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Volumn 90, Issue 18, 2016, Pages 8036-8046

Development of potent antiviral drugs inspired by viral hexameric DNA-packaging motors with revolving mechanism

Author keywords

[No Author keywords available]

Indexed keywords

ANTIVIRUS AGENT; DOUBLE STRANDED DNA; DOUBLE STRANDED RNA; MOLECULAR MOTOR; VIRUS DNA; VIRUS RNA; DNA VIRUS; VIRAL PROTEIN;

EID: 84984619803     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.00508-16     Document Type: Article
Times cited : (16)

References (122)
  • 1
    • 84895852851 scopus 로고    scopus 로고
    • Multimodal mechanism of action of allosteric HIV-1 integrase inhibitors
    • Jurado KA, Engelman A. 2013. Multimodal mechanism of action of allosteric HIV-1 integrase inhibitors. Expert Rev Mol Med 15:e14. http: //dx.doi.org/10.1017/erm.2013.15.
    • (2013) Expert Rev Mol Med , vol.15 , pp. e14
    • Jurado, K.A.1    Engelman, A.2
  • 2
    • 84954342160 scopus 로고    scopus 로고
    • Optimized combination therapies with adefovir dipivoxil (ADV) and lamivudine, telbivudine, or entecavir may be effective for chronic hepatitis B patients with a suboptimal response to ADV monotherapy
    • Li X, Jie Y, You X, Shi H, Zhang M, Wu Y, Lin G, Li X, Gao Z, Chong Y. 2015. Optimized combination therapies with adefovir dipivoxil (ADV) and lamivudine, telbivudine, or entecavir may be effective for chronic hepatitis B patients with a suboptimal response to ADV monotherapy. Int J Clin Exp Med 8:21062-21070.
    • (2015) Int J Clin Exp Med , vol.8 , pp. 21062-21070
    • Li, X.1    Jie, Y.2    You, X.3    Shi, H.4    Zhang, M.5    Wu, Y.6    Lin, G.7    Li, X.8    Gao, Z.9    Chong, Y.10
  • 3
    • 84901842119 scopus 로고    scopus 로고
    • Targeting Myc in KSHV-associated primary effusion lymphoma with BET bromodomain inhibitors
    • Tolani B, Gopalakrishnan R, Punj V, Matta H, Chaudhary PM. 2014. Targeting Myc in KSHV-associated primary effusion lymphoma with BET bromodomain inhibitors. Oncogene 33:2928-2937. http://dx.doi.org/10.1038/onc.2013.242.
    • (2014) Oncogene , vol.33 , pp. 2928-2937
    • Tolani, B.1    Gopalakrishnan, R.2    Punj, V.3    Matta, H.4    Chaudhary, P.M.5
  • 4
    • 49449093199 scopus 로고    scopus 로고
    • Functional studies indicate amantadine binds to the pore of the influenza A virus M2 proton-selective ion channel
    • Jing X, Ma C, Ohigashi Y, Oliveira FA, Jardetzky TS, Pinto LH, Lamb RA. 2008. Functional studies indicate amantadine binds to the pore of the influenza A virus M2 proton-selective ion channel. Proc Natl Acad Sci U S A 105:10967-10972. http://dx.doi.org/10.1073/pnas.0804958105.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 10967-10972
    • Jing, X.1    Ma, C.2    Ohigashi, Y.3    Oliveira, F.A.4    Jardetzky, T.S.5    Pinto, L.H.6    Lamb, R.A.7
  • 5
    • 84963808217 scopus 로고    scopus 로고
    • Biochemical characterization of a multi-drug resistant HIV-1 subtype AG reverse transcriptase: antagonism of AZT discrimination and excision pathways and sensitivity to RNaseHinhibitors
    • Schneider A, Corona A, Sporing I, Jordan M, Buchholz B, Maccioni E, Di SR, Bodem J, Tramontano E, Wohrl BM. 2016. Biochemical characterization of a multi-drug resistant HIV-1 subtype AG reverse transcriptase: antagonism of AZT discrimination and excision pathways and sensitivity to RNaseHinhibitors. Nucleic Acids Res 44:2310-2322. http: //dx.doi.org/10.1093/nar/gkw060.
    • (2016) Nucleic Acids Res , vol.44 , pp. 2310-2322
    • Schneider, A.1    Corona, A.2    Sporing, I.3    Jordan, M.4    Buchholz, B.5    Maccioni, E.6    Di, S.R.7    Bodem, J.8    Tramontano, E.9    Wohrl, B.M.10
  • 6
    • 27244442206 scopus 로고    scopus 로고
    • Achievements and challenges in antiviral drug discovery
    • Littler E, Oberg B. 2005. Achievements and challenges in antiviral drug discovery. Antivir Chem Chemother 16:155-168. http://dx.doi.org/10.1177/095632020501600302.
    • (2005) Antivir Chem Chemother , vol.16 , pp. 155-168
    • Littler, E.1    Oberg, B.2
  • 7
    • 84877853462 scopus 로고    scopus 로고
    • Structures of the phage Sf6 large terminase provide new insights into DNA translocation and cleavage
    • Zhao H, Christensen TE, Kamau YN, Tang L. 2013. Structures of the phage Sf6 large terminase provide new insights into DNA translocation and cleavage. Proc Natl Acad SciUS A 110:8075-8080. http://dx.doi.org /10.1073/pnas.1301133110.
    • (2013) Proc Natl Acad SciUS A , vol.110 , pp. 8075-8080
    • Zhao, H.1    Christensen, T.E.2    Kamau, Y.N.3    Tang, L.4
  • 8
    • 26444561955 scopus 로고    scopus 로고
    • Control of adenovirus packaging
    • Ostapchuk P, Hearing P. 2005. Control of adenovirus packaging. J Cell Biochem 96:25-35. http://dx.doi.org/10.1002/jcb.20523.
    • (2005) J Cell Biochem , vol.96 , pp. 25-35
    • Ostapchuk, P.1    Hearing, P.2
  • 9
    • 58649102251 scopus 로고    scopus 로고
    • Phylogenetic analysis of parapoxviruses and the C-terminal heterogeneity of viral ATPase proteins
    • Chan KW, Yang CH, Lin JW, Wang HC, Lin FY, Kuo ST, Wong ML, Hsu WL. 2009. Phylogenetic analysis of parapoxviruses and the C-terminal heterogeneity of viral ATPase proteins. Gene 432:44-53. http://dx.doi.org/10.1016/j.gene.2008.10.029.
    • (2009) Gene , vol.432 , pp. 44-53
    • Chan, K.W.1    Yang, C.H.2    Lin, J.W.3    Wang, H.C.4    Lin, F.Y.5    Kuo, S.T.6    Wong, M.L.7    Hsu, W.L.8
  • 10
    • 0036510764 scopus 로고    scopus 로고
    • ATPase activity of the terminase subunit pUL56 of human cytomegalovirus
    • Hwang JS, Bogner E. 2002. ATPase activity of the terminase subunit pUL56 of human cytomegalovirus. J Biol Chem 277:6943-6948. http: //dx.doi.org/10.1074/jbc.M108984200.
    • (2002) J Biol Chem , vol.277 , pp. 6943-6948
    • Hwang, J.S.1    Bogner, E.2
  • 11
    • 34250734534 scopus 로고    scopus 로고
    • Viral capsids: mechanical characteristics, genome packaging and delivery mechanisms
    • Roos WH, Ivanovska IL, Evilevitch A, Wuite GJL. 2007. Viral capsids: mechanical characteristics, genome packaging and delivery mechanisms. Cell Mol Life Sci 64:1484-1497. http://dx.doi.org/10.1007/s00018-007-6451-1.
    • (2007) Cell Mol Life Sci , vol.64 , pp. 1484-1497
    • Roos, W.H.1    Ivanovska, I.L.2    Evilevitch, A.3    Wuite, G.J.L.4
  • 12
    • 0016312775 scopus 로고
    • Catalytic head assembly protein in virus morphogenesis
    • King J, Casjens S. 1974. Catalytic head assembly protein in virus morphogenesis. Nature 251:112-119. http://dx.doi.org/10.1038/251112a0.
