메뉴 건너뛰기




Volumn 325, Issue 1, 2004, Pages 21-27

Preparation and utilization of a reagent for the isolation and purification of low-molecular-mass thiols

Author keywords

[No Author keywords available]

Indexed keywords

ADDITION REACTIONS; SULFUR COMPOUNDS;

EID: 0346728691     PISSN: 00032697     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ab.2003.10.011     Document Type: Article
Times cited : (13)

References (20)
  • 1
    • 0027990965 scopus 로고
    • Thiols of intracellular pathogens: Identification of ovothiol a in Leishmania donovani and structural analysis of a novel thiol from Mycobacterium bovis (BCG)
    • Spies H.S.C., Steenkamp D.J. Thiols of intracellular pathogens: identification of ovothiol A in Leishmania donovani and structural analysis of a novel thiol from Mycobacterium bovis (BCG). Eur. J. Biochem. 224:1994;203-213.
    • (1994) Eur. J. Biochem. , vol.224 , pp. 203-213
    • Spies, H.S.C.1    Steenkamp, D.J.2
  • 2
    • 0034775463 scopus 로고    scopus 로고
    • Novel thiols of prokaryotes
    • Fahey R.C. Novel thiols of prokaryotes. Annu. Rev. Microbiol. 55:2001;33-356.
    • (2001) Annu. Rev. Microbiol. , vol.55 , pp. 33-356
    • Fahey, R.C.1
  • 3
    • 0022002912 scopus 로고
    • Trypanothione: A novel bis (glutathionyl) spermidine cofactor for glutathione reductase in trypanosomatids
    • Fairlamb A.H., Blackburn P., Ulrich P., Chait B.T., Cerami A. Trypanothione: a novel bis (glutathionyl) spermidine cofactor for glutathione reductase in trypanosomatids. Science. 227:1985;1485-1487.
    • (1985) Science , vol.227 , pp. 1485-1487
    • Fairlamb, A.H.1    Blackburn, P.2    Ulrich, P.3    Chait, B.T.4    Cerami, A.5
  • 4
    • 0026793462 scopus 로고
    • Metabolism and functions of trypanothione in the Kinetoplastida
    • Fairlamb A.H., Cerami A. Metabolism and functions of trypanothione in the Kinetoplastida. Annu. Rev. Microbiol. 46:1992;695-729.
    • (1992) Annu. Rev. Microbiol. , vol.46 , pp. 695-729
    • Fairlamb, A.H.1    Cerami, A.2
  • 5
    • 0034255209 scopus 로고    scopus 로고
    • Reactive oxygen and nitrogen intermediates in the relationship between mammalian hosts and microbial pathogens
    • Nathan C., Shiloh M.U. Reactive oxygen and nitrogen intermediates in the relationship between mammalian hosts and microbial pathogens. Proc. Natl. Acad. Sci. USA. 97:2000;8841-8848.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 8841-8848
    • Nathan, C.1    Shiloh, M.U.2
  • 6
    • 0034609546 scopus 로고    scopus 로고
    • A novel mycothiol dependent detoxification pathway in mycobacteria involving mycothiol S-conjugate amidase
    • Newton G.L., Av-Gay Y., Fahey R.C. A novel mycothiol dependent detoxification pathway in mycobacteria involving mycothiol S-conjugate amidase. Biochemistry. 39:2000;10739-10746.
    • (2000) Biochemistry , vol.39 , pp. 10739-10746
    • Newton, G.L.1    Av-Gay, Y.2    Fahey, R.C.3
  • 7
    • 0035815655 scopus 로고    scopus 로고
    • Trypanothione-dependent synthesis of deoxyribonucleotides by Trypanosoma brucei ribonucleotide reductase
    • Dormeyer M., Reckenfelderbaumer N., Ludemann H., Krauth-Siegel R.L. Trypanothione-dependent synthesis of deoxyribonucleotides by Trypanosoma brucei ribonucleotide reductase. J. Biol. Chem. 276:2001;10602-10606.
    • (2001) J. Biol. Chem. , vol.276 , pp. 10602-10606
    • Dormeyer, M.1    Reckenfelderbaumer, N.2    Ludemann, H.3    Krauth-Siegel, R.L.4
  • 8
    • 0028061437 scopus 로고
    • Two additional glutaredoxins exist in Escherichia coli: Glutaredoxin is a hydrogen donor for ribonucleotide reductase in a thioredoxin/glutaredoxin1 double mutant
    • Aslund F., Ehn B., Miranda-Vizuete A., Pueyo C., Holmgren A. Two additional glutaredoxins exist in Escherichia coli: glutaredoxin is a hydrogen donor for ribonucleotide reductase in a thioredoxin/glutaredoxin1 double mutant. Proc. Natl. Acad. Sci. USA. 91:1994;9813-9817.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 9813-9817
    • Aslund, F.1    Ehn, B.2    Miranda-Vizuete, A.3    Pueyo, C.4    Holmgren, A.5
  • 9
    • 0033650023 scopus 로고    scopus 로고
    • Cellular thiols and redox regulated signal transduction
    • Sen C.K. Cellular thiols and redox regulated signal transduction. Curr. Top. Cell. Regul. 36:2000;1-30.
    • (2000) Curr. Top. Cell. Regul. , vol.36 , pp. 1-30
    • Sen, C.K.1
  • 10
    • 0035371184 scopus 로고    scopus 로고
    • Redox environment of the cell as viewed through the redox state of the glutathione disulfide/glutathione redox couple
