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Volumn 402, Issue 4, 2010, Pages 731-740

Visualizing the Structural Changes of Bacteriophage Epsilon15 and Its Salmonella Host during Infection

Author keywords

Cryotomography; Electron; Infection; Salmonella; Virus

Indexed keywords

CELL RECEPTOR; DOUBLE STRANDED DNA; NUCLEASE; VIRUS DNA;

EID: 77956892290     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2010.07.058     Document Type: Article
Times cited : (52)

References (69)
  • 1
    • 0642312312 scopus 로고    scopus 로고
    • The source of laterally transferred genes in bacterial genomes
    • Daubin V., Lerat E., Perrière G. The source of laterally transferred genes in bacterial genomes. Genome Biol. 2003, 4:R57.
    • (2003) Genome Biol. , vol.4
    • Daubin, V.1    Lerat, E.2    Perrière, G.3
  • 2
    • 0014095550 scopus 로고
    • The infection of Escherichia coli by T2 and T4 bacteriophages as seen in the electron microscope. I. Attachment and penetration
    • Simon L.D., Anderson T.F. The infection of Escherichia coli by T2 and T4 bacteriophages as seen in the electron microscope. I. Attachment and penetration. Virology 1967, 32:279-297.
    • (1967) Virology , vol.32 , pp. 279-297
    • Simon, L.D.1    Anderson, T.F.2
  • 3
    • 0014098795 scopus 로고
    • The infection of Escherichia coli by T2 and T4 bacteriophages as seen in the electron microscope. II. Structure and function of the baseplate
    • Simon L.D., Anderson T.F. The infection of Escherichia coli by T2 and T4 bacteriophages as seen in the electron microscope. II. Structure and function of the baseplate. Virology 1967, 32:298-305.
    • (1967) Virology , vol.32 , pp. 298-305
    • Simon, L.D.1    Anderson, T.F.2
  • 4
    • 0014532446 scopus 로고
    • The infection of Escherichia coli by T2 and T4 bacteriophages as seen in the electron microscope. 3. Membrane-associated intracellular bacteriophages
    • Simon L.D. The infection of Escherichia coli by T2 and T4 bacteriophages as seen in the electron microscope. 3. Membrane-associated intracellular bacteriophages. Virology 1969, 38:285-296.
    • (1969) Virology , vol.38 , pp. 285-296
    • Simon, L.D.1
  • 5
    • 0015329979 scopus 로고
    • Infection of Escherichia coli by T2 and T4 bacteriophages as seen in the electron microscope: T4 head morphogenesis
    • Simon L.D. Infection of Escherichia coli by T2 and T4 bacteriophages as seen in the electron microscope: T4 head morphogenesis. Proc. Natl Acad. Sci. USA 1972, 69:907-911.
    • (1972) Proc. Natl Acad. Sci. USA , vol.69 , pp. 907-911
    • Simon, L.D.1
  • 7
    • 66749084492 scopus 로고    scopus 로고
    • The structure of gene product 6 of bacteriophage T4, the hinge-pin of the baseplate
    • Aksyuk A.A., Leiman P.G., Shneider M.M., Mesyanzhinov V.V., Rossmann M.G. The structure of gene product 6 of bacteriophage T4, the hinge-pin of the baseplate. Structure 2009, 17:800-808.
    • (2009) Structure , vol.17 , pp. 800-808
    • Aksyuk, A.A.1    Leiman, P.G.2    Shneider, M.M.3    Mesyanzhinov, V.V.4    Rossmann, M.G.5
  • 8
    • 4644242580 scopus 로고    scopus 로고
    • Three-dimensional rearrangement of proteins in the tail of bacteriophage T4 on infection of its host
    • Leiman P.G., Chipman P.R., Kostyuchenko V.A., Mesyanzhinov V.V., Rossmann M.G. Three-dimensional rearrangement of proteins in the tail of bacteriophage T4 on infection of its host. Cell 2004, 118:419-429.