    • (1974) Nature , vol.251 , pp. 112-119
    • King, J.1    Casjens, S.2
  • 13
    • 84880948085 scopus 로고    scopus 로고
    • Ultrastable pRNA hexameric ring gearing hexameric phi29 DNA-packaging motor by revolving without rotating and coiling
    • Schwartz C, Guo P. 2013. Ultrastable pRNA hexameric ring gearing hexameric phi29 DNA-packaging motor by revolving without rotating and coiling. Curr Opin Biotechnol 24:581-590. http://dx.doi.org/10.1016/j.copbio.2013.03.019.
    • (2013) Curr Opin Biotechnol , vol.24 , pp. 581-590
    • Schwartz, C.1    Guo, P.2
  • 14
    • 84936972846 scopus 로고    scopus 로고
    • New approach to develop ultra-high inhibitory drug using the power-function of the stoichiometry of the targeted nanomachine or biocomplex
    • Shu D, Pi F, Wang C, Zhang P, Guo P. 2015. New approach to develop ultra-high inhibitory drug using the power-function of the stoichiometry of the targeted nanomachine or biocomplex. Nanomedicine (Lond) 10: 1881-1897. http://dx.doi.org/10.2217/nnm.15.37.
    • (2015) Nanomedicine (Lond) , vol.10 , pp. 1881-1897
    • Shu, D.1    Pi, F.2    Wang, C.3    Zhang, P.4    Guo, P.5
  • 15
    • 84964068517 scopus 로고    scopus 로고
    • Biological nanomotors with revolving, linear, or rotation motion mechanism
    • Guo P, Noji H, Yengo CM, Zhao Z, Grainge I. 2016. Biological nanomotors with revolving, linear, or rotation motion mechanism. Microbiol Mol Biol Rev 80:161-186. http://dx.doi.org/10.1128/MMBR.00056-15.
    • (2016) Microbiol Mol Biol Rev , vol.80 , pp. 161-186
    • Guo, P.1    Noji, H.2    Yengo, C.M.3    Zhao, Z.4    Grainge, I.5
  • 16
    • 84879787373 scopus 로고    scopus 로고
    • Revolving rather than rotation of AAA+ hexameric phi29 nanomotor for viral dsDNA packaging without coiling
    • Schwartz C, De Donatis GM, Zhang H, Fang H, Guo P. 2013. Revolving rather than rotation of AAA+ hexameric phi29 nanomotor for viral dsDNA packaging without coiling. Virology 443:28-39. http://dx.doi.org/10.1016/j.virol.2013.04.019.
    • (2013) Virology , vol.443 , pp. 28-39
    • Schwartz, C.1    De Donatis, G.M.2    Zhang, H.3    Fang, H.4    Guo, P.5
  • 17
    • 84902546969 scopus 로고    scopus 로고
    • Finding of widespread viral and bacterial revolving dsDNA translocation motors distinct from rotation motors by channel chirality and size
    • De-Donatis G, Zhao Z, Wang S, Huang PL, Schwartz C, Tsodikov VO, Zhang H, Haque F, Guo P. 2014. Finding of widespread viral and bacterial revolving dsDNA translocation motors distinct from rotation motors by channel chirality and size. Cell Biosci 4:30. http://dx.doi.org /10.1186/2045-3701-4-30.
    • (2014) Cell Biosci , vol.4 , pp. 30
    • De-Donatis, G.1    Zhao, Z.2    Wang, S.3    Huang, P.L.4    Schwartz, C.5    Tsodikov, V.O.6    Zhang, H.7    Haque, F.8    Guo, P.9
  • 18
    • 84955189930 scopus 로고    scopus 로고
    • Discovery of a new method for potent drug development using power function of stoichiometry of homomeric biocomplexes or biological nanomotors
    • Pi F, Vieweger M, Zhao Z, Wang S, Guo P. 2016. Discovery of a new method for potent drug development using power function of stoichiometry of homomeric biocomplexes or biological nanomotors. Expert Opin Drug Deliv 13:23-36. http://dx.doi.org/10.1517/17425247.2015.1082544.
    • (2016) Expert Opin Drug Deliv , vol.13 , pp. 23-36
    • Pi, F.1    Vieweger, M.2    Zhao, Z.3    Wang, S.4    Guo, P.5
  • 19
    • 84857648622 scopus 로고    scopus 로고
    • Comparative sequence analysis of poxvirus A32 gene encoded ATPase protein and carboxyl terminal heterogeneity of Indian orf viruses
    • Yogisharadhya R, Bhanuprakash V, Venkatesan G, Balamurugan V, Pandey AB, Shivachandra SB. 2012. Comparative sequence analysis of poxvirus A32 gene encoded ATPase protein and carboxyl terminal heterogeneity of Indian orf viruses. Vet Microbiol 156:72-80. http://dx.doi.org/10.1016/j.vetmic.2011.10.021.
    • (2012) Vet Microbiol , vol.156 , pp. 72-80
    • Yogisharadhya, R.1    Bhanuprakash, V.2    Venkatesan, G.3    Balamurugan, V.4    Pandey, A.B.5    Shivachandra, S.B.6
  • 20
    • 67649852610 scopus 로고    scopus 로고
    • Scaffold expulsion and genome packaging trigger stabilization of herpes simplex virus capsids
    • Roos WH, Radtke K, Kniesmeijer E, Geertsema H, Sodeik B, Wuite GJ. 2009. Scaffold expulsion and genome packaging trigger stabilization of herpes simplex virus capsids. Proc Natl Acad SciUSA106:9673-9678. http://dx.doi.org/10.1073/pnas.0901514106.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 9673-9678
    • Roos, W.H.1    Radtke, K.2    Kniesmeijer, E.3    Geertsema, H.4    Sodeik, B.5    Wuite, G.J.6
  • 21
    • 84908135466 scopus 로고    scopus 로고
    • Two classes of nucleic acid translocation motors: rotation and revolution without rotation
    • Guo P, Grainge I, Zhao Z, Vieweger M. 2014. Two classes of nucleic acid translocation motors: rotation and revolution without rotation. Cell Biosci 4:54. http://dx.doi.org/10.1186/2045-3701-4-54.
    • (2014) Cell Biosci , vol.4 , pp. 54
    • Guo, P.1    Grainge, I.2    Zhao, Z.3    Vieweger, M.4
  • 22
    • 84940004805 scopus 로고    scopus 로고
    • Old, new, and widely true: the bacteriophage T4 DNA packaging mechanism
    • Black LW. 2015. Old, new, and widely true: the bacteriophage T4 DNA packaging mechanism. Virology 479-480:650-656. http://dx.doi.org/10.1016/j.virol.2015.01.015.
    • (2015) Virology , vol.479-480 , pp. 650-656
    • Black, L.W.1
  • 23
    • 77349091984 scopus 로고    scopus 로고
    • DNApackaging-associated hyper-capsid expansion of bacteriophage T3
    • Serwer P, Wright ET, Hakala K, Weintraub ST, Su M, Jiang W. 2010. DNApackaging-associated hyper-capsid expansion of bacteriophage T3. J Mol Biol 397:361-374. http://dx.doi.org/10.1016/j.jmb.2010.01.058.
    • (2010) J Mol Biol , vol.397 , pp. 361-374
    • Serwer, P.1    Wright, E.T.2    Hakala, K.3    Weintraub, S.T.4    Su, M.5    Jiang, W.6
  • 24
    • 0019378381 scopus 로고
    • DNA replication of bacteriophage T5. 3. Studies on the structure of concatemeric T5 DNA
    • Everett RD. 1981. DNA replication of bacteriophage T5. 3. Studies on the structure of concatemeric T5 DNA. J Gen Virol 52:25-38.
    • (1981) J Gen Virol , vol.52 , pp. 25-38
    • Everett, R.D.1
  • 25
    • 75849141082 scopus 로고    scopus 로고
    • Gp15 and gp16 cooperate in translocating bacteriophage T7 DNA into the infected cell
    • Chang CY, Kemp P, Molineux IJ. 2010. Gp15 and gp16 cooperate in translocating bacteriophage T7 DNA into the infected cell. Virology 398: 176-186. http://dx.doi.org/10.1016/j.virol.2009.12.002.
    • (2010) Virology , vol.398 , pp. 176-186
    • Chang, C.Y.1    Kemp, P.2    Molineux, I.J.3
  • 26
    • 0027463091 scopus 로고
    • Physical and kinetic characterization of the DNA packaging enzyme from bacteriophage lambda
    • Tomka MA, Catalano CE. 1993. Physical and kinetic characterization of the DNA packaging enzyme from bacteriophage lambda. J Biol Chem 268:3056-3065.
