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Volumn 726, Issue , 2012, Pages 511-547

The dsDNA packaging motor in bacteriophage ø29

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE; CAPSID PROTEIN; DOUBLE STRANDED DNA; MOLECULAR MOTOR; VIRUS DNA;

EID: 84858193894     PISSN: 00652598     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-1-4614-0980-9_23     Document Type: Article
Times cited : (33)

References (123)
  • 2
    • 0028114231 scopus 로고
    • Structure at 2.8 A resolution of F1-ATPase from bovine heart mitochondria
    • Abrahams JP, Leslie AG, Lutter R, Walker JE (1994) Structure at 2.8 A resolution of F1-ATPase from bovine heart mitochondria. Nature 370(6491):621-628
    • (1994) Nature , vol.370 , Issue.6491 , pp. 621-628
    • Abrahams, J.P.1    Leslie, A.G.2    Lutter, R.3    Walker, J.E.4
  • 3
    • 34147110201 scopus 로고    scopus 로고
    • Quasi-Atomic Model of Bacteriophage T7 Procapsid Shell: Insights into the Structure and Evolution of a Basic Fold
    • DOI 10.1016/j.str.2007.03.004, PII S0969212607001116
    • Agirrezabala X, Velazquez-Muriel JA, Gomez-Puertas P, Scheres SH, Carazo JM, Carrascosa JL (2007) Quasi-atomic model of bacteriophage t7 procapsid shell: insights into the structure and evolution of a basic fold. Structure 15(4): 461-472 (Pubitemid 46553832)
    • (2007) Structure , vol.15 , Issue.4 , pp. 461-472
    • Agirrezabala, X.1    Velazquez-Muriel, J.A.2    Gomez-Puertas, P.3    Scheres, S.H.W.4    Carazo, J.M.5    Carrascosa, J.L.6
  • 5
    • 34247356107 scopus 로고    scopus 로고
    • Alanine Scanning and Fe-BABE Probing of the Bacteriophage ø29 Prohead RNA-Connector Interaction
    • DOI 10.1016/j.jmb.2007.03.033, PII S0022283607003750
    • Atz R, Ma S, Gao J, Anderson DL, Grimes S (2007) Alanine scanning and Fe-BABE probing of the bacteriophage '29 prohead RNA-connector interaction. J Mol Biol 369(1):239-248 (Pubitemid 46635444)
    • (2007) Journal of Molecular Biology , vol.369 , Issue.1 , pp. 239-248
    • Atz, R.1    Ma, S.2    Gao, J.3    Anderson, D.L.4    Grimes, S.5
  • 7
    • 0032712359 scopus 로고    scopus 로고
    • Adding the third dimension to virus life cycles: Three-dimensional reconstruction of icosahedral viruses from cryo-electron micrographs
    • table of contents
    • Baker TS, Olson NH, Fuller SD (1999) Adding the third dimension to virus life cycles: three-dimensional reconstruction of icosahedral viruses from cryo-electron micrographs. Microbiol Mol Biol Rev 63(4):862-922, table of contents
    • (1999) Microbiol Mol Biol Rev , vol.63 , Issue.4 , pp. 862-922
    • Baker, T.S.1    Olson, N.H.2    Fuller, S.D.3
  • 8
    • 33745190954 scopus 로고    scopus 로고
    • Portal fusion protein constraints on function in DNA packaging of bacteriophage T4
    • Baumann RG, Mullaney J, Black LW (2006) Portal fusion protein constraints on function in DNA packaging of bacteriophage T4. Mol Microbiol 61(1):16-32
    • (2006) Mol Microbiol , vol.61 , Issue.1 , pp. 16-32
    • Baumann, R.G.1    Mullaney, J.2    Black, L.W.3
  • 9
    • 0020694653 scopus 로고
    • Morphogenesis of bacteriophage φ29 of Bacillus subtilis: Oriented and quantized in vitro packaging of DNA protein gp3
    • Bjornsti MA, Reilly BE, Anderson DL (1983) Morphogenesis of bacteriophage phi 29 of Bacillus subtilis : oriented and quantized in vitro packaging of DNA protein gp3. J Virol 45(1):383-396 (Pubitemid 13166313)
    • (1983) Journal of Virology , vol.45 , Issue.1 , pp. 383-396
    • Bjornsti, M.A.1    Reilly, B.E.2    Anderson, D.L.3
  • 10
    • 0021269756 scopus 로고
    • Bacteriophage φ29 proteins required for in vitro DNA-gp3 packaging
    • Bjornsti MA, Reilly BE, Anderson DL (1984) Bacteriophage phi 29 proteins required for in vitro DNA-gp3 packaging. J Virol 50(3):766-772 (Pubitemid 14104261)
    • (1984) Journal of Virology , vol.50 , Issue.3 , pp. 766-772
    • Bjornsti, M.A.1    Reilly, B.E.2    Anderson, D.L.3
  • 11
    • 0029879312 scopus 로고    scopus 로고
    • Relating structure to function in φ29 DNA polymerase
    • DOI 10.1074/jbc.271.15.8509
    • Blanco L, Salas M (1996) Relating structure to function in phi29 DNA polymerase. J Biol Chem 271(15):8509-8512 (Pubitemid 26123264)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.15 , pp. 8509-8512
    • Blanco, L.1    Salas, M.2
  • 12
    • 0034659905 scopus 로고    scopus 로고
    • 2+ADP and aluminium fluoride
    • DOI 10.1016/S0969-2126(00)00145-3
    • Braig K, Menz RI, Montgomery MG, Leslie AG, Walker JE (2000) Structure of bovine mitochondrial F(1)-ATPase inhibited by Mg(2+) ADP and aluminium fl uoride. Structure 8(6):567-573 (Pubitemid 30409309)
    • (2000) Structure , vol.8 , Issue.6 , pp. 567-573
    • Braig, K.1    Menz, R.I.2    Montgomery, M.G.3    Leslie, A.G.4    Walker, J.E.5
  • 13
    • 48749086251 scopus 로고    scopus 로고
    • Comparative genomics and evolutionary trajectories of viral ATP dependent DNA-packaging systems
    • Burroughs AM, Iyer LM, Aravind L (2007) Comparative genomics and evolutionary trajectories of viral ATP dependent DNA-packaging systems. Genome Dyn 3:48-65
    • (2007) Genome Dyn , vol.3 , pp. 48-65
    • Burroughs, A.M.1    Iyer, L.M.2    Aravind, L.3
  • 14
    • 0017594208 scopus 로고
    • Assembly of Bacillus subtilis phage Phi29. 1. Mutants in the cistrons coding for the structural proteins
