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Volumn 80, Issue 1, 2016, Pages 161-186

Biological nanomotors with a revolution, linear, or rotation motion mechanism

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE; BACTERIAL PROTEIN; BACTERIOPHAGE DNA; CARRIER PROTEIN; DNA POLYMERASE; DOUBLE STRANDED DNA; DYNEIN ADENOSINE TRIPHOSPHATASE; HELICASE; KINESIN; MOLECULAR MOTOR; MYOSIN; RNA POLYMERASE; SINGLE STRANDED DNA; VIRUS DNA; DNA DIRECTED RNA POLYMERASE; DNA HELICASE; VIRAL PROTEIN;

EID: 84964068517     PISSN: 10922172     EISSN: 10985557     Source Type: Journal    
DOI: 10.1128/MMBR.00056-15     Document Type: Review
Times cited : (59)

References (227)
  • 1
    • 84964056348 scopus 로고    scopus 로고
    • The Sixth Scottish University. The Scots colleges abroad: 1575 to 1799
    • McCluskey R. 2013. The Sixth Scottish University. The Scots colleges abroad: 1575 to 1799. Catholic Histor Rev 99:360-361.
    • (2013) Catholic Histor Rev , vol.99 , pp. 360-361
    • McCluskey, R.1
  • 2
    • 0039538633 scopus 로고
    • Symmetry mismatch and DNA packaging in large bacteriophages
    • Hendrix RW. 1978. Symmetry mismatch and DNA packaging in large bacteriophages. Proc Natl Acad Sci U S A 75:4779-4783. http://dx.doi.org/10.1073/pnas.75.10.4779.
    • (1978) Proc Natl Acad Sci U S A , vol.75 , pp. 4779-4783
    • Hendrix, R.W.1
  • 3
    • 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 61:16-32. http://dx.doi.org/10.1111/j.1365-2958.2006.05203.x.
    • (2006) Mol Microbiol , vol.61 , pp. 16-32
    • Baumann, R.G.1    Mullaney, J.2    Black, L.W.3
  • 5
    • 54149110817 scopus 로고    scopus 로고
    • Bright-field analysis of phi29 DNA packaging motor using a magnetomechanical system
    • Chang C, Zhang H, Shu D, Guo P, Savran C. 2008. Bright-field analysis of phi29 DNA packaging motor using a magnetomechanical system. Appl Phys Lett 93:153902-153903. http://dx.doi.org/10.1063/1.3000606.
    • (2008) Appl Phys Lett , vol.93 , pp. 153902-153903
    • Chang, C.1    Zhang, H.2    Shu, D.3    Guo, P.4    Savran, C.5
  • 6
    • 84899563168 scopus 로고    scopus 로고
    • A viral packaging motor varies its DNA rotation and step size to preserve subunit coordination as the capsid fills
    • Liu S, Chistol G, Hetherington CL, Tafoya S, Aathavan K, Schnitzbauer J, Grimes S, Jardine PJ, Bustamante C. 2014. A viral packaging motor varies its DNA rotation and step size to preserve subunit coordination as the capsid fills. Cell 157:702-713. http://dx.doi.org/10.1016/j.cell.2014.02.034.
    • (2014) Cell , vol.157 , pp. 702-713
    • Liu, S.1    Chistol, G.2    Hetherington, C.L.3    Tafoya, S.4    Aathavan, K.5    Schnitzbauer, J.6    Grimes, S.7    Jardine, P.J.8    Bustamante, C.9
  • 7
    • 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
  • 9
    • 0036496185 scopus 로고    scopus 로고
    • Mechanism of the F1F0-type ATP synthase, a biological rotary motor
    • Capaldi RA, Aggeler R. 2002. Mechanism of the F1F0-type ATP synthase, a biological rotary motor. Trends Biochem Sci 27:154-160. http://dx.doi.org/10.1016/S0968-0004 (01) 02051-5.
    • (2002) Trends Biochem Sci , vol.27 , pp. 154-160
    • Capaldi, R.A.1    Aggeler, R.2
  • 10
    • 0003140116 scopus 로고
    • Motor proteins
    • Kreis T, Vale R ed, Oxford University Press, Oxford, United Kingdom
    • Vale R. 1993. Motor proteins, p 175-211. In Kreis T, Vale R (ed), Guidebook to the cytoskeletal and motor proteins. Oxford University Press, Oxford, United Kingdom.
    • (1993) Guidebook to the Cytoskeletal and Motor Proteins , pp. 175-211
    • Vale, R.1
  • 11
    • 0026425404 scopus 로고
    • Motor proteins. A brave new world for dynein
    • Goldstein L, Vale R. 1991. Motor proteins. A brave new world for dynein. Nature 352:569-570.
    • (1991) Nature , vol.352 , pp. 569-570
    • Goldstein, L.1    Vale, R.2
  • 12
    • 84879787373 scopus 로고    scopus 로고
    • Revolution 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. Revolution 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
  • 13
    • 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
  • 14
    • 84899892055 scopus 로고    scopus 로고
    • Biophysical studies reveal new evidence for one-way revolution mechanism of bacteriophage phi29 DNA packaging motor
    • Guo P. 2014. Biophysical studies reveal new evidence for one-way revolution mechanism of bacteriophage phi29 DNA packaging motor. Biophys J 106:1837-1838. http://dx.doi.org/10.1016/j.bpj.2014.03.041.
    • (2014) Biophys J , vol.106 , pp. 1837-1838
    • Guo, P.1
  • 15
    • 84901951285 scopus 로고    scopus 로고
    • Commonmechanisms 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. Commonmechanisms 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
  • 16
    • 84884504887 scopus 로고    scopus 로고
    • Discovery of a new motion mechanism of biomotors similar to the earth revolving around the sun without rotation
    • Guo P, Schwartz C, Haak J, Zhao Z. 2013. Discovery of a new motion mechanism of biomotors similar to the earth revolving around the sun without rotation. Virology 446:133-143. http://dx.doi.org/10.1016/j.virol.2013.07.025.
    • (2013) Virology , vol.446 , pp. 133-143
    • Guo, P.1    Schwartz, C.2    Haak, J.3    Zhao, Z.4
  • 17
    • 77952934976 scopus 로고    scopus 로고
    • Structural and functional insights into the myosin motor mechanism
    • Sweeney HL, Houdusse A. 2010. Structural and functional insights into the myosin motor mechanism. Annu Rev Biophys 39:539-557. http://dx.doi.org/10.1146/annurev. biophys.050708.133751.
    • (2010) Annu Rev Biophys , vol.39 , pp. 539-557
    • Sweeney, H.L.1    Houdusse, A.2
  • 18
    • 0031468103 scopus 로고    scopus 로고
    • The design plan of kinesin motors
    • Vale RD, Fletterick RJ. 1997. The design plan of kinesin motors. Annu Rev Cell Dev Biol 13:745-777. http://dx.doi.org/10.1146/annurev. cellbio.13.1.745.
    • (1997) Annu Rev Cell Dev Biol , vol.13 , pp. 745-777
    • Vale, R.D.1    Fletterick, R.J.2
  • 19
    • 84880597484 scopus 로고    scopus 로고
    • Big steps toward understanding dynein
    • Kikkawa M. 2013. Big steps toward understanding dynein. J Cell Biol 202:15-23. http://dx.doi.org/10.1083/jcb.201304099.
    • (2013) J Cell Biol , vol.202 , pp. 15-23
    • Kikkawa, M.1
  • 20
    • 0030715561 scopus 로고    scopus 로고
    • ATP synthase: An electrochemical transducer with rotatory mechanics
    • Junge W, Lill H, Engelbrecht S. 1997. ATP synthase: an electrochemical transducer with rotatory mechanics. Trends Biochem Sci 22:420-423. http://dx.doi.org/10.1016/S0968-0004 (97) 01129-8.
    • (1997) Trends Biochem Sci , vol.22 , pp. 420-423
    • Junge, W.1    Lill, H.2    Engelbrecht, S.3
  • 21
    • 0032478505 scopus 로고    scopus 로고
    • The turn of the screw: The bacterial flagellar motor
    • DeRosier DJ. 1998. The turn of the screw: the bacterial flagellar motor. Cell 93:17-20. http://dx.doi.org/10.1016/S0092-8674 (00) 81141-1.
    • (1998) Cell , vol.93 , pp. 17-20
    • DeRosier, D.J.1
  • 22
    • 33748768732 scopus 로고    scopus 로고
    • The archaeabacterial flagellar filament: A bacterial propeller with a pilus-like structure
    • Trachtenberg S, Cohen-Krausz S. 2006. The archaeabacterial flagellar filament: a bacterial propeller with a pilus-like structure. J Mol Microbiol Biotechnol 11:208-220. http://dx.doi.org/10.1159/000094055.
    • (2006) J Mol Microbiol Biotechnol , vol.11 , pp. 208-220
    • Trachtenberg, S.1    Cohen-Krausz, S.2
  • 23
    • 84964030719 scopus 로고
    • Generation of propulsive forces by cilia and flagella
    • Bereiter-Hahn J, Anderson OR, Reif WE ed, Springer, Berlin, Germany
    • Holwill MEJ, Satir P. 1987. Generation of propulsive forces by cilia and flagella, p 120-130. In: Bereiter-Hahn J, Anderson OR, Reif WE (ed), Cytomechanics-the mechanical basis of cell form and structure. Springer, Berlin, Germany.
    • (1987) Cytomechanics- The Mechanical Basis of Cell Form and Structure , pp. 120-130
    • Holwill, M.E.J.1    Satir, P.2
  • 24
    • 0034719392 scopus 로고    scopus 로고
    • The DExH protein NPH-II is a processive and directional motor for unwinding RNA
    • Jankowsky E, Gross CH, Shuman S, Pyle AM. 2000. The DExH protein NPH-II is a processive and directional motor for unwinding RNA. Nature 403:447-451. http://dx.doi.org/10.1038/35000239.