    • (2004) Cell , vol.118 , pp. 419-429
    • Leiman, P.G.1    Chipman, P.R.2    Kostyuchenko, V.A.3    Mesyanzhinov, V.V.4    Rossmann, M.G.5
  • 10
    • 33644505795 scopus 로고    scopus 로고
    • Interaction of bacteriophage lambda with its cell surface receptor: an in vitro study of binding of the viral tail protein gpJ to LamB (Maltoporin)
    • Berkane E., Orlik F., Stegmeier J.F., Charbit A., Winterhalter M., Benz R. Interaction of bacteriophage lambda with its cell surface receptor: an in vitro study of binding of the viral tail protein gpJ to LamB (Maltoporin). Biochemistry 2006, 45:2708-2720.
    • (2006) Biochemistry , vol.45 , pp. 2708-2720
    • Berkane, E.1    Orlik, F.2    Stegmeier, J.F.3    Charbit, A.4    Winterhalter, M.5    Benz, R.6
  • 11
    • 0022621195 scopus 로고
    • Formation of transmembrane channels in liposomes during injection of lambda DNA
    • Roessner C.A., Ihler G.M. Formation of transmembrane channels in liposomes during injection of lambda DNA. J. Biol. Chem. 1986, 261:386-390.
    • (1986) J. Biol. Chem. , vol.261 , pp. 386-390
    • Roessner, C.A.1    Ihler, G.M.2
  • 15
    • 0024292372 scopus 로고
    • Molecular substructure of a viral receptor-recognition protein. The gp17 tail-fiber of bacteriophage T7
    • Steven A.C., Trus B.L., Maizel J.V., Unser M., Parry D.A., Wall J.S., et al. Molecular substructure of a viral receptor-recognition protein. The gp17 tail-fiber of bacteriophage T7. J. Mol. Biol. 1988, 200:351-365.
    • (1988) J. Mol. Biol. , vol.200 , pp. 351-365
    • Steven, A.C.1    Trus, B.L.2    Maizel, J.V.3    Unser, M.4    Parry, D.A.5    Wall, J.S.6
  • 16
    • 0035043999 scopus 로고    scopus 로고
    • No syringes please, ejection of phage T7 DNA from the virion is enzyme driven
    • Molineux I.J. No syringes please, ejection of phage T7 DNA from the virion is enzyme driven. Mol. Microbiol. 2001, 40:1-8.
    • (2001) Mol. Microbiol. , vol.40 , pp. 1-8
    • Molineux, I.J.1
  • 17
    • 24944579983 scopus 로고    scopus 로고
    • Changes in bacteriophage T7 virion structure at the initiation of infection
    • Kemp P., Garcia L.R., Molineux I.J. Changes in bacteriophage T7 virion structure at the initiation of infection. Virology 2005, 340:307-317.
    • (2005) Virology , vol.340 , pp. 307-317
    • Kemp, P.1    Garcia, L.R.2    Molineux, I.J.3
  • 18
    • 0019460574 scopus 로고
    • Bacteriophage T3 and bacteriophage T7 virus-host cell interactions
    • Krüger D.H., Schroeder C. Bacteriophage T3 and bacteriophage T7 virus-host cell interactions. Microbiol. Rev. 1981, 45:9-51.
    • (1981) Microbiol. Rev. , vol.45 , pp. 9-51
    • Krüger, D.H.1    Schroeder, C.2
  • 19
    • 1442300823 scopus 로고    scopus 로고
    • Peptidoglycan hydrolytic activities associated with bacteriophage virions
    • Moak M., Molineux I.J. Peptidoglycan hydrolytic activities associated with bacteriophage virions. Mol. Microbiol. 2004, 51:1169-1183.
    • (2004) Mol. Microbiol. , vol.51 , pp. 1169-1183
    • Moak, M.1    Molineux, I.J.2
  • 20
    • 75849141082 scopus 로고    scopus 로고
    • Gp15 and gp16 cooperate in translocating bacteriophage T7 DNA into the infected cell
    • Chang C.Y., Kemp P., Molineux I.J. Gp15 and gp16 cooperate in translocating bacteriophage T7 DNA into the infected cell. Virology 2010, 398:176-186.
    • (2010) Virology , vol.398 , pp. 176-186
    • Chang, C.Y.1    Kemp, P.2    Molineux, I.J.3
  • 21
    • 27744487093 scopus 로고    scopus 로고
    • Common ancestry of herpesviruses and tailed DNA bacteriophages
    • Baker M.L., Jiang W., Rixon F.J., Chiu W. Common ancestry of herpesviruses and tailed DNA bacteriophages. J. Virol. 2005, 79:14967-14970.