    • Camacho A, Jimenez F, De La Torre J, Carrascosa JL, Mellado RP, Vasquez C, Vinuela E, Salas M (1977) Assembly of Bacillus subtilis phage phi29. 1. Mutants in the cistrons coding for the structural proteins. Eur J Biochem 73(1):39-55 (Pubitemid 8044262)
    • (1977) European Journal of Biochemistry , vol.73 , Issue.1 , pp. 39-55
    • Camacho, A.1    Jimenez, F.2    De La Torre, J.3
  • 15
    • 24144478521 scopus 로고    scopus 로고
    • Mechanism of force generation of a viral DNA packaging motor
    • DOI 10.1016/j.cell.2005.06.024, PII S0092867405006434
    • Chemla YR, Aathavan K, Michaelis J, Grimes S, Jardine PJ, Anderson DL, Bustamante C (2005) Mechanism of force generation of a viral DNA packaging motor. Cell 122(5):683-692 (Pubitemid 41242634)
    • (2005) Cell , vol.122 , Issue.5 , pp. 683-692
    • Chemla, Y.R.1    Aathavan, K.2    Michaelis, J.3    Grimes, S.4    Jardine, P.J.5    Anderson, D.L.6    Bustamante, C.7
  • 16
    • 0032981057 scopus 로고    scopus 로고
    • Sequence requirement for hand-in-hand interaction in formation of RNA dimers and hexamers to gear φ29 DNA translocation motor
    • DOI 10.1017/S1355838299990350
    • Chen C, Zhang C, Guo P (1999) Sequence requirement for hand-in-hand interaction in formation of RNA dimers and hexamers to gear phi29 DNA translocation motor. RNA 5(6):805-818 (Pubitemid 29283782)
    • (1999) RNA , vol.5 , Issue.6 , pp. 805-818
    • Chen, C.1    Zhang, C.2    Guo, P.3
  • 17
    • 0034625371 scopus 로고    scopus 로고
    • A dimer as a building block in assembling RNA: A hexamer that gears bacterial virus phi29 DNA-translocating machinery
    • DOI 10.1074/jbc.M909662199
    • Chen C, Sheng S, Shao Z, Guo P (2000) A dimer as a building block in assembling RNA. A hexamer that gears bacterial virus phi29 DNA-translocating machinery. J Biol Chem 275(23):17510-17516 (Pubitemid 30430792)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.23 , pp. 17510-17516
    • Chen, C.1    Sheng, S.2    Shao, Z.3    Guo, P.4
  • 20
    • 77749279748 scopus 로고    scopus 로고
    • Three-dimensional structure of tropism-switching Bordetella bacteriophage
    • Dai W, Hodes A, Hui WH, Gingery M, Miller JF, Zhou ZH (2010) Three-dimensional structure of tropism-switching Bordetella bacteriophage. Proc Natl Acad Sci USA 107(9):4347-4352
    • (2010) Proc Natl Acad Sci USA , vol.107 , Issue.9 , pp. 4347-4352
    • Dai, W.1    Hodes, A.2    Hui, W.H.3    Gingery, M.4    Miller, J.F.5    Zh, Z.6
  • 22
    • 34247368838 scopus 로고    scopus 로고
    • An ATP Hydrolysis Sensor in the DNA Packaging Motor from Bacteriophage T4 Suggests an Inchworm-Type Translocation Mechanism
    • DOI 10.1016/j.jmb.2007.03.019, PII S0022283607003439
    • Draper B, Rao VB (2007) An ATP hydrolysis sensor in the DNA packaging motor from bacteriophage T4 suggests an inchworm-type translocation mechanism. J Mol Biol 369(1):79-94 (Pubitemid 46635439)
    • (2007) Journal of Molecular Biology , vol.369 , Issue.1 , pp. 79-94
    • Draper, B.1    Rao, V.B.2
  • 23
    • 0018932980 scopus 로고
    • DNA packaging by the double-stranded DNA bacteriophages
    • Earnshaw WC, Casjens SR (1980) DNA packaging by the double-stranded DNA bacteriophages. Cell 21(2):319-331 (Pubitemid 10047085)
    • (1980) Cell , vol.21 , Issue.2 , pp. 319-331
    • Earnshaw, W.C.1    Casjens, S.R.2
  • 26
    • 70350128857 scopus 로고    scopus 로고
    • In vitro incorporation of the phage Phi29 connector complex
    • Fu CY, Prevelige PE Jr (2009) In vitro incorporation of the phage Phi29 connector complex. Virology 394(1):149-153
    • (2009) Virology , vol.394 , Issue.1 , pp. 149-153
    • Fu, C.Y.1    Prevelige Jr., P.E.2
  • 28
    • 0030817119 scopus 로고    scopus 로고
    • Boundary of pRNA functional domains and minimum pRNA sequence requirement for specifi c connector binding and DNA packaging of phage phi29
    • Garver K, Guo P (1997) Boundary of pRNA functional domains and minimum pRNA sequence requirement for specifi c connector binding and DNA packaging of phage phi29. RNA 3(9):1068-1079
    • (1997) RNA , vol.3 , Issue.9 , pp. 1068-1079
    • Garver, K.1    Guo, P.2
  • 30
    • 0024428084 scopus 로고
    • In vitro packaging of bacteriophage Φ29 DNA restriction fragments and the role of the terminal protein gp3
    • DOI 10.1016/0022-2836(89)90172-1
    • Grimes S, Anderson D (1989) In vitro packaging of bacteriophage phi 29 DNA restriction fragments and the role of the terminal protein gp3. J Mol Biol 209(1):91-100 (Pubitemid 19237809)
    • (1989) Journal of Molecular Biology , vol.209 , Issue.1 , pp. 91-100
    • Grimes, S.1    Anderson, D.2
  • 31
    • 0025028872 scopus 로고
    • RNA dependence of the bacteriophage Φ29 DNA packaging ATPase
    • Grimes S, Anderson D (1990) RNA dependence of the bacteriophage phi 29 DNA packaging ATPase. J Mol Biol 215(4):559-566 (Pubitemid 20361392)
    • (1990) Journal of Molecular Biology , vol.215 , Issue.4 , pp. 559-566
    • Grimes, S.1    Anderson, D.2
  • 33
    • 0036301072 scopus 로고    scopus 로고
    • Detailed architecture of a DNA translocating machine: The high-resolution structure of the bacteriophage φ29 connector particle
    • DOI 10.1006/jmbi.2001.5278
    • Guasch A, Pous J, Ibarra B, Gomis-Ruth FX, Valpuesta JM, Sousa N, Carrascosa JL, Coll M (2002) Detailed architecture of a DNA translocating machine: the high-resolution structure of the bacteriophage phi29 connector particle. J Mol Biol 315(4):663-676 (Pubitemid 34729317)
