메뉴 건너뛰기




Volumn 9, Issue 12, 2014, Pages 1319-1337

Structure and function of bacteriophage T4

Author keywords

assembly; bacteriophage T4; baseplate; contractile tail; genome packaging; T4 infection

Indexed keywords

GENOMIC DNA; VIRUS PROTEIN;

EID: 84919828897     PISSN: 17460913     EISSN: 17460921     Source Type: Journal    
DOI: 10.2217/fmb.14.91     Document Type: Review
Times cited : (117)

References (146)
  • 1
    • 0342943124 scopus 로고
    • Electron microscopy of phages
    • Cairns J, Stent GS, Watson JD (Eds). Cold Spring Harbor Laboratory Press, NY, USA
    • Anderson TF. Electron microscopy of phages. In: Phage and the Origins of Molecular Biology. Cairns J, Stent GS, Watson JD (Eds). Cold Spring Harbor Laboratory Press, NY, USA, 63-78 (1992).
    • (1992) Phage and the Origins of Molecular Biology , pp. 63-78
    • Anderson, T.F.1
  • 2
    • 0001639497 scopus 로고
    • Bacteriophage-resistant mutants in Escherichia coli
    • Demerec M, Fano U. Bacteriophage-resistant mutants in Escherichia coli. Genetics 30(2), 119-136 (1945).
    • (1945) Genetics , vol.30 , Issue.2 , pp. 119-136
    • Demerec, M.1    Fano, U.2
  • 3
    • 0000818999 scopus 로고
    • General nature of the genetic code for proteins
    • Crick FH, Barnett L, Brenner S, Watts-Tobin RJ. General nature of the genetic code for proteins. Nature 192(4809), 1227-1232 (1961).
    • (1961) Nature , vol.192 , Issue.4809 , pp. 1227-1232
    • Crick, F.H.1    Barnett, L.2    Brenner, S.3    Watts-Tobin, R.J.4
  • 4
    • 0002610948 scopus 로고
    • Independent functions of viral protein and nucleic acid in growth of bacteriophage
    • Hershey AD, Chase M. Independent functions of viral protein and nucleic acid in growth of bacteriophage. J. Gen. Physiol. 36(1), 39-56 (1952).
    • (1952) J. Gen. Physiol. , vol.36 , Issue.1 , pp. 39-56
    • Hershey, A.D.1    Chase, M.2
  • 5
    • 85025374668 scopus 로고
    • Structural components of bacteriophage
    • Brenner S, Streisinger G, Horne RW et al. Structural components of bacteriophage. J. Mol. Biol. 1(3), 281-292 (1959).
    • (1959) J. Mol. Biol. , vol.1 , Issue.3 , pp. 281-292
    • Brenner, S.1    Streisinger, G.2    Horne, R.W.3
  • 6
    • 0342741557 scopus 로고
    • The structure of coliphages
    • Bradley DE. The structure of coliphages. J. Gen. Microbiol. 31, 435-445 (1963).
    • (1963) J. Gen. Microbiol. , vol.31 , pp. 435-445
    • Bradley, D.E.1
  • 7
    • 0014945329 scopus 로고
    • Reconstruction of three-dimensional images from electron micrographs of structures with helical symmetry
    • DeRosier DJ, Moore PB. Reconstruction of three-dimensional images from electron micrographs of structures with helical symmetry. J. Mol. Biol. 52(2), 355-369 (1970).
    • (1970) J. Mol. Biol. , vol.52 , Issue.2 , pp. 355-369
    • Derosier, D.J.1    Moore, P.B.2
  • 8
    • 72949149555 scopus 로고
    • Some remarks on the morphology of bacteriophage T4B
    • Daems WT, van de Pol JH, Cohen JA. Some remarks on the morphology of bacteriophage T4B. J. Mol. Biol. 3(2), 225-227 (1961).
    • (1961) J. Mol. Biol. , vol.3 , Issue.2 , pp. 225-227
    • Daems, W.T.1    Van De-Pol, J.H.2    Cohen, J.A.3
  • 9
    • 0343176035 scopus 로고
    • New approaches in the study of biological ultrastructure by high resolution electron microscopy
    • Harris RJC (Ed.). Academic Press, NY, USA
    • Fernandez-Moran H. New approaches in the study of biological ultrastructure by high resolution electron microscopy. In: The Interpretation of Ultrastructure. Harris RJC (Ed.). Academic Press, NY, USA, 411-427 (1962).
    • (1962) The Interpretation of Ultrastructure , pp. 411-427
    • Fernandez-Moran, H.1
  • 10
    • 0342741558 scopus 로고
    • On the fine structure of normal and 'polymerized' tail sheath of phage T4
    • Kellenberger E, de la Tour EB. On the fine structure of normal and 'polymerized' tail sheath of phage T4. J. Ultrastruct. Res. 11, 545-563 (1964).
    • (1964) J. Ultrastruct. Res. , vol.11 , pp. 545-563
    • Kellenberger, E.1    De La-Tour, E.B.2
  • 11
    • 0014219704 scopus 로고
    • Structure of normal and contracted tail sheaths of T4 bacteriophage
    • Krimm S, Anderson TF. Structure of normal and contracted tail sheaths of T4 bacteriophage. J. Mol. Biol. 27(2), 197-202 (1967).
    • (1967) J. Mol. Biol. , vol.27 , Issue.2 , pp. 197-202
    • Krimm, S.1    Anderson, T.F.2
  • 12
    • 0016771607 scopus 로고
    • Three-dimensional image reconstruction of the contractile tail of T4 bacteriophage
    • Amos LA, Klug A. Three-dimensional image reconstruction of the contractile tail of T4 bacteriophage. J. Mol. Biol. 99(1), 51-64 (1975).
    • (1975) J. Mol. Biol. , vol.99 , Issue.1 , pp. 51-64
    • Amos, L.A.1    Klug, A.2
  • 14
    • 0742299990 scopus 로고
    • The structure of the 'polyheads' of T4 bacteriophage
    • Finch JT, Klug A, Stretton AOW. The structure of the 'polyheads' of T4 bacteriophage. J. Mol. Biol. 10(3), 570-575 (1964).
    • (1964) J. Mol. Biol. , vol.10 , Issue.3 , pp. 570-575
    • Finch, J.T.1    Klug, A.2    Stretton, A.O.W.3
  • 15
    • 0015505690 scopus 로고
    • Structure of the tubular variants of the head of bacteriophage T4 (polyheads). I. Arrangement of subunits in some classes of polyheads
    • DeRosier DJ, Klug A. Structure of the tubular variants of the head of bacteriophage T4 (polyheads). I. Arrangement of subunits in some classes of polyheads. J. Mol. Biol. 65(3), 469-488 (1972).
    • (1972) J. Mol. Biol. , vol.65 , Issue.3 , pp. 469-488
    • Derosier, D.J.1    Klug, A.2
  • 16
    • 0015505704 scopus 로고
    • Structure of the tubular variants of the head of bacteriophage T4 (polyheads). II. Structural transition from a hexamer to a 6+1 morphological unit
    • Yanagida M, DeRosier DJ, Klug A. Structure of the tubular variants of the head of bacteriophage T4 (polyheads). II. Structural transition from a hexamer to a 6+1 morphological unit. J. Mol. Biol. 65(3), 489-499 (1972).
    • (1972) J. Mol. Biol. , vol.65 , Issue.3 , pp. 489-499
    • Yanagida, M.1    Derosier, D.J.2    Klug, A.3
  • 17
    • 0013954606 scopus 로고
    • Optical filtering of electron micrographs: Reconstruction of one-sided images
    • Klug A, De Rosier DJ. Optical filtering of electron micrographs: reconstruction of one-sided images. Nature 212(5057), 29-32 (1966).
    • (1966) Nature , vol.212 , Issue.5057 , pp. 29-32
    • Klug, A.1    De Rosier, D.J.2
  • 18
    • 0017757241 scopus 로고
    • Molecular reorganization in the hexagon to star transition of the baseplate of bacteriophage T4
    • Crowther RA, Lenk EV, Kikuchi Y, King J. Molecular reorganization in the hexagon to star transition of the baseplate of bacteriophage T4. J. Mol. Biol. 116(3), 489-523 (1977).
    • (1977) J. Mol. Biol. , vol.116 , Issue.3 , pp. 489-523
    • Crowther, R.A.1    Lenk, E.V.2    Kikuchi, Y.3    King, J.4
  • 20
    • 0041819526 scopus 로고    scopus 로고
    • Three-dimensional structure of bacteriophage T4 baseplate
    • Kostyuchenko VA, Leiman PG, Chipman PR et al. Three-dimensional structure of bacteriophage T4 baseplate. Nat. Struct. Biol. 10(9), 688-693 (2003).