    • (2005) J. Virol. , vol.79 , pp. 14967-14970
    • Baker, M.L.1    Jiang, W.2    Rixon, F.J.3    Chiu, W.4
  • 22
    • 31844435708 scopus 로고    scopus 로고
    • Structure of epsilon15 bacteriophage reveals genome organization and DNA packaging/injection apparatus
    • Jiang W., Chang J., Jakana J., Weigele P., King J., Chiu W. Structure of epsilon15 bacteriophage reveals genome organization and DNA packaging/injection apparatus. Nature 2006, 439:612-616.
    • (2006) Nature , vol.439 , pp. 612-616
    • Jiang, W.1    Chang, J.2    Jakana, J.3    Weigele, P.4    King, J.5    Chiu, W.6
  • 23
    • 77954384340 scopus 로고    scopus 로고
    • Structural changes in a marine podovirus associated with release of its genome into Prochlorococcus
    • Liu X., Zhang Q., Murata K., Baker M.L., Sullivan M.B., Fu C., et al. Structural changes in a marine podovirus associated with release of its genome into Prochlorococcus. Nat. Struct. Mol. Biol. 2010, 17:830-836.
    • (2010) Nat. Struct. Mol. Biol. , vol.17 , pp. 830-836
    • Liu, X.1    Zhang, Q.2    Murata, K.3    Baker, M.L.4    Sullivan, M.B.5    Fu, C.6
  • 24
    • 33744811672 scopus 로고    scopus 로고
    • Cryo-EM asymmetric reconstruction of bacteriophage P22 reveals organization of its DNA packaging and infecting machinery
    • Chang J., Weigele P., King J., Chiu W., Jiang W. Cryo-EM asymmetric reconstruction of bacteriophage P22 reveals organization of its DNA packaging and infecting machinery. Structure 2006, 14:1073-1082.
    • (2006) Structure , vol.14 , pp. 1073-1082
    • Chang, J.1    Weigele, P.2    King, J.3    Chiu, W.4    Jiang, W.5
  • 25
    • 0021329694 scopus 로고
    • Steps in the stabilization of newly packaged DNA during phage P22 morphogenesis
    • Strauss H., King J. Steps in the stabilization of newly packaged DNA during phage P22 morphogenesis. J. Mol. Biol. 1984, 172:523-543.
    • (1984) J. Mol. Biol. , vol.172 , pp. 523-543
    • Strauss, H.1    King, J.2
  • 27
    • 33745506037 scopus 로고    scopus 로고
    • The structure of an infectious P22 virion shows the signal for headful DNA packaging
    • Lander G.C., Tang L., Casjens S.R., Gilcrease E.B., Prevelige P., Poliakov A., et al. The structure of an infectious P22 virion shows the signal for headful DNA packaging. Science 2006, 312:1791-1795.
    • (2006) Science , vol.312 , pp. 1791-1795
    • Lander, G.C.1    Tang, L.2    Casjens, S.R.3    Gilcrease, E.B.4    Prevelige, P.5    Poliakov, A.6
  • 28
    • 0021637494 scopus 로고
    • DNA injection proteins are targets of acridine-sensitized photoinactivation of bacteriophage P22
    • Bryant J.L., King J. DNA injection proteins are targets of acridine-sensitized photoinactivation of bacteriophage P22. J. Mol. Biol. 1984, 180:837-863.
    • (1984) J. Mol. Biol. , vol.180 , pp. 837-863
    • Bryant, J.L.1    King, J.2
  • 29
    • 0016753519 scopus 로고
    • Bacteriophage P22 virion protein which performs an essential early function. I. Analysis of 16-ts mutants
    • Hoffman B., Levine M. Bacteriophage P22 virion protein which performs an essential early function. I. Analysis of 16-ts mutants. J. Virol. 1975, 16:1536-1546.