    • (2002) Journal of Molecular Biology , vol.315 , Issue.4 , pp. 663-676
    • Guasch, A.1    Pous, J.2    Ibarra, B.3    Gomis-Ruth, F.X.4    Valpuesta, J.M.5    Sousa, N.6    Carrascosa, J.L.7    Coll, M.8
  • 35
    • 0023660929 scopus 로고
    • Initiation events in in-vitro packaging of bacteriophage phi 29 DNA-gp3
    • Guo P, Peterson C, Anderson D (1987a) Initiation events in in-vitro packaging of bacteriophage phi 29 DNA-gp3. J Mol Biol 197(2):219-228
    • (1987) J Mol Biol , vol.197 , Issue.2 , pp. 219-228
    • Guo, P.1    Peterson, C.2    Anderson, D.3
  • 36
    • 0023660940 scopus 로고
    • Prohead and DNA-gp3-dependent ATPase activity of the DNA packaging protein gp16 of bacteriophage phi 29
    • Guo P, Peterson C, Anderson D (1987b) Prohead and DNA-gp3-dependent ATPase activity of the DNA packaging protein gp16 of bacteriophage phi 29. J Mol Biol 197(2):229-236
    • (1987) J Mol Biol , vol.197 , Issue.2 , pp. 229-236
    • Guo, P.1    Peterson, C.2    Anderson, D.3
  • 37
    • 0025923286 scopus 로고
    • Regulation of the phage phi 29 prohead shape and size by the portal vertex
    • Guo PX, Erickson S, Xu W, Olson N, Baker TS, Anderson D (1991a) Regulation of the phage phi 29 prohead shape and size by the portal vertex. Virology 183(1):366-373
    • (1991) Virology , vol.183 , Issue.1 , pp. 366-373
    • Guo, P.X.1    Erickson, S.2    Xu, W.3    Olson, N.4    Baker, T.S.5    Anderson, D.6
  • 38
    • 0025925179 scopus 로고
    • SRNA of phage phi 29 of Bacillus subtilis mediates DNA packaging of phi 29 proheads assembled in Escherichia coli
    • Guo PX, Rajagopal BS, Anderson D, Erickson S, Lee CS (1991b) sRNA of phage phi 29 of Bacillus subtilis mediates DNA packaging of phi 29 proheads assembled in Escherichia coli. Virology 185(1):395-400
    • (1991) Virology , vol.185 , Issue.1 , pp. 395-400
    • Guo, P.X.1    Rajagopal, B.S.2    Anderson, D.3    Erickson, S.4    Lee, C.S.5
  • 39
    • 0032110708 scopus 로고    scopus 로고
    • Inter-RNA interaction of phage θ29 pRNA to form a hexameric complex for viral DNA transportation
    • Guo P, Zhang C, Chen C, Garver K, Trottier M (1998) Inter-RNA interaction of phage phi29 pRNA to form a hexameric complex for viral DNA transportation. Mol Cell 2(1):149-155 (Pubitemid 128378977)
    • (1998) Molecular Cell , vol.2 , Issue.1 , pp. 149-155
    • Guo, P.1    Zhang, C.2    Chen, C.3    Garver, K.4    Trottier, M.5
  • 40
    • 0017079544 scopus 로고
    • Analysis of gene function of bacteriophage phi 29 of Bacillus subtilis: Identifi cation of cistrons essential for viral assembly
    • Hagen EW, Reilly BE, Tosi ME, Anderson DL (1976) Analysis of gene function of bacteriophage phi 29 of Bacillus subtilis : identifi cation of cistrons essential for viral assembly. J Virol 19(2):501-517
    • (1976) J Virol , vol.19 , Issue.2 , pp. 501-517
    • Hagen, E.W.1    Reilly, B.E.2    Tosi, M.E.3    Anderson, D.L.4
  • 41
    • 0017844502 scopus 로고
    • Identification of the firmly bound to the ends of bacteriophage phi 29 DNA
    • Harding NE, Ito J, David GS (1978) Identifi cation of the protein fi rmly bound to the ends of bacteriophage phi 29 DNA. Virology 84(2):279-292 (Pubitemid 8286073)
    • (1978) Virology , vol.84 , Issue.2 , pp. 279-292
    • Harding, N.E.1    Ito, J.2    David, G.S.3
  • 42
    • 77954821676 scopus 로고    scopus 로고
    • Nuclear magnetic resonance structure of the prohead RNA E-loop hairpin
    • Harris S, Schroeder SJ (2010) Nuclear magnetic resonance structure of the prohead RNA E-loop hairpin. Biochemistry 49(29):5989-5997
    • (2010) Biochemistry , vol.49 , Issue.29 , pp. 5989-5997
    • Harris, S.1    Schroeder, S.J.2
  • 44
    • 0036597231 scopus 로고    scopus 로고
    • Bacteriophages: Evolution of the majority
    • DOI 10.1006/tpbi.2002.1590
    • Hendrix RW (2002) Bacteriophages: evolution of the majority. Theor Popul Biol 61(4):471-480 (Pubitemid 38051050)
    • (2002) Theoretical Population Biology , vol.61 , Issue.4 , pp. 471-480
    • Hendrix, R.W.1
  • 46
    • 0032542358 scopus 로고    scopus 로고
    • Crystal structure of the ATP-binding subunit of an ABC transporter
    • DOI 10.1038/25393
    • Hung LW, Wang IX, Nikaido K, Liu PQ, Ames GF, Kim SH (1998) Crystal structure of the ATP-binding subunit of an ABC transporter. Nature 396(6712):703-707 (Pubitemid 29003952)
    • (1998) Nature , vol.396 , Issue.6712 , pp. 703-707
    • Hung, L.-W.1    Wang, I.X.2    Nikaido, K.3    Liu, P.-Q.4    Ames, G.F.-L.5    Kim, S.-H.6
  • 47
    • 1642325936 scopus 로고    scopus 로고
    • Evolutionary history and higher order classification of AAA+ ATPases
    • DOI 10.1016/j.jsb.2003.10.010, PII S1047847703002235
    • Iyer LM, Leipe DD, Koonin EV, Aravind L (2004a) Evolutionary history and higher order classifi cation of AAA + ATPases. J Struct Biol 146(1-2):11-31 (Pubitemid 38369015)
    • (2004) Journal of Structural Biology , vol.146 , Issue.1-2 , pp. 11-31
    • Iyer, L.M.1    Leipe, D.D.2    Koonin, E.V.3    Aravind, L.4
  • 48
    • 5144223072 scopus 로고    scopus 로고
    • Comparative genomics of the FtsK-HerA superfamily of pumping ATPases: Implications for the origins of chromosome segregation, cell division and viral capsid packaging
    • DOI 10.1093/nar/gkh828
