메뉴 건너뛰기




Volumn 14, Issue 8, 2015, Pages 2138-2149

The human pathogen Streptococcus pyogenes releases lipoproteins as lipoprotein-rich membrane vesicles

Author keywords

[No Author keywords available]

Indexed keywords

DIHYDROLIPOAMIDE DEHYDROGENASE; ENOLASE; LIPOPROTEIN; PENICILLIN BINDING PROTEIN; PENICILLIN BINDING PROTEIN 1A; PENICILLIN BINDING PROTEIN 1B; PENICILLIN BINDING PROTEIN 2A; PENICILLIN DERIVATIVE; PHOSPHATIDYLGLYCEROL; RIBOSOMAL PROTEIN L1; RIBOSOMAL PROTEIN L5; RIBOSOMAL PROTEIN S2; RIBOSOMAL PROTEIN S4; RIBOSOME PROTEIN; SERINE PROTEINASE; SIGNAL PEPTIDASE I; SORTASE; SORTASE A; STREPTOLYSIN O; TOLL LIKE RECEPTOR 2; UNCLASSIFIED DRUG; BACTERIAL PROTEIN; CULTURE MEDIUM;

EID: 84938944684     PISSN: 15359476     EISSN: 15359484     Source Type: Journal    
DOI: 10.1074/mcp.M114.045880     Document Type: Article
Times cited : (45)

References (58)
  • 1
    • 0024393453 scopus 로고
    • The structure of signal peptides from bacterial lipoproteins
    • von Heijne, G. (1989) The structure of signal peptides from bacterial lipoproteins. Protein Eng. 2, 531-534
    • (1989) Protein Eng. , vol.2 , pp. 531-534
    • Von Heijne, G.1
  • 2
    • 0036066456 scopus 로고    scopus 로고
    • Pattern searches for the identification of putative lipoprotein genes in Gram-positive bacterial genomes
    • Sutcliffe, I. C., and Harrington, D. J. (2002) Pattern searches for the identification of putative lipoprotein genes in Gram-positive bacterial genomes. Microbiology 148, 2065-2077
    • (2002) Microbiology , vol.148 , pp. 2065-2077
    • Sutcliffe, I.C.1    Harrington, D.J.2
  • 3
    • 0020322927 scopus 로고
    • Mechanism of signal peptide cleavage in the biosynthesis of the major lipoprotein of the Escherichia coli outer membrane
    • Hussain, M., Ichihara, S., and Mizushima, S. (1982) Mechanism of signal peptide cleavage in the biosynthesis of the major lipoprotein of the Escherichia coli outer membrane. J. Biol. Chem. 257, 5177-5182
    • (1982) J. Biol. Chem. , vol.257 , pp. 5177-5182
    • Hussain, M.1    Ichihara, S.2    Mizushima, S.3
  • 4
    • 0028067877 scopus 로고
    • Lipid modification of bacterial prolipoprotein. Transfer of diacylglyceryl moiety from phosphatidylglycerol
    • Sankaran, K., and Wu, H. C. (1994) Lipid modification of bacterial prolipoprotein. Transfer of diacylglyceryl moiety from phosphatidylglycerol. J. Biol. Chem. 269, 19701-19706
    • (1994) J. Biol. Chem. , vol.269 , pp. 19701-19706
    • Sankaran, K.1    Wu, H.C.2
  • 6
    • 34250303119 scopus 로고    scopus 로고
    • Identification of essential residues in apolipoprotein N-acyl transferase, a member of the CN hydrolase family
    • Vidal-Ingigliardi, D., Lewenza, S., and Buddelmeijer, N. (2007) Identification of essential residues in apolipoprotein N-acyl transferase, a member of the CN hydrolase family. J. Bacteriol. 189, 4456-4464
    • (2007) J. Bacteriol. , vol.189 , pp. 4456-4464
    • Vidal-Ingigliardi, D.1    Lewenza, S.2    Buddelmeijer, N.3
  • 12
    • 0036644042 scopus 로고    scopus 로고
    • Cutting edge: Role of Toll-like receptor1 in mediating immune response to microbial lipoproteins
    • Takeuchi, O., Sato, S., Horiuchi, T., Hoshino, K., Takeda, K., Dong, Z., Modlin, R. L., and Akira, S. (2002) Cutting edge: role of Toll-like receptor1 in mediating immune response to microbial lipoproteins. J. Immunol. 169, 10-14
    • (2002) J. Immunol. , vol.169 , pp. 10-14
    • Takeuchi, O.1    Sato, S.2    Horiuchi, T.3    Hoshino, K.4    Takeda, K.5    Dong, Z.6    Modlin, R.L.7    Akira, S.8
