메뉴 건너뛰기




Volumn 3, Issue 5, 2012, Pages

Occurrence and evolution of the paralogous zinc metalloproteases IgA1 protease, ZmpB, ZmpC, and ZmpD in streptococcus pneumoniae and related commensal species

Author keywords

[No Author keywords available]

Indexed keywords


EID: 84868382780     PISSN: 21612129     EISSN: 21507511     Source Type: Journal    
DOI: 10.1128/mBio.00303-12     Document Type: Article
Times cited : (44)

References (57)
  • 1
    • 0034961107 scopus 로고    scopus 로고
    • Annotated draft genomic sequence from a Streptococcus pneumoniae type 19F clinical isolate
    • Dopazo J, et al. 2001. Annotated draft genomic sequence from a Streptococcus pneumoniae type 19F clinical isolate. Microb. Drug Resist. 7:99-125.
    • (2001) Microb. Drug Resist , vol.7 , pp. 99-125
    • Dopazo, J.1
  • 2
    • 0034806849 scopus 로고    scopus 로고
    • Genome of the bacterium Streptococcus pneu-moniae strain R6
    • Hoskins J, et al. 2001. Genome of the bacterium Streptococcus pneu-moniae strain R6. J. Bacteriol. 183:5709-5717.
    • (2001) J. Bacteriol , vol.183 , pp. 5709-5717
    • Hoskins, J.1
  • 3
    • 0035919670 scopus 로고    scopus 로고
    • Complete genome sequence of a virulent isolate of Streptococcus pneumoniae
    • Tettelin H, et al. 2001. Complete genome sequence of a virulent isolate of Streptococcus pneumoniae. Science 293:498-506.
    • (2001) Science , vol.293 , pp. 498-506
    • Tettelin, H.1
  • 4
    • 0026019690 scopus 로고
    • Analysis of the immunoglobulin A protease gene of Streptococcus sanguis
    • Gilbert JV, Plaut AG, Wright A. 1991. Analysis of the immunoglobulin A protease gene of Streptococcus sanguis. Infect. Immun. 59:7-17.
    • (1991) Infect. Immun , vol.59 , pp. 7-17
    • Gilbert, J.V.1    Plaut, A.G.2    Wright, A.3
  • 5
    • 28844461772 scopus 로고    scopus 로고
    • Cloning, expression, purification, and characterization of Streptococcus pneumoniae IgA1 protease
    • Romanello V, et al. 2006. Cloning, expression, purification, and characterization of Streptococcus pneumoniae IgA1 protease. Protein Expr. Purif. 45:142-149.
    • (2006) Protein Expr. Purif , vol.45 , pp. 142-149
    • Romanello, V.1
  • 6
    • 0043166893 scopus 로고    scopus 로고
    • Pneumococcal zinc metalloproteinase ZmpC cleaves human matrix metalloproteinase 9 and is a virulence factor in experimental pneumonia
    • Oggioni MR, et al. 2003. Pneumococcal zinc metalloproteinase ZmpC cleaves human matrix metalloproteinase 9 and is a virulence factor in experimental pneumonia. Mol. Microbiol. 49:795-805.
    • (2003) Mol. Microbiol , vol.49 , pp. 795-805
    • Oggioni, M.R.1
  • 7
    • 33748507350 scopus 로고    scopus 로고
    • The atypical amino-terminal LPNTG-containing domain of the pneumococcal human IgA1-specific protease is required for proper enzyme localization and function
    • Bender MH, Weiser JN. 2006. The atypical amino-terminal LPNTG-containing domain of the pneumococcal human IgA1-specific protease is required for proper enzyme localization and function. Mol. Microbiol. 61:526-543.
    • (2006) Mol. Microbiol , vol.61 , pp. 526-543
    • Bender, M.H.1    Weiser, J.N.2
  • 8
    • 33746033795 scopus 로고    scopus 로고
    • Horizontal transfer of the immunoglobulin A1 protease gene (iga) from Streptococcus to Gemella haemolysans
    • Takenouchi-Ohkubo N, Mortensen LM, Drasbek KR, Kilian M, Poulsen K. 2006. Horizontal transfer of the immunoglobulin A1 protease gene (iga) from Streptococcus to Gemella haemolysans. Microbiology 152: 2171-2180.
