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Volumn 82, Issue , 2012, Pages 155-178

Phage λ-New Insights into Regulatory Circuits

Author keywords

Bacteriophage lambda; Genetic switches; Regulation of biological processes; Viral development

Indexed keywords


EID: 84858211116     PISSN: 00653527     EISSN: 15578399     Source Type: Book Series    
DOI: 10.1016/B978-0-12-394621-8.00016-9     Document Type: Chapter
Times cited : (53)

References (107)
  • 1
    • 44449154784 scopus 로고    scopus 로고
    • DNA looping can enhance lysogenic CI transcription in phage lambda
    • Anderson L.M., Yang H. DNA looping can enhance lysogenic CI transcription in phage lambda. Proc. Natl. Acad. Sci. USA 2008, 105:5827-5832.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 5827-5832
    • Anderson, L.M.1    Yang, H.2
  • 2
    • 35548990232 scopus 로고    scopus 로고
    • A synthetic phage lambda regulatory circuit
    • Atsumi S., Little J.W. A synthetic phage lambda regulatory circuit. Proc. Natl. Acad. Sci. USA 2006, 103:19045-19050.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 19045-19050
    • Atsumi, S.1    Little, J.W.2
  • 4
    • 70449519963 scopus 로고    scopus 로고
    • Minimal gene regulatory circuits that can count like bacteriophage lambda
    • Avlund M., Dodd I.B., Sneppen K., Krishna S. Minimal gene regulatory circuits that can count like bacteriophage lambda. J. Mol. Biol. 2009, 394:681-693.
    • (2009) J. Mol. Biol. , vol.394 , pp. 681-693
    • Avlund, M.1    Dodd, I.B.2    Sneppen, K.3    Krishna, S.4
  • 5
    • 36749054068 scopus 로고    scopus 로고
    • Cooperative DNA binding by CI repressor is dispensable in a phage lambda variant
    • Babić A.C., Little J.W. Cooperative DNA binding by CI repressor is dispensable in a phage lambda variant. Proc. Natl. Acad. Sci. USA 2007, 104:17741-17746.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 17741-17746
    • Babić, A.C.1    Little, J.W.2
  • 6
    • 17144391041 scopus 로고    scopus 로고
    • Transcriptional activation mechanisms of the PRM promoter of lambda phage
    • Bakk A. Transcriptional activation mechanisms of the PRM promoter of lambda phage. Biophys. Chem. 2005, 114:229-234.
    • (2005) Biophys. Chem. , vol.114 , pp. 229-234
    • Bakk, A.1
  • 7
    • 77956171847 scopus 로고    scopus 로고
    • Escherichia coli HflK and HflC can individually inhibit the HflB (FtsH)-mediated proteolysis of lambdaCII in vitro
    • Bandyopadhyay K., Parua P.K., Datta A.B., Parrack P. Escherichia coli HflK and HflC can individually inhibit the HflB (FtsH)-mediated proteolysis of lambdaCII in vitro. Arch. Biochem. Biophys. 2010, 501:239-243.
    • (2010) Arch. Biochem. Biophys. , vol.501 , pp. 239-243
    • Bandyopadhyay, K.1    Parua, P.K.2    Datta, A.B.3    Parrack, P.4
  • 8
    • 77957307926 scopus 로고    scopus 로고
    • The lambda spanin components Rz and Rz1 undergo tertiary and quaternary rearrangements upon complex formation
    • Berry J., Savva C., Holzenburg A., Young R. The lambda spanin components Rz and Rz1 undergo tertiary and quaternary rearrangements upon complex formation. Protein Sci. 2010, 19:1967-1977.
    • (2010) Protein Sci. , vol.19 , pp. 1967-1977
    • Berry, J.1    Savva, C.2    Holzenburg, A.3    Young, R.4
  • 9
    • 0022413842 scopus 로고
    • Transcriptional antitermination activity of the synthetic nut elements of coliphage lambda. I. Assembly of the nutR recognition site from boxA and nut core elements
    • Brown A.L., Szybalski W. Transcriptional antitermination activity of the synthetic nut elements of coliphage lambda. I. Assembly of the nutR recognition site from boxA and nut core elements. Gene 1985, 39:121-127.
    • (1985) Gene , vol.39 , pp. 121-127
    • Brown, A.L.1    Szybalski, W.2
  • 11
    • 75649100484 scopus 로고    scopus 로고
    • Fine tuning of the E. coli NusB:NusE complex affinity to BoxA RNA is required for processive antitermination
    • Burmann B.M., Luo X., Rösch P., Wahl M.C., Gottesman M.E. Fine tuning of the E. coli NusB:NusE complex affinity to BoxA RNA is required for processive antitermination. Nucleic Acids Res 2010, 38:314-326.
    • (2010) Nucleic Acids Res , vol.38 , pp. 314-326
    • Burmann, B.M.1    Luo, X.2    Rösch, P.3    Wahl, M.C.4    Gottesman, M.E.5
  • 12
    • 61849182998 scopus 로고    scopus 로고
    • Stochastic probability landscape model for switching efficiency, robustness, and differential threshold for induction of genetic circuit in phage
    • Cao Y., Lu H.M., Liang J. Stochastic probability landscape model for switching efficiency, robustness, and differential threshold for induction of genetic circuit in phage. Med. Biol. Soc. 2008, 611-614.
    • (2008) Med. Biol. Soc. , pp. 611-614
    • Cao, Y.1    Lu, H.M.2    Liang, J.3
  • 13
    • 78649871073 scopus 로고    scopus 로고
    • Probability landscape of heritable and robust epigenetic state of lysogeny in phage lambda
    • Cao Y., Lu H.M., Liang J. Probability landscape of heritable and robust epigenetic state of lysogeny in phage lambda. Proc. Natal. Acad. Sci. USA 2010, 107:18445-18450.
    • (2010) Proc. Natal. Acad. Sci. USA , vol.107 , pp. 18445-18450
    • Cao, Y.1    Lu, H.M.2    Liang, J.3
  • 14
    • 77954362019 scopus 로고    scopus 로고
    • DNA linking number change induced by sequence-specific DNA-binding proteins
    • Chen B., Xiao Y., Liu C., Li C., Leng F. DNA linking number change induced by sequence-specific DNA-binding proteins. Nucleic Acids Res. 2010, 38:3643-3654.
