메뉴 건너뛰기




Volumn 188, Issue 5, 2012, Pages 2316-2327

Glutathione reductase facilitates host defense by sustaining phagocytic oxidative burst and promoting the development of neutrophil extracellular traps

Author keywords

[No Author keywords available]

Indexed keywords

GLUTATHIONE; GLUTATHIONE REDUCTASE; REACTIVE OXYGEN METABOLITE;

EID: 84863172698     PISSN: 00221767     EISSN: 15506606     Source Type: Journal    
DOI: 10.4049/jimmunol.1102683     Document Type: Article
Times cited : (61)

References (61)
  • 2
    • 85027922094 scopus 로고    scopus 로고
    • Lipopolysaccharide and sepsis-associated myocardial dysfunction
    • Balija, T. M., and S. F. Lowry. 2011. Lipopolysaccharide and sepsis-associated myocardial dysfunction. Curr. Opin. Infect. Dis. 24: 248-253.
    • (2011) Curr. Opin. Infect. Dis. , vol.24 , pp. 248-253
    • Balija, T.M.1    Lowry, S.F.2
  • 3
    • 33344468233 scopus 로고    scopus 로고
    • Neutrophils and immunity: Challenges and opportunities
    • DOI 10.1038/nri1785
    • Nathan, C. 2006. Neutrophils and immunity: challenges and opportunities. Nat. Rev. Immunol. 6: 173-182. (Pubitemid 43290987)
    • (2006) Nature Reviews Immunology , vol.6 , Issue.3 , pp. 173-182
    • Nathan, C.1
  • 4
    • 1542406446 scopus 로고    scopus 로고
    • NOX enzymes and the biology of reactive oxygen
    • Lambeth, J. D. 2004. NOX enzymes and the biology of reactive oxygen. Nat. Rev. Immunol. 4: 181-189. (Pubitemid 38339084)
    • (2004) Nature Reviews Immunology , vol.4 , Issue.3 , pp. 181-189
    • Lambeth, J.D.1
  • 5
    • 1042278903 scopus 로고    scopus 로고
    • NADPH oxidase
    • DOI 10.1016/j.coi.2003.12.001
    • Babior, B. M. 2004. NADPH oxidase. Curr. Opin. Immunol. 16: 42-47. (Pubitemid 38198116)
    • (2004) Current Opinion in Immunology , vol.16 , Issue.1 , pp. 42-47
    • Babior, B.M.1
  • 6
    • 0032534597 scopus 로고    scopus 로고
    • Isolation and characterization of a variant HL60 cell line defective in the activation of the NADPH oxidase by phorbol myristate acetate
    • Tardif, M., M. J. Rabiet, T. Christophe, M. D. Milcent, and F. Boulay. 1998. Isolation and characterization of a variant HL60 cell line defective in the activation of the NADPH oxidase by phorbol myristate acetate. J. Immunol. 161: 6885-6895. (Pubitemid 28562234)
    • (1998) Journal of Immunology , vol.161 , Issue.12 , pp. 6885-6895
    • Tardif, M.1    Rabiet, M.-J.2    Christophe, T.3    Milcent, M.-D.4    Boulay, F.5
  • 7
    • 61849133901 scopus 로고    scopus 로고
    • PI3K and NADPH oxidase: A class act
    • Kennedy, A. D., and F. R. DeLeo. 2008. PI3K and NADPH oxidase: a class act. Blood 112: 4788-4789.
    • (2008) Blood , vol.112 , pp. 4788-4789
    • Kennedy, A.D.1    DeLeo, F.R.2
  • 9
    • 0026335622 scopus 로고
    • Regulation of phagocyte oxygen radical production by the GTP-binding protein Rac 2
    • Knaus, U. G., P. G. Heyworth, T. Evans, J. T. Curnutte, and G. M. Bokoch. 1991. Regulation of phagocyte oxygen radical production by the GTP-binding protein Rac 2. Science 254: 1512-1515. (Pubitemid 21917492)
    • (1991) Science , vol.254 , Issue.5037 , pp. 1512-1515
    • Knaus, U.G.1    Heyworth, P.G.2    Evans, T.3    Curnutte, J.T.4    Bokoch, G.M.5
  • 10
    • 0025944684 scopus 로고
    • rac1
    • Abo, A., E. Pick, A. Hall, N. Totty, C. G. Teahan, and A. W. Segal. 1991. Activation of the NADPH oxidase involves the small GTP-binding protein p21rac1. Nature 353: 668-670. (Pubitemid 21912587)
    • (1991) Nature , vol.353 , Issue.6345 , pp. 668-670
    • Abo, A.1    Pick, E.2    Hall, A.3    Totty, N.4    Teahan, C.G.5    Segal, A.W.6
  • 11
    • 77953626900 scopus 로고    scopus 로고
    • Akt isoforms differentially regulate neutrophil functions
    • Chen, J., H. Tang, N. Hay, J. Xu, and R. D. Ye. 2010. Akt isoforms differentially regulate neutrophil functions. Blood 115: 4237-4246.
