메뉴 건너뛰기




Volumn 50, Issue 2, 2011, Pages 371-380

The effects of aging on pulmonary oxidative damage, protein nitration, and extracellular superoxide dismutase down-regulation during systemic inflammation

Author keywords

Aging; EC SOD; Lung injury; Nitrotyrosine; Oxidative damage; Proteomics

Indexed keywords

EXTRACELLULAR SUPEROXIDE DISMUTASE; MYOSIN; PROFILIN; TRANSGELIN; TROPOMYOSIN;

EID: 78651239219     PISSN: 08915849     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.freeradbiomed.2010.11.013     Document Type: Article
Times cited : (66)

References (61)
  • 3
    • 0026710191 scopus 로고
    • Definitions for sepsis and organ failure and guidelines for the use of innovative therapies in sepsis. The ACCP/SCCM Consensus Conference Committee, American College of Chest Physicians/Society of Critical Care Medicine
    • Bone R.C., Balk R.A., Cerra F.B., Dellinger R.P., Fein A.M., Knaus W.A., Schein R.M., and Sibbald W.J. Definitions for sepsis and organ failure and guidelines for the use of innovative therapies in sepsis. The ACCP/SCCM Consensus Conference Committee, American College of Chest Physicians/Society of Critical Care Medicine Chest 101 1992 1644 1655
    • (1992) Chest , vol.101 , pp. 1644-1655
    • Bone, R.C.1    Balk, R.A.2    Cerra, F.B.3    Dellinger, R.P.4    Fein, A.M.5    Knaus, W.A.6    Schein, R.M.7    Sibbald, W.J.8
  • 4
    • 0032537394 scopus 로고    scopus 로고
    • Septic shock
    • M.E. Astiz, and E.C. Rackow Septic shock Lancet 351 1998 1501 1505
    • (1998) Lancet , vol.351 , pp. 1501-1505
    • Astiz, M.E.1    Rackow, E.C.2
  • 7
    • 29744447480 scopus 로고    scopus 로고
    • The effect of age on the development and outcome of adult sepsis
    • G.S. Martin, D.M. Mannino, and M. Moss The effect of age on the development and outcome of adult sepsis Crit. Care Med. 34 2006 15 21
    • (2006) Crit. Care Med. , vol.34 , pp. 15-21
    • Martin, G.S.1    Mannino, D.M.2    Moss, M.3
  • 8
    • 58949087473 scopus 로고    scopus 로고
    • Trends in causes of death among older persons in the United States
    • Gorina Y., Hoyert D., Lentzner H., and Goulding M. Trends in causes of death among older persons in the United States Aging Trends 6 2005 1 12
    • (2005) Aging Trends , Issue.6 , pp. 1-12
    • Gorina, Y.1    Hoyert, D.2    Lentzner, H.3    Goulding, M.4
  • 9
    • 0344628673 scopus 로고    scopus 로고
    • Effects of aging on mortality, hypothermia, and cytokine induction in mice with endotoxemia or sepsis
    • H. Saito, E.R. Sherwood, T.K. Varma, and B.M. Evers Effects of aging on mortality, hypothermia, and cytokine induction in mice with endotoxemia or sepsis Mech. Ageing Dev. 124 2003 1047 1058
    • (2003) Mech. Ageing Dev. , vol.124 , pp. 1047-1058
    • Saito, H.1    Sherwood, E.R.2    Varma, T.K.3    Evers, B.M.4
  • 10
    • 77954738683 scopus 로고    scopus 로고
    • Age-dependent vulnerability to endotoxemia is associated with reduction of anti-coagulant factors, activated protein C and thrombomodulin
    • M.E. Starr, J. Ueda, H. Takahashi, H. Weiler, C.T. Esmon, B.M. Evers, and H. Saito Age-dependent vulnerability to endotoxemia is associated with reduction of anti-coagulant factors, activated protein C and thrombomodulin Blood 115 2010 4886 4893
    • (2010) Blood , vol.115 , pp. 4886-4893
    • Starr, M.E.1    Ueda, J.2    Takahashi, H.3    Weiler, H.4    Esmon, C.T.5    Evers, B.M.6    Saito, H.7
  • 11
    • 0036841486 scopus 로고    scopus 로고
