메뉴 건너뛰기




Volumn 40, Issue 6, 2009, Pages

Glycoprotein analysis of porcine bronchoalveolar lavage fluid reveals potential biomarkers corresponding to resistance to Actinobacillus pleuropneumoniae infection

Author keywords

Biomarker; Bronchoalveolar lavage fluid; Glycoprotein analysis; Porcine respiratory disease

Indexed keywords

ALPHA 1 ANTICHYMOTRYPSIN; FETUIN A; GLYCOPHORIN A; GLYCOPROTEIN; HAPTOGLOBIN; HEMOGLOBIN; HYALURONIDASE; INTER ALPHA TRYPSIN INHIBITOR; OROSOMUCOID; PROPERDIN; SURFACTANT PROTEIN D; TRANSFERRIN; BIOLOGICAL MARKER;

EID: 70349558546     PISSN: 09284249     EISSN: 12979716     Source Type: Journal    
DOI: 10.1051/vetres/2009043     Document Type: Article
Times cited : (7)

References (54)
  • 1
    • 0026045918 scopus 로고
    • Isolation and molecular characterization of spontaneously occurring cytolysin-negative mutants of Actinobacillus pleuropneumoniae serotype 7
    • Anderson C., Potter A.A., Gerlach G.F., Isolation and molecular characterization of spontaneously occurring cytolysin-negative mutants of Actinobacillus pleuropneumoniae serotype 7, Infect. Immun. (1991) 59:4110-4116.
    • (1991) Infect. Immun. , vol.59 , pp. 4110-4116
    • Anderson, C.1    Potter, A.A.2    Gerlach, G.F.3
  • 2
    • 0032754473 scopus 로고    scopus 로고
    • On the frequency of protein glycosylation, as deduced from analysis of the SWISS-PROT database
    • Apweiler R., Hermjakob H., Sharon N., On the frequency of protein glycosylation, as deduced from analysis of the SWISS-PROT database, Biochim. Biophys. Acta (1999) 1473:4-8.
    • (1999) Biochim. Biophys. Acta , vol.1473 , pp. 4-8
    • Apweiler, R.1    Hermjakob, H.2    Sharon, N.3
  • 3
    • 1042269503 scopus 로고    scopus 로고
    • Innate immunity in the lung: How epithelial cells fight against respiratory pathogens
    • Bals R., Hiemstra P.S., Innate immunity in the lung: how epithelial cells fight against respiratory pathogens, Eur. Respir. J. (2004) 23:327-333.
    • (2004) Eur. Respir. J. , vol.23 , pp. 327-333
    • Bals, R.1    Hiemstra, P.S.2
  • 5
    • 49449112313 scopus 로고    scopus 로고
    • Innate immune functions of the airway epithelium, Contrib
    • Bartlett J.A., Fischer A.J., McCray P.B. Jr, Innate immune functions of the airway epithelium, Contrib. Microbiol. (2008) 15:147-163.
    • (2008) Microbiol. , vol.15 , pp. 147-163
    • Bartlett, J.A.1    Fischer, A.J.2    McCray Jr., P.B.3
  • 6
    • 66249093160 scopus 로고    scopus 로고
    • Analysis of the Actinobacillus pleuropneumoniae HlyX (FNR) regulon and identification of iron-regulated protein B as an essential virulence factor
    • Buettner F.F., Bendalla I.M., Bosse J.T., Meens J., Nash J.H., Hartig E., et al., Analysis of the Actinobacillus pleuropneumoniae HlyX (FNR) regulon and identification of iron-regulated protein B as an essential virulence factor, Proteomics (2009) 9:2383-2398.