    • Iyer LM, Makarova KS, Koonin EV, Aravind L (2004b) Comparative genomics of the FtsK-HerA superfamily of pumping ATPases: implications for the origins of chromosome segregation, cell division and viral capsid packaging. Nucleic Acids Res 32(17):5260-5279 (Pubitemid 39445514)
    • (2004) Nucleic Acids Research , vol.32 , Issue.17 , pp. 5260-5279
    • Iyer, L.M.1    Makarova, K.S.2    Koonin, E.V.3    Aravind, L.4
  • 49
    • 0037313264 scopus 로고    scopus 로고
    • Coat protein fold and maturation transition of bacteriophage P22 seen at subnanometer resolutions
    • DOI 10.1038/nsb891
    • Jiang W, Li Z, Zhang Z, Baker ML, Prevelige PE Jr, Chiu W (2003) Coat protein fold and maturation transition of bacteriophage P22 seen at subnanometer resolutions. Nat Struct Biol 10(2):131-135 (Pubitemid 36177094)
    • (2003) Nature Structural Biology , vol.10 , Issue.2 , pp. 131-135
    • Jiang, W.1    Li, Z.2    Zhang, Z.3    Baker, M.L.4    Prevelige Jr., P.E.5    Chiu, W.6
  • 50
    • 39849102970 scopus 로고    scopus 로고
    • Backbone structure of the infectious ε15 virus capsid revealed by electron cryomicroscopy
    • DOI 10.1038/nature06665, PII NATURE06665
    • Jiang W, Baker ML, Jakana J, Weigele PR, King J, Chiu W (2008) Backbone structure of the infectious epsilon 15 virus capsid revealed by electron cryomicroscopy. Nature 451(7182):1130-1134 (Pubitemid 351317451)
    • (2008) Nature , vol.451 , Issue.7182 , pp. 1130-1134
    • Jiang, W.1    Baker, M.L.2    Jakana, J.3    Weigele, P.R.4    King, J.5    Chiu, W.6
  • 51
    • 33751086144 scopus 로고    scopus 로고
    • 1 ATPase
    • DOI 10.1038/sj.emboj.7601410, PII 7601410
    • Kabaleeswaran V, Puri N, Walker JE, Leslie AG, Mueller DM (2006) Novel features of the rotary catalytic mechanism revealed in the structure of yeast F1 ATPase. EMBO J 25(22):5433-5442 (Pubitemid 44764152)
    • (2006) EMBO Journal , vol.25 , Issue.22 , pp. 5433-5442
    • Kabaleeswaran, V.1    Puri, N.2    Walker, J.E.3    Leslie, A.G.W.4    Mueller, D.M.5
  • 53
    • 33645303495 scopus 로고    scopus 로고
    • The phi29 DNA polymerase: Protein-primer structure suggests a model for the initiation to elongation transition
    • Kamtekar S, Berman AJ, Wang J, Lazaro JM, de Vega M, Blanco L, Salas M, Steitz TA (2006) The phi29 DNA polymerase: protein-primer structure suggests a model for the initiation to elongation transition. EMBO J 25(6): 1335-1343
    • (2006) EMBO J , vol.25 , Issue.6 , pp. 1335-1343
    • Kamtekar, S.1    Berman, A.J.2    Wang, J.3    Lazaro, J.M.4    De Vega, M.5    Blanco, L.6    Salas, M.7    Steitz, T.A.8
  • 54
    • 0013666301 scopus 로고
    • Electron microscopical studies of phage multiplication. IV. The establishment of the DNA pool of vegetative phage and the maturation of phage particles
    • Kellenberger E, Sechaud J, Ryter A (1959) Electron microscopical studies of phage multiplication. IV. The establishment of the DNA pool of vegetative phage and the maturation of phage particles. Virology 8:478-498
    • (1959) Virology , vol.8 , pp. 478-498
    • Kellenberger, E.1    Sechaud, J.2    Ryter, A.3
  • 56
    • 66349109579 scopus 로고    scopus 로고
    • The P22 tail machine at subnanometer resolution reveals the architecture of an infection conduit
    • Lander GC, Khayat R, Li R, Prevelige PE, Potter CS, Carragher B, Johnson JE (2009) The P22 tail machine at subnanometer resolution reveals the architecture of an infection conduit. Structure 17(6):789-799
    • (2009) Structure , vol.17 , Issue.6 , pp. 789-799
    • Lander, G.C.1    Khayat, R.2    Li, R.3    Prevelige, P.E.4    Potter, C.S.5    Carragher, B.6    Johnson, J.E.7
  • 58
    • 31344436408 scopus 로고    scopus 로고
    • Interaction of gp16 with pRNA and DNA for genome packaging by the motor of bacterial virus phi29
    • DOI 10.1016/j.jmb.2005.10.045, PII S0022283605012891
    • Lee TJ, Guo P (2006) Interaction of gp16 with pRNA and DNA for genome packaging by the motor of bacterial virus phi29. J Mol Biol 356(3):589-599 (Pubitemid 43139322)
    • (2006) Journal of Molecular Biology , vol.356 , Issue.3 , pp. 589-599
    • Lee, T.-J.1    Guo, P.2
  • 59
    • 33845657428 scopus 로고    scopus 로고
    • UvrD Helicase Unwinds DNA One Base Pair at a Time by a Two-Part Power Stroke
    • DOI 10.1016/j.cell.2006.10.049, PII S0092867406016011
    • Lee JY, Yang W (2006) UvrD helicase unwinds DNA one base pair at a time by a two-part power stroke. Cell 127(7): 1349-1360 (Pubitemid 44960421)
    • (2006) Cell , vol.127 , Issue.7 , pp. 1349-1360
    • Lee, J.Y.1    Yang, W.2
  • 60
    • 0036295212 scopus 로고    scopus 로고
    • Classification and evolution of P-loop GTPases and related ATPases
    • DOI 10.1006/jmbi.2001.5378
    • Leipe DD, Wolf YI, Koonin EV, Aravind L (2002) Classifi cation and evolution of P-loop GTPases and related ATPases. J Mol Biol 317(1):41-72 (Pubitemid 34722199)
    • (2002) Journal of Molecular Biology , vol.317 , Issue.1 , pp. 41-72
    • Leipe, D.D.1    Wolf, Y.I.2    Koonin, E.V.3    Aravind, L.4
  • 61
    • 34347236451 scopus 로고    scopus 로고
    • Visualizing flexibility at molecular resolution: Analysis of heterogeneity in single-particle electron microscopy reconstructions
    • DOI 10.1146/annurev.biophys.36.040306.132742
