메뉴 건너뛰기




Volumn , Issue , 2006, Pages 659-670

Comparative three-dimensional structure of cholesterol-dependent cytolysins

Author keywords

[No Author keywords available]

Indexed keywords


EID: 33947102359     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1016/B978-012088445-2/50042-1     Document Type: Chapter
Times cited : (5)

References (46)
  • 1
    • 0033576256 scopus 로고    scopus 로고
    • Streptolysin O: inhibition of the conformational change during membrane binding of the monomer prevents oligomerization and pore formation
    • Abdel Ghani E.M., Weis S., Walev I., Kehoe M., Bhakdi S., Palmer M. Streptolysin O: inhibition of the conformational change during membrane binding of the monomer prevents oligomerization and pore formation. Biochemistry 1999, 38:15204-15211.
    • (1999) Biochemistry , vol.38 , pp. 15204-15211
    • Abdel Ghani, E.M.1    Weis, S.2    Walev, I.3    Kehoe, M.4    Bhakdi, S.5    Palmer, M.6
  • 2
    • 0002027172 scopus 로고
    • The family of the antigenicallyrelated, cholesterol-binding ("sulphydryl-activated") cytolytic toxins
    • Academic Press, Berlin, J.E. Alouf, J.J. Freer (Eds.)
    • Alouf J.E., Geoffroy C. The family of the antigenicallyrelated, cholesterol-binding ("sulphydryl-activated") cytolytic toxins. Sourcebook of Bacterial Toxins 1991, 147-186. Academic Press, Berlin. J.E. Alouf, J.J. Freer (Eds.).
    • (1991) Sourcebook of Bacterial Toxins , pp. 147-186
    • Alouf, J.E.1    Geoffroy, C.2
  • 3
    • 0033735354 scopus 로고    scopus 로고
    • Cholesterol-binding cytolytic protein toxins
    • Alouf J.E. Cholesterol-binding cytolytic protein toxins. Int. J. Med. Microbiol. 2000, 290:351-356.
    • (2000) Int. J. Med. Microbiol. , vol.290 , pp. 351-356
    • Alouf, J.E.1
  • 4
    • 0030920430 scopus 로고    scopus 로고
    • The Arcanobacterium (Actinomyces) hemolysin, pyolysin, is a novel member of the thiol-activated cytolysin family
    • Billington S.J., Jost B.H., Cuevas W.A., Bright K.R., Songer J.G. The Arcanobacterium (Actinomyces) hemolysin, pyolysin, is a novel member of the thiol-activated cytolysin family. J. Bacteriol. 1997, 179:6100-6106.
    • (1997) J. Bacteriol. , vol.179 , pp. 6100-6106
    • Billington, S.J.1    Jost, B.H.2    Cuevas, W.A.3    Bright, K.R.4    Songer, J.G.5
  • 5
    • 4444291857 scopus 로고    scopus 로고
    • Vertical collapse of a cytolysin prepore moves its transmembrane beta-hairpins to the membrane
    • Czajkowsky D.M., Hotze E.M., Shao Z., Tweten R.K. Vertical collapse of a cytolysin prepore moves its transmembrane beta-hairpins to the membrane. EMBO J. 2004, 23:3206-3215.
    • (2004) EMBO J. , vol.23 , pp. 3206-3215
    • Czajkowsky, D.M.1    Hotze, E.M.2    Shao, Z.3    Tweten, R.K.4
  • 6
    • 0027246044 scopus 로고
    • Purification and characterization of streptolysin O secreted by Streptococcus equisimilis (group C)
    • Gerlach D., Kohler W., Gunther E., Mann K. Purification and characterization of streptolysin O secreted by Streptococcus equisimilis (group C). Infect. Immun. 1993, 61:2727-2731.