    • (2006) Microbiology , vol.152 , pp. 2171-2180
    • Takenouchi-Ohkubo, N.1    Mortensen, L.M.2    Drasbek, K.R.3    Kilian, M.4    Poulsen, K.5
  • 9
    • 0035061058 scopus 로고    scopus 로고
    • The puzzle of zmpB and extensive chain formation, autolysis defect and non-translocation of choline-binding proteins in Streptococcus pneumoniae
    • Bergé M, et al. 2001. The puzzle of zmpB and extensive chain formation, autolysis defect and non-translocation of choline-binding proteins in Streptococcus pneumoniae. Mol. Microbiol. 39:1651-1660.
    • (2001) Mol. Microbiol , vol.39 , pp. 1651-1660
    • Bergé, M.1
  • 10
    • 0029794015 scopus 로고    scopus 로고
    • Characterization of the Streptococcus pneumoniae immunoglobulin A1 protease gene (iga) and its translation product
    • Poulsen K, Reinholdt J, Kilian M. 1996. Characterization of the Streptococcus pneumoniae immunoglobulin A1 protease gene (iga) and its translation product. Infect. Immun. 64:3957-3966.
    • (1996) Infect. Immun , vol.64 , pp. 3957-3966
    • Poulsen, K.1    Reinholdt, J.2    Kilian, M.3
  • 11
    • 0029797254 scopus 로고    scopus 로고
    • Identification, cloning, and sequencing of the immunoglobulin A1 protease gene of Streptococcus pneumoniae
    • Wani JH, Gilbert JV, Plaut AG, Weiser JN. 1996. Identification, cloning, and sequencing of the immunoglobulin A1 protease gene of Streptococcus pneumoniae. Infect. Immun. 64:3967-3974.
    • (1996) Infect. Immun , vol.64 , pp. 3967-3974
    • Wani, J.H.1    Gilbert, J.V.2    Plaut, A.G.3    Weiser, J.N.4
  • 12
    • 17444418689 scopus 로고    scopus 로고
    • The G5 domain: A potential N-acetylglucosamine recognition domain involved in biofilm formation
    • Bateman A, Holden MT, Yeats C. 2005. The G5 domain: a potential N-acetylglucosamine recognition domain involved in biofilm formation. Bioinformatics 21:1301-1303.
    • (2005) Bioinformatics , vol.21 , pp. 1301-1303
    • Bateman, A.1    Holden, M.T.2    Yeats, C.3
  • 13
    • 0025077034 scopus 로고
    • Conservation of a hexa-peptide sequence in the anchor region of surface proteins from gram-positive cocci
    • Fischetti VA, Pancholi V, Schneewind O. 1990. Conservation of a hexa-peptide sequence in the anchor region of surface proteins from gram-positive cocci. Mol. Microbiol. 4:1603-1605.
    • (1990) Mol. Microbiol , vol.4 , pp. 1603-1605
    • Fischetti, V.A.1    Pancholi, V.2    Schneewind, O.3
  • 14
    • 0018693212 scopus 로고
    • Pathogenic species of the genus Haemophilus and Streptococcus pneumoniae produce immunoglob-ulin A1 protease
    • Kilian M, Mestecky J, Schrohenloher RE. 1979. Pathogenic species of the genus Haemophilus and Streptococcus pneumoniae produce immunoglob-ulin A1 protease. Infect. Immun. 26:143-149.
    • (1979) Infect. Immun , vol.26 , pp. 143-149
    • Kilian, M.1    Mestecky, J.2    Schrohenloher, R.E.3
  • 15
    • 0018533105 scopus 로고
    • Immunoglobulin A1 protease production by Haemophilus influenzae and Streptococcus pneumoniae
    • Male CJ. 1979. Immunoglobulin A1 protease production by Haemophilus influenzae and Streptococcus pneumoniae. Infect. Immun. 26:254-261.