    • Leschziner AE, Nogales E (2007) Visualizing fl exibility at molecular resolution: analysis of heterogeneity in singleparticle electron microscopy reconstructions. Annu Rev Biophys Biomol Struct 36:43-62 (Pubitemid 46998109)
    • (2007) Annual Review of Biophysics and Biomolecular Structure , vol.36 , pp. 43-62
    • Leschziner, A.E.1    Nogales, E.2
  • 62
    • 20744434561 scopus 로고    scopus 로고
    • Cooperative mechanism of RNA packaging motor
    • DOI 10.1074/jbc.M502658200
    • Lisal J, Tuma R (2005) Cooperative mechanism of RNA packaging motor. J Biol Chem 280(24):23157-23164 (Pubitemid 40853227)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.24 , pp. 23157-23164
    • Lisal, J.1    Tuma, R.2
  • 63
    • 0033377664 scopus 로고    scopus 로고
    • EMAN: Semiautomated software for high-resolution single-particle reconstructions
    • DOI 10.1006/jsbi.1999.4174
    • Ludtke SJ, Baldwin PR, Chiu W (1999) EMAN: semiautomated software for high-resolution single-particle reconstructions. J Struct Biol 128(1):82-97 (Pubitemid 30013436)
    • (1999) Journal of Structural Biology , vol.128 , Issue.1 , pp. 82-97
    • Ludtke, S.J.1    Baldwin, P.R.2    Chiu, W.3
  • 64
    • 4544386863 scopus 로고    scopus 로고
    • Atomic snapshots of an RNA packaging motor reveal conformational changes linking ATP hydrolysis to RNA translocation
    • DOI 10.1016/j.cell.2004.09.007, PII S0092867404008372
    • Mancini EJ, Kainov DE, Grimes JM, Tuma R, Bamford DH, Stuart DI (2004) Atomic snapshots of an RNA packaging motor reveal conformational changes linking ATP hydrolysis to RNA translocation. Cell 118(6):743-755 (Pubitemid 39221733)
    • (2004) Cell , vol.118 , Issue.6 , pp. 743-755
    • Mancini, E.J.1    Kainov, D.E.2    Grimes, J.M.3    Tuma, R.4    Bamford, D.H.5    Stuart, D.I.6
  • 65
    • 0037106323 scopus 로고    scopus 로고
    • Sequence analysis of bacteriophage T4 DNA packaging/terminase genes 16 and 17 reveals a common ATPase center in the large subunit of viral terminases
    • Mitchell MS, Matsuzaki S, Imai S, Rao VB (2002) Sequence analysis of bacteriophage T4 DNA packaging/terminase genes 16 and 17 reveals a common ATPase center in the large subunit of viral terminases. Nucleic Acids Res 30(18): 4009-4021
    • (2002) Nucleic Acids Res , vol.30 , Issue.18 , pp. 4009-4021
    • Mitchell, M.S.1    Matsuzaki, S.2    Imai, S.3    Rao, V.B.4
  • 70
    • 17044395121 scopus 로고    scopus 로고
    • Conservation of the capsid structure in tailed dsDNA bacteriophages: The pseudoatomic structure of phi29
    • Morais MC, Choi KH, Koti JS, Chipman PR, Anderson DL, Rossmann MG (2005) Conservation of the capsid structure in tailed dsDNA bacteriophages: the pseudoatomic structure of phi29. Mol Cell 18(2):149-159
    • (2005) Mol Cell , vol.18 , Issue.2 , pp. 149-159
    • Morais, M.C.1    Choi, K.H.2    Koti, J.S.3    Chipman, P.R.4    Anderson, D.L.5    Rossmann, M.G.6
  • 72
    • 84858179369 scopus 로고
    • Complementary Strands of Bacteriophage phi29 Deoxyribonucleic Acid: Preparative Separation and Transcription Studies
    • Mosharrafa ET, Schachtele CF, Reilly BE, Anderson DL (1970) Complementary Strands of Bacteriophage phi29 Deoxyribonucleic Acid: Preparative Separation and Transcription Studies. J Virol 6(6):855-864
    • (1970) J Virol , vol.6 , Issue.6 , pp. 855-864
    • Mosharrafa, E.T.1    Schachtele, C.F.2    Reilly, B.E.3    Anderson, D.L.4
  • 73
    • 0343811707 scopus 로고    scopus 로고
    • The bacteriophage φ29 head-tail connector imaged at high resolution with the atomic force microscope in buffer solution
    • DOI 10.1093/emboj/16.10.2547
    • Muller DJ, Engel A, Carrascosa JL, Velez M (1997) The bacteriophage phi29 head-tail connector imaged at high resolution with the atomic force microscope in buffer solution. EMBO J 16(10):2547-2553 (Pubitemid 27226194)
    • (1997) EMBO Journal , vol.16 , Issue.10 , pp. 2547-2553
    • Muller, D.J.1    Engel, A.2    Carrascosa, J.L.3    Velez, M.4
  • 74
    • 0033598667 scopus 로고    scopus 로고
    • 1-ATPase residue α-Arg-376 for catalytic transition state stabilization
    • Nadanaciva S, Weber J, Wilke-Mounts S, Senior AE (1999) Importance of F1-ATPase residue alpha-Arg-376 for catalytic transition state stabilization. Biochemistry 38(47):15493-15499 (Pubitemid 129503589)
    • (1999) Biochemistry , vol.38 , Issue.47 , pp. 15493-15499
    • Nadanaciva, S.1    Weber, J.2    Wilke-Mounts, S.3    Senior, A.E.4
  • 75
    • 1642377971 scopus 로고    scopus 로고
    • + ATPases
    • DOI 10.1016/j.jsb.2003.11.008, PII S1047847703002843
    • Ogura T, Whiteheart SW, Wilkinson AJ (2004) Conserved arginine residues implicated in ATP hydrolysis, nucleotidesensing, and inter-subunit interactions in AAA and AAA + ATPases. J Struct Biol 146(1-2):106-112 (Pubitemid 38369023)
    • (2004) Journal of Structural Biology , vol.146 , Issue.1-2 , pp. 106-112
    • Ogura, T.1    Whiteheart, S.W.2    Wilkinson, A.J.3
  • 76
    • 0037451286 scopus 로고    scopus 로고
    • Structure of a viral DNA gatekeeper at 10 A resolution by cryo-electron microscopy
    • DOI 10.1093/emboj/cdg123
    • Orlova EV, Gowen B, Droge A, Stiege A, Weise F, Lurz R, van Heel M, Tavares P (2003) Structure of a viral DNA gatekeeper at 10 A resolution by cryo-electron microscopy. EMBO J 22(6):1255-1262 (Pubitemid 36362689)
    • (2003) EMBO Journal , vol.22 , Issue.6 , pp. 1255-1262