    • (1993) Infect. Immun. , vol.61 , pp. 2727-2731
    • Gerlach, D.1    Kohler, W.2    Gunther, E.3    Mann, K.4
  • 7
    • 0141706347 scopus 로고    scopus 로고
    • Redefining cholesterol's role in the mechanism of the cholesterol-dependent cytolysins
    • Giddings K.S., Johnson A.E., Tweten R.K. Redefining cholesterol's role in the mechanism of the cholesterol-dependent cytolysins. Proc. Natl. Acad. Sci. USA 2003, 100:11315-11320.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 11315-11320
    • Giddings, K.S.1    Johnson, A.E.2    Tweten, R.K.3
  • 8
    • 0033612389 scopus 로고    scopus 로고
    • Two structural transitions in membrane pore formation by pneumolysin, the poreforming toxin of Streptococcus pneumoniae
    • Gilbert R.J.C., Jiménez J.L., Chen S., Tickle I.J., Rossjohn J., Parker M.W., Andrew P.W., Saibil H.R. Two structural transitions in membrane pore formation by pneumolysin, the poreforming toxin of Streptococcus pneumoniae. Cell 1999, 97:647-655.
    • (1999) Cell , vol.97 , pp. 647-655
    • Gilbert, R.J.C.1    Jiménez, J.L.2    Chen, S.3    Tickle, I.J.4    Rossjohn, J.5    Parker, M.W.6    Andrew, P.W.7    Saibil, H.R.8
  • 11
    • 0033636662 scopus 로고    scopus 로고
    • Mechanism of membrane insertion of a multimeric beta-barrel protein: perfringolysin O creates a pore using ordered and coupled conformational changes
    • Heuck A.P., Hotze E.M., Tweten R.K., Johnson A.E. Mechanism of membrane insertion of a multimeric beta-barrel protein: perfringolysin O creates a pore using ordered and coupled conformational changes. Mol. Cell 2000, 6:1233-1242.
    • (2000) Mol. Cell , vol.6 , pp. 1233-1242
    • Heuck, A.P.1    Hotze, E.M.2    Tweten, R.K.3    Johnson, A.E.4
  • 12
    • 0035822706 scopus 로고    scopus 로고
    • β-barrel poreforming toxins: intriguing dimorphic proteins
    • Heuck A.P., Tweten R.K., Johnson A.E. β-barrel poreforming toxins: intriguing dimorphic proteins. Biochemistry 2001, 40:9065-9073.
    • (2001) Biochemistry , vol.40 , pp. 9065-9073
    • Heuck, A.P.1    Tweten, R.K.2    Johnson, A.E.3
  • 13
    • 0043234285 scopus 로고    scopus 로고
    • Assembly and topography of the prepore complex in cholesterol-dependent cytolysins
    • Heuck A.P., Tweten R.K., Johnson A.E. Assembly and topography of the prepore complex in cholesterol-dependent cytolysins. J. Biol. Chem. 2003, 278:31218-31225.
    • (2003) J. Biol. Chem. , vol.278 , pp. 31218-31225
    • Heuck, A.P.1    Tweten, R.K.2    Johnson, A.E.3
  • 14
    • 0035896507 scopus 로고    scopus 로고
    • Arresting pore formation of a cholesterol-dependent cytolysin by disulfide trapping synchronizes the insertion of the transmembrane beta-sheet from a prepore intermediate
    • Hotze E.M., Wilson-Kubalek E.M., Rossjohn J., Parker M.W., Johnson A.E., Tweten R.K. Arresting pore formation of a cholesterol-dependent cytolysin by disulfide trapping synchronizes the insertion of the transmembrane beta-sheet from a prepore intermediate. J. Biol. Chem. 2001, 276:8261-8268.
    • (2001) J. Biol. Chem. , vol.276 , pp. 8261-8268
    • Hotze, E.M.1    Wilson-Kubalek, E.M.2    Rossjohn, J.3    Parker, M.W.4    Johnson, A.E.5    Tweten, R.K.6
  • 15
    • 0037192791 scopus 로고    scopus 로고
    • Monomer-monomer interactions drive the prepore to pore conversion of a beta barrel-forming, cholesterol-dependent cytolysin
    • Hotze E.M., Heuck A.P., Czajkowsky D.M., Shao Z., Johnson A.E., Tweten R.K. Monomer-monomer interactions drive the prepore to pore conversion of a beta barrel-forming, cholesterol-dependent cytolysin. J. Biol. Chem. 2002, 277:11597-11605.
    • (2002) J. Biol. Chem. , vol.277 , pp. 11597-11605
    • Hotze, E.M.1    Heuck, A.P.2    Czajkowsky, D.M.3    Shao, Z.4    Johnson, A.E.5    Tweten, R.K.6
  • 16
    • 0023656177 scopus 로고
    • Role of the essential thiol group in the thiol-activated cytolysin from Clostridium perfringens
    • Iwamoto M., Ohno-Iwashita Y., Ando S. Role of the essential thiol group in the thiol-activated cytolysin from Clostridium perfringens. Eur. J. Biochem. 1987, 167:425-430.