    • (1975) J. Virol. , vol.16 , pp. 1536-1546
    • Hoffman, B.1    Levine, M.2
  • 30
    • 0016809125 scopus 로고
    • Bacteriophage P22 virion protein which performs an essential early function. II. Characterization of the gene 16 function
    • Hoffman B., Levine M. Bacteriophage P22 virion protein which performs an essential early function. II. Characterization of the gene 16 function. J. Virol. 1975, 16:1547-1559.
    • (1975) J. Virol. , vol.16 , pp. 1547-1559
    • Hoffman, B.1    Levine, M.2
  • 31
  • 32
    • 14844330221 scopus 로고    scopus 로고
    • Structural studies by electron tomography: from cells to molecules
    • Lucić V., Förster F., Baumeister W. Structural studies by electron tomography: from cells to molecules. Annu. Rev. Biochem. 2005, 74:833-865.
    • (2005) Annu. Rev. Biochem. , vol.74 , pp. 833-865
    • Lucić, V.1    Förster, F.2    Baumeister, W.3
  • 33
    • 0015588589 scopus 로고
    • Studies on the mechanism of phage adsorption: interaction between phage epsilon15 and its cellular receptor
    • Kanegasaki S., Wright A. Studies on the mechanism of phage adsorption: interaction between phage epsilon15 and its cellular receptor. Virology 1973, 52:160-173.
    • (1973) Virology , vol.52 , pp. 160-173
    • Kanegasaki, S.1    Wright, A.2
  • 34
    • 0018346605 scopus 로고
    • Variation in the structure and bacteriophage-inactivating capacity of Salmonella anatum lipopolysaccharide as a function of growth temperature
    • McConnell M., Wright A. Variation in the structure and bacteriophage-inactivating capacity of Salmonella anatum lipopolysaccharide as a function of growth temperature. J. Bacteriol. 1979, 137:746-751.
    • (1979) J. Bacteriol. , vol.137 , pp. 746-751
    • McConnell, M.1    Wright, A.2
  • 35
    • 0015588594 scopus 로고
    • In vitro interaction between phage and receptor lipopolysaccharide: a novel glycosidase associated with Salmonella phage 15
    • Takeda K., Uetake H. In vitro interaction between phage and receptor lipopolysaccharide: a novel glycosidase associated with Salmonella phage 15. Virology 1973, 52:148-159.
    • (1973) Virology , vol.52 , pp. 148-159
    • Takeda, K.1    Uetake, H.2
  • 36
    • 0027938423 scopus 로고
    • Translocation of DNA across bacterial membranes
    • Dreiseikelmann B. Translocation of DNA across bacterial membranes. Microbiol. Rev. 1994, 58:293-316.
    • (1994) Microbiol. Rev. , vol.58 , pp. 293-316
    • Dreiseikelmann, B.1
  • 37
    • 77957010716 scopus 로고
    • Bacterial membranes
    • Academic Press, San Diego, CA, W.B. Jakoby (Ed.)
    • Kaback H.R. Bacterial membranes. Methods in Enzymology 1971, 22:99-120. Academic Press, San Diego, CA. W.B. Jakoby (Ed.).
    • (1971) Methods in Enzymology , vol.22 , pp. 99-120
    • Kaback, H.R.1
  • 38
    • 33846785568 scopus 로고    scopus 로고
    • Electron cryotomography reveals the portal in the herpesvirus capsid
    • Chang J.T., Schmid M.F., Rixon F.J., Chiu W. Electron cryotomography reveals the portal in the herpesvirus capsid. J. Virol. 2007, 81:2065-2068.
    • (2007) J. Virol. , vol.81 , pp. 2065-2068
    • Chang, J.T.1    Schmid, M.F.2    Rixon, F.J.3    Chiu, W.4
  • 39
    • 40649109028 scopus 로고    scopus 로고
    • Methods for aligning and for averaging 3D volumes with missing data
    • Schmid M.F., Booth C.R. Methods for aligning and for averaging 3D volumes with missing data. J. Struct. Biol. 2008, 161:243-248.
    • (2008) J. Struct. Biol. , vol.161 , pp. 243-248
    • Schmid, M.F.1    Booth, C.R.2
  • 41
    • 0029914253 scopus 로고    scopus 로고
    • FhuA, a transporter of the Escherichia coli outer membrane, is converted into a channel upon binding of bacteriophage T5
    • Bonhivers M., Ghazi A., Boulanger P., Letellier L. FhuA, a transporter of the Escherichia coli outer membrane, is converted into a channel upon binding of bacteriophage T5. EMBO J. 1996, 15:1850-1856.