    • (2003) Nat. Struct. Biol. , vol.10 , Issue.9 , pp. 688-693
    • Kostyuchenko, V.A.1    Leiman, P.G.2    Chipman, P.R.3
  • 21
    • 4644242580 scopus 로고    scopus 로고
    • Three-dimensional rearrangement of proteins in the tail of bacteriophage T4 on infection of its host
    • Leiman PG, Chipman PR, Kostyuchenko VA, Mesyanzhinov VV, Rossmann MG. Three-dimensional rearrangement of proteins in the tail of bacteriophage T4 on infection of its host. Cell 118(4), 419-429 (2004).
    • (2004) Cell , vol.118 , Issue.4 , pp. 419-429
    • Leiman, P.G.1    Chipman, P.R.2    Kostyuchenko, V.A.3    Mesyanzhinov, V.V.4    Rossmann, M.G.5
  • 24
    • 0025778388 scopus 로고
    • Mass analysis of bacteriophage T4 proheads and mature heads by scanning transmission electron microscopy and hydrodynamic measurements
    • Baschong W, Baschong-Prescianotto C, Engel A et al. Mass analysis of bacteriophage T4 proheads and mature heads by scanning transmission electron microscopy and hydrodynamic measurements. J. Struct. Biol. 106(2), 93-101 (1991).
    • (1991) J. Struct. Biol. , vol.106 , Issue.2 , pp. 93-101
    • Baschong, W.1    Baschong-Prescianotto, C.2    Engel, A.3
  • 25
    • 0015949769 scopus 로고
    • Electron microscope heteroduplex study of sequence relations of T2, T4, and T6 bacteriophage DNAs
    • Kim JS, Davidson N. Electron microscope heteroduplex study of sequence relations of T2, T4, and T6 bacteriophage DNAs. Virology 57(1), 93-111 (1974).
    • (1974) Virology , vol.57 , Issue.1 , pp. 93-111
    • Kim, J.S.1    Davidson, N.2
  • 27
    • 0032727550 scopus 로고    scopus 로고
    • Geometry of phage head construction
    • Moody MF. Geometry of phage head construction. J. Mol. Biol. 293(2), 401-433 (1999).
    • (1999) J. Mol. Biol. , vol.293 , Issue.2 , pp. 401-433
    • Moody, M.F.1
  • 29
    • 0017881643 scopus 로고
    • Isolation and characterization of bacteriophage T4 mutant preheads
    • Onorato L, Stirmer B, Showe MK. Isolation and characterization of bacteriophage T4 mutant preheads. J. Virol. 27(2), 409-426 (1978).
    • (1978) J. Virol. , vol.27 , Issue.2 , pp. 409-426
    • Onorato, L.1    Stirmer, B.2    Showe, M.K.3
  • 30
    • 0021551932 scopus 로고
    • Molecular organization of the head of bacteriophage T-even: Underlying design principles
    • Yanagida M, Suzuki Y, Toda T. Molecular organization of the head of bacteriophage T-even: underlying design principles. Adv. Biophys. 17, 97-146 (1984).
    • (1984) Adv. Biophys. , vol.17 , pp. 97-146
    • Yanagida, M.1    Suzuki, Y.2    Toda, T.3
  • 31
    • 18844400837 scopus 로고    scopus 로고
    • Structural and functional similarities between the capsid proteins of bacteriophages T4 and HK97 point to a common ancestry
    • Fokine A, Leiman PG, Shneider MM et al. Structural and functional similarities between the capsid proteins of bacteriophages T4 and HK97 point to a common ancestry. Proc. Natl Acad. Sci. USA 102(20), 7163-7168 (2005).
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , Issue.20 , pp. 7163-7168
    • Fokine, A.1    Leiman, P.G.2    Shneider, M.M.3
  • 32
    • 0022219750 scopus 로고
    • The structure of the adenovirus capsid. II. The packing symmetry of hexon and its implications for viral architecture
    • Burnett RM. The structure of the adenovirus capsid. II. The packing symmetry of hexon and its implications for viral architecture. J. Mol. Biol. 185(1), 125-143 (1985).
    • (1985) J. Mol. Biol. , vol.185 , Issue.1 , pp. 125-143
    • Burnett, R.M.1
  • 33
    • 0026006259 scopus 로고
    • Image reconstruction reveals the complex molecular organization of adenovirus
    • Stewart PL, Burnett RM, Cyrklaff M, Fuller SD. Image reconstruction reveals the complex molecular organization of adenovirus. Cell 67(1), 145-154 (1991).
    • (1991) Cell , vol.67 , Issue.1 , pp. 145-154
    • Stewart, P.L.1    Burnett, R.M.2    Cyrklaff, M.3    Fuller, S.D.4
  • 36
    • 0019816862 scopus 로고
    • Gene 20 product of bacteriophage T4. Its purification and structure
    • Driedonks RA, Engel A, ten Heggeler B, van Driel R. Gene 20 product of bacteriophage T4. Its purification and structure. J. Mol. Biol. 152(4), 641-662 (1981).
    • (1981) J. Mol. Biol. , vol.152 , Issue.4 , pp. 641-662
    • Driedonks, R.A.1    Engel, A.2    Ten Heggeler, B.3    Van Driel, R.4
  • 37
    • 0020571396 scopus 로고
    • Gene 20 product of bacteriophage T4. II. Its structural organization in prehead and bacteriophage
    • Driedonks RA, Caldentey J. Gene 20 product of bacteriophage T4. II. Its structural organization in prehead and bacteriophage. J. Mol. Biol. 166(3), 341-360 (1983).
    • (1983) J. Mol. Biol. , vol.166 , Issue.3 , pp. 341-360
    • Driedonks, R.A.1    Caldentey, J.2
  • 38
    • 0017698623 scopus 로고
    • DNA packaging and pathway of bacteriophage T4 head assembly
    • Hsiao CL, Black LW. DNA packaging and pathway of bacteriophage T4 head assembly. Proc. Natl Acad. Sci. USA 74(9), 3652-3656 (1977).
    • (1977) Proc. Natl Acad. Sci. USA , vol.74 , Issue.9 , pp. 3652-3656
    • Hsiao, C.L.1    Black, L.W.2
  • 39
    • 73649087232 scopus 로고    scopus 로고
    • Structure of the small outer capsid protein, Soc: A clamp for stabilizing capsids of T4-like phages
    • Qin L, Fokine A, O'Donnell E, Rao VB, Rossmann MG. Structure of the small outer capsid protein, Soc: a clamp for stabilizing capsids of T4-like phages. J. Mol. Biol. 395(4), 728-741 (2010).
    • (2010) J. Mol. Biol. , vol.395 , Issue.4 , pp. 728-741
    • Qin, L.1    Fokine, A.2    O'Donnell, E.3    Rao, V.B.4    Rossmann, M.G.5
  • 40
    • 0017597092 scopus 로고
    • The two dispensable structural proteins (soc and hoc) of the T4 phage capsid: Their properties, isolation and characterization of defective mutants, and their binding with the defective heads in vitro
    • Ishii T, Yanagida M. The two dispensable structural proteins (soc and hoc) of the T4 phage capsid: their properties, isolation and characterization of defective mutants, and their binding with the defective heads in vitro. J. Mol. Biol. 109(4), 487-514 (1977).
    • (1977) J. Mol. Biol. , vol.109 , Issue.4 , pp. 487-514
    • Ishii, T.1    Yanagida, M.2
  • 41
    • 79961196704 scopus 로고    scopus 로고
    • Structure of the three N-terminal immunoglobulin domains of the highly immunogenic outer capsid protein from a T4-like bacteriophage
    • Fokine A, Islam MZ, Zhang Z, Bowman VD, Rao VB, Rossmann MG. Structure of the three N-terminal immunoglobulin domains of the highly immunogenic outer capsid protein from a T4-like bacteriophage. J. Virol. 85(16), 8141-8148 (2011).
    • (2011) J. Virol. , vol.85 , Issue.16 , pp. 8141-8148
    • Fokine, A.1    Islam, M.Z.2    Zhang, Z.3    Bowman, V.D.4    Rao, V.B.5    Rossmann, M.G.6
  • 42
    • 0018077877 scopus 로고
    • Head morphogenesis of bacteriophage T4. III. The role of gene 20 in DNA packaging
    • Hsiao CL, Black LW. Head morphogenesis of bacteriophage T4. III. The role of gene 20 in DNA packaging. Virology 91(1), 26-38 (1978).
