메뉴 건너뛰기




Volumn 110, Issue 6 SUPPL., 1996, Pages 261S-266S

Use of secretory leukoprotease inhibitor to augment lung antineutrophil elastase activity

Author keywords

antiproteases; secretory leukoprotease inhibitor; therapy

Indexed keywords

LEUKOCYTE ELASTASE; SECRETORY LEUKOCYTE PROTEINASE INHIBITOR;

EID: 0030448955     PISSN: 00123692     EISSN: None     Source Type: Journal    
DOI: 10.1378/chest.110.6_Supplement.261S     Document Type: Article
Times cited : (52)

References (58)
  • 1
    • 0013841509 scopus 로고
    • Über einen hormonabhängigen inhibitor für proteolytische Enzyme in männlichen accessorischen Geschlechtsdrüsen und im Sperma
    • Haendle H, Fritz H, Trautschold I, et al. Über einen hormonabhängigen inhibitor für proteolytische Enzyme in männlichen accessorischen Geschlechtsdrüsen und im Sperma. Hoppe Seyler Z Physiol Chem 1965; 343:185-88
    • (1965) Hoppe Seyler Z Physiol Chem , vol.343 , pp. 185-188
    • Haendle, H.1    Fritz, H.2    Trautschold, I.3
  • 2
    • 0015289767 scopus 로고
    • Isolierung und Charakterisierung eines Proteaseninhibitors aus menschlichem Bronchialsekret
    • Hochstrasser K, Reichert R, Schwarz S, et al. Isolierung und Charakterisierung eines Proteaseninhibitors aus menschlichem Bronchialsekret. Hoppe Seyler Z Physiol Chem 1972; 353:221-26
    • (1972) Hoppe Seyler Z Physiol Chem , vol.353 , pp. 221-226
    • Hochstrasser, K.1    Reichert, R.2    Schwarz, S.3
  • 3
    • 0016248240 scopus 로고
    • Characterization of an acid-stable proteinase inhibitor in human cervical mucus
    • Wallner O, Fritz H. Characterization of an acid-stable proteinase inhibitor in human cervical mucus. Hoppe Seyler Z Physiol Chem 1974; 355:709-15
    • (1974) Hoppe Seyler Z Physiol Chem , vol.355 , pp. 709-715
    • Wallner, O.1    Fritz, H.2
  • 4
    • 0022622799 scopus 로고
    • Inhibitors of trypsin, chymotrypsin and elastase in human uterine fluid
    • Casslen B. Inhibitors of trypsin, chymotrypsin and elastase in human uterine fluid. Acta Obstet Gynecol Scand 1986; 65:121-24
    • (1986) Acta Obstet Gynecol Scand , vol.65 , pp. 121-124
    • Casslen, B.1
  • 5
    • 0024498944 scopus 로고
    • Tissue distribution of antileukoprotease and lysozyme in humans
    • Franken C, Meijer CJLM, Dijkman JH. Tissue distribution of antileukoprotease and lysozyme in humans. J Histochem Cytochem 1989; 37:493-98
    • (1989) J Histochem Cytochem , vol.37 , pp. 493-498
    • Franken, C.1    Meijer, C.J.L.M.2    Dijkman, J.H.3
  • 6
    • 0026026199 scopus 로고
    • Purification of a serine-proteinase inhibitor from human articular cartilage
    • Böhm B, Deutzmann R, Burkhardt H. Purification of a serine-proteinase inhibitor from human articular cartilage. Biochem J 1991; 274:269-73
    • (1991) Biochem J , vol.274 , pp. 269-273
    • Böhm, B.1    Deutzmann, R.2    Burkhardt, H.3
  • 7
    • 0023890859 scopus 로고
    • Human mucus proteinase inhibitor (human MPI)
    • Fritz H. Human mucus proteinase inhibitor (human MPI). Biol Chem Hoppe-Seyler 1988; 369:79-82
    • (1988) Biol Chem Hoppe-Seyler , vol.369 , pp. 79-82
    • Fritz, H.1
  • 8
    • 0025274374 scopus 로고
    • Location of the protease-inhibitory region of secretory leukocyte protease inhibitor
    • Eisenberg SP, Hale KK, Heimdal P, et al. Location of the protease-inhibitory region of secretory leukocyte protease inhibitor. J Biol Chem 1990; 265:7976-81
    • (1990) J Biol Chem , vol.265 , pp. 7976-7981
    • Eisenberg, S.P.1    Hale, K.K.2    Heimdal, P.3
  • 9
    • 0025228671 scopus 로고
