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Volumn 16, Issue 3, 2010, Pages 175-182

Chemical and structural modifications of pulmonary collectins and their functional consequences

Author keywords

Biomarker; Collectins; Lung; Nitric oxide; Surfactant proteins

Indexed keywords

COLLECTIN; CYTOKINE; NITRIC OXIDE; NITROGEN; SURFACTANT PROTEIN A; SURFACTANT PROTEIN D; AUTACOID;

EID: 77953315227     PISSN: 17534259     EISSN: 17534267     Source Type: Journal    
DOI: 10.1177/1753425910368871     Document Type: Review
Times cited : (28)

References (50)
  • 1
    • 0032474233 scopus 로고    scopus 로고
    • Bronchodilator S-nitrosothiol deficiency in asthmatic respiratory failure
    • Gaston B., Sears S., Woods J. et al. Bronchodilator S-nitrosothiol deficiency in asthmatic respiratory failure. Lancet 1998 ; 351: 1317-1319.
    • (1998) Lancet , vol.351 , pp. 1317-1319
    • Gaston, B.1    Sears, S.2    Woods, J.3
  • 2
    • 0032823702 scopus 로고    scopus 로고
    • Inhaled nitric oxide in acute lung injury and acute respiratory distress syndrome. Inability to translate physiologic benefit to clinical outcome benefit in adult clinical trials
    • Dellinger RP Inhaled nitric oxide in acute lung injury and acute respiratory distress syndrome. Inability to translate physiologic benefit to clinical outcome benefit in adult clinical trials. Intensive Care Med 1999 ; 25: 881-883.
    • (1999) Intensive Care Med , vol.25 , pp. 881-883
    • Dellinger, R.P.1
  • 3
    • 0029805172 scopus 로고    scopus 로고
    • Nitric oxide, superoxide, and peroxynitrite: The good, the bad, and ugly
    • Beckman JS, Koppenol WH Nitric oxide, superoxide, and peroxynitrite: the good, the bad, and ugly. Am J Physiol 1996 ; 271: C1424 - C1437.
    • (1996) Am J Physiol , vol.271
    • Beckman, J.S.1    Koppenol, W.H.2
  • 4
    • 0032147208 scopus 로고    scopus 로고
    • Biological tyrosine nitration: A pathophysiological function of nitric oxide and reactive oxygen species
    • Ischiropoulos H. Biological tyrosine nitration: a pathophysiological function of nitric oxide and reactive oxygen species. Arch Biochem Biophys 1998 ; 356: 1-11.
    • (1998) Arch Biochem Biophys , vol.356 , pp. 1-11
    • Ischiropoulos, H.1
  • 5
    • 0037155791 scopus 로고    scopus 로고
    • Basal and stimulated protein S-nitrosylation in multiple cell types and tissues
    • Gow AJ, Chen Q., Hess DT et al. Basal and stimulated protein S-nitrosylation in multiple cell types and tissues. J Biol Chem 2002 ; 277: 9637-9640.
    • (2002) J Biol Chem , vol.277 , pp. 9637-9640
    • Gow, A.J.1    Chen, Q.2    Hess, D.T.3
  • 6
    • 0033520499 scopus 로고    scopus 로고
    • Eosinophil peroxidase nitrates protein tyrosyl residues. Implications for oxidative damage by nitrating intermediates in eosinophilic inflammatory disorders
    • Wu W., Chen Y., Hazen SL Eosinophil peroxidase nitrates protein tyrosyl residues. Implications for oxidative damage by nitrating intermediates in eosinophilic inflammatory disorders. J Biol Chem 1999 ; 274: 25933-25944.
    • (1999) J Biol Chem , vol.274 , pp. 25933-25944
    • Wu, W.1    Chen, Y.2    Hazen, S.L.3
  • 7
    • 0027303364 scopus 로고
    • Interaction of myeloperoxidase with peroxynitrite. A comparison with lactoperoxidase, horseradish peroxidase and catalase
    • Floris R., Piersma SR, Yang G. et al. Interaction of myeloperoxidase with peroxynitrite. A comparison with lactoperoxidase, horseradish peroxidase and catalase. Eur J Biochem 1993 ; 215: 767-775.