    • (2000) Nature , vol.403 , pp. 447-451
    • Jankowsky, E.1    Gross, C.H.2    Shuman, S.3    Pyle, A.M.4
  • 25
    • 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
  • 26
    • 33645828216 scopus 로고    scopus 로고
    • Single-particle light microscopy of bacteriophages
    • Serwer P, Wang HY. 2005. Single-particle light microscopy of bacteriophages. J Nanosci Nanotechnol 5:2014-2028. http://dx.doi.org/10.1166/jnn. 2005.447.
    • (2005) J Nanosci Nanotechnol , vol.5 , pp. 2014-2028
    • Serwer, P.1    Wang, H.Y.2
  • 27
    • 33746375404 scopus 로고    scopus 로고
    • Mechanism of DNA translocation in a replicative hexameric helicase
    • Enemark EJ, Joshua-Tor L. 2006. Mechanism of DNA translocation in a replicative hexameric helicase. Nature 442:270-275. http://dx.doi.org/10.1038/nature04943.
    • (2006) Nature , vol.442 , pp. 270-275
    • Enemark, E.J.1    Joshua-Tor, L.2
  • 28
    • 35348979683 scopus 로고    scopus 로고
    • Structure of hexameric DnaB helicase and its complex with a domain of DnaG primase
    • Bailey S, Eliason WK, Steitz TA. 2007. Structure of hexameric DnaB helicase and its complex with a domain of DnaG primase. Science 318:459-463. http://dx.doi.org/10.1126/science.1147353.
    • (2007) Science , vol.318 , pp. 459-463
    • Bailey, S.1    Eliason, W.K.2    Steitz, T.A.3
  • 29
    • 33748749364 scopus 로고    scopus 로고
    • Role of ATP hydrolysis in the DNA translocase activity of the bovine papillomavirus (BPV-1) E1 helicase
    • Castella S, Burgin D, Sanders CM. 2006. Role of ATP hydrolysis in the DNA translocase activity of the bovine papillomavirus (BPV-1) E1 helicase. Nucleic Acids Res 34:3731-3741. http://dx.doi.org/10.1093/nar/gkl554.
    • (2006) Nucleic Acids Res , vol.34 , pp. 3731-3741
    • Castella, S.1    Burgin, D.2    Sanders, C.M.3
  • 30
    • 0032582494 scopus 로고    scopus 로고
    • Force and velocity measured for single molecules of RNA polymerase
    • Wang MD, Schnitzer MJ, Yin H, Landick R, Gelles J, Block SM. 1998. Force and velocity measured for single molecules of RNA polymerase. Science 282:902-907. http://dx.doi.org/10.1126/science.282.5390.902.
    • (1998) Science , vol.282 , pp. 902-907
    • Wang, M.D.1    Schnitzer, M.J.2    Yin, H.3    Landick, R.4    Gelles, J.5    Block, S.M.6
  • 31
    • 0027976995 scopus 로고
    • Evidence supporting a tethered tracking model for helicase activity of Escherichia coli Rho factor
    • Steinmetz EJ, Platt T. 1994. Evidence supporting a tethered tracking model for helicase activity of Escherichia coli Rho factor. Proc Natl Acad Sci U S A 91:1401-1405. http://dx.doi.org/10.1073/pnas.91.4.1401.
    • (1994) Proc Natl Acad Sci U S A , vol.91 , pp. 1401-1405
    • Steinmetz, E.J.1    Platt, T.2
  • 32
    • 11144255128 scopus 로고    scopus 로고
    • Crystal structures of Escherichia coli RecA in complex with MgADP and MnAMP-PNP
    • Xing X, Bell CE. 2004. Crystal structures of Escherichia coli RecA in complex with MgADP and MnAMP-PNP. Biochemistry 43:16142-16152. http://dx.doi.org/10.1021/bi048165y.
    • (2004) Biochemistry , vol.43 , pp. 16142-16152
    • Xing, X.1    Bell, C.E.2
  • 33
    • 0242692609 scopus 로고    scopus 로고
    • The bacterial RecA protein as a motor protein
    • Cox MM. 2003. The bacterial RecA protein as a motor protein. Annu Rev Microbiol 57:551-577. http://dx.doi.org/10.1146/annurev. micro.57.030502.090953.
    • (2003) Annu Rev Microbiol , vol.57 , pp. 551-577
    • Cox, M.M.1
  • 34
    • 0035461311 scopus 로고    scopus 로고
    • ATP synthase- A marvellous rotary engine of the cell
    • Yoshida M, Muneyuki E, Hisabori T. 2001. ATP synthase-a marvellous rotary engine of the cell. Nat Rev Mol Cell Biol 2:669-677. http://dx.doi.org/10.1038/35089509.
    • (2001) Nat Rev Mol Cell Biol , vol.2 , pp. 669-677
    • Yoshida, M.1    Muneyuki, E.2    Hisabori, T.3
  • 35
    • 79957819196 scopus 로고    scopus 로고
    • Rotation and structure of FoF1-ATP synthase
    • Okuno D, Iino R, Noji H. 2011. Rotation and structure of FoF1-ATP synthase. J Biochem 149:655-664. http://dx.doi.org/10.1093/jb/mvr049.
    • (2011) J Biochem , vol.149 , pp. 655-664
    • Okuno, D.1    Iino, R.2    Noji, H.3
  • 36
    • 84861951502 scopus 로고    scopus 로고
    • Bacterial flagella: Flagellar motor
    • 19 April, John Wiley & Sons Ltd., Chichester, United Kingdom
    • Berry RM. 19 April 2001. Bacterial flagella: flagellar motor. In Encyclopedia of life sciences. John Wiley & Sons Ltd., Chichester, United Kingdom. http://dx.doi.org/10.1038/npg.els.0000744.
    • (2001) Encyclopedia of Life Sciences
    • Berry, R.M.1
  • 38
    • 0035804245 scopus 로고    scopus 로고
    • Direct observation of DNA rotation during transcription by Escherichia coliRNApolymerase
    • Harada Y, Ohara O, Takatsuki A, Itoh H, Shimamoto N, Kinosita K, Jr. 2001. Direct observation of DNA rotation during transcription by Escherichia coliRNApolymerase. Nature 409:113-115. http://dx.doi.org/10.1038/35051126.
    • (2001) Nature , vol.409 , pp. 113-115
    • Harada, Y.1    Ohara, O.2    Takatsuki, A.3    Itoh, H.4    Shimamoto, N.5    Kinosita, K.6
  • 39
    • 48249113056 scopus 로고    scopus 로고
    • Translocation and unwinding mechanisms of RNA and DNA helicases
    • Pyle AM. 2008. Translocation and unwinding mechanisms of RNA and DNA helicases. Annu Rev Biophys 37:317-336. http://dx.doi.org/10.1146/annurev. biophys.37.032807.125908.
    • (2008) Annu Rev Biophys , vol.37 , pp. 317-336
    • Pyle, A.M.1
  • 40
    • 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. http://dx.doi.org/10.1146/annurev. biochem.76.052305.115300.
    • (2007) Annu Rev Biochem , vol.76 , pp. 23-50
    • Singleton, M.R.1    Dillingham, M.S.2    Wigley, D.B.3
  • 42
    • 84946423579 scopus 로고    scopus 로고
    • An overview of the molecular mechanisms of recombinational DNA repair
    • Kowalczykowski SC. 2015. An overview of the molecular mechanisms of recombinational DNA repair. Cold Spring Harb Perspect Biol http://dx.doi.org/10.1101/cshperspect.a016410.
    • (2015) Cold Spring Harb Perspect Biol
    • Kowalczykowski, S.C.1
  • 43
    • 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
  • 44
    • 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
  • 45
    • 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
  • 46
    • 84919673907 scopus 로고    scopus 로고
    • The scrunchworm hypothesis: Transitions between A-DNA and B-DNA provide the driving force for genome packaging in double-stranded DNA bacteriophages
    • Harvey SC. 2015. The scrunchworm hypothesis: Transitions between A-DNA and B-DNA provide the driving force for genome packaging in double-stranded DNA bacteriophages. J Struct Biol 189:1-8. http://dx.doi.org/10.1016/j.jsb.2014.11.012.
    • (2015) J Struct Biol , vol.189 , pp. 1-8
    • Harvey, S.C.1
  • 47
    • 84870885884 scopus 로고    scopus 로고
    • Compression of the DNA substrate by a viral packaging motor is supported by removal of intercalating dye during translocation
    • Dixit AB, Ray K, Black LW. 2012. Compression of the DNA substrate by a viral packaging motor is supported by removal of intercalating dye during translocation. Proc Natl Acad Sci U S A 109:20419-20424. http://dx.doi.org/10.1073/pnas.1214318109.
    • (2012) Proc Natl Acad Sci U S A , vol.109 , pp. 20419-20424
    • Dixit, A.B.1    Ray, K.2    Black, L.W.3
  • 48
    • 75849131151 scopus 로고    scopus 로고
    • DNA crunching by a viral packaging motor: Compression of a procapsid-portal stalled Y-DNA substrate
    • Ray K, Sabanayagam CR, Lakowicz JR, Black LW. 2010. DNA crunching by a viral packaging motor: compression of a procapsid-portal stalled Y-DNA substrate. Virology 398:224-232. http://dx.doi.org/10.1016/j.virol.2009.11.047.
    • (2010) Virology , vol.398 , pp. 224-232
    • Ray, K.1    Sabanayagam, C.R.2    Lakowicz, J.R.3    Black, L.W.4
  • 49
    • 80052342523 scopus 로고    scopus 로고
    • Three reversible and controllable discrete steps of channel gating of a viralDNApackaging motor
    • Geng J, Fang H, Haque F, Zhang L, Guo P. 2011. Three reversible and controllable discrete steps of channel gating of a viralDNApackaging motor. Biomaterials 32:8234-8242. http://dx.doi.org/10.1016/j.biomaterials.2011.07.034.