    • (1979) Infect. Immun , vol.26 , pp. 254-261
    • Male, C.J.1
  • 16
    • 0024232318 scopus 로고
    • Production and isolation of neissereal IgA proteases
    • Plaut AG. 1988. Production and isolation of neissereal IgA proteases. Methods Enzymol. 165:117-120.
    • (1988) Methods Enzymol , vol.165 , pp. 117-120
    • Plaut, A.G.1
  • 17
    • 0030014069 scopus 로고    scopus 로고
    • Biological significance of IgA1 proteases in bacterial colonization and pathogenesis: Critical evaluation of experimental evidence
    • Kilian M, Reinholdt J, Lomholt H, Poulsen K, Frandsen EV. 1996. Biological significance of IgA1 proteases in bacterial colonization and pathogenesis: critical evaluation of experimental evidence. APMIS 104: 321-338.
    • (1996) APMIS , vol.104 , pp. 321-338
    • Kilian, M.1    Reinholdt, J.2    Lomholt, H.3    Poulsen, K.4    Frandsen, E.V.5
  • 18
    • 0023932283 scopus 로고
    • Defense mechanisms involving Fc-dependent functions of immunoglobulin A and their subversion by bacterial immunoglobulin A proteases
    • Kilian M, Mestecky J, Russell MW. 1988. Defense mechanisms involving Fc-dependent functions of immunoglobulin A and their subversion by bacterial immunoglobulin A proteases. Microbiol. Rev. 52:296-303.
    • (1988) Microbiol. Rev , vol.52 , pp. 296-303
    • Kilian, M.1    Mestecky, J.2    Russell, M.W.3
  • 19
    • 0023286279 scopus 로고
    • Interference of IgA protease with the effect of secretory IgA on adherence of oral streptococci to saliva-coated hydroxy-apatite
    • Reinholdt J, Kilian M. 1987. Interference of IgA protease with the effect of secretory IgA on adherence of oral streptococci to saliva-coated hydroxy-apatite. J. Dent. Res. 66:492- 497.
    • (1987) J. Dent. Res , vol.66 , pp. 492-497
    • Reinholdt, J.1    Kilian, M.2
  • 20
    • 0037386570 scopus 로고    scopus 로고
    • Antibody-enhanced pneumococcal adherence requires IgA1 protease
    • Weiser JN, et al. 2003. Antibody-enhanced pneumococcal adherence requires IgA1 protease. Proc. Natl. Acad. Sci. U. S. A. 100:4215-4220.
    • (2003) Proc. Natl. Acad. Sci. U. S. A , vol.100 , pp. 4215-4220
    • Weiser, J.N.1
  • 21
    • 2942718793 scopus 로고    scopus 로고
    • The three extracellular zinc metalloproteinases of Streptococcus pneumoniae have a different impact on virulence in mice
    • Chiavolini D, et al. 2003. The three extracellular zinc metalloproteinases of Streptococcus pneumoniae have a different impact on virulence in mice. BMC Microbiol. 3:14.
    • (2003) BMC Microbiol , vol.3 , pp. 14
    • Chiavolini, D.1
  • 22
    • 0031740873 scopus 로고    scopus 로고
    • Large-scale identification of virulence genes from Streptococcus pneumoniae
    • Polissi A, et al. 1998. Large-scale identification of virulence genes from Streptococcus pneumoniae. Infect. Immun. 66:5620-5629.
    • (1998) Infect. Immun , vol.66 , pp. 5620-5629
    • Polissi, A.1
  • 23
    • 0030838399 scopus 로고    scopus 로고
    • The Neisseria type 2 IgA1 protease cleaves LAMP1 and promotes survival of bacteria within epithelial cells
    • Lin L, et al. 1997. The Neisseria type 2 IgA1 protease cleaves LAMP1 and promotes survival of bacteria within epithelial cells. Mol. Microbiol. 24: 1083-1094.
    • (1997) Mol. Microbiol , vol.24 , pp. 1083-1094
    • Lin, L.1
  • 24
    • 0034725019 scopus 로고    scopus 로고
    • IgA1 protease from Neisseria gonorrhoeaeinhibits TNFalpha-mediated apoptosis of human monocytic cells
    • Beck SC, Meyer TF. 2000. IgA1 protease from Neisseria gonorrhoeaeinhibits TNFalpha-mediated apoptosis of human monocytic cells. FEBS Lett. 472:287-292.