    • (1978) Virology , vol.91 , Issue.1 , pp. 26-38
    • Hsiao, C.L.1    Black, L.W.2
  • 43
    • 0018129413 scopus 로고
    • Head morphogenesis of bacteriophage T4. II. The role of gene 40 in initiating prehead assembly
    • Hsiao CL, Black LW. Head morphogenesis of bacteriophage T4. II. The role of gene 40 in initiating prehead assembly. Virology 91(1), 15-25 (1978).
    • (1978) Virology , vol.91 , Issue.1 , pp. 15-25
    • Hsiao, C.L.1    Black, L.W.2
  • 44
    • 0018172689 scopus 로고
    • Head morphogenesis of bacteriophage T4. I. Isolation and characterization of gene 40 mutants
    • Hsiao CL, Black LW. Head morphogenesis of bacteriophage T4. I. Isolation and characterization of gene 40 mutants. Virology 91(1), 1-14 (1978).
    • (1978) Virology , vol.91 , Issue.1 , pp. 1-14
    • Hsiao, C.L.1    Black, L.W.2
  • 45
    • 0024388826 scopus 로고
    • Membrane-associated assembly of a phage T4 DNA entrance vertex structure studied with expression vectors
    • Michaud G, Zachary A, Rao VB, Black LW. Membrane-associated assembly of a phage T4 DNA entrance vertex structure studied with expression vectors. J. Mol. Biol. 209(4), 667-681 (1989).
    • (1989) J. Mol. Biol. , vol.209 , Issue.4 , pp. 667-681
    • Michaud, G.1    Zachary, A.2    Rao, V.B.3    Black, L.W.4
  • 46
    • 0000956277 scopus 로고
    • Morphogenesis of the T4 head
    • Karam JD (Ed.). American Society for Microbiology, Washington, DC, USA
    • Black LW, Showe MK, Steven AC. Morphogenesis of the T4 head. In: Molecular Biology of Bacteriophage T4. Karam JD (Ed.). American Society for Microbiology, Washington, DC, USA, 218-258 (1994).
    • (1994) Molecular Biology of Bacteriophage T4 , pp. 218-258
    • Black, L.W.1    Showe, M.K.2    Steven, A.C.3
  • 47
    • 0018184953 scopus 로고
    • Assembly of bacteriophage T4 head-related strucutres. II. in vitro assembly of prehead-like structures
    • Van Driel R, Couture E. Assembly of bacteriophage T4 head-related strucutres. II. In vitro assembly of prehead-like structures. J. Mol. Biol. 123(2), 115-128 (1978).
    • (1978) J. Mol. Biol. , vol.123 , Issue.2 , pp. 115-128
    • Van Driel, R.1    Couture, E.2
  • 48
    • 0018276730 scopus 로고
    • Assembly of the scaffolding core of bacteriophage T4 preheads
    • Van Driel R, Couture E. Assembly of the scaffolding core of bacteriophage T4 preheads. J. Mol. Biol. 123(4), 713-719 (1978).
    • (1978) J. Mol. Biol. , vol.123 , Issue.4 , pp. 713-719
    • Van Driel, R.1    Couture, E.2
  • 49
    • 0023644971 scopus 로고
    • Isolation and reassembly of bacteriophage T4 core proteins
    • Caldentey J, Lepault J, Kellenberger E. Isolation and reassembly of bacteriophage T4 core proteins. J. Mol. Biol. 195(3), 637-647 (1987).
    • (1987) J. Mol. Biol. , vol.195 , Issue.3 , pp. 637-647
    • Caldentey, J.1    Lepault, J.2    Kellenberger, E.3
  • 50
    • 0019747519 scopus 로고
    • Bacteriophage T4 head assembly. in vivo characterization of the morphopoietic core
    • Dubow M (Ed.). Alan R. Liss, Inc., NY. USA
    • Traub F, Maeder M, Kellenberger E. Bacteriophage T4 head assembly. In vivo characterization of the morphopoietic core. In: Bacteriophage Assembly. Dubow M (Ed.). Alan R. Liss, Inc., NY. USA, 127-137 (1981).
    • (1981) Bacteriophage Assembly , pp. 127-137
    • Traub, F.1    Maeder, M.2    Kellenberger, E.3
  • 51
    • 0015808773 scopus 로고
    • Assembly core of bacteriophage T4: An intermediate in head formation
    • Showe MK, Black LW. Assembly core of bacteriophage T4: an intermediate in head formation. Nat. New Biol. 242(116), 70-75 (1973).
    • (1973) Nat. New Biol. , vol.242 , Issue.116 , pp. 70-75
    • Showe, M.K.1    Black, L.W.2
  • 52
    • 0014944179 scopus 로고
    • A factor preventing the major head protein of bacteriophage T4 from random aggregation
    • Laemmli UK, Beguin F, Gujer-Kellenberger G. A factor preventing the major head protein of bacteriophage T4 from random aggregation. J. Mol. Biol. 47(1), 69-85 (1970).
    • (1970) J. Mol. Biol. , vol.47 , Issue.1 , pp. 69-85
    • Laemmli, U.K.1    Beguin, F.2    Gujer-Kellenberger, G.3
  • 53
    • 0014944824 scopus 로고
    • Form-determining function of the genes required for the assembly of the head of bacteriophage T4
    • Laemmli UK, Molbert E, Showe M, Kellenberger E. Form-determining function of the genes required for the assembly of the head of bacteriophage T4. J. Mol. Biol. 49(1), 99-113 (1970).
    • (1970) J. Mol. Biol. , vol.49 , Issue.1 , pp. 99-113
    • Laemmli, U.K.1    Molbert, E.2    Showe, M.3    Kellenberger, E.4
  • 55
    • 0017681093 scopus 로고
    • Studies related to the head-maturation pathway of bacteriophages T4 and T2: II. Nuclear disruption, protein synthesis and particle formation with the mutant 43-.30-.46
    • Wunderli H, Couture E, Vince DA, Kellenberger E. Studies related to the head-maturation pathway of bacteriophages T4 And T2: II. Nuclear disruption, protein synthesis and particle formation with the mutant 43-.30-.46. J. Supramol. Struct. 7(2), 163-190 (1977).
    • (1977) J. Supramol. Struct. , vol.7 , Issue.2 , pp. 163-190
    • Wunderli, H.1    Couture, E.2    Vince, D.A.3    Kellenberger, E.4
  • 56
    • 0018837431 scopus 로고
    • Head maturation pathway of bacteriophages T4 and T2. V. Maturable epsilon-particle accumulating an acridine-treated bacteriophage T4-infected cells
    • Schaerli C, Kellenberger. Head maturation pathway of bacteriophages T4 and T2. V. Maturable epsilon-particle accumulating an acridine-treated bacteriophage T4-infected cells. J. Virol. 33(2), 830-844 (1980).
    • (1980) J. Virol. , vol.33 , Issue.2 , pp. 830-844
    • Schaerli, C.1    Kellenberger2
  • 57
    • 0017804515 scopus 로고
    • Head maturation pathway of bacteriophages T4 and T2. III. Isolation and characterization of particles produced by mutants in gene 17
    • Carrascosa JL, Kellenberger E. Head maturation pathway of bacteriophages T4 and T2. III. Isolation and characterization of particles produced by mutants in gene 17. J. Virol. 25(3), 831-844 (1978).
    • (1978) J. Virol. , vol.25 , Issue.3 , pp. 831-844
    • Carrascosa, J.L.1    Kellenberger, E.2
  • 58
    • 0015848554 scopus 로고
    • Maturation of the head of bacteriophage T4. II. Head-related, aberrant tau-particles
    • Laemmli UK, Johnson RA. Maturation of the head of bacteriophage T4. II. Head-related, aberrant tau-particles. J. Mol. Biol. 80(4), 601-611 (1973).
    • (1973) J. Mol. Biol. , vol.80 , Issue.4 , pp. 601-611
    • Laemmli, U.K.1    Johnson, R.A.2
  • 59
    • 0016360218 scopus 로고
    • Maturation of the head of bacteriophage T4. IV. The proteins of the core of the tubular polyheads and in vitro cleavage of the head proteins
    • Laemmli UK, Quittner SF. Maturation of the head of bacteriophage T4. IV. The proteins of the core of the tubular polyheads and in vitro cleavage of the head proteins. Virology 62(2), 483-499 (1974).
    • (1974) Virology , vol.62 , Issue.2 , pp. 483-499
    • Laemmli, U.K.1    Quittner, S.F.2
  • 60
    • 0017367895 scopus 로고
    • Identification and properties of bacteriophage T4 capsid-formation gene products
    • Castillo CJ, Hsiao CL, Coon P, Black LW. Identification and properties of bacteriophage T4 capsid-formation gene products. J. Mol. Biol. 110(3), 585-601 (1977).
