dis , vol.24 , pp. 894-900
    • Nachamkin, I.1    Kang, C.2    Weinstein, M.P.3
  • 85
    • 0033711560 scopus 로고    scopus 로고
    • Mutations at amino acid position 315 of the katG gene are associated with high-level resistance to isoniazid, other drug resistance, and successful transmission of Mycobacterium tuberculosis in the Netherlands
    • van Soolingen D, de Haas PE, van Doorn HR, Kuijper E, Rinder H, Borgdorff MW. 2000. Mutations at amino acid position 315 of the katG gene are associated with high-level resistance to isoniazid, other drug resistance, and successful transmission of Mycobacterium tuberculosis in the Netherlands. J Infect Dis 182:1788-1790.
    • (2000) J Infect Dis , vol.182 , pp. 1788-1790
    • van Soolingen, D.1    de Haas, P.E.2    van Doorn, H.R.3    Kuijper, E.4    Rinder, H.5    Borgdorff, M.W.6
  • 87
    • 0029915633 scopus 로고    scopus 로고
    • ahpC, a gene involved in isoniazid resistance of the Mycobacterium tuberculosis complex
    • Wilson TM, Collins DM. 1996. ahpC, a gene involved in isoniazid resistance of the Mycobacterium tuberculosis complex. Mol Microbiol 19: 1025-1034.
    • (1996) Mol Microbiol , vol.19 , pp. 1025-1034
    • Wilson, T.M.1    Collins, D.M.2
  • 88
    • 0036772990 scopus 로고    scopus 로고
    • Oxidative stress response genes in Mycobacterium tuberculosis: role of ahpC in resistance to peroxynitrite and stage-specific survival in macrophages
    • Master SS, Springer B, Sander P, Boettger EC, Deretic V, Timmins GS. 2002. Oxidative stress response genes in Mycobacterium tuberculosis: role of ahpC in resistance to peroxynitrite and stage-specific survival in macrophages. Microbiology 148:3139-3144.
    • (2002) Microbiology , vol.148 , pp. 3139-3144
    • Master, S.S.1    Springer, B.2    Sander, P.3    Boettger, E.C.4    Deretic, V.5    Timmins, G.S.6
  • 89
    • 0033102656 scopus 로고    scopus 로고
    • Reduction of peroxides and dinitrobenzenes by Mycobacterium tuberculosis thioredoxin and thioredoxin reductase
    • Zhang Z, Hillas PJ, Ortiz de Montellano PR. 1999. Reduction of peroxides and dinitrobenzenes by Mycobacterium tuberculosis thioredoxin and thioredoxin reductase. Arch Biochem Biophys 363:19-26.
    • (1999) Arch Biochem Biophys , vol.363 , pp. 19-26
    • Zhang, Z.1    Hillas, P.J.2    Ortiz de Montellano, P.R.3
  • 90
    • 0037039818 scopus 로고    scopus 로고
    • Metabolic enzymes of mycobacteria linked to antioxidant defense by a thioredoxin-like protein
    • Bryk R, Lima CD, Erdjument-Bromage H, Tempst P, Nathan C. 2002. Metabolic enzymes of mycobacteria linked to antioxidant defense by a thioredoxin-like protein. Science 295:1073-1077.
    • (2002) Science , vol.295 , pp. 1073-1077
    • Bryk, R.1    Lima, C.D.2    Erdjument-Bromage, H.3    Tempst, P.4    Nathan, C.5
  • 92
    • 38749106235 scopus 로고    scopus 로고
    • Peroxiredoxin systems in mycobacteria
    • Jaeger T. 2007. Peroxiredoxin systems in mycobacteria. Subcell Biochem 44:207-217.
    • (2007) Subcell Biochem , vol.44 , pp. 207-217
    • Jaeger, T.1
  • 94
    • 0029165589 scopus 로고
    • Thioredoxin: a fold for all reasons
    • Martin JL. 1995. Thioredoxin: a fold for all reasons. Structure 3:245-250.
    • (1995) Structure , vol.3 , pp. 245-250
    • Martin, J.L.1
  • 95
    • 0028785378 scopus 로고
    • Mechanism and structure of thioredoxin reductase from Escherichia coli
    • Williams CH, Jr. 1995. Mechanism and structure of thioredoxin reductase from Escherichia coli. FASEB J 9:1267-1276.
    • (1995) FASEB J , vol.9 , pp. 1267-1276
    • Williams, C.H.1
  • 96
    • 0042768090 scopus 로고    scopus 로고
    • Protein disulfide bond formation in prokaryotes
    • Kadokura H, Katzen F, Beckwith J. 2003. Protein disulfide bond formation in prokaryotes. Annu Rev Biochem 72:111-135.
    • (2003) Annu Rev Biochem , vol.72 , pp. 111-135
    • Kadokura, H.1    Katzen, F.2    Beckwith, J.3
  • 97
    • 55749110937 scopus 로고    scopus 로고
    • Functional studies of multiple thioredoxins from Mycobacterium tuberculosis
    • Akif M, Khare G, Tyagi AK, Mande SC, Sardesai AA. 2008. Functional studies of multiple thioredoxins from Mycobacterium tuberculosis. J Bacteriol 190:7087-7095.
    • (2008) J Bacteriol , vol.190 , pp. 7087-7095
    • Akif, M.1    Khare, G.2    Tyagi, A.K.3    Mande, S.C.4    Sardesai, A.A.5
  • 98
    • 0037059826 scopus 로고    scopus 로고
    • Truncated hemoglobins: a new family of hemoglobins widely distributed in bacteria, unicellular eukaryotes, and plants
    • Wittenberg JB, Bolognesi M, Wittenberg BA, Guertin M. 2002. Truncated hemoglobins: a new family of hemoglobins widely distributed in bacteria, unicellular eukaryotes, and plants. J Biol Chem 277:871-874.
    • (2002) J Biol Chem , vol.277 , pp. 871-874
    • Wittenberg, J.B.1    Bolognesi, M.2    Wittenberg, B.A.3    Guertin, M.4
  • 99
    • 34147154024 scopus 로고    scopus 로고
    • Reaction of Mycobacterium tuberculosis truncated hemoglobin O with hydrogen peroxide: evidence for peroxidatic activity and formation of protein-based radicals
    • Ouellet H, Ranguelova K, Labarre M, Wittenberg JB, Wittenberg BA, Magliozzo RS, Guertin M. 2007. Reaction of Mycobacterium tuberculosis truncated hemoglobin O with hydrogen peroxide: evidence for peroxidatic activity and formation of protein-based radicals. J Biol Chem 282:7491-7503.
    • (2007) J Biol Chem , vol.282 , pp. 7491-7503
    • Ouellet, H.1    Ranguelova, K.2    Labarre, M.3    Wittenberg, J.B.4    Wittenberg, B.A.5    Magliozzo, R.S.6    Guertin, M.7
  • 100
    • 35148877224 scopus 로고    scopus 로고
    • Scavenging of reactive nitrogen species by mycobacterial truncated hemoglobins
    • Ascenzi P, Visca P. 2008. Scavenging of reactive nitrogen species by mycobacterial truncated hemoglobins. Methods Enzymol 436:317-337.