    • (2010) Nucleic Acids Res. , vol.38 , pp. 3643-3654
    • Chen, B.1    Xiao, Y.2    Liu, C.3    Li, C.4    Leng, F.5
  • 15
    • 48149104997 scopus 로고    scopus 로고
    • Complex regulation of the DnaJ homolog CbpA by the global regulators sigmaS and Lrp, by the specific inhibitor CbpM, and by the proteolytic degradation of CbpM
    • Chenoweth M.R., Wickner S. Complex regulation of the DnaJ homolog CbpA by the global regulators sigmaS and Lrp, by the specific inhibitor CbpM, and by the proteolytic degradation of CbpM. J. Bacteriol. 2008, 190:5153-5161.
    • (2008) J. Bacteriol. , vol.190 , pp. 5153-5161
    • Chenoweth, M.R.1    Wickner, S.2
  • 16
    • 54249128774 scopus 로고    scopus 로고
    • The antitermination activity of bacteriophage lambda N protein is controlled by the kinetics of an RNA-looping-facilitated interaction with the transcription complex
    • Conant C.R., Goodarzi J.P., Weitzel S.E., von Hippel P.H. The antitermination activity of bacteriophage lambda N protein is controlled by the kinetics of an RNA-looping-facilitated interaction with the transcription complex. J. Mol. Biol. 2008, 384:87-108.
    • (2008) J. Mol. Biol. , vol.384 , pp. 87-108
    • Conant, C.R.1    Goodarzi, J.P.2    Weitzel, S.E.3    von Hippel, P.H.4
  • 17
    • 18044396557 scopus 로고    scopus 로고
    • A quantitative description of the binding states and in vitro function of antitermination protein N of bacteriophage lambda
    • Conant C.R., Van Gilst M.R., Weitzel S.E., Rees W.A., von Hippel P.H. A quantitative description of the binding states and in vitro function of antitermination protein N of bacteriophage lambda. J. Mol. Biol. 2005, 348:1039-1057.
    • (2005) J. Mol. Biol. , vol.348 , pp. 1039-1057
    • Conant, C.R.1    Van Gilst, M.R.2    Weitzel, S.E.3    Rees, W.A.4    von Hippel, P.H.5
  • 18
    • 33846329120 scopus 로고    scopus 로고
    • A new look at bacteriophage lambda genetic networks
    • Court D.L., Oppenheim A.B., Adhya S.L. A new look at bacteriophage lambda genetic networks. J. Bacteriol. 2007, 189:298-304.
    • (2007) J. Bacteriol. , vol.189 , pp. 298-304
    • Court, D.L.1    Oppenheim, A.B.2    Adhya, S.L.3
  • 19
    • 34447290425 scopus 로고    scopus 로고
    • The crystal structure of lambda-Gam protein suggests a model for RecBCD inhibition
    • Court R., Cook N., Saikrishnan K., Wigley D. The crystal structure of lambda-Gam protein suggests a model for RecBCD inhibition. J. Mol. Biol. 2007, 371:25-33.
    • (2007) J. Mol. Biol. , vol.371 , pp. 25-33
    • Court, R.1    Cook, N.2    Saikrishnan, K.3    Wigley, D.4
  • 20
    • 23844445773 scopus 로고    scopus 로고
    • Structure of lambda CII: Implications for recognition of direct-repeat DNA by an unusual tetrameric organization
    • Datta A.B., Panjikar S., Weiss M.S., Chakrabarti P., Parrack P. Structure of lambda CII: Implications for recognition of direct-repeat DNA by an unusual tetrameric organization. Proc. Natl. Acad. Sci. USA 2005, 102:11242-11247.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 11242-11247
    • Datta, A.B.1    Panjikar, S.2    Weiss, M.S.3    Chakrabarti, P.4    Parrack, P.5
  • 21
    • 9644264006 scopus 로고    scopus 로고
    • Role of C-terminal residues in oligomerization and stability of lambda CII: Implications for lysis-lysogeny decision of the phage
    • Datta A.B., Roy S., Parrack P. Role of C-terminal residues in oligomerization and stability of lambda CII: Implications for lysis-lysogeny decision of the phage. J. Mol. Biol. 2005, 345:315-324.
    • (2005) J. Mol. Biol. , vol.345 , pp. 315-324
    • Datta, A.B.1    Roy, S.2    Parrack, P.3
  • 22
    • 21244502219 scopus 로고    scopus 로고
    • The mutation that makes Escherichia coli resistant to lambda P gene-mediated host lethality is located within the DNA initiator Gene dnaA of the bacterium
    • Datta I., Banik-Maiti S., Adhakari L., Sau S., Das N., Mandal N.C. The mutation that makes Escherichia coli resistant to lambda P gene-mediated host lethality is located within the DNA initiator Gene dnaA of the bacterium. J. Biochem. Mol. Biol. 2005, 38:89-96.
    • (2005) J. Biochem. Mol. Biol. , vol.38 , pp. 89-96
    • Datta, I.1    Banik-Maiti, S.2    Adhakari, L.3    Sau, S.4    Das, N.5    Mandal, N.C.6
  • 23
    • 21244454089 scopus 로고    scopus 로고
    • The bacteriophage lambda DNA replication protein P inhibits the oriC DNA- and ATP-binding functions of the DNA replication initiator protein DnaA of Eshcerichia coli
    • Datta I., Sau S., Sil A.K., Mandal N.C. The bacteriophage lambda DNA replication protein P inhibits the oriC DNA- and ATP-binding functions of the DNA replication initiator protein DnaA of Eshcerichia coli. J. Biochem. Mol. Biol. 2005, 38:97-103.
    • (2005) J. Biochem. Mol. Biol. , vol.38 , pp. 97-103
    • Datta, I.1    Sau, S.2    Sil, A.K.3    Mandal, N.C.4
  • 24
    • 33846260077 scopus 로고    scopus 로고
    • The bacteriophage lambdaQ anti-terminator protein regulates late gene expression as a stable component of the transcription elongation complex
    • Deighan P., Hochschild A. The bacteriophage lambdaQ anti-terminator protein regulates late gene expression as a stable component of the transcription elongation complex. Mol. Microbiol. 2007, 63:911-920.