    • Aging accelerates endotoxin-induced thrombosis: Increased responses of plasminogen activator inhibitor-1 and lipopolysaccharide signaling with aging
    • K. Yamamoto, T. Shimokawa, H. Yi, K. Isobe, T. Kojima, D.J. Loskutoff, and H. Saito Aging accelerates endotoxin-induced thrombosis: increased responses of plasminogen activator inhibitor-1 and lipopolysaccharide signaling with aging Am. J. Pathol. 161 2002 1805 1814
    • (2002) Am. J. Pathol. , vol.161 , pp. 1805-1814
    • Yamamoto, K.1    Shimokawa, T.2    Yi, H.3    Isobe, K.4    Kojima, T.5    Loskutoff, D.J.6    Saito, H.7
  • 14
    • 17844375087 scopus 로고    scopus 로고
    • Lipopolysaccharide-induced tyrosine nitration and inactivation of hepatic glutamine synthetase in the rat
    • B. Gorg, M. Wettstein, S. Metzger, F. Schliess, and D. Haussinger Lipopolysaccharide-induced tyrosine nitration and inactivation of hepatic glutamine synthetase in the rat Hepatology 41 2005 1065 1073
    • (2005) Hepatology , vol.41 , pp. 1065-1073
    • Gorg, B.1    Wettstein, M.2    Metzger, S.3    Schliess, F.4    Haussinger, D.5
  • 15
    • 0032147208 scopus 로고    scopus 로고
    • Biological tyrosine nitration: A pathophysiological function of nitric oxide and reactive oxygen species
    • H. Ischiropoulos Biological tyrosine nitration: a pathophysiological function of nitric oxide and reactive oxygen species Arch. Biochem. Biophys. 356 1998 1 11
    • (1998) Arch. Biochem. Biophys. , vol.356 , pp. 1-11
    • Ischiropoulos, H.1
  • 17
    • 1642570319 scopus 로고    scopus 로고
    • Nitric oxide, oxidants, and protein tyrosine nitration
    • R. Radi Nitric oxide, oxidants, and protein tyrosine nitration Proc. Natl Acad. Sci. USA 101 2004 4003 4008
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 4003-4008
    • Radi, R.1
  • 19
    • 1242329363 scopus 로고    scopus 로고
    • Mode of action of endotoxin: Role of free radicals and antioxidants
    • J. Bhattacharyya, S. Biswas, and A.G. Datta Mode of action of endotoxin: role of free radicals and antioxidants Curr. Med. Chem. 11 2004 359 368
    • (2004) Curr. Med. Chem. , vol.11 , pp. 359-368
    • Bhattacharyya, J.1    Biswas, S.2    Datta, A.G.3
  • 20
    • 0142012094 scopus 로고    scopus 로고
    • Extracellular superoxide dismutase in biology and medicine
    • C.L. Fattman, L.M. Schaefer, and T.D. Oury Extracellular superoxide dismutase in biology and medicine Free Radic. Biol. Med. 35 2003 236 256
    • (2003) Free Radic. Biol. Med. , vol.35 , pp. 236-256
    • Fattman, C.L.1    Schaefer, L.M.2    Oury, T.D.3
  • 21
  • 22
    • 0038545583 scopus 로고    scopus 로고
    • Superoxide dismutases in the lung and human lung diseases
    • V.L. Kinnula, and J.D. Crapo Superoxide dismutases in the lung and human lung diseases Am. J. Respir. Crit. Care Med. 167 2003 1600 1619
    • (2003) Am. J. Respir. Crit. Care Med. , vol.167 , pp. 1600-1619
    • Kinnula, V.L.1    Crapo, J.D.2
  • 23
    • 0006157248 scopus 로고
    • Human copper-containing superoxide dismutase of high molecular weight
    • S.L. Marklund Human copper-containing superoxide dismutase of high molecular weight Proc. Natl Acad. Sci. USA 79 1982 7634 7638
    • (1982) Proc. Natl Acad. Sci. USA , vol.79 , pp. 7634-7638
    • Marklund, S.L.1
  • 24
    • 0020415065 scopus 로고
    • Superoxide dismutase in extracellular fluids
    • S.L. Marklund, E. Holme, and L. Hellner Superoxide dismutase in extracellular fluids Clin. Chim. Acta 126 1982 41 51
    • (1982) Clin. Chim. Acta , vol.126 , pp. 41-51