    • Orlova, E.V.1    Gowen, B.2    Droge, A.3    Stiege, A.4    Weise, F.5    Lurz, R.6    Van Heel, M.7    Tavares, P.8
  • 77
    • 47749092360 scopus 로고    scopus 로고
    • Packaging double-helical DNA into viral capsids: Structures, forces, and energetics
    • Petrov AS, Harvey SC (2008) Packaging double-helical DNA into viral capsids: structures, forces, and energetics. Biophys J 95(2):497-502
    • (2008) Biophys J , vol.95 , Issue.2 , pp. 497-502
    • Petrov, A.S.1    Harvey, S.C.2
  • 78
    • 0027992332 scopus 로고
    • Characterization of the prohead-pRNA interaction of bacteriophage φ29
    • Reid RJ, Bodley JW, Anderson D (1994a) Characterization of the prohead-pRNA interaction of bacteriophage phi 29. J Biol Chem 269(7):5157-5162 (Pubitemid 24239507)
    • (1994) Journal of Biological Chemistry , vol.269 , Issue.7 , pp. 5157-5162
    • Reid, R.J.D.1    Bodley, J.W.2    Anderson, D.3
  • 79
    • 0028175938 scopus 로고
    • Identifi cation of bacteriophage phi 29 prohead RNA domains necessary for in vitro DNA-gp3 packaging
    • Reid RJ, Bodley JW, Anderson D (1994b) Identifi cation of bacteriophage phi 29 prohead RNA domains necessary for in vitro DNA-gp3 packaging. J Biol Chem 269(12):9084-9089
    • (1994) J Biol Chem , vol.269 , Issue.12 , pp. 9084-9089
    • Reid, R.J.1    Bodley, J.W.2    Anderson, D.3
  • 80
    • 0028358819 scopus 로고
    • Probing the structure of bacteriophage φ29 prohead RNA with specific mutations
    • Reid RJ, Zhang F, Benson S, Anderson D (1994c) Probing the structure of bacteriophage phi 29 prohead RNA with specifi c mutations. J Biol Chem 269(28):18656-18661 (Pubitemid 24224108)
    • (1994) Journal of Biological Chemistry , vol.269 , Issue.28 , pp. 18656-18661
    • Reid, R.J.D.1    Zhang, F.2    Benson, S.3    Anderson, D.4
  • 81
    • 37749051185 scopus 로고    scopus 로고
    • Portal motor velocity and internal force resisting viral DNA packaging in bacteriophage phi29
    • Rickgauer JP, Fuller DN, Grimes S, Jardine PJ, Anderson DL, Smith DE (2008) Portal motor velocity and internal force resisting viral DNA packaging in bacteriophage phi29. Biophys J 94(1):159-167
    • (2008) Biophys J , vol.94 , Issue.1 , pp. 159-167
    • Rickgauer, J.P.1    Fuller, D.N.2    Grimes, S.3    Jardine, P.J.4    Anderson, D.L.5    Smith, D.E.6
  • 82
    • 0016345760 scopus 로고
    • Chemical and biological evolution of nucleotide-binding protein
    • Rossmann MG, Moras D, Olsen KW (1974) Chemical and biological evolution of nucleotide-binding protein. Nature 250(463):194-199
    • (1974) Nature , vol.250 , Issue.463 , pp. 194-199
    • Rossmann, M.G.1    Moras, D.2    Olsen, K.W.3
  • 83
    • 14844338484 scopus 로고    scopus 로고
    • Combining X-ray crystallography and electron microscopy
    • DOI 10.1016/j.str.2005.01.005
    • Rossmann MG, Morais MC, Leiman PG, Zhang W (2005) Combining X-ray crystallography and electron microscopy. Structure 13(3):355-362 (Pubitemid 40342874)
    • (2005) Structure , vol.13 , Issue.3 , pp. 355-362
    • Rossmann, M.G.1    Morais, M.C.2    Leiman, P.G.3    Zhang, W.4
  • 84
    • 0017893449 scopus 로고
    • Characterization of a protein covalently linked to the 5' termini of the DNA of Bacillus subtilis phage phi29
    • Salas M, Mellado RP, Vinuela E (1978) Characterization of a protein covalently linked to the 5 ' termini of the DNA of Bacillus subtilis phage phi29. J Mol Biol 119(2):269-291 (Pubitemid 8279212)
    • (1978) Journal of Molecular Biology , vol.119 , Issue.2 , pp. 269-291
    • Salas, M.1    Mellado, R.P.2    Vinuela, E.3
  • 85
    • 0015549276 scopus 로고
    • Transcription during the development of bacteriophage phi29: Defi - Nition of 'early' and 'late' phi29 ribonucleic acid
    • Schachtele CF, De Sain CV, Anderson DL (1973) Transcription during the development of bacteriophage phi29: defi - nition of 'early' and 'late' phi29 ribonucleic acid. J Virol 11(1):9-16
    • (1973) J Virol , vol.11 , Issue.1 , pp. 9-16
    • Schachtele, C.F.1    De Sain, C.V.2    Anderson, D.L.3
  • 86
    • 33846551354 scopus 로고    scopus 로고
    • Counting of six pRNAs of phi29 DNA-packaging motor with customized single-molecule dual-view system
    • DOI 10.1038/sj.emboj.7601506, PII 7601506
    • Shu D, Zhang H, Jin J, Guo P (2007) Counting of six pRNAs of phi29 DNA-packaging motor with customized singlemolecule dual-view system. EMBO J 26(2):527-537 (Pubitemid 46160952)
    • (2007) EMBO Journal , vol.26 , Issue.2 , pp. 527-537
    • Shu, D.1    Zhang, H.2    Jin, J.3    Guo, P.4
  • 89
    • 0034625236 scopus 로고    scopus 로고
    • Crystal structure of T7 gene 4 ring helicase indicates a mechanism for sequential hydrolysis of nucleotides
    • Singleton MR, Sawaya MR, Ellenberger T, Wigley DB (2000) Crystal structure of T7 gene 4 ring helicase indicates a mechanism for sequential hydrolysis of nucleotides. Cell 101(6):589-600
    • (2000) Cell , vol.101 , Issue.6 , pp. 589-600
    • Singleton, M.R.1    Sawaya, M.R.2    Ellenberger, T.3    Wigley, D.B.4
  • 90
    • 34548638261 scopus 로고    scopus 로고
    • Structure and mechanism of helicases and nucleic acid translocases
    • Singleton MR, Dillingham MS, Wigley DB (2007) Structure and mechanism of helicases and nucleic acid translocases. Annu Rev Biochem 76:23-50
    • (2007) Annu Rev Biochem , vol.76 , pp. 23-50
    • Singleton, M.R.1    Dillingham, M.S.2    Wigley, D.B.3