    • (1996) EMBO J. , vol.15 , pp. 1850-1856
    • Bonhivers, M.1    Ghazi, A.2    Boulanger, P.3    Letellier, L.4
  • 42
    • 0018648947 scopus 로고
    • Requirement for membrane potential in injection of phage T4 DNA
    • Labedan B., Goldberg E.B. Requirement for membrane potential in injection of phage T4 DNA. Proc. Natl Acad. Sci. USA 1979, 76:4669-4673.
    • (1979) Proc. Natl Acad. Sci. USA , vol.76 , pp. 4669-4673
    • Labedan, B.1    Goldberg, E.B.2
  • 43
    • 0020569495 scopus 로고
    • Studies on energy supply for genetic processes. Requirement for membrane potential in Escherichia coli infection by phage T4
    • Kalasauskaite E.V., Kadisaite D.L., Daugelavicius R.J., Grinius L.L., Jasaitis A.A. Studies on energy supply for genetic processes. Requirement for membrane potential in Escherichia coli infection by phage T4. Eur. J. Biochem. 1983, 130:123-130.
    • (1983) Eur. J. Biochem. , vol.130 , pp. 123-130
    • Kalasauskaite, E.V.1    Kadisaite, D.L.2    Daugelavicius, R.J.3    Grinius, L.L.4    Jasaitis, A.A.5
  • 44
    • 58149479226 scopus 로고    scopus 로고
    • Transport of phage P22 DNA across the cytoplasmic membrane
    • Perez G.L., Huynh B., Slater M., Maloy S. Transport of phage P22 DNA across the cytoplasmic membrane. J. Bacteriol. 2009, 191:135-140.
    • (2009) J. Bacteriol. , vol.191 , pp. 135-140
    • Perez, G.L.1    Huynh, B.2    Slater, M.3    Maloy, S.4
  • 45
    • 0016709158 scopus 로고
    • Reversible interaction between coliphage lambda and its receptor protein
    • Schwartz M. Reversible interaction between coliphage lambda and its receptor protein. J. Mol. Biol. 1975, 99:185-201.
    • (1975) J. Mol. Biol. , vol.99 , pp. 185-201
    • Schwartz, M.1
  • 46
    • 0141994975 scopus 로고    scopus 로고
    • Cryo-transmission electron microscopy of frozen-hydrated sections of Escherichia coli and Pseudomonas aeruginosa
    • Matias V.R., Al-Amoudi A., Dubochet J., Beveridge T.J. Cryo-transmission electron microscopy of frozen-hydrated sections of Escherichia coli and Pseudomonas aeruginosa. J. Bacteriol. 2003, 185:6112-6118.
    • (2003) J. Bacteriol. , vol.185 , pp. 6112-6118
    • Matias, V.R.1    Al-Amoudi, A.2    Dubochet, J.3    Beveridge, T.J.4
  • 47
    • 0014413854 scopus 로고
    • Endonuclease-I-deficient and ribonuclease I-deficient Escherichia coli mutants
    • Dürwald H., Hoffmann-Berling H. Endonuclease-I-deficient and ribonuclease I-deficient Escherichia coli mutants. J. Mol. Biol. 1968, 34:331-346.
    • (1968) J. Mol. Biol. , vol.34 , pp. 331-346
    • Dürwald, H.1    Hoffmann-Berling, H.2
  • 48
    • 0035162346 scopus 로고    scopus 로고
    • Cloning and characterization of a periplasmic nuclease of Vibrio vulnificus and its role in preventing uptake of foreign DNA
    • Wu S.I., Lo S.K., Shao C.P., Tsai H.W., Hor L.I. Cloning and characterization of a periplasmic nuclease of Vibrio vulnificus and its role in preventing uptake of foreign DNA. Appl. Environ. Microbiol. 2001, 67:82-88.