    • (2010) Blood , vol.115 , pp. 4237-4246
    • Chen, J.1    Tang, H.2    Hay, N.3    Xu, J.4    Ye, R.D.5
  • 12
    • 38849142607 scopus 로고    scopus 로고
    • phox and rapid activation of nicotinamide adenine dinucleotide phosphate oxidase
    • phox and rapid activation of nicotinamide adenine dinucleotide phosphate oxidase. J. Immunol. 179: 7720-7728.
    • (2007) J. Immunol. , vol.179 , pp. 7720-7728
    • Cheng, N.1    He, R.2    Tian, J.3    Dinauer, M.C.4    Ye, R.D.5
  • 13
    • 0032540225 scopus 로고    scopus 로고
    • Activation of the leukocyte NADPH oxidase by phorbol ester requires the phosphorylation of p47(PHOX) on serine 303 or 304
    • DOI 10.1074/jbc.273.16.9539
    • Inanami, O., J. L. Johnson, J. K. McAdara, J. E. Benna, L. R. Faust, P. E. Newburger, and B. M. Babior. 1998. Activation of the leukocyte NADPH oxidase by phorbol ester requires the phosphorylation of p47PHOX on serine 303 or 304. J. Biol. Chem. 273: 9539-9543. (Pubitemid 28183039)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.16 , pp. 9539-9543
    • Inanami, O.1    Johnson, J.L.2    McAdara, J.K.3    El, B.J.4    Faust, L.R.P.5    Newburger, P.E.6    Babior, B.M.7
  • 16
    • 34447525439 scopus 로고    scopus 로고
    • Beneficial suicide: Why neutrophils die to make NETs
    • DOI 10.1038/nrmicro1710, PII NRMICRO1710
    • Brinkmann, V., and A. Zychlinsky. 2007. Beneficial suicide: why neutrophils die to make NETs. Nat. Rev. Microbiol. 5: 577-582. (Pubitemid 47074113)
    • (2007) Nature Reviews Microbiology , vol.5 , Issue.8 , pp. 577-582
    • Brinkmann, V.1    Zychlinsky, A.2
  • 21
    • 79955596509 scopus 로고    scopus 로고
    • Restoration of anti-Aspergillus defense by neutrophil extracellular traps in human chronic granulomatous disease after gene therapy is calprotectin-dependent
    • Bianchi, M., M. J. Niemiec, U. Siler, C. F. Urban, and J. Reichenbach. 2011. Restoration of anti-Aspergillus defense by neutrophil extracellular traps in human chronic granulomatous disease after gene therapy is calprotectin-dependent. J. Allergy Clin. Immunol. 127: 1243-1252, e7.
    • (2011) J. Allergy Clin. Immunol. , vol.127
    • Bianchi, M.1    Niemiec, M.J.2    Siler, U.3    Urban, C.F.4    Reichenbach, J.5
  • 23
    • 0014669906 scopus 로고
    • Glutathione and the hexose monophosphate shunt in phagocytizing and hydrogen peroxide-treated rat leukocytes
    • Reed, P. W. 1969. Glutathione and the hexose monophosphate shunt in phagocytizing and hydrogen peroxide-treated rat leukocytes. J. Biol. Chem. 244: 2459-2464.
    • (1969) J. Biol. Chem. , vol.244 , pp. 2459-2464
    • Reed, P.W.1
  • 24
    • 0014627868 scopus 로고
    • The role of the phagocyte in host-parasite interactions. XIX. Leukocytic glutathione reductase and its involvement in phagocytosis
    • Strauss, R. R., B. B. Paul, A. A. Jacobs, and A. J. Sbarra. 1969. The role of the phagocyte in host-parasite interactions. XIX. Leukocytic glutathione reductase and its involvement in phagocytosis. Arch. Biochem. Biophys. 135: 265-271.