    • Proteinase inhibitory activities of antileukoprotease are represented by its second COOH-terminal domain
    • Kramps JA, van Twisk Ch, Appelhans H, et al. Proteinase inhibitory activities of antileukoprotease are represented by its second COOH-terminal domain. Biochim Biophys Acta 1990; 1038: 178-85
    • (1990) Biochim Biophys Acta , vol.1038 , pp. 178-185
    • Kramps, J.A.1    Van Twisk, Ch.2    Appelhans, H.3
  • 10
    • 0025938090 scopus 로고
    • Separation of the two domains of human mucus proteinase inhibitor: Inhibitory activity is only located in the carboxy-terminal domain
    • Van-Seuningen I, Davril M. Separation of the two domains of human mucus proteinase inhibitor: inhibitory activity is only located in the carboxy-terminal domain. Biochem Biophys Res Commun 1991; 179:1587-92
    • (1991) Biochem Biophys Res Commun , vol.179 , pp. 1587-1592
    • Van-Seuningen, I.1    Davril, M.2
  • 11
    • 0022479785 scopus 로고
    • The acid-stable proteinase inhibitor of human mucous secretions (HUSI-I, antileukoprotease)
    • Seemüller U, Arnhold M, Fritz H, et al. The acid-stable proteinase inhibitor of human mucous secretions (HUSI-I, antileukoprotease). FEBS Lett 1986; 199:43-8
    • (1986) FEBS Lett , vol.199 , pp. 43-48
    • Seemüller, U.1    Arnhold, M.2    Fritz, H.3
  • 12
    • 0012030796 scopus 로고
    • Isolation, properties, and complete amino acid sequence of human secretory leukocyte protease inhibitor, a potent inhibitor of leukocyte elastase
    • Thompson RC, Ohlsson K. Isolation, properties, and complete amino acid sequence of human secretory leukocyte protease inhibitor, a potent inhibitor of leukocyte elastase. Proc Natl Acad Sci USA 1986; 83:6692-96
    • (1986) Proc Natl Acad Sci USA , vol.83 , pp. 6692-6696
    • Thompson, R.C.1    Ohlsson, K.2
  • 13
    • 0023614958 scopus 로고
    • Purification and characterization of human bronchial proteinase inhibitor
    • Boudier C, Carvallo D, Roitsch C, et al. Purification and characterization of human bronchial proteinase inhibitor. Arch Biochem Biophys 1987; 253:439-45
    • (1987) Arch Biochem Biophys , vol.253 , pp. 439-445
    • Boudier, C.1    Carvallo, D.2    Roitsch, C.3
  • 14
    • 0040469390 scopus 로고
    • The 2.5 Å x-ray crystal structure of the acid-stable proteinase inhibitor from human mucous secretions analysed in its complex with bovine alpha-chymotrypsin
    • Grütter MG, Fendrich G, Huber R, et al. The 2.5 Å x-ray crystal structure of the acid-stable proteinase inhibitor from human mucous secretions analysed in its complex with bovine alpha-chymotrypsin. EMBO J 1988; 7:345-51
    • (1988) EMBO J , vol.7 , pp. 345-351
    • Grütter, M.G.1    Fendrich, G.2    Huber, R.3
  • 15
    • 0001446596 scopus 로고
    • Antiproteases
    • Crystal RG, West JB, Barnes PJ, et al, eds. New York: Raven Press
    • Hubbard RC, Crystal RG. Antiproteases. In: Crystal RG, West JB, Barnes PJ, et al, eds. The lung - scientific foundations. New York: Raven Press, 1991; 1775-87
    • (1991) The Lung - Scientific Foundations , pp. 1775-1787
    • Hubbard, R.C.1    Crystal, R.G.2
  • 16
    • 0023056196 scopus 로고
    • Isolation and sequence of a human gene encoding a potent inhibitor of leukocyte proteases
    • Stetler G, Brewer MT, Thompson RC. Isolation and sequence of a human gene encoding a potent inhibitor of leukocyte proteases. Nucleic Acids Res 1986; 14:7883-96
    • (1986) Nucleic Acids Res , vol.14 , pp. 7883-7896
    • Stetler, G.1    Brewer, M.T.2    Thompson, R.C.3
  • 17