    • (2011) Biomaterials , vol.32 , pp. 8234-8242
    • Geng, J.1    Fang, H.2    Haque, F.3    Zhang, L.4    Guo, P.5
  • 50
    • 84902546969 scopus 로고    scopus 로고
    • Finding of widespread viral and bacterial revolution 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 revolution 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
  • 51
    • 0022927155 scopus 로고
    • Computer graphic display method for visualizing three-dimensional biological structures
    • Jimenez J, Santisteban A, Carazo JM, Carrascosa JL. 1986. Computer graphic display method for visualizing three-dimensional biological structures. Science 232:1113-1115. http://dx.doi.org/10.1126/science.3754654.
    • (1986) Science , vol.232 , pp. 1113-1115
    • Jimenez, J.1    Santisteban, A.2    Carazo, J.M.3    Carrascosa, J.L.4
  • 52
    • 0036301072 scopus 로고    scopus 로고
    • Detailed architecture of a DNA translocating machine: The high-resolution structure of the bacteriophage phi29 connector particle
    • 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 315:663-676. http://dx.doi.org/10.1006/jmbi.2001.5278.
    • (2002) J Mol Biol , vol.315 , 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
  • 53
    • 0023225629 scopus 로고
    • A small viral RNA is required for in vitro packaging of bacteriophage phi29 DNA
    • Guo P, Erickson S, Anderson D. 1987. A small viral RNA is required for in vitro packaging of bacteriophage phi29 DNA. Science 236:690-694. http://dx.doi.org/10.1126/science.3107124.
    • (1987) Science , vol.236 , pp. 690-694
    • Guo, P.1    Erickson, S.2    Anderson, D.3
  • 54
    • 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
  • 55
    • 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
  • 56
    • 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
  • 57
    • 0023660940 scopus 로고
    • Prohead and DNA-gp3-dependent ATPase activity of the DNA packaging protein gp16 of bacteriophage phi29
    • Guo P, Peterson C, Anderson D. 1987. Prohead and DNA-gp3-dependent ATPase activity of the DNA packaging protein gp16 of bacteriophage phi29. J Mol Biol 197:229-236. http://dx.doi.org/10.1016/0022-2836 (87) 90121-5.
    • (1987) J Mol Biol , vol.197 , pp. 229-236
    • Guo, P.1    Peterson, C.2    Anderson, D.3
  • 58
    • 34248340401 scopus 로고    scopus 로고
    • Viral nanomotors for packaging of dsDNA and dsRNA
    • Guo PX, Lee TJ. 2007. Viral nanomotors for packaging of dsDNA and dsRNA. Mol Microbiol 64:886-903. http://dx.doi.org/10.1111/j.1365-2958.2007.05706.x.
    • (2007) Mol Microbiol , vol.64 , pp. 886-903
    • Guo, P.X.1    Lee, T.J.2
  • 59
    • 57649226492 scopus 로고    scopus 로고
    • The bacteriophage DNA packaging motor
    • Rao VB, Feiss M. 2008. The bacteriophage DNA packaging motor. Annu Rev Genet 42:647-681. http://dx.doi.org/10.1146/annurev. genet.42.110807.091545.
    • (2008) Annu Rev Genet , vol.42 , pp. 647-681
    • Rao, V.B.1    Feiss, M.2
  • 60
    • 84862878463 scopus 로고    scopus 로고
    • "Push through one-way valve" mechanism of viral DNA packaging
    • Zhang H, Schwartz C, De Donatis GM, Guo P. 2012. "Push through one-way valve" mechanism of viral DNA packaging. Adv Virus Res 83:415-465. http://dx.doi.org/10.1016/B978-0-12-394438-2.00009-8.
    • (2012) Adv Virus Res , vol.83 , pp. 415-465
    • Zhang, H.1    Schwartz, C.2    De Donatis, G.M.3    Guo, P.4
  • 62
    • 15244343074 scopus 로고    scopus 로고
    • Structure of the connector of bacteriophage T7 at 8A resolution: Structural homologies of a basic component of a DNA translocating machinery
    • Agirrezabala X, Martin-Benito J, Valle M, Gonzalez JM, Valencia A, Valpuesta JM, Carrascosa JL. 2005. Structure of the connector of bacteriophage T7 at 8A resolution: structural homologies of a basic component of a DNA translocating machinery. J Mol Biol 347:895-902. http://dx.doi.org/10.1016/j.jmb.2005.02.005.
    • (2005) J Mol Biol , vol.347 , pp. 895-902
    • Agirrezabala, X.1    Martin-Benito, J.2    Valle, M.3    Gonzalez, J.M.4    Valencia, A.5    Valpuesta, J.M.6    Carrascosa, J.L.7
  • 63
    • 0034716946 scopus 로고    scopus 로고
    • Genomic sequences of bacteriophages HK97 and HK022: Pervasive genetic mosaicism in the lambdoid bacteriophages
    • Juhala RJ, Ford ME, Duda RL, Youlton A, Hatfull GF, Hendrix RW. 2000. Genomic sequences of bacteriophages HK97 and HK022: pervasive genetic mosaicism in the lambdoid bacteriophages. J Mol Biol 299:27-51. http://dx.doi.org/10.1006/jmbi.2000.3729.
    • (2000) J Mol Biol , vol.299 , pp. 27-51
    • Juhala, R.J.1    Ford, M.E.2    Duda, R.L.3    Youlton, A.4    Hatfull, G.F.5    Hendrix, R.W.6
  • 64
    • 85027920272 scopus 로고    scopus 로고
    • Three-dimensional structure of a viral genome-delivery portal vertex
    • Olia AS, Prevelige PE, Johnson JE, Cingolani G. 2011. Three-dimensional structure of a viral genome-delivery portal vertex. Nat Struct Mol Biol 18:597-603. http://dx.doi.org/10.1038/nsmb.2023.
    • (2011) Nat Struct Mol Biol , vol.18 , pp. 597-603
    • Olia, A.S.1    Prevelige, P.E.2    Johnson, J.E.3    Cingolani, G.4
  • 66
    • 85027930977 scopus 로고    scopus 로고
    • Popping the cork: Mechanisms of phage genome ejection
    • Molineux IJ, Panja D. 2013. Popping the cork: mechanisms of phage genome ejection. Nat Rev Microbiol 11:194-204. http://dx.doi.org/10.1038/nrmicro2988.
    • (2013) Nat Rev Microbiol , vol.11 , pp. 194-204
    • Molineux, I.J.1    Panja, D.2
  • 67
    • 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 95:497-502. http://dx.doi.org/10.1529/biophysj.108.131797.
    • (2008) Biophys J , vol.95 , pp. 497-502
    • Petrov, A.S.1    Harvey, S.C.2
  • 68
    • 31844435708 scopus 로고    scopus 로고
    • Structure of epsilon15 bacteriophage reveals genome organization and DNA packaging/injection apparatus
    • Jiang W, Chang J, Jakana J, Weigele P, King J, Chiu W. 2006. Structure of epsilon15 bacteriophage reveals genome organization and DNA packaging/injection apparatus. Nature 439:612-616. http://dx.doi.org/10.1038/nature04487.
    • (2006) Nature , vol.439 , pp. 612-616
    • Jiang, W.1    Chang, J.2    Jakana, J.3    Weigele, P.4    King, J.5    Chiu, W.6
  • 69
    • 84941011872 scopus 로고    scopus 로고
    • Structural remodeling of bacteriophage T4 and host membranes during infection initiation
    • Hu B, Margolin W, Molineux IJ, Liu J. 2015. Structural remodeling of bacteriophage T4 and host membranes during infection initiation. Proc Natl Acad Sci U S A 112:E4919-E4928. http://dx.doi.org/10.1073/pnas.1501064112.
    • (2015) Proc Natl Acad Sci U S A , vol.112 , pp. E4919-E4928
    • Hu, B.1    Margolin, W.2    Molineux, I.J.3    Liu, J.4
  • 71
    • 44649136828 scopus 로고    scopus 로고
    • Asymmetric EM reveals new twists in phage phi29 biology
    • Duda RL, Conway JF. 2008. Asymmetric EM reveals new twists in phage phi29 biology. Structure 16:831-832. http://dx.doi.org/10.1016/j.str.2008.05.004.
    • (2008) Structure , vol.16 , pp. 831-832
    • Duda, R.L.1    Conway, J.F.2
  • 73
    • 84873097195 scopus 로고    scopus 로고
    • The bacteriophage t7 virion undergoes extensive structural remodeling during infection
    • Hu B, Margolin W, Molineux IJ, Liu J. 2013. The bacteriophage t7 virion undergoes extensive structural remodeling during infection. Science 339:576-579. http://dx.doi.org/10.1126/science.1231887.
    • (2013) Science , vol.339 , pp. 576-579
    • Hu, B.1    Margolin, W.2    Molineux, I.J.3    Liu, J.4
  • 74
    • 0031786575 scopus 로고    scopus 로고
    • Role of the C terminus of FtsK in Escherichia coli chromosome segregation
    • Yu XC, Weihe EK, Margolin W. 1998. Role of the C terminus of FtsK in Escherichia coli chromosome segregation. J Bacteriol 180:6424-6428.
    • (1998) J Bacteriol , vol.180 , pp. 6424-6428
    • Yu, X.C.1    Weihe, E.K.2    Margolin, W.3
  • 75
    • 0032927732 scopus 로고    scopus 로고
    • The cytoplasmic domain of FtsK protein is required for resolution of chromosome dimers
    • Steiner W, Liu G, Donachie WD, Kuempel P. 1999. The cytoplasmic domain of FtsK protein is required for resolution of chromosome dimers. Mol Microbiol 31:579-583. http://dx.doi.org/10.1046/j.1365-2958.1999.01198.x.
    • (1999) Mol Microbiol , vol.31 , pp. 579-583
    • Steiner, W.1    Liu, G.2    Donachie, W.D.3    Kuempel, P.4
  • 76
    • 78649610196 scopus 로고    scopus 로고
    • FtsK- A bacterial cell division checkpoint?