    • (1987) Eur. J. Biochem. , vol.167 , pp. 425-430
    • Iwamoto, M.1    Ohno-Iwashita, Y.2    Ando, S.3
  • 17
    • 0028072474 scopus 로고
    • Characterization of Listeria monocytogenes pathogenesis in a strain expressing perfringolysin O instead of listeriolysin O
    • Jones S., Portnoy D.A. Characterization of Listeria monocytogenes pathogenesis in a strain expressing perfringolysin O instead of listeriolysin O. Infect. Immun. 1994, 62:5608-5613.
    • (1994) Infect. Immun. , vol.62 , pp. 5608-5613
    • Jones, S.1    Portnoy, D.A.2
  • 18
    • 0023491913 scopus 로고
    • Nucleotide sequence of the streptolysin O (SLO) gene: structural homologies between SLO and other membrane-damaging, thiolactivated toxins
    • Kehoe M.A., Miller L., Walker J.A., Boulrois G.J. Nucleotide sequence of the streptolysin O (SLO) gene: structural homologies between SLO and other membrane-damaging, thiolactivated toxins. Infect. Immun. 1987, 55:3228-3232.
    • (1987) Infect. Immun. , vol.55 , pp. 3228-3232
    • Kehoe, M.A.1    Miller, L.2    Walker, J.A.3    Boulrois, G.J.4
  • 19
    • 0026244229 scopus 로고
    • MOLSCRIPT: a program to produce both detailed and schematic plots of proteins
    • Kraulis P. MOLSCRIPT: a program to produce both detailed and schematic plots of proteins. J. Appl. Crystallogr. 1991, 24:946-950.
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.1
  • 20
    • 0034823866 scopus 로고    scopus 로고
    • Effect on polymorphonuclear cell function of a human-specific cytotoxin, intermedilysin, expressed by Streptococcus intermedius
    • Macey M.G., Whiley R.A., Miller L., Nagamune H. Effect on polymorphonuclear cell function of a human-specific cytotoxin, intermedilysin, expressed by Streptococcus intermedius. Infect. Immun. 2001, 69:6102-6109.
    • (2001) Infect. Immun. , vol.69 , pp. 6102-6109
    • Macey, M.G.1    Whiley, R.A.2    Miller, L.3    Nagamune, H.4
  • 21
    • 0030037295 scopus 로고    scopus 로고
    • Intermedilysin, a novel cytotoxin specific for human cells secreted by Streptococcus intermedius UNS46 isolated from a human liver abscess
    • Nagamune H., Ohnishi C., Katsuura A., Fushitani K., Whiley R.A., Tsuji A., Matsuda Y. Intermedilysin, a novel cytotoxin specific for human cells secreted by Streptococcus intermedius UNS46 isolated from a human liver abscess. Infect. Immun. 1996, 64:3093-3100.
    • (1996) Infect. Immun. , vol.64 , pp. 3093-3100
    • Nagamune, H.1    Ohnishi, C.2    Katsuura, A.3    Fushitani, K.4    Whiley, R.A.5    Tsuji, A.6    Matsuda, Y.7
  • 22
    • 0033628592 scopus 로고    scopus 로고
    • Distribution of the intermedilysin gene among the anginosus group streptococci and correlation between intermedilysin production and deep-seated infection with Streptococcus intermedius
    • Nagamune H., Whiley R.A., Goto T., Inai Y., Maeda T., Hardie J.M., Kourai H. Distribution of the intermedilysin gene among the anginosus group streptococci and correlation between intermedilysin production and deep-seated infection with Streptococcus intermedius. J. Clin. Microbiol. 2000, 38:220-226.
    • (2000) J. Clin. Microbiol. , vol.38 , pp. 220-226
    • Nagamune, H.1    Whiley, R.A.2    Goto, T.3    Inai, Y.4    Maeda, T.5    Hardie, J.M.6    Kourai, H.7
  • 23
    • 0028988973 scopus 로고
    • Interaction of θ{symbol}-toxin (perfringolysin O), a cholesterol-binding cytlysin, with liposomal membranes: change in the aromatic side chains upon binding and insertion
    • Nakamura M., Sekino N., Iwamoto M., Ohno-Iwashita Y. Interaction of θ{symbol}-toxin (perfringolysin O), a cholesterol-binding cytlysin, with liposomal membranes: change in the aromatic side chains upon binding and insertion. Biochemistry 1995, 34:6513-6520.