    • (1977) J. Mol. Biol. , vol.110 , Issue.3 , pp. 585-601
    • Castillo, C.J.1    Hsiao, C.L.2    Coon, P.3    Black, L.W.4
  • 61
    • 0017148706 scopus 로고
    • Bacteriophage T4 prehead proteinase. II. Its cleavage from the product of gene 21 and regulation in phage-infected cells
    • Showe MK, Isobe E, Onorato L. Bacteriophage T4 prehead proteinase. II. Its cleavage from the product of gene 21 and regulation in phage-infected cells. J. Mol. Biol. 107(1), 55-69 (1976).
    • (1976) J. Mol. Biol. , vol.107 , Issue.1 , pp. 55-69
    • Showe, M.K.1    Isobe, E.2    Onorato, L.3
  • 62
    • 0017190085 scopus 로고
    • Bacteriophage T4 prehead proteinase. I. Purification and properties of a bacteriophage enzyme which cleaves the capsid precursor proteins
    • Showe MK, Isobe E, Onorato L. Bacteriophage T4 prehead proteinase. I. Purification and properties of a bacteriophage enzyme which cleaves the capsid precursor proteins. J. Mol. Biol. 107(1), 35-54 (1976).
    • (1976) J. Mol. Biol. , vol.107 , Issue.1 , pp. 35-54
    • Showe, M.K.1    Isobe, E.2    Onorato, L.3
  • 63
    • 0017230701 scopus 로고
    • Primary structure of bacteriophage T4 internal protein II and characterization of the cleavage upon phage maturation
    • Isobe T, Black LW, Tsugita A. Primary structure of bacteriophage T4 internal protein II and characterization of the cleavage upon phage maturation. J. Mol. Biol. 102(2), 349-365 (1976).
    • (1976) J. Mol. Biol. , vol.102 , Issue.2 , pp. 349-365
    • Isobe, T.1    Black, L.W.2    Tsugita, A.3
  • 64
    • 0017724734 scopus 로고
    • A mutation which bypasses the requirement for p24 in bacteriophage T4 capsid morphogenesis
    • McNicol LA, Simon LD, Black LW. A mutation which bypasses the requirement for p24 in bacteriophage T4 capsid morphogenesis. J. Mol. Biol. 116(2), 261-283 (1977).
    • (1977) J. Mol. Biol. , vol.116 , Issue.2 , pp. 261-283
    • McNicol, L.A.1    Simon, L.D.2    Black, L.W.3
  • 65
    • 79952264222 scopus 로고    scopus 로고
    • A promiscuous DNA packaging machine from bacteriophage T4
    • Zhang Z, Kottadiel VI, Vafabakhsh R et al. A promiscuous DNA packaging machine from bacteriophage T4. PLoS Biol. 9(2), e1000592 (2011).
    • (2011) PLoS Biol. , vol.9 , Issue.2 , pp. e1000592
    • Zhang, Z.1    Kottadiel, V.I.2    Vafabakhsh, R.3
  • 66
    • 0023933829 scopus 로고
    • Cloning, overexpression and purification of the terminase proteins gp16 and gp17 of bacteriophage T4: Construction of a defined in-vitro DNA packaging system using purified terminase proteins
    • Rao VB, Black LW. Cloning, overexpression and purification of the terminase proteins gp16 and gp17 of bacteriophage T4: construction of a defined in-vitro DNA packaging system using purified terminase proteins. J. Mol. Biol. 200(3), 475-488 (1988).
    • (1988) J. Mol. Biol. , vol.200 , Issue.3 , pp. 475-488
    • Rao, V.B.1    Black, L.W.2
  • 67
    • 57649226492 scopus 로고    scopus 로고
    • The bacteriophage DNA packaging motor
    • Rao VB, Feiss M. The bacteriophage DNA packaging motor. Annu. Rev. Genet. 42, 642-681 (2008).
    • (2008) Annu. Rev. Genet. , vol.42 , pp. 642-681
    • Rao, V.B.1    Feiss, M.2
  • 68
    • 0034619668 scopus 로고    scopus 로고
    • Structure of the bacteriophage f29 DNA packaging motor
    • Simpson AA, Tao Y, Leiman PG et al. Structure of the bacteriophage f29 DNA packaging motor. Nature 408(6813), 745-750 (2000).
    • (2000) Nature , vol.408 , Issue.6813 , pp. 745-750
    • Simpson, A.A.1    Tao, Y.2    Leiman, P.G.3
  • 69
    • 34247268349 scopus 로고    scopus 로고
    • Structural framework for DNA translocation via the viral portal protein
    • Lebedev AA, Krause MH, Isidro AL et al. Structural framework for DNA translocation via the viral portal protein. EMBO J. 26(7), 1984-1994 (2007).
    • (2007) EMBO J. , vol.26 , Issue.7 , pp. 1984-1994
    • Lebedev, A.A.1    Krause, M.H.2    Isidro, A.L.3
  • 71
    • 0024278591 scopus 로고
    • Bacteriophage T3 connector: Three-dimensional structure and comparison with other viral head-tail connecting regions
    • Donate LE, Herranz L, Secilla JP, Carazo JM, Fujisawa H, Carrascosa JL. Bacteriophage T3 connector: three-dimensional structure and comparison with other viral head-tail connecting regions. J. Mol. Biol. 201(1), 91-100 (1988).
    • (1988) J. Mol. Biol. , vol.201 , Issue.1 , pp. 91-100
    • Donate, L.E.1    Herranz, L.2    Secilla, J.P.3    Carazo, J.M.4    Fujisawa, H.5    Carrascosa, J.L.6
  • 72
    • 0026532074 scopus 로고
    • Three-dimensional structure of T3 connector purified from overexpressing bacteria
    • Valpuesta JM, Fujisawa H, Marco S, Carazo JM, Carrascosa JL. Three-dimensional structure of T3 connector purified from overexpressing bacteria. J. Mol. Biol. 224(1), 103-112 (1992).
    • (1992) J. Mol. Biol. , vol.224 , Issue.1 , pp. 103-112
    • Valpuesta, J.M.1    Fujisawa, H.2    Marco, S.3    Carazo, J.M.4    Carrascosa, J.L.5
  • 73
    • 57649228017 scopus 로고    scopus 로고
    • The structure of the phage T4 DNA packaging motor suggests a mechanism dependent on electrostatic forces
    • Sun S, Kondabagil K, Draper B et al. The structure of the phage T4 DNA packaging motor suggests a mechanism dependent on electrostatic forces. Cell 135(7), 1251-1262 (2008).
    • (2008) Cell , vol.135 , Issue.7 , pp. 1251-1262
    • Sun, S.1    Kondabagil, K.2    Draper, B.3
  • 74
    • 0032483313 scopus 로고    scopus 로고
    • Functional analysis of the DNA-packaging/terminase protein gp17 from bacteriophage T4
    • Kuebler D, Rao VB. Functional analysis of the DNA-packaging/terminase protein gp17 from bacteriophage T4. J. Mol. Biol. 281(5), 803-814 (1998).
    • (1998) J. Mol. Biol. , vol.281 , Issue.5 , pp. 803-814
    • Kuebler, D.1    Rao, V.B.2
  • 75
    • 0035976782 scopus 로고    scopus 로고
    • The N-terminal ATPase site in the large terminase protein gp17 is critically required for DNA packaging in bacteriophage T4
    • Rao VB, Mitchell MS. The N-terminal ATPase site in the large terminase protein gp17 is critically required for DNA packaging in bacteriophage T4. J. Mol. Biol. 314(3), 401-411 (2001).
    • (2001) J. Mol. Biol. , vol.314 , Issue.3 , pp. 401-411
    • Rao, V.B.1    Mitchell, M.S.2
  • 76
    • 0016345760 scopus 로고
    • Chemical and biological evolution of a nucleotide-binding protein
    • Rossmann MG, Moras D, Olsen KW. Chemical and biological evolution of a nucleotide-binding protein. Nature 250(463), 194-199 (1974).
    • (1974) Nature , vol.250 , Issue.463 , pp. 194-199
    • Rossmann, M.G.1    Moras, D.2    Olsen, K.W.3
  • 77
    • 4644330957 scopus 로고    scopus 로고
    • The functional domains of bacteriophage T4 terminase
    • Kanamaru S, Kondabagil K, Rossmann MG, Rao VB. The functional domains of bacteriophage T4 terminase. J. Biol. Chem. 279(39), 40795-40801 (2004).
    • (2004) J. Biol. Chem. , vol.279 , Issue.39 , pp. 40795-40801
    • Kanamaru, S.1    Kondabagil, K.2    Rossmann, M.G.3    Rao, V.B.4
  • 78
    • 0031023655 scopus 로고    scopus 로고
    • Purification and characterization of the small subunit of phage T4 terminase, gp16, required for DNA packaging
    • Lin H, Simon MN, Black LW. Purification and characterization of the small subunit of phage T4 terminase, gp16, required for DNA packaging. J. Biol. Chem. 272(6), 3495-3501 (1997).