    • 0020058870 scopus 로고
    • Kinetics of the inhibition of leukocyte elastase by the bronchial inhibitor
    • Gauthier F, Fryksmark U, Ohlsson K, et al. Kinetics of the inhibition of leukocyte elastase by the bronchial inhibitor. Biochem Biophys Acta 1982; 700:178-83
    • (1982) Biochem Biophys Acta , vol.700 , pp. 178-183
    • Gauthier, F.1    Fryksmark, U.2    Ohlsson, K.3
  • 18
    • 0021960034 scopus 로고
    • Human bronchial leucocyte proteinase inhibitor
    • Smith CE, Johnson DA. Human bronchial leucocyte proteinase inhibitor. Biochem J 1985; 225:463-72
    • (1985) Biochem J , vol.225 , pp. 463-472
    • Smith, C.E.1    Johnson, D.A.2
  • 19
    • 0022967879 scopus 로고
    • Inhibition of mast cell chymase by eglin c and antileukoprotease (HUSI-I)
    • Fink E, Nettelbeck R, Fritz H. Inhibition of mast cell chymase by eglin c and antileukoprotease (HUSI-I). Biol Chem Hoppe Seyler 1986; 367:567-71
    • (1986) Biol Chem Hoppe Seyler , vol.367 , pp. 567-571
    • Fink, E.1    Nettelbeck, R.2    Fritz, H.3
  • 20
    • 0025782538 scopus 로고
    • Potential problems in designing elastase inhibitors for therapy
    • Travis J, Fritz H. Potential problems in designing elastase inhibitors for therapy. Am Rev Respir Dis 1991; 143:1412-15
    • (1991) Am Rev Respir Dis , vol.143 , pp. 1412-1415
    • Travis, J.1    Fritz, H.2
  • 21
    • 0026827058 scopus 로고
    • Inhibition of human, ovine, and baboon neutrophil elastase with eglin c and secretory leukocyte proteinase inhibitor
    • Junger WG, Hallström S, Redl H, et al. Inhibition of human, ovine, and baboon neutrophil elastase with eglin c and secretory leukocyte proteinase inhibitor. Biol Chem Hoppe Seyler 1992; 373:119-22
    • (1992) Biol Chem Hoppe Seyler , vol.373 , pp. 119-122
    • Junger, W.G.1    Hallström, S.2    Redl, H.3
  • 22
    • 0019981121 scopus 로고
    • Distribution of antileukoprotease in upper respiratory mucosa
    • Fryksmark U, Ohlsson K, Polling A, et al. Distribution of antileukoprotease in upper respiratory mucosa. Ann Otol Rhinol Laryngol 1982; 91:268-71
    • (1982) Ann Otol Rhinol Laryngol , vol.91 , pp. 268-271
    • Fryksmark, U.1    Ohlsson, K.2    Polling, A.3
  • 23
    • 0020676623 scopus 로고
    • Localisation of a low-molecular-weight bronchial protease inhibitor in the peripheral human lung
    • Mooren HWD, Kramps JA, Franken C, et al. Localisation of a low-molecular-weight bronchial protease inhibitor in the peripheral human lung. Thorax 1983; 38:180-83
    • (1983) Thorax , vol.38 , pp. 180-183
    • Mooren, H.W.D.1    Kramps, J.A.2    Franken, C.3
  • 24
    • 0022620754 scopus 로고
    • Ultrastructural localization of bronchial antileukoprotease in central and peripheral human airways by a gold-labeling technique using monoclonal antibodies
    • De Water R, Willems LNA, Van Muijen GNP, et al. Ultrastructural localization of bronchial antileukoprotease in central and peripheral human airways by a gold-labeling technique using monoclonal antibodies. Am Rev Respir Dis 1986; 133:882-90
    • (1986) Am Rev Respir Dis , vol.133 , pp. 882-890
    • De Water, R.1    Willems, L.N.A.2    Van Muijen, G.N.P.3
  • 26
    • 0026042309 scopus 로고
    • Expression of the secretory leukoprotease inhibitor gene in epithelial cells
    • Abe T, Kobayashi N, Yoshimura K, et al. Expression of the secretory leukoprotease inhibitor gene in epithelial cells. J Clin Invest 1991; 87:2207-15
    • (1991) J Clin Invest , vol.87 , pp. 2207-2215
    • Abe, T.1    Kobayashi, N.2    Yoshimura, K.3
  • 27