  • 15
    • 33747806614 scopus 로고    scopus 로고
    • Not lipoteichoic acid but lipoproteins appear to be the dominant immunobiologically active compounds in Staphylococcus aureus
    • Hashimoto, M., Tawaratsumida, K., Kariya, H., Kiyohara, A., Suda, Y., Krikae, F., Kirikae, T., and Gotz, F. (2006) Not lipoteichoic acid but lipoproteins appear to be the dominant immunobiologically active compounds in Staphylococcus aureus. J. Immunol. 177, 3162-3169
    • (2006) J. Immunol. , vol.177 , pp. 3162-3169
    • Hashimoto, M.1    Tawaratsumida, K.2    Kariya, H.3    Kiyohara, A.4    Suda, Y.5    Krikae, F.6    Kirikae, T.7    Gotz, F.8
  • 16
    • 58149295961 scopus 로고    scopus 로고
    • Lipoprotein biogenesis in Gram-positive bacteria: Knowing when to hold 'em, knowing when to fold 'em
    • Hutchings, M. I., Palmer, T., Harrington, D. J., and Sutcliffe, I. C. (2009) Lipoprotein biogenesis in Gram-positive bacteria: knowing when to hold 'em, knowing when to fold 'em. Trends Microbiol. 17, 13-21
    • (2009) Trends Microbiol. , vol.17 , pp. 13-21
    • Hutchings, M.I.1    Palmer, T.2    Harrington, D.J.3    Sutcliffe, I.C.4
  • 17
    • 80053510070 scopus 로고    scopus 로고
    • Group A streptococcal infections
    • Langlois, D. M., and Andreae, M. (2011) Group A streptococcal infections. Pediatr. Rev. 32, 423-429
    • (2011) Pediatr. Rev. , vol.32 , pp. 423-429
    • Langlois, D.M.1    Andreae, M.2
  • 18
    • 27944484031 scopus 로고    scopus 로고
    • The ExPortal: An organelle dedicated to the biogenesis of secreted proteins in Streptococcus pyogenes
    • Rosch, J. W., and Caparon, M. G. (2005) The ExPortal: an organelle dedicated to the biogenesis of secreted proteins in Streptococcus pyogenes. Mol. Microbiol. 58, 959-968
    • (2005) Mol. Microbiol. , vol.58 , pp. 959-968
    • Rosch, J.W.1    Caparon, M.G.2
  • 20
    • 33846603187 scopus 로고    scopus 로고
    • Anionic lipids enriched at the ExPortal of Streptococcus pyogenes
    • Rosch, J. W., Hsu, F. F., and Caparon, M. G. (2007) Anionic lipids enriched at the ExPortal of Streptococcus pyogenes. J. Bacteriol. 189, 801-806
    • (2007) J. Bacteriol. , vol.189 , pp. 801-806
    • Rosch, J.W.1    Hsu, F.F.2    Caparon, M.G.3
  • 21
    • 1342323730 scopus 로고    scopus 로고
    • Role for serine protease HtrA (DegP) of Streptococcus pyogenes in the biogenesis of virulence factors SpeB and the hemolysin streptolysin S
    • Lyon, W. R., and Caparon, M. G. (2004) Role for serine protease HtrA (DegP) of Streptococcus pyogenes in the biogenesis of virulence factors SpeB and the hemolysin streptolysin S. Infect. Immun. 72, 1618-1625
    • (2004) Infect. Immun. , vol.72 , pp. 1618-1625
    • Lyon, W.R.1    Caparon, M.G.2
  • 22
    • 84887139738 scopus 로고    scopus 로고
    • An association between peptidoglycan synthesis and organization of the Streptococcus pyogenes ExPortal
    • Vega, L. A., Port, G. C., and Caparon, M. G. (2013) An association between peptidoglycan synthesis and organization of the Streptococcus pyogenes ExPortal. mBio 4, e00485-00413
    • (2013) mBio , vol.4 , pp. e00485-e100413
    • Vega, L.A.1    Port, G.C.2    Caparon, M.G.3
  • 23
    • 0027208133 scopus 로고
    • An M protein with a single C repeat prevents phagocytosis of Streptococcus pyogenes: Use of a temperature-sensitive shuttle vector to deliver homologous sequences to the chromosome of S. pyogenes