    • (2009) Proteomics , vol.9 , pp. 2383-2398
    • Buettner, F.F.1    Bendalla, I.M.2    Bosse, J.T.3    Meens, J.4    Nash, J.H.5    Hartig, E.6
  • 7
    • 0036709842 scopus 로고    scopus 로고
    • Evaluation of serology, bacteriological isolation and polymerase chain reaction for the detection of pigs carrying Actinobacillus pleuropneumoniae in the upper respiratory tract after experimental infection
    • Chiers K., Donne E., Van Overbeke I., Ducatelle R., Haesebrouck F., Evaluation of serology, bacteriological isolation and polymerase chain reaction for the detection of pigs carrying Actinobacillus pleuropneumoniae in the upper respiratory tract after experimental infection, Vet. Microbiol. (2002) 88:385-392.
    • (2002) Vet. Microbiol. , vol.88 , pp. 385-392
    • Chiers, K.1    Donne, E.2    Van Overbeke, I.3    Ducatelle, R.4    Haesebrouck, F.5
  • 8
    • 0033933474 scopus 로고    scopus 로고
    • The novel acute phase protein, IHRP, inhibits actin polymerization and phagocytosis of polymorphonuclear cells
    • Choi-Miura N.H., Takahashi K., Yoda M., Saito K., Hori M., Ozaki H., et al., The novel acute phase protein, IHRP, inhibits actin polymerization and phagocytosis of polymorphonuclear cells, Inflamm. Res. (2000) 49:305-310.
    • (2000) Inflamm. Res. , vol.49 , pp. 305-310
    • Choi-Miura, N.H.1    Takahashi, K.2    Yoda, M.3    Saito, K.4    Hori, M.5    Ozaki, H.6
  • 9
    • 44449145140 scopus 로고    scopus 로고
    • Patterns of neutrophil serine protease-dependent cleavage of surfactant protein D in inflammatory lung disease
    • Cooley J., McDonald B., Accurso F.J., Crouch E.C., Remold-O'Donnell E., Patterns of neutrophil serine protease-dependent cleavage of surfactant protein D in inflammatory lung disease, J. Leukoc. Biol. (2008) 83:946-955.
    • (2008) J. Leukoc. Biol. , vol.83 , pp. 946-955
    • Cooley, J.1    McDonald, B.2    Accurso, F.J.3    Crouch, E.C.4    Remold-O'Donnell, E.5
  • 10
    • 0026758355 scopus 로고
    • Influence of Actinobacillus pleuropneumoniae serotype 2 and its cytolysins on porcine neutrophil chemiluminescence Infect
    • Dom P., Haesebrouck F., Kamp E.M., Smits M.A., Influence of Actinobacillus pleuropneumoniae serotype 2 and its cytolysins on porcine neutrophil chemiluminescence, Infect. Immun. (1992) 60: 4328-4334.
    • (1992) Immun. , vol.60 , pp. 4328-4334
    • Dom, P.1    Haesebrouck, F.2    Kamp, E.M.3    Smits, M.A.4
  • 11
    • 0026429899 scopus 로고
    • Environmental factors affecting the severity of pneumonia in pigs
    • Done S.H., Environmental factors affecting the severity of pneumonia in pigs, Vet. Rec. (1991) 128: 582-586.
    • (1991) Vet. Rec. , vol.128 , pp. 582-586
    • Done, S.H.1
  • 12
    • 0031889843 scopus 로고    scopus 로고
    • Modification of macrophage response to lipopolysaccharide by fetuin Immunol
    • Dziegielewska K.M., Andersen N.A., Saunders N.R., Modification of macrophage response to lipopolysaccharide by fetuin, Immunol. Lett. (1998) 60: 31-35.
    • (1998) Lett. , vol.60 , pp. 31-35
    • Dziegielewska, K.M.1    Andersen, N.A.2    Saunders, N.R.3
  • 13
    • 70350580352 scopus 로고    scopus 로고
    • Analysis of bronchoalveolar lavage fluid proteome from systemic sclerosis patients with or without functional, clinical and radiological signs of lung
    • Fietta A., Bardoni A., Salvini R., Passadore I., Morosini M., Cavagna L., et al., Analysis of bronchoalveolar lavage fluid proteome from systemic sclerosis patients with or without functional, clinical and radiological signs of lung .brosis, Arthritis Res. Ther. (2006) 8:R160.