    • 0023686059 scopus 로고
    • 1-proteinase inhibitor in peripheral airspaces of the human lung
    • 1-proteinase inhibitor in peripheral airspaces of the human lung. Clin Sci 1988; 75:351-53
    • (1988) Clin Sci , vol.75 , pp. 351-353
    • Kramps, J.A.1    Franken, C.2    Dijkman, J.H.3
  • 28
    • 0022580099 scopus 로고
    • Comparison of concentrations of two proteinase inhibitors, porcine pancreatic elastase inhibitory capacity, and cell profiles in sequential bronchoalveolar lavage samples
    • Morrison HM, Kramps JA, Dijkman JH, et al. Comparison of concentrations of two proteinase inhibitors, porcine pancreatic elastase inhibitory capacity, and cell profiles in sequential bronchoalveolar lavage samples. Thorax 1986; 41:435-41
    • (1986) Thorax , vol.41 , pp. 435-441
    • Morrison, H.M.1    Kramps, J.A.2    Dijkman, J.H.3
  • 29
    • 0026029117 scopus 로고
    • Anti-neutrophil elastase defense of the normal human respiratory epithelial surface provided by the secretory leukoprotease inhibitor
    • Vogelmeier C, Hubbard RC, Fells GA, et al. Anti-neutrophil elastase defense of the normal human respiratory epithelial surface provided by the secretory leukoprotease inhibitor. J Clin Invest 1991; 87:482-88
    • (1991) J Clin Invest , vol.87 , pp. 482-488
    • Vogelmeier, C.1    Hubbard, R.C.2    Fells, G.A.3
  • 31
    • 0023925114 scopus 로고
    • Replacement therapy for alpha-1-protease inhibitor deficiency in PiZ subjects with chronic obstructive lung disease
    • Schmidt EW, Rasche B, Ulmer WT, et al. Replacement therapy for alpha-1-protease inhibitor deficiency in PiZ subjects with chronic obstructive lung disease. Am J Med 1988; 84:63S-9S
    • (1988) Am J Med , vol.84
    • Schmidt, E.W.1    Rasche, B.2    Ulmer, W.T.3
  • 35
    • 0018876040 scopus 로고
    • The degradation of human lung elastin by neutrophil proteinases
    • Reilly CF, Travis J. The degradation of human lung elastin by neutrophil proteinases. Biochim Biophys Acta 1980; 621:147-57
    • (1980) Biochim Biophys Acta , vol.621 , pp. 147-157
    • Reilly, C.F.1    Travis, J.2
  • 36
    • 0019985854 scopus 로고
    • Effect of different elastase inhibitors on leukocyte elastase pre-adsorbed to elastin
    • Hornebeck W, Schnebli HP. Effect of different elastase inhibitors on leukocyte elastase pre-adsorbed to elastin. Hoppe Seyler Z Physiol Chem 1982; 363:455-58
    • (1982) Hoppe Seyler Z Physiol Chem , vol.363 , pp. 455-458
    • Hornebeck, W.1    Schnebli, H.P.2
  • 37
    • 0022461518 scopus 로고
    • 1-proteinase inhibitor and bronchial inhibitor
    • 1-proteinase inhibitor and bronchial inhibitor. Biochem J 1986; 238:269-73
    • (1986) Biochem J , vol.238 , pp. 269-273
    • Bruch, M.1    Bieth, J.G.2
  • 38
    • 0024524860 scopus 로고
    • Secretory leukocyte protease inhibitor binding to mRNA and DNA as a possible cause of toxicity to Escherichia coli
    • Miller KW, Evans RJ, Eisenberg SP, et al. Secretory leukocyte protease inhibitor binding to mRNA and DNA as a possible cause of toxicity to Escherichia coli. J Bacteriol 1989; 171:2166-72
    • (1989) J Bacteriol , vol.171 , pp. 2166-2172
    • Miller, K.W.1    Evans, R.J.2    Eisenberg, S.P.3
  • 40
    • 0023588232 scopus 로고
    • Augmentation of lung antineutrophil elastase capacity with recombinant human alpha-1-antitrypsin
    • Casolaro MA, Fells G, Wewers M, et al. Augmentation of lung antineutrophil elastase capacity with recombinant human alpha-1-antitrypsin. J Appl Physiol 1987; 63:2015-23
    • (1987) J Appl Physiol , vol.63 , pp. 2015-2023