    • (2001) Appl. Environ. Microbiol. , vol.67 , pp. 82-88
    • Wu, S.I.1    Lo, S.K.2    Shao, C.P.3    Tsai, H.W.4    Hor, L.I.5
  • 50
    • 0003025772 scopus 로고
    • The DNA injection apparatus of phage p22
    • Hartwieg E., Bazinet C., King J. The DNA injection apparatus of phage p22. Biophys. J. 1986, 49:24-26.
    • (1986) Biophys. J. , vol.49 , pp. 24-26
    • Hartwieg, E.1    Bazinet, C.2    King, J.3
  • 51
    • 0015450017 scopus 로고
    • Binding of bacteriophage P22 tail parts to cells
    • Israel V., Rosen H., Levine M. Binding of bacteriophage P22 tail parts to cells. J. Virol. 1972, 10:1152-1158.
    • (1972) J. Virol. , vol.10 , pp. 1152-1158
    • Israel, V.1    Rosen, H.2    Levine, M.3
  • 52
    • 33744962964 scopus 로고    scopus 로고
    • The ectodomain of the viral receptor YueB forms a fiber that triggers ejection of bacteriophage SPP1 DNA
    • São-José C., Lhuillier S., Lurz R., Melki R., Lepault J., Santos M.A., Tavares P. The ectodomain of the viral receptor YueB forms a fiber that triggers ejection of bacteriophage SPP1 DNA. J. Biol. Chem. 2006, 281:11464-11470.
    • (2006) J. Biol. Chem. , vol.281 , pp. 11464-11470
    • São-José, C.1    Lhuillier, S.2    Lurz, R.3    Melki, R.4    Lepault, J.5    Santos, M.A.6    Tavares, P.7
  • 53
    • 0015841378 scopus 로고
    • Mechanism of head assembly and DNA encapsulation in Salmonella phage p22. I. Genes, proteins, structures and DNA maturation
    • Botstein D., Waddell C.H., King J. Mechanism of head assembly and DNA encapsulation in Salmonella phage p22. I. Genes, proteins, structures and DNA maturation. J. Mol. Biol. 1973, 80:669-695.
    • (1973) J. Mol. Biol. , vol.80 , pp. 669-695
    • Botstein, D.1    Waddell, C.H.2    King, J.3
  • 54
    • 0017581778 scopus 로고
    • Functions of two new genes in Salmonella phage P22 assembly
    • Poteete A.R., King J. Functions of two new genes in Salmonella phage P22 assembly. Virology 1977, 76:725-739.
    • (1977) Virology , vol.76 , pp. 725-739
    • Poteete, A.R.1    King, J.2
  • 56
    • 35348943866 scopus 로고    scopus 로고
    • DNA organization and thermodynamics during viral packing
    • Locker C.R., Fuller S.D., Harvey S.C. DNA organization and thermodynamics during viral packing. Biophys. J. 2007, 93:2861-2869.
    • (2007) Biophys. J. , vol.93 , pp. 2861-2869
    • Locker, C.R.1    Fuller, S.D.2    Harvey, S.C.3
  • 57
    • 38549093508 scopus 로고    scopus 로고
    • Effects of salt concentrations and bending energy on the extent of ejection of phage genomes
    • Evilevitch A., Fang L.T., Yoffe A.M., Castelnovo M., Rau D.C., Parsegian V.A., et al. Effects of salt concentrations and bending energy on the extent of ejection of phage genomes. Biophys. J. 2008, 94:1110-1120.
    • (2008) Biophys. J. , vol.94 , pp. 1110-1120
    • Evilevitch, A.1    Fang, L.T.2    Yoffe, A.M.3    Castelnovo, M.4    Rau, D.C.5    Parsegian, V.A.6
  • 58
    • 33947325925 scopus 로고    scopus 로고
    • Forces controlling the rate of DNA ejection from phage lambda
    • Löf D., Schillén K., Jönsson B., Evilevitch A. Forces controlling the rate of DNA ejection from phage lambda. J. Mol. Biol. 2007, 368:55-65.
    • (2007) J. Mol. Biol. , vol.368 , pp. 55-65
    • Löf, D.1    Schillén, K.2    Jönsson, B.3    Evilevitch, A.4
  • 59
  • 60
    • 0000250208 scopus 로고
    • The growth of bacteriophage and lysis of the host
    • Delbrück M. The growth of bacteriophage and lysis of the host. J. Gen. Physiol. 1940, 23:643-660.