    • (2008) Methods Enzymol , vol.436 , pp. 317-337
    • Ascenzi, P.1    Visca, P.2
  • 102
    • 14844327782 scopus 로고    scopus 로고
    • Functional demonstration of reverse transsulfuration in the Mycobacterium tuberculosis complex reveals that methionine is the preferred sulfur source for pathogenic mycobacteria
    • Wheeler PR, Coldham NG, Keating L, Gordon SV, Wooff EE, Parish T, Hewinson RG. 2005. Functional demonstration of reverse transsulfuration in the Mycobacterium tuberculosis complex reveals that methionine is the preferred sulfur source for pathogenic mycobacteria. J Biol Chem 280:8069-8078.
    • (2005) J Biol Chem , vol.280 , pp. 8069-8078
    • Wheeler, P.R.1    Coldham, N.G.2    Keating, L.3    Gordon, S.V.4    Wooff, E.E.5    Parish, T.6    Hewinson, R.G.7
  • 104
    • 12244293660 scopus 로고    scopus 로고
    • S-nitroso proteome of Mycobacterium tuberculosis: enzymes of intermediary metabolism and antioxidant defense
    • Rhee KY, Erdjument-Bromage H, Tempst P, Nathan CF. 2005. S-nitroso proteome of Mycobacterium tuberculosis: enzymes of intermediary metabolism and antioxidant defense. Proc Natl Acad Sci USA 102: 467-472.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 467-472
    • Rhee, K.Y.1    Erdjument-Bromage, H.2    Tempst, P.3    Nathan, C.F.4
  • 105
    • 0035859807 scopus 로고    scopus 로고
    • Peptide methionine sulfoxide reductase from Escherichia coli and Mycobacterium tuberculosis protects bacteria against oxidative damage from reactive nitrogen intermediates
    • St John G, Brot N, Ruan J, Erdjument-Bromage H, Tempst P, Weissbach H, Nathan C. 2001. Peptide methionine sulfoxide reductase from Escherichia coli and Mycobacterium tuberculosis protects bacteria against oxidative damage from reactive nitrogen intermediates. Proc Natl Acad Sci USA 98:9901-9906.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 9901-9906
    • St John, G.1    Brot, N.2    Ruan, J.3    Erdjument-Bromage, H.4    Tempst, P.5    Weissbach, H.6    Nathan, C.7
  • 106
  • 108
    • 2442701595 scopus 로고    scopus 로고
    • Methionine sulfoxide reductase A (MsrA) deficiency affects the survival of Mycobacterium smegmatis within macrophages
    • Douglas T, Daniel DS, Parida BK, Jagannath C, Dhandayuthapani S. 2004. Methionine sulfoxide reductase A (MsrA) deficiency affects the survival of Mycobacterium smegmatis within macrophages. J Bacteriol 186:3590-3598.
    • (2004) J Bacteriol , vol.186 , pp. 3590-3598
    • Douglas, T.1    Daniel, D.S.2    Parida, B.K.3    Jagannath, C.4    Dhandayuthapani, S.5
  • 110
    • 0034775463 scopus 로고    scopus 로고
    • Novel thiols of prokaryotes
    • Fahey RC. 2001. Novel thiols of prokaryotes. Annu Rev Microbiol 55:333-356.
    • (2001) Annu Rev Microbiol , vol.55 , pp. 333-356
    • Fahey, R.C.1
  • 111
    • 0032508871 scopus 로고    scopus 로고
    • Synthesis of Des-myo-Inositol mycothiol and demonstration of a mycobacterial specific reductase activity
    • Patel MP, Blanchard JS. 1998. Synthesis of Des-myo-Inositol mycothiol and demonstration of a mycobacterial specific reductase activity. J Am Chem Soc 120:11538-11539.
    • (1998) J Am Chem Soc , vol.120 , pp. 11538-11539
    • Patel, M.P.1    Blanchard, J.S.2
  • 112
    • 0023733793 scopus 로고
    • Glutathione reductase: solvent equilibrium and kinetic isotope effects
    • Wong KK, Vanoni MA, Blanchard JS. 1988. Glutathione reductase: solvent equilibrium and kinetic isotope effects. Biochemistry 27:7091-7096.
    • (1988) Biochemistry , vol.27 , pp. 7091-7096
    • Wong, K.K.1    Vanoni, M.A.2    Blanchard, J.S.3
  • 113
    • 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
    • del Cardayre SB, Stock KP, Newton GL, Fahey RC, Davies JE. 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
    • del Cardayre, S.B.1    Stock, K.P.2    Newton, G.L.3    Fahey, R.C.4    Davies, J.E.5
  • 115
    • 84871811336 scopus 로고    scopus 로고
    • Bacterial mechanisms of reversible protein S-thiolation: structural and mechanistic insights into mycoredoxins
    • Antelmann H, Hamilton CJ. 2012. Bacterial mechanisms of reversible protein S-thiolation: structural and mechanistic insights into mycoredoxins. Mol Microbiol 86:759-764.
    • (2012) Mol Microbiol , vol.86 , pp. 759-764
    • Antelmann, H.1    Hamilton, C.J.2
  • 116
    • 49349112856 scopus 로고    scopus 로고
    • Redox control in trypanosomatids, parasitic protozoa with trypanothione-based thiol metabolism
    • Krauth-Siegel RL, Comini MA. 2008. Redox control in trypanosomatids, parasitic protozoa with trypanothione-based thiol metabolism. Biochim Biophys Acta 1780:1236-1248.
    • (2008) Biochim Biophys Acta , vol.1780 , pp. 1236-1248
    • Krauth-Siegel, R.L.1    Comini, M.A.2
  • 117
    • 33751050875 scopus 로고    scopus 로고
    • Cloning, expression and rapid purification of active recombinant mycothiol ligase as B1 immunoglobulin binding domain of streptococcal protein G, glutathione-S-transferase and maltose binding protein fusion proteins in Mycobacterium smegmatis
    • Gutierrez-Lugo M-T, Newton GL, Fahey RC, Bewley CA. 2006. Cloning, expression and rapid purification of active recombinant mycothiol ligase as B1 immunoglobulin binding domain of streptococcal protein G, glutathione-S-transferase and maltose binding protein fusion proteins in Mycobacterium smegmatis. Protein Expr Purif 50:128-136.
    • (2006) Protein Expr Purif , vol.50 , pp. 128-136
    • Gutierrez-Lugo, M.-T.1    Newton, G.L.2    Fahey, R.C.3    Bewley, C.A.4
  • 118
    • 82955194511 scopus 로고    scopus 로고
    • The DinB superfamily includes novel mycothiol, bacillithiol, and glutathione S-transferases
    • Newton GL, Leung SS, Wakabayashi JI, Rawat M, Fahey RC. 2011. The DinB superfamily includes novel mycothiol, bacillithiol, and glutathione S-transferases. Biochemistry 50:10751-10760.
    • (2011) Biochemistry , vol.50 , pp. 10751-10760
    • Newton, G.L.1    Leung, S.S.2    Wakabayashi, J.I.3    Rawat, M.4    Fahey, R.C.5
  • 119
    • 84858153376 scopus 로고    scopus 로고
    • Ergothioneine: antioxidant potential, physiological function and role in disease
    • Cheah IK, Halliwell B. 2012. Ergothioneine: antioxidant potential, physiological function and role in disease. Biochim Biophys Acta 1822: 784-793.
    • (2012) Biochim Biophys Acta , vol.1822 , pp. 784-793
    • Cheah, I.K.1    Halliwell, B.2
  • 120
    • 84856890456 scopus 로고    scopus 로고
    • Redox outside the box: linking extracellular redox remodeling with intracellular redox metabolism
    • Banerjee R. 2012. Redox outside the box: linking extracellular redox remodeling with intracellular redox metabolism. J Biol Chem 287:4397-4402.