    • (1995) Biochemistry , vol.34 , pp. 6513-6520
    • Nakamura, M.1    Sekino, N.2    Iwamoto, M.3    Ohno-Iwashita, Y.4
  • 24
    • 0032932083 scopus 로고    scopus 로고
    • Crystal structure of Staphylococcal LukF delineates conformational changes accompanying formation of a transmembrane channel
    • Olson R., Nariya H., Yokota K., Kamio Y., Gouaux E. Crystal structure of Staphylococcal LukF delineates conformational changes accompanying formation of a transmembrane channel. Nature Struct. Biol. 1999, 6:134-140.
    • (1999) Nature Struct. Biol. , vol.6 , pp. 134-140
    • Olson, R.1    Nariya, H.2    Yokota, K.3    Kamio, Y.4    Gouaux, E.5
  • 25
    • 0032562167 scopus 로고    scopus 로고
    • Streptolysin O: a proposed model of allosteric interaction between a pore-forming protein and its target lipid bilayer
    • Palmer M., Vulicevic I., Saweljew P., Valeva A., Kehoe M., Bhakdi S. Streptolysin O: a proposed model of allosteric interaction between a pore-forming protein and its target lipid bilayer. Biochemistry 1998, 37:2378-2383.
    • (1998) Biochemistry , vol.37 , pp. 2378-2383
    • Palmer, M.1    Vulicevic, I.2    Saweljew, P.3    Valeva, A.4    Kehoe, M.5    Bhakdi, S.6
  • 26
    • 0034877296 scopus 로고    scopus 로고
    • The family of thiol-activated, cholesterol-binding cytolysins
    • Palmer M. The family of thiol-activated, cholesterol-binding cytolysins. Toxicon 2001, 39:1681-1689.
    • (2001) Toxicon , vol.39 , pp. 1681-1689
    • Palmer, M.1
  • 28
    • 0033103175 scopus 로고    scopus 로고
    • The structure of a Staphylococcus aureus leucocidin component (LukF-PV) reveals the fold of the water-soluble species of a family of transmembrane pore-forming toxins
    • Pédelacq J-D., Maveyraud L., Prévost G., Baba-Moussa L., González A., Courcelle E., Shepard W., Monteil H., Samama J-P., Mourey L. The structure of a Staphylococcus aureus leucocidin component (LukF-PV) reveals the fold of the water-soluble species of a family of transmembrane pore-forming toxins. Structure 1999, 7:277-287.
    • (1999) Structure , vol.7 , pp. 277-287
    • Pédelacq, J.-D.1    Maveyraud, L.2    Prévost, G.3    Baba-Moussa, L.4    González, A.5    Courcelle, E.6    Shepard, W.7    Monteil, H.8    Samama, J.-P.9    Mourey, L.10
  • 30
    • 0024720325 scopus 로고
    • The thiol-activated toxin streptolysin O does not require a thiol group for cytolytic activity
    • Pinkney M., Beachey E., Kehoe M. The thiol-activated toxin streptolysin O does not require a thiol group for cytolytic activity. Infect. Immun. 1989, 57:2553-2558.
    • (1989) Infect. Immun. , vol.57 , pp. 2553-2558
    • Pinkney, M.1    Beachey, E.2    Kehoe, M.3
  • 31
    • 4644297669 scopus 로고    scopus 로고
    • Crystallization and preliminary x-ray analysis of the human specific toxin intermedilysin
    • Polekhina G., Giddings K.S., Tweten R.K., Parker M.W. Crystallization and preliminary x-ray analysis of the human specific toxin intermedilysin. Acta Crystallogr. D 2004, 60:347-349.