    • Casolaro, M.A.1    Fells, G.2    Wewers, M.3
  • 42
    • 0025640798 scopus 로고
    • Aerosolization of recombinant SLPI to augment antineutrophil elastase protection of pulmonary epithelium
    • Vogelmeier C, Buhl R, Hoyt RF, et al. Aerosolization of recombinant SLPI to augment antineutrophil elastase protection of pulmonary epithelium. J Appl Physiol 1990; 69:1843-48
    • (1990) J Appl Physiol , vol.69 , pp. 1843-1848
    • Vogelmeier, C.1    Buhl, R.2    Hoyt, R.F.3
  • 43
    • 0019321009 scopus 로고
    • Kinetics of association of serine proteinases with native and oxidized alpha-1-proteinase inhibitor and alpha-1-antichymotrypsin
    • Beatty K, Bieth J, Travis J. Kinetics of association of serine proteinases with native and oxidized alpha-1-proteinase inhibitor and alpha-1-antichymotrypsin. J Biol Chem 1980; 255:3931-34
    • (1980) J Biol Chem , vol.255 , pp. 3931-3934
    • Beatty, K.1    Bieth, J.2    Travis, J.3
  • 45
    • 0022204452 scopus 로고
    • Estimation of volume of epithelial lining fluid recovered by lavage using urea as marker of dilution
    • Rennard SI, Basset G, Lecossier D, et al. Estimation of volume of epithelial lining fluid recovered by lavage using urea as marker of dilution. J Appl Physiol 1986; 60:532-38
    • (1986) J Appl Physiol , vol.60 , pp. 532-538
    • Rennard, S.I.1    Basset, G.2    Lecossier, D.3
  • 46
    • 0016819747 scopus 로고
    • Preparation of chronic lung lymph fistulas in sheep
    • Staub NC, Bland RD, Brigham KL, et al. Preparation of chronic lung lymph fistulas in sheep. J Surg Res 1975; 19:315-20
    • (1975) J Surg Res , vol.19 , pp. 315-320
    • Staub, N.C.1    Bland, R.D.2    Brigham, K.L.3
  • 47
    • 0024344262 scopus 로고
    • Chronic obstructive pulmonary disease: Risk factors, pathophysiology and pathogenesis
    • Snider GL. Chronic obstructive pulmonary disease: risk factors, pathophysiology and pathogenesis. Annu Rev Med 1989; 40: 411-29
    • (1989) Annu Rev Med , vol.40 , pp. 411-429
    • Snider, G.L.1
  • 48
    • 0025212549 scopus 로고
    • Recombinant human secretory leukocyte-protease inhibitor: In vitro properties, and amelioration of human neutrophil elastase-induced emphysema and secretory cell metaplasia in the hamster
    • Lucey EC, Stone PJ, Ciccolella DE, et al. Recombinant human secretory leukocyte-protease inhibitor: in vitro properties, and amelioration of human neutrophil elastase-induced emphysema and secretory cell metaplasia in the hamster. J Lab Clin Med 1990; 115:224-32
    • (1990) J Lab Clin Med , vol.115 , pp. 224-232
    • Lucey, E.C.1    Stone, P.J.2    Ciccolella, D.E.3
  • 49
    • 0027533675 scopus 로고
    • Inhibition of lipopolysaccharide-induced pulmonary emphysema by intratracheally instilled recombinant secretory leukocyte proteinase inhibitor
    • Rudolphus A, Stolk J, Dijkman JH, et al. Inhibition of lipopolysaccharide-induced pulmonary emphysema by intratracheally instilled recombinant secretory leukocyte proteinase inhibitor. Am Rev Respir Dis 1993; 147:442-47
    • (1993) Am Rev Respir Dis , vol.147 , pp. 442-447
    • Rudolphus, A.1    Stolk, J.2    Dijkman, J.H.3
  • 50
    • 0025233869 scopus 로고
    • Pharmacokinetics and distribution of recombinant secretory leukocyte proteinase inhibitor in rats
    • Gast A, Anderson W, Probst A, et al. Pharmacokinetics and distribution of recombinant secretory leukocyte proteinase inhibitor in rats. Am Rev Respir Dis 1990; 141:889-94
    • (1990) Am Rev Respir Dis , vol.141 , pp. 889-894