    • (2012) J Biol Chem , vol.287 , pp. 4397-4402
    • Banerjee, R.1
  • 123
    • 84871596563 scopus 로고    scopus 로고
    • Gasotransmitters are emerging as new guard cell signaling molecules and regulators of leaf gas exchange
    • Garcia-Mata C, Lamattina L. 2013. Gasotransmitters are emerging as new guard cell signaling molecules and regulators of leaf gas exchange. Plant Sci 201-202:66-73.
    • (2013) Plant Sci , vol.201-202 , pp. 66-73
    • Garcia-Mata, C.1    Lamattina, L.2
  • 125
    • 0027267127 scopus 로고
    • Lowmolecular-weight thiols in streptomycetes and their potential role as antioxidants
    • Newton GL, Fahey RC, Cohen G, Aharonowitz Y. 1993. Lowmolecular-weight thiols in streptomycetes and their potential role as antioxidants. J Bacteriol 175:2734-2742.
    • (1993) J Bacteriol , vol.175 , pp. 2734-2742
    • Newton, G.L.1    Fahey, R.C.2    Cohen, G.3    Aharonowitz, Y.4
  • 126
    • 0028469774 scopus 로고
    • Structure of a novel disulfide of 2-(N-acetylcysteinyl)amido-2-deoxy-alpha-D-glucopyran-osyl-myoinositol produced by Streptomyces sp
    • Sakuda S, Zhou Z-Y, Yamada Y. 1994. Structure of a novel disulfide of 2-(N-acetylcysteinyl)amido-2-deoxy-alpha-D-glucopyran-osyl-myoinositol produced by Streptomyces sp. Biosci Biotechnol Biochem 58: 1347-1348.
    • (1994) Biosci Biotechnol Biochem , vol.58 , pp. 1347-1348
    • Sakuda, S.1    Zhou, Z.-Y.2    Yamada, Y.3
  • 127
    • 0027990965 scopus 로고
    • Thiols of intracellular pathogens. Identification of ovothiol A in Leishmania donovani and structural analysis of a novel thiol from Mycobacterium bovis
    • Spies HSC, Steenkamp DJ. 1994. Thiols of intracellular pathogens. Identification of ovothiol A in Leishmania donovani and structural analysis of a novel thiol from Mycobacterium bovis. Eur J Biochem 224:203-213.
    • (1994) Eur J Biochem , vol.224 , pp. 203-213
    • Spies, H.S.C.1    Steenkamp, D.J.2
  • 129
    • 0036118315 scopus 로고    scopus 로고
    • Crystal structure of inositol 1-phosphate synthase from Mycobacterium tuberculosis, a key enzyme in phosphatidylinositol synthesis
    • Norman RA, McAlister MSB, Murray-Rust J, Movahedzadeh F, Stoker NG, McDonald NQ. 2002. Crystal structure of inositol 1-phosphate synthase from Mycobacterium tuberculosis, a key enzyme in phosphatidylinositol synthesis. Structure 10:393-402.
    • (2002) Structure , vol.10 , pp. 393-402
    • Norman, R.A.1    McAlister, M.S.B.2    Murray-Rust, J.3    Movahedzadeh, F.4    Stoker, N.G.5    McDonald, N.Q.6
  • 131
    • 0038662691 scopus 로고    scopus 로고
    • The glycosyltransferase gene encoding the enzyme catalyzing the first step of mycothiol biosynthesis (mshA)
    • Newton GL, Koledin T, Gorovitz B, Rawat M, Fahey RC, Av-Gay Y. 2003. The glycosyltransferase gene encoding the enzyme catalyzing the first step of mycothiol biosynthesis (mshA). J Bacteriol 185:3476-3479.
    • (2003) J Bacteriol , vol.185 , pp. 3476-3479
    • Newton, G.L.1    Koledin, T.2    Gorovitz, B.3    Rawat, M.4    Fahey, R.C.5    Av-Gay, Y.6
  • 132
    • 33845962040 scopus 로고    scopus 로고
    • Biochemistry of the initial steps of mycothiol biosynthesis
    • Newton GL, Ta P, Bzymek KP, Fahey RC. 2006. Biochemistry of the initial steps of mycothiol biosynthesis. J Biol Chem 281:33910-33920.
    • (2006) J Biol Chem , vol.281 , pp. 33910-33920
    • Newton, G.L.1    Ta, P.2    Bzymek, K.P.3    Fahey, R.C.4
  • 133
    • 0034460953 scopus 로고    scopus 로고
    • N-Acetyl-1-D-myo-inosityl-2-amino-2-deoxy-a-D-glucopyranoside deacetylase (MshB) is a key enzyme in mycothiol biosynthesis
    • Newton GL, Av-Gay Y, Fahey RC. 2000.N-Acetyl-1-D-myo-inosityl-2-amino-2-deoxy-a-D-glucopyranoside deacetylase (MshB) is a key enzyme in mycothiol biosynthesis. J Bacteriol 182:6958-6963.
    • (2000) J Bacteriol , vol.182 , pp. 6958-6963
    • Newton, G.L.1    Av-Gay, Y.2    Fahey, R.C.3
  • 134
    • 33646546739 scopus 로고    scopus 로고
    • Purification and characterization of Mycobacterium tuberculosis 1D-myo-inosityl-2-acetamido-2-deoxy-a-D-glucopyranoside deacetylase, MshB, a mycothiol biosynthetic enzyme
    • Newton GL, Ko M, Ta P, Av-Gay Y, Fahey RC. 2006. Purification and characterization of Mycobacterium tuberculosis 1D-myo-inosityl-2-acetamido-2-deoxy-a-D-glucopyranoside deacetylase, MshB, a mycothiol biosynthetic enzyme. Protein Expr Purif 47:542-550.
    • (2006) Protein Expr Purif , vol.47 , pp. 542-550
    • Newton, G.L.1    Ko, M.2    Ta, P.3    Av-Gay, Y.4    Fahey, R.C.5
  • 135
    • 79957983435 scopus 로고    scopus 로고
    • The activity and cofactor preferences of N-acetyl-1-D-myo-inositol-2-amino-2-deoxy-a-Dglucopyranoside deacetylase (MshB) change depending on environmental conditions
    • Huang X, Kocabas E, Hernick M. 2011. The activity and cofactor preferences of N-acetyl-1-D-myo-inositol-2-amino-2-deoxy-a-Dglucopyranoside deacetylase (MshB) change depending on environmental conditions. J Biol Chem 286(23):20275-20282.
    • (2011) J Biol Chem , vol.286 , Issue.23 , pp. 20275-20282
    • Huang, X.1    Kocabas, E.2    Hernick, M.3
  • 136
    • 68049095940 scopus 로고    scopus 로고
    • Toward the catalytic mechanism of a cysteine ligase (MshC) from Mycobacterium smegmatis: an enzyme involved in the biosynthetic pathway of mycothiol
    • Fan F, Blanchard JS. 2009. Toward the catalytic mechanism of a cysteine ligase (MshC) from Mycobacterium smegmatis: an enzyme involved in the biosynthetic pathway of mycothiol. Biochemistry 48: 7150-7159.