    • (1997) J. Biol. Chem. , vol.272 , Issue.6 , pp. 3495-3501
    • Lin, H.1    Simon, M.N.2    Black, L.W.3
  • 79
    • 0032030444 scopus 로고    scopus 로고
    • DNA requirements in vivo for phage T4 packaging
    • Lin H, Black LW. DNA requirements in vivo for phage T4 packaging. Virology 242(1), 118-127 (1998).
    • (1998) Virology , vol.242 , Issue.1 , pp. 118-127
    • Lin, H.1    Black, L.W.2
  • 80
    • 69949139694 scopus 로고    scopus 로고
    • The small terminase, gp16, of bacteriophage T4 is a regulator of the DNA packaging motor
    • Al-Zahrani AS, Kondabagil K, Gao S, Kelly N, Ghosh-Kumar M, Rao VB. The small terminase, gp16, of bacteriophage T4 is a regulator of the DNA packaging motor. J. Biol. Chem. 284(36), 24490-24500 (2009).
    • (2009) J. Biol. Chem. , vol.284 , Issue.36 , pp. 24490-24500
    • Al-Zahrani, A.S.1    Kondabagil, K.2    Gao, S.3    Kelly, N.4    Ghosh-Kumar, M.5    Rao, V.B.6
  • 81
    • 0029129145 scopus 로고
    • Virus DNA packaging: The strategy used by phage L
    • Catalano CE, Cue D, Feiss M. Virus DNA packaging: the strategy used by phage l. Mol. Microbiol. 16(6), 1075-1086 (1995).
    • (1995) Mol. Microbiol. , vol.16 , Issue.6 , pp. 1075-1086
    • Catalano, C.E.1    Cue, D.2    Feiss, M.3
  • 82
    • 0029093926 scopus 로고
    • The small subunit of the terminase enzyme of Bacillus subtilis bacteriophage SPP1 forms a specialized nucleoprotein complex with the packaging initiation region
    • Chai S, Lurz R, Alonso JC. The small subunit of the terminase enzyme of Bacillus subtilis bacteriophage SPP1 forms a specialized nucleoprotein complex with the packaging initiation region. J. Mol. Biol. 252(4), 386-398 (1995).
    • (1995) J. Mol. Biol. , vol.252 , Issue.4 , pp. 386-398
    • Chai, S.1    Lurz, R.2    Alonso, J.C.3
  • 83
    • 0019903730 scopus 로고
    • High-frequency transduction of pBR322 by cytosine-substituted T4 bacteriophage: Evidence for encapsulation and transfer of head-to-tail plasmid concatemers
    • Takahashi H, Saito H. High-frequency transduction of pBR322 by cytosine-substituted T4 bacteriophage: evidence for encapsulation and transfer of head-to-tail plasmid concatemers. Plasmid 8(1), 29-35 (1982).
    • (1982) Plasmid , vol.8 , Issue.1 , pp. 29-35
    • Takahashi, H.1    Saito, H.2
  • 84
    • 0018701477 scopus 로고
    • High-frequency generalised transduction by bacteriophage T4
    • Wilson GG, Young KY, Edlin GJ, Konigsberg W. High-frequency generalised transduction by bacteriophage T4. Nature 280(5717), 80-82 (1979).
    • (1979) Nature , vol.280 , Issue.5717 , pp. 80-82
    • Wilson, G.G.1    Young, K.Y.2    Edlin, G.J.3    Konigsberg, W.4
  • 85
    • 84856373698 scopus 로고    scopus 로고
    • Structural basis for DNA recognition and loading into a viral packaging motor
    • Büttner CR, Chechik M, Ortiz-Lombardia M et al. Structural basis for DNA recognition and loading into a viral packaging motor. Proc. Natl Acad. Sci. USA 109(3), 811-816 (2012).
    • (2012) Proc. Natl Acad. Sci. USA , vol.109 , Issue.3 , pp. 811-816
    • Büttner, C.R.1    Chechik, M.2    Ortiz-Lombardia, M.3
  • 86
    • 76649104763 scopus 로고    scopus 로고
    • Crystal structure of the DNA-recognition component of the bacterial virus Sf6 genome-packaging machine
    • Zhao H, Finch CJ, Sequeira RD et al. Crystal structure of the DNA-recognition component of the bacterial virus Sf6 genome-packaging machine. Proc. Natl Acad. Sci. USA 107(5), 1971-1976 (2010).
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , Issue.5 , pp. 1971-1976
    • Zhao, H.1    Finch, C.J.2    Sequeira, R.D.3
  • 87
    • 84856402988 scopus 로고    scopus 로고
    • Structure and function of the small terminase component of the DNA packaging machine in T4-like bacteriophages
    • Sun S, Gao S, Kondabagil K, Xiang Y, Rossmann MG, Rao VB. Structure and function of the small terminase component of the DNA packaging machine in T4-like bacteriophages. Proc. Natl Acad. Sci. USA 109(3), 817-822 (2012).
    • (2012) Proc. Natl Acad. Sci. USA , vol.109 , Issue.3 , pp. 817-822
    • Sun, S.1    Gao, S.2    Kondabagil, K.3    Xiang, Y.4    Rossmann, M.G.5    Rao, V.B.6
  • 88
    • 84867041485 scopus 로고    scopus 로고
    • Structural and functional studies of the phage Sf6 terminase small subunit reveal a DNA-spooling device facilitated by structural plasticity
    • Zhao H, Kamau YN, Christensen TE, Tang L. Structural and functional studies of the phage Sf6 terminase small subunit reveal a DNA-spooling device facilitated by structural plasticity. J. Mol. Biol. 423(3), 413-426 (2012).
    • (2012) J. Mol. Biol. , vol.423 , Issue.3 , pp. 413-426
    • Zhao, H.1    Kamau, Y.N.2    Christensen, T.E.3    Tang, L.4
  • 89
    • 79952802006 scopus 로고    scopus 로고
    • Specificity of interactions among the DNA-packaging machine components of T4-related bacteriophages
    • Gao S, Rao VB. Specificity of interactions among the DNA-packaging machine components of T4-related bacteriophages. J. Biol. Chem. 286(5), 3944-3956 (2011).
    • (2011) J. Biol. Chem. , vol.286 , Issue.5 , pp. 3944-3956
    • Gao, S.1    Rao, V.B.2
  • 90
    • 84858226068 scopus 로고    scopus 로고
    • Structure, assembly, and DNA packaging of the bacteriophage T4 head
    • Black LW, Rao VB. Structure, assembly, and DNA packaging of the bacteriophage T4 head. Adv. Virus Res. 82, 119-153 (2012).
    • (2012) Adv. Virus Res. , vol.82 , pp. 119-153
    • Black, L.W.1    Rao, V.B.2
  • 91
    • 0016378040 scopus 로고
    • The transformation of tau particles into T4 heads. II. Transformations of the surface lattice and related observations on form determination
    • Aebi U, Bijlenga R, van den Broek J et al. The transformation of tau particles into T4 heads. II. Transformations of the surface lattice and related observations on form determination. J. Supramol. Struct. 2(2-4), 253-275 (1974).
    • (1974) J. Supramol. Struct. , vol.2 , Issue.2-4 , pp. 253-275
    • Aebi, U.1    Bijlenga, R.2    Van Den-Broek, J.3
  • 92
    • 0017594878 scopus 로고
    • Capsid fine structure of T-even bacteriophages. Binding and localization of two dispensable capsid proteins into the P23 surface lattice
    • Aebi UR, van Driel R, Bijlenga RKL et al. Capsid fine structure of T-even bacteriophages. Binding and localization of two dispensable capsid proteins into the P23 surface lattice. J. Mol. Biol. 110(4), 687-698 (1977).
    • (1977) J. Mol. Biol. , vol.110 , Issue.4 , pp. 687-698
    • Aebi, U.R.1    Van Driel, R.2    Bijlenga, R.K.L.3
  • 93
    • 0017284902 scopus 로고
    • Folding and capsomere morphology of the P23 surface shell of bacteriophage T4 polyheads from mutants in five different head genes
    • Steven AC, Aebi U, Showe MK. Folding and capsomere morphology of the P23 surface shell of bacteriophage T4 polyheads from mutants in five different head genes. J. Mol. Biol. 102(3), 373-400 (1976).
    • (1976) J. Mol. Biol. , vol.102 , Issue.3 , pp. 373-400
    • Steven, A.C.1    Aebi, U.2    Showe, M.K.3
  • 94
    • 0017200229 scopus 로고
    • Structure of T4 polyheads. II. A pathway of polyhead transformation as a model for T4 capsid maturation
    • Steven AC, Couture E, Aebi U, Showe MK. Structure of T4 polyheads. II. A pathway of polyhead transformation as a model for T4 capsid maturation. J. Mol. Biol. 106(1), 187-221 (1976).