    • (1993) J Biol Chem , vol.268 , pp. 3056-3065
    • Tomka, M.A.1    Catalano, C.E.2
  • 27
    • 77951245717 scopus 로고    scopus 로고
    • Direct interaction of the bacteriophage SPP1 packaging ATPase with the portal protein
    • Oliveira L, Cuervo A, Tavares P. 2010. Direct interaction of the bacteriophage SPP1 packaging ATPase with the portal protein. J Biol Chem 285:7366-7373. http://dx.doi.org/10.1074/jbc.M109.061010.
    • (2010) J Biol Chem , vol.285 , pp. 7366-7373
    • Oliveira, L.1    Cuervo, A.2    Tavares, P.3
  • 28
    • 84901951285 scopus 로고    scopus 로고
    • Common mechanisms of DNA translocation motors in bacteria and viruses using one-way revolution mechanism without rotation
    • Guo P, Zhao Z, Haak J, Wang S, Wu D, Meng B, Weitao T. 2014. Common mechanisms of DNA translocation motors in bacteria and viruses using one-way revolution mechanism without rotation. Biotechnol Adv 32:853-872. http://dx.doi.org/10.1016/j.biotechadv.2014.01.006.
    • (2014) Biotechnol Adv , vol.32 , pp. 853-872
    • Guo, P.1    Zhao, Z.2    Haak, J.3    Wang, S.4    Wu, D.5    Meng, B.6    Weitao, T.7
  • 29
    • 74549198854 scopus 로고    scopus 로고
    • Eukaryotic large nucleocytoplasmic DNA viruses: clusters of orthologous genes and reconstruction of viral genome evolution
    • Yutin N, Wolf YI, Raoult D, Koonin EV. 2009. Eukaryotic large nucleocytoplasmic DNA viruses: clusters of orthologous genes and reconstruction of viral genome evolution. Virol J 6:223. http://dx.doi.org/10.1186 /1743-422X-6-223.
    • (2009) Virol J , vol.6 , pp. 223
    • Yutin, N.1    Wolf, Y.I.2    Raoult, D.3    Koonin, E.V.4
  • 30
    • 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
    • Iyer LM, Makarova KS, Koonin EV, Aravind L. 2004. 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 32:5260-5279. http://dx.doi.org/10.1093/nar/gkh828.
    • (2004) Nucleic Acids Res , vol.32 , pp. 5260-5279
    • Iyer, L.M.1    Makarova, K.S.2    Koonin, E.V.3    Aravind, L.4
  • 31
    • 0032146388 scopus 로고    scopus 로고
    • ATP-reactive sites in the bacteriophage lambda packaging protein terminase lie in the N-termini of its subunits, gpA and gpNu1
    • Babbar BK, Gold M. 1998. ATP-reactive sites in the bacteriophage lambda packaging protein terminase lie in the N-termini of its subunits, gpA and gpNu1. Virology 247:251-264. http://dx.doi.org/10.1006/viro.1998.9221.
    • (1998) Virology , vol.247 , pp. 251-264
    • Babbar, B.K.1    Gold, M.2
  • 32
    • 0032110708 scopus 로고    scopus 로고
    • Inter-RNA interaction of phage phi29 pRNA to form a hexameric complex for viral DNA transportation
    • Guo P, Zhang C, Chen C, Trottier M, Garver K. 1998. Inter-RNA interaction of phage phi29 pRNA to form a hexameric complex for viral DNA transportation. Mol Cell 2:149-155. http://dx.doi.org/10.1016 /S1097-2765(00)80124-0.
    • (1998) Mol Cell , vol.2 , pp. 149-155
    • Guo, P.1    Zhang, C.2    Chen, C.3    Trottier, M.4    Garver, K.5
  • 33
    • 0032111970 scopus 로고    scopus 로고
    • Function of hexameric RNA in packaging of bacteriophage phi29 DNA in vitro
    • Zhang F, Lemieux S, Wu X, St-Arnaud S, McMurray CT, Major F, Anderson D. 1998. Function of hexameric RNA in packaging of bacteriophage phi29 DNA in vitro. Mol Cell 2:141-147. http://dx.doi.org/10.1016/S1097-2765(00)80123-9.
    • (1998) Mol Cell , vol.2 , pp. 141-147
    • Zhang, F.1    Lemieux, S.2    Wu, X.3    St-Arnaud, S.4    McMurray, C.T.5    Major, F.6    Anderson, D.7
  • 34
    • 0032563227 scopus 로고    scopus 로고
    • BacteriophageDNApackaging: RNA gears in aDNA transport machine
    • Hendrix RW. 1998. BacteriophageDNApackaging: RNA gears in aDNA transport machine. Cell 94:147-150. http://dx.doi.org/10.1016/S0092-8674(00)81413-0.
    • (1998) Cell , vol.94 , pp. 147-150
    • Hendrix, R.W.1
  • 35
    • 84879785627 scopus 로고    scopus 로고
    • The ATPase of the phi29 DNA-packaging motor is a member of the hexameric AAA+ superfamily
    • Schwartz C, De Donatis GM, Fang H, Guo P. 2013. The ATPase of the phi29 DNA-packaging motor is a member of the hexameric AAA+ superfamily. Virology 443:20-27. http://dx.doi.org/10.1016/j.virol.2013.04.004.
    • (2013) Virology , vol.443 , pp. 20-27
    • Schwartz, C.1    De Donatis, G.M.2    Fang, H.3    Guo, P.4
  • 36
    • 0034685605 scopus 로고    scopus 로고
    • Topology of the components of the DNA packaging machinery in the phage phi29 prohead
    • Ibarra B, Caston JR, Llorca O, Valle M, Valpuesta JM, Carrascosa JL. 2000. Topology of the components of the DNA packaging machinery in the phage phi29 prohead. J Mol Biol 298:807-815. http://dx.doi.org/10.1006/jmbi.2000.3712.
    • (2000) J Mol Biol , vol.298 , pp. 807-815
    • Ibarra, B.1    Caston, J.R.2    Llorca, O.3    Valle, M.4    Valpuesta, J.M.5    Carrascosa, J.L.6
  • 37
    • 33846551354 scopus 로고    scopus 로고
    • Counting of six pRNAs of phi29 DNA-packaging motor with customized single molecule dual-view system
    • Shu D, Zhang H, Jin J, Guo P. 2007. Counting of six pRNAs of phi29 DNA-packaging motor with customized single molecule dual-view system. EMBO J 26:527-537. http://dx.doi.org/10.1038/sj.emboj.7601506.
    • (2007) EMBO J , vol.26 , pp. 527-537
    • Shu, D.1    Zhang, H.2    Jin, J.3    Guo, P.4
  • 38
    • 38449092849 scopus 로고    scopus 로고
    • Grouping of ferritin and gold nanoparticles conjugated to pRNA of the phage phi29 DNA-packaging motor
    • Moll D, Guo P. 2007. Grouping of ferritin and gold nanoparticles conjugated to pRNA of the phage phi29 DNA-packaging motor. J Nanosci Nanotech 7:3257-3267. http://dx.doi.org/10.1166/jnn.2007.914.
    • (2007) J Nanosci Nanotech , vol.7 , pp. 3257-3267
    • Moll, D.1    Guo, P.2
  • 39
    • 56649091437 scopus 로고    scopus 로고
    • Novel mechanism of hexamer ring assembly in protein/RNA interactions revealed by single molecule imaging
    • Xiao F, Zhang H, Guo P. 2008. Novel mechanism of hexamer ring assembly in protein/RNA interactions revealed by single molecule imaging. Nucleic Acids Res 36:6620-6632. http://dx.doi.org/10.1093/nar /gkn669.
    • (2008) Nucleic Acids Res , vol.36 , pp. 6620-6632
    • Xiao, F.1    Zhang, H.2    Guo, P.3
  • 40
    • 84883203974 scopus 로고    scopus 로고
    • Crystal structure of 3WJ core revealing divalent ion-promoted thermostability and assembly of the Phi29 hexameric motor pRNA
    • Zhang H, Endrizzi JA, Shu Y, Haque F, Sauter C, Shlyakhtenko LS, Lyubchenko Y, Guo P, Chi YI. 2013. Crystal structure of 3WJ core revealing divalent ion-promoted thermostability and assembly of the Phi29 hexameric motor pRNA. RNA 19:1226-1237. http://dx.doi.org /10.1261/rna.037077.112.