    • (2004) Acta Crystallogr. D , vol.60 , pp. 347-349
    • Polekhina, G.1    Giddings, K.S.2    Tweten, R.K.3    Parker, M.W.4
  • 32
    • 14144251524 scopus 로고    scopus 로고
    • Insights into the action of the superfamily of cholesterol-dependent cytolysins from studies of intermedilysin
    • Polekhina G., Giddings K.S., Tweten R.K., Parker M.W. Insights into the action of the superfamily of cholesterol-dependent cytolysins from studies of intermedilysin. Proc. Natl. Acad. Sci. USA 2005, 102:600-605.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 600-605
    • Polekhina, G.1    Giddings, K.S.2    Tweten, R.K.3    Parker, M.W.4
  • 33
    • 0036830653 scopus 로고    scopus 로고
    • Structural insights into the membrane-anchoring mechanism of a cholesterol-dependent cytolysin
    • Ramachandran R., Heuck A.P., Tweten R.K., Johnson A.E. Structural insights into the membrane-anchoring mechanism of a cholesterol-dependent cytolysin. Nature Struct. Biol. 2002, 11:823-827.
    • (2002) Nature Struct. Biol. , vol.11 , pp. 823-827
    • Ramachandran, R.1    Heuck, A.P.2    Tweten, R.K.3    Johnson, A.E.4
  • 34
    • 3543016107 scopus 로고    scopus 로고
    • Membrane-dependent conformational changes initiate cholesterol-dependent cytolysin oligomerization and intersubunit beta-strand alignment
    • Ramachandran R., Tweten R.K., Johnson A.E. Membrane-dependent conformational changes initiate cholesterol-dependent cytolysin oligomerization and intersubunit beta-strand alignment. Nature Struct. Mol. Biol. 2004, 11:697-705.
    • (2004) Nature Struct. Mol. Biol. , vol.11 , pp. 697-705
    • Ramachandran, R.1    Tweten, R.K.2    Johnson, A.E.3
  • 35
    • 0031726607 scopus 로고    scopus 로고
    • Virulence genes of Clostridium perfringens
    • Rood J.I. Virulence genes of Clostridium perfringens. Annu. Rev. Microbiol. 1998, 52:333-360.
    • (1998) Annu. Rev. Microbiol. , vol.52 , pp. 333-360
    • Rood, J.I.1
  • 36
    • 0030666371 scopus 로고    scopus 로고
    • Structure of a cholesterol-binding, thiol-activated cytolysin and a model of its membrane form
    • Rossjohn J., Feil S.C., McKinstry W.J., Tweten R.K., Parker M.W. Structure of a cholesterol-binding, thiol-activated cytolysin and a model of its membrane form. Cell 1997, 89:685-692.
    • (1997) Cell , vol.89 , pp. 685-692
    • Rossjohn, J.1    Feil, S.C.2    McKinstry, W.J.3    Tweten, R.K.4    Parker, M.W.5
  • 37
    • 0023375195 scopus 로고
    • The neighbor-joining method: a new method for reconstructing phylogenetic trees
    • Saitou N., Nei M. The neighbor-joining method: a new method for reconstructing phylogenetic trees. Mol. Biol. Evol. 1987, 4:406-425.
    • (1987) Mol. Biol. Evol. , vol.4 , pp. 406-425
    • Saitou, N.1    Nei, M.2
  • 38
    • 0024407229 scopus 로고
    • Pneumolysin, the thiol-activated toxin of Streptococcus pneumoniae, does not require a thiol group for in vitro activity
    • Saunders F.K., Mitchell T.J., Walker J.A., Andrew P.W., Boulnois G.J. Pneumolysin, the thiol-activated toxin of Streptococcus pneumoniae, does not require a thiol group for in vitro activity. Infect. Immun. 1989, 57:2547-2552.
    • (1989) Infect. Immun. , vol.57 , pp. 2547-2552
    • Saunders, F.K.1    Mitchell, T.J.2    Walker, J.A.3    Andrew, P.W.4    Boulnois, G.J.5
  • 39
    • 0033615736 scopus 로고    scopus 로고
    • The mechanism of membrane insertion for a cholesterol-dependent cytolysin: a novel paradigm for pore-forming toxins
    • Shatursky O., Heuck A.P., Shepard L.A., Rossjohn J., Parker M.W., Johnson A.E., Tweten R.K. The mechanism of membrane insertion for a cholesterol-dependent cytolysin: a novel paradigm for pore-forming toxins. Cell 1999, 99:293-299.
