메뉴 건너뛰기




Volumn 94, Issue PART4, 2013, Pages 896-905

Proteomic profiles and kinetics of development of bacteriophage T4 and its ri and riii mutants in slowly growing Escherichia coli

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIUM LYSATE; PROTEOME;

EID: 84875658113     PISSN: 00221317     EISSN: 14652099     Source Type: Journal    
DOI: 10.1099/vir.0.048686-0     Document Type: Article
Times cited : (13)

References (31)
  • 1
    • 0002439524 scopus 로고
    • Lysis and interaction between free phage and infected cells
    • Edited by J. D. Karam. Washington, DC: American Society for Microbiology
    • Abedon, S. T. (1994). Lysis and interaction between free phage and infected cells. In Molecular Biology of Bacteriophage T4, pp. 397-405. Edited by J. D. Karam. Washington, DC: American Society for Microbiology.
    • (1994) Molecular Biology of Bacteriophage T4 , pp. 397-405
    • Abedon, S.T.1
  • 2
    • 0035461237 scopus 로고    scopus 로고
    • Bacteriophage latent-period evolution as a response to resource availability
    • Abedon, S. T., Herschler, T. D. Stopar, D. (2001). Bacteriophage latent-period evolution as a response to resource availability. Appl Environ Microbiol 67, 4233-4241.
    • (2001) Appl Environ Microbiol , vol.67 , pp. 4233-4241
    • Abedon, S.T.1    Herschler, T.D.2    Stopar, D.3
  • 3
    • 2142693752 scopus 로고    scopus 로고
    • Experimental examination of bacteriophage latent-period evolution as a response to bacterial availability
    • Abedon, S. T., Hyman, P. Thomas, C. (2003). Experimental examination of bacteriophage latent-period evolution as a response to bacterial availability. Appl Environ Microbiol 69, 7499-7506.
    • (2003) Appl Environ Microbiol , vol.69 , pp. 7499-7506
    • Abedon, S.T.1    Hyman, P.2    Thomas, C.3
  • 4
    • 0344329881 scopus 로고    scopus 로고
    • Dual channel imaging of two-dimensional electropherograms in Bacillus subtilis
    • Bernhardt, J., Buttner, K., Scharf, C. Hecker, M. (1999). Dual channel imaging of two-dimensional electropherograms in Bacillus subtilis. Electrophoresis 20, 2225-2240.
    • (1999) Electrophoresis , vol.20 , pp. 2225-2240
    • Bernhardt, J.1    Buttner, K.2    Scharf, C.3    Hecker, M.4
  • 5
    • 0014142403 scopus 로고
    • Lysis inhibition in Escherichia coli infected with bacteriophage T4
    • Bode, W. (1967). Lysis inhibition in Escherichia coli infected with bacteriophage T4. J Virol 1, 948-955.
    • (1967) J Virol , vol.1 , pp. 948-955
    • Bode, W.1
  • 6
    • 79960405193 scopus 로고    scopus 로고
    • The bacteriophage T4 rapid-lysis genes and their mutational proclivities
    • Burch, L. H., Zhang, L., Chao, F. G., Xu, H. Drake, J. W. (2011). The bacteriophage T4 rapid-lysis genes and their mutational proclivities. J Bacteriol 193, 3537-3545.
    • (2011) J Bacteriol , vol.193 , pp. 3537-3545
    • Burch, L.H.1    Zhang, L.2    Chao, F.G.3    Xu, H.4    Drake, J.W.5
  • 7
    • 84925025794 scopus 로고
    • Lysis and lysis inhibition with Escherichia coli bacteriophage
    • Doermann, A. H. (1948). Lysis and lysis inhibition with Escherichia coli bacteriophage. J Bacteriol 55, 257-276.
    • (1948) J Bacteriol , vol.55 , pp. 257-276
    • Doermann, A.H.1
  • 8
    • 8544271785 scopus 로고
    • Genetic structure of bacteriophage T4 as described by recombination studies of factors influencing plaque morphology
    • Doermann, A. H. Hill, M. B. (1953). Genetic structure of bacteriophage T4 as described by recombination studies of factors influencing plaque morphology. Genetics 38, 79-90.