    • (2013) RNA , vol.19 , pp. 1226-1237
    • Zhang, H.1    Endrizzi, J.A.2    Shu, Y.3    Haque, F.4    Sauter, C.5    Shlyakhtenko, L.S.6    Lyubchenko, Y.7    Guo, P.8    Chi, Y.I.9
  • 41
    • 0000019034 scopus 로고    scopus 로고
    • New approaches to stoichiometry determination and mechanism investigation on RNA involved in intermediate reactions
    • Chen C, Trottier M, Guo P. 1997. New approaches to stoichiometry determination and mechanism investigation on RNA involved in intermediate reactions. Nucleic Acids Symp Ser 36:190-193.
    • (1997) Nucleic Acids Symp Ser , vol.36 , pp. 190-193
    • Chen, C.1    Trottier, M.2    Guo, P.3
  • 42
    • 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 71:487-494.
    • (1997) J Virol , vol.71 , pp. 487-494
    • Trottier, M.1    Guo, P.2
  • 43
    • 1642325936 scopus 로고    scopus 로고
    • Evolutionary history and higher order classification of AAA plus ATPases
    • Iyer LM, Leipe DD, Koonin EV, Aravind L. 2004. Evolutionary history and higher order classification of AAA plus ATPases. J Struct Biol 146: 11-31. http://dx.doi.org/10.1016/j.jsb.2003.10.010.
    • (2004) J Struct Biol , vol.146 , pp. 11-31
    • Iyer, L.M.1    Leipe, D.D.2    Koonin, E.V.3    Aravind, L.4
  • 44
    • 79952816898 scopus 로고    scopus 로고
    • Structure and mechanism of the hexameric MecA-ClpC molecular machine
    • Wang F, Mei Z, Qi Y, Yan C, Hu Q, Wang J, Shi Y. 2011. Structure and mechanism of the hexameric MecA-ClpC molecular machine. Nature 471:331-335. http://dx.doi.org/10.1038/nature09780.
    • (2011) Nature , vol.471 , pp. 331-335
    • Wang, F.1    Mei, Z.2    Qi, Y.3    Yan, C.4    Hu, Q.5    Wang, J.6    Shi, Y.7
  • 45
    • 1642265785 scopus 로고    scopus 로고
    • EM single particle analysis of the ATP-dependent BchI complex of magnesium chelatase: an AAA(+) hexamer
    • Willows RD, Hansson A, Birch D, Al-Karadaghi S, Hansson M. 2004. EM single particle analysis of the ATP-dependent BchI complex of magnesium chelatase: an AAA(+) hexamer. J Struct Biol 146:227-233. http: //dx.doi.org/10.1016/j.jsb.2003.11.019.
    • (2004) J Struct Biol , vol.146 , pp. 227-233
    • Willows, R.D.1    Hansson, A.2    Birch, D.3    Al-Karadaghi, S.4    Hansson, M.5
  • 46
    • 33746987484 scopus 로고    scopus 로고
    • Double-stranded DNA translocation: structure and mechanism of hexa-meric FtsK
    • Massey TH, Mercogliano CP, Yates J, Sherratt DJ, Lowe J. 2006. Double-stranded DNA translocation: structure and mechanism of hexa-meric FtsK. Mol Cell 23:457-469. http://dx.doi.org/10.1016/j.molcel.2006.06.019.
    • (2006) Mol Cell , vol.23 , pp. 457-469
    • Massey, T.H.1    Mercogliano, C.P.2    Yates, J.3    Sherratt, D.J.4    Lowe, J.5
  • 47
    • 50949102397 scopus 로고    scopus 로고
    • Presence of the adenovirus IVa2 protein at a single vertex of the mature virion
    • Christensen JB, Byrd SA, Walker AK, Strahler JR, Andrews PC, Imperiale MJ. 2008. Presence of the adenovirus IVa2 protein at a single vertex of the mature virion. J Virol 82:9086-9093. http://dx.doi.org/10.1128/JVI.01024-08.
    • (2008) J Virol , vol.82 , pp. 9086-9093
    • Christensen, J.B.1    Byrd, S.A.2    Walker, A.K.3    Strahler, J.R.4    Andrews, P.C.5    Imperiale, M.J.6
  • 48
    • 13944275170 scopus 로고    scopus 로고
    • Functional interaction of the adenovirus IVa2 protein with adenovirus type 5 packaging sequences
    • Ostapchuk P, Yang J, Auffarth E, Hearing P. 2005. Functional interaction of the adenovirus IVa2 protein with adenovirus type 5 packaging sequences. J Virol 79:2831-2838. http://dx.doi.org/10.1128/JVI.79.5.2831-2838.2005.
    • (2005) J Virol , vol.79 , pp. 2831-2838
    • Ostapchuk, P.1    Yang, J.2    Auffarth, E.3    Hearing, P.4
  • 49
    • 0030871678 scopus 로고    scopus 로고
    • Capsid assembly and DNA packaging in herpes simplex virus
    • Homa FL, Brown JC. 1997. Capsid assembly and DNA packaging in herpes simplex virus. Rev Med Virol 7:107-122. http://dx.doi.org/10.1002/(SICI)1099-1654(199707)7:2<107::AID-RMV191>3.0.CO;2-M.
    • (1997) Rev Med Virol , vol.7 , pp. 107-122
    • Homa, F.L.1    Brown, J.C.2
  • 51
    • 84878563524 scopus 로고    scopus 로고
    • The structure of the herpes simplex virus DNA-packaging terminase pUL15 nuclease domain suggests an evolutionary lineage among eukaryotic and prokaryotic viruses
    • Selvarajan Sigamani S, Zhao H, Kamau YN, Baines JD, Tang L. 2013. The structure of the herpes simplex virus DNA-packaging terminase pUL15 nuclease domain suggests an evolutionary lineage among eukaryotic and prokaryotic viruses. J Virol 87:7140-7148. http://dx.doi.org/10.1128/JVI.00311-13.
    • (2013) J Virol , vol.87 , pp. 7140-7148
    • Selvarajan Sigamani, S.1    Zhao, H.2    Kamau, Y.N.3    Baines, J.D.4    Tang, L.5
  • 53
    • 80054814749 scopus 로고    scopus 로고
    • Distant Mimivirus relative with a larger genome highlights the fundamental features of Megaviridae
    • Arslan D, Legendre M, Seltzer V, Abergel C, Claverie JM. 2011. Distant Mimivirus relative with a larger genome highlights the fundamental features of Megaviridae. Proc Natl Acad Sci U S A 108:17486-17491. http: //dx.doi.org/10.1073/pnas.1110889108.
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 17486-17491
    • Arslan, D.1    Legendre, M.2    Seltzer, V.3    Abergel, C.4    Claverie, J.M.5
  • 55
    • 84899845883 scopus 로고    scopus 로고
    • Genome segregation and packaging machinery in Acanthamoeba polyphaga mimivirus is reminiscent of bacterial apparatus
    • Chelikani V, Ranjan T, Zade A, Shukla A, Kondabagil K. 2014. Genome segregation and packaging machinery in Acanthamoeba polyphaga mimivirus is reminiscent of bacterial apparatus. J Virol 88: 6069-6075. http://dx.doi.org/10.1128/JVI.03199-13.
    • (2014) J Virol , vol.88 , pp. 6069-6075
    • Chelikani, V.1    Ranjan, T.2    Zade, A.3    Shukla, A.4    Kondabagil, K.5
  • 56
    • 12944326291 scopus 로고    scopus 로고
    • A virus with big ambitions
    • Ghedin E, Fraser CM. 2005. A virus with big ambitions. Trends Microbiol 13:56-57. http://dx.doi.org/10.1016/j.tim.2004.12.008.
    • (2005) Trends Microbiol , vol.13 , pp. 56-57
    • Ghedin, E.1    Fraser, C.M.2
  • 57
    • 34250855598 scopus 로고    scopus 로고
    • The discovery and characterization of Mimivirus, the largest known virus and putative pneumonia agent
    • Raoult D, La Scola B, Birtles R. 2007. The discovery and characterization of Mimivirus, the largest known virus and putative pneumonia agent. Clin Infect Dis 45:95-102. http://dx.doi.org/10.1086/518608.