    • (2007) Mol. Microbiol. , vol.63 , pp. 911-920
    • Deighan, P.1    Hochschild, A.2
  • 25
    • 55749096593 scopus 로고    scopus 로고
    • The bacteriophage lambda Q antiterminator protein contacts the beta-flap domain of RNA polymerase
    • Deighan P., Diez C.M., Leibman M., Hochschild A., Nickels B.E. The bacteriophage lambda Q antiterminator protein contacts the beta-flap domain of RNA polymerase. Proc. Natl. Acad. Sci. USA 2008, 105:15305-15310.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 15305-15310
    • Deighan, P.1    Diez, C.M.2    Leibman, M.3    Hochschild, A.4    Nickels, B.E.5
  • 28
    • 78649342032 scopus 로고    scopus 로고
    • The Escherichia coli CRISPR system protects from λ lysogenization, lysogens, and prophage induction
    • Edgar R., Qimron U. The Escherichia coli CRISPR system protects from λ lysogenization, lysogens, and prophage induction. J. Bacteriol. 2010, 192:6291-6294.
    • (2010) J. Bacteriol. , vol.192 , pp. 6291-6294
    • Edgar, R.1    Qimron, U.2
  • 29
    • 74249110550 scopus 로고    scopus 로고
    • DNA packaging by lambda-like bacteriophages: Mutations broadening the packaging specificity of terminase, the lambda-packaging enzyme
    • Feiss M., Reynolds E., Schrock M., Sippy J. DNA packaging by lambda-like bacteriophages: Mutations broadening the packaging specificity of terminase, the lambda-packaging enzyme. Genetics 2010, 184:43-52.
    • (2010) Genetics , vol.184 , pp. 43-52
    • Feiss, M.1    Reynolds, E.2    Schrock, M.3    Sippy, J.4
  • 30
    • 79953695956 scopus 로고    scopus 로고
    • Characterization of the relationship between integrase, excisionase and antirepressor activities associated with a superinfecting Shiga toxin encoding bacteriophage
    • Fogg P.C., Rigden D.J., Saunders J.R., McCarthy A.J., Allison H.E. Characterization of the relationship between integrase, excisionase and antirepressor activities associated with a superinfecting Shiga toxin encoding bacteriophage. Nucleic Acids Res. 2011, 39:2116-2129.
    • (2011) Nucleic Acids Res. , vol.39 , pp. 2116-2129
    • Fogg, P.C.1    Rigden, D.J.2    Saunders, J.R.3    McCarthy, A.J.4    Allison, H.E.5
  • 31
    • 0035072062 scopus 로고    scopus 로고
    • Bacteriophage lambda: Alive and well and still doing its thing
    • Friedman D.I., Court D.L. Bacteriophage lambda: Alive and well and still doing its thing. Curr. Opin. Microbiol. 2001, 4:201-207.
    • (2001) Curr. Opin. Microbiol. , vol.4 , pp. 201-207
    • Friedman, D.I.1    Court, D.L.2
  • 33
    • 43649092195 scopus 로고    scopus 로고
    • Binding cooperativity in phage lambda is not sufficient to produce an effective switch
    • Gedeon T., Mischaikow K., Patterson K., Traldi E. Binding cooperativity in phage lambda is not sufficient to produce an effective switch. Biophys. J. 2008, 94:3384-3392.
    • (2008) Biophys. J. , vol.94 , pp. 3384-3392
    • Gedeon, T.1    Mischaikow, K.2    Patterson, K.3    Traldi, E.4
  • 34
    • 70449412955 scopus 로고    scopus 로고
    • Acyl-homoserine lactones can induce virus production in lysogenic bacteria: An alternative paradigm for prophage induction
    • Ghosh D., Roy K., Williamson K.E., Srinivasiah S., Wommack K.E., Radosevich M. Acyl-homoserine lactones can induce virus production in lysogenic bacteria: An alternative paradigm for prophage induction. Appl. Environ. Microbiol. 2009, 75:7142-7152.
    • (2009) Appl. Environ. Microbiol. , vol.75 , pp. 7142-7152
    • Ghosh, D.1    Roy, K.2    Williamson, K.E.3    Srinivasiah, S.4    Wommack, K.E.5    Radosevich, M.6
  • 37
    • 77952541862 scopus 로고    scopus 로고
    • Rule-based simulation of temperate bacteriophage infection: Restriction-modification as a limiter to infection in bacterial populations
    • Gregory R., Saunders V.A., Saunders J.R. Rule-based simulation of temperate bacteriophage infection: Restriction-modification as a limiter to infection in bacterial populations. Biosystems 2010, 100:166-177.
    • (2010) Biosystems , vol.100 , pp. 166-177
    • Gregory, R.1    Saunders, V.A.2    Saunders, J.R.3
  • 38
    • 51749104418 scopus 로고    scopus 로고
    • Direct CIII-HflB interaction is responsible for the inhibition of the HflB (FtsH)-mediated proteolysis of Escherichia coli sigma(32) by lambda CIII
    • Halder S., Banerjee S., Parrack P. Direct CIII-HflB interaction is responsible for the inhibition of the HflB (FtsH)-mediated proteolysis of Escherichia coli sigma(32) by lambda CIII. FEBS J. 2008, 275:4767-4772.
    • (2008) FEBS J. , vol.275 , pp. 4767-4772
    • Halder, S.1    Banerjee, S.2    Parrack, P.3
  • 39
    • 36549080451 scopus 로고    scopus 로고
    • Probing the antiprotease activity of lambdaCIII, an inhibitor of the Escherichia coli metalloprotease HflB (FtsH)
    • Halder S., Datta A.B., Parrack P. Probing the antiprotease activity of lambdaCIII, an inhibitor of the Escherichia coli metalloprotease HflB (FtsH). J. Bacteriol. 2007, 189:8130-8138.
    • (2007) J. Bacteriol. , vol.189 , pp. 8130-8138
    • Halder, S.1    Datta, A.B.2    Parrack, P.3
  • 40
    • 0027236950 scopus 로고
    • Expression of the Rz gene and the overlapping Rz1 reading frame present at the right end of the bacteriophage lambda genome
    • Hanych B., Ke{ogonek}dzierska S., Walderich B., Uznański B., Taylor A. Expression of the Rz gene and the overlapping Rz1 reading frame present at the right end of the bacteriophage lambda genome. Gene 1993, 129:1-8.