    • (1993) Eur J Biochem , vol.215 , pp. 767-775
    • Floris, R.1    Piersma, S.R.2    Yang, G.3
  • 8
    • 0026693724 scopus 로고
    • Nitric oxide circulates in mammalian plasma primarily as an S-nitroso adduct of serum albumin
    • Stamler JS, Jaraki O., Osborne J. et al. Nitric oxide circulates in mammalian plasma primarily as an S-nitroso adduct of serum albumin. Proc Natl Acad Sci USA 1992 ; 89: 7674-7677.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 7674-7677
    • Stamler, J.S.1    Jaraki, O.2    Osborne, J.3
  • 9
    • 0035929149 scopus 로고    scopus 로고
    • Nitrosylation. The prototypic redox-based signaling mechanism
    • Stamler JS, Lamas S., Fang FC Nitrosylation. the prototypic redox-based signaling mechanism. Cell 2001 ; 106: 675-683.
    • (2001) Cell , vol.106 , pp. 675-683
    • Stamler, J.S.1    Lamas, S.2    Fang, F.C.3
  • 10
    • 3242676183 scopus 로고    scopus 로고
    • Biological significance of nitric oxide-mediated protein modifications
    • Gow AJ, Farkouh CR, Munson DA et al. Biological significance of nitric oxide-mediated protein modifications. Am J Physiol 2004 ; 287: L262 - L268.
    • (2004) Am J Physiol , vol.287
    • Gow, A.J.1    Farkouh, C.R.2    Munson, D.A.3
  • 11
    • 33646580362 scopus 로고    scopus 로고
    • Identification of Snitrosylation motifs by site-specific mapping of the S-nitrosocysteine proteome in human vascular smooth muscle cells
    • Greco TM, Hodara R., Parastatidis I. et al. Identification of Snitrosylation motifs by site-specific mapping of the S-nitrosocysteine proteome in human vascular smooth muscle cells. Proc Natl Acad Sci USA 2006 ; 103: 7420-7425.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 7420-7425
    • Greco, T.M.1    Hodara, R.2    Parastatidis, I.3
  • 12
    • 13444282230 scopus 로고    scopus 로고
    • Protein S-nitrosylation: Purview and parameters
    • Hess DT, Matsumoto A., Kim SO et al. Protein S-nitrosylation: purview and parameters. Nat Rev Mol Cell Biol 2005 ; 6: 150-166.
    • (2005) Nat Rev Mol Cell Biol , vol.6 , pp. 150-166
    • Hess, D.T.1    Matsumoto, A.2    Kim, S.O.3
  • 13
    • 0035029362 scopus 로고    scopus 로고
    • Nitric oxide chemistry and cellular signaling
    • Gow AJ, Ischiropoulos H. Nitric oxide chemistry and cellular signaling. J Cell Physiol 2001 ; 187: 277-282.
    • (2001) J Cell Physiol , vol.187 , pp. 277-282
    • Gow, A.J.1    Ischiropoulos, H.2
  • 14
    • 33744908081 scopus 로고    scopus 로고
    • S-nitrosothiol signaling in respiratory biology
    • Gaston B., Singel D., Doctor A. et al. S-nitrosothiol signaling in respiratory biology. Am J Respir Crit Care Med 2006 ; 173: 1186-1193.
    • (2006) Am J Respir Crit Care Med , vol.173 , pp. 1186-1193
    • Gaston, B.1    Singel, D.2    Doctor, A.3
  • 15
    • 0029785710 scopus 로고    scopus 로고
    • Biosynthesis of surfactant protein D. Contributions of conserved NH2-terminal cysteine residues and collagen helix formation to assembly and secretion
    • Brown-Augsburger P., Chang D., Rust K. et al. Biosynthesis of surfactant protein D. Contributions of conserved NH2-terminal cysteine residues and collagen helix formation to assembly and secretion. J Biol Chem 1996 ; 271: 18912-18919.
    • (1996) J Biol Chem , vol.271 , pp. 18912-18919
    • Brown-Augsburger, P.1    Chang, D.2    Rust, K.3
  • 16
    • 0025811419 scopus 로고
    • Assembly of the surfactant protein SP-A. Deletions in the globular domain interfere with the correct folding of the molecule
    • Spissinger T., Schafer KP, Voss T. Assembly of the surfactant protein SP-A. Deletions in the globular domain interfere with the correct folding of the molecule. Eur J Biochem 1991 ; 199: 65-71.