    • Perez-Casal, J., Price, J. A., Maguin, E., and Scott, J. R. (1993) An M protein with a single C repeat prevents phagocytosis of Streptococcus pyogenes: use of a temperature-sensitive shuttle vector to deliver homologous sequences to the chromosome of S. pyogenes. Mol. Microbiol. 8, 809-819
    • (1993) Mol. Microbiol. , vol.8 , pp. 809-819
    • Perez-Casal, J.1    Price, J.A.2    Maguin, E.3    Scott, J.R.4
  • 24
    • 0033434080 scopus 로고    scopus 로고
    • Probability-based protein identification by searching sequence databases using mass spectrometry data
    • Perkins, D. N., Pappin, D. J., Creasy, D. M., and Cottrell, J. S. (1999) Probability-based protein identification by searching sequence databases using mass spectrometry data. Electrophoresis 20, 3551-3567
    • (1999) Electrophoresis , vol.20 , pp. 3551-3567
    • Perkins, D.N.1    Pappin, D.J.2    Creasy, D.M.3    Cottrell, J.S.4
  • 26
    • 0032972509 scopus 로고    scopus 로고
    • PSORT: A program for detecting sorting signals in proteins and predicting their subcellular localization
    • Nakai, K., and Horton, P. (1999) PSORT: a program for detecting sorting signals in proteins and predicting their subcellular localization. Trends Biochem. Sci. 24, 34-36
    • (1999) Trends Biochem. Sci. , vol.24 , pp. 34-36
    • Nakai, K.1    Horton, P.2
  • 28
    • 0036091972 scopus 로고    scopus 로고
    • DOLOP - Database of bacterial lipoproteins
    • Madan Babu, M., and Sankaran, K. (2002) DOLOP - database of bacterial lipoproteins. Bioinformatics 18, 641-643
    • (2002) Bioinformatics , vol.18 , pp. 641-643
    • Madan Babu, M.1    Sankaran, K.2
  • 29
    • 61549096272 scopus 로고    scopus 로고
    • Prediction of lipoprotein signal peptides in Gram-positive bacteria with a Hidden Markov Model
    • Bagos, P. G., Tsirigos, K. D., Liakopoulos, T. D., and Hamodrakas, S. J. (2008) Prediction of lipoprotein signal peptides in Gram-positive bacteria with a Hidden Markov Model. J. Proteome Res. 7, 5082-5093
    • (2008) J. Proteome Res. , vol.7 , pp. 5082-5093
    • Bagos, P.G.1    Tsirigos, K.D.2    Liakopoulos, T.D.3    Hamodrakas, S.J.4
  • 30
    • 1642498273 scopus 로고    scopus 로고
    • Identification of new candidate vaccine antigens made by Streptococcus pyogenes: Purification and characterization of 16 putative extracellular lipoproteins
    • Lei, B., Liu, M., Chesney, G. L., and Musser, J. M. (2004) Identification of new candidate vaccine antigens made by Streptococcus pyogenes: purification and characterization of 16 putative extracellular lipoproteins. J. Infect. Dis. 189, 79-89
    • (2004) J. Infect. Dis. , vol.189 , pp. 79-89
    • Lei, B.1    Liu, M.2    Chesney, G.L.3    Musser, J.M.4
  • 31
    • 77954199597 scopus 로고    scopus 로고
    • PSORTb 3.0: Improved protein subcellular localization prediction with refined localization subcategories and predictive capabilities for all prokaryotes
    • Yu, N. Y., Wagner, J. R., Laird, M. R., Melli, G., Rey, S., Lo, R., Dao, P., Sahinalp, S. C., Ester, M., Foster, L. J., and Brinkman, F. S. (2010) PSORTb 3.0: improved protein subcellular localization prediction with refined localization subcategories and predictive capabilities for all prokaryotes. Bioinformatics 26, 1608-1615
    • (2010) Bioinformatics , vol.26 , pp. 1608-1615
    • Yu, N.Y.1    Wagner, J.R.2    Laird, M.R.3    Melli, G.4    Rey, S.5    Lo, R.6    Dao, P.7    Sahinalp, S.C.8    Ester, M.9    Foster, L.J.10    Brinkman, F.S.11
  • 33
    • 33845261493 scopus 로고
    • A rapid method of total lipid extraction and purification