    • (2009) Biochemistry , vol.48 , pp. 7150-7159
    • Fan, F.1    Blanchard, J.S.2
  • 137
    • 35048813938 scopus 로고    scopus 로고
    • Steady-state and pre-steady-state kinetic analysis of Mycobacterium smegmatis cysteine ligase (MshC)
    • Fan F, Luxenburger A, Painter GF, Blanchard JS. 2007. Steady-state and pre-steady-state kinetic analysis of Mycobacterium smegmatis cysteine ligase (MshC). Biochemistry 46:11421-11429.
    • (2007) Biochemistry , vol.46 , pp. 11421-11429
    • Fan, F.1    Luxenburger, A.2    Painter, G.F.3    Blanchard, J.S.4
  • 138
    • 0042511920 scopus 로고    scopus 로고
    • Crystal structure of mycothiol synthase (Rv0819) from Mycobacterium tuberculosis shows structural homology to the GNAT family of N-acetyltransferases
    • Vetting MW, Roderick SL, Yu M, Blanchard JS. 2003. Crystal structure of mycothiol synthase (Rv0819) from Mycobacterium tuberculosis shows structural homology to the GNAT family of N-acetyltransferases. Protein Sci 12:1954-1959.
    • (2003) Protein Sci , vol.12 , pp. 1954-1959
    • Vetting, M.W.1    Roderick, S.L.2    Yu, M.3    Blanchard, J.S.4
  • 139
    • 0036401562 scopus 로고    scopus 로고
    • Identification of the mycothiol synthase gene (mshD) encoding the acetyltransferase producing mycothiol in actinomycetes
    • Koledin T, Newton GL, Fahey RC. 2002. Identification of the mycothiol synthase gene (mshD) encoding the acetyltransferase producing mycothiol in actinomycetes. Arch Microbiol 178:331-337.
    • (2002) Arch Microbiol , vol.178 , pp. 331-337
    • Koledin, T.1    Newton, G.L.2    Fahey, R.C.3
  • 140
    • 47049105152 scopus 로고    scopus 로고
    • Structural and enzymatic analysis of MshA from Corynebacterium glutamicum
    • Vetting MW, Frantom PA, Blanchard JS. 2008. Structural and enzymatic analysis of MshA from Corynebacterium glutamicum. J Biol Chem 283:15834-15844.
    • (2008) J Biol Chem , vol.283 , pp. 15834-15844
    • Vetting, M.W.1    Frantom, P.A.2    Blanchard, J.S.3
  • 141
    • 33646367436 scopus 로고    scopus 로고
    • The substrateinduced conformational change of Mycobacterium tuberculosis mycothiol synthase
    • Vetting MW, Yu M, Rendle PM, Blanchard JS. 2006. The substrateinduced conformational change of Mycobacterium tuberculosis mycothiol synthase. J Biol Chem 281:2795-2802.
    • (2006) J Biol Chem , vol.281 , pp. 2795-2802
    • Vetting, M.W.1    Yu, M.2    Rendle, P.M.3    Blanchard, J.S.4
  • 143
    • 28844475855 scopus 로고    scopus 로고
    • Rv2131c gene product: an unconventional enzyme that is both inositol monophosphatase and fructose-1, 6-bisphosphatase
    • Gu X, Chen M, Shen H, Jiang X, Huang Y, Wang H. 2006. Rv2131c gene product: an unconventional enzyme that is both inositol monophosphatase and fructose-1, 6-bisphosphatase. Biochem Biophys Res Commun 339:897-904.
    • (2006) Biochem Biophys Res Commun , vol.339 , pp. 897-904
    • Gu, X.1    Chen, M.2    Shen, H.3    Jiang, X.4    Huang, Y.5    Wang, H.6
  • 144
    • 44349161838 scopus 로고    scopus 로고
    • Rv2131c from Mycobacterium tuberculosis is a CysQ 3'-phosphoadenosine-5'-phosphatase
    • Hatzios SK, Iavarone AT, Bertozzi CR. 2008. Rv2131c from Mycobacterium tuberculosis is a CysQ 3'-phosphoadenosine-5'-phosphatase. Biochemistry 47:5823-5831.
    • (2008) Biochemistry , vol.47 , pp. 5823-5831
    • Hatzios, S.K.1    Iavarone, A.T.2    Bertozzi, C.R.3
  • 145
    • 9644257036 scopus 로고    scopus 로고
    • Chemistry and biology of deoxy-myo-inositol phosphates: stereospecificity of substrate interactions within an archaeal and a bacterial IMPase
    • Morgan AJ, Wang YK, Roberts MF, Miller SJ. 2004. Chemistry and biology of deoxy-myo-inositol phosphates: stereospecificity of substrate interactions within an archaeal and a bacterial IMPase. J Am Chem Soc 126:15370-15371.
    • (2004) J Am Chem Soc , vol.126 , pp. 15370-15371
    • Morgan, A.J.1    Wang, Y.K.2    Roberts, M.F.3    Miller, S.J.4
  • 146
    • 42549162094 scopus 로고    scopus 로고
    • Regulation of mycothiol metabolism by sR and the thiol redox sensor anti-sigma factor RsrA
    • Newton GL, Fahey RC. 2008. Regulation of mycothiol metabolism by sR and the thiol redox sensor anti-sigma factor RsrA. Mol Microbiol 68:805-809.
    • (2008) Mol Microbiol , vol.68 , pp. 805-809
    • Newton, G.L.1    Fahey, R.C.2
  • 147
    • 42549139480 scopus 로고    scopus 로고
    • Mycothiol regulates and is regulated by a thiol-specific antisigma factor RsrA and sR in Streptomyces coelicolor
    • Park J-H, Roe J-H. 2008. Mycothiol regulates and is regulated by a thiol-specific antisigma factor RsrA and sR in Streptomyces coelicolor. Mol Microbiol 68:861-870.
    • (2008) Mol Microbiol , vol.68 , pp. 861-870
    • Park, J.-H.1    Roe, J.-H.2
  • 150
    • 79959226734 scopus 로고    scopus 로고
    • Precise null deletion mutations of the mycothiol synthesis genes reveal their role in isoniazid and ethionamide resistance in Mycobacterium smegmatis
    • Xu X, Vilcheze C, Av-Gay Y, Gomez-Velasco A, Jacobs WR, Jr. 2011. Precise null deletion mutations of the mycothiol synthesis genes reveal their role in isoniazid and ethionamide resistance in Mycobacterium smegmatis. Antimicrob Agents Chemother 55:3133-3139.
    • (2011) Antimicrob Agents Chemother , vol.55 , pp. 3133-3139
    • Xu, X.1    Vilcheze, C.2    Av-Gay, Y.3    Gomez-Velasco, A.4    Jacobs, W.R.5
  • 151
    • 0037853400 scopus 로고    scopus 로고
    • Inactivation of mshB, a key gene in the mycothiol biosynthesis pathway in Mycobacterium smegmatis
    • Rawat M, Kovacevic S, Billman-Jacobe H, Av-Gay Y. 2003. Inactivation of mshB, a key gene in the mycothiol biosynthesis pathway in Mycobacterium smegmatis. Microbiology 149:1341-1349.
    • (2003) Microbiology , vol.149 , pp. 1341-1349
    • Rawat, M.1    Kovacevic, S.2    Billman-Jacobe, H.3    Av-Gay, Y.4
  • 152
    • 0036840388 scopus 로고    scopus 로고
    • Mycothiol-deficient Mycobacterium smegmatis mutants are hypersensitive to alkylating agents, free radicals, and antibiotics
    • Rawat M, Newton GL, Ko M, Martinez GJ, Fahey RC, Av-Gay Y. 2002. Mycothiol-deficient Mycobacterium smegmatis mutants are hypersensitive to alkylating agents, free radicals, and antibiotics. Antimicrob Agents Chemother 46:3348-3355.