    • (2000) FEBS Lett , vol.472 , pp. 287-292
    • Beck, S.C.1    Meyer, T.F.2
  • 25
    • 0035479132 scopus 로고    scopus 로고
    • Cleavage of the hormone human chorionic gonadotropin, by the type 1 IgA1 protease of Neisseria gonorrhoeae, and its implications
    • Senior BW, Stewart WW, Galloway C, Kerr MA. 2001. Cleavage of the hormone human chorionic gonadotropin, by the type 1 IgA1 protease of Neisseria gonorrhoeae, and its implications. J. Infect. Dis. 184:922-925.
    • (2001) J. Infect. Dis , vol.184 , pp. 922-925
    • Senior, B.W.1    Stewart, W.W.2    Galloway, C.3    Kerr, M.A.4
  • 26
    • 0028918032 scopus 로고
    • IgA protease from Neisseria gonorrhoeae inhibits exocytosis in bovine chromaffin cells like tetanus toxin
    • Binscheck T, et al. 1995. IgA protease from Neisseria gonorrhoeae inhibits exocytosis in bovine chromaffin cells like tetanus toxin. J. Biol. Chem. 270:1770-1774.
    • (1995) J. Biol. Chem , vol.270 , pp. 1770-1774
    • Binscheck, T.1
  • 27
    • 33846979112 scopus 로고    scopus 로고
    • Streptococcus pneumoniae sheds syndecan-1 ectodomains through ZmpC, a metalloproteinase virulence factor
    • Chen Y, Hayashida A, Bennett AE, Hollingshead SK, Park PW. 2007. Streptococcus pneumoniae sheds syndecan-1 ectodomains through ZmpC, a metalloproteinase virulence factor. J. Biol. Chem. 282:159-167.
    • (2007) J. Biol. Chem , vol.282 , pp. 159-167
    • Chen, Y.1    Hayashida, A.2    Bennett, A.E.3    Hollingshead, S.K.4    Park, P.W.5
  • 28
    • 84857828122 scopus 로고    scopus 로고
    • A metalloproteinase secreted by Streptococcus pneumoniae removes membrane mucin MUC16 from the epithelial glycocalyx barrier
    • Govindarajan B, et al. 2012. A metalloproteinase secreted by Streptococcus pneumoniae removes membrane mucin MUC16 from the epithelial glycocalyx barrier. PLoS One 7:e32418.
    • (2012) PLoS One , vol.7
    • Govindarajan, B.1
  • 29
    • 0041823519 scopus 로고    scopus 로고
    • ZmpB, a novel virulence factor of Streptococcus pneumoniae that induces tumor necrosis factor alpha production in the respiratory tract
    • Blue CE, et al. 2003. ZmpB, a novel virulence factor of Streptococcus pneumoniae that induces tumor necrosis factor alpha production in the respiratory tract. Infect. Immun. 71:4925-4935.
    • (2003) Infect Immun , vol.71 , pp. 4925-4935
    • Blue, C.E.1
  • 30
    • 0036047758 scopus 로고    scopus 로고
    • Large-scale identification of serotype 4 Streptococcus pneumoniae virulence factors
    • Hava DL, Camilli A. 2002. Large-scale identification of serotype 4 Streptococcus pneumoniae virulence factors. Mol. Microbiol. 45:1389-1406.
    • (2002) Mol. Microbiol , vol.45 , pp. 1389-1406
    • Hava, D.L.1    Camilli, A.2
  • 31
    • 0024453078 scopus 로고
    • Taxonomic study of viridans streptococci: Description of Streptococcus gordonii sp. nov., and emended description ofStreptococcus sanguis (White and Niven 1946),Streptococcus oralis (Bridge and Sneath 1982), and Streptococcus mitis (Andrewes and Horder 1906)
    • Kilian M, Mikkelsen L, Henrichsen J. 1989. Taxonomic study of viridans streptococci: description of Streptococcus gordonii sp. nov., and emended description ofStreptococcus sanguis (White and Niven 1946),Streptococcus oralis (Bridge and Sneath 1982), and Streptococcus mitis (Andrewes and Horder 1906). Int. J. Syst. Bacteriol. 39:471-484.