    • (1976) J. Mol. Biol. , vol.106 , Issue.1 , pp. 187-221
    • Steven, A.C.1    Couture, E.2    Aebi, U.3    Showe, M.K.4
  • 95
    • 0001273526 scopus 로고
    • Homing endonucleases
    • Linn SM, Lloyd RS, Roberts RJ (Eds). Cold Spring Harbor Press, NY, USA
    • Mueller JE, Bryk M, Loizos N, Belfort M. Homing endonucleases. In: The Nucleases. Linn SM, Lloyd RS, Roberts RJ (Eds). Cold Spring Harbor Press, NY, USA, 111-143 (1993).
    • (1993) The Nucleases , pp. 111-143
    • Mueller, J.E.1    Bryk, M.2    Loizos, N.3    Belfort, M.4
  • 96
    • 0027085892 scopus 로고
    • Conformational changes of a viral capsid protein. Thermodynamic rationale for proteolytic regulation of bacteriophage T4 capsid expansion, cooperativity, and super-stabilization by soc binding
    • Steven AC, Greenstone HL, Booy FP, Black LW, Ross PD. Conformational changes of a viral capsid protein. Thermodynamic rationale for proteolytic regulation of bacteriophage T4 capsid expansion, cooperativity, and super-stabilization by soc binding. J. Mol. Biol. 228(3), 870-884 (1992).
    • (1992) J. Mol. Biol. , vol.228 , Issue.3 , pp. 870-884
    • Steven, A.C.1    Greenstone, H.L.2    Booy, F.P.3    Black, L.W.4    Ross, P.D.5
  • 97
    • 0016774768 scopus 로고
    • Molecular organization of the shell of the T-even bacteriophage head
    • Ishii T, Yanagida M. Molecular organization of the shell of the T-even bacteriophage head. J. Mol. Biol. 97(4), 655-660 (1975).
    • (1975) J. Mol. Biol. , vol.97 , Issue.4 , pp. 655-660
    • Ishii, T.1    Yanagida, M.2
  • 98
    • 0039538633 scopus 로고
    • Symmetry mismatch and DNA packaging in large bacteriophages
    • Hendrix RW. Symmetry mismatch and DNA packaging in large bacteriophages. Proc. Natl Acad. Sci. USA 75(10), 4779-4783 (1978).
    • (1978) Proc. Natl Acad. Sci. USA , vol.75 , Issue.10 , pp. 4779-4783
    • Hendrix, R.W.1
  • 99
    • 33745190954 scopus 로고    scopus 로고
    • Portal fusion protein constraints on function in DNA packaging of bacteriophage T4
    • Baumann RG, Mullaney J, Black LW. Portal fusion protein constraints on function in DNA packaging of bacteriophage T4. Mol. Microbiol. 61(1), 16-32 (2006).
    • (2006) Mol. Microbiol. , vol.61 , Issue.1 , pp. 16-32
    • Baumann, R.G.1    Mullaney, J.2    Black, L.W.3
  • 100
    • 36749028241 scopus 로고    scopus 로고
    • Single phage T4 DNA packaging motors exhibit large force generation, high velocity, and dynamic variability
    • Fuller DN, Raymer DM, Kottadiel V, Rao VB, Smith DE. Single phage T4 DNA packaging motors exhibit large force generation, high velocity, and dynamic variability. Proc. Natl Acad. Sci. USA 104(43), 16868-16873 (2007).
    • (2007) Proc. Natl Acad. Sci. USA , vol.104 , Issue.43 , pp. 16868-16873
    • Fuller, D.N.1    Raymer, D.M.2    Kottadiel, V.3    Rao, V.B.4    Smith, D.E.5
  • 101
    • 38649114349 scopus 로고    scopus 로고
    • Three-dimensional architecture of the bacteriophage phi29 packaged genome and elucidation of its packaging process
    • Comolli LR, Spakowitz AJ, Siegerist CE et al. Three-dimensional architecture of the bacteriophage phi29 packaged genome and elucidation of its packaging process. Virology 371(2), 267-277 (2008).
    • (2008) Virology , vol.371 , Issue.2 , pp. 267-277
    • Comolli, L.R.1    Spakowitz, A.J.2    Siegerist, C.E.3
  • 102
    • 78649536914 scopus 로고    scopus 로고
    • Morphogenesis of the T4 tail and tail fibers
    • Leiman PG, Arisaka F, van Raaij MJ et al. Morphogenesis of the T4 tail and tail fibers. Virol. J. 7, 355 (2010).
    • (2010) Virol. J. , vol.7 , pp. 355
    • Leiman, P.G.1    Arisaka, F.2    Van Raaij, M.J.3
  • 103
    • 0016621820 scopus 로고
    • Genetic control of bacteriophage T4 baseplate morphogenesis. I. Sequential assembly of the major precursor, in vivo and in vitro
    • Kikuchi Y, King J. Genetic control of bacteriophage T4 baseplate morphogenesis. I. Sequential assembly of the major precursor, in vivo and in vitro. J. Mol. Biol. 99(4), 645-672 (1975).
    • (1975) J. Mol. Biol. , vol.99 , Issue.4 , pp. 645-672
    • Kikuchi, Y.1    King, J.2
  • 104
    • 0016587670 scopus 로고
    • Genetic control of bacteriophage T4 baseplate morphogenesis. II. Mutants unable to form the central part of the baseplate
    • Kikuchi Y, King J. Genetic control of bacteriophage T4 baseplate morphogenesis. II. Mutants unable to form the central part of the baseplate. J. Mol. Biol. 99(4), 673-694 (1975).
    • (1975) J. Mol. Biol. , vol.99 , Issue.4 , pp. 673-694
    • Kikuchi, Y.1    King, J.2
  • 105
    • 0016599239 scopus 로고
    • Genetic control of bacteriophage T4 baseplate morphogenesis. III. Formation of the central plug and overall assembly pathway
    • Kikuchi Y, King J. Genetic control of bacteriophage T4 baseplate morphogenesis. III. Formation of the central plug and overall assembly pathway. J. Mol. Biol. 99(4), 695-716 (1975).
    • (1975) J. Mol. Biol. , vol.99 , Issue.4 , pp. 695-716
    • Kikuchi, Y.1    King, J.2
  • 106
    • 0023850194 scopus 로고
    • Isolation of bacteriophage T4 baseplate proteins P7 and P8 and in vitro formation of the P10/P7/P8 assembly intermediate
    • Plishker MF, Rangwala SH, Berget PB. Isolation of bacteriophage T4 baseplate proteins P7 and P8 and in vitro formation of the P10/P7/P8 assembly intermediate. J. Virol. 62(2), 400-406 (1988).
    • (1988) J. Virol. , vol.62 , Issue.2 , pp. 400-406
    • Plishker, M.F.1    Rangwala, S.H.2    Berget, P.B.3
  • 107
    • 0034677667 scopus 로고    scopus 로고
    • Pulse-chase analysis of the in vivo assembly of the bacteriophage T4 tail
    • Ferguson PL, Coombs DH. Pulse-chase analysis of the in vivo assembly of the bacteriophage T4 tail. J. Mol. Biol. 297(1), 99-117 (2000).
    • (2000) J. Mol. Biol. , vol.297 , Issue.1 , pp. 99-117
    • Ferguson, P.L.1    Coombs, D.H.2
  • 108
    • 73149122099 scopus 로고    scopus 로고
    • The baseplate wedges of bacteriophage T4 spontaneously assemble into hubless baseplate-like structure in vitro
    • Yap ML, Mio K, Leiman PG, Kanamaru S, Arisaka F. The baseplate wedges of bacteriophage T4 spontaneously assemble into hubless baseplate-like structure in vitro. J. Mol. Biol. 395(2), 349-360 (2010).
    • (2010) J. Mol. Biol. , vol.395 , Issue.2 , pp. 349-360
    • Yap, M.L.1    Mio, K.2    Leiman, P.G.3    Kanamaru, S.4    Arisaka, F.5
  • 109
    • 0028307501 scopus 로고
    • Tail length determination in bacteriophage T4
    • Abuladze NK, Gingery M, Tsai J, Eiserling FA. Tail length determination in bacteriophage T4. Virology 199(2), 301-310 (1994).