    • (1969) Arch. Biochem. Biophys. , vol.135 , pp. 265-271
    • Strauss, R.R.1    Paul, B.B.2    Jacobs, A.A.3    Sbarra, A.J.4
  • 25
    • 0023151844 scopus 로고
    • 2
    • Cohen, H. J., E. H. Tape, J. Novak, M. E. Chovaniec, P. Liegey, and J. C. Whitin. 1987. The role of glutathione reductase in maintaining human granulocyte function and sensitivity to exogenous H2O2. Blood 69: 493-500. (Pubitemid 17022019)
    • (1987) Blood , vol.69 , Issue.2 , pp. 493-500
    • Cohen, H.J.1    Tape, E.H.2    Novak, J.3
  • 26
    • 0017062372 scopus 로고
    • Familial deficiency of glutathione reductase in human blood cells
    • Loos, H., D. Roos, R. Weening, and J. Houwerzijl. 1976. Familial deficiency of glutathione reductase in human blood cells. Blood 48: 53-62.
    • (1976) Blood , vol.48 , pp. 53-62
    • Loos, H.1    Roos, D.2    Weening, R.3    Houwerzijl, J.4
  • 27
    • 0018764370 scopus 로고
    • Protection of phagocytic leukocytes by endogenous glutathione: Studies in a family with glutathione reductase deficiency
    • Roos, D., R. S. Weening, A. A. Voetman, M. L. van Schaik, A. A. Bot, L. J. Meerhof, and J. A. Loos. 1979. Protection of phagocytic leukocytes by endogenous glutathione: studies in a family with glutathione reductase deficiency. Blood 53: 851-866. (Pubitemid 9178658)
    • (1979) Blood , vol.53 , Issue.5 , pp. 851-866
    • Roos, D.1    Weening, R.S.2    Voetman, A.A.3
  • 28
    • 0033009796 scopus 로고    scopus 로고
    • a1Neu mice does not cause haemolytic anaemia
    • a1Neu mice does not cause haemolytic anaemia. Genet. Res. 73: 1-5.
    • (1999) Genet. Res. , vol.73 , pp. 1-5
    • Pretsch, W.1
  • 29
    • 10044237714 scopus 로고    scopus 로고
    • Analyses of glutathione reductase hypomorphic mice indicate a genetic knockout
    • DOI 10.1093/toxsci/kfh268
    • Rogers, L. K., T. Tamura, B. J. Rogers, S. E. Welty, T. N. Hansen, and C. V. Smith. 2004. Analyses of glutathione reductase hypomorphic mice indicate a genetic knockout. Toxicol. Sci. 82: 367-373. (Pubitemid 39600063)
    • (2004) Toxicological Sciences , vol.82 , Issue.2 , pp. 367-373
    • Rogers, L.K.1    Tamura, T.2    Rogers, B.J.3    Welty, S.E.4    Hansen, T.N.5    Smith, C.V.6
  • 31
    • 34247142019 scopus 로고    scopus 로고
    • Knockout of Mkp-1 enhances the host inflammatory responses to gram-positive bacteria
    • Wang, X., X. Meng, J. R. Kuhlman, L. D. Nelin, K. K. Nicol, B. K. English, and Y. Liu. 2007. Knockout of Mkp-1 enhances the host inflammatory responses to Gram-positive bacteria. J. Immunol. 178: 5312-5320. (Pubitemid 46595317)
    • (2007) Journal of Immunology , vol.178 , Issue.8 , pp. 5312-5320
    • Wang, X.1    Meng, X.2    Kuhlman, J.R.3    Nelin, L.D.4    Nicol, K.K.5    English, B.K.6    Liu, Y.7
  • 32
    • 73349120613 scopus 로고    scopus 로고
    • Increased inflammation, impaired bacterial clearance, and metabolic disruption after Gram-negative sepsis in Mkp-1-deficient mice
    • Frazier, W. J., X. Wang, L. M. Wancket, X. A. Li, X. Meng, L. D. Nelin, A. C. Cato, and Y. Liu. 2009. Increased inflammation, impaired bacterial clearance, and metabolic disruption after Gram-negative sepsis in Mkp-1-deficient mice. J. Immunol. 183: 7411-7419.