    • (1991) Eur J Biochem , vol.199 , pp. 65-71
    • Spissinger, T.1    Schafer, K.P.2    Voss, T.3
  • 17
    • 0037111230 scopus 로고    scopus 로고
    • CL-46, a novel collectin highly expressed in bovine thymus and liver
    • Hansen S., Holm D., Moeller V. et al. CL-46, a novel collectin highly expressed in bovine thymus and liver. J Immunol 2002 ; 169: 5726-5734.
    • (2002) J Immunol , vol.169 , pp. 5726-5734
    • Hansen, S.1    Holm, D.2    Moeller, V.3
  • 18
    • 0028233879 scopus 로고
    • Molecular structure of pulmonary surfactant protein D (SP-D)
    • Crouch E., Persson A., Chang D. et al. Molecular structure of pulmonary surfactant protein D (SP-D). J Biol Chem 1994 ; 269: 17311-17319.
    • (1994) J Biol Chem , vol.269 , pp. 17311-17319
    • Crouch, E.1    Persson, A.2    Chang, D.3
  • 19
    • 0021943585 scopus 로고
    • Characteristics of human surfactant-associated glycoproteins A
    • Whitsett JA, Hull W., Ross G. et al. Characteristics of human surfactant-associated glycoproteins A. Pediatr Res 1985 ; 19: 501-508.
    • (1985) Pediatr Res , vol.19 , pp. 501-508
    • Whitsett, J.A.1    Hull, W.2    Ross, G.3
  • 20
    • 1842583880 scopus 로고    scopus 로고
    • Differences in biochemical properties and in biological function between human SP-A1 and SP-A2 variants, and the impact of ozone-induced oxidation
    • Wang G., Bates-Kenney SR, Tao JQ et al. Differences in biochemical properties and in biological function between human SP-A1 and SP-A2 variants, and the impact of ozone-induced oxidation. Biochemistry 2004 ; 43: 4227-4239.
    • (2004) Biochemistry , vol.43 , pp. 4227-4239
    • Wang, G.1    Bates-Kenney, S.R.2    Tao, J.Q.3
  • 21
    • 14844297019 scopus 로고    scopus 로고
    • Role of the degree of oligomerization in the structure and function of human surfactant protein A
    • Sanchez-Barbero F., Strassner J., Garcia-Canero R. et al. Role of the degree of oligomerization in the structure and function of human surfactant protein A. J Biol Chem 2005 ; 280: 7659-7670.
    • (2005) J Biol Chem , vol.280 , pp. 7659-7670
    • Sanchez-Barbero, F.1    Strassner, J.2    Garcia-Canero, R.3
  • 22
    • 0026085036 scopus 로고
    • Structural comparison of recombinant pulmonary surfactant protein SP-A derived from two human coding sequences: Implications for the chain composition of natural human SP-A
    • Voss T., Melchers K., Scheirle G. et al. Structural comparison of recombinant pulmonary surfactant protein SP-A derived from two human coding sequences: implications for the chain composition of natural human SP-A. Am J Respir Cell Mol Biol 1991 ; 4: 88-94.
    • (1991) Am J Respir Cell Mol Biol , vol.4 , pp. 88-94
    • Voss, T.1    Melchers, K.2    Scheirle, G.3
  • 23
    • 0022483273 scopus 로고
    • Post-translational modification of the major human surfactant-associated proteins
    • Phelps DS, Floros J., Taeusch Jr HW. Post-translational modification of the major human surfactant-associated proteins. Biochem J 1986 ; 237: 373-377.
    • (1986) Biochem J , vol.237 , pp. 373-377
    • Phelps, D.S.1    Floros, J.2    Taeusch Jr., H.W.3
  • 24
    • 0031740744 scopus 로고    scopus 로고
    • Structure, processing and properties of surfactant protein A
    • McCormack FX Structure, processing and properties of surfactant protein A. Biochim Biophys Acta 1998 ; 1408: 109-131.
    • (1998) Biochim Biophys Acta , vol.1408 , pp. 109-131
    • McCormack, F.X.1
  • 25
    • 0030961939 scopus 로고    scopus 로고
    • Surfactant protein A, but not surfactant protein D, is an opsonin for influenza A virus phagocytosis by rat alveolar macrophages
    • Benne CA, Benaissa-Trouw B., van Strijp JA et al. Surfactant protein A, but not surfactant protein D, is an opsonin for influenza A virus phagocytosis by rat alveolar macrophages. Eur J Immunol 1997 ; 27: 886-890.