    • (2002) Antimicrob Agents Chemother , vol.46 , pp. 3348-3355
    • Rawat, M.1    Newton, G.L.2    Ko, M.3    Martinez, G.J.4    Fahey, R.C.5    Av-Gay, Y.6
  • 153
    • 27144496052 scopus 로고    scopus 로고
    • A mycothiol synthase mutant of Mycobacterium smegmatis produces novel thiols and has an altered thiol redox status
    • Newton GL, Ta P, Fahey RC. 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
  • 154
    • 79958784137 scopus 로고    scopus 로고
    • Molecular basis and mechanisms of drug resistance in Mycobacterium tuberculosis: classical and new drugs
    • Almeida Da Silva PE, Palomino JC. 2011. Molecular basis and mechanisms of drug resistance in Mycobacterium tuberculosis: classical and new drugs. J Antimicrob Chemother 66:1417-1430.
    • (2011) J Antimicrob Chemother , vol.66 , pp. 1417-1430
    • Almeida Da Silva, P.E.1    Palomino, J.C.2
  • 155
    • 51949098757 scopus 로고    scopus 로고
    • Biosynthesis and functions of mycothiol, the unique protective thiol of actinobacteria
    • Newton GL, Buchmeier N, Fahey RC. 2008. Biosynthesis and functions of mycothiol, the unique protective thiol of actinobacteria. Microbiol Mol Biol Rev 72:471-494.
    • (2008) Microbiol Mol Biol Rev , vol.72 , pp. 471-494
    • Newton, G.L.1    Buchmeier, N.2    Fahey, R.C.3
  • 156
    • 34548781274 scopus 로고    scopus 로고
    • Comparative analysis of mutants in the mycothiol biosynthesis pathway in Mycobacterium smegmatis
    • Rawat M, Johnson C, Cadiz V, Av-Gay Y. 2007. Comparative analysis of mutants in the mycothiol biosynthesis pathway in Mycobacterium smegmatis. Biochem Biophys Res Commun 363:71-76.
    • (2007) Biochem Biophys Res Commun , vol.363 , pp. 71-76
    • Rawat, M.1    Johnson, C.2    Cadiz, V.3    Av-Gay, Y.4
  • 157
    • 33749428834 scopus 로고    scopus 로고
    • The mshA gene encoding the glycosyltransferase of mycothiol biosynthesis is essential in Mycobacterium tuberculosis Erdman
    • Buchmeier N, Fahey RC. 2006. The mshA gene encoding the glycosyltransferase of mycothiol biosynthesis is essential in Mycobacterium tuberculosis Erdman. FEMS Microbiol Lett 264:74-79.
    • (2006) FEMS Microbiol Lett , vol.264 , pp. 74-79
    • Buchmeier, N.1    Fahey, R.C.2
  • 159
    • 0037347862 scopus 로고    scopus 로고
    • Association of mycothiol with protection of Mycobacterium tuberculosis from toxic oxidants and antibiotics
    • Buchmeier NA, Newton GL, Koledin T, Fahey RC. 2003. Association of mycothiol with protection of Mycobacterium tuberculosis from toxic oxidants and antibiotics. Mol Microbiol 47:1723-1732.
    • (2003) Mol Microbiol , vol.47 , pp. 1723-1732
    • Buchmeier, N.A.1    Newton, G.L.2    Koledin, T.3    Fahey, R.C.4
  • 160
    • 0242407452 scopus 로고    scopus 로고
    • Mycothiol is essential for growth of Mycobacterium tuberculosis Erdman
    • Sareen D, Newton GL, Fahey RC, Buchmeier NA. 2003. Mycothiol is essential for growth of Mycobacterium tuberculosis Erdman. J Bacteriol 185:6736-6740.
    • (2003) J Bacteriol , vol.185 , pp. 6736-6740
    • Sareen, D.1    Newton, G.L.2    Fahey, R.C.3    Buchmeier, N.A.4
  • 161
    • 33748987070 scopus 로고    scopus 로고
    • A mycothiol synthase mutant of Mycobacterium tuberculosis has an altered thiol-disulfide content and limited tolerance to stress
    • Buchmeier NA, Newton GL, Fahey RC. 2006. A mycothiol synthase mutant of Mycobacterium tuberculosis has an altered thiol-disulfide content and limited tolerance to stress. J Bacteriol 188:6245-6252.
    • (2006) J Bacteriol , vol.188 , pp. 6245-6252
    • Buchmeier, N.A.1    Newton, G.L.2    Fahey, R.C.3
  • 162
    • 20444419421 scopus 로고    scopus 로고
    • Genome-wide requirements for Mycobacterium tuberculosis adaptation and survival in macrophages
    • Rengarajan J, Bloom BR, Rubin EJ. 2005. Genome-wide requirements for Mycobacterium tuberculosis adaptation and survival in macrophages. Proc Natl Acad Sci USA 102:8327-8332.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 8327-8332
    • Rengarajan, J.1    Bloom, B.R.2    Rubin, E.J.3
  • 163
    • 0033533411 scopus 로고    scopus 로고
    • Expression, purification, and characterization of Mycobacterium tuberculosis mycothione reductase
    • Patel MP, Blanchard JS. 1999. Expression, purification, and characterization of Mycobacterium tuberculosis mycothione reductase. Biochemistry 38:11827-11833.
    • (1999) Biochemistry , vol.38 , pp. 11827-11833
    • Patel, M.P.1    Blanchard, J.S.2
  • 164
    • 0035339865 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis mycothione reductase: pH dependence of the kinetic parameters and kinetic isotope effects
    • Patel MP, Blanchard JS. 2001. Mycobacterium tuberculosis mycothione reductase: pH dependence of the kinetic parameters and kinetic isotope effects. Biochemistry 40:5119-5126.
    • (2001) Biochemistry , vol.40 , pp. 5119-5126
    • Patel, M.P.1    Blanchard, J.S.2
  • 165
    • 2442651619 scopus 로고    scopus 로고
    • Differential expression of mycothiol pathway genes: are they affected by antituberculosis drugs?
    • Hayward D, Wiid I, van Helden P. 2004. Differential expression of mycothiol pathway genes: are they affected by antituberculosis drugs? IUBMB Life 56:131-138.
    • (2004) IUBMB Life , vol.56 , pp. 131-138
    • Hayward, D.1    Wiid, I.2    van Helden, P.3
  • 167
    • 0141567701 scopus 로고    scopus 로고
    • The metabolism of nitrosothiols in the mycobacteria: identification and characterization of S-nitrosomycothiol reductase
    • Vogt RN, Steenkamp DJ, Zheng RJ, Blanchard JS. 2003. The metabolism of nitrosothiols in the mycobacteria: identification and characterization of S-nitrosomycothiol reductase. Biochem J 375: 657-665.
    • (2003) Biochem J , vol.375 , pp. 657-665
    • Vogt, R.N.1    Steenkamp, D.J.2    Zheng, R.J.3    Blanchard, J.S.4
  • 168
    • 34548722154 scopus 로고    scopus 로고
    • Innate protection of Mycobacterium smegmatis against the antimicrobial activity of nitric oxide is provided by mycothiol
    • Miller CC, Rawat M, Johnson T, Av-Gay Y. 2007. Innate protection of Mycobacterium smegmatis against the antimicrobial activity of nitric oxide is provided by mycothiol. Antimicrob Agents Chemother 51:3364-3366.