    • (2007) Clin Infect Dis , vol.45 , pp. 95-102
    • Raoult, D.1    La Scola, B.2    Birtles, R.3
  • 58
    • 45149118680 scopus 로고    scopus 로고
    • Distinct DNA exit and packaging portals in the virus Acanthamoeba polyphaga mimivirus
    • Zauberman N, Mutsafi Y, Halevy DB, Shimoni E, Klein E, Xiao C, Sun S, Minsky A. 2008. Distinct DNA exit and packaging portals in the virus Acanthamoeba polyphaga mimivirus. PLoS Biol 6:e114. http://dx.doi.org/10.1371/journal.pbio.0060114.
    • (2008) PLoS Biol , vol.6 , pp. e114
    • Zauberman, N.1    Mutsafi, Y.2    Halevy, D.B.3    Shimoni, E.4    Klein, E.5    Xiao, C.6    Sun, S.7    Minsky, A.8
  • 60
    • 0002971370 scopus 로고
    • Replication of poxviruses
    • Fields BN, (ed). Raven Press, New York, NY.
    • Moss B. 1985. Replication of poxviruses, p 685-703. In Fields BN, (ed), Virology. Raven Press, New York, NY.
    • (1985) Virology , pp. 685-703
    • Moss, B.1
  • 61
    • 84859298657 scopus 로고    scopus 로고
    • Sequential action of ATPase, ATP, ADP, Pi and dsDNA in procapsid-free system to enlighten mechanism in viral dsDNA packaging
    • Schwartz C, Fang H, Huang L, Guo P. 2012. Sequential action of ATPase, ATP, ADP, Pi and dsDNA in procapsid-free system to enlighten mechanism in viral dsDNA packaging. Nucleic Acids Res 40:2577-2586. http://dx.doi.org/10.1093/nar/gkr841.
    • (2012) Nucleic Acids Res , vol.40 , pp. 2577-2586
    • Schwartz, C.1    Fang, H.2    Huang, L.3    Guo, P.4
  • 62
    • 0030896203 scopus 로고    scopus 로고
    • Sequential action of six virus-encoded DNApackaging RNAs during phage phi29 genomic DNA translocation
    • Chen C, Guo P. 1997. Sequential action of six virus-encoded DNApackaging RNAs during phage phi29 genomic DNA translocation. J Virol 71:3864-3871.
    • (1997) J Virol , vol.71 , pp. 3864-3871
    • Chen, C.1    Guo, P.2
  • 63
    • 84880368657 scopus 로고    scopus 로고
    • The adenovirus L4-22K protein has distinct functions in the posttranscriptional regulation of gene expression and encapsidation of the viral genome
    • Guimet D, Hearing P. 2013. The adenovirus L4-22K protein has distinct functions in the posttranscriptional regulation of gene expression and encapsidation of the viral genome. J Virol 87:7688-7699. http://dx.doi.org/10.1128/JVI.00859-13.
    • (2013) J Virol , vol.87 , pp. 7688-7699
    • Guimet, D.1    Hearing, P.2
  • 64
    • 84878535432 scopus 로고    scopus 로고
    • The adenovirus L4-33K protein regulates both late gene expression patterns and viral DNA packaging
    • Wu K, Guimet D, Hearing P. 2013. The adenovirus L4-33K protein regulates both late gene expression patterns and viral DNA packaging. J Virol 87:6739-6747. http://dx.doi.org/10.1128/JVI.00652-13.
    • (2013) J Virol , vol.87 , pp. 6739-6747
    • Wu, K.1    Guimet, D.2    Hearing, P.3
  • 65
    • 0033604295 scopus 로고    scopus 로고
    • The role of the L4 33K gene in adenovirus infection
    • Fessler SP, Young CS. 1999. The role of the L4 33K gene in adenovirus infection. Virology 263:507-516. http://dx.doi.org/10.1006/viro.1999.9951.
    • (1999) Virology , vol.263 , pp. 507-516
    • Fessler, S.P.1    Young, C.S.2
  • 66
    • 0035950604 scopus 로고    scopus 로고
    • Truncation of the human adenovirus type 5 L4 33-kDa protein: evidence for an essential role of the carboxy-terminus in the viral infectious cycle
    • Finnen RL, Biddle JF, Flint J. 2001. Truncation of the human adenovirus type 5 L4 33-kDa protein: evidence for an essential role of the carboxy-terminus in the viral infectious cycle. Virology 289:388-399. http://dx.doi.org/10.1006/viro.2001.1130.
    • (2001) Virology , vol.289 , pp. 388-399
    • Finnen, R.L.1    Biddle, J.F.2    Flint, J.3
  • 67
    • 0019789301 scopus 로고
    • Late nonstructural 100,000-and 33,000-dalton proteins of adenovirus type 2. II. Immunological and protein chemical analysis
    • Gambke C, Deppert W. 1981. Late nonstructural 100,000-and 33,000-dalton proteins of adenovirus type 2. II. Immunological and protein chemical analysis. J Virol 40:594-598.
    • (1981) J Virol , vol.40 , pp. 594-598
    • Gambke, C.1    Deppert, W.2
  • 68
    • 2542489189 scopus 로고    scopus 로고
    • Role of bovine adenovirus-3 33K protein in viral replication
    • Kulshreshtha V, Babiuk LA, Tikoo SK. 2004. Role of bovine adenovirus-3 33K protein in viral replication. Virology 323:59-69. http://dx.doi.org/10.1016/j.virol.2004.02.024.
    • (2004) Virology , vol.323 , pp. 59-69
    • Kulshreshtha, V.1    Babiuk, L.A.2    Tikoo, S.K.3
  • 69
    • 0027413261 scopus 로고
    • Gene A32 product of vaccinia virus may be an ATPase involved in viral-DNA packaging as indicated by sequence comparisons with other putative viral ATPases
    • Koonin EV, Senkevich TG, Chernos VI. 1993. Gene A32 product of vaccinia virus may be an ATPase involved in viral-DNA packaging as indicated by sequence comparisons with other putative viral ATPases. Virus Genes 7:89-94. http://dx.doi.org/10.1007/BF01702351.
    • (1993) Virus Genes , vol.7 , pp. 89-94
    • Koonin, E.V.1    Senkevich, T.G.2    Chernos, V.I.3
  • 70
    • 0038027004 scopus 로고    scopus 로고
    • Herpes simplex virus type 1 portal protein UL6 interacts with the putative terminase subunits UL15 and UL28
    • White CA, Stow ND, Patel AH, Hughes M, Preston VG. 2003. Herpes simplex virus type 1 portal protein UL6 interacts with the putative terminase subunits UL15 and UL28. J Virol 77:6351-6358. http://dx.doi.org/10.1128/JVI.77.11.6351-6358.2003.
    • (2003) J Virol , vol.77 , pp. 6351-6358
    • White, C.A.1    Stow, N.D.2    Patel, A.H.3    Hughes, M.4    Preston, V.G.5
  • 71
    • 33744931114 scopus 로고    scopus 로고
    • The putative terminase subunit of herpes simplex virus 1 encoded by UL28 is necessary and sufficient to mediate interaction between pUL15 and pUL33
    • Yang K, Baines JD. 2006. The putative terminase subunit of herpes simplex virus 1 encoded by UL28 is necessary and sufficient to mediate interaction between pUL15 and pUL33. J Virol 80:5733-5739. http://dx.doi.org/10.1128/JVI.00125-06.
    • (2006) J Virol , vol.80 , pp. 5733-5739
    • Yang, K.1    Baines, J.D.2
  • 72
    • 0036529667 scopus 로고    scopus 로고
    • The terminase subunits pUL56 and pUL89 of human cytomegalovirus are DNA-metabolizing proteins with toroidal structure
    • Scheffczik H, Savva CG, Holzenburg A, Kolesnikova L, Bogner E. 2002. The terminase subunits pUL56 and pUL89 of human cytomegalovirus are DNA-metabolizing proteins with toroidal structure. Nucleic Acids Res 30:1695-1703. http://dx.doi.org/10.1093/nar/30.7.1695.