    • (1997) Eur J Immunol , vol.27 , pp. 886-890
    • Benne, C.A.1    Benaissa-Trouw, B.2    Van Strijp, J.A.3
  • 27
    • 33746680420 scopus 로고    scopus 로고
    • Nitrated SP-A does not enhance adherence of Pneumocystis carinii to alveolar macrophages
    • Zhu S., Kachel DL, Martin WJ et al. Nitrated SP-A does not enhance adherence of Pneumocystis carinii to alveolar macrophages. Am J Physiol 1998 ; 275: L1031 - L1039.
    • (1998) Am J Physiol , vol.275
    • Zhu, S.1    Kachel, D.L.2    Martin, W.J.3
  • 28
    • 0029995083 scopus 로고    scopus 로고
    • Nitration of surfactant protein A results in decreased ability to aggregate lipids
    • Haddad IY, Zhu S., Ischiropoulos H. et al. Nitration of surfactant protein A results in decreased ability to aggregate lipids. Am J Physiol 1996 ; 270: L281 - L288.
    • (1996) Am J Physiol , vol.270
    • Haddad, I.Y.1    Zhu, S.2    Ischiropoulos, H.3
  • 29
    • 0037114968 scopus 로고    scopus 로고
    • Inhibition of human surfactant protein A function by oxidation intermediates of nitrite
    • Davis IC, Zhu S., Sampson JB et al. Inhibition of human surfactant protein A function by oxidation intermediates of nitrite. Free Radic Biol Med 2002 ; 33: 1703-1713.
    • (2002) Free Radic Biol Med , vol.33 , pp. 1703-1713
    • Davis, I.C.1    Zhu, S.2    Sampson, J.B.3
  • 30
    • 33746847261 scopus 로고    scopus 로고
    • Surfactant protein A directly interacts with TLR4 and MD-2 and regulates inflammatory cellular response. Importance of supratrimeric oligomerization
    • Yamada C., Sano H., Shimizu T. et al. Surfactant protein A directly interacts with TLR4 and MD-2 and regulates inflammatory cellular response. Importance of supratrimeric oligomerization. J Biol Chem 2006 ; 281: 21771-21780.
    • (2006) J Biol Chem , vol.281 , pp. 21771-21780
    • Yamada, C.1    Sano, H.2    Shimizu, T.3
  • 31
    • 34447133735 scopus 로고    scopus 로고
    • Immunomodulatory roles of surfactant proteins A and D: Implications in lung disease
    • Pastva AM, Wright JR, Williams KL Immunomodulatory roles of surfactant proteins A and D: implications in lung disease. Proc Am Thorac Soc 2007 ; 4: 252-257.
    • (2007) Proc Am Thorac Soc , vol.4 , pp. 252-257
    • Pastva, A.M.1    Wright, J.R.2    Williams, K.L.3
  • 32
    • 0028356020 scopus 로고
    • Recombinant pulmonary surfactant protein D. Post-translational modification and molecular assembly
    • Crouch E., Chang D., Rust K. et al. Recombinant pulmonary surfactant protein D. Post-translational modification and molecular assembly. J Biol Chem 1994 ; 269: 15808-15813.
    • (1994) J Biol Chem , vol.269 , pp. 15808-15813
    • Crouch, E.1    Chang, D.2    Rust, K.3
  • 33
    • 0033103527 scopus 로고    scopus 로고
    • Crystal structure of the trimeric alpha-helical coiled-coil and the three lectin domains of human lung surfactant protein D
    • Hakansson K., Lim NK, Hoppe HJ et al. Crystal structure of the trimeric alpha-helical coiled-coil and the three lectin domains of human lung surfactant protein D. Structure 1999 ; 7: 255-264.
    • (1999) Structure , vol.7 , pp. 255-264
    • Hakansson, K.1    Lim, N.K.2    Hoppe, H.J.3
  • 34
    • 0035374390 scopus 로고    scopus 로고
    • Activity of pulmonary surfactant protein-D (SP-D) in vivo is dependent on oligomeric structure
    • Zhang L., Ikegami M., Crouch EC et al. Activity of pulmonary surfactant protein-D (SP-D) in vivo is dependent on oligomeric structure. J Biol Chem 2001 ; 276: 19214-19219.