    • (1993) Gene , vol.129 , pp. 1-8
    • Hanych, B.1    Kedzierska, S.2    Walderich, B.3    Uznański, B.4    Taylor, A.5
  • 41
    • 60349130270 scopus 로고    scopus 로고
    • The bacteriophage lambda CI protein finds an asymmetric solution
    • Hochschild A., Lewis M. The bacteriophage lambda CI protein finds an asymmetric solution. Curr. Opin. Struct. Biol. 2009, 19:79-86.
    • (2009) Curr. Opin. Struct. Biol. , vol.19 , pp. 79-86
    • Hochschild, A.1    Lewis, M.2
  • 42
    • 77952478241 scopus 로고    scopus 로고
    • Analysis of the spacial requirements for RNA-protein interactions within the N antitermination complex of bacteriophage lambda
    • Horiya S., Inaba M., Koh C.S., Uehara H., Masui N., Ishibashi M., Matsufuji S., Harada K. Analysis of the spacial requirements for RNA-protein interactions within the N antitermination complex of bacteriophage lambda. Nucleic Acids Symp. Ser. 2009, 53:91-92.
    • (2009) Nucleic Acids Symp. Ser. , vol.53 , pp. 91-92
    • Horiya, S.1    Inaba, M.2    Koh, C.S.3    Uehara, H.4    Masui, N.5    Ishibashi, M.6    Matsufuji, S.7    Harada, K.8
  • 43
    • 21744443969 scopus 로고    scopus 로고
    • Slow assembly and disassembly of lambda Cro repressor dimers
    • Jia H., Satumba W.J., Bidwell G.L., Mossing M.C. Slow assembly and disassembly of lambda Cro repressor dimers. J. Mol. Biol. 2005, 350:919-929.
    • (2005) J. Mol. Biol. , vol.350 , pp. 919-929
    • Jia, H.1    Satumba, W.J.2    Bidwell, G.L.3    Mossing, M.C.4
  • 44
    • 0041885344 scopus 로고    scopus 로고
    • Toxicity of the bacteriophage lambda cII gene product to Escherichia coli arises from inhibition of host cell DNA replication
    • Ke{ogonek}dzierska B., Glinkowska M., Iwanicki A., Obuchowski M., Sojka P., Thomas M.S., We{ogonek}grzyn G. Toxicity of the bacteriophage lambda cII gene product to Escherichia coli arises from inhibition of host cell DNA replication. Virology 2003, 313:622-628.
    • (2003) Virology , vol.313 , pp. 622-628
    • Kedzierska, B.1    Glinkowska, M.2    Iwanicki, A.3    Obuchowski, M.4    Sojka, P.5    Thomas, M.S.6    Wegrzyn, G.7
  • 45
    • 1342327607 scopus 로고    scopus 로고
    • Role of the RNA polymerase alpha subunits in CII-dependent activation of the bacteriophage lambda pE promoter: Identification of important residues and positioning of the alpha C-terminal domains
    • Ke{ogonek}dzierska B., Lee D.J., We{ogonek}grzyn G., Busby S.J., Thomas M.S. Role of the RNA polymerase alpha subunits in CII-dependent activation of the bacteriophage lambda pE promoter: Identification of important residues and positioning of the alpha C-terminal domains. Nucleic Acids Res. 2004, 32:834-841.
    • (2004) Nucleic Acids Res. , vol.32 , pp. 834-841
    • Kedzierska, B.1    Lee, D.J.2    Wegrzyn, G.3    Busby, S.J.4    Thomas, M.S.5
  • 46
    • 34249862579 scopus 로고    scopus 로고
    • The C-terminal domain of the Escherichia coli RNA polymerase alpha subunit plays a role in the CI-dependent activation of the bacteriophage lambda pM promoter
    • Ke{ogonek}dzierska B., Szambowska A., Herman-Antosiewicz A., Lee D.J., Busby S.J., We{ogonek}grzyn G., Thomas M.S. The C-terminal domain of the Escherichia coli RNA polymerase alpha subunit plays a role in the CI-dependent activation of the bacteriophage lambda pM promoter. Nucleic Acids Res. 2007, 35:2311-2320.
    • (2007) Nucleic Acids Res. , vol.35 , pp. 2311-2320
    • Kedzierska, B.1    Szambowska, A.2    Herman-Antosiewicz, A.3    Lee, D.J.4    Busby, S.J.5    Wegrzyn, G.6    Thomas, M.S.7
  • 48
    • 34547929879 scopus 로고    scopus 로고
    • Phage lambda CIII: A protease inhibitor regulating the lysis-lysogeny decision
    • Kobiler O., Rokney A., Oppenheim A.B. Phage lambda CIII: A protease inhibitor regulating the lysis-lysogeny decision. PLoS One 2007, 2:e363.
    • (2007) PLoS One , vol.2
    • Kobiler, O.1    Rokney, A.2    Oppenheim, A.B.3
  • 49
    • 33144477944 scopus 로고    scopus 로고
    • Solute probes of conformational changes in open complex (RPo) formation by Escherichia coli RNA polymerase at the lambdaPR promoter: Evidence for unmasking of the active site in the isomerization step and for large-scale coupled folding in the subsequent conversion to RPo
    • Kontur W.S., Saecker R.M., Davis C.A., Capp M.W., Record M.T. Solute probes of conformational changes in open complex (RPo) formation by Escherichia coli RNA polymerase at the lambdaPR promoter: Evidence for unmasking of the active site in the isomerization step and for large-scale coupled folding in the subsequent conversion to RPo. Biochemistry 2006, 45:2161-2177.
    • (2006) Biochemistry , vol.45 , pp. 2161-2177
    • Kontur, W.S.1    Saecker, R.M.2    Davis, C.A.3    Capp, M.W.4    Record, M.T.5
  • 50
    • 70349928561 scopus 로고    scopus 로고
    • Influence of internal capsid pressure on viral infection by phage lambda
    • Köster S., Evilevitch A., Jeembaeva M., Weitz D.A. Influence of internal capsid pressure on viral infection by phage lambda. Biophys. J. 2009, 97:1525-1529.
    • (2009) Biophys. J. , vol.97 , pp. 1525-1529
    • Köster, S.1    Evilevitch, A.2    Jeembaeva, M.3    Weitz, D.A.4
  • 51
    • 47749126576 scopus 로고    scopus 로고
    • Holin of bacteriophage lambda: Structural insights into a membrane lesion
    • Krupovic M., Bamford D.H. Holin of bacteriophage lambda: Structural insights into a membrane lesion. Mol. Microbiol. 2008, 69:781-783.