    • Grainge I. 2010. FtsK-a bacterial cell division checkpoint? Mol Microbiol 78:1055-1057. http://dx.doi.org/10.1111/j.1365-2958.2010.07411.x.
    • (2010) Mol Microbiol , vol.78 , pp. 1055-1057
    • Grainge, I.1
  • 77
    • 84860204938 scopus 로고    scopus 로고
    • Singlemolecule imaging of DNA curtains reveals mechanisms of KOPS sequence targeting by the DNA translocase FtsK
    • Lee JY, Finkelstein IJ, Crozat E, Sherratt DJ, Greene EC. 2012. Singlemolecule imaging of DNA curtains reveals mechanisms of KOPS sequence targeting by the DNA translocase FtsK. Proc Natl Acad Sci U S A 109:6531-6536. http://dx.doi.org/10.1073/pnas.1201613109.
    • (2012) Proc Natl Acad Sci U S A , vol.109 , pp. 6531-6536
    • Lee, J.Y.1    Finkelstein, I.J.2    Crozat, E.3    Sherratt, D.J.4    Greene, E.C.5
  • 79
    • 84873642146 scopus 로고    scopus 로고
    • The FtsK family of DNA pumps
    • Demarre G, Galli E, Barre FX. 2013. The FtsK family of DNA pumps. Adv Exp Med Biol 767:245-262. http://dx.doi.org/10.1007/978-1-4614-5037-5-12.
    • (2013) Adv Exp Med Biol , vol.767 , pp. 245-262
    • Demarre, G.1    Galli, E.2    Barre, F.X.3
  • 80
    • 33746987484 scopus 로고    scopus 로고
    • Double-stranded DNA translocation: Structure and mechanism of hexameric FtsK
    • Massey TH, Mercogliano CP, Yates J, Sherratt DJ, Lowe J. 2006. Double-stranded DNA translocation: structure and mechanism of hexameric 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
  • 81
    • 79960223131 scopus 로고    scopus 로고
    • Activation of XerCD-dif recombination by the FtsKDNAtranslocase
    • Grainge I, Lesterlin C, Sherratt DJ. 2011. Activation of XerCD-dif recombination by the FtsKDNAtranslocase. Nucleic Acids Res 39:5140-5148. http://dx.doi.org/10.1093/nar/gkr078.
    • (2011) Nucleic Acids Res , vol.39 , pp. 5140-5148
    • Grainge, I.1    Lesterlin, C.2    Sherratt, D.J.3
  • 83
    • 29144519710 scopus 로고    scopus 로고
    • Identification of oligonucleotide sequences that direct the movement of the Escherichia coli FtsK translocase
    • Levy O, Ptacin JL, Pease PJ, Gore J, Eisen MB, Bustamante C, Cozzarelli NR. 2005. Identification of oligonucleotide sequences that direct the movement of the Escherichia coli FtsK translocase. Proc Natl Acad SciUSA 102:17618-17623. http://dx.doi.org/10.1073/pnas.0508932102.
    • (2005) Proc Natl Acad SciUSA , vol.102 , pp. 17618-17623
    • Levy, O.1    Ptacin, J.L.2    Pease, P.J.3    Gore, J.4    Eisen, M.B.5    Bustamante, C.6    Cozzarelli, N.R.7
  • 84
    • 49349104892 scopus 로고    scopus 로고
    • Molecular mechanism of sequence-directed DNA loading and translocation by FtsK
    • Lowe J, Ellonen A, Allen MD, Atkinson C, Sherratt DJ, Grainge I. 2008. Molecular mechanism of sequence-directed DNA loading and translocation by FtsK. Mol Cell 31:498-509. http://dx.doi.org/10.1016/j.molcel.2008.05.027.
    • (2008) Mol Cell , vol.31 , pp. 498-509
    • Lowe, J.1    Ellonen, A.2    Allen, M.D.3    Atkinson, C.4    Sherratt, D.J.5    Grainge, I.6
  • 85
    • 0028179987 scopus 로고
    • Bacillus subtilis SpoIIIE protein required for DNA segregation during asymmetric cell division
    • Wu LJ, Errington J. 1994. Bacillus subtilis SpoIIIE protein required for DNA segregation during asymmetric cell division. Science 264:572-575. http://dx.doi.org/10.1126/science.8160014.
    • (1994) Science , vol.264 , pp. 572-575
    • Wu, L.J.1    Errington, J.2
  • 86
    • 84878278855 scopus 로고    scopus 로고
    • Recruitment, assembly, and molecular architecture of the SpoIIIEDNApump revealed by superresolution microscopy
    • Fiche JB, Cattoni DI, Diekmann N, Langerak JM, Clerte C, Royer CA, Margeat E, Doan T, Nollmann M. 2013. Recruitment, assembly, and molecular architecture of the SpoIIIEDNApump revealed by superresolution microscopy. PLoS Biol 11:e1001557. http://dx.doi.org/10.1371/journal.pbio.1001557.
    • (2013) PLoS Biol , vol.11 , pp. e1001557
    • Fiche, J.B.1    Cattoni, D.I.2    Diekmann, N.3    Langerak, J.M.4    Clerte, C.5    Royer, C.A.6    Margeat, E.7    Doan, T.8    Nollmann, M.9
  • 87
    • 82555176571 scopus 로고    scopus 로고
    • Players between the worlds: Multifunctional DNA translocases
    • Kaimer C, Graumann PL. 2011. Players between the worlds: multifunctional DNA translocases. Curr Opin Microbiol 14:719-725. http://dx.doi.org/10.1016/j.mib.2011.10.004.
    • (2011) Curr Opin Microbiol , vol.14 , pp. 719-725
    • Kaimer, C.1    Graumann, P.L.2
  • 88
    • 36148931768 scopus 로고    scopus 로고
    • FtsK and SpoIIIE: The tale of the conserved tails
    • Barre FX. 2007. FtsK and SpoIIIE: the tale of the conserved tails. Mol Microbiol 66:1051-1055. http://dx.doi.org/10.1111/j.1365-2958.2007.05981.x.
    • (2007) Mol Microbiol , vol.66 , pp. 1051-1055
    • Barre, F.X.1
  • 90
    • 0034602330 scopus 로고    scopus 로고
    • Role of Bacillus subtilis SpoIIIE in DNA transport across the mother cell-prespore division septum
    • Bath J, Wu LJ, Errington J, Wang JC. 2000. Role of Bacillus subtilis SpoIIIE in DNA transport across the mother cell-prespore division septum. Science 290:995-997. http://dx.doi.org/10.1126/science.290.5493.995.
    • (2000) Science , vol.290 , pp. 995-997
    • Bath, J.1    Wu, L.J.2    Errington, J.3    Wang, J.C.4
  • 91
    • 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
  • 92
    • 37549069575 scopus 로고    scopus 로고
    • Drawing the tree of eukaryotic life based on the analysis of 2, 269 manually annotated myosins from 328 species
    • Odronitz F, Kollmar M. 2007. Drawing the tree of eukaryotic life based on the analysis of 2, 269 manually annotated myosins from 328 species. Genome Biol 8:R196. http://dx.doi.org/10.1186/gb-2007-8-9-r196.
    • (2007) Genome Biol , vol.8 , pp. R196
    • Odronitz, F.1    Kollmar, M.2
  • 95
    • 84875590005 scopus 로고    scopus 로고
    • Force generation by kinesin and myosin cytoskeletal motor proteins
    • Kull FJ, Endow SA. 2013. Force generation by kinesin and myosin cytoskeletal motor proteins. J Cell Sci 126:9-19. http://dx.doi.org/10.1242/jcs.103911.
    • (2013) J Cell Sci , vol.126 , pp. 9-19
    • Kull, F.J.1    Endow, S.A.2
  • 96
    • 0030267349 scopus 로고    scopus 로고
    • Switches, latches, and amplifiers: Common themes of G proteins and molecular motors
    • Vale RD. 1996. Switches, latches, and amplifiers: common themes of G proteins and molecular motors. J Cell Biol 135:291-302. http://dx.doi.org/10.1083/jcb.135.2.291.
    • (1996) J Cell Biol , vol.135 , pp. 291-302
    • Vale, R.D.1
  • 97
    • 0032410805 scopus 로고    scopus 로고
    • The case for a common ancestor: Kinesin and myosin motor proteins and G proteins
    • Kull FJ, Vale RD, Fletterick RJ. 1998. The case for a common ancestor: kinesin and myosin motor proteins and G proteins. J Muscle Res Cell Motil 19:877-886. http://dx.doi.org/10.1023/A:1005489907021.
    • (1998) J Muscle Res Cell Motil , vol.19 , pp. 877-886
    • Kull, F.J.1    Vale, R.D.2    Fletterick, R.J.3
  • 98
    • 0032478549 scopus 로고    scopus 로고
    • RNA polymerase as a molecular motor
    • Gelles J, Landick R. 1998. RNA polymerase as a molecular motor. Cell 93:13-16. http://dx.doi.org/10.1016/S0092-8674 (00) 81140-X.
    • (1998) Cell , vol.93 , pp. 13-16
    • Gelles, J.1    Landick, R.2
  • 99
    • 0032478504 scopus 로고    scopus 로고
    • Staying on track: Common features of DNA helicases and microtubule motors
    • Lohman TM, Thorn K, Vale RD. 1998. Staying on track: common features of DNA helicases and microtubule motors. Cell 93:9-12. http://dx.doi.org/10.1016/S0092-8674 (00) 81139-3.
    • (1998) Cell , vol.93 , pp. 9-12
    • Lohman, T.M.1    Thorn, K.2    Vale, R.D.3
  • 100
    • 0030602794 scopus 로고    scopus 로고
    • DNA helicases: New breeds of translocating motors and molecular pumps
    • West SC. 1996. DNA helicases: new breeds of translocating motors and molecular pumps. Cell 86:177-180. http://dx.doi.org/10.1016/S0092-8674 (00) 80088-4.