    • (2009) J. Immunol. , vol.183 , pp. 7411-7419
    • Frazier, W.J.1    Wang, X.2    Wancket, L.M.3    Li, X.A.4    Meng, X.5    Nelin, L.D.6    Cato, A.C.7    Liu, Y.8
  • 34
    • 71849096722 scopus 로고    scopus 로고
    • Spatiotemporal progression of localized bacterial peritonitis before and after open abdomen lavage monitored by in vivo bioluminescent imaging
    • Sharma, P. K., E. Engels, W. Van Oeveren, R. J. Ploeg, C. van Henny der Mei, H. J. Busscher, G. M. Van Dam, and G. Rakhorst. 2010. Spatiotemporal progression of localized bacterial peritonitis before and after open abdomen lavage monitored by in vivo bioluminescent imaging. Surgery 147: 89-97.
    • (2010) Surgery , vol.147 , pp. 89-97
    • Sharma, P.K.1    Engels, E.2    Van Oeveren, W.3    Ploeg, R.J.4    Van Henny Der Mei, C.5    Busscher, H.J.6    Van Dam, G.M.7    Rakhorst, G.8
  • 37
    • 0020608442 scopus 로고
    • The effect of BCNU (carmustine) on tissue glutathione reductase activity
    • Kehrer, J. P. 1983. The effect of BCNU (carmustine) on tissue glutathione reductase activity. Toxicol. Lett. 17: 63-68. (Pubitemid 13054054)
    • (1983) Toxicology Letters , vol.17 , Issue.1-2 , pp. 63-68
    • Kehrer, J.P.1
  • 38
    • 0015712796 scopus 로고
    • Rheumatoid sera and soluble complexes: Nitroblue tetrazolium dye test and hexose monophosphate shunt activation
    • Pachman, L. M., P. Jayanetra, and R. M. Rothberg. 1973. Rheumatoid sera and soluble complexes: nitroblue tetrazolium dye test and hexose monophosphate shunt activation. Pediatrics 52: 823-830.
    • (1973) Pediatrics , vol.52 , pp. 823-830
    • Pachman, L.M.1    Jayanetra, P.2    Rothberg, R.M.3
  • 39
    • 0035168692 scopus 로고    scopus 로고
    • Transcriptional induction of MKP-1 in response to stress is associated with histone H3 phosphorylation-acetylation
    • DOI 10.1128/MCB.21.23.8213-8224.2001
    • Li, J., M. Gorospe, D. Hutter, J. Barnes, S. M. Keyse, and Y. Liu. 2001. Transcriptional induction of MKP-1 in response to stress is associated with histone H3 phosphorylation-acetylation. Mol. Cell. Biol. 21: 8213-8224. (Pubitemid 33051810)
    • (2001) Molecular and Cellular Biology , vol.21 , Issue.23 , pp. 8213-8224
    • Li, J.1    Gorospe, M.2    Hutter, D.3    Barnes, J.4    Keyse, S.M.5    Liu, Y.6
  • 40
    • 0035800855 scopus 로고    scopus 로고
    • Discordance between the binding affinity of mitogen-activated protein kinase sub-family members for MAP kinase phosphatase-2 and their ability to catalytically activate the phosphatase
    • Chen, P., D. Hutter, X. Yang, M. Gorospe, R. J. Davis, and Y. Liu. 2001. Discordance between the binding affinity of mitogen-activated protein kinase sub-family members for MAP kinase phosphatase-2 and their ability to catalytically activate the phosphatase. J. Biol. Chem. 276: 29440-29449.
    • (2001) J. Biol. Chem. , vol.276 , pp. 29440-29449
    • Chen, P.1    Hutter, D.2    Yang, X.3    Gorospe, M.4    Davis, R.J.5    Liu, Y.6
  • 41
    • 0033850043 scopus 로고    scopus 로고
    • Neisseria gonorrhoeae elicits membrane ruffling and cytoskeletal rearrangements upon infection of primary human endocervical and ectocervical cells
    • Edwards, J. L., J. Q. Shao, K. A. Ault, and M. A. Apicella. 2000. Neisseria gonorrhoeae elicits membrane ruffling and cytoskeletal rearrangements upon infection of primary human endocervical and ectocervical cells. Infect. Immun. 68: 5354-5363.