  • 91
    • 0037559627 scopus 로고    scopus 로고
    • Structure of the Rho transcription terminator: Mechanism of mRNA recognition and helicase loading
    • DOI 10.1016/S0092-8674(03)00512-9
    • Skordalakes E, Berger JM (2003) Structure of the Rho transcription terminator: mechanism of mRNA recognition and helicase loading. Cell 114(1):135-146 (Pubitemid 36869001)
    • (2003) Cell , vol.114 , Issue.1 , pp. 135-146
    • Skordalakes, E.1    Berger, J.M.2
  • 92
    • 0035909370 scopus 로고    scopus 로고
    • The bacteriophage φ29 portal motor can package DNA against a large internal force
    • DOI 10.1038/35099581
    • Smith DE, Tans SJ, Smith SB, Grimes S, Anderson DL, Bustamante C (2001) The bacteriophage straight phi29 portal motor can package DNA against a large internal force. Nature 413(6857):748-752 (Pubitemid 33009954)
    • (2001) Nature , vol.413 , Issue.6857 , pp. 748-752
    • Smith, D.E.1    Tans, S.J.2    Smith, S.B.3    Grimes, S.4    Anderson, D.L.5    Bustamante, C.6
  • 93
    • 0026584599 scopus 로고
    • Structure of the recA protein-ADP complex
    • Story RM, Steitz TA (1992) Structure of the recA protein-ADP complex. Nature 355(6358):374-376
    • (1992) Nature , vol.355 , Issue.6358 , pp. 374-376
    • Story, R.M.1    Steitz, T.A.2
  • 94
    • 0026500416 scopus 로고
    • The structure of the E. coli recA protein monomer and polymer
    • Story RM, Weber IT, Steitz TA (1992) The structure of the E. coli recA protein monomer and polymer. Nature 355(6358):318-325
    • (1992) Nature , vol.355 , Issue.6358 , pp. 318-325
    • Story, R.M.1    Weber, I.T.2    Steitz, T.A.3
  • 95
    • 0029856618 scopus 로고    scopus 로고
    • Crystal structure of a DExx box DNA helicase
    • DOI 10.1038/384379a0
    • Subramanya HS, Bird LE, Brannigan JA, Wigley DB (1996) Crystal structure of a DExx box DNA helicase. Nature 384(6607):379-383 (Pubitemid 26408523)
    • (1996) Nature , vol.384 , Issue.6607 , pp. 379-383
    • Subramanya, H.S.1    Bird, L.E.2    Brannigan, J.A.3    Wigley, D.B.4
  • 96
    • 33947281384 scopus 로고    scopus 로고
    • The Structure of the ATPase that Powers DNA Packaging into Bacteriophage T4 Procapsids
    • DOI 10.1016/j.molcel.2007.02.013, PII S109727650700113X
    • Sun S, Kondabagil K, Gentz PM, Rossmann MG, Rao VB (2007) The structure of the ATPase that powers DNA packaging into bacteriophage T4 procapsids. Mol Cell 25(6):943-949 (Pubitemid 46436529)
    • (2007) Molecular 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
  • 98
    • 44649135211 scopus 로고    scopus 로고
    • DNA Poised for Release in Bacteriophage ø29
    • DOI 10.1016/j.str.2008.02.024, PII S0969212608001482
    • Tang J, Olson N, Jardine PJ, Grimes S, Anderson DL, Baker TS (2008) DNA poised for release in bacteriophage phi29. Structure 16(6):935-943 (Pubitemid 351778380)
    • (2008) Structure , vol.16 , Issue.6 , pp. 935-943
    • Tang, J.1    Olson, N.2    Jardine, P.J.3    Grimes, S.4    Anderson, D.L.5    Baker, T.S.6
  • 99
    • 0032582665 scopus 로고    scopus 로고
    • Assembly of a tailed bacterial virus and its genome release studied in three dimensions
    • DOI 10.1016/S0092-8674(00)81773-0
    • Tao Y, Olson NH, Xu W, Anderson DL, Rossmann MG, Baker TS (1998) Assembly of a tailed bacterial virus and its genome release studied in three dimensions. Cell 95(3):431-437 (Pubitemid 28507330)
    • (1998) Cell , vol.95 , Issue.3 , pp. 431-437
    • Tao, Y.1    Olson, N.H.2    Xu, W.3    Anderson, D.L.4    Rossmann, M.G.5    Baker, T.S.6
  • 100
    • 49249093920 scopus 로고    scopus 로고
    • Structural frameworks for considering microbial protein- and nucleic acid-dependent motor ATPases
    • Thomsen ND, Berger JM (2008) Structural frameworks for considering microbial protein- and nucleic acid-dependent motor ATPases. Mol Microbiol 69(5):1071-1090
    • (2008) Mol Microbiol , vol.69 , Issue.5 , pp. 1071-1090
    • Thomsen, N.D.1    Berger, J.M.2
  • 101
    • 0031060162 scopus 로고    scopus 로고
    • Approaches to determine stoichiometry of viral assembly components
    • Trottier M, Guo P (1997) Approaches to determine stoichiometry of viral assembly components. J Virol 71(1): 487-494 (Pubitemid 26412317)
    • (1997) Journal of Virology , vol.71 , Issue.1 , pp. 487-494
    • Trottier, M.1    Guo, P.2
  • 102
    • 0028176714 scopus 로고
    • The bacteriophage phi 29 head-tail connector shows 13-fold symmetry in both hexagonally packed arrays and as single particles
    • Tsuprun V, Anderson D, Egelman EH (1994) The bacteriophage phi 29 head-tail connector shows 13-fold symmetry in both hexagonally packed arrays and as single particles. Biophys J 66(6):2139-2150
    • (1994) Biophys J , vol.66 , Issue.6 , pp. 2139-2150
    • Tsuprun, V.1    Anderson, D.2    Egelman, E.H.3
  • 104
    • 0028000731 scopus 로고
    • Structure of viral connectors and their function in bacteriophage assembly and DNA packaging
    • Valpuesta JM, Carrascosa JL (1994) Structure of viral connectors and their function in bacteriophage assembly and DNA packaging. Q Rev Biophys 27(2):107-155 (Pubitemid 24246113)
    • (1994) Quarterly Reviews of Biophysics , vol.27 , Issue.2 , pp. 107-155
    • Valpuesta, J.M.1    Carrascosa, J.L.2
  • 105
    • 0039786701 scopus 로고    scopus 로고
    • The three-dimensional structure of a DNA translocating machine at 10 A resolution