    • (1996) Cell , vol.86 , pp. 177-180
    • West, S.C.1
  • 101
    • 0029762774 scopus 로고    scopus 로고
    • DNA is bound within the central hole to one or two of the six subunits of the T7DNAhelicase
    • Yu X, Hingorani MM, Patel SS, Egelman EH. 1996. DNA is bound within the central hole to one or two of the six subunits of the T7DNAhelicase. Nat Struct Biol 3:740-743. http://dx.doi.org/10.1038/nsb0996-740.
    • (1996) Nat Struct Biol , vol.3 , pp. 740-743
    • Yu, X.1    Hingorani, M.M.2    Patel, S.S.3    Egelman, E.H.4
  • 102
    • 0032883413 scopus 로고    scopus 로고
    • Structural mechanism of muscle contraction
    • Geeves MA, Holmes KC. 1999. Structural mechanism of muscle contraction. Annu Rev Biochem 68:687-728. http://dx.doi.org/10.1146/annurev.biochem.68.1.687.
    • (1999) Annu Rev Biochem , vol.68 , pp. 687-728
    • Geeves, M.A.1    Holmes, K.C.2
  • 103
    • 0343415156 scopus 로고    scopus 로고
    • The way things move: Looking under the hood of molecular motor proteins
    • Vale RD, Milligan RA. 2000. The way things move: looking under the hood of molecular motor proteins. Science 288:88-95. http://dx.doi.org/10.1126/science.288.5463.88.
    • (2000) Science , vol.288 , pp. 88-95
    • Vale, R.D.1    Milligan, R.A.2
  • 104
    • 0025078730 scopus 로고
    • The generation of concatemeric plasmid DNA in Bacillus subtilis as a consequence of bacteriophage SPP1 infection
    • Bravo A, Alonso JC. 1990. The generation of concatemeric plasmid DNA in Bacillus subtilis as a consequence of bacteriophage SPP1 infection. Nucleic Acids Res 18:4651-4657. http://dx.doi.org/10.1093/nar/18.16.4651.
    • (1990) Nucleic Acids Res , vol.18 , pp. 4651-4657
    • Bravo, A.1    Alonso, J.C.2
  • 105
    • 0023664536 scopus 로고
    • Processing of concatemers of bacteriophage T7 DNA in vitro
    • White JH, Richardson CC. 1987. Processing of concatemers of bacteriophage T7 DNA in vitro. J Biol Chem 262:8854-8860.
    • (1987) J Biol Chem , vol.262 , pp. 8854-8860
    • White, J.H.1    Richardson, C.C.2
  • 106
    • 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
  • 107
    • 73649156890 scopus 로고
    • Physical principles in the construction of regular viruses
    • Caspar DLD, Klug A. 1962. Physical principles in the construction of regular viruses. Cold Spr Harb Symp Quant Biol 27:1-24. http://dx.doi.org/10.1101/SQB.1962.027.001.005.
    • (1962) Cold Spr Harb Symp Quant Biol , vol.27 , pp. 1-24
    • Caspar, D.L.D.1    Klug, A.2
  • 108
    • 0021783271 scopus 로고
    • The DNA translocation vertex of dsDNA bacteriophages
    • Bazinet C, King J. 1985. The DNA translocation vertex of dsDNA bacteriophages. Annu Rev Microbiol 39:109-129. http://dx.doi.org/10.1146/annurev. mi.39.100185.000545.
    • (1985) Annu Rev Microbiol , vol.39 , pp. 109-129
    • Bazinet, C.1    King, J.2
  • 110
    • 0026532074 scopus 로고
    • Three-dimensional structure of T3 connector purified from overexpressing bacteria
    • Valpuesta JM, Fujisawa H, Marco S, Carazo JM, Carrascosa J. 1992. Three-dimensional structure of T3 connector purified from overexpressing bacteria. J Mol Biol 224:103-112. http://dx.doi.org/10.1016/0022-2836 (92) 90579-9.
    • (1992) J Mol Biol , vol.224 , pp. 103-112
    • Valpuesta, J.M.1    Fujisawa, H.2    Marco, S.3    Carazo, J.M.4    Carrascosa, J.5
  • 111
    • 0021632866 scopus 로고
    • Bacteriophage lambda preconnectors: Purification and structure
    • Kochan J, Carrascosa JL, Murialdo H. 1984. Bacteriophage lambda preconnectors: purification and structure. J Mol Biol 174:433-447. http://dx.doi.org/10.1016/0022-2836 (84) 90330-9.
    • (1984) J Mol Biol , vol.174 , pp. 433-447
    • Kochan, J.1    Carrascosa, J.L.2    Murialdo, H.3
  • 112
    • 33846209611 scopus 로고    scopus 로고
    • The gpQ portal protein of bacteriophage P2 forms dodecameric connectors in crystals
    • Doan DN, Dokland T. 2007. The gpQ portal protein of bacteriophage P2 forms dodecameric connectors in crystals. J Struct Biol 157:432-436. http://dx.doi.org/10.1016/j.jsb.2006.08.009.
    • (2007) J Struct Biol , vol.157 , pp. 432-436
    • Doan, D.N.1    Dokland, T.2
  • 113
    • 0020073216 scopus 로고
    • Structure of the head-tail connector of bacteriophage phi 29
    • Carrascosa JL, Vinuela E, Garcia N, Santisteban A. 1982. Structure of the head-tail connector of bacteriophage phi 29. J Mol Biol 154:311-324. http://dx.doi.org/10.1016/0022-2836 (82) 90066-3.
    • (1982) J Mol Biol , vol.154 , pp. 311-324
    • Carrascosa, J.L.1    Vinuela, E.2    Garcia, N.3    Santisteban, A.4
  • 114
    • 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
  • 115
    • 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
  • 116
    • 84869987562 scopus 로고    scopus 로고
    • High degree of coordination and division of labor among subunits in a homomeric ring ATPase
    • Chistol G, Liu S, Hetherington CL, Moffitt JR, Grimes S, Jardine PJ, Bustamante C. 2012. High degree of coordination and division of labor among subunits in a homomeric ring ATPase. Cell 151:1017-1028. http://dx.doi.org/10.1016/j.cell.2012.10.031.
    • (2012) Cell , vol.151 , pp. 1017-1028
    • Chistol, G.1    Liu, S.2    Hetherington, C.L.3    Moffitt, J.R.4    Grimes, S.5    Jardine, P.J.6    Bustamante, C.7
  • 117
  • 118
    • 48149087104 scopus 로고    scopus 로고
    • Defining molecular and domain boundaries in the bacteriophage phi29 DNA packaging motor
    • Morais MC, Koti JS, Bowman VD, Reyes-Aldrete E, Anderson D, Rossman MG. 2008. Defining molecular and domain boundaries in the bacteriophage phi29 DNA packaging motor. Structure 16:1267-1274. http://dx.doi.org/10.1016/j.str.2008.05.010.
    • (2008) Structure , vol.16 , pp. 1267-1274
    • Morais, M.C.1    Koti, J.S.2    Bowman, V.D.3    Reyes-Aldrete, E.4    Anderson, D.5    Rossman, M.G.6
  • 119
    • 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
  • 120
    • 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 Nanotechnol 7:3257-3267. http://dx.doi.org/10.1166/jnn. 2007.914.
    • (2007) J Nanosci Nanotechnol , vol.7 , pp. 3257-3267
    • Moll, D.1    Guo, P.2
  • 121
    • 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
  • 124
    • 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
  • 125
    • 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
  • 126
    • 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
  • 127
    • 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
  • 128
    • 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
  • 130
    • 84867538324 scopus 로고    scopus 로고
    • The hexameric helicase DnaB adopts a nonplanar conformation during translocation
    • Itsathitphaisarn O, Wing RA, Eliason WK, Wang J, Steitz TA. 2012. The hexameric helicase DnaB adopts a nonplanar conformation during translocation. Cell 151:267-277. http://dx.doi.org/10.1016/j.cell.2012.09.014.
    • (2012) Cell , vol.151 , pp. 267-277
    • Itsathitphaisarn, O.1    Wing, R.A.2    Eliason, W.K.3    Wang, J.4    Steitz, T.A.5
  • 131
    • 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
  • 132
    • 77956448643 scopus 로고    scopus 로고
    • One-way traffic of a viral motor channel for double-stranded DNA translocation
    • Jing P, Haque F, Shu D, Montemagno C, Guo P. 2010. One-way traffic of a viral motor channel for double-stranded DNA translocation. Nano Lett 10:3620-3627. http://dx.doi.org/10.1021/nl101939e.
    • (2010) Nano Lett , vol.10 , pp. 3620-3627
    • Jing, P.1    Haque, F.2    Shu, D.3    Montemagno, C.4    Guo, P.5
  • 133
    • 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
  • 134
    • 0041561083 scopus 로고    scopus 로고
    • Use of acetone to attain highly active and solubleDNApackaging protein gp16 of phi29 for ATPase assay
    • Huang LP, Guo P. 2003. Use of acetone to attain highly active and solubleDNApackaging protein gp16 of phi29 for ATPase assay. Virology 312:449-457. http://dx.doi.org/10.1016/S0042-6822 (03) 00241-1.
    • (2003) Virology , vol.312 , pp. 449-457
    • Huang, L.P.1    Guo, P.2
  • 135
    • 84861404367 scopus 로고    scopus 로고
    • Molecular mechanism of ATP hydrolysis in F1-ATPase revealed by molecular simulations and single-molecule observations
    • Hayashi S, Ueno H, Shaikh AR, Umemura M, Kamiya M, Ito Y, Ikeguchi M, Komoriya Y, Iino R, Noji H. 2012. Molecular mechanism of ATP hydrolysis in F1-ATPase revealed by molecular simulations and single-molecule observations. J Am Chem Soc 134:8447-8454. http://dx.doi.org/10.1021/ja211027m.