    • (2006) Fibrosis Arthritis Res. Ther. , vol.8
    • Fietta, A.1    Bardoni, A.2    Salvini, R.3    Passadore, I.4    Morosini, M.5    Cavagna, L.6
  • 15
    • 0033545342 scopus 로고    scopus 로고
    • Acute-phase proteins and other systemic responses to inflammation
    • Gabay C., Kushner I., Acute-phase proteins and other systemic responses to inflammation, N. Engl. J. Med. (1999) 340:448-454.
    • (1999) N. Engl. J. Med. , vol.340 , pp. 448-454
    • Gabay, C.1    Kushner, I.2
  • 17
    • 0020316141 scopus 로고
    • Tylosin tartrate and tiamutilin effects on experimental piglet pneumonia induced with pneumonic pig lung homogenate containing mycoplasmas
    • Hannan P.C., Bhogal B.S., Fish J.P., Tylosin tartrate and tiamutilin effects on experimental piglet pneumonia induced with pneumonic pig lung homogenate containing mycoplasmas, bacteria and viruses, Res. Vet. Sci. (1982) 33:76-88.
    • (1982) Bacteria and Viruses, Res. Vet. Sci. , vol.33 , pp. 76-88
    • Hannan, P.C.1    Bhogal, B.S.2    Fish, J.P.3
  • 18
    • 0031899479 scopus 로고    scopus 로고
    • The porcine acute phase response to infection with Actinobacillus pleuropneumoniae. Haptoglobin, C-reactive protein, major acute phase protein and serum amyloid A protein are sensitive indicators of infection
    • Heegaard P.M., Klausen J., Nielsen J.P., Gonzalez-Ramon N., Pineiro M., Lampreave F., Alava M.A., The porcine acute phase response to infection with Actinobacillus pleuropneumoniae. Haptoglobin, C-reactive protein, major acute phase protein and serum amyloid A protein are sensitive indicators of infection, Comp. Biochem. Physiol. B Biochem. Mol. Biol. (1998) 119:365-373.
    • (1998) Comp. Biochem. Physiol. B Biochem. Mol. Biol. , vol.119 , pp. 365-373
    • Heegaard, P.M.1    Klausen, J.2    Nielsen, J.P.3    Gonzalez-Ramon, N.4    Pineiro, M.5    Lampreave, F.6    Alava, M.A.7
  • 19
    • 0036984422 scopus 로고    scopus 로고
    • Incidence of reinfections with Mycoplasma hyopneumoniae and Actinobacillus pleuropneumoniae in pig farms located in respiratorydisease- free regions of Switzerland-identification and quantification of risk factors
    • Hege R., Zimmermann W., Scheidegger R., Stark K.D., Incidence of reinfections with Mycoplasma hyopneumoniae and Actinobacillus pleuropneumoniae in pig farms located in respiratorydisease- free regions of Switzerland- identification and quantification of risk factors, Acta Vet. Scand. (2002) 43:145-156.
    • (2002) Acta Vet. Scand. , vol.43 , pp. 145-156
    • Hege, R.1    Zimmermann, W.2    Scheidegger, R.3    Stark, K.D.4
  • 20
    • 30344489018 scopus 로고    scopus 로고
    • Differential proteomic analysis reveals increased cathelicidin expression in porcine bronchoalveolar lavage fluid after an Actinobacillus pleuropneumoniae infection
    • Hennig-Pauka I., Jacobsen I., Blecha F., Waldmann K.H., Gerlach G.F., Differential proteomic analysis reveals increased cathelicidin expression in porcine bronchoalveolar lavage fluid after an Actinobacillus pleuropneumoniae infection, Vet. Res. (2006) 37:75-87.