    • Bligh, E. G., and Dyer, W. J. (1959) A rapid method of total lipid extraction and purification. Can. J. Biochem. Physiol. 37, 911-917
    • (1959) Can. J. Biochem. Physiol. , vol.37 , pp. 911-917
    • Bligh, E.G.1    Dyer, W.J.2
  • 35
    • 58149295188 scopus 로고    scopus 로고
    • Label-free quantitative analysis of one-dimensional PAGE LC/MS/MS proteome: Application on angiotensin II-stimulated smooth muscle cells secretome
    • Gao, B. B., Stuart, L., and Feener, E. P. (2008) Label-free quantitative analysis of one-dimensional PAGE LC/MS/MS proteome: application on angiotensin II-stimulated smooth muscle cells secretome. Mol. Cell. Proteomics 7, 2399-2409
    • (2008) Mol. Cell. Proteomics , vol.7 , pp. 2399-2409
    • Gao, B.B.1    Stuart, L.2    Feener, E.P.3
  • 36
  • 37
    • 0033588339 scopus 로고    scopus 로고
    • Anchor structure of staphylococcal surface proteins. IV. Inhibitors of the cell wall sorting reaction
    • Ton-That, H., and Schneewind, O. (1999) Anchor structure of staphylococcal surface proteins. IV. Inhibitors of the cell wall sorting reaction. J. Biol. Chem. 274, 24316-24320
    • (1999) J. Biol. Chem. , vol.274 , pp. 24316-24320
    • Ton-That, H.1    Schneewind, O.2
  • 38
    • 0032582528 scopus 로고    scopus 로고
    • Anchor structure of staphylococcal surface proteins. III. Role of the FemA, FemB, and FemX factors in anchoring surface proteins to the bacterial cell wall
    • Ton-That, H., Labischinski, H., Berger-Bachi, B., and Schneewind, O. (1998) Anchor structure of staphylococcal surface proteins. III. Role of the FemA, FemB, and FemX factors in anchoring surface proteins to the bacterial cell wall. J. Biol. Chem. 273, 29143-29149
    • (1998) J. Biol. Chem. , vol.273 , pp. 29143-29149
    • Ton-That, H.1    Labischinski, H.2    Berger-Bachi, B.3    Schneewind, O.4
  • 39
    • 0030881921 scopus 로고    scopus 로고
    • Anchor structure of staphylococcal surface proteins. A branched peptide that links the carboxyl terminus of proteins to the cell wall
    • Ton-That, H., Faull, K. F., and Schneewind, O. (1997) Anchor structure of staphylococcal surface proteins. A branched peptide that links the carboxyl terminus of proteins to the cell wall. J. Biol. Chem. 272, 22285-22292
    • (1997) J. Biol. Chem. , vol.272 , pp. 22285-22292
    • Ton-That, H.1    Faull, K.F.2    Schneewind, O.3
  • 41
    • 0343981619 scopus 로고
    • Chemically defined medium for growth Streptococcus pyogenes
    • Mickelson, M. N. (1964) Chemically defined medium for growth Streptococcus pyogenes. J. Bacteriol. 88, 158-164
    • (1964) J. Bacteriol. , vol.88 , pp. 158-164
    • Mickelson, M.N.1
  • 42
    • 0033031388 scopus 로고    scopus 로고
    • Visualization of membrane domains in Escherichia coli
    • Fishov, I., and Woldringh, C. L. (1999) Visualization of membrane domains in Escherichia coli. Mol. Microbiol. 32, 1166-1172
    • (1999) Mol. Microbiol. , vol.32 , pp. 1166-1172
    • Fishov, I.1    Woldringh, C.L.2
  • 43
    • 0042565977 scopus 로고    scopus 로고
    • Phosphatidylethanolamine and phosphatidylglycerol are segregated into different domains in bacterial membrane. A study with pyrene-labeled phospholipids
    • Vanounou, S., Parola, A. H., and Fishov, I. (2003) Phosphatidylethanolamine and phosphatidylglycerol are segregated into different domains in bacterial membrane. A study with pyrene-labeled phospholipids. Mol. Microbiol. 49, 1067-1079
    • (2003) Mol. Microbiol. , vol.49 , pp. 1067-1079
    • Vanounou, S.1    Parola, A.H.2    Fishov, I.3