    • (2008) Mol. Microbiol. , vol.69 , pp. 781-783
    • Krupovic, M.1    Bamford, D.H.2
  • 52
    • 80355140848 scopus 로고    scopus 로고
    • Direct observation of enzymes replicating DNA using a single-molecule DNA stretching assay
    • Kulczyk A.W., Tanner N.A., Loparo J.J., Richardson C.C., van Oijen A.M. Direct observation of enzymes replicating DNA using a single-molecule DNA stretching assay. J. Vis. Exp. 2010, 37:1689.
    • (2010) J. Vis. Exp. , vol.37 , pp. 1689
    • Kulczyk, A.W.1    Tanner, N.A.2    Loparo, J.J.3    Richardson, C.C.4    van Oijen, A.M.5
  • 53
    • 77956545119 scopus 로고    scopus 로고
    • Evolution of complex gene regulatory circuits by addition of refinements
    • Little J.W. Evolution of complex gene regulatory circuits by addition of refinements. Curr. Biol. 2010, 20:R724-R734.
    • (2010) Curr. Biol. , vol.20
    • Little, J.W.1
  • 54
    • 78049435111 scopus 로고    scopus 로고
    • Stability and instability in the lysogenic state of phage lambda
    • Little J.W., Michalowski C.B. Stability and instability in the lysogenic state of phage lambda. J. Bacteriol. 2010, 192:6064-6076.
    • (2010) J. Bacteriol. , vol.192 , pp. 6064-6076
    • Little, J.W.1    Michalowski, C.B.2
  • 55
    • 34147185608 scopus 로고    scopus 로고
    • A quantitative study of lambda-phage SWITCH and its components
    • Lou C., Yang X., Liu X., He B., Ouyang Q. A quantitative study of lambda-phage SWITCH and its components. Biophys. J. 2007, 92:2685-2693.
    • (2007) Biophys. J. , vol.92 , pp. 2685-2693
    • Lou, C.1    Yang, X.2    Liu, X.3    He, B.4    Ouyang, Q.5
  • 56
    • 57649232814 scopus 로고    scopus 로고
    • Role of the bacteriophage lambda exo-xis region in the virus development
    • ŁoŚ J.M., ŁoŚ M., We{ogonek}grzyn A., We{ogonek}grzyn G. Role of the bacteriophage lambda exo-xis region in the virus development. Folia Microbiol. 2008, 53:443-450.
    • (2008) Folia Microbiol. , vol.53 , pp. 443-450
    • ŁoŚ, J.M.1    ŁoŚ, M.2    Wegrzyn, A.3    Wegrzyn, G.4
  • 57
    • 71249101533 scopus 로고    scopus 로고
    • Differential efficiency of induction of various lambdoid prophages responsible for production of Shiga toxins in response to different induction agents
    • Łoś J.M., ŁoŚ M., We{ogonek}grzyn G., We{ogonek}grzyn A. Differential efficiency of induction of various lambdoid prophages responsible for production of Shiga toxins in response to different induction agents. Microb. Pathog. 2009, 47:289-298.
    • (2009) Microb. Pathog. , vol.47 , pp. 289-298
    • Łoś, J.M.1    ŁoŚ, M.2    Wegrzyn, G.3    Wegrzyn, A.4
  • 58
    • 77949417099 scopus 로고    scopus 로고
    • Hydrogen peroxide-mediated induction of the Shiga toxin-converting lambdoid prophage ST2-8624 in Escherichia coli O157:H7
    • Łoś J.M., Łoś M., We{ogonek}grzyn A., We{ogonek}grzyn G. Hydrogen peroxide-mediated induction of the Shiga toxin-converting lambdoid prophage ST2-8624 in Escherichia coli O157:H7. FEMS Immunol. Med. Microbiol. 2010, 58:322-329.
    • (2010) FEMS Immunol. Med. Microbiol. , vol.58 , pp. 322-329
    • Łoś, J.M.1    Łoś, M.2    Wegrzyn, A.3    Wegrzyn, G.4
  • 59
    • 49949096474 scopus 로고    scopus 로고
    • IHF- and SeqA-binding sites, present in plasmid cloning vectors, may significantly influence activities of promoters
    • Łyżeń R., Kochanowska M., We{ogonek}grzyn G., Szalewska-Pałasz A. IHF- and SeqA-binding sites, present in plasmid cloning vectors, may significantly influence activities of promoters. Plasmid 2008, 60:125-130.
    • (2008) Plasmid , vol.60 , pp. 125-130
    • Łyzeń, R.1    Kochanowska, M.2    Wegrzyn, G.3    Szalewska-Pałasz, A.4
  • 60
    • 73349100378 scopus 로고    scopus 로고
    • Transcription from bacteriophage lambda pR promoter is regulated independently and antagonistically by DksA and ppGpp
    • Łyżeń R., Kochanowska M., We{ogonek}grzyn G., Szalewska-Palasz A. Transcription from bacteriophage lambda pR promoter is regulated independently and antagonistically by DksA and ppGpp. Nucleic Acids Res. 2009, 37:6655-6664.
    • (2009) Nucleic Acids Res. , vol.37 , pp. 6655-6664
    • Łyzeń, R.1    Kochanowska, M.2    Wegrzyn, G.3    Szalewska-Palasz, A.4
  • 61
    • 33749643554 scopus 로고    scopus 로고
    • Stimulation of the lambda pR promoter by Escherichia coli SeqA protein requires downstream GATC sequences and involves late stages of transcription initiation
    • Łyżeń R., We{ogonek}grzyn G., We{ogonek}grzyn A., Szalewska-Pałasz A. Stimulation of the lambda pR promoter by Escherichia coli SeqA protein requires downstream GATC sequences and involves late stages of transcription initiation. Microbiology 2006, 152:2985-2992.
    • (2006) Microbiology , vol.152 , pp. 2985-2992
    • Łyzeń, R.1    Wegrzyn, G.2    Wegrzyn, A.3    Szalewska-Pałasz, A.4
  • 62
    • 77955488715 scopus 로고    scopus 로고
    • Single-stranded heteroduplex intermediates in lambda Red homologous recombination
    • Maresca M., Erler A., Fu J., Friedrich A., Zhang Y., Stewart A.F. Single-stranded heteroduplex intermediates in lambda Red homologous recombination. BMC Mol. Biol. 2010, 11:54.