    • (2006) Vet. Res. , vol.37 , pp. 75-87
    • Hennig-Pauka, I.1    Jacobsen, I.2    Blecha, F.3    Waldmann, K.H.4    Gerlach, G.F.5
  • 22
    • 66149133357 scopus 로고    scopus 로고
    • A novel clinical scoring system reveals the role of innate immunity and breed in resistance to Actinobacillus pleuropneumoniae infection
    • Hoeltig D., Hennig-Pauka I., Thies K., Rehm T., Beyerbach M., Strutzberg-Minder K., et al., A novel clinical scoring system reveals the role of innate immunity and breed in resistance to Actinobacillus pleuropneumoniae infection, BMC Vet. Res. (2009) 5:14.
    • (2009) BMC Vet. Res. , vol.5 , pp. 14
    • Hoeltig, D.1    Hennig-Pauka, I.2    Thies, K.3    Rehm, T.4    Beyerbach, M.5    Strutzberg-Minder, K.6
  • 23
    • 0036567867 scopus 로고    scopus 로고
    • Characterization of the carrier state in porcine reproductive and respiratory syndrome virus infection
    • Horter D.C., Pogranichniy R.M., Chang C.C., Evans R.B., Yoon K.J., Zimmerman J.J., Characterization of the carrier state in porcine reproductive and respiratory syndrome virus infection, Vet. Microbiol. (2002) 86:213-228.
    • (2002) Vet. Microbiol. , vol.86 , pp. 213-228
    • Horter, D.C.1    Pogranichniy, R.M.2    Chang, C.C.3    Evans, R.B.4    Yoon, K.J.5    Zimmerman, J.J.6
  • 24
    • 19744370658 scopus 로고    scopus 로고
    • Deletion of the ferric uptake regulator fur impairs the in vitro growth and virulence of Actinobacillus pleuropneumoniae
    • Jacobsen I., Gerstenberger J., Gruber A.D., Bossé J.T., Langford P.R., Hennig-Pauka I., et al., Deletion of the ferric uptake regulator Fur impairs the in vitro growth and virulence of Actinobacillus pleuropneumoniae, Infect. Immun. (2005) 73: 3740-3744.
    • (2005) Infect. Immun. , vol.73 , pp. 3740-3744
    • Jacobsen, I.1    Gerstenberger, J.2    Gruber, A.D.3    Bossé, J.T.4    Langford, P.R.5    Hennig-Pauka, I.6
  • 25
    • 0035952980 scopus 로고    scopus 로고
    • Conformational properties of serine proteinase inhibitors (serpins) confer multiple pathophysiological roles
    • Janciauskiene S., Conformational properties of serine proteinase inhibitors (serpins) confer multiple pathophysiological roles, Biochim. Biophys. Acta (2001) 1535:221-235.
    • (2001) Biochim. Biophys. Acta , vol.1535 , pp. 221-235
    • Janciauskiene, S.1
  • 26
    • 13644257223 scopus 로고    scopus 로고
    • Prediction, conservation analysis, and structural characterization of mammalian mucin-type O-glycosylation sites
    • Julenius K., Molgaard A., Gupta R., Brunak S., Prediction, conservation analysis, and structural characterization of mammalian mucin-type O-glycosylation sites, Glycobiology (2005) 15:153-164.
    • (2005) Glycobiology , vol.15 , pp. 153-164
    • Julenius, K.1    Molgaard, A.2    Gupta, R.3    Brunak, S.4
  • 27
    • 0034747064 scopus 로고    scopus 로고
    • Levels of alpha1 acid glycoprotein and ceruloplasmin predict future albumin levels in hemodialysis patients
    • Kaysen G.A., Dubin J.A., Muller H.G., Mitch W.E., Levin N.W., Levels of alpha1 acid glycoprotein and ceruloplasmin predict future albumin levels in hemodialysis patients, Kidney Int. (2001) 60: 2360-2366.