    • (2002) Nucleic Acids Res , vol.30 , pp. 1695-1703
    • Scheffczik, H.1    Savva, C.G.2    Holzenburg, A.3    Kolesnikova, L.4    Bogner, E.5
  • 73
    • 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. http://dx.doi.org/10.1159/000107603.
    • (2007) Genome Dyn , vol.3 , pp. 48-65
    • Burroughs, A.M.1    Iyer, L.M.2    Aravind, L.3
  • 74
    • 84908258828 scopus 로고    scopus 로고
    • Revisiting the genome packaging in viruses with lessons from the "Giants."
    • Chelikani V, Ranjan T, Kondabagil K. 2014. Revisiting the genome packaging in viruses with lessons from the "Giants." Virology 466-467: 15-26. http://dx.doi.org/10.1016/j.virol.2014.06.022.
    • (2014) Virology , vol.466-467 , pp. 15-26
    • Chelikani, V.1    Ranjan, T.2    Kondabagil, K.3
  • 75
    • 0032500539 scopus 로고    scopus 로고
    • Sequential hydrolysis of ATP molecules bound in interacting catalytic sites of Escherichia coli transcription termination protein Rho
    • Stitt BL, Xu Y. 1998. Sequential hydrolysis of ATP molecules bound in interacting catalytic sites of Escherichia coli transcription termination protein Rho. J Biol Chem 273:26477-26486. http://dx.doi.org/10.1074 /jbc.273.41.26477.
    • (1998) J Biol Chem , vol.273 , pp. 26477-26486
    • Stitt, B.L.1    Xu, Y.2
  • 76
    • 0032562663 scopus 로고    scopus 로고
    • Tenascin-C hexabrachion assembly is a sequential two-step process initiated by coiled-coil alpha-helices
    • Kammerer RA, Schulthess T, Landwehr R, Lustig A, Fischer D, Engel J. 1998. Tenascin-C hexabrachion assembly is a sequential two-step process initiated by coiled-coil alpha-helices. J Biol Chem 273:10602-10608. http://dx.doi.org/10.1074/jbc.273.17.10602.
    • (1998) J Biol Chem , vol.273 , pp. 10602-10608
    • Kammerer, R.A.1    Schulthess, T.2    Landwehr, R.3    Lustig, A.4    Fischer, D.5    Engel, J.6
  • 77
    • 20744434561 scopus 로고    scopus 로고
    • Cooperative mechanism of RNA packaging motor
    • Lisal J, Tuma R. 2005. Cooperative mechanism of RNA packaging motor. J Biol Chem 280:23157-23164. http://dx.doi.org/10.1074/jbc.M502658200.
    • (2005) J Biol Chem , vol.280 , pp. 23157-23164
    • Lisal, J.1    Tuma, R.2
  • 78
    • 0034254813 scopus 로고    scopus 로고
    • Detailed characterization of the cooperative mechanism of Ca(2+) binding and catalytic activation in the Ca(2+) transport (SERCA) ATPase
    • Zhang Z, Lewis D, Strock C, Inesi G, Nakasako M, Nomura H, Toyoshima C. 2000. Detailed characterization of the cooperative mechanism of Ca(2+) binding and catalytic activation in the Ca(2+) transport (SERCA) ATPase. Biochemistry 39:8758-8767. http://dx.doi.org /10.1021/bi000185m.
    • (2000) Biochemistry , vol.39 , pp. 8758-8767
    • Zhang, Z.1    Lewis, D.2    Strock, C.3    Inesi, G.4    Nakasako, M.5    Nomura, H.6    Toyoshima, C.7
  • 79
    • 0034695601 scopus 로고    scopus 로고
    • Ordered and cooperative binding of opposing globular domains of calmodulin to the plasma membrane Ca-ATPase
    • Sun H, Squier TC. 2000. Ordered and cooperative binding of opposing globular domains of calmodulin to the plasma membrane Ca-ATPase. J Biol Chem 275:1731-1738. http://dx.doi.org/10.1074/jbc.275.3.1731.
    • (2000) J Biol Chem , vol.275 , pp. 1731-1738
    • Sun, H.1    Squier, T.C.2
  • 80
    • 0025316679 scopus 로고
    • Kinetic analysis of cooperative interactions induced by Mn2+ binding to the chloroplast H(+)-ATPase
    • Hiller R, Carmeli C. 1990. Kinetic analysis of cooperative interactions induced by Mn2+ binding to the chloroplast H(+)-ATPase. Biochemistry 29:6186-6192. http://dx.doi.org/10.1021/bi00478a011.
    • (1990) Biochemistry , vol.29 , pp. 6186-6192
    • Hiller, R.1    Carmeli, C.2
  • 81
    • 0020410192 scopus 로고
    • Cooperative behavior of smooth muscle myosin
    • Persechini A, Hartshorne DJ. 1982. Cooperative behavior of smooth muscle myosin. Fed Proc 41:2868-2872.
    • (1982) Fed Proc , vol.41 , pp. 2868-2872
    • Persechini, A.1    Hartshorne, D.J.2
  • 82
    • 0029039737 scopus 로고
    • Sequential interactions of structural proteins in phage phi29 procapsid assembly
    • Lee CS, Guo P. 1995. Sequential interactions of structural proteins in phage phi29 procapsid assembly. J Virol 69:5024-5032.
    • (1995) J Virol , vol.69 , pp. 5024-5032
    • Lee, C.S.1    Guo, P.2
  • 83
    • 84878292282 scopus 로고    scopus 로고
    • Mechanism of one-way traffic of hexameric phi29 DNA packaging motor with four electropositive relaying layers facilitating anti-parallel revolution
    • Zhao Z, Khisamutdinov E, Schwartz C, Guo P. 2013. Mechanism of one-way traffic of hexameric phi29 DNA packaging motor with four electropositive relaying layers facilitating anti-parallel revolution. ACS Nano 7:4082-4092. http://dx.doi.org/10.1021/nn4002775.
    • (2013) ACS Nano , vol.7 , pp. 4082-4092
    • Zhao, Z.1    Khisamutdinov, E.2    Schwartz, C.3    Guo, P.4
  • 84
    • 84855423787 scopus 로고    scopus 로고
    • Role of channel lysines and "push through a one-way valve" mechanism of viral DNA packaging motor
    • Fang H, Jing P, Haque F, Guo P. 2012. Role of channel lysines and "push through a one-way valve" mechanism of viral DNA packaging motor. Biophys J 102:127-135. http://dx.doi.org/10.1016/j.bpj.2011.11.4013.
    • (2012) Biophys J , vol.102 , pp. 127-135
    • Fang, H.1    Jing, P.2    Haque, F.3    Guo, P.4
  • 85
    • 53749095256 scopus 로고    scopus 로고
    • Adenovirus IVa2 protein binds ATP
    • Ostapchuk P, Hearing P. 2008. Adenovirus IVa2 protein binds ATP. J Virol 82:10290-10294. http://dx.doi.org/10.1128/JVI.00882-08.
    • (2008) J Virol , vol.82 , pp. 10290-10294
    • Ostapchuk, P.1    Hearing, P.2
  • 86
    • 33745780727 scopus 로고    scopus 로고
    • The L4 22-kilodalton protein plays a role in packaging of the adenovirus genome
    • Ostapchuk P, Anderson ME, Chandrasekhar S, Hearing P. 2006. The L4 22-kilodalton protein plays a role in packaging of the adenovirus genome. J Virol 80:6973-6981. http://dx.doi.org/10.1128/JVI.00123-06.
    • (2006) J Virol , vol.80 , pp. 6973-6981
    • Ostapchuk, P.1    Anderson, M.E.2    Chandrasekhar, S.3    Hearing, P.4
  • 87
    • 36048969242 scopus 로고    scopus 로고
    • Ternary complex formation on the adenovirus packaging sequence by the IVa2 and L4 22-kilodalton proteins
    • Ewing SG, Byrd SA, Christensen JB, Tyler RE, Imperiale MJ. 2007. Ternary complex formation on the adenovirus packaging sequence by the IVa2 and L4 22-kilodalton proteins. J Virol 81:12450-12457. http: //dx.doi.org/10.1128/JVI.01470-07.