    • (2010) BMC Mol. Biol. , vol.11 , pp. 54
    • Maresca, M.1    Erler, A.2    Fu, J.3    Friedrich, A.4    Zhang, Y.5    Stewart, A.F.6
  • 64
    • 77957376210 scopus 로고    scopus 로고
    • A forward-genetic screen and dynamic analysis of lambda phage host-dependencies reveals an extensive interaction network and a new anti-viral strategy
    • Maynard N.D., Birch E.W., Sanghvi J.C., Chen L., Gutschow M.V., Covert M.W. A forward-genetic screen and dynamic analysis of lambda phage host-dependencies reveals an extensive interaction network and a new anti-viral strategy. PLoS Genet. 2010, 6:e1001017.
    • (2010) PLoS Genet. , vol.6
    • Maynard, N.D.1    Birch, E.W.2    Sanghvi, J.C.3    Chen, L.4    Gutschow, M.V.5    Covert, M.W.6
  • 65
    • 77955551129 scopus 로고    scopus 로고
    • Assembly and maturation of the bacteriophage lambda procapsid: gpC is the viral protease
    • Medina E., Wieczorek D., Medina E.M., Yang Q., Feiss M., Catalano C.E. Assembly and maturation of the bacteriophage lambda procapsid: gpC is the viral protease. J. Mol. Biol. 2010, 401:813-830.
    • (2010) J. Mol. Biol. , vol.401 , pp. 813-830
    • Medina, E.1    Wieczorek, D.2    Medina, E.M.3    Yang, Q.4    Feiss, M.5    Catalano, C.E.6
  • 66
    • 66249124272 scopus 로고    scopus 로고
    • DNA looping provides stability and robustness to the bacteriophage lambda switch
    • Morelli M.J., Ten Wolde P.R., Allen R.J. DNA looping provides stability and robustness to the bacteriophage lambda switch. Proc. Natl. Acad. Sci. USA 2009, 106:8101-8106.
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 8101-8106
    • Morelli, M.J.1    Ten Wolde, P.R.2    Allen, R.J.3
  • 67
    • 78951480559 scopus 로고    scopus 로고
    • Lambda Red recombineering in Escherichia coli occurs through a fully single-stranded intermediate
    • Mosberg J.A., Lajoie M.J., Church G.M. Lambda Red recombineering in Escherichia coli occurs through a fully single-stranded intermediate. Genetics 2010, 186:791-799.
    • (2010) Genetics , vol.186 , pp. 791-799
    • Mosberg, J.A.1    Lajoie, M.J.2    Church, G.M.3
  • 68
    • 34249005369 scopus 로고    scopus 로고
    • Modulation of lambda plasmid and phage DNA replication by Escherichia coli SeqA protein
    • Narajczyk M., Barańska S., Szambowska A., Glinkowska M., We{ogonek}grzyn A., We{ogonek}grzyn G. Modulation of lambda plasmid and phage DNA replication by Escherichia coli SeqA protein. Microbiology 2007, 153:1653-1663.
    • (2007) Microbiology , vol.153 , pp. 1653-1663
    • Narajczyk, M.1    Barańska, S.2    Szambowska, A.3    Glinkowska, M.4    Wegrzyn, A.5    Wegrzyn, G.6
  • 69
    • 34250313233 scopus 로고    scopus 로고
    • Switch from theta to sigma replication of bacteriophage lambda DNA: Factors involved in process and a model for its regulation
    • Narajczyk M., Barańska S., We{ogonek}grzyn A., We{ogonek}grzyn G. Switch from theta to sigma replication of bacteriophage lambda DNA: Factors involved in process and a model for its regulation. Mol. Genet. Genomics 2007, 278:65-74.
    • (2007) Mol. Genet. Genomics , vol.278 , pp. 65-74
    • Narajczyk, M.1    Barańska, S.2    Wegrzyn, A.3    Wegrzyn, G.4
  • 70
    • 70349594185 scopus 로고    scopus 로고
    • Plasmids derived from lambdoid bacteriophages as models for studying replication of mobile genetic elements responsible for the production of Shiga toxins by pathogenic Escherichia coli strains
    • Nejman B., Łoś J.M., Łoś M., We{ogonek}grzyn G., We{ogonek}grzyn A. Plasmids derived from lambdoid bacteriophages as models for studying replication of mobile genetic elements responsible for the production of Shiga toxins by pathogenic Escherichia coli strains. J. Mol. Microbiol. Biotechnol. 2009, 17:211-220.
    • (2009) J. Mol. Microbiol. Biotechnol. , vol.17 , pp. 211-220
    • Nejman, B.1    Łoś, J.M.2    Łoś, M.3    Wegrzyn, G.4    Wegrzyn, A.5
  • 71
    • 78650798383 scopus 로고    scopus 로고
    • Replication of plasmids derived from Shiga toxin-converting bacteriophages in starved Escherichia coli
    • Nejman B., Nadratowska-Wesołowska B., Szalewska-Pałasz A., We{ogonek}grzyn A., We{ogonek}grzyn G. Replication of plasmids derived from Shiga toxin-converting bacteriophages in starved Escherichia coli. Microbiology 2011, 157:220-233.
    • (2011) Microbiology , vol.157 , pp. 220-233
    • Nejman, B.1    Nadratowska-Wesołowska, B.2    Szalewska-Pałasz, A.3    Wegrzyn, A.4    Wegrzyn, G.5
  • 72
    • 33750493565 scopus 로고    scopus 로고
    • RNA-mediated destabilization of the sigma(70) region 4/beta flap interaction facilitates engagement of RNA polymerase by the Q antiterminator
    • Nickels B.E., Roberts C.W., Roberts J.W., Hochschild A. RNA-mediated destabilization of the sigma(70) region 4/beta flap interaction facilitates engagement of RNA polymerase by the Q antiterminator. Mol. Cell 2006, 24:457-468.
    • (2006) Mol. Cell , vol.24 , pp. 457-468
    • Nickels, B.E.1    Roberts, C.W.2    Roberts, J.W.3    Hochschild, A.4
  • 74
    • 33847128325 scopus 로고    scopus 로고
    • Fis targets assembly of the Xis nucleoprotein filament to promote excisive recombination by phage lambda
    • Papagiannis C.V., Sam M.D., Abbani M.A., Yoo D., Cascio D., Clubb R.T., Johnson R.C. Fis targets assembly of the Xis nucleoprotein filament to promote excisive recombination by phage lambda. J. Mol. Biol. 2007, 367:328-343.