    • (2000) Infect. Immun. , vol.68 , pp. 5354-5363
    • Edwards, J.L.1    Shao, J.Q.2    Ault, K.A.3    Apicella, M.A.4
  • 42
    • 0036884621 scopus 로고    scopus 로고
    • Restraint of proinflammatory cytokine biosynthesis by mitogen-activated protein kinase phosphatase-1 in lipopolysaccharide-stimulated macrophages
    • Chen, P., J. Li, J. Barnes, G. C. Kokkonen, J. C. Lee, and Y. Liu. 2002. Restraint of proinflammatory cytokine biosynthesis by mitogen-activated protein kinase phosphatase-1 in lipopolysaccharide-stimulated macrophages. J. Immunol. 169: 6408-6416. (Pubitemid 36903490)
    • (2002) Journal of Immunology , vol.169 , Issue.11 , pp. 6408-6416
    • Chen, P.1    Li, J.2    Barnes, J.3    Kokkonen, G.C.4    Lee, J.C.5    Liu, Y.6
  • 44
    • 38549180598 scopus 로고    scopus 로고
    • The immunology of sepsis
    • DOI 10.1002/path.2274
    • Sriskandan, S., and D. M. Altmann. 2008. The immunology of sepsis. J. Pathol. 214: 211-223. (Pubitemid 351160158)
    • (2008) Journal of Pathology , vol.214 , Issue.2 , pp. 211-223
    • Sriskandan, S.1    Altmann, D.M.2
  • 45
    • 18244390487 scopus 로고    scopus 로고
    • Myeloperoxidase: Friend and foe
    • DOI 10.1189/jlb.1204697
    • Klebanoff, S. J. 2005. Myeloperoxidase: friend and foe. J. Leukoc. Biol. 77: 598-625. (Pubitemid 40628741)
    • (2005) Journal of Leukocyte Biology , vol.77 , Issue.5 , pp. 598-625
    • Klebanoff, S.J.1
  • 46
    • 0029892010 scopus 로고    scopus 로고
    • Rapid killing of human neutrophils by the potent activator phorbol 12-myristate 13-acetate (PMA) accompanied by changes different from typical apoptosis or necrosis
    • Takei, H., A. Araki, H. Watanabe, A. Ichinose, and F. Sendo. 1996. Rapid killing of human neutrophils by the potent activator phorbol 12-myristate 13-acetate (PMA) accompanied by changes different from typical apoptosis or necrosis. J. Leukoc. Biol. 59: 229-240. (Pubitemid 26098707)
    • (1996) Journal of Leukocyte Biology , vol.59 , Issue.2 , pp. 229-240
    • Takei, H.1    Araki, A.2    Watanabe, H.3    Ichinose, A.4    Sendo, F.5
  • 47
    • 77952865796 scopus 로고    scopus 로고
    • Phagocyte partnership during the onset and resolution of inflammation
    • Soehnlein, O., and L. Lindbom. 2010. Phagocyte partnership during the onset and resolution of inflammation. Nat. Rev. Immunol. 10: 427-439.
    • (2010) Nat. Rev. Immunol. , vol.10 , pp. 427-439
    • Soehnlein, O.1    Lindbom, L.2
  • 50
    • 0026004924 scopus 로고
    • Phagocytosis and stimulation of the respiratory burst by phorbol diester initiate S-thiolation of specific proteins in macrophages
    • Rokutan, K., J. A. Thomas, and R. B. Johnston, Jr. 1991. Phagocytosis and stimulation of the respiratory burst by phorbol diester initiate S-thiolation of specific proteins in macrophages. J. Immunol. 147: 260-264.
    • (1991) J. Immunol. , vol.147 , pp. 260-264
    • Rokutan, K.1    Thomas, J.A.2    Johnston Jr., R.B.3
  • 51
    • 0030057750 scopus 로고    scopus 로고
    • Protein S-thiolation and dethiolation during the respiratory burst in human monocytes: A reversible post-translational modification with potential for buffering the effects of oxidant stress
    • Seres, T., V. Ravichandran, T. Moriguchi, K. Rokutan, J. A. Thomas, and R. B. Johnston, Jr. 1996. Protein S-thiolation and dethiolation during the respiratory burst in human monocytes: a reversible post-translational modification with potential for buffering the effects of oxidant stress. J. Immunol. 156: 1973-1980. (Pubitemid 26069333)
    • (1996) Journal of Immunology , vol.156 , Issue.5 , pp. 1973-1980
    • Seres, T.1    Ravichandran, V.2    Moriguchi, T.3    Rokutan, K.4    Thomas, J.A.5    Johnston Jr., R.B.6
  • 52
    • 33745006817 scopus 로고    scopus 로고
    • Stimulation of the alveolar macrophage respiratory burst by ADP causes selective glutathionylation of protein tyrosine phosphatase 1B
    • DOI 10.1016/j.freeradbiomed.2006.03.010, PII S0891584906001857
    • Rinna, A., M. Torres, and H. J. Forman. 2006. Stimulation of the alveolar macrophage respiratory burst by ADP causes selective glutathionylation of protein tyrosine phosphatase 1B. Free Radic. Biol. Med. 41: 86-91. (Pubitemid 43866455)
    • (2006) Free Radical Biology and Medicine , vol.41 , Issue.1 , pp. 86-91
    • Rinna, A.1    Torres, M.2    Forman, H.J.3
  • 53
    • 77951979741 scopus 로고    scopus 로고
    • S-glutathionylation regulates inflammatory activities of S100A9
    • Lim, S. Y., M. J. Raftery, J. Goyette, and C. L. Geczy. 2010. S-glutathionylation regulates inflammatory activities of S100A9. J. Biol. Chem. 285: 14377-14388.