    • (1940) J. Gen. Physiol. , vol.23 , pp. 643-660
    • Delbrück, M.1
  • 61
    • 46649087608 scopus 로고    scopus 로고
    • Phage T5 straight tail fiber is a multifunctional protein acting as a tape measure and carrying fusogenic and muralytic activities
    • Boulanger P., Jacquot P., Plançon L., Chami M., Engel A., Parquet C., et al. Phage T5 straight tail fiber is a multifunctional protein acting as a tape measure and carrying fusogenic and muralytic activities. J. Biol. Chem. 2008, 283:13556-13564.
    • (2008) J. Biol. Chem. , vol.283 , pp. 13556-13564
    • Boulanger, P.1    Jacquot, P.2    Plançon, L.3    Chami, M.4    Engel, A.5    Parquet, C.6
  • 62
    • 0002610948 scopus 로고
    • Independent functions of viral protein and nucleic acid in growth of bacteriophage
    • Hershey A.D., Chase M. Independent functions of viral protein and nucleic acid in growth of bacteriophage. J. Gen. Physiol. 1952, 36:39-56.
    • (1952) J. Gen. Physiol. , vol.36 , pp. 39-56
    • Hershey, A.D.1    Chase, M.2
  • 63
    • 0014748362 scopus 로고
    • Rapid bacteriophage sedimentation in the presence of polyethylene glycol and its application to large-scale virus purification
    • Yamamoto K.R., Alberts B.M., Benzinger R., Lawhorne L., Treiber G. Rapid bacteriophage sedimentation in the presence of polyethylene glycol and its application to large-scale virus purification. Virology 1970, 40:734-744.
    • (1970) Virology , vol.40 , pp. 734-744
    • Yamamoto, K.R.1    Alberts, B.M.2    Benzinger, R.3    Lawhorne, L.4    Treiber, G.5
  • 64
    • 0001172501 scopus 로고
    • Equilibrium sedimentation of macromolecules in density gradients
    • Meselson M., Stahl F.W., Vinograd J. Equilibrium sedimentation of macromolecules in density gradients. Proc. Natl Acad. Sci. USA 1957, 43:581-588.
    • (1957) Proc. Natl Acad. Sci. USA , vol.43 , pp. 581-588
    • Meselson, M.1    Stahl, F.W.2    Vinograd, J.3
  • 66
    • 25644458666 scopus 로고    scopus 로고
    • Automated electron microscope tomography using robust prediction of specimen movements
    • Mastronarde D.N. Automated electron microscope tomography using robust prediction of specimen movements. J. Struct. Biol. 2005, 152:36-51.
    • (2005) J. Struct. Biol. , vol.152 , pp. 36-51
    • Mastronarde, D.N.1
  • 67
    • 0031422417 scopus 로고    scopus 로고
    • Dual-axis tomography: an approach with alignment methods that preserve resolution
    • Mastronarde D.N. Dual-axis tomography: an approach with alignment methods that preserve resolution. J. Struct. Biol. 1997, 120:343-352.
    • (1997) J. Struct. Biol. , vol.120 , pp. 343-352
    • Mastronarde, D.N.1
  • 68
    • 0000313739 scopus 로고
    • Exact filters for general geometry three dimensional reconstruction
    • Harauz G., van Heel M. Exact filters for general geometry three dimensional reconstruction. Optik 1986, 73:146-156.
    • (1986) Optik , vol.73 , pp. 146-156
    • Harauz, G.1    van Heel, M.2
  • 69
    • 21344461027 scopus 로고    scopus 로고
    • Three Prochlorococcus cyanophage genomes: signature features and ecological interpretations
    • Sullivan M.B., Coleman M.L., Weigele P., Rohwer F., Chisholm S.W. Three Prochlorococcus cyanophage genomes: signature features and ecological interpretations. PLoS Biol. 2005, 3:e144.
    • (2005) PLoS Biol. , vol.3
    • Sullivan, M.B.1    Coleman, M.L.2    Weigele, P.3    Rohwer, F.4    Chisholm, S.W.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.