    • (2001) J Biol Chem , vol.276 , pp. 19214-19219
    • Zhang, L.1    Ikegami, M.2    Crouch, E.C.3
  • 35
    • 56849117935 scopus 로고    scopus 로고
    • S-Nitrosylation of surfactant protein-D controls inflammatory function
    • Guo CJ, Atochina-Vasserman EN, Abramova E. et al. S-Nitrosylation of surfactant protein-D controls inflammatory function. PLoS Biol 2008 ; 6: e266.
    • (2008) PLoS Biol , vol.6 , pp. 266
    • Guo, C.J.1    Atochina-Vasserman, E.N.2    Abramova, E.3
  • 36
    • 68749102352 scopus 로고    scopus 로고
    • Modification of surfactant protein D by reactive oxygen-nitrogen intermediates is accompanied by loss of aggregating activity, in vitro and in vivo
    • Matalon S., Shrestha K., Kirk M. et al. Modification of surfactant protein D by reactive oxygen-nitrogen intermediates is accompanied by loss of aggregating activity, in vitro and in vivo. FASEB J 2009 ; 23: 1415-1430.
    • (2009) FASEB J , vol.23 , pp. 1415-1430
    • Matalon, S.1    Shrestha, K.2    Kirk, M.3
  • 37
    • 34249671245 scopus 로고    scopus 로고
    • Surfactant protein A and surfactant protein D variation in pulmonary disease
    • Sorensen GL, Husby S., Holmskov U. Surfactant protein A and surfactant protein D variation in pulmonary disease. Immunobiology 2007 ; 212: 381-416.
    • (2007) Immunobiology , vol.212 , pp. 381-416
    • Sorensen, G.L.1    Husby, S.2    Holmskov, U.3
  • 38
    • 19944430458 scopus 로고    scopus 로고
    • A common polymorphism in the SFTPD gene influences assembly, function, and concentration of surfactant protein D
    • Leth-Larsen R., Garred P., Jensenius H. et al. A common polymorphism in the SFTPD gene influences assembly, function, and concentration of surfactant protein D. J Immunol 2005 ; 174: 1532-1538.
    • (2005) J Immunol , vol.174 , pp. 1532-1538
    • Leth-Larsen, R.1    Garred, P.2    Jensenius, H.3
  • 39
    • 17844408477 scopus 로고    scopus 로고
    • Polymorphisms in the human surfactant protein-D (SFTPD) gene: Strong evidence that serum levels of surfactant protein-D (SP-D) are genetically influenced
    • Heidinger K., Konig IR, Bohnert A. et al. Polymorphisms in the human surfactant protein-D (SFTPD) gene: strong evidence that serum levels of surfactant protein-D (SP-D) are genetically influenced. Immunogenetics 2005 ; 57: 1-7.
    • (2005) Immunogenetics , vol.57 , pp. 1-7
    • Heidinger, K.1    Konig, I.R.2    Bohnert, A.3
  • 40
    • 0031799387 scopus 로고    scopus 로고
    • Pulmonary surfactant proteins A and D enhance neutrophil uptake of bacteria
    • Hartshorn KL, Crouch E., White MR et al. Pulmonary surfactant proteins A and D enhance neutrophil uptake of bacteria. Am J Physiol 1998 ; 274: L958 - L969.
    • (1998) Am J Physiol , vol.274
    • Hartshorn, K.L.1    Crouch, E.2    White, M.R.3
  • 42
    • 0033790682 scopus 로고    scopus 로고
    • Surfactant protein genetic marker alleles identify a subgroup of tuberculosis in a Mexican population
    • Floros J., Lin HM, Garcia A. et al. Surfactant protein genetic marker alleles identify a subgroup of tuberculosis in a Mexican population. J Infect Dis 2000 ; 182: 1473-1478.
    • (2000) J Infect Dis , vol.182 , pp. 1473-1478
    • Floros, J.1    Lin, H.M.2    Garcia, A.3
  • 43
    • 36148955605 scopus 로고    scopus 로고
    • Reduced influenza viral neutralizing activity of natural human trimers of surfactant protein D
    • Hartshorn KL, White MR, Tecle T. et al. Reduced influenza viral neutralizing activity of natural human trimers of surfactant protein D. Respir Res 2007 ; 8: 9.