    • Marklund, S.L.1    Holme, E.2    Hellner, L.3
  • 25
    • 0027421112 scopus 로고
    • Heparin-affinity patterns and composition of extracellular superoxide dismutase in human plasma and tissues
    • J. Sandstrom, K. Karlsson, T. Edlund, and S.L. Marklund Heparin-affinity patterns and composition of extracellular superoxide dismutase in human plasma and tissues Biochem. J. 294 Pt 3 1993 853 857
    • (1993) Biochem. J. , vol.294 , Issue.PART 3 , pp. 853-857
    • Sandstrom, J.1    Karlsson, K.2    Edlund, T.3    Marklund, S.L.4
  • 26
    • 0028106271 scopus 로고
    • Extracellular superoxide dismutase (SOD3): Tissue-specific expression, genomic characterization, and computer-assisted sequence analysis of the human EC SOD gene
    • R.J. Folz, and J.D. Crapo Extracellular superoxide dismutase (SOD3): tissue-specific expression, genomic characterization, and computer-assisted sequence analysis of the human EC SOD gene Genomics 22 1994 162 171
    • (1994) Genomics , vol.22 , pp. 162-171
    • Folz, R.J.1    Crapo, J.D.2
  • 27
    • 0031253163 scopus 로고    scopus 로고
    • Mouse extracellular superoxide dismutase: Primary structure, tissue-specific gene expression, chromosomal localization, and lung in situ hybridization
    • R.J. Folz, J. Guan, M.F. Seldin, T.D. Oury, J.J. Enghild, and J.D. Crapo Mouse extracellular superoxide dismutase: primary structure, tissue-specific gene expression, chromosomal localization, and lung in situ hybridization Am. J. Respir. Cell Mol. Biol. 17 1997 393 403
    • (1997) Am. J. Respir. Cell Mol. Biol. , vol.17 , pp. 393-403
    • Folz, R.J.1    Guan, J.2    Seldin, M.F.3    Oury, T.D.4    Enghild, J.J.5    Crapo, J.D.6
  • 28
    • 67650095391 scopus 로고    scopus 로고
    • Extracellular SOD and aged blood vessels
    • T. Fukai Extracellular SOD and aged blood vessels Am. J. Physiol. Heart Circ. Physiol. 297 2009 H10 12
    • (2009) Am. J. Physiol. Heart Circ. Physiol. , vol.297 , pp. 10-12
    • Fukai, T.1
  • 30
    • 3943073829 scopus 로고    scopus 로고
    • Vascular protection: Superoxide dismutase isoforms in the vessel wall
    • F.M. Faraci, and S.P. Didion Vascular protection: superoxide dismutase isoforms in the vessel wall Arterioscler. Thromb. Vasc. Biol. 24 2004 1367 1373
    • (2004) Arterioscler. Thromb. Vasc. Biol. , vol.24 , pp. 1367-1373
    • Faraci, F.M.1    Didion, S.P.2
  • 31
    • 0036468850 scopus 로고    scopus 로고
    • Post-ischemic transcriptional and translational responses of EC-SOD in mouse brain and serum
    • S. Fukui, T. Ookawara, H. Nawashiro, K. Suzuki, and K. Shima Post-ischemic transcriptional and translational responses of EC-SOD in mouse brain and serum Free Radic. Biol. Med. 32 2002 289 298
    • (2002) Free Radic. Biol. Med. , vol.32 , pp. 289-298
    • Fukui, S.1    Ookawara, T.2    Nawashiro, H.3    Suzuki, K.4    Shima, K.5
  • 32
    • 0023277545 scopus 로고
    • Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction
    • P. Chomczynski, and N. Sacchi Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction Anal. Biochem. 162 1987 156 159
    • (1987) Anal. Biochem. , vol.162 , pp. 156-159
    • Chomczynski, P.1    Sacchi, N.2
  • 33
    • 0034604129 scopus 로고    scopus 로고
    • The acute respiratory distress syndrome
    • L.B. Ware, and M.A. Matthay The acute respiratory distress syndrome N. Engl. J. Med. 342 2000 1334 1349
    • (2000) N. Engl. J. Med. , vol.342 , pp. 1334-1349
    • Ware, L.B.1    Matthay, M.A.2
  • 35
    • 0141864392 scopus 로고    scopus 로고