    • (2001) Kidney Int. , vol.60 , pp. 2360-2366
    • Kaysen, G.A.1    Dubin, J.A.2    Muller, H.G.3    Mitch, W.E.4    Levin, N.W.5
  • 28
    • 38849125493 scopus 로고    scopus 로고
    • Usefulness of C-reactive protein and interleukin-6 as predictors of outcomes in patients with chronic obstructive pulmonary disease receiving pravastatin
    • Lee T.M., Lin M.S., Chang N.C., Usefulness of C-reactive protein and interleukin-6 as predictors of outcomes in patients with chronic obstructive pulmonary disease receiving pravastatin, Am. J. Cardiol. (2008) 101:530-535.
    • (2008) Am. J. Cardiol. , vol.101 , pp. 530-535
    • Lee, T.M.1    Lin, M.S.2    Chang, N.C.3
  • 29
    • 0344494027 scopus 로고    scopus 로고
    • Applications of af.nity chromatography in proteomics
    • Lee W.C., Lee K.H., Applications of af.nity chromatography in proteomics, Anal. Biochem. (2004) 324:1-10.
    • (2004) Anal. Biochem. , vol.324 , pp. 1-10
    • Lee, W.C.1    Lee, K.H.2
  • 31
    • 3142689755 scopus 로고    scopus 로고
    • The hyaluronate lyase of Staphylococcus aureus-a virulence factor?
    • Makris G., Wright J.D., Ingham E., Holland K.T., The hyaluronate lyase of Staphylococcus aureus-a virulence factor?, Microbiology (2004) 150:2005-2013.
    • (2004) Microbiology , vol.150 , pp. 2005-2013
    • Makris, G.1    Wright, J.D.2    Ingham, E.3    Holland, K.T.4
  • 32
    • 43049179603 scopus 로고    scopus 로고
    • Alpha-1-acid glycoprotein, its local production and immunopathological participation in experimental pulmonary tuberculosis
    • Martinez Cordero E., Gonzalez M.M., Aguilar L.D., Orozco E.H., Hernandez Pando R., Alpha-1-acid glycoprotein, its local production and immunopathological participation in experimental pulmonary tuberculosis, Tuberculosis (Edinb.) (2008) 88:203-211.
    • (2008) Tuberculosis (Edinb.) , vol.88 , pp. 203-211
    • Martinez Cordero, E.1    Gonzalez, M.M.2    Aguilar, L.D.3    Orozco, E.H.4    Hernandez Pando, R.5
  • 34
    • 0032589276 scopus 로고    scopus 로고
    • Extraction of Escherichia coli proteins with organic solvents prior to two-dimensional electrophoresis
    • Molloy M.P., Herbert B.R., Williams K.L., Gooley A.A., Extraction of Escherichia coli proteins with organic solvents prior to two-dimensional electrophoresis, Electrophoresis (1999) 20:701-704.
    • (1999) Electrophoresis , vol.20 , pp. 701-704
    • Molloy, M.P.1    Herbert, B.R.2    Williams, K.L.3    Gooley, A.A.4
  • 35
    • 41149127399 scopus 로고    scopus 로고
    • Kerbs von Lungren 6 antigen is a marker of alveolar inflammation but not of infection in patients with acute respiratory distress syndrome
    • Nathani N., Perkins G.D., Tunnicliffe W., Murphy N., Manji M., Thickett D.R., Kerbs von Lungren 6 antigen is a marker of alveolar inflammation but not of infection in patients with acute respiratory distress syndrome, Crit. Care (2008) 12:R12.
    • (2008) Crit. Care , vol.12
    • Nathani, N.1    Perkins, G.D.2    Tunnicliffe, W.3    Murphy, N.4    Manji, M.5    Thickett, D.R.6
  • 36
    • 23244461281 scopus 로고    scopus 로고
    • Assessment of the economic impact of porcine reproductive and respiratory syndrome on swine production in the United States
    • Neumann E.J., Kliebenstein J.B., Johnson C.D., Mabry J.W., Bush E.J., Seitzinger A.H., et al., Assessment of the economic impact of porcine reproductive and respiratory syndrome on swine production in the United States, J. Am. Vet. Med. Assoc. (2005) 227:385-392.