    • (1994) Virology , vol.199 , Issue.2 , pp. 301-310
    • Abuladze, N.K.1    Gingery, M.2    Tsai, J.3    Eiserling, F.A.4
  • 111
    • 0037203891 scopus 로고    scopus 로고
    • Structure of the cell-puncturing device of bacteriophage T4
    • Kanamaru S, Leiman PG, Kostyuchenko VA et al. Structure of the cell-puncturing device of bacteriophage T4. Nature 415(6871), 553-557 (2002).
    • (2002) Nature , vol.415 , Issue.6871 , pp. 553-557
    • Kanamaru, S.1    Leiman, P.G.2    Kostyuchenko, V.A.3
  • 115
    • 0035861998 scopus 로고    scopus 로고
    • Crystal structure of a heat and protease-stable part of the bacteriophage T4 short tail fibre
    • Van Raaij MJ, Schoehn G, Burda MR, Miller S. Crystal structure of a heat and protease-stable part of the bacteriophage T4 short tail fibre. J. Mol. Biol. 314(5), 1137-1146 (2001).
    • (2001) J. Mol. Biol. , vol.314 , Issue.5 , pp. 1137-1146
    • Van Raaij, M.J.1    Schoehn, G.2    Burda, M.R.3    Miller, S.4
  • 116
    • 0042463705 scopus 로고    scopus 로고
    • Thestructure of the receptor-binding domain of the bacteriophage T4 short tail fibre reveals a knitted trimeric metal-binding fold
    • Thomassen E, Gielen G, Schutz M et al. Thestructure of the receptor-binding domain of the bacteriophage T4 short tail fibre reveals a knitted trimeric metal-binding fold. J. Mol. Biol. 331(2), 361-373 (2003).
    • (2003) J. Mol. Biol. , vol.331 , Issue.2 , pp. 361-373
    • Thomassen, E.1    Gielen, G.2    Schutz, M.3
  • 118
    • 66749084492 scopus 로고    scopus 로고
    • The structure of gene product 6 of bacteriophage T4, the hinge-pin of the baseplate
    • Aksyuk AA, Leiman PG, Shneider MM, Mesyanzhinov VV, Rossmann MG. The structure of gene product 6 of bacteriophage T4, the hinge-pin of the baseplate. Structure 17(6), 800-808 (2009).
    • (2009) Structure , vol.17 , Issue.6 , pp. 800-808
    • Aksyuk, A.A.1    Leiman, P.G.2    Shneider, M.M.3    Mesyanzhinov, V.V.4    Rossmann, M.G.5
  • 119
    • 0013852463 scopus 로고
    • Structure of hen egg-white lysozyme. A three-dimensional Fourier synthesis at 2 Å resolution
    • Blake CCF, Koenig DF, Mair GA, North ACT, Phillips DC, Sarma VR. Structure of hen egg-white lysozyme. A three-dimensional Fourier synthesis at 2 Å resolution. Nature 206(4986), 757-761 (1965).
    • (1965) Nature , vol.206 , Issue.4986 , pp. 757-761
    • Blake, C.C.F.1    Koenig, D.F.2    Mair, G.A.3    North, A.C.T.4    Phillips, D.C.5    Sarma, V.R.6
  • 120
    • 0032925288 scopus 로고    scopus 로고
    • The C-terminal fragment of the precursor tail lysozyme of bacteriophage T4 stays as a structural component of the baseplate after cleavage
    • Kanamaru S, Gassner NC, Ye N, Takeda S, Arisaka F. The C-terminal fragment of the precursor tail lysozyme of bacteriophage T4 stays as a structural component of the baseplate after cleavage. J. Bacteriol. 181, 2739-2744 (1999).
    • (1999) J. Bacteriol. , vol.181 , pp. 2739-2744
    • Kanamaru, S.1    Gassner, N.C.2    Ye, N.3    Takeda, S.4    Arisaka, F.5
  • 121
    • 13444283414 scopus 로고    scopus 로고
    • Control of bacteriophage T4 tail lysozyme activity during the infection process
    • Kanamaru S, Ishiwata Y, Suzuki T, Rossmann MG, Arisaka F. Control of bacteriophage T4 tail lysozyme activity during the infection process. J. Mol. Biol. 346, 1013-1020 (2005).
    • (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
  • 122
    • 84881666828 scopus 로고    scopus 로고
    • PAAR-repeat proteins sharpen and diversify the type VI secretion system spike
    • Shneider MM, Buth SA, Ho BT, Basler M, Mekalanos JJ, Leiman PG. PAAR-repeat proteins sharpen and diversify the type VI secretion system spike. Nature 500(7462), 350-353 (2013).
    • (2013) Nature , vol.500 , Issue.7462 , pp. 350-353
    • Shneider, M.M.1    Buth, S.A.2    Ho, B.T.3    Basler, M.4    Mekalanos, J.J.5    Leiman, P.G.6
  • 123
    • 65449163376 scopus 로고    scopus 로고
    • The tail sheath structure of bacteriophage T4: A molecular machine for infecting bacteria
    • Aksyuk AA, Leiman PG, Kurochkina LP et al. The tail sheath structure of bacteriophage T4: a molecular machine for infecting bacteria. EMBO J. 28(7), 821-829 (2009).
    • (2009) EMBO J. , vol.28 , Issue.7 , pp. 821-829
    • Aksyuk, A.A.1    Leiman, P.G.2    Kurochkina, L.P.3
  • 124
    • 84877576710 scopus 로고    scopus 로고
    • Themolecular architecture of the bacterio-phage T4 neck
    • Fokine A, Zhang Z, Kanamaru S et al. Themolecular architecture of the bacterio-phage T4 neck. J. Mol. Biol. 425(10), 1731-1744 (2013).
    • (2013) J. Mol. Biol. , vol.425 , Issue.10 , pp. 1731-1744
    • Fokine, A.1    Zhang, Z.2    Kanamaru, S.3
  • 125
    • 0029957949 scopus 로고    scopus 로고
    • Characterization of the helper proteins for the assembly of tail fibers of coliphages T4 and L
    • Hashemolhosseini S, Stierhof YD, Hindennach I, Henning U. Characterization of the helper proteins for the assembly of tail fibers of coliphages T4 and l. J. Bacteriol. 178(21), 6258-6265 (1996).
    • (1996) J. Bacteriol. , vol.178 , Issue.21 , pp. 6258-6265
    • Hashemolhosseini, S.1    Stierhof, Y.D.2    Hindennach, I.3    Henning, U.4
  • 126
    • 0014674116 scopus 로고
    • Assembly of bacteriophage T4 tail fibers: The sequence of gene product interaction
    • King J, Wood WB. Assembly of bacteriophage T4 tail fibers: the sequence of gene product interaction. J. Mol. Biol. 39(3), 583-601 (1969).
    • (1969) J. Mol. Biol. , vol.39 , Issue.3 , pp. 583-601
    • King, J.1    Wood, W.B.2
  • 127
    • 0030564888 scopus 로고    scopus 로고
    • Stoichiometry and domainal organization of the long tail-fiber of bacteriophage T4: A hinged viral adhesin
    • Cerritelli ME, Wall JS, Simon MN, Conway JF, Steven AC. Stoichiometry and domainal organization of the long tail-fiber of bacteriophage T4: a hinged viral adhesin. J. Mol. Biol. 260(5), 767-780 (1996).
    • (1996) J. Mol. Biol. , vol.260 , Issue.5 , pp. 767-780
    • Cerritelli, M.E.1    Wall, J.S.2    Simon, M.N.3    Conway, J.F.4    Steven, A.C.5
  • 128
    • 78650549528 scopus 로고    scopus 로고
    • Structure of the bacteriophage T4 long tail fiber receptor-binding tip
    • Bartual SG, Otero JM, Garcia-Doval C et al. Structure of the bacteriophage T4 long tail fiber receptor-binding tip. Proc. Natl Acad. Sci. USA 107(47), 20287-20292 (2010).
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , Issue.47 , pp. 20287-20292
    • Bartual, S.G.1    Otero, J.M.2    Garcia-Doval, C.3
  • 129
    • 0025641363 scopus 로고
    • Receptor-recognizing proteins of T-even type bacteriophages. The receptor-recognizing area of proteins 37 of phages T4 TuIa and TuIb
    • Montag D, Hashemolhosseini S, Henning U. Receptor-recognizing proteins of T-even type bacteriophages. The receptor-recognizing area of proteins 37 of phages T4 TuIa and TuIb. J. Mol. Biol. 216(2), 327-334 (1990).
    • (1990) J. Mol. Biol. , vol.216 , Issue.2 , pp. 327-334
    • Montag, D.1    Hashemolhosseini, S.2    Henning, U.3
  • 130
    • 0017650024 scopus 로고
    • Studies on the structure, protein composition and assembly of the neck of bacteriophage T4
    • Coombs DH, Eiserling FA. Studies on the structure, protein composition and assembly of the neck of bacteriophage T4. J. Mol. Biol. 116(3), 375-405 (1977).