    • Extracellular superoxide dismutase is a major determinant of nitric oxide bioavailability: In vivo and ex vivo evidence from ecSOD-deficient mice
    • O. Jung, S.L. Marklund, H. Geiger, T. Pedrazzini, R. Busse, and R.P. Brandes Extracellular superoxide dismutase is a major determinant of nitric oxide bioavailability: in vivo and ex vivo evidence from ecSOD-deficient mice Circ. Res. 93 2003 622 629
    • (2003) Circ. Res. , vol.93 , pp. 622-629
    • Jung, O.1    Marklund, S.L.2    Geiger, H.3    Pedrazzini, T.4    Busse, R.5    Brandes, R.P.6
  • 36
    • 0029064709 scopus 로고
    • Mice lacking extracellular superoxide dismutase are more sensitive to hyperoxia
    • L.M. Carlsson, J. Jonsson, T. Edlund, and S.L. Marklund Mice lacking extracellular superoxide dismutase are more sensitive to hyperoxia Proc. Natl Acad. Sci. USA 92 1995 6264 6268
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 6264-6268
    • Carlsson, L.M.1    Jonsson, J.2    Edlund, T.3    Marklund, S.L.4
  • 37
    • 66949146904 scopus 로고    scopus 로고
    • Protective effect of extracellular superoxide dismutase on endothelial function during aging
    • D.D. Lund, Y. Chu, J.D. Miller, and D.D. Heistad Protective effect of extracellular superoxide dismutase on endothelial function during aging Am. J. Physiol. Heart Circ. Physiol. 296 2009 H1920 1925
    • (2009) Am. J. Physiol. Heart Circ. Physiol. , vol.296 , pp. 1920-1925
    • Lund, D.D.1    Chu, Y.2    Miller, J.D.3    Heistad, D.D.4
  • 38
    • 4644240800 scopus 로고    scopus 로고
    • Sp1 and Sp3 transcription factors mediate trichostatin A-induced and basal expression of extracellular superoxide dismutase
    • I.N. Zelko, and R.J. Folz Sp1 and Sp3 transcription factors mediate trichostatin A-induced and basal expression of extracellular superoxide dismutase Free Radic. Biol. Med. 37 2004 1256 1271
    • (2004) Free Radic. Biol. Med. , vol.37 , pp. 1256-1271
    • Zelko, I.N.1    Folz, R.J.2
  • 39
    • 48649091699 scopus 로고    scopus 로고
    • Transcription factors sp1 and sp3 regulate expression of human extracellular superoxide dismutase in lung fibroblasts
    • I.N. Zelko, M.R. Mueller, and R.J. Folz Transcription factors sp1 and sp3 regulate expression of human extracellular superoxide dismutase in lung fibroblasts Am. J. Respir. Cell Mol. Biol. 39 2008 243 251
    • (2008) Am. J. Respir. Cell Mol. Biol. , vol.39 , pp. 243-251
    • Zelko, I.N.1    Mueller, M.R.2    Folz, R.J.3
  • 40
    • 77249099223 scopus 로고    scopus 로고
    • CpG methylation attenuates Sp1 and Sp3 binding to the human extracellular superoxide dismutase promoter and regulates its cell-specific expression
    • I.N. Zelko, M.R. Mueller, and R.J. Folz CpG methylation attenuates Sp1 and Sp3 binding to the human extracellular superoxide dismutase promoter and regulates its cell-specific expression Free Radic. Biol. Med. 48 2010 895 904
    • (2010) Free Radic. Biol. Med. , vol.48 , pp. 895-904
    • Zelko, I.N.1    Mueller, M.R.2    Folz, R.J.3
  • 41
    • 0032775099 scopus 로고    scopus 로고
    • Nitrotyrosine formation with endotoxin-induced kidney injury detected by immunohistochemistry
    • K. Bian, K. Davis, J. Kuret, L. Binder, and F. Murad Nitrotyrosine formation with endotoxin-induced kidney injury detected by immunohistochemistry Am. J. Physiol. 277 1999 F33 40
    • (1999) Am. J. Physiol. , vol.277 , pp. 33-40
    • Bian, K.1    Davis, K.2    Kuret, J.3    Binder, L.4    Murad, F.5
  • 42
    • 59849109478 scopus 로고    scopus 로고