    • (2007) J. Mol. Biol. , vol.367 , pp. 328-343
    • Papagiannis, C.V.1    Sam, M.D.2    Abbani, M.A.3    Yoo, D.4    Cascio, D.5    Clubb, R.T.6    Johnson, R.C.7
  • 75
    • 73149094712 scopus 로고    scopus 로고
    • Specific hydrophobic residues in the alpha4 helix of lambda CII are crucial for maintaining its tetrameric structure and directing the lysogenic choice
    • Parua P.K., Datta A.B., Parrack P. Specific hydrophobic residues in the alpha4 helix of lambda CII are crucial for maintaining its tetrameric structure and directing the lysogenic choice. J. Gen. Virol. 2010, 91:306-312.
    • (2010) J. Gen. Virol. , vol.91 , pp. 306-312
    • Parua, P.K.1    Datta, A.B.2    Parrack, P.3
  • 76
    • 73149107446 scopus 로고    scopus 로고
    • HflD, an Escherichia coli protein involved in the lambda lysis-lysogeny switch, impairs transcription activation by lambda CII
    • Parua P.K., Mondal A., Parrack P. HflD, an Escherichia coli protein involved in the lambda lysis-lysogeny switch, impairs transcription activation by lambda CII. Arch. Biochem. Biophys. 2010, 493:175-183.
    • (2010) Arch. Biochem. Biophys. , vol.493 , pp. 175-183
    • Parua, P.K.1    Mondal, A.2    Parrack, P.3
  • 77
    • 40549083336 scopus 로고    scopus 로고
    • Involvement of DNA replication in phage lambda Red-mediated homologous recombination
    • Poteete A.R. Involvement of DNA replication in phage lambda Red-mediated homologous recombination. Mol. Microbiol. 2008, 68:66-74.
    • (2008) Mol. Microbiol. , vol.68 , pp. 66-74
    • Poteete, A.R.1
  • 78
    • 2442550836 scopus 로고    scopus 로고
    • Direct stimulation of the lambdapaQ promoter by the transcription effector guanosine-3',5'-(bis)pyrophosphate in a defined in vitro system
    • Potrykus K., We{ogonek}grzyn G., Hernandez V.J. Direct stimulation of the lambdapaQ promoter by the transcription effector guanosine-3',5'-(bis)pyrophosphate in a defined in vitro system. J. Biol. Chem. 2004, 279:19860-19866.
    • (2004) J. Biol. Chem. , vol.279 , pp. 19860-19866
    • Potrykus, K.1    Wegrzyn, G.2    Hernandez, V.J.3
  • 80
    • 33645653047 scopus 로고    scopus 로고
    • Interaction of the intrinsically unstructured phage lambda N protein with Escherichia coli NusA
    • Prasch S., Schwarz S., Eisenmann A., Wöhrl B.M., Schweimer K., Rösch P. Interaction of the intrinsically unstructured phage lambda N protein with Escherichia coli NusA. Biochemistry 2006, 45:4542-4549.
    • (2006) Biochemistry , vol.45 , pp. 4542-4549
    • Prasch, S.1    Schwarz, S.2    Eisenmann, A.3    Wöhrl, B.M.4    Schweimer, K.5    Rösch, P.6
  • 81
    • 20444382737 scopus 로고    scopus 로고
    • Regulation of transcription: From lambda to eukaryotes
    • Ptashne M. Regulation of transcription: From lambda to eukaryotes. Trends Biochem. Sci. 2005, 30:275-279.
    • (2005) Trends Biochem. Sci. , vol.30 , pp. 275-279
    • Ptashne, M.1
  • 82
    • 33744984357 scopus 로고    scopus 로고
    • Lambda's switch: Lessons from a module swap
    • Ptashne M. Lambda's switch: Lessons from a module swap. Curr. Biol. 2006, 16:R459-R462.
    • (2006) Curr. Biol. , vol.16
    • Ptashne, M.1
  • 83
    • 77954968376 scopus 로고    scopus 로고
    • Tuning a genetic switch: Experimental evolution and natural variation of prophage induction
    • Refardt D., Rainey P.B. Tuning a genetic switch: Experimental evolution and natural variation of prophage induction. Evolution 2010, 64:1086-1097.
    • (2010) Evolution , vol.64 , pp. 1086-1097
    • Refardt, D.1    Rainey, P.B.2
  • 86
    • 34948874664 scopus 로고    scopus 로고
    • Cro's role in the CI Cro bistable switch is critical for λ's transition from lysogeny to lytic development
    • Schubert R.A., Dodd I.B., Egan J.B., Shearwin K.E. Cro's role in the CI Cro bistable switch is critical for λ's transition from lysogeny to lytic development. Genes Dev. 2007, 21:2461-2472.
    • (2007) Genes Dev. , vol.21 , pp. 2461-2472
    • Schubert, R.A.1    Dodd, I.B.2    Egan, J.B.3    Shearwin, K.E.4
  • 87
    • 67650284139 scopus 로고    scopus 로고
    • Effect of late promoter activity on bacteriophage lambda fitness
    • Shao Y., Wang I.N. Effect of late promoter activity on bacteriophage lambda fitness. Genetics 2009, 181:1467-7145.
    • (2009) Genetics , vol.181 , pp. 1467-7145
    • Shao, Y.1    Wang, I.N.2
  • 89
    • 42549086222 scopus 로고    scopus 로고
    • Crystal structure of the lambda repressor and a model for pairwise cooperative operator binding
    • Stayrook S., Jaru-Ampornpan P., Ni J., Hochschild A., Lewis M. Crystal structure of the lambda repressor and a model for pairwise cooperative operator binding. Nature 2008, 452:1022-1025.
    • (2008) Nature , vol.452 , pp. 1022-1025
    • Stayrook, S.1    Jaru-Ampornpan, P.2    Ni, J.3    Hochschild, A.4    Lewis, M.5
  • 90
    • 33751010184 scopus 로고    scopus 로고
    • Architecture of the 99 bp DNA-six-protein regulatory complex of the lambda att site
    • Sun X., Mierke D.F., Biswas T., Lee S.Y., Landy A., Radman-Livaja M. Architecture of the 99 bp DNA-six-protein regulatory complex of the lambda att site. Mol. Cell. 2006, 24:569-580.