    • (2007) J Virol , vol.81 , pp. 12450-12457
    • Ewing, S.G.1    Byrd, S.A.2    Christensen, J.B.3    Tyler, R.E.4    Imperiale, M.J.5
  • 88
    • 33947427084 scopus 로고    scopus 로고
    • Formation of a multiple protein complex on the adenovirus packaging sequence by the IVa2 protein
    • Tyler RE, Ewing SG, Imperiale MJ. 2007. Formation of a multiple protein complex on the adenovirus packaging sequence by the IVa2 protein. J Virol 81:3447-3454. http://dx.doi.org/10.1128/JVI.02097-06.
    • (2007) J Virol , vol.81 , pp. 3447-3454
    • Tyler, R.E.1    Ewing, S.G.2    Imperiale, M.J.3
  • 89
    • 0026093940 scopus 로고
    • Regulation of the biosynthesis of subgroup C adenovirus protein IVa2
    • Winter N, D'Halluin JC. 1991. Regulation of the biosynthesis of subgroup C adenovirus protein IVa2. J Virol 65:5250-5259.
    • (1991) J Virol , vol.65 , pp. 5250-5259
    • Winter, N.1    D'Halluin, J.C.2
  • 90
    • 33645094402 scopus 로고    scopus 로고
    • Evidence that the SpoIIIE DNA translocase participates in membrane fusion during cytokinesis and engulfment
    • Liu NJ, Dutton RJ, Pogliano K. 2006. Evidence that the SpoIIIE DNA translocase participates in membrane fusion during cytokinesis and engulfment. Mol Microbiol 59:1097-1113. http://dx.doi.org/10.1111/j.1365-2958.2005.05004.x.
    • (2006) Mol Microbiol , vol.59 , pp. 1097-1113
    • Liu, N.J.1    Dutton, R.J.2    Pogliano, K.3
  • 93
    • 79954421946 scopus 로고    scopus 로고
    • Condensed DNA: condensing the concepts
    • Teif VB, Bohinc K. 2011. Condensed DNA: condensing the concepts. Prog Biophys Mol Biol 105:208-222. http://dx.doi.org/10.1016/j.pbiomolbio.2010.07.002.
    • (2011) Prog Biophys Mol Biol , vol.105 , pp. 208-222
    • Teif, V.B.1    Bohinc, K.2
  • 94
    • 77950455981 scopus 로고    scopus 로고
    • Strong intranucleoid interactions organize the Escherichia coli chromosome into a nucleoid filament
    • Wiggins PA, Cheveralls KC, Martin JS, Lintner R, Kondev J. 2010. Strong intranucleoid interactions organize the Escherichia coli chromosome into a nucleoid filament. Proc Natl Acad Sci U S A 107:4991-4995. http://dx.doi.org/10.1073/pnas.0912062107.
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 4991-4995
    • Wiggins, P.A.1    Cheveralls, K.C.2    Martin, J.S.3    Lintner, R.4    Kondev, J.5
  • 95
    • 0003903126 scopus 로고
    • Springer Verlag, New York, NY.
    • van Holde KE. 1989. Chromatin, p 69-180. Springer Verlag, New York, NY.
    • (1989) Chromatin , pp. 69-180
    • van Holde, K.E.1
  • 96
    • 0027965277 scopus 로고
    • A highly sensitive system for the assay of in vitro viral assembly of bacteriophage phi29 of Bacillus subtilis
    • Lee CS, Guo P. 1994. A highly sensitive system for the assay of in vitro viral assembly of bacteriophage phi29 of Bacillus subtilis. Virology 202: 1039-1042. http://dx.doi.org/10.1006/viro.1994.1434.
    • (1994) Virology , vol.202 , pp. 1039-1042
    • Lee, C.S.1    Guo, P.2
  • 97
    • 84901933120 scopus 로고    scopus 로고
    • Single-molecule imaging of FtsK translocation reveals mechanistic features of protein-protein collisions on DNA
    • Lee JY, Finkelstein IJ, Arciszewska LK, Sherratt DJ, Greene EC. 2014. Single-molecule imaging of FtsK translocation reveals mechanistic features of protein-protein collisions on DNA. Mol Cell 54:832-843. http: //dx.doi.org/10.1016/j.molcel.2014.03.033.
    • (2014) Mol Cell , vol.54 , pp. 832-843
    • Lee, J.Y.1    Finkelstein, I.J.2    Arciszewska, L.K.3    Sherratt, D.J.4    Greene, E.C.5
  • 98
    • 0029655643 scopus 로고    scopus 로고
    • Complete inhibition of virion assembly in vivo with mutantpRNAessential for phage phi29DNApackaging
    • Trottier M, Zhang CL, Guo P. 1996. Complete inhibition of virion assembly in vivo with mutantpRNAessential for phage phi29DNApackaging. J Virol 70:55-61.
    • (1996) J Virol , vol.70 , pp. 55-61
    • Trottier, M.1    Zhang, C.L.2    Guo, P.3
  • 99
    • 84912150523 scopus 로고    scopus 로고
    • Binomial distribution for quantification of protein subunits in biological nanoassemblies and functional nanomachines
    • Fang H, Zhang P, Huang LP, Zhao Z, Pi F, Montemagno C, Guo P. 2014. Binomial distribution for quantification of protein subunits in biological nanoassemblies and functional nanomachines. Nanomedicine 10:1433-1440. http://dx.doi.org/10.1016/j.nano.2014.03.005.
    • (2014) Nanomedicine , vol.10 , pp. 1433-1440
    • Fang, H.1    Zhang, P.2    Huang, L.P.3    Zhao, Z.4    Pi, F.5    Montemagno, C.6    Guo, P.7
  • 100
    • 0027185716 scopus 로고
    • Ion channel activity of influenza A virus M2 protein: characterization of the amantadine block
    • Wang C, Takeuchi K, Pinto LH, Lamb RA. 1993. Ion channel activity of influenza A virus M2 protein: characterization of the amantadine block. J Virol 67:5585-5594.
    • (1993) J Virol , vol.67 , pp. 5585-5594
    • Wang, C.1    Takeuchi, K.2    Pinto, L.H.3    Lamb, R.A.4
  • 102
    • 84927758199 scopus 로고    scopus 로고
    • Visualizing the global secondary structure of a viral RNA genome with cryo-electron microscopy
    • Garmann RF, Gopal A, Athavale SS, Knobler CM, Gelbart WM, Harvey SC. 2015. Visualizing the global secondary structure of a viral RNA genome with cryo-electron microscopy. RNA 21:877-886. http: //dx.doi.org/10.1261/rna.047506.114.
    • (2015) RNA , vol.21 , pp. 877-886
    • Garmann, R.F.1    Gopal, A.2    Athavale, S.S.3    Knobler, C.M.4    Gelbart, W.M.5    Harvey, S.C.6
  • 104
    • 84895109493 scopus 로고    scopus 로고
    • Bedaquiline-the first ATP synthase inhibitor against multi drug resistant tuberculosis
    • Lakshmanan M, Xavier AS. 2013. Bedaquiline-the first ATP synthase inhibitor against multi drug resistant tuberculosis. J Young Pharm 5:112-115. http://dx.doi.org/10.1016/j.jyp.2013.12.002.
    • (2013) J Young Pharm , vol.5 , pp. 112-115
    • Lakshmanan, M.1    Xavier, A.S.2
  • 105
    • 84904197168 scopus 로고    scopus 로고
    • Robustness of the rotary catalysis mechanism of F-1-ATPase
    • Watanabe R, Matsukage Y, Yukawa A, Tabata KV, Noji H. 2014. Robustness of the rotary catalysis mechanism of F-1-ATPase. J Biol Chem 289:19331-19340. http://dx.doi.org/10.1074/jbc.M114.569905.
    • (2014) J Biol Chem , vol.289 , pp. 19331-19340
    • Watanabe, R.1    Matsukage, Y.2    Yukawa, A.3    Tabata, K.V.4    Noji, H.5
  • 106
    • 0032568695 scopus 로고    scopus 로고
    • F1-ATPase is a highly efficient molecular motor that rotates with discrete 120 degree steps
    • Yasuda R, Noji H, Kinosita K, Jr, Yoshida M. 1998. F1-ATPase is a highly efficient molecular motor that rotates with discrete 120 degree steps. Cell 93:1117-1124. http://dx.doi.org/10.1016/S0092-8674(00) 81456-7.