    • (1953) Genetics , vol.38 , pp. 79-90
    • Doermann, A.H.1    Hill, M.B.2
  • 11
    • 78449248547 scopus 로고    scopus 로고
    • A role for accessory genes rI.-1 and rI.1 in the regulation of lysis inhibition by bacteriophage T4
    • Golec, P., Wiczk, A., Majchrzyk, A., Łoś J M., Wȩgrzyn, G. Łoś M. (2010). A role for accessory genes rI.-1 and rI.1 in the regulation of lysis inhibition by bacteriophage T4. Virus Genes 41, 459-468.
    • (2010) Virus Genes , vol.41 , pp. 459-468
    • Golec, P.1    Wiczk, A.2    Majchrzyk, A.3    Łoś, J.M.4    Wȩgrzyn, G.5    Łoś, M.6
  • 12
    • 79955773882 scopus 로고    scopus 로고
    • Persistence of bacteriophage T4 in a starved Escherichia coli culture: Evidence for the presence of phage subpopulations
    • Golec, P., Wiczk, A., Łoś, J. M., Konopa, G., Wȩgrzyn, G. Łoś M. (2011). Persistence of bacteriophage T4 in a starved Escherichia coli culture: evidence for the presence of phage subpopulations. J Gen Virol 92, 997-1003.
    • (2011) J Gen Virol , vol.92 , pp. 997-1003
    • Golec, P.1    Wiczk, A.2    Łoś, J.M.3    Konopa, G.4    Wȩgrzyn, G.5    Łoś, M.6
  • 13
    • 0032901126 scopus 로고    scopus 로고
    • Recent developments in two-dimensional gel electrophoresis with immobilized pH gradients: Wide pH gradients up to pH 12, longer separation distances and simplified procedures
    • Gorg, A., Obermaier, C., Boguth, G. Weiss, W. (1999). Recent developments in two-dimensional gel electrophoresis with immobilized pH gradients: wide pH gradients up to pH 12, longer separation distances and simplified procedures. Electrophoresis 20, 712-717.
    • (1999) Electrophoresis , vol.20 , pp. 712-717
    • Gorg, A.1    Obermaier, C.2    Boguth, G.3    Weiss, W.4
  • 14
    • 0031036488 scopus 로고    scopus 로고
    • Bacteriophage T4 development depends on the physiology of its host Escherichia coli
    • Hadas, H., Einav, M., Fishov, I. Zaritsky, A. (1997). Bacteriophage T4 development depends on the physiology of its host Escherichia coli. Microbiology 143, 179-185.
    • (1997) Microbiology , vol.143 , pp. 179-185
    • Hadas, H.1    Einav, M.2    Fishov, I.3    Zaritsky, A.4
  • 15
    • 27144469038 scopus 로고    scopus 로고
    • Continuous culture making a comeback?
    • Hoskisson, P. A. Hobbs, G. (2005). Continuous culture making a comeback? Microbiology 151, 3153-3159.
    • (2005) Microbiology , vol.151 , pp. 3153-3159
    • Hoskisson, P.A.1    Hobbs, G.2
  • 16
    • 0027251266 scopus 로고
    • The Escherichia coli K-12 "wild types" W3110 and MG1655 have an rph frameshift mutation that leads to pyrimidine starvation due to low pyrE expression levels
    • Jensen, K. F. (1993). The Escherichia coli K-12 "wild types" W3110 and MG1655 have an rph frameshift mutation that leads to pyrimidine starvation due to low pyrE expression levels. J Bacteriol 175, 3401-3407.
    • (1993) J Bacteriol , vol.175 , pp. 3401-3407
    • Jensen, K.F.1
  • 17
    • 0037146488 scopus 로고    scopus 로고
    • Highly sensitive and fast protein detection with Coomassie brilliant blue in sodium dodecyl sulfate-polyacrylamide gel electrophoresis
    • Kang, D., Gho, Y. S., Suh, M. Kang, C. (2002). Highly sensitive and fast protein detection with Coomassie brilliant blue in sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Bull Korean Chem Soc 23, 1511-1512.
    • (2002) Bull Korean Chem Soc , vol.23 , pp. 1511-1512
    • Kang, D.1    Gho, Y.S.2    Suh, M.3    Kang, C.4
  • 18
    • 0015163742 scopus 로고