  • 44
    • 41649115159 scopus 로고    scopus 로고
    • TLR2 - Promiscuous or specific? A critical re-evaluation of a receptor expressing apparent broad specificity
    • Zahringer, U., Lindner, B., Inamura, S., Heine, H., and Alexander, C. (2008) TLR2 - promiscuous or specific? A critical re-evaluation of a receptor expressing apparent broad specificity. Immunobiology 213, 205-224
    • (2008) Immunobiology , vol.213 , pp. 205-224
    • Zahringer, U.1    Lindner, B.2    Inamura, S.3    Heine, H.4    Alexander, C.5
  • 45
    • 0016615840 scopus 로고
    • Degradation of phospholipid and release of diglyceride-rich membrane vesicles during protoplast formation in certain grampositive bacteria
    • Kusaka, I. (1975) Degradation of phospholipid and release of diglyceride-rich membrane vesicles during protoplast formation in certain grampositive bacteria. J. Bacteriol. 121, 1173-1179
    • (1975) J. Bacteriol. , vol.121 , pp. 1173-1179
    • Kusaka, I.1
  • 46
    • 77953120880 scopus 로고    scopus 로고
    • Differential activation of the Toll-like receptor 2/6 complex by lipoproteins of Streptococcus suis serotypes 2 and 9
    • Wichgers Schreur, P. J., Rebel, J. M., Smits, M. A., van Putten, J. P., and Smith, H. E. (2010) Differential activation of the Toll-like receptor 2/6 complex by lipoproteins of Streptococcus suis serotypes 2 and 9. Vet. Microbiol. 143, 363-370
    • (2010) Vet. Microbiol. , vol.143 , pp. 363-370
    • Wichgers Schreur, P.J.1    Rebel, J.M.2    Smits, M.A.3    Van Putten, J.P.4    Smith, H.E.5
  • 47
    • 80053578401 scopus 로고    scopus 로고
    • Lgt processing is an essential step in Streptococcus suis lipoprotein mediated innate immune activation
    • Wichgers Schreur, P. J., Rebel, J. M., Smits, M. A., van Putten, J. P., and Smith, H. E. (2011) Lgt processing is an essential step in Streptococcus suis lipoprotein mediated innate immune activation. PLoS One 6, e22299
    • (2011) PLoS One , vol.6
    • Wichgers Schreur, P.J.1    Rebel, J.M.2    Smits, M.A.3    Van Putten, J.P.4    Smith, H.E.5
  • 49
    • 73149088617 scopus 로고    scopus 로고
    • Gram-positive bacteria produce membrane vesicles: Proteomics-based characterization of Staphylococcus aureus-derived membrane vesicles
    • Lee, E. Y., Choi, D. Y., Kim, D. K., Kim, J. W., Park, J. O., Kim, S., Kim, S. H., Desiderio, D. M., Kim, Y. K., Kim, K. P., and Gho, Y. S. (2009) Gram-positive bacteria produce membrane vesicles: proteomics-based characterization of Staphylococcus aureus-derived membrane vesicles. Proteomics 9, 5425-5436
    • (2009) Proteomics , vol.9 , pp. 5425-5436
    • Lee, E.Y.1    Choi, D.Y.2    Kim, D.K.3    Kim, J.W.4    Park, J.O.5    Kim, S.6    Kim, S.H.7    Desiderio, D.M.8    Kim, Y.K.9    Kim, K.P.10    Gho, Y.S.11
  • 51
    • 0033030028 scopus 로고    scopus 로고
    • Transcription- and translation-dependent changes in membrane dynamics in bacteria: Testing the transertion model for domain formation
    • Binenbaum, Z., Parola, A. H., Zaritsky, A., and Fishov, I. (1999) Transcription- and translation-dependent changes in membrane dynamics in bacteria: testing the transertion model for domain formation. Mol. Microbiol. 32, 1173-1182
    • (1999) Mol. Microbiol. , vol.32 , pp. 1173-1182
    • Binenbaum, Z.1    Parola, A.H.2    Zaritsky, A.3    Fishov, I.4
  • 52
    • 27144531235 scopus 로고    scopus 로고
    • Mutations in HlyD, part of the type 1 translocator for hemolysin secretion, affect the folding of the secreted toxin