    • (2007) Antimicrob Agents Chemother , vol.51 , pp. 3364-3366
    • Miller, C.C.1    Rawat, M.2    Johnson, T.3    Av-Gay, Y.4
  • 169
    • 0034609546 scopus 로고    scopus 로고
    • A novel mycothioldependent detoxification pathway in mycobacteria involving mycothiol S-conjugate amidase
    • Newton GL, Av-Gay Y, Fahey RC. 2000. A novel mycothioldependent detoxification pathway in mycobacteria involving mycothiol S-conjugate amidase. Biochemistry 39:10739-10746.
    • (2000) Biochemistry , vol.39 , pp. 10739-10746
    • Newton, G.L.1    Av-Gay, Y.2    Fahey, R.C.3
  • 170
    • 0142040351 scopus 로고    scopus 로고
    • Characterization of Mycobacterium tuberculosis mycothiol S-conjugate amidase
    • Steffek M, Newton GL, Av-Gay Y, Fahey RC. 2003. Characterization of Mycobacterium tuberculosis mycothiol S-conjugate amidase. Biochemistry 42:12067-12076.
    • (2003) Biochemistry , vol.42 , pp. 12067-12076
    • Steffek, M.1    Newton, G.L.2    Av-Gay, Y.3    Fahey, R.C.4
  • 171
    • 4444241900 scopus 로고    scopus 로고
    • Targeted mutagenesis of the Mycobacterium smegmatis mca gene, encoding a mycothiol-dependent detoxification protein
    • Rawat M, Uppal M, Newton G, Steffek M, Fahey RC, Av-Gay Y. 2004. Targeted mutagenesis of the Mycobacterium smegmatis mca gene, encoding a mycothiol-dependent detoxification protein. J Bacteriol 186: 6050-6058.
    • (2004) J Bacteriol , vol.186 , pp. 6050-6058
    • Rawat, M.1    Uppal, M.2    Newton, G.3    Steffek, M.4    Fahey, R.C.5    Av-Gay, Y.6
  • 172
    • 84860754443 scopus 로고    scopus 로고
    • Thiols screened by the neocarzinostatin protein for preserving or detoxifying its bound enediyne antibiotic
    • Chi H-W, Huang C-C, Chin D-H. 2012. Thiols screened by the neocarzinostatin protein for preserving or detoxifying its bound enediyne antibiotic. Chemistry 18:6238-6249.
    • (2012) Chemistry , vol.18 , pp. 6238-6249
    • Chi, H.-W.1    Huang, C.-C.2    Chin, D.-H.3
  • 173
    • 0037245381 scopus 로고    scopus 로고
    • Inhibition and kinetics of Mycobacterium tuberculosis and Mycobacterium smegmatis mycothiol-S-conjugate amidase by natural product inhibitors
    • Nicholas GM, Eckman LL, Newton GL, Fahey RC, Ray S, Bewley CA. 2003. Inhibition and kinetics of Mycobacterium tuberculosis and Mycobacterium smegmatis mycothiol-S-conjugate amidase by natural product inhibitors. Bioorg Med Chem 11:601-608.
    • (2003) Bioorg Med Chem , vol.11 , pp. 601-608
    • Nicholas, G.M.1    Eckman, L.L.2    Newton, G.L.3    Fahey, R.C.4    Ray, S.5    Bewley, C.A.6
  • 175
    • 2942532643 scopus 로고    scopus 로고
    • Synthesis of a bromotyrosine-derived natural product inhibitor of mycothiol-S-conjugate amidase
    • Fetterolf B, Bewley CA. 2004. Synthesis of a bromotyrosine-derived natural product inhibitor of mycothiol-S-conjugate amidase. Bioorg Med Chem Lett 14:3785-3788.
    • (2004) Bioorg Med Chem Lett , vol.14 , pp. 3785-3788
    • Fetterolf, B.1    Bewley, C.A.2
  • 176
    • 33846112198 scopus 로고    scopus 로고
    • Design and synthesis of substrate-mimic inhibitors of mycothiol-S-conjugate amidase from Mycobacterium tuberculosis
    • Metaferia BB, Ray S, Smith JA, Bewley CA. 2007. Design and synthesis of substrate-mimic inhibitors of mycothiol-S-conjugate amidase from Mycobacterium tuberculosis. Bioorg Med Chem Lett 17:444-447.
    • (2007) Bioorg Med Chem Lett , vol.17 , pp. 444-447
    • Metaferia, B.B.1    Ray, S.2    Smith, J.A.3    Bewley, C.A.4
  • 177
    • 34948818221 scopus 로고    scopus 로고
    • Mycothiol import by Mycobacterium smegmatis and function as a resource for metabolic precursors and energy production
    • Bzymek KP, Newton GL, Ta P, Fahey RC. 2007. Mycothiol import by Mycobacterium smegmatis and function as a resource for metabolic precursors and energy production. J Bacteriol 189:6796-6805.
    • (2007) J Bacteriol , vol.189 , pp. 6796-6805
    • Bzymek, K.P.1    Newton, G.L.2    Ta, P.3    Fahey, R.C.4
  • 178
    • 0032515068 scopus 로고    scopus 로고
    • Mycothiol biosynthesis and metabolism. Cellular levels of potential intermediates in the biosynthesis and degradation of mycothiol in Mycobacterium smegmatis
    • Anderberg SJ, Newton GL, Fahey RC. 1998. Mycothiol biosynthesis and metabolism. Cellular levels of potential intermediates in the biosynthesis and degradation of mycothiol in Mycobacterium smegmatis. J Biol Chem 273:30391-30397.
    • (1998) J Biol Chem , vol.273 , pp. 30391-30397
    • Anderberg, S.J.1    Newton, G.L.2    Fahey, R.C.3
  • 179
    • 77952368044 scopus 로고    scopus 로고
    • In vitro reconstitution of mycobacterial ergothioneine biosynthesis
    • Seebeck FP. 2010. In vitro reconstitution of mycobacterial ergothioneine biosynthesis. J Am Chem Soc 132:6632-6633.
    • (2010) J Am Chem Soc , vol.132 , pp. 6632-6633
    • Seebeck, F.P.1
  • 180
    • 0002890943 scopus 로고
    • Sur une base novelle retirée du seigle ergote, l'ergothioneine
    • Tanret C. 1909. Sur une base novelle retirée du seigle ergote, l'ergothioneine. Compt Rend 149:222-224.
    • (1909) Compt Rend , vol.149 , pp. 222-224
    • Tanret, C.1
  • 181
    • 0011254610 scopus 로고
    • The constitution of ergothioneine: a betaine related to histidine
    • Barger G, Ewins AJ. 1911. The constitution of ergothioneine: a betaine related to histidine. J Chem Soc Trans 99:2336-2341.
    • (1911) J Chem Soc Trans , vol.99 , pp. 2336-2341
    • Barger, G.1    Ewins, A.J.2
  • 183
    • 0002888426 scopus 로고
    • Biosynthesis of ergothioneine and hercynine by mycobacteria
    • Genghof DS, Vandamme O. 1964. Biosynthesis of ergothioneine and hercynine by mycobacteria. J Bacteriol 87:852-862.