    • (1977) J. Mol. Biol. , vol.116 , Issue.3 , pp. 375-405
    • Coombs, D.H.1    Eiserling, F.A.2
  • 131
    • 0031570687 scopus 로고    scopus 로고
    • Structure of bacteriophage T4 fibritin: A segmented coiled coil and the role of the C-terminal domain
    • Tao Y, Strelkov SV, Mesyanzhinov VV, Rossmann MG. Structure of bacteriophage T4 fibritin: a segmented coiled coil and the role of the C-terminal domain. Structure 5(6), 789-798 (1997).
    • (1997) Structure , vol.5 , Issue.6 , pp. 789-798
    • Tao, Y.1    Strelkov, S.V.2    Mesyanzhinov, V.V.3    Rossmann, M.G.4
  • 133
    • 2542468691 scopus 로고    scopus 로고
    • Design and crystal structure of bacteriophage T4 mini-fibritin NCCF
    • Boudko SP, Strelkov SV, Engel J, Stetefeld J. Design and crystal structure of bacteriophage T4 mini-fibritin NCCF. J. Mol. Biol. 339(4), 927-935 (2004).
    • (2004) J. Mol. Biol. , vol.339 , Issue.4 , pp. 927-935
    • Boudko, S.P.1    Strelkov, S.V.2    Engel, J.3    Stetefeld, J.4
  • 134
    • 0027946253 scopus 로고
    • Fibritin encoded by bacteriophage T4 gene wac has a parallel triple-stranded a-helical coiled-coil structure
    • Efimov VP, Nepluev IV, Sobolev BN et al. Fibritin encoded by bacteriophage T4 gene wac has a parallel triple-stranded a-helical coiled-coil structure. J. Mol. Biol. 242(4), 470-486 (1994).
    • (1994) J. Mol. Biol. , vol.242 , Issue.4 , pp. 470-486
    • Efimov, V.P.1    Nepluev, I.V.2    Sobolev, B.N.3
  • 135
    • 0033160840 scopus 로고    scopus 로고
    • The carboxy-terminal domain initiates trimerization of bacteriophage T4 fibritin
    • Letarov AV, Londer YY, Boudko SP, Mesyanzhinov VV. The carboxy-terminal domain initiates trimerization of bacteriophage T4 fibritin. Biochemistry (Mosc.) 64(7), 817-823 (1999).
    • (1999) Biochemistry (Mosc.) , vol.64 , Issue.7 , pp. 817-823
    • Letarov, A.V.1    Londer, Y.Y.2    Boudko, S.P.3    Mesyanzhinov, V.V.4
  • 136
    • 0016834742 scopus 로고
    • Bacteriophage T4 whiskers: A rudimentary environment-sensing device
    • Conley MP, Wood WB. Bacteriophage T4 whiskers: a rudimentary environment-sensing device. Proc. Natl Acad. Sci. USA 72(9), 3701-3705 (1975).
    • (1975) Proc. Natl Acad. Sci. USA , vol.72 , Issue.9 , pp. 3701-3705
    • Conley, M.P.1    Wood, W.B.2
  • 137
    • 33947281384 scopus 로고    scopus 로고
    • The structure of the ATPase that powers DNA packaging into bacteriophage T4 procapsids
    • Sun S, Kondabagil K, Gentz PM, Rossmann MG, Rao VB. The structure of the ATPase that powers DNA packaging into bacteriophage T4 procapsids. Mol. Cell 25(6), 943-949 (2007).
    • (2007) Mol. Cell , vol.25 , Issue.6 , pp. 943-949
    • Sun, S.1    Kondabagil, K.2    Gentz, P.M.3    Rossmann, M.G.4    Rao, V.B.5
  • 138
  • 139
    • 0038419606 scopus 로고    scopus 로고
    • Bacteriophage f29 scaffolding protein gp7 before and after prohead assembly
    • Morais MC, Kanamaru S, Badasso MO et al. Bacteriophage f29 scaffolding protein gp7 before and after prohead assembly. Nat. Struct. Biol. 10, 572-576 (2003).
    • (2003) Nat. Struct. Biol. , vol.10 , pp. 572-576
    • Morais, M.C.1    Kanamaru, S.2    Badasso, M.O.3
  • 140
    • 7644228864 scopus 로고    scopus 로고
    • Structure and polymorphism of the UL6 portal protein of herpes simplex virus type 1
    • Trus BL, Cheng N, Newcomb WW, Homa FL, Brown JC, Steven AC. Structure and polymorphism of the UL6 portal protein of herpes simplex virus type 1. J. Virol. 78(22), 12668-12671 (2004).
    • (2004) J. Virol. , vol.78 , Issue.22 , pp. 12668-12671
    • Trus, B.L.1    Cheng, N.2    Newcomb, W.W.3    Homa, F.L.4    Brown, J.C.5    Steven, A.C.6
  • 141
    • 34848887124 scopus 로고    scopus 로고
    • Cryo-electron microscopy study of bacteriophage T4 displaying anthrax toxin proteins
    • Fokine A, Bowman VD, Battisti AJ et al. Cryo-electron microscopy study of bacteriophage T4 displaying anthrax toxin proteins. Virology 367(2), 422-427 (2007).
    • (2007) Virology , vol.367 , Issue.2 , pp. 422-427
    • Fokine, A.1    Bowman, V.D.2    Battisti, A.J.3
  • 142
    • 0029839322 scopus 로고    scopus 로고
    • Phage display of intact domains at high copy number: A system based on SOC, the small outer capsid protein of bacteriophage T4
    • Ren ZJ, Lewis GK, Wingfield PT, Locke EG, Steven AC, Black LW. Phage display of intact domains at high copy number: a system based on SOC, the small outer capsid protein of bacteriophage T4. Protein Sci. 5(9), 1833-1843 (1996).
    • (1996) Protein Sci. , vol.5 , Issue.9 , pp. 1833-1843
    • Ren, Z.J.1    Lewis, G.K.2    Wingfield, P.T.3    Locke, E.G.4    Steven, A.C.5    Black, L.W.6
  • 143
    • 39749183406 scopus 로고    scopus 로고
    • Orally delivered foot-and-mouth disease virus capsid protomer vaccine displayed on T4 bacteriophage surface: 100% protection from potency challenge in mice
    • Ren ZJ, Tian CJ, Zhu QS et al. Orally delivered foot-and-mouth disease virus capsid protomer vaccine displayed on T4 bacteriophage surface: 100% protection from potency challenge in mice. Vaccine 26(11), 1471-1481 (2008).
    • (2008) Vaccine , vol.26 , Issue.11 , pp. 1471-1481
    • Ren, Z.J.1    Tian, C.J.2    Zhu, Q.S.3
  • 144
    • 0030833999 scopus 로고    scopus 로고
    • Display of a PorA peptide from Neisseria meningitidis on the bacteriophage T4 capsid surface
    • Jiang J, Abu-Shilbayeh L, Rao VB. Display of a PorA peptide from Neisseria meningitidis on the bacteriophage T4 capsid surface. Infect. Immun. 65(11), 4770-4777 (1997).
    • (1997) Infect. Immun. , vol.65 , Issue.11 , pp. 4770-4777
    • Jiang, J.1    Abu-Shilbayeh, L.2    Rao, V.B.3
  • 145
    • 33746190697 scopus 로고    scopus 로고
    • Assembly of human immunodeficiency virus (HIV) antigens on bacteriophage T4: A novel in vitro approach to construct multicomponent HIV vaccines
    • Sathaliyawala T, Rao M, Maclean DM, Birx DL, Alving CR, Rao VB. Assembly of human immunodeficiency virus (HIV) antigens on bacteriophage T4: a novel in vitro approach to construct multicomponent HIV vaccines. J. Virol. 80(15), 7688-7698 (2006).
    • (2006) J. Virol. , vol.80 , Issue.15 , pp. 7688-7698
    • Sathaliyawala, T.1    Rao, M.2    MacLean, D.M.3    Birx, D.L.4    Alving, C.R.5    Rao, V.B.6
  • 146
    • 33845219639 scopus 로고    scopus 로고
    • Bacteriophage T4 nanoparticle capsid surface SOC and HOC bipartite display with enhanced classical swine fever virus immunogenicity: A powerful immunological approach
    • Wu J, Tu C, Yu X et al. Bacteriophage T4 nanoparticle capsid surface SOC and HOC bipartite display with enhanced classical swine fever virus immunogenicity: a powerful immunological approach. J. Virol. Methods 139(1), 50-60 (2007).
    • (2007) J. Virol. Methods , vol.139 , Issue.1 , pp. 50-60
    • Wu, J.1    Tu, C.2    Yu, X.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.