    • (2005) J. Am. Vet. Med. Assoc. , vol.227 , pp. 385-392
    • Neumann, E.J.1    Kliebenstein, J.B.2    Johnson, C.D.3    Mabry, J.W.4    Bush, E.J.5    Seitzinger, A.H.6
  • 38
    • 2342424208 scopus 로고    scopus 로고
    • Application of acute phase protein measurements in veterinary clinical chemistry
    • Petersen H.H., Nielsen J.P., Heegaard P.M., Application of acute phase protein measurements in veterinary clinical chemistry, Vet. Res. (2004) 35: 163-187.
    • (2004) Vet. Res. , vol.35 , pp. 163-187
    • Petersen, H.H.1    Nielsen, J.P.2    Heegaard, P.M.3
  • 39
    • 0032618278 scopus 로고    scopus 로고
    • Silver staining of 2-D electrophoresis gels Methods
    • Rabilloud T., Silver staining of 2-D electrophoresis gels, Methods Mol. Biol. (1999) 112:297-305.
    • (1999) Mol. Biol. , vol.112 , pp. 297-305
    • Rabilloud, T.1
  • 40
    • 50549103808 scopus 로고    scopus 로고
    • Actinobacillus pleuropneumoniae vaccines: From bacterins to new insights into vaccination strategies
    • Ramjeet M., Deslandes V., Goure J., Jacques M., Actinobacillus pleuropneumoniae vaccines: from bacterins to new insights into vaccination strategies, Anim. Health Res. Rev. (2008) 9:25-45.
    • (2008) Anim. Health Res. Rev. , vol.9 , pp. 25-45
    • Ramjeet, M.1    Deslandes, V.2    Goure, J.3    Jacques, M.4
  • 41
    • 20444433960 scopus 로고    scopus 로고
    • Serine protease cathepsin G regulates adhesion-dependent neutrophil effector functions by modulating integrin clustering
    • Raptis S.Z., Shapiro S.D., Simmons P.M., Cheng A.M., Pham C.T., Serine protease cathepsin G regulates adhesion-dependent neutrophil effector functions by modulating integrin clustering, Immunity (2005) 22:679-691.
    • (2005) Immunity , vol.22 , pp. 679-691
    • Raptis, S.Z.1    Shapiro, S.D.2    Simmons, P.M.3    Cheng, A.M.4    Pham, C.T.5
  • 42
    • 0030879806 scopus 로고    scopus 로고
    • Collectin-mediated antiviral host defense of the lung: Evidence from influenza virus infection of mice
    • Reading P.C., Morey L.S., Crouch E.C., Anders E.M., Collectin-mediated antiviral host defense of the lung: evidence from influenza virus infection of mice, J. Virol. (1997) 71:8204-8212.
    • (1997) J. Virol. , vol.71 , pp. 8204-8212
    • Reading, P.C.1    Morey, L.S.2    Crouch, E.C.3    Anders, E.M.4
  • 43
    • 0029927505 scopus 로고    scopus 로고
    • Mass spectrometric sequencing of proteins silverstained polyacrylamide gels
    • Shevchenko A., Wilm M., Vorm O., Mann M., Mass spectrometric sequencing of proteins silverstained polyacrylamide gels, Anal. Chem. (1996) 68:850-858.
    • (1996) Anal. Chem. , vol.68 , pp. 850-858
    • Shevchenko, A.1    Wilm, M.2    Vorm, O.3    Mann, M.4
  • 44
    • 22744444021 scopus 로고    scopus 로고
    • Pulmonary infections in swine induce altered porcine surfactant protein D expression and localization to dendritic cells in bronchial-associated lymphoid tissue
    • Soerensen C.M., Holmskov U., Aalbaek B., Boye M., Heegaard P.M., Nielsen O.L., Pulmonary infections in swine induce altered porcine surfactant protein D expression and localization to dendritic cells in bronchial-associated lymphoid tissue, Immunology (2005) 115:526-535.