    • (1964) J Bacteriol , vol.87 , pp. 852-862
    • Genghof, D.S.1    Vandamme, O.2
  • 185
    • 5344262736 scopus 로고
    • Ergothioneine
    • Harris RH, Marrian GF, Thimann KV (ed). Academic Press, New York
    • Melville DB. 1959. Ergothioneine, p. 155-204. In Harris RH, Marrian GF, Thimann KV (ed), Vitamins&Hormones, vol. 17. Academic Press, New York.
    • (1959) Vitamins&Hormones , vol.17 , pp. 155-204
    • Melville, D.B.1
  • 186
    • 14544303903 scopus 로고
    • The occurrence of ergothioneine in plant material
    • Melville DB, Eich S. 1956. The occurrence of ergothioneine in plant material. J Biol Chem 218:647-651.
    • (1956) J Biol Chem , vol.218 , pp. 647-651
    • Melville, D.B.1    Eich, S.2
  • 187
    • 84875715041 scopus 로고    scopus 로고
    • Glutathione analogs in prokaryotes
    • Fahey RC. 2013. Glutathione analogs in prokaryotes. Biochim Biophys Acta 1830:3182-3198.
    • (2013) Biochim Biophys Acta , vol.1830 , pp. 3182-3198
    • Fahey, R.C.1
  • 188
    • 0015954510 scopus 로고
    • Generation of superoxide free radical during the autoxidation of thiols
    • Misra HP. 1974. Generation of superoxide free radical during the autoxidation of thiols. J Biol Chem 249:2151-2155.
    • (1974) J Biol Chem , vol.249 , pp. 2151-2155
    • Misra, H.P.1
  • 189
    • 0034810075 scopus 로고    scopus 로고
    • Oxidation and generation of hydrogen peroxide by thiol compounds in commonly used cell culture media
    • Hua Long L, Halliwell B. 2001. Oxidation and generation of hydrogen peroxide by thiol compounds in commonly used cell culture media. Biochem Biophys Res Commun 286:991-994.
    • (2001) Biochem Biophys Res Commun , vol.286 , pp. 991-994
    • Hua Long, L.1    Halliwell, B.2
  • 190
    • 0018239047 scopus 로고
    • Studies on ergothioneine. V. Determination by high performance liquid chromatography and application to metabolic research
    • Mayumi T, Kawano H, Sakamoto Y, Suehisa E, Kawai Y, Hama T. 1978. Studies on ergothioneine. V. Determination by high performance liquid chromatography and application to metabolic research. Chem Pharm Bull 26:3772-3778.
    • (1978) Chem Pharm Bull , vol.26 , pp. 3772-3778
    • Mayumi, T.1    Kawano, H.2    Sakamoto, Y.3    Suehisa, E.4    Kawai, Y.5    Hama, T.6
  • 191
    • 13344276484 scopus 로고
    • The preparation and properties of ergothioneine disulphide
    • Heath H, Toennies G. 1958. The preparation and properties of ergothioneine disulphide. Biochem J 68:204-210.
    • (1958) Biochem J , vol.68 , pp. 204-210
    • Heath, H.1    Toennies, G.2
  • 192
    • 77952368044 scopus 로고    scopus 로고
    • In vitro reconstitution of mycobacterial ergothioneine biosynthesis
    • Seebeck FP. 2010. In vitro reconstitution of mycobacterial ergothioneine biosynthesis. J Am Chem Soc 132:6632-6633.
    • (2010) J Am Chem Soc , vol.132 , pp. 6632-6633
    • Seebeck, F.P.1
  • 194
    • 0015149670 scopus 로고
    • Interaction of ergothioneine with metal ions and metalloenzymes
    • Hanlon DP. 1971. Interaction of ergothioneine with metal ions and metalloenzymes. J Med Chem 14:1084-1087.
    • (1971) J Med Chem , vol.14 , pp. 1084-1087
    • Hanlon, D.P.1
  • 196
    • 78651469381 scopus 로고    scopus 로고
    • Ergothioneine prevents copper-induced oxidative damage to DNA and protein by forming a redox-inactive ergothioneine-copper complex
    • Zhu BZ, Mao L, Fan RM, Zhu JG, Zhang YN, Wang J, Kalyanaraman B, Frei B. 2011. Ergothioneine prevents copper-induced oxidative damage to DNA and protein by forming a redox-inactive ergothioneine-copper complex. Chem Res Toxicol 24:30-34.
    • (2011) Chem Res Toxicol , vol.24 , pp. 30-34
    • Zhu, B.Z.1    Mao, L.2    Fan, R.M.3    Zhu, J.G.4    Zhang, Y.N.5    Wang, J.6    Kalyanaraman, B.7    Frei, B.8
  • 197
    • 0020458720 scopus 로고
    • Studies on ergothioneine. VII. Some effects on ergothioneine on glycolytic metabolism in red blood cells from rats
    • Kawano H, Higuchi F, Mayumi T, Hama T. 1982. Studies on ergothioneine. VII. Some effects on ergothioneine on glycolytic metabolism in red blood cells from rats. Chem Pharm Bull 30:2611-2613.
    • (1982) Chem Pharm Bull , vol.30 , pp. 2611-2613
    • Kawano, H.1    Higuchi, F.2    Mayumi, T.3    Hama, T.4
  • 198
    • 67649769428 scopus 로고    scopus 로고
    • Modulation of palmitic acid-induced cell death by ergothioneine: evidence of an anti-inflammatory action
    • Laurenza I, Colognato R, Migliore L, Del Prato S, Benzi L. 2008. Modulation of palmitic acid-induced cell death by ergothioneine: evidence of an anti-inflammatory action. Biofactors 33:237-247.
    • (2008) Biofactors , vol.33 , pp. 237-247
    • Laurenza, I.1    Colognato, R.2    Migliore, L.3    Del Prato, S.4    Benzi, L.5
  • 199
    • 0037459190 scopus 로고    scopus 로고
    • Ergothioneine inhibits oxidative stress-and TNFalpha-induced NF-kappa B activation and interleukin-8 release in alveolar epithelial cells
    • Rahman I, Gilmour PS, Jimenez LA, Biswas SK, Antonicelli F, Aruoma OI. 2003. Ergothioneine inhibits oxidative stress-and TNFalpha-induced NF-kappa B activation and interleukin-8 release in alveolar epithelial cells. Biochem Biophys Res Commun 302:860-864.
    • (2003) Biochem Biophys Res Commun , vol.302 , pp. 860-864
    • Rahman, I.1    Gilmour, P.S.2    Jimenez, L.A.3    Biswas, S.K.4    Antonicelli, F.5    Aruoma, O.I.6
  • 201
    • 0032721380 scopus 로고    scopus 로고
    • Protection against oxidative damage and cell death by the natural antioxidant ergothioneine
    • Aruoma OI, Spencer JP, Mahmood N. 1999. Protection against oxidative damage and cell death by the natural antioxidant ergothioneine. Food Chem Toxicol 37:1043-1053.
    • (1999) Food Chem Toxicol , vol.37 , pp. 1043-1053
    • Aruoma, O.I.1    Spencer, J.P.2    Mahmood, N.3
  • 202
    • 0032863046 scopus 로고    scopus 로고
    • Uptake and antioxidant effects of ergothioneine in human erythrocytes
    • Mitsuyama H, May JM. 1999. Uptake and antioxidant effects of ergothioneine in human erythrocytes. Clin Sci (Lond) 97:407-411.
