메뉴 건너뛰기




Volumn 46, Issue 3-4, 2010, Pages 268-271

Identification of Pseudomonas bacteriophage PaP3 lysozyme

Author keywords

Bacteriophage; Gene expression; Lysozyme; Pseudomonas aeruginosa

Indexed keywords

BIOINFORMATIC ANALYSIS; CELL WALLS; COMPLETE GENOMES; E. COLI; ESCHERICHIA COLI JM109; GEL-DIFFUSION; GRAM-NEGATIVE BACTERIA; HOMOLOGY SEARCH; INHIBITORY EFFECT; LYSOZYME; LYSOZYME GENES; NEW MEMBERS; P.AERUGINOSA; PEPTIDOGLYCANS; PSEUDOMONAS AERUGINOSA; RECOMBINANT EXPRESSION; RECOMBINANT PLASMID; SECONDARY STRUCTURES; STAPHYLOCOCCUS AUREUS;

EID: 74149084452     PISSN: 01410229     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.enzmictec.2009.10.010     Document Type: Article
Times cited : (1)

References (18)
  • 1
    • 33846208695 scopus 로고    scopus 로고
    • Whole genome sequencing of a novel temperate bacteriophage of P. aeruginosa: evidence of tRNA gene mediating integration of the phage genome into the host bacterial chromosome
    • Tan Y., Zhang K., Rao X., Jin X., Huang J., Zhu J., et al. Whole genome sequencing of a novel temperate bacteriophage of P. aeruginosa: evidence of tRNA gene mediating integration of the phage genome into the host bacterial chromosome. Cell Microbiol 9 (2007) 479-491
    • (2007) Cell Microbiol , vol.9 , pp. 479-491
    • Tan, Y.1    Zhang, K.2    Rao, X.3    Jin, X.4    Huang, J.5    Zhu, J.6
  • 2
    • 24944587206 scopus 로고    scopus 로고
    • Bacteriophage lytic enzymes: novel anti-infectives
    • Fischetti V.A. Bacteriophage lytic enzymes: novel anti-infectives. Trends Microbiol 13 (2005) 491-496
    • (2005) Trends Microbiol , vol.13 , pp. 491-496
    • Fischetti, V.A.1
  • 3
    • 45049085846 scopus 로고    scopus 로고
    • The intron-containing genome of the lytic Pseudomonas phage LUZ24 resembles the temperate phage PaP3
    • Ceyssens P.J., Hertveldt K., Ackermann H.W., Noben J.P., Demeke M., Volckaert G., et al. The intron-containing genome of the lytic Pseudomonas phage LUZ24 resembles the temperate phage PaP3. Virology 377 (2008) 233-238
    • (2008) Virology , vol.377 , pp. 233-238
    • Ceyssens, P.J.1    Hertveldt, K.2    Ackermann, H.W.3    Noben, J.P.4    Demeke, M.5    Volckaert, G.6
  • 5
    • 0024289285 scopus 로고
    • Investigation of the bicinchoninic acid protein assay: identification of the groups responsible for color formation
    • Wiechelman K.J., Braun R.D., and Fitzpatrick J.D. Investigation of the bicinchoninic acid protein assay: identification of the groups responsible for color formation. Anal Biochem 175 (1988) 231-237
    • (1988) Anal Biochem , vol.175 , pp. 231-237
    • Wiechelman, K.J.1    Braun, R.D.2    Fitzpatrick, J.D.3
  • 6
    • 0037350314 scopus 로고    scopus 로고
    • Characterization of AcmB, an N-acetylglucosaminidase autolysin from Lactococcus lactis
    • Huard C., Miranda G., Wessner F., Bolotin A., Hansen J., Foster S.J., et al. Characterization of AcmB, an N-acetylglucosaminidase autolysin from Lactococcus lactis. Microbiology 149 (2003) 695-705
    • (2003) Microbiology , vol.149 , pp. 695-705
    • Huard, C.1    Miranda, G.2    Wessner, F.3    Bolotin, A.4    Hansen, J.5    Foster, S.J.6
  • 7
    • 2942554875 scopus 로고    scopus 로고
    • Analysis of the peptidoglycan hydrolase complement of Lactococcus lactis: identification of a third N-acetylglucosaminidase, AcmC
    • Huard C., Miranda G., Redko Y., Wessner F., Foster S.J., and Chapot-Chartier M.P. Analysis of the peptidoglycan hydrolase complement of Lactococcus lactis: identification of a third N-acetylglucosaminidase, AcmC. Appl Environ Microbiol 70 (2004) 3493-3499
    • (2004) Appl Environ Microbiol , vol.70 , pp. 3493-3499
    • Huard, C.1    Miranda, G.2    Redko, Y.3    Wessner, F.4    Foster, S.J.5    Chapot-Chartier, M.P.6
  • 8
    • 0017873321 scopus 로고
    • Analysis of the accuracy and implications of simple methods for predicting the secondary structure of globular proteins