    • (2005) Immunology , vol.115 , pp. 526-535
    • Soerensen, C.M.1    Holmskov, U.2    Aalbaek, B.3    Boye, M.4    Heegaard, P.M.5    Nielsen, O.L.6
  • 45
    • 0026574265 scopus 로고
    • Analysis of the .ve glycosylation sites of human alpha 1-acid glycoprotein
    • Treuheit M.J., Costello C.E., Halsall H.B., Analysis of the .ve glycosylation sites of human alpha 1-acid glycoprotein, Biochem. J. (1992) 283:105-112.
    • (1992) Biochem. J. , vol.283 , pp. 105-112
    • Treuheit, M.J.1    Costello, C.E.2    Halsall, H.B.3
  • 46
    • 0026772958 scopus 로고
    • N-glycosylation of serum proteins in disease and its investigation using lectins
    • Turner G.A., N-glycosylation of serum proteins in disease and its investigation using lectins, Clin. Chim. Acta (1992) 208:149-171.
    • (1992) Clin. Chim. Acta , vol.208 , pp. 149-171
    • Turner, G.A.1
  • 48
    • 0034074007 scopus 로고    scopus 로고
    • Lung surfactant proteins A and D in innate immune defense
    • Vaandrager A.B., van Golde L.M., Lung surfactant proteins A and D in innate immune defense, Biol. Neonate (2000) 77 (Suppl. 1):9-13.
    • (2000) Biol. Neonate , vol.77 , Issue.SUPPL. 1 , pp. 9-13
    • Vaandrager, A.B.1    Van Golde, L.M.2
  • 49
    • 0036014838 scopus 로고    scopus 로고
    • Porcine surfactant protein D is N-glycosylated in its carbohydrate recognition domain and is assembled into differently charged oligomers
    • Van Eijk M., van de Lest C.H., Batenburg J.J., Vaandrager A.B., Meschi J., Hartshorn K.L., et al., Porcine surfactant protein D is N-glycosylated in its carbohydrate recognition domain and is assembled into differently charged oligomers, Am. J. Respir. Cell Mol. Biol. (2002) 26:739-747.
    • (2002) Am. J. Respir. Cell Mol. Biol. , vol.26 , pp. 739-747
    • Van Eijk, M.1    Van De Lest, C.H.2    Batenburg, J.J.3    Vaandrager, A.B.4    Meschi, J.5    Hartshorn, K.L.6
  • 50
    • 33646730688 scopus 로고    scopus 로고
    • Inflammation inhibitors were remarkably upregulated in plasma of severe acute respiratory syndrome patients at progressive phase
    • Wan J., Sun W., Li X., Ying W., Dai J., Kuai X., et al., inflammation inhibitors were remarkably upregulated in plasma of severe acute respiratory syndrome patients at progressive phase, Proteomics (2006) 6:2886-2894.
    • (2006) Proteomics , vol.6 , pp. 2886-2894
    • Wan, J.1    Sun, W.2    Li, X.3    Ying, W.4    Dai, J.5    Kuai, X.6
  • 51
  • 53
    • 26844454132 scopus 로고    scopus 로고
    • Differential proteomic analysis of bronchoalveolar lavage fluid in asthmatics following segmental antigen challenge
    • Wu J., Kobayashi M., Sousa E.A., Liu W., Cai J., Goldman S.J., et al., Differential proteomic analysis of bronchoalveolar lavage fluid in asthmatics following segmental antigen challenge, Mol. Cell. Proteomics (2005) 4:1251-1264.
    • (2005) Mol. Cell. Proteomics , vol.4 , pp. 1251-1264
    • Wu, J.1    Kobayashi, M.2    Sousa, E.A.3    Liu, W.4    Cai, J.5    Goldman, S.J.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.