    • (2012) J Am Chem Soc , vol.134 , pp. 8447-8454
    • Hayashi, S.1    Ueno, H.2    Shaikh, A.R.3    Umemura, M.4    Kamiya, M.5    Ito, Y.6    Ikeguchi, M.7    Komoriya, Y.8    Iino, R.9    Noji, H.10
  • 136
    • 55549132236 scopus 로고    scopus 로고
    • The 'glutamate switch' provides a link between ATPase activity and ligand binding in AAA+ proteins
    • Zhang X, Wigley DB. 2008. The 'glutamate switch' provides a link between ATPase activity and ligand binding in AAA+ proteins. Nat Struct Mol Biol 15:1223-1227. http://dx.doi.org/10.1038/nsmb.1501.
    • (2008) Nat Struct Mol Biol , vol.15 , pp. 1223-1227
    • Zhang, X.1    Wigley, D.B.2
  • 137
    • 0033598667 scopus 로고    scopus 로고
    • Importance of F-1-ATPase residue alpha-Arg-376 for catalytic transition state stabilization
    • Nadanaciva S, Weber J, Wilke-Mounts S, Senior AE. 1999. Importance of F-1-ATPase residue alpha-Arg-376 for catalytic transition state stabilization. Biochemistry 38:15493-15499. http://dx.doi.org/10.1021/bi9917683.
    • (1999) Biochemistry , vol.38 , pp. 15493-15499
    • Nadanaciva, S.1    Weber, J.2    Wilke-Mounts, S.3    Senior, A.E.4
  • 138
    • 0141642135 scopus 로고    scopus 로고
    • On the mechanism of ATP hydrolysis in F (1)-ATPase
    • Dittrich M, Hayashi S, Schulten K. 2003. On the mechanism of ATP hydrolysis in F (1)-ATPase. Biophys J 85:2253-2266. http://dx.doi.org/10.1016/S0006-3495 (03) 74650-5.
    • (2003) Biophys J , vol.85 , pp. 2253-2266
    • Dittrich, M.1    Hayashi, S.2    Schulten, K.3
  • 139
    • 84860359572 scopus 로고    scopus 로고
    • Principal role of the arginine finger in rotary catalysis of F-1-ATPase
    • Komoriya Y, Ariga T, Iino R, Imamura H, Okuno D, Noji H. 2012. Principal role of the arginine finger in rotary catalysis of F-1-ATPase. J Biol Chem 287:15134-15142. http://dx.doi.org/10.1074/jbc. M111.328153.
    • (2012) J Biol Chem , vol.287 , pp. 15134-15142
    • Komoriya, Y.1    Ariga, T.2    Iino, R.3    Imamura, H.4    Okuno, D.5    Noji, H.6
  • 140
    • 0030666224 scopus 로고    scopus 로고
    • Crystal structure of the delta= subunit of the clamp-loader complex of E. Coli DNA polymerase III
    • Guenther B, Onrust R, Sali A, O'Donnell M, Kuriyan J. 1997. Crystal structure of the delta= subunit of the clamp-loader complex of E. Coli DNA polymerase III. Cell 91:335-345. http://dx.doi.org/10.1016/S0092-8674 (00) 80417-1.
    • (1997) Cell , vol.91 , pp. 335-345
    • Guenther, B.1    Onrust, R.2    Sali, A.3    O'Donnell, M.4    Kuriyan, J.5
  • 141
    • 33745041480 scopus 로고    scopus 로고
    • Evolutionary relationships and structural mechanisms of AAA+ proteins
    • Erzberger JP, Berger JM. 2006. Evolutionary relationships and structural mechanisms of AAA+ proteins. Annu Rev Biophys Biomol Struct 35:93-114. http://dx.doi.org/10.1146/annurev. biophys.35.040 405.101933.
    • (2006) Annu Rev Biophys Biomol Struct , vol.35 , pp. 93-114
    • Erzberger, J.P.1    Berger, J.M.2
  • 142
    • 0030934380 scopus 로고    scopus 로고
    • Direct observation of the rotation of F1-ATPase
    • Noji H, Yasuda R, Yoshida M, Kinosita K, Jr. 1997. Direct observation of the rotation of F1-ATPase. Nature 386:299-302. http://dx.doi.org/10.1038/386299a0.
    • (1997) Nature , vol.386 , pp. 299-302
    • Noji, H.1    Yasuda, R.2    Yoshida, M.3    Kinosita, K.4
  • 143
    • 0033407488 scopus 로고    scopus 로고
    • The gamma subunit in chloroplast F-1-ATPase can rotate in a unidirectional and counter-clockwise manner
    • Hisabori T, Kondoh A, Yoshida M. 1999. The gamma subunit in chloroplast F-1-ATPase can rotate in a unidirectional and counter-clockwise manner. FEBS Lett 463:35-38. http://dx.doi.org/10.1016/S0014-5793 (99) 01 602-6.
    • (1999) FEBS Lett , vol.463 , pp. 35-38
    • Hisabori, T.1    Kondoh, A.2    Yoshida, M.3
  • 144
    • 84925018731 scopus 로고    scopus 로고
    • Chemomechanical coupling of human mitochondrial F1-ATPase motor
    • Suzuki T, Tanaka K, Wakabayashi C, Saita E, Yoshida M. 2014. Chemomechanical coupling of human mitochondrial F1-ATPase motor. Nat Chem Biol 10:930-936. http://dx.doi.org/10.1038/nchembio.1635.
    • (2014) Nat Chem Biol , vol.10 , pp. 930-936
    • Suzuki, T.1    Tanaka, K.2    Wakabayashi, C.3    Saita, E.4    Yoshida, M.5
  • 147
    • 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
  • 149
    • 0345166868 scopus 로고    scopus 로고
    • Catalysis and rotation of F-1 motor: Cleavage of ATP at the catalytic site occurs in 1 ms before 40 degrees substep rotation
    • Shimabukuro K, Yasuda R, Muneyuki E, Hara KY, Kinosita K, Yoshida M. 2003. Catalysis and rotation of F-1 motor: cleavage of ATP at the catalytic site occurs in 1 ms before 40 degrees substep rotation. Proc Natl Acad Sci U S A 100:14731-14736. http://dx.doi.org/10.1073/pnas.2434983100.
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 14731-14736
    • Shimabukuro, K.1    Yasuda, R.2    Muneyuki, E.3    Hara, K.Y.4    Kinosita, K.5    Yoshida, M.6
  • 150
    • 77958163287 scopus 로고    scopus 로고
    • Phosphate release in F-1-ATPase catalytic cycle follows ADP release
    • Watanabe R, Iino R, Noji H. 2010. Phosphate release in F-1-ATPase catalytic cycle follows ADP release. Nat Chem Biol 6:814-820. http://dx.doi.org/10.1038/nchembio.443.
    • (2010) Nat Chem Biol , vol.6 , pp. 814-820
    • Watanabe, R.1    Iino, R.2    Noji, H.3
  • 151
    • 0035912221 scopus 로고    scopus 로고
    • Resolution of distinct rotational substeps by submillisecond kinetic analysis of F1-ATPase
    • Yasuda R, Noji H, Yoshida M, Kinosita K, Jr, Itoh H. 2001. Resolution of distinct rotational substeps by submillisecond kinetic analysis of F1-ATPase. Nature 410:898-904. http://dx.doi.org/10.1038/35073513.
    • (2001) Nature , vol.410 , pp. 898-904
    • Yasuda, R.1    Noji, H.2    Yoshida, M.3    Kinosita, K.4    Itoh, H.5
  • 152
    • 84923196865 scopus 로고    scopus 로고
    • High-speed angle-resolved imaging of a single gold nanorod with microsecond temporal resolution and one-degree angle precision
    • Enoki S, Iino R, Niitani Y, Minagawa Y, Tomishige M, Noji H. 2015. High-speed angle-resolved imaging of a single gold nanorod with microsecond temporal resolution and one-degree angle precision. Anal Chem 87:2079-2086. http://dx.doi.org/10.1021/ac502408c.
    • (2015) Anal Chem , vol.87 , pp. 2079-2086
    • Enoki, S.1    Iino, R.2    Niitani, Y.3    Minagawa, Y.4    Tomishige, M.5    Noji, H.6
  • 153
    • 33644856865 scopus 로고    scopus 로고
    • Microsecond time scale rotation measurements of single F-1-ATPase molecules
    • Spetzler D, York J, Daniel D, Fromme R, Lowry D, Frasch W. 2006. Microsecond time scale rotation measurements of single F-1-ATPase molecules. Biochemistry 45:3117-3124. http://dx.doi.org/10.1021/bi052363n.
    • (2006) Biochemistry , vol.45 , pp. 3117-3124
    • Spetzler, D.1    York, J.2    Daniel, D.3    Fromme, R.4    Lowry, D.5    Frasch, W.6
  • 156
    • 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 370:621-628. http://dx.doi.org/10.1038/370621a0.
    • (1994) Nature , vol.370 , pp. 621-628
    • Abrahams, J.P.1    Leslie, A.G.2    Lutter, R.3    Walker, J.E.4
  • 157
    • 77951707330 scopus 로고    scopus 로고
    • Analysis of the open and closed conformations of the beta subunits in thermophilic F-1-ATPase by solution NMR
    • Kobayashi M, Akutsu H, Suzuki T, Yoshida M, Yagi H. 2010. Analysis of the open and closed conformations of the beta subunits in thermophilic F-1-ATPase by solution NMR. J Mol Biol 398:189-199. http://dx.doi.org/10.1016/j.jmb.2010.03.013.
    • (2010) J Mol Biol , vol.398 , pp. 189-199
    • Kobayashi, M.1    Akutsu, H.2    Suzuki, T.3    Yoshida, M.4    Yagi, H.5
  • 158
    • 57149107555 scopus 로고    scopus 로고
    • Cooperative three-step motions in catalytic subunits of F (1)-ATPase correlate with 80 degrees and 40 degrees substep rotations
    • Masaike T, Koyama-Horibe F, Oiwa K, Yoshida M, Nishizaka T. 2008. Cooperative three-step motions in catalytic subunits of F (1)-ATPase correlate with 80 degrees and 40 degrees substep rotations. Nat Struct Mol Biol 15:1326-1333. http://dx.doi.org/10.1038/nsmb.1510.