    • DOI 10.1016/S0969-2126(99)80039-2
    • Valpuesta JM, Fernandez JJ, Carazo JM, Carrascosa JL (1999) The three-dimensional structure of a DNA translocating machine at 10 A resolution. Structure 7(3):289-296 (Pubitemid 29159688)
    • (1999) Structure , vol.7 , Issue.3 , pp. 289-296
    • Valpuesta, J.M.1    Fernandez, J.J.2    Carazo, J.M.3    Carrascosa, J.L.4
  • 107
    • 0033515425 scopus 로고    scopus 로고
    • Crystal structures of complexes of PcrA DNA helicase with a DNA substrate indicate an inchworm mechanism
    • Velankar SS, Soultanas P, Dillingham MS, Subramanya HS, Wigley DB (1999) Crystal structures of complexes of PcrA DNA helicase with a DNA substrate indicate an inchworm mechanism. Cell 97(1):75-84 (Pubitemid 29165891)
    • (1999) Cell , vol.97 , Issue.1 , pp. 75-84
    • Velankar, S.S.1    Soultanas, P.2    Dillingham, M.S.3    Subramanya, H.S.4    Wigley, D.B.5
  • 108
    • 0001607723 scopus 로고
    • Distantly related sequences in the alpha- and beta-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold
    • Walker JE, Saraste M, Runswick MJ, Gay NJ (1982) Distantly related sequences in the alpha- and beta-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold. EMBO J 1(8):945-951
    • (1982) EMBO J , vol.1 , Issue.8 , pp. 945-951
    • Walker, J.E.1    Saraste, M.2    Runswick, M.J.3    Gay, N.J.4
  • 109
    • 0024967168 scopus 로고
    • Prohead RNA of bacteriophage phi 29: Size, stoichiometry and biological activity
    • Wichitwechkarn J, Bailey S, Bodley JW, Anderson D (1989) Prohead RNA of bacteriophage phi 29: size, stoichiometry and biological activity. Nucleic Acids Res 17(9):3459-3468
    • (1989) Nucleic Acids Res , vol.17 , Issue.9 , pp. 3459-3468
    • Wichitwechkarn, J.1    Bailey, S.2    Bodley, J.W.3    Anderson, D.4
  • 111
    • 0030738592 scopus 로고    scopus 로고
    • The interaction of Ras with GTPase-activating proteins
    • DOI 10.1016/S0014-5793(97)00321-9, PII S0014579397003219
    • Wittinghofer A, Scheffzek K, Ahmadian MR (1997) The interaction of Ras with GTPase-activating proteins. FEBS Lett 410(1):63-67 (Pubitemid 27283385)
    • (1997) FEBS Letters , vol.410 , Issue.1 , pp. 63-67
    • Wittinghofer, A.1    Scheffzek, K.2    Ahmadian, M.R.3
  • 114
    • 19444373849 scopus 로고    scopus 로고
    • Binding of pRNA to the N-terminal 14 amino acids of connector protein of bacteriophage phi29
    • DOI 10.1093/nar/gki554
    • Xiao F, Moll WD, Guo S, Guo P (2005) Binding of pRNA to the N-terminal 14 amino acids of connector protein of bacteriophage phi29. Nucleic Acids Res 33(8):2640-2649 (Pubitemid 41511283)
    • (2005) Nucleic Acids Research , vol.33 , Issue.8 , pp. 2640-2649
    • Xiao, F.1    Moll, W.-D.2    Guo, S.3    Guo, P.4
  • 115
    • 0018089244 scopus 로고
    • Genome-linked protein associated with the 5' termini of bacteriophage Φ29 DNA
    • Yehle CO (1978) Genome-linked protein associated with the 5 ' termini of bacteriophage phi29 DNA. J Virol 27(3):776-783 (Pubitemid 9009118)
    • (1978) Journal of Virology , vol.27 , Issue.3 , pp. 776-783
    • Yehle, C.O.1
  • 116
    • 0028796334 scopus 로고
    • A common topology of proteins catalyzing ATP-triggered reactions
    • Yoshida M, Amano T (1995) A common topology of proteins catalyzing ATP-triggered reactions. FEBS Lett 359(1):1-5
    • (1995) FEBS Lett , vol.359 , Issue.1 , pp. 1-5
    • Yoshida, M.1    Amano, T.2
  • 118
    • 0028361637 scopus 로고
    • The proximate 5 ' and 3 ' ends of the 120-base viral RNA (pRNA) are crucial for the packaging of bacteriophage phi 29 DNA
    • Zhang C, Lee CS, Guo P (1994) The proximate 5 ' and 3 ' ends of the 120-base viral RNA (pRNA) are crucial for the packaging of bacteriophage phi 29 DNA. Virology 201(1):77-85
    • (1994) Virology , vol.201 , Issue.1 , pp. 77-85
    • Zhang, C.1    Lee, C.S.2    Guo, P.3
  • 119
    • 0029437961 scopus 로고
    • Confi rmation of the helical structure of the 5 ' /3 ' termini of the essential DNA packaging pRNA of phage phi 29
    • Zhang C, Tellinghuisen T, Guo P (1995) Confi rmation of the helical structure of the 5 ' /3 ' termini of the essential DNA packaging pRNA of phage phi 29. RNA 1(10):1041-1050
    • (1995) RNA , vol.1 , Issue.10 , pp. 1041-1050
    • Zhang, C.1    Tellinghuisen, T.2    Guo, P.3
  • 121
    • 52949145603 scopus 로고    scopus 로고
    • Role of the CCA bulge of prohead RNA of bacteriophage '29 in DNA packaging
    • Zhao W, Morais MC, Anderson DL, Jardine PJ, Grimes S (2008) Role of the CCA bulge of prohead RNA of bacteriophage '29 in DNA packaging. J Mol Biol 383(3):520-528
    • (2008) J Mol Biol , vol.383 , Issue.3 , pp. 520-528
    • Zhao, W.1    Morais, M.C.2    Anderson, D.L.3    Jardine, P.J.4    Grimes, S.5
  • 122
    • 38949104355 scopus 로고    scopus 로고
    • A conformational switch in bacteriophage P22 portal protein primes genome injection
    • DOI 10.1016/j.molcel.2007.11.034, PII S1097276508000063
    • Zheng H, Olia AS, Gonen M, Andrews S, Cingolani G, Gonen T (2008) A conformational switch in bacteriophage p22 portal protein primes genome injection. Mol Cell 29(3):376-383 (Pubitemid 351215935)
    • (2008) Molecular Cell , vol.29 , Issue.3 , pp. 376-383
    • Zheng, H.1    Olia, A.S.2    Gonen, M.3    Andrews, S.4    Cingolani, G.5    Gonen, T.6


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