    • (2007) Respir Res , vol.8 , pp. 9
    • Hartshorn, K.L.1    White, M.R.2    Tecle, T.3
  • 44
    • 0036606189 scopus 로고    scopus 로고
    • Surfactant proteins A and D in children with pulmonary disease due to gastroesophageal reflux
    • Griese M., Maderlechner N., Ahrens P. et al. Surfactant proteins A and D in children with pulmonary disease due to gastroesophageal reflux. Am J Respir Crit Care Med 2002 ; 165: 1546-1550.
    • (2002) Am J Respir Crit Care Med , vol.165 , pp. 1546-1550
    • Griese, M.1    Maderlechner, N.2    Ahrens, P.3
  • 45
    • 33344476292 scopus 로고    scopus 로고
    • Oxidative changes of bronchoalveolar proteins in cystic fibrosis
    • Starosta V., Rietschel E., Paul K. et al. Oxidative changes of bronchoalveolar proteins in cystic fibrosis. Chest 2006 ; 129: 431-437.
    • (2006) Chest , vol.129 , pp. 431-437
    • Starosta, V.1    Rietschel, E.2    Paul, K.3
  • 46
    • 58149090577 scopus 로고    scopus 로고
    • Pulmonary surfactant protein D inhibits lipopolysaccharide (LPS)-induced inflammatory cell responses by altering LPS binding to its receptors
    • Yamazoe M., Nishitani C., Takahashi M. et al. Pulmonary surfactant protein D inhibits lipopolysaccharide (LPS)-induced inflammatory cell responses by altering LPS binding to its receptors. J Biol Chem 2008 ; 283: 35878-35888.
    • (2008) J Biol Chem , vol.283 , pp. 35878-35888
    • Yamazoe, M.1    Nishitani, C.2    Takahashi, M.3
  • 47
    • 71849086029 scopus 로고    scopus 로고
    • Multimerization of surfactant protein D, but not its collagen domain, is required for antiviral and opsonic activities related to influenza virus
    • White M., Kingma P., Tecle T. et al. Multimerization of surfactant protein D, but not its collagen domain, is required for antiviral and opsonic activities related to influenza virus. J Immunol 2008 ; 181: 7936-7943.
    • (2008) J Immunol , vol.181 , pp. 7936-7943
    • White, M.1    Kingma, P.2    Tecle, T.3
  • 48
    • 77953320596 scopus 로고    scopus 로고
    • Segmental antigen challenge produces alterations in surfactant protein D expression and multimeric structure in humans
    • Atochina-Vasserman EN, Winkler C., Abramova H. et al. Segmental antigen challenge produces alterations in surfactant protein D expression and multimeric structure in humans. Am J Respir Crit Care Med 2009 ; 179: A6272.
    • (2009) Am J Respir Crit Care Med , vol.179 , pp. 6272
    • Atochina-Vasserman, E.N.1    Winkler, C.2    Abramova, H.3
  • 49
    • 0141918823 scopus 로고    scopus 로고
    • By binding SIRPalpha or calreticulin/CD91, lung collectins act as dual function surveillance molecules to suppress or enhance inflammation
    • Gardai SJ, Xiao YQ, Dickinson M. et al. By binding SIRPalpha or calreticulin/CD91, lung collectins act as dual function surveillance molecules to suppress or enhance inflammation. Cell 2003 ; 115: 13-23.
    • (2003) Cell , vol.115 , pp. 13-23
    • Gardai, S.J.1    Xiao, Y.Q.2    Dickinson, M.3
  • 50
    • 61449239078 scopus 로고    scopus 로고
    • Immune reconstitution during Pneumocystis lung infection: Disruption of surfactant component expression and function by S-nitrosylation
    • Atochina-Vasserman EN, Gow AJ, Abramova H. et al. Immune reconstitution during Pneumocystis lung infection: disruption of surfactant component expression and function by S-nitrosylation. J Immunol 2009 ; 182: 2277-2287.
    • (2009) J Immunol , vol.182 , pp. 2277-2287
    • Atochina-Vasserman, E.N.1    Gow, A.J.2    Abramova, H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.