    • Schafer F.Q., Buettner G.R. Redox environment of the cell as viewed through the redox state of the glutathione disulfide/glutathione redox couple. Free Radic. Biol. Med. 30:2001;1191-1212.
    • (2001) Free Radic. Biol. Med. , vol.30 , pp. 1191-1212
    • Schafer, F.Q.1    Buettner, G.R.2
  • 12
    • 0031854156 scopus 로고    scopus 로고
    • Evidence that trypanothione reductase is an essential enzyme in Leishmania by targeted replacement of the tryA gene locus
    • Tovar J., Wilkinson S., Mottram J.C., Fairlamb A.H. Evidence that trypanothione reductase is an essential enzyme in Leishmania by targeted replacement of the tryA gene locus. Mol. Microbiol. 29:1998;653-660.
    • (1998) Mol. Microbiol. , vol.29 , pp. 653-660
    • Tovar, J.1    Wilkinson, S.2    Mottram, J.C.3    Fairlamb, A.H.4
  • 13
    • 0030926411 scopus 로고    scopus 로고
    • Disruption of the trypanothione reductase gene of Leishmania decreases its ability to survive oxidative stress in macrophages
    • C. Dumas, M. Quellette, J. Tovar, A.H. Fairlamb, S. Tamar, M. Olivier, B. Papadopoulou, Disruption of the trypanothione reductase gene of Leishmania decreases its ability to survive oxidative stress in macrophages, EMBO J. 16, 2590-2598.
    • EMBO J. , vol.16 , pp. 2590-2598
    • Dumas, C.1    Quellette, M.2    Tovar, J.3    Fairlamb, A.H.4    Tamar, S.5    Olivier, M.6    Papadopoulou, B.7
  • 14
    • 0036173507 scopus 로고    scopus 로고
    • Synthesis of mycothiol, 1D-1-O-(2-[N-acetyl-D-cysteinyl]amino-2-deoxy- α-D-glucopyranosyl)-myo-inositol, principal low molecular mass thiol in the Actinomycetes
    • Jardine M.A., Spies H.S.C., Nkambule C.M., Gammon D.W., Steenkamp D.J. Synthesis of mycothiol, 1D-1-O-(2-[N-acetyl-D-cysteinyl]amino-2-deoxy-α-D- glucopyranosyl)-myo-inositol, principal low molecular mass thiol in the Actinomycetes. Bioorg. Med. Chem. 10:2002;875-881.
    • (2002) Bioorg. Med. Chem. , vol.10 , pp. 875-881
    • Jardine, M.A.1    Spies, H.S.C.2    Nkambule, C.M.3    Gammon, D.W.4    Steenkamp, D.J.5
  • 15
    • 0027175927 scopus 로고
    • Simple methods for the detection and quantification of thiols from Crithidia fasciculata and for the isolation of trypanothione
    • Steenkamp D.J. Simple methods for the detection and quantification of thiols from Crithidia fasciculata and for the isolation of trypanothione. Biochem. J. 292:1993;295-301.
    • (1993) Biochem. J. , vol.292 , pp. 295-301
    • Steenkamp, D.J.1
  • 16
    • 0027267127 scopus 로고
    • Low molecular weight thiols in Streptomyces and their potential role as antioxidants
    • Newton G.L., Fahey R.C., Cohen G., Aharonowitz Y. Low molecular weight thiols in Streptomyces and their potential role as antioxidants. J. Bacteriol. 175:1993;2734-2742.
    • (1993) J. Bacteriol. , vol.175 , pp. 2734-2742
    • Newton, G.L.1    Fahey, R.C.2    Cohen, G.3    Aharonowitz, Y.4
  • 17
    • 0142019721 scopus 로고
    • Histochemical demonstration of protein-bound sulfhydryl groups
    • Barnett R.J., Seligman A.M. Histochemical demonstration of protein-bound sulfhydryl groups. Science. 116:1952;323-327.
    • (1952) Science , vol.116 , pp. 323-327
    • Barnett, R.J.1    Seligman, A.M.2
  • 18
    • 0030792817 scopus 로고    scopus 로고
    • Biosynthesis of mycothiol: Elucidation of the sequence of steps in Mycobacterium smegmatis
    • Bornemann C., Jardine M.A., Spies H.S.C., Steenkamp D.J. Biosynthesis of mycothiol: elucidation of the sequence of steps in Mycobacterium smegmatis. Biochem. J. 325:1997;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
  • 19
    • 0141567701 scopus 로고    scopus 로고
    • The metabolism of nitrosothiols in the mycobacteria: Identification and characterization of S-nitrosomycothiol reductase
    • Vogt R.N., Steenkamp D.J., Zheng R., Blanchard J.S. The metabolism of nitrosothiols in the mycobacteria: identification and characterization of S-nitrosomycothiol reductase. Biochem. J. 374:2003;657-666.
    • (2003) Biochem. J. , vol.374 , pp. 657-666
    • Vogt, R.N.1    Steenkamp, D.J.2    Zheng, R.3    Blanchard, J.S.4
  • 20
    • 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. Inactivation of mshB, a key gene in the mycothiol biosynthesis pathway in Mycobacterium smegmatis. Microbiology. 149:2003;1341-1349.
    • (2003) Microbiology , vol.149 , pp. 1341-1349
    • Rawat, M.1    Kovacevic, S.2    Billman-Jacobe, H.3    Av-Gay, Y.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.