    • The adaptive responses of Escherichia coli to a feast and famine existence
    • Koch, A. L. (1971). The adaptive responses of Escherichia coli to a feast and famine existence. Adv Microb Physiol 6, 147-217.
    • (1971) Adv Microb Physiol , vol.6 , pp. 147-217
    • Koch, A.L.1
  • 21
    • 0141532944 scopus 로고    scopus 로고
    • A role for bacteriophage T4 rI gene function in the control of phage development during pseudolysogeny and in slowly growing host cells
    • Łoś M, Wȩgrzyn, G. Neubauer, P. (2003). A role for bacteriophage T4 rI gene function in the control of phage development during pseudolysogeny and in slowly growing host cells. Res Microbiol 154, 547-552.
    • (2003) Res Microbiol , vol.154 , pp. 547-552
    • Łoś, M.1    Wȩgrzyn, G.2    Neubauer, P.3
  • 24
  • 25
    • 0036301681 scopus 로고    scopus 로고
    • Bacteriophage T4 development in Escherichia coli is growth rate dependent
    • Rabinovitch, A., Fishov, I., Hadas, H., Einav, M. Zaritsky, A. (2002). Bacteriophage T4 development in Escherichia coli is growth rate dependent. J Theor Biol 216, 1-4.
    • (2002) J Theor Biol , vol.216 , pp. 1-4
    • Rabinovitch, A.1    Fishov, I.2    Hadas, H.3    Einav, M.4    Zaritsky, A.5
  • 26
    • 0035053290 scopus 로고    scopus 로고
    • Functional analysis of the phage T4 holin in a l context
    • Ramanculov, E. Young, R. (2001). Functional analysis of the phage T4 holin in a l context. Mol Genet Genomics 265, 345-353.
    • (2001) Mol Genet Genomics , vol.265 , pp. 345-353
    • Ramanculov, E.1    Young, R.2
  • 28
    • 0032219184 scopus 로고    scopus 로고
    • Amplification of ColE1 related plasmids in recombinant cultures of Escherichia coli after IPTG induction
    • Teich, A., Lin, H. Y., Andersson, L., Meyer, S. Neubauer, P. (1998). Amplification of ColE1 related plasmids in recombinant cultures of Escherichia coli after IPTG induction. J Biotechnol 64, 197-210.
    • (1998) J Biotechnol , vol.64 , pp. 197-210
    • Teich, A.1    Lin, H.Y.2    Andersson, L.3    Meyer, S.4    Neubauer, P.5
  • 29
    • 81855185401 scopus 로고    scopus 로고
    • Proteomic analysis of the extremely thermoacidophilic archaeon Picrophilus torridus at pH and temperature values close to its growth limit
    • Thurmer, A., Voigt, B., Angelov, A., Albrecht, D., Hecker, M. Liebl, W. (2011). Proteomic analysis of the extremely thermoacidophilic archaeon Picrophilus torridus at pH and temperature values close to its growth limit. Proteomics 11, 4559-4568.
    • (2011) Proteomics , vol.11 , pp. 4559-4568
    • Thurmer, A.1    Voigt, B.2    Angelov, A.3    Albrecht, D.4    Hecker, M.5    Liebl, W.6
  • 30
    • 25144505528 scopus 로고    scopus 로고
    • Periplasmic domains define holin-antiholin interactions in T4 lysis inhibition
    • Tran, T. A., Struck, D. K. Young, R. (2005). Periplasmic domains define holin-antiholin interactions in T4 lysis inhibition. J Bacteriol 187, 6631-6640.
    • (2005) J Bacteriol , vol.187 , pp. 6631-6640
    • Tran, T.A.1    Struck, D.K.2    Young, R.3
  • 31
    • 35648978139 scopus 로고    scopus 로고
    • The T4 RI antiholin has an N-terminal signal anchor release domain that targets it for degradation by DegP
    • Tran, T. A., Struck, D. K. Young, R. (2007). The T4 RI antiholin has an N-terminal signal anchor release domain that targets it for degradation by DegP. J Bacteriol 189, 7618-7625.
    • (2007) J Bacteriol , vol.189 , pp. 7618-7625
    • Tran, T.A.1    Struck, D.K.2    Young, R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.