    • Pimenta, A. L., Racher, K., Jamieson, L., Blight, M. A., and Holland, I. B. (2005) Mutations in HlyD, part of the type 1 translocator for hemolysin secretion, affect the folding of the secreted toxin. J. Bacteriol. 187, 7471-7480
    • (2005) J. Bacteriol. , vol.187 , pp. 7471-7480
    • Pimenta, A.L.1    Racher, K.2    Jamieson, L.3    Blight, M.A.4    Holland, I.B.5
  • 53
    • 16244387909 scopus 로고    scopus 로고
    • Cryo-electron microscopy reveals native polymeric cell wall structure in Bacillus subtilis 168 and the existence of a periplasmic space
    • Matias, V. R., and Beveridge, T. J. (2005) Cryo-electron microscopy reveals native polymeric cell wall structure in Bacillus subtilis 168 and the existence of a periplasmic space. Mol. Microbiol. 56, 240-251
    • (2005) Mol. Microbiol. , vol.56 , pp. 240-251
    • Matias, V.R.1    Beveridge, T.J.2
  • 54
    • 33947282277 scopus 로고    scopus 로고
    • Cryo-electron microscopy of cell division in Staphylococcus aureus reveals a midzone between nascent cross walls
    • Matias, V. R., and Beveridge, T. J. (2007) Cryo-electron microscopy of cell division in Staphylococcus aureus reveals a midzone between nascent cross walls. Mol. Microbiol. 64, 195-206
    • (2007) Mol. Microbiol. , vol.64 , pp. 195-206
    • Matias, V.R.1    Beveridge, T.J.2
  • 55
    • 0037100250 scopus 로고    scopus 로고
    • Practice guidelines for the diagnosis and management of group A streptococcal pharyngitis. Infectious Diseases Society of America
    • Bisno, A. L., Gerber, M. A., Gwaltney, J. M., Jr., Kaplan, E. L., and Schwartz, R. H. (2002) Practice guidelines for the diagnosis and management of group A streptococcal pharyngitis. Infectious Diseases Society of America. Clin. Infect. Dis. 35, 113-125
    • (2002) Clin. Infect. Dis. , vol.35 , pp. 113-125
    • Bisno, A.L.1    Gerber, M.A.2    Gwaltney, J.M.3    Kaplan, E.L.4    Schwartz, R.H.5
  • 56
    • 0029165921 scopus 로고
    • Treatment of acute streptococcal pharyngitis and prevention of rheumatic fever: A statement for health professionals. Committee on rheumatic fever, endocarditis, and kawasaki disease of the council on cardiovascular disease in the young, the american heart association
    • Dajani, A., Taubert, K., Ferrieri, P., Peter, G., and Shulman, S. (1995) Treatment of acute streptococcal pharyngitis and prevention of rheumatic fever: a statement for health professionals. Committee on rheumatic fever, endocarditis, and kawasaki disease of the council on cardiovascular disease in the young, the american heart association. Pediatrics 96, 758-764
    • (1995) Pediatrics , vol.96 , pp. 758-764
    • Dajani, A.1    Taubert, K.2    Ferrieri, P.3    Peter, G.4    Shulman, S.5
  • 57
    • 77957959533 scopus 로고    scopus 로고
    • Biological functions and biogenesis of secreted bacterial outer membrane vesicles
    • Kulp, A., and Kuehn, M. J. (2010) Biological functions and biogenesis of secreted bacterial outer membrane vesicles. Annu. Rev. Microbiol. 64, 163-184
    • (2010) Annu. Rev. Microbiol. , vol.64 , pp. 163-184
    • Kulp, A.1    Kuehn, M.J.2
  • 58
    • 77749309281 scopus 로고    scopus 로고
    • Virulence and immunomodulatory roles of bacterial outer membrane vesicles
    • Ellis, T. N., and Kuehn, M. J. (2010) Virulence and immunomodulatory roles of bacterial outer membrane vesicles. Microbiol. Mol. Biol. Rev. 74, 81-94
    • (2010) Microbiol. Mol. Biol. Rev. , vol.74 , pp. 81-94
    • Ellis, T.N.1    Kuehn, M.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.