    • (1999) Clin Sci (Lond) , vol.97 , pp. 407-411
    • Mitsuyama, H.1    May, J.M.2
  • 203
    • 0023818820 scopus 로고
    • Spin-echo 1H NMR detected response of ergothioneine to oxidative stress in the intact human erythrocyte
    • Reglinski J, Smith WE, Sturrock RD. 1988. Spin-echo 1H NMR detected response of ergothioneine to oxidative stress in the intact human erythrocyte. Magn Reson Med 6:217-223.
    • (1988) Magn Reson Med , vol.6 , pp. 217-223
    • Reglinski, J.1    Smith, W.E.2    Sturrock, R.D.3
  • 204
    • 0025040577 scopus 로고
    • Ergothioneine as antioxidant
    • Hartman PE. 1990. Ergothioneine as antioxidant. Methods Enzymol 186:310-318.
    • (1990) Methods Enzymol , vol.186 , pp. 310-318
    • Hartman, P.E.1
  • 205
    • 34548016273 scopus 로고    scopus 로고
    • Dietary sources and antioxidant effects of ergothioneine
    • Ey J, Schomig E, Taubert D. 2007. Dietary sources and antioxidant effects of ergothioneine. J Agric Food Chem 55:6466-6474.
    • (2007) J Agric Food Chem , vol.55 , pp. 6466-6474
    • Ey, J.1    Schomig, E.2    Taubert, D.3
  • 206
    • 77953620630 scopus 로고    scopus 로고
    • The unusual amino acid L-ergothioneine is a physiologic cytoprotectant
    • Paul BD, Snyder SH. 2010. The unusual amino acid L-ergothioneine is a physiologic cytoprotectant. Cell Death Differ 17:1134-1140.
    • (2010) Cell Death Differ , vol.17 , pp. 1134-1140
    • Paul, B.D.1    Snyder, S.H.2
  • 207
    • 84856802134 scopus 로고    scopus 로고
    • The Neurospora crassa mutant NcDeltaEgt-1 identifies an ergothioneine biosynthetic gene and demonstrates that ergothioneine enhances conidial survival and protects against peroxide toxicity during conidial germination
    • Bello MH, Barrera-Perez V, Morin D, Epstein L. 2012. The Neurospora crassa mutant NcDeltaEgt-1 identifies an ergothioneine biosynthetic gene and demonstrates that ergothioneine enhances conidial survival and protects against peroxide toxicity during conidial germination. Fungal Genet Biol 49:160-172.
    • (2012) Fungal Genet Biol , vol.49 , pp. 160-172
    • Bello, M.H.1    Barrera-Perez, V.2    Morin, D.3    Epstein, L.4
  • 208
    • 79955378872 scopus 로고    scopus 로고
    • Organic hydroperoxide resistance protein and ergothioneine compensate for loss of mycothiol in Mycobacterium smegmatis mutants
    • Ta P, Buchmeier N, Newton GL, Rawat M, Fahey RC. 2011. Organic hydroperoxide resistance protein and ergothioneine compensate for loss of mycothiol in Mycobacterium smegmatis mutants. J Bacteriol 193: 1981-1990.
    • (2011) J Bacteriol , vol.193 , pp. 1981-1990
    • Ta, P.1    Buchmeier, N.2    Newton, G.L.3    Rawat, M.4    Fahey, R.C.5
  • 209
    • 76549243800 scopus 로고
    • Blood ergothioneine levels in disease
    • Fraser RS. 1951. Blood ergothioneine levels in disease. J Lab Clin Med 37:199-206.
    • (1951) J Lab Clin Med , vol.37 , pp. 199-206
    • Fraser, R.S.1
  • 212
    • 0242405665 scopus 로고    scopus 로고
    • Aerobic denitrification of Pseudomonas aeruginosa monitored by online NAD(P)H fluorescence
    • Chen F, Xia Q, Ju LK. 2003. Aerobic denitrification of Pseudomonas aeruginosa monitored by online NAD(P)H fluorescence. Appl Environ Microbiol 69:6715-6722.
    • (2003) Appl Environ Microbiol , vol.69 , pp. 6715-6722
    • Chen, F.1    Xia, Q.2    Ju, L.K.3
  • 214
    • 0026698060 scopus 로고
    • Oxidized redox state of glutathione in the endoplasmic reticulum
    • Hwang C, Sinskey AJ, Lodish HF. 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
  • 215
    • 29144496897 scopus 로고    scopus 로고
    • Oxidizing potential of endosomes and lysosomes limits intracellular cleavage of disulfide-based antibody-drug conjugates
    • Austin CD, Wen X, Gazzard L, Nelson C, Scheller RH, Scales SJ. 2005. Oxidizing potential of endosomes and lysosomes limits intracellular cleavage of disulfide-based antibody-drug conjugates. Proc Natl Acad Sci USA 102:17987-17992.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 17987-17992
    • Austin, C.D.1    Wen, X.2    Gazzard, L.3    Nelson, C.4    Scheller, R.H.5    Scales, S.J.6
  • 216
    • 0035502932 scopus 로고    scopus 로고
    • Shedding light on disulfide bond formation: engineering a redox switch in green fluorescent protein
    • Ostergaard H, Henriksen A, Hansen FG, Winther JR. 2001. Shedding light on disulfide bond formation: engineering a redox switch in green fluorescent protein. EMBO J 20:5853-5862.
    • (2001) EMBO J , vol.20 , pp. 5853-5862
    • Ostergaard, H.1    Henriksen, A.2    Hansen, F.G.3    Winther, J.R.4
  • 217
    • 0021913571 scopus 로고
    • Glutathione reductase is not required for maintenance of reduced glutathione in Escherichia coli K-12
    • Tuggle CK, Fuchs JA. 1985. Glutathione reductase is not required for maintenance of reduced glutathione in Escherichia coli K-12. J Bacteriol 162:448-450.
    • (1985) J Bacteriol , vol.162 , pp. 448-450
    • Tuggle, C.K.1    Fuchs, J.A.2
  • 219
    • 0030792817 scopus 로고    scopus 로고
    • Biosynthesis of mycothiol: elucidation of the sequence of steps in Mycobacterium smegmatis
    • Bornemann C, Jardine MA, Spies HSC, Steenkamp DJ. 1997. Biosynthesis of mycothiol: elucidation of the sequence of steps in Mycobacterium smegmatis. Biochem J 325:623-629.
    • (1997) Biochem J , vol.325 , pp. 623-629
    • Bornemann, C.1    Jardine, M.A.2    Spies, H.S.C.3    Steenkamp, D.J.4
  • 221
    • 80051546929 scopus 로고    scopus 로고
    • Mass spectrometric analysis of mycothiol levels in wild-type and mycothiol disulfide reductase mutant Mycobacterium smegmatis
    • Holsclaw CM, Muse WB, 3rd, Carroll KS, Leary JA. 2011. Mass spectrometric analysis of mycothiol levels in wild-type and mycothiol disulfide reductase mutant Mycobacterium smegmatis. Int J Mass Spectrom 305:151-156.
    • (2011) Int J Mass Spectrom , vol.305 , pp. 151-156
    • Holsclaw, C.M.1    Muse, W.B.2    Carroll, K.S.3    Leary, J.A.4
  • 222
    • 33745518017 scopus 로고    scopus 로고
    • Mycothiol-dependent mycobacterial response to oxidative stress
    • Ung KSE, 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.E.1    Av-Gay, Y.2


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