    • (1999) Cell , vol.99 , pp. 293-299
    • Shatursky, O.1    Heuck, A.P.2    Shepard, L.A.3    Rossjohn, J.4    Parker, M.W.5    Johnson, A.E.6    Tweten, R.K.7
  • 40
    • 0029972377 scopus 로고    scopus 로고
    • Contribution of individual tryptophan residues to the structure and activity of θ{symbol}-toxin (perfringolysin-O), a cholesterol-binding cytolysin
    • Sekino-Suzuki N., Nakamura M., Mitsui K.I., Ohno-Iwashita Y. Contribution of individual tryptophan residues to the structure and activity of θ{symbol}-toxin (perfringolysin-O), a cholesterol-binding cytolysin. Eur. J. Biochem. 1996, 241:941-947.
    • (1996) Eur. J. Biochem. , vol.241 , pp. 941-947
    • Sekino-Suzuki, N.1    Nakamura, M.2    Mitsui, K.I.3    Ohno-Iwashita, Y.4
  • 41
    • 0032514655 scopus 로고    scopus 로고
    • Identification of a membrane-spanning domain of the thiol-activated, pore-forming toxin Clostridium perfringens perfringolysin O: an alpha-helical to beta-sheet transition identified by fluorescence spectroscopy
    • Shepard L.A., Heuck A.P., Hamman B.D., Rossjohn J., Parker M.W., Ryan K.R., Johnson A.E., Tweten R.K. Identification of a membrane-spanning domain of the thiol-activated, pore-forming toxin Clostridium perfringens perfringolysin O: an alpha-helical to beta-sheet transition identified by fluorescence spectroscopy. Biochemistry 1998, 37:14563-14574.
    • (1998) Biochemistry , vol.37 , pp. 14563-14574
    • Shepard, L.A.1    Heuck, A.P.2    Hamman, B.D.3    Rossjohn, J.4    Parker, M.W.5    Ryan, K.R.6    Johnson, A.E.7    Tweten, R.K.8
  • 42
    • 0034702810 scopus 로고    scopus 로고
    • The mechanism of assembly and insertion of the membrane complex of the cholesterol-dependent cytolysin perfringolysin O: Formation of a large prepore complex
    • Shepard L.A., Shatursky O., Johnson A.E., Tweten R.K. The mechanism of assembly and insertion of the membrane complex of the cholesterol-dependent cytolysin perfringolysin O: Formation of a large prepore complex. Biochemistry 2000, 39:10284-10293.
    • (2000) Biochemistry , vol.39 , pp. 10284-10293
    • Shepard, L.A.1    Shatursky, O.2    Johnson, A.E.3    Tweten, R.K.4
  • 43
    • 0030447720 scopus 로고    scopus 로고
    • Structure of Staphylococcal α-hemolysin, a heptameric transmembrane pore
    • Song L., Hobaugh M.R., Shustak C., Cheley S., Bayley H., Gouaux J.E. Structure of Staphylococcal α-hemolysin, a heptameric transmembrane pore. Science 1996, 274:1859-1866.
    • (1996) Science , vol.274 , pp. 1859-1866
    • Song, L.1    Hobaugh, M.R.2    Shustak, C.3    Cheley, S.4    Bayley, H.5    Gouaux, J.E.6
  • 44
    • 0023757453 scopus 로고
    • Nucleotide sequence of the gene for perfringolysin O (theta toxin) from Clostridium perfringens has significant homology with the genes for streptolysin O and pneumolysin
    • Tweten R.K. Nucleotide sequence of the gene for perfringolysin O (theta toxin) from Clostridium perfringens has significant homology with the genes for streptolysin O and pneumolysin. Infect. Immun. 1988, 56:3235-3240.
    • (1988) Infect. Immun. , vol.56 , pp. 3235-3240
    • Tweten, R.K.1
  • 46
    • 0023251174 scopus 로고
    • Molecular cloning, characterization, and complete nucleotide sequence of the gene for pneumolysin, the sulfhydryl-activated toxin of Streptococcus pneumoniae
    • Walker J.A., Allen R.L., Falmagne P., Johnson MK., Boulnois G.J. Molecular cloning, characterization, and complete nucleotide sequence of the gene for pneumolysin, the sulfhydryl-activated toxin of Streptococcus pneumoniae. Infect. Immun. 1987, 55:1184-1189.
    • (1987) Infect. Immun. , vol.55 , pp. 1184-1189
    • Walker, J.A.1    Allen, R.L.2    Falmagne, P.3    Johnson, M.K.4    Boulnois, G.J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.