    • (2008) Nat Struct Mol Biol , vol.15 , pp. 1326-1333
    • Masaike, T.1    Koyama-Horibe, F.2    Oiwa, K.3    Yoshida, M.4    Nishizaka, T.5
  • 159
    • 79961236945 scopus 로고    scopus 로고
    • High-speed atomic force microscopy reveals rotary catalysis of rotorless F-1-ATPase
    • Uchihashi T, Iino R, Ando T, Noji H. 2011. High-speed atomic force microscopy reveals rotary catalysis of rotorless F-1-ATPase. Science 333:755-758. http://dx.doi.org/10.1126/science.1205510.
    • (2011) Science , vol.333 , pp. 755-758
    • Uchihashi, T.1    Iino, R.2    Ando, T.3    Noji, H.4
  • 161
    • 21844466207 scopus 로고    scopus 로고
    • Movements of the epsilon-subunit during catalysis and activation in single membrane-bound H+-ATP synthase
    • Zimmermann B, Diez M, Zarrabi N, Graber P, Borsch M. 2005. Movements of the epsilon-subunit during catalysis and activation in single membrane-bound H+-ATP synthase. EMBO J 24:2053-2063. http://dx.doi.org/10.1038/sj.emboj.7600682.
    • (2005) EMBO J , vol.24 , pp. 2053-2063
    • Zimmermann, B.1    Diez, M.2    Zarrabi, N.3    Graber, P.4    Borsch, M.5
  • 162
    • 84875888783 scopus 로고    scopus 로고
    • Biased Brownian stepping rotation of FoF1-ATP synthase driven by proton motive force
    • Watanabe R, Tabata KV, Iino R, Ueno H, Iwamoto M, Oiki S, Noji H. 2013. Biased Brownian stepping rotation of FoF1-ATP synthase driven by proton motive force. Nat Commun 4:1631. http://dx.doi.org/10.1038/ncomms2631.
    • (2013) Nat Commun , vol.4 , pp. 1631
    • Watanabe, R.1    Tabata, K.V.2    Iino, R.3    Ueno, H.4    Iwamoto, M.5    Oiki, S.6    Noji, H.7
  • 164
    • 33745823112 scopus 로고    scopus 로고
    • Mechanisms of helicases
    • Patel SS, Donmez I. 2006. Mechanisms of helicases. J Biol Chem 281:18265-18268. http://dx.doi.org/10.1074/jbc. R600008200.
    • (2006) J Biol Chem , vol.281 , pp. 18265-18268
    • Patel, S.S.1    Donmez, I.2
  • 165
    • 42449141601 scopus 로고    scopus 로고
    • Non-hexameric DNA helicases and translocases: Mechanisms and regulation
    • Lohman TM, Tomko EJ, Wu CG. 2008. Non-hexameric DNA helicases and translocases: mechanisms and regulation. Nat Rev Mol Cell Biol 9:391-401. http://dx.doi.org/10.1038/nrm2394.
    • (2008) Nat Rev Mol Cell Biol , vol.9 , pp. 391-401
    • Lohman, T.M.1    Tomko, E.J.2    Wu, C.G.3
  • 166
    • 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
  • 167
    • 79958703404 scopus 로고    scopus 로고
    • Role of phi29 connector channel loops in late-stage DNA packaging
    • Grimes S, Ma S, Gao J, Atz R, Jardine PJ. 2011. Role of phi29 connector channel loops in late-stage DNA packaging. J Mol Biol 410:50-59. http://dx.doi.org/10.1016/j.jmb.2011.04.070.
    • (2011) J Mol Biol , vol.410 , pp. 50-59
    • Grimes, S.1    Ma, S.2    Gao, J.3    Atz, R.4    Jardine, P.J.5
  • 168
    • 79952154608 scopus 로고    scopus 로고
    • A hypothesis for bacteriophage DNA packaging motors
    • Serwer P. 2010. A hypothesis for bacteriophage DNA packaging motors. Viruses 2:1821-1843. http://dx.doi.org/10.3390/v2091821.
    • (2010) Viruses , vol.2 , pp. 1821-1843
    • Serwer, P.1
  • 169
    • 84876585976 scopus 로고    scopus 로고
    • Channel size conversion of Phi29 DNA-packaging nanomotor for discrimination of single- and doublestranded nucleic acids
    • Geng J, Wang S, Fang H, Guo P. 2013. Channel size conversion of Phi29 DNA-packaging nanomotor for discrimination of single- and doublestranded nucleic acids. ACS Nano 7:3315-3323. http://dx.doi.org/10.1021/nn400020z.
    • (2013) ACS Nano , vol.7 , pp. 3315-3323
    • Geng, J.1    Wang, S.2    Fang, H.3    Guo, P.4
  • 170
    • 0037451286 scopus 로고    scopus 로고
    • Structure of a viral DNA gatekeeper at 10 A resolution by cryo-electron microscopy
    • Orlova EV, Gowen B, Droge A, Stiege A, Weise F, Lurz R, van HM, Tavares P. 2003. Structure of a viral DNA gatekeeper at 10 A resolution by cryo-electron microscopy. EMBO J 22:1255-1262. http://dx.doi.org/10.1093/emboj/cdg123.
    • (2003) EMBO J , vol.22 , pp. 1255-1262
    • Orlova, E.V.1    Gowen, B.2    Droge, A.3    Stiege, A.4    Weise, F.5    Lurz, R.6    Van, H.M.7    Tavares, P.8
  • 171
    • 22044451059 scopus 로고    scopus 로고
    • Translocation of nicked but not gapped DNA by the packaging motor of bacteriophage phi29
    • Moll W-D, Guo P. 2005. Translocation of nicked but not gapped DNA by the packaging motor of bacteriophage phi29. J Mol Biol 351:100-107. http://dx.doi.org/10.1016/j.jmb.2005.05.038.
    • (2005) J Mol Biol , vol.351 , pp. 100-107
    • Moll, W.-D.1    Guo, P.2
  • 173
    • 46649088725 scopus 로고    scopus 로고
    • Modulation of the packaging reaction of bacteriophage T4 terminase by DNA structure
    • Oram M, Sabanayagam C, Black LW. 2008. Modulation of the packaging reaction of bacteriophage T4 terminase by DNA structure. J Mol Biol 381:61-72. http://dx.doi.org/10.1016/j.jmb.2008.05.074.
    • (2008) J Mol Biol , vol.381 , pp. 61-72
    • Oram, M.1    Sabanayagam, C.2    Black, L.W.3
  • 174
    • 84870589316 scopus 로고    scopus 로고
    • The dynamic pauseunpackaging state, an off-translocation recovery state of a DNA packaging motor from bacteriophage T4
    • Kottadiel VI, Rao VB, Chemla YR. 2012. The dynamic pauseunpackaging state, an off-translocation recovery state of a DNA packaging motor from bacteriophage T4. Proc Natl Acad Sci U S A 109:20000-20005. http://dx.doi.org/10.1073/pnas.1209214109.
    • (2012) Proc Natl Acad Sci U S A , vol.109 , pp. 20000-20005
    • Kottadiel, V.I.1    Rao, V.B.2    Chemla, Y.R.3
  • 175
    • 0027299633 scopus 로고
    • DNA packaging ATPase of bacteriophage T3
    • Morita M, Tasaka M, Fujisawa H. 1993. DNA packaging ATPase of bacteriophage T3. Virology 193:748-752. http://dx.doi.org/10.1006/viro.1993.1183.
    • (1993) Virology , vol.193 , pp. 748-752
    • Morita, M.1    Tasaka, M.2    Fujisawa, H.3
  • 176
    • 0037169328 scopus 로고    scopus 로고
    • FtsK is a DNA motor protein that activates chromosome dimer resolution by switching the catalytic state of the XerC and XerD recombinases
    • Aussel L, Barre FX, Aroyo M, Stasiak A, Stasiak AZ, Sherratt D. 2002. FtsK is a DNA motor protein that activates chromosome dimer resolution by switching the catalytic state of the XerC and XerD recombinases. Cell 108:195-205. http://dx.doi.org/10.1016/S0092-8674 (02) 00624-4.
    • (2002) Cell , vol.108 , pp. 195-205
    • Aussel, L.1    Barre, F.X.2    Aroyo, M.3    Stasiak, A.4    Stasiak, A.Z.5    Sherratt, D.6
  • 177
    • 20444500568 scopus 로고    scopus 로고
    • Analysis of DNA supercoil induction by FtsK indicates translocation without groovetracking
    • Saleh OA, Bigot S, Barre FX, Allemand JF. 2005. Analysis of DNA supercoil induction by FtsK indicates translocation without groovetracking. Nat Struct Mol Biol 12:436-440. http://dx.doi.org/10.1038/nsmb926.
    • (2005) Nat Struct Mol Biol , vol.12 , pp. 436-440
    • Saleh, O.A.1    Bigot, S.2    Barre, F.X.3    Allemand, J.F.4
  • 179
    • 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
  • 180
    • 70350344051 scopus 로고    scopus 로고
    • Running in reverse: The structural basis for translocation polarity in hexameric helicases
    • Thomsen ND, Berger JM. 2009. Running in reverse: the structural basis for translocation polarity in hexameric helicases. Cell 139:523-534. http://dx.doi.org/10.1016/j.cell.2009.08.043.
    • (2009) Cell , vol.139 , pp. 523-534
    • Thomsen, N.D.1    Berger, J.M.2
  • 182
    • 33746796409 scopus 로고    scopus 로고
    • Direct observation of DNA rotation during branch migration of Holliday junction DNA by Escherichia coli RuvA-RuvB protein complex
    • Han YW, Tani T, Hayashi M, Hishida T, Iwasaki H, Shinagawa H, Harada Y. 2006. Direct observation of DNA rotation during branch migration of Holliday junction DNA by Escherichia coli RuvA-RuvB protein complex. Proc Natl Acad Sci U S A 103:11544-11548. http://dx.doi.org/10.1073/pnas.0600753103.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 11544-11548
    • Han, Y.W.1    Tani, T.2    Hayashi, M.3    Hishida, T.4    Iwasaki, H.5    Shinagawa, H.6    Harada, Y.7
  • 183
    • 0030791973 scopus 로고    scopus 로고
    • Actomyosin interaction in striated muscle
    • Cooke R. 1997. Actomyosin interaction in striated muscle. Physiol Rev 77:671-697.