    • Garnier J., Osguthorpe D.J., and Robson B. Analysis of the accuracy and implications of simple methods for predicting the secondary structure of globular proteins. J Mol Biol 120 (1978) 97-120
    • (1978) J Mol Biol , vol.120 , pp. 97-120
    • Garnier, J.1    Osguthorpe, D.J.2    Robson, B.3
  • 9
    • 33751108305 scopus 로고    scopus 로고
    • A Consensus Data Mining secondary structure prediction by combining GOR V and Fragment Database Mining
    • Sen T.Z., Cheng H., Kloczkowski A., and Jernigan R.L. A Consensus Data Mining secondary structure prediction by combining GOR V and Fragment Database Mining. Protein Sci 15 (2006) 2499-2506
    • (2006) Protein Sci , vol.15 , pp. 2499-2506
    • Sen, T.Z.1    Cheng, H.2    Kloczkowski, A.3    Jernigan, R.L.4
  • 10
  • 11
    • 0036836642 scopus 로고    scopus 로고
    • Combining the GOR V algorithm with evolutionary information for protein secondary structure prediction from amino acid sequence
    • Kloczkowski A., Ting K.L., Jernigan R.L., and Garnier J. Combining the GOR V algorithm with evolutionary information for protein secondary structure prediction from amino acid sequence. Proteins 49 (2002) 154-166
    • (2002) Proteins , vol.49 , pp. 154-166
    • Kloczkowski, A.1    Ting, K.L.2    Jernigan, R.L.3    Garnier, J.4
  • 12
    • 0035910270 scopus 로고    scopus 로고
    • Predicting transmembrane protein topology with a hidden Markov model: application to complete genomes
    • Krogh A., Larsson B., von Heijne G., and Sonnhammer E.L. Predicting transmembrane protein topology with a hidden Markov model: application to complete genomes. J Mol Biol 305 (2001) 567-580
    • (2001) J Mol Biol , vol.305 , pp. 567-580
    • Krogh, A.1    Larsson, B.2    von Heijne, G.3    Sonnhammer, E.L.4
  • 13
    • 0030614959 scopus 로고    scopus 로고
    • Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites
    • Nielsen H., Engelbrecht J., Brunak S., and von Heijne G. Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites. Protein Eng 10 (1997) 1-6
    • (1997) Protein Eng , vol.10 , pp. 1-6
    • Nielsen, H.1    Engelbrecht, J.2    Brunak, S.3    von Heijne, G.4
  • 14
    • 0027121406 scopus 로고
    • Structural analysis and biological significance of the cell wall lytic enzymes of Streptococcus pneumoniae and its bacteriophage
    • Lopez R., Garcia J.L., Garcia E., Ronda C., and Garcia P. Structural analysis and biological significance of the cell wall lytic enzymes of Streptococcus pneumoniae and its bacteriophage. FEMS Microbiol Lett 79 (1992) 439-447
    • (1992) FEMS Microbiol Lett , vol.79 , pp. 439-447
    • Lopez, R.1    Garcia, J.L.2    Garcia, E.3    Ronda, C.4    Garcia, P.5
  • 15
    • 0018256159 scopus 로고
    • Low-molecular-weight substrate for the lysozyme of T4 bacteriophage
    • Bienkowska K., and Taylor A. Low-molecular-weight substrate for the lysozyme of T4 bacteriophage. Eur J Biochem 96 (1979) 581-584
    • (1979) Eur J Biochem , vol.96 , pp. 581-584
    • Bienkowska, K.1    Taylor, A.2
  • 16
    • 36548999782 scopus 로고    scopus 로고
    • Genomic analysis of Bartonella identifies type IV secretion systems as host adaptability factors
    • Saenz H.L., Engel P., Stoeckli M.C., Lanz C., Raddatz G., Vayssier-Taussat M., et al. Genomic analysis of Bartonella identifies type IV secretion systems as host adaptability factors. Nat Genet 39 (2007) 1469-1476
    • (2007) Nat Genet , vol.39 , pp. 1469-1476
    • Saenz, H.L.1    Engel, P.2    Stoeckli, M.C.3    Lanz, C.4    Raddatz, G.5    Vayssier-Taussat, M.6
  • 17
    • 13444283414 scopus 로고    scopus 로고
    • Control of bacteriophage T4 tail lysozyme activity during the infection process
    • Kanamaru S., Ishiwata Y., Suzuki T., Rossmann M.G., and Arisaka F. Control of bacteriophage T4 tail lysozyme activity during the infection process. J Mol Biol 346 (2005) 1013-1020
    • (2005) J Mol Biol , vol.346 , pp. 1013-1020
    • Kanamaru, S.1    Ishiwata, Y.2    Suzuki, T.3    Rossmann, M.G.4    Arisaka, F.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.