    • The coagulation system and pulmonary endothelial function in acute lung injury
    • Finigan J.H. The coagulation system and pulmonary endothelial function in acute lung injury Microvasc. Res. 77 2009 35 38
    • (2009) Microvasc. Res. , vol.77 , pp. 35-38
    • Finigan, J.H.1
  • 43
    • 0034807581 scopus 로고    scopus 로고
    • Cytoskeletal regulation of pulmonary vascular permeability
    • S.M. Dudek, and J.G. Garcia Cytoskeletal regulation of pulmonary vascular permeability J. Appl. Physiol. 91 2001 1487 1500
    • (2001) J. Appl. Physiol. , vol.91 , pp. 1487-1500
    • Dudek, S.M.1    Garcia, J.G.2
  • 45
    • 0027471907 scopus 로고
    • Effect of fibronectin on permeability of normal and TNF-treated lung endothelial cell monolayers
    • E.M. Wheatley, P.A. Vincent, P.J. McKeown-Longo, and T.M. Saba Effect of fibronectin on permeability of normal and TNF-treated lung endothelial cell monolayers Am. J. Physiol. 264 1993 R90 96
    • (1993) Am. J. Physiol. , vol.264 , pp. 90-96
    • Wheatley, E.M.1    Vincent, P.A.2    McKeown-Longo, P.J.3    Saba, T.M.4
  • 48
    • 0023655235 scopus 로고
    • An abundant and novel protein of 22 kDa (SM22) is widely distributed in smooth muscles: Purification from bovine aorta
    • J.P. Lees-Miller, D.H. Heeley, and L.B. Smillie An abundant and novel protein of 22 kDa (SM22) is widely distributed in smooth muscles: purification from bovine aorta Biochem. J. 244 1987 705 709
    • (1987) Biochem. J. , vol.244 , pp. 705-709
    • Lees-Miller, J.P.1    Heeley, D.H.2    Smillie, L.B.3
  • 49
    • 0023644595 scopus 로고
    • Isolation and characterization of an abundant and novel 22-kDa protein (SM22) from chicken gizzard smooth muscle
    • J.P. Lees-Miller, D.H. Heeley, L.B. Smillie, and C.M. Kay Isolation and characterization of an abundant and novel 22-kDa protein (SM22) from chicken gizzard smooth muscle J. Biol. Chem. 262 1987 2988 2993
    • (1987) J. Biol. Chem. , vol.262 , pp. 2988-2993
    • Lees-Miller, J.P.1    Heeley, D.H.2    Smillie, L.B.3    Kay, C.M.4
  • 50
    • 77952508026 scopus 로고    scopus 로고
    • Disruption of SM22 promotes inflammation after artery injury via nuclear factor kappaB activation
    • J. Shen, M. Yang, D. Ju, H. Jiang, J.P. Zheng, Z. Xu, and L. Li Disruption of SM22 promotes inflammation after artery injury via nuclear factor kappaB activation Circ. Res. 106 2010 1351 1362
    • (2010) Circ. Res. , vol.106 , pp. 1351-1362
    • Shen, J.1    Yang, M.2    Ju, D.3    Jiang, H.4    Zheng, J.P.5    Xu, Z.6    Li, L.7
  • 51
    • 77956325999 scopus 로고    scopus 로고
    • LIM and SH3 protein-1 modulates CXCR2-mediated cell migration
    • D. Raman, J. Sai, N.F. Neel, C.S. Chew, and A. Richmond LIM and SH3 protein-1 modulates CXCR2-mediated cell migration PLoS ONE 5 2010 e10050
    • (2010) PLoS ONE , vol.5 , pp. 10050
    • Raman, D.1    Sai, J.2    Neel, N.F.3    Chew, C.S.4    Richmond, A.5
  • 52
    • 70449366424 scopus 로고    scopus 로고
    • Integrin-dependent translocation of LASP-1 to the cytoskeleton of activated platelets correlates with LASP-1 phosphorylation at tyrosine 171 by Src-kinase
    • J. Traenka, C.R. Hauck, U. Lewandrowski, A. Sickmann, S. Gambaryan, P. Thalheimer, and E. Butt Integrin-dependent translocation of LASP-1 to the cytoskeleton of activated platelets correlates with LASP-1 phosphorylation at tyrosine 171 by Src-kinase Thromb. Haemost. 102 2009 520 528
    • (2009) Thromb. Haemost. , vol.102 , pp. 520-528