    • (1989) Int. J. Syst. Bacteriol , vol.39 , pp. 471-484
    • Kilian, M.1    Mikkelsen, L.2    Henrichsen, J.3
  • 32
    • 0028823899 scopus 로고
    • Evidence of recombination and an antigenically diverse immunoglobulin A1 protease among strains of Streptococcus pneumoniae
    • LomholtH
    • Lomholt H. 1995. Evidence of recombination and an antigenically diverse immunoglobulin A1 protease among strains of Streptococcus pneumoniae. Infect. Immun. 63:4238-4243.
    • (1995) Infect. Immun , vol.63 , pp. 4238-4243
    • Lomholt, H.1
  • 33
    • 32244435886 scopus 로고    scopus 로고
    • Zinc metalloproteinase genes in clinical isolates of Streptococcus pneumoniae: Association ofthe full array with a clonal cluster comprising serotypes 8 and 11A
    • Camilli R, et al. 2006. Zinc metalloproteinase genes in clinical isolates of Streptococcus pneumoniae: association ofthe full array with a clonal cluster comprising serotypes 8 and 11A. Microbiology 152:313-321.
    • (2006) Microbiology , vol.152 , pp. 313-321
    • Camilli, R.1
  • 34
    • 0025270701 scopus 로고
    • Molecular aspects of immunoglobulin A1 degradation by oral streptococci
    • Reinholdt J, Tomana M, Mortensen SB, Kilian M. 1990. Molecular aspects of immunoglobulin A1 degradation by oral streptococci. Infect. Immun. 58:1186-1194.
    • (1990) Infect. Immun , vol.58 , pp. 1186-1194
    • Reinholdt, J.1    Tomana, M.2    Mortensen, S.B.3    Kilian, M.4
  • 35
    • 79951580740 scopus 로고    scopus 로고
    • IgA1 protease contributes to the virulence of Streptococcus suis
    • Zhang A, et al. 2011. IgA1 protease contributes to the virulence of Streptococcus suis. Vet. Microbiol. 148:436-439.
    • (2011) Vet. Microbiol , vol.148 , pp. 436-439
    • Zhang, A.1
  • 36
    • 71549118508 scopus 로고    scopus 로고
    • Identification and characterization of IgA1 protease from Streptococcus suis
    • Zhang A, et al. 2010. Identification and characterization of IgA1 protease from Streptococcus suis. Vet. Microbiol. 140:171-175.
    • (2010) Vet. Microbiol , vol.140 , pp. 171-175
    • Zhang, A.1
  • 37
    • 60549102164 scopus 로고    scopus 로고
    • Assigning strains to bacterial species via the internet
    • Bishop CJ, et al. 2009. Assigning strains to bacterial species via the internet. BMC Biol. 7: 3.
    • (2009) BMC Biol , vol.7 , pp. 3
    • Bishop, C.J.1
  • 38
    • 0018833761 scopus 로고
    • IgA1 proteases from Haemophilus influenzae, Streptococcus pneumoniae, Neis-seria meningitidis, and Streptococcus sanguis: Comparative immunochemi-cal studies
    • Kilian M, Mestecky J, Kulhavy R, Tomana M, Butler WT. 1980. IgA1 proteases from Haemophilus influenzae, Streptococcus pneumoniae, Neis-seria meningitidis, and Streptococcus sanguis: comparative immunochemi-cal studies. J. Immunol. 124:2596-2600.
    • (1980) J. Immunol , vol.124 , pp. 2596-2600
    • Kilian, M.1    Mestecky, J.2    Kulhavy, R.3    Tomana, M.4    Butler, W.T.5
  • 39
    • 49949099910 scopus 로고    scopus 로고
    • Evolution of Streptococcus pneumoniae and its close commensal relatives
    • Kilian M, et al. 2008. Evolution of Streptococcus pneumoniae and its close commensal relatives. PLoS One 3: e2683.