    • Gast, A.1    Anderson, W.2    Probst, A.3
  • 51
    • 0026769518 scopus 로고
    • Intravenous recombinant secretory leukoprotease inhibitor augments antineutrophil elastase defense
    • Birrer P, McElvaney NG, Gillissen A, et al. Intravenous recombinant secretory leukoprotease inhibitor augments antineutrophil elastase defense. J Appl Physiol 1992; 73:317-23
    • (1992) J Appl Physiol , vol.73 , pp. 317-323
    • Birrer, P.1    McElvaney, N.G.2    Gillissen, A.3
  • 52
    • 0024421453 scopus 로고
    • Neutrophil-activating peptide-1/interleukin 8, a novel cytokine that activates neutrophils
    • Baggiolini M, Walz A, Kunkel SL. Neutrophil-activating peptide-1/interleukin 8, a novel cytokine that activates neutrophils. J Clin Invest 1989; 84:1045-49
    • (1989) J Clin Invest , vol.84 , pp. 1045-1049
    • Baggiolini, M.1    Walz, A.2    Kunkel, S.L.3
  • 53
    • 0026681802 scopus 로고
    • Neutrophil elastase in respiratory epithelial lining fluid of individuals with cystic fibrosis induces interleukin-8 gene expression in a human bronchial epithelial cell line
    • Nakamura H, Yoshimura K, McElvaney NG, et al. Neutrophil elastase in respiratory epithelial lining fluid of individuals with cystic fibrosis induces interleukin-8 gene expression in a human bronchial epithelial cell line. J Clin Invest 1992; 89:1478-84
    • (1992) J Clin Invest , vol.89 , pp. 1478-1484
    • Nakamura, H.1    Yoshimura, K.2    McElvaney, N.G.3
  • 54
    • 0026474443 scopus 로고
    • Modulation of airway inflammation in cystic fibrosis
    • McElvaney NG, Nakamura H, Birrer P, et al. Modulation of airway inflammation in cystic fibrosis. J Clin Invest 1992; 90:1296-1301
    • (1992) J Clin Invest , vol.90 , pp. 1296-1301
    • McElvaney, N.G.1    Nakamura, H.2    Birrer, P.3
  • 55
    • 0027184036 scopus 로고
    • Recombinant secretory leukoprotease inhibitor augments glutathione levels in respiratory epithelial lining fluid
    • Gillissen A, Birrer P, Buhl R, et al. Recombinant secretory leukoprotease inhibitor augments glutathione levels in respiratory epithelial lining fluid. J Appl Phjsiol 1993; 75:825-32
    • (1993) J Appl Phjsiol , vol.75 , pp. 825-832
    • Gillissen, A.1    Birrer, P.2    Buhl, R.3
  • 56
    • 0025282179 scopus 로고
    • Augmentation of glutathione in the fluid lining the epithelium of the lower respiratory tract by directly administering glutathione aerosol
    • Buhl R, Vogelmeier C, Critenden M, et al. Augmentation of glutathione in the fluid lining the epithelium of the lower respiratory tract by directly administering glutathione aerosol. Proc Natl Acad Sci USA 1990; 87:4063-67
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 4063-4067
    • Buhl, R.1    Vogelmeier, C.2    Critenden, M.3
  • 57
    • 0345654274 scopus 로고
    • Glutathione: Interorgan translocation, turnover, and metabolism
    • Griffith OW, Meister A. Glutathione: interorgan translocation, turnover, and metabolism. Proc Natl Acad Sci USA 1979; 76:5606-10
    • (1979) Proc Natl Acad Sci USA , vol.76 , pp. 5606-5610
    • Griffith, O.W.1    Meister, A.2
  • 58
    • 0028230612 scopus 로고
    • The effect of oral N-acetylcysteine on lung glutathione levels in idiopathic pulmonary fibrosis
    • Meyer A, Buhl R, Magnussen H. The effect of oral N-acetylcysteine on lung glutathione levels in idiopathic pulmonary fibrosis. Eur Respir J 1994; 7:431-36
    • (1994) Eur Respir J , vol.7 , pp. 431-436
    • Meyer, A.1    Buhl, R.2    Magnussen, H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.