    • (2010) J. Biol. Chem. , vol.285 , pp. 14377-14388
    • Lim, S.Y.1    Raftery, M.J.2    Goyette, J.3    Geczy, C.L.4
  • 55
    • 0036216769 scopus 로고    scopus 로고
    • Phagocytosis of microbes: Complexity in action
    • DOI 10.1146/annurev.immunol.20.103001.114744
    • Underhill, D. M., and A. Ozinsky. 2002. Phagocytosis of microbes: complexity in action. Annu. Rev. Immunol. 20: 825-852. (Pubitemid 34293441)
    • (2002) Annual Review of Immunology , vol.20 , pp. 825-852
    • Underhill, D.M.1    Ozinsky, A.2
  • 56
    • 0036467393 scopus 로고    scopus 로고
    • Phagocytosis and innate immunity
    • DOI 10.1016/S0952-7915(01)00309-0
    • Greenberg, S., and S. Grinstein. 2002. Phagocytosis and innate immunity. Curr. Opin. Immunol. 14: 136-145. (Pubitemid 34085118)
    • (2002) Current Opinion in Immunology , vol.14 , Issue.1 , pp. 136-145
    • Greenberg, S.1    Grinstein, S.2
  • 57
    • 0014020468 scopus 로고
    • Relationship of glycolytic and oxidative metabolism to particle entry and destruction in phagocytosing cells
    • Selvaraj, R. J., and A. J. Sbarra. 1966. Relationship of glycolytic and oxidative metabolism to particle entry and destruction in phagocytosing cells. Nature 211: 1272-1276.
    • (1966) Nature , vol.211 , pp. 1272-1276
    • Selvaraj, R.J.1    Sbarra, A.J.2
  • 59
    • 0035899183 scopus 로고    scopus 로고
    • Human thioredoxin reductase is efficiently inhibited by (2,2′:6′,2″-terpyridine)platinum(II) complexes. Possible implications for a novel antitumor strategy
    • DOI 10.1021/jm001014i
    • Becker, K., C. Herold-Mende, J. J. Park, G. Lowe, and R. H. Schirmer. 2001. Human thioredoxin reductase is efficiently inhibited by (2,2′:6′,2″-terpyridine) platinum(II) complexes: possible implications for a novel antitumor strategy. J. Med. Chem. 44: 2784-2792. (Pubitemid 32879719)
    • (2001) Journal of Medicinal Chemistry , vol.44 , Issue.17 , pp. 2784-2792
    • Becker, K.1    Herold-Mende, C.2    Park, J.J.3    Lowe, G.4    Heiner, S.R.5
  • 60
    • 0037427472 scopus 로고    scopus 로고
    • Glutathione reductase of the malarial parasite Plasmodium falciparum: Crystal structure and inhibitor development
    • DOI 10.1016/S0022-2836(03)00347-4
    • Sarma, G. N., S. N. Savvides, K. Becker, M. Schirmer, R. H. Schirmer, and P. A. Karplus. 2003. Glutathione reductase of the malarial parasite Plasmodium falciparum: crystal structure and inhibitor development. J. Mol. Biol. 328: 893-907. (Pubitemid 36506894)
    • (2003) Journal of Molecular Biology , vol.328 , Issue.4 , pp. 893-907
    • Sarma, G.N.1    Savvides, S.N.2    Becker, K.3    Schirmer, M.4    Schirmer, R.H.5    Karplus, P.A.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.