    • (1998) Cell , vol.93 , pp. 1117-1124
    • Yasuda, R.1    Noji, H.2    Kinosita, K.3    Yoshida, M.4
  • 107
    • 0032478354 scopus 로고    scopus 로고
    • F1-ATPase: a rotary motor made of a single molecule
    • Kinosita K, Jr, Yasuda R, Noji H, Ishiwata S, Yoshida M. 1998. F1-ATPase: a rotary motor made of a single molecule. Cell 93:21-24. http://dx.doi.org/10.1016/S0092-8674(00)81142-3.
    • (1998) Cell , vol.93 , pp. 21-24
    • Kinosita, K.1    Yasuda, R.2    Noji, H.3    Ishiwata, S.4    Yoshida, M.5
  • 108
    • 0033607504 scopus 로고    scopus 로고
    • Molecular architecture of the rotary motor in ATP synthase
    • Stock D, Leslie AG, Walker JE. 1999. Molecular architecture of the rotary motor in ATP synthase. Science 286:1700-1705. http://dx.doi.org /10.1126/science.286.5445.1700.
    • (1999) Science , vol.286 , pp. 1700-1705
    • Stock, D.1    Leslie, A.G.2    Walker, J.E.3
  • 109
    • 0033581939 scopus 로고    scopus 로고
    • What makes ATP synthase spin?
    • Boyer PD. 1999. What makes ATP synthase spin? Nature 402:247-249. http://dx.doi.org/10.1038/46193.
    • (1999) Nature , vol.402 , pp. 247-249
    • Boyer, P.D.1
  • 110
    • 0034690806 scopus 로고    scopus 로고
    • Stepping rotation of F1-ATPase visualized through angleresolved single-fluorophore imaging
    • Adachi K, Yasuda R, Noji H, Itoh H, Harada Y, Yoshida M, Kinosita K, Jr. 2000. Stepping rotation of F1-ATPase visualized through angleresolved single-fluorophore imaging. Proc Natl Acad Sci U S A 97:7243-7247. http://dx.doi.org/10.1073/pnas.120174297.
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 7243-7247
    • Adachi, K.1    Yasuda, R.2    Noji, H.3    Itoh, H.4    Harada, Y.5    Yoshida, M.6    Kinosita, K.7
  • 111
    • 0034640290 scopus 로고    scopus 로고
    • The role of the DELSEED motif of the beta subunit in rotation of F1-ATPase
    • Hara KY, Noji H, Bald D, Yasuda R, Kinosita K, Jr, Yoshida M. 2000. The role of the DELSEED motif of the beta subunit in rotation of F1-ATPase. J Biol Chem 275:14260-14263. http://dx.doi.org/10.1074/jbc.275.19.14260.
    • (2000) J Biol Chem , vol.275 , pp. 14260-14263
    • Hara, K.Y.1    Noji, H.2    Bald, D.3    Yasuda, R.4    Kinosita, K.5    Yoshida, M.6
  • 113
    • 0034663715 scopus 로고    scopus 로고
    • Biological nano motor, ATP synthase F(o)F(1): from catalysis to gammaepsilonc(10-12) subunit assembly rotation
    • Wada Y, Sambongi Y, Futai M. 2000. Biological nano motor, ATP synthase F(o)F(1): from catalysis to gammaepsilonc(10-12) subunit assembly rotation. Biochim Biophys Acta 1459:499-505. http://dx.doi.org /10.1016/S0005-2728(00)00189-4.
    • (2000) Biochim Biophys Acta , vol.1459 , pp. 499-505
    • Wada, Y.1    Sambongi, Y.2    Futai, M.3
  • 114
    • 84885349814 scopus 로고    scopus 로고
    • Phosphate release coupled to rotary motion of F-1-ATPase
    • Okazaki K, Hummer G. 2013. Phosphate release coupled to rotary motion of F-1-ATPase. Proc Natl Acad SciUSA110:16468-16473. http: //dx.doi.org/10.1073/pnas.1305497110.
    • (2013) Proc Natl Acad Sci USA , vol.110 , pp. 16468-16473
    • Okazaki, K.1    Hummer, G.2
  • 115
    • 84875702025 scopus 로고    scopus 로고
    • Molecular dynamics simulations of yeast F-1-ATPase before and after 16 degrees rotation of the gamma subunit
    • Ito Y, Yoshidome T, Matubayasi N, Kinoshita M, Ikeguchi M. 2013. Molecular dynamics simulations of yeast F-1-ATPase before and after 16 degrees rotation of the gamma subunit. J Phys Chem B 117:3298-3307. http://dx.doi.org/10.1021/jp312499u.
    • (2013) J Phys Chem B , vol.117 , pp. 3298-3307
    • Ito, Y.1    Yoshidome, T.2    Matubayasi, N.3    Kinoshita, M.4    Ikeguchi, M.5
  • 117
    • 38749106195 scopus 로고    scopus 로고
    • Structure and mechanism of the M2 proton channel of influenza A virus
    • Schnell JR, Chou JJ. 2008. Structure and mechanism of the M2 proton channel of influenza A virus. Nature 451:591-595. http://dx.doi.org/10.1038/nature06531.
    • (2008) Nature , vol.451 , pp. 591-595
    • Schnell, J.R.1    Chou, J.J.2
  • 118
    • 0031800615 scopus 로고    scopus 로고
    • DNApackaging mutant: repression of the vaccinia virus A32 gene results in noninfectious, DNA-deficient, spherical, enveloped particles
    • Cassetti MC, Merchlinsky M, Wolffe EJ, Weisberg AS, Moss B. 1998. DNApackaging mutant: repression of the vaccinia virus A32 gene results in noninfectious, DNA-deficient, spherical, enveloped particles. J Virol 72:5769-5780.
    • (1998) J Virol , vol.72 , pp. 5769-5780
    • Cassetti, M.C.1    Merchlinsky, M.2    Wolffe, E.J.3    Weisberg, A.S.4    Moss, B.5
  • 119
    • 0141677711 scopus 로고    scopus 로고
    • Genetic analysis of the vaccinia virus I6 telomere-binding protein uncovers a key role in genome encapsidation
    • Grubisha O, Traktman P. 2003. Genetic analysis of the vaccinia virus I6 telomere-binding protein uncovers a key role in genome encapsidation. J Virol 77:10929-10942. http://dx.doi.org/10.1128/JVI.77.20.10929-10942.2003.
    • (2003) J Virol , vol.77 , pp. 10929-10942
    • Grubisha, O.1    Traktman, P.2
  • 120
    • 84990061958 scopus 로고    scopus 로고
    • Arginine finger regulates sequential action of asymmetrical hexameric ATPase in double-stranded DNA translocation motor
    • in press
    • Zhao Z, De-Donatis GM, Schwartz C, Fang H, Li J, Guo P. Arginine finger regulates sequential action of asymmetrical hexameric ATPase in double-stranded DNA translocation motor. Mol Cel Biol, in press. http: //dx.doi.org/10.1128/MCB.00142-16.
    • Mol Cel Biol
    • Zhao, Z.1    De-Donatis, G.M.2    Schwartz, C.3    Fang, H.4    Li, J.5    Guo, P.6
  • 121
    • 78049300491 scopus 로고    scopus 로고
    • FtsK DNA translocase: the fast motor that knows where it's going
    • Crozat E, Grainge I. 2010. FtsK DNA translocase: the fast motor that knows where it's going. Chembiochem 11:2232-2243. http://dx.doi.org /10.1002/cbic.201000347.
    • (2010) Chembiochem , vol.11 , pp. 2232-2243
    • Crozat, E.1    Grainge, I.2
  • 122
    • 84876817617 scopus 로고    scopus 로고
    • Visualization of uncorrelated, tandem symmetry mismatches in the internal genome packaging apparatus of bacteriophage T7
    • Guo F, Liu Z, Vago F, Ren Y, Wu W, Wright ET, Serwer P, Jiang W. 2013. Visualization of uncorrelated, tandem symmetry mismatches in the internal genome packaging apparatus of bacteriophage T7. Proc Natl Acad Sci U S A 110:6811-6816. http://dx.doi.org/10.1073 /pnas.1215563110.
    • (2013) Proc Natl Acad Sci U S A , vol.110 , pp. 6811-6816
    • Guo, F.1    Liu, Z.2    Vago, F.3    Ren, Y.4    Wu, W.5    Wright, E.T.6    Serwer, P.7    Jiang, W.8


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