    • (2008) PLoS One , vol.3
    • Kilian, M.1
  • 40
    • 0041810300 scopus 로고    scopus 로고
    • Streptococcus oligofermentans sp. nov., a novel oral isolate from caries-free humans
    • Tong H, Gao X, Dong X. 2003. Streptococcus oligofermentans sp. nov., a novel oral isolate from caries-free humans. Int. J. Syst. Evol. Microbiol. 53:1101-1104.
    • (2003) Int. J. Syst. Evol. Microbiol , vol.53 , pp. 1101-1104
    • Tong, H.1    Gao, X.2    Dong, X.3
  • 41
    • 77949769229 scopus 로고    scopus 로고
    • The genome of Streptococcus mitis B6-what is a commensal?
    • Denapaite D, et al. 2010. The genome of Streptococcus mitis B6-what is a commensal? PLoS One 5: e9426.
    • (2010) PLoS One , vol.5
    • Denapaite, D.1
  • 42
    • 33746078976 scopus 로고    scopus 로고
    • Immunoglobulin A1 proteases of pathogenic and commensal bacteria of the respiratory tract
    • In Na-tarro JP, Cohen PS, Mobley HLT, Weiser JN, ASM Press, Washington, DC
    • Kilian M, Reinholdt J. 2005. Immunoglobulin A1 proteases of pathogenic and commensal bacteria of the respiratory tract, p 119-129. In Na-tarro JP, Cohen PS, Mobley HLT, Weiser JN (ed), Colonization of muco-sal surfaces. ASM Press, Washington, DC.
    • (2005) Colonization of Muco-sal Surfaces , pp. 119-129
    • Kilian, M.1    Reinholdt, J.2
  • 43
    • 0031975583 scopus 로고    scopus 로고
    • A comprehensive genetic study of streptococcal immunoglobulin A1 proteases: Evidence for recombination within and between species
    • Poulsen K, et al. 1998. A comprehensive genetic study of streptococcal immunoglobulin A1 proteases: evidence for recombination within and between species. Infect. Immun. 66:181-190.
    • (1998) Infect. Immun , vol.66 , pp. 181-190
    • Poulsen, K.1
  • 44
    • 0031962770 scopus 로고    scopus 로고
    • Recombinational exchanges at the capsular poly-saccharide biosynthetic locus lead to frequent serotype changes among natural isolates of Streptococcus pneumoniae
    • Coffey TJ, et al. 1998. Recombinational exchanges at the capsular poly-saccharide biosynthetic locus lead to frequent serotype changes among natural isolates of Streptococcus pneumoniae. Mol. Microbiol. 27:73-83.
    • (1998) Mol. Microbiol , vol.27 , pp. 73-83
    • Coffey, T.J.1
  • 45
    • 79251544864 scopus 로고    scopus 로고
    • Rapid pneumococcal evolution in response to clinical interventions
    • Croucher NJ, et al. 2011. Rapid pneumococcal evolution in response to clinical interventions. Science 331:430-434.
    • (2011) Science , vol.331 , pp. 430-434
    • Croucher, N.J.1
  • 46
    • 33645774644 scopus 로고    scopus 로고
    • Genetic analysis of the capsular biosynthetic locus from all 90 pneumococcal serotypes
    • Bentley SD, et al. 2006. Genetic analysis of the capsular biosynthetic locus from all 90 pneumococcal serotypes. PLoS Genet. 2: e31.
    • (2006) PLoS Genet , vol.2
    • Bentley, S.D.1
  • 47
    • 0033959357 scopus 로고    scopus 로고
    • Barriers to genetic exchange between bacterial species: Streptococcus pneu-moniae transformation
    • Majewski J, Zawadzki P, Pickerill P, Cohan FM, Dowson CG. 2000. Barriers to genetic exchange between bacterial species:Streptococcus pneu-moniae transformation. J. Bacteriol. 182:1016-1023.
    • (2000) J. Bacteriol , vol.182 , pp. 1016-1023
    • Majewski, J.1    Zawadzki, P.2    Pickerill, P.3    Cohan, F.M.4    Dowson, C.G.5
  • 49
    • 0027991824 scopus 로고
    • Antigenic relationships among immuno-globulin A1 proteases from Haemophilus, Neisseria, and Streptococcusspecies
    • Lomholt H, Kilian M. 1994. Antigenic relationships among immuno-globulin A1 proteases from Haemophilus, Neisseria, and Streptococcusspecies. Infect. Immun. 62:3178-3183.