    • (2006) Mol. Cell. , vol.24 , pp. 569-580
    • Sun, X.1    Mierke, D.F.2    Biswas, T.3    Lee, S.Y.4    Landy, A.5    Radman-Livaja, M.6
  • 92
    • 78651340722 scopus 로고    scopus 로고
    • Coupling of transcription and replication machineries in λ DNA replication initiation: Evidence for direct interaction of Escherichia coli RNA polymerase and λO protein
    • Szambowska A., Pierechod M., We{ogonek}grzyn G., Glinkowska M. Coupling of transcription and replication machineries in λ DNA replication initiation: Evidence for direct interaction of Escherichia coli RNA polymerase and λO protein. Nucleic Acids Res. 2011, 39:168-177.
    • (2011) Nucleic Acids Res. , vol.39 , pp. 168-177
    • Szambowska, A.1    Pierechod, M.2    Wegrzyn, G.3    Glinkowska, M.4
  • 93
    • 77951182287 scopus 로고    scopus 로고
    • Selection of bacteriophage lambda integrases with altered recombination specificity by in vitro compartmentalization
    • Tay Y., Ho C., Droge P., Ghadessy F.J. Selection of bacteriophage lambda integrases with altered recombination specificity by in vitro compartmentalization. Nucleic Acids Res. 2010, 38:e25.
    • (2010) Nucleic Acids Res. , vol.38
    • Tay, Y.1    Ho, C.2    Droge, P.3    Ghadessy, F.J.4
  • 94
    • 0021070654 scopus 로고
    • Location of the Rz gene in bacteriophage lambda
    • Taylor A., Benedik M., Campbell A. Location of the Rz gene in bacteriophage lambda. Gene 1983, 26:159-163.
    • (1983) Gene , vol.26 , pp. 159-163
    • Taylor, A.1    Benedik, M.2    Campbell, A.3
  • 96
    • 77951237154 scopus 로고    scopus 로고
    • Production of recombinant proteins in E. coli by the heat inducible expression system based on the phage lambda pL and/or pR promoters
    • Valdez-Cruz N.A., Caspeta L., Pérez N.O., Ramirez O.T., Trujillo-Roldán M.A. Production of recombinant proteins in E. coli by the heat inducible expression system based on the phage lambda pL and/or pR promoters. Microb. Cell Fact 2010, 9:18.
    • (2010) Microb. Cell Fact , vol.9 , pp. 18
    • Valdez-Cruz, N.A.1    Caspeta, L.2    Pérez, N.O.3    Ramirez, O.T.4    Trujillo-Roldán, M.A.5
  • 97
    • 24044498937 scopus 로고    scopus 로고
    • Lambda integrase: Armed for recombination
    • Van Duyne G.D. Lambda integrase: Armed for recombination. Curr. Biol. 2005, 15:R658-R660.
    • (2005) Curr. Biol. , vol.15
    • Van Duyne, G.D.1
  • 98
    • 70350455297 scopus 로고    scopus 로고
    • AFM studies of lambda repressor oligomers securing DNA loops
    • Wang H., Finzi L., Lewis D.E., Dunlap D. AFM studies of lambda repressor oligomers securing DNA loops. Curr. Pharm. Biotechnol. 2009, 10:494-501.
    • (2009) Curr. Pharm. Biotechnol. , vol.10 , pp. 494-501
    • Wang, H.1    Finzi, L.2    Lewis, D.E.3    Dunlap, D.4
  • 99
    • 33645463597 scopus 로고    scopus 로고
    • Bacteriophage replication modules
    • Weigel C., Seitz H. Bacteriophage replication modules. FEMS Microbiol. Rev. 2006, 30:321-381.
    • (2006) FEMS Microbiol. Rev. , vol.30 , pp. 321-381
    • Weigel, C.1    Seitz, H.2
  • 100
    • 23944469082 scopus 로고    scopus 로고
    • Genetic switches during bacteriophage lambda development
    • We{ogonek}grzyn G., We{ogonek}grzyn A. Genetic switches during bacteriophage lambda development. Prog. Nucleic Acid Res. Mol. Biol. 2005, 79:1-48.
    • (2005) Prog. Nucleic Acid Res. Mol. Biol. , vol.79 , pp. 1-48
    • Wegrzyn, G.1    Wegrzyn, A.2
  • 103
    • 77958192416 scopus 로고    scopus 로고
    • Ion-dependent dynamics of DNA ejections for bacteriophage lambda
    • Wu D., Van Valen D., Hu Q., Phillips R. Ion-dependent dynamics of DNA ejections for bacteriophage lambda. Biophys. J. 2010, 99:1101-1109.
    • (2010) Biophys. J. , vol.99 , pp. 1101-1109
    • Wu, D.1    Van Valen, D.2    Hu, Q.3    Phillips, R.4
  • 104
    • 70449584723 scopus 로고    scopus 로고
    • Kinetic analysis of the genome packaging reaction in bacteriophage lambda
    • Yang Q., Catalano C.E., Maluf N.K. Kinetic analysis of the genome packaging reaction in bacteriophage lambda. Biochemistry 2009, 48:10705-10715.
    • (2009) Biochemistry , vol.48 , pp. 10705-10715
    • Yang, Q.1    Catalano, C.E.2    Maluf, N.K.3
  • 105
    • 79955677906 scopus 로고    scopus 로고
    • Probing the viral metallome: Searching for metalloproteins in bacteriophage λ: The hunt begins
    • Zhang Y., Thompson R., Caruso J. Probing the viral metallome: Searching for metalloproteins in bacteriophage λ: The hunt begins. Metallomics 2011, 3:472-481.
    • (2011) Metallomics , vol.3 , pp. 472-481
    • Zhang, Y.1    Thompson, R.2    Caruso, J.3
  • 106
  • 107
    • 78649838304 scopus 로고    scopus 로고
    • Lysogen stability is determined by the frequency of activity bursts from the fate-determining gene
    • Zong C., So L.H., Sepúlveda L.A., Skinner S.O., Golding I. Lysogen stability is determined by the frequency of activity bursts from the fate-determining gene. Mol. Syst. Biol. 2010, 6:440.
    • (2010) Mol. Syst. Biol. , vol.6 , pp. 440
    • Zong, C.1    So, L.H.2    Sepúlveda, L.A.3    Skinner, S.O.4    Golding, I.5


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