    • Traenka, J.1    Hauck, C.R.2    Lewandrowski, U.3    Sickmann, A.4    Gambaryan, S.5    Thalheimer, P.6    Butt, E.7
  • 54
    • 59549106445 scopus 로고    scopus 로고
    • Proteomic analysis of protein tyrosine nitration after ischemia reperfusion injury: Mitochondria as the major target
    • B. Liu, A.K. Tewari, L. Zhang, K.B. Green-Church, J.L. Zweier, Y.R. Chen, and G. He Proteomic analysis of protein tyrosine nitration after ischemia reperfusion injury: mitochondria as the major target Biochim. Biophys. Acta 1794 2009 476 485
    • (2009) Biochim. Biophys. Acta , vol.1794 , pp. 476-485
    • Liu, B.1    Tewari, A.K.2    Zhang, L.3    Green-Church, K.B.4    Zweier, J.L.5    Chen, Y.R.6    He, G.7
  • 55
    • 0028932550 scopus 로고
    • Cloning, expression and tissue distribution of mouse tetrameric carbonyl reductase: Identity with an adipocyte 27-kDa protein
    • M. Nakanishi, Y. Deyashiki, K. Ohshima, and A. Hara Cloning, expression and tissue distribution of mouse tetrameric carbonyl reductase: identity with an adipocyte 27-kDa protein Eur. J. Biochem. 228 1995 381 387
    • (1995) Eur. J. Biochem. , vol.228 , pp. 381-387
    • Nakanishi, M.1    Deyashiki, Y.2    Ohshima, K.3    Hara, A.4
  • 57
    • 0344009504 scopus 로고    scopus 로고
    • 1-Cys peroxiredoxin knock-out mice express mRNA but not protein for a highly related intronless gene
    • Y. Mo, S.I. Feinstein, Y. Manevich, Q. Zhang, L. Lu, Y.S. Ho, and A.B. Fisher 1-Cys peroxiredoxin knock-out mice express mRNA but not protein for a highly related intronless gene FEBS Lett. 555 2003 192 198
    • (2003) FEBS Lett. , vol.555 , pp. 192-198
    • Mo, Y.1    Feinstein, S.I.2    Manevich, Y.3    Zhang, Q.4    Lu, L.5    Ho, Y.S.6    Fisher, A.B.7
  • 59
    • 34547734976 scopus 로고    scopus 로고
    • The neutrophil serine protease inhibitor serpinb1 preserves lung defense functions in Pseudomonas aeruginosa infection
    • C. Benarafa, G.P. Priebe, and E. Remold-O'Donnell The neutrophil serine protease inhibitor serpinb1 preserves lung defense functions in Pseudomonas aeruginosa infection J. Exp. Med. 204 2007 1901 1909
    • (2007) J. Exp. Med. , vol.204 , pp. 1901-1909
    • Benarafa, C.1    Priebe, G.P.2    Remold-O'Donnell, E.3
  • 60
    • 13444287817 scopus 로고    scopus 로고
    • Aerosol treatment with MNEI suppresses bacterial proliferation in a model of chronic Pseudomonas aeruginosa lung infection
    • D.E. Woods, A. Cantin, J. Cooley, D.M. Kenney, and E. Remold-O'Donnell Aerosol treatment with MNEI suppresses bacterial proliferation in a model of chronic Pseudomonas aeruginosa lung infection Pediatr. Pulmonol. 39 2005 141 149
    • (2005) Pediatr. Pulmonol. , vol.39 , pp. 141-149
    • Woods, D.E.1    Cantin, A.2    Cooley, J.3    Kenney, D.M.4    Remold-O'Donnell, E.5
  • 61
    • 0032880537 scopus 로고    scopus 로고
    • Oxidative damage to proteins of bronchoalveolar lavage fluid in patients with acute respiratory distress syndrome: Evidence for neutrophil-mediated hydroxylation, nitration, and chlorination
    • N.J. Lamb, J.M. Gutteridge, C. Baker, T.W. Evans, and G.J. Quinlan Oxidative damage to proteins of bronchoalveolar lavage fluid in patients with acute respiratory distress syndrome: evidence for neutrophil-mediated hydroxylation, nitration, and chlorination Crit. Care Med. 27 1999 1738 1744
    • (1999) Crit. Care Med. , vol.27 , pp. 1738-1744
    • Lamb, N.J.1    Gutteridge, J.M.2    Baker, C.3    Evans, T.W.4    Quinlan, G.J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.