    • (1994) Infect. Immun , vol.62 , pp. 3178-3183
    • Lomholt, H.1    Kilian, M.2
  • 50
    • 0026722514 scopus 로고
    • Concerted evolution of the primate immunoglobulin alpha-gene through gene conversion
    • Kawamura S, Saitou N, Ueda S. 1992. Concerted evolution of the primate immunoglobulin alpha-gene through gene conversion. J. Biol. Chem. 267:7359-7367.
    • (1992) J. Biol. Chem , vol.267 , pp. 7359-7367
    • Kawamura, S.1    Saitou, N.2    Ueda, S.3
  • 51
    • 33847253862 scopus 로고    scopus 로고
    • Genomic relationships and speciation times of human, chimpanzee, and gorilla inferred from a coalescent hidden Markov model
    • Hobolth A, Christensen OF, Mailund T, Schierup MH. 2007. Genomic relationships and speciation times of human, chimpanzee, and gorilla inferred from a coalescent hidden Markov model. PLoS Genet. 3: e7.
    • (2007) PLoS Genet , vol.3
    • Hobolth, A.1    Christensen, O.F.2    Mailund, T.3    Schierup, M.H.4
  • 52
    • 68049142320 scopus 로고    scopus 로고
    • Multiple alignment of DNA sequences with MAFFT
    • Katoh K, Asimenos G, Toh H. 2009. Multiple alignment of DNA sequences with MAFFT. Methods Mol. Biol. 537:39-64.
    • (2009) Methods Mol. Biol , vol.537 , pp. 39-64
    • Katoh, K.1    Asimenos, G.2    Toh, H.3
  • 53
    • 79957613599 scopus 로고    scopus 로고
    • MEGA5: Molecular Evolutionary Genetics Analysis using maximum likelihood, evolutionary distance, and maximum parsimony methods
    • Tamura K, et al. 2011. MEGA5: Molecular Evolutionary Genetics Analysis using maximum likelihood, evolutionary distance, and maximum parsimony methods. Mol. Biol. Evol. 28:2731-2739.
    • (2011) Mol. Biol. Evol , vol.28 , pp. 2731-2739
    • Tamura, K.1
  • 54
    • 0028889839 scopus 로고
    • Construction and evaluation of new drug-resistance cassettes for gene disruption mutagenesis in Streptococcus pneumoniae, using an ami test platform
    • Claverys JP, Dintilhac A, Pestova EV, Martin B, Morrison DA. 1995. Construction and evaluation of new drug-resistance cassettes for gene disruption mutagenesis in Streptococcus pneumoniae, using an ami test platform. Gene 164: 123-128.
    • (1995) Gene , vol.164 , pp. 123-128
    • Claverys, J.P.1    Dintilhac, A.2    Pestova, E.V.3    Martin, B.4    Morrison, D.A.5
  • 55
    • 0030668266 scopus 로고    scopus 로고
    • Natural competence in the genus Streptococcus: Evidence that streptococci can change pherotype by interspecies recombinational exchanges
    • Håvarstein LS, Hakenbeck R, Gaustad P. 1997. Natural competence in the genus Streptococcus: evidence that streptococci can change pherotype by interspecies recombinational exchanges. J. Bacteriol. 179:6589-6594.
    • (1997) J. Bacteriol , vol.179 , pp. 6589-6594
    • Håvarstein, L.S.1    Hakenbeck, R.2    Gaustad, P.3
  • 56
    • 0029795692 scopus 로고    scopus 로고
    • Competence for genetic transformation in encapsulated strains of Streptococcus pneumoniae: Two allelic variants of the pep-tide pheromone
    • Pozzi G, et al. 1996. Competence for genetic transformation in encapsulated strains of Streptococcus pneumoniae: two allelic variants of the pep-tide pheromone. J. Bacteriol. 178:6087-6090.
    • (1996) J. Bacteriol , vol.178 , pp. 6087-6090
    • Pozzi, G.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.