    • (1997) Physiol Rev , vol.77 , pp. 671-697
    • Cooke, R.1
  • 187
    • 0015214368 scopus 로고
    • Mechanism of adenosine triphosphate hydrolysis by actomyosin
    • Lymn RW, Taylor EW. 1971. Mechanism of adenosine triphosphate hydrolysis by actomyosin. Biochemistry 10:4617-4624. http://dx.doi.org/10.1021/bi00801a004.
    • (1971) Biochemistry , vol.10 , pp. 4617-4624
    • Lymn, R.W.1    Taylor, E.W.2
  • 189
    • 1642333310 scopus 로고    scopus 로고
    • Relating biochemistry and function in the myosin superfamily
    • De la Cruz EM, Ostap EM. 2004. Relating biochemistry and function in the myosin superfamily. Curr Opin Cell Biol 16:61-67. http://dx.doi.org/10.1016/j.ceb.2003.11.011.
    • (2004) Curr Opin Cell Biol , vol.16 , pp. 61-67
    • De La Cruz, E.M.1    Ostap, E.M.2
  • 190
    • 0018816862 scopus 로고
    • The relation of muscle biochemistry to muscle physiology
    • Eisenberg E, Greene LE. 1980. The relation of muscle biochemistry to muscle physiology. Annu Rev Physiol 42:293-309. http://dx.doi.org/10.1146/annurev. ph.42.030180.001453.
    • (1980) Annu Rev Physiol , vol.42 , pp. 293-309
    • Eisenberg, E.1    Greene, L.E.2
  • 192
    • 0032493769 scopus 로고    scopus 로고
    • Mutational analysis of the switch II loop of Dictyostelium myosin II
    • Sasaki N, Shimada T, Sutoh K. 1998. Mutational analysis of the switch II loop of Dictyostelium myosin II. J Biol Chem 273:20334-20340. http://dx.doi.org/10.1074/jbc.273.32.20334.
    • (1998) J Biol Chem , vol.273 , pp. 20334-20340
    • Sasaki, N.1    Shimada, T.2    Sutoh, K.3
  • 193
    • 0037180422 scopus 로고    scopus 로고
    • Early stages of energy transduction by myosin: Roles of Arg in switch I, of Glu in switch II, and of the salt-bridge between them
    • Onishi H, Ohki T, Mochizuki N, Morales MF. 2002. Early stages of energy transduction by myosin: roles of Arg in switch I, of Glu in switch II, and of the salt-bridge between them. Proc Natl Acad Sci U S A 99:15339-15344. http://dx.doi.org/10.1073/pnas.242604099.
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 15339-15344
    • Onishi, H.1    Ohki, T.2    Mochizuki, N.3    Morales, M.F.4
  • 194
    • 10644225267 scopus 로고    scopus 로고
    • Three myosin V structures delineate essential features of chemo-mechanical transduction
    • Coureux PD, Sweeney HL, Houdusse A. 2004. Three myosin V structures delineate essential features of chemo-mechanical transduction. EMBO J 23:4527-4537. http://dx.doi.org/10.1038/sj.emboj.7600458.
    • (2004) EMBO J , vol.23 , pp. 4527-4537
    • Coureux, P.D.1    Sweeney, H.L.2    Houdusse, A.3
  • 195
    • 14044268874 scopus 로고    scopus 로고
    • Magnesium regulates ADP dissociation from myosin V
    • Rosenfeld SS, Houdusse A, Sweeney HL. 2005. Magnesium regulates ADP dissociation from myosin V. J Biol Chem 280:6072-6079. http://dx.doi.org/10.1074/jbc. M412717200.
    • (2005) J Biol Chem , vol.280 , pp. 6072-6079
    • Rosenfeld, S.S.1    Houdusse, A.2    Sweeney, H.L.3
  • 196
    • 20544475925 scopus 로고    scopus 로고
    • Magnesium, ADP, and actin binding linkage of myosin V: Evidence for multiple myosin V-ADP and actomyosin V-ADP states
    • Hannemann DE, Cao W, Olivares AO, Robblee JP, De la Cruz EM. 2005. Magnesium, ADP, and actin binding linkage of myosin V: evidence for multiple myosin V-ADP and actomyosin V-ADP states. Biochemistry 44:8826-8840. http://dx.doi.org/10.1021/bi0473509.
    • (2005) Biochemistry , vol.44 , pp. 8826-8840
    • Hannemann, D.E.1    Cao, W.2    Olivares, A.O.3    Robblee, J.P.4    De La Cruz, E.M.5
  • 197
    • 84880070665 scopus 로고    scopus 로고
    • Magnesium impacts myosin V motor activity by altering key conformational changes in the mechanochemical cycle
    • Trivedi DV, Muretta JM, Swenson AM, Thomas DD, Yengo CM. 2013. Magnesium impacts myosin V motor activity by altering key conformational changes in the mechanochemical cycle. Biochemistry 52:4710-4722. http://dx.doi.org/10.1021/bi4004364.
    • (2013) Biochemistry , vol.52 , pp. 4710-4722
    • Trivedi, D.V.1    Muretta, J.M.2    Swenson, A.M.3    Thomas, D.D.4    Yengo, C.M.5
  • 198
    • 73649085109 scopus 로고    scopus 로고
    • Mechanical coupling in myosin V: A simulation study
    • Ovchinnikov V, Trout BL, Karplus M. 2010. Mechanical coupling in myosin V: a simulation study. J Mol Biol 395:815-833. http://dx.doi.org/10.1016/j.jmb.2009.10.029.
    • (2010) J Mol Biol , vol.395 , pp. 815-833
    • Ovchinnikov, V.1    Trout, B.L.2    Karplus, M.3
  • 199
    • 0037025360 scopus 로고    scopus 로고
    • Actin-induced closure of the actin-binding cleft of smooth muscle myosin
    • Yengo CM, De la Cruz EM, Chrin LR, Gaffney DP, Berger CL. 2002. Actin-induced closure of the actin-binding cleft of smooth muscle myosin. J Biol Chem 277:24114-24119. http://dx.doi.org/10.1074/jbc. M111253200.
    • (2002) J Biol Chem , vol.277 , pp. 24114-24119
    • Yengo, C.M.1    De La Cruz, E.M.2    Chrin, L.R.3    Gaffney, D.P.4    Berger, C.L.5
  • 201
    • 84876890444 scopus 로고    scopus 로고
    • Direct real-time detection of the actin-activated power stroke within the myosin catalytic domain
    • Muretta JM, Petersen KJ, Thomas DD. 2013. Direct real-time detection of the actin-activated power stroke within the myosin catalytic domain. Proc Natl Acad SciUSA 110:7211-7216. http://dx.doi.org/10.1073/pnas.1222257110.
    • (2013) Proc Natl Acad SciUSA , vol.110 , pp. 7211-7216
    • Muretta, J.M.1    Petersen, K.J.2    Thomas, D.D.3
  • 202
    • 10644225269 scopus 로고    scopus 로고
    • The effect of F-actin on the relay helix position of myosin II, as revealed by tryptophan fluorescence, and its implications for mechanochemical coupling
    • Conibear PB, Malnasi-Csizmadia A, Bagshaw CR. 2004. The effect of F-actin on the relay helix position of myosin II, as revealed by tryptophan fluorescence, and its implications for mechanochemical coupling. Biochemistry 43:15404-15417. http://dx.doi.org/10.1021/bi048338j.
    • (2004) Biochemistry , vol.43 , pp. 15404-15417
    • Conibear, P.B.1    Malnasi-Csizmadia, A.2    Bagshaw, C.R.3
  • 203
    • 0034719112 scopus 로고    scopus 로고
    • Resolution of conformational states of Dictyostelium myosin II motor domain using tryptophan (W501) mutants: Implications for the open-closed transition identified by crystallography
    • Malnasi-Csizmadia A, Woolley RJ, Bagshaw CR. 2000. Resolution of conformational states of Dictyostelium myosin II motor domain using tryptophan (W501) mutants: implications for the open-closed transition identified by crystallography. Biochemistry 39:16135-16146. http://dx.doi.org/10.1021/bi001125j.
    • (2000) Biochemistry , vol.39 , pp. 16135-16146
    • Malnasi-Csizmadia, A.1    Woolley, R.J.2    Bagshaw, C.R.3
  • 205
    • 0037468838 scopus 로고    scopus 로고
    • Three-dimensional structural dynamics of myosin V by single-molecule fluorescence polarization
    • Forkey JN, Quinlan ME, Shaw MA, Corrie JE, Goldman YE. 2003. Three-dimensional structural dynamics of myosin V by single-molecule fluorescence polarization. Nature 422:399-404. http://dx.doi.org/10.1038/nature01529.
    • (2003) Nature , vol.422 , pp. 399-404
    • Forkey, J.N.1    Quinlan, M.E.2    Shaw, M.A.3    Corrie, J.E.4    Goldman, Y.E.5
  • 206
    • 0032539847 scopus 로고    scopus 로고
    • A large and distinct rotation of the myosin light chain domain occurs upon muscle contraction
    • Baker JE, Brust-Mascher I, Ramachandran S, LaConte LE, Thomas DD. 1998. A large and distinct rotation of the myosin light chain domain occurs upon muscle contraction. Proc Natl Acad Sci U S A 95:2944-2949. http://dx.doi.org/10.1073/pnas.95.6.2944.
    • (1998) Proc Natl Acad Sci U S A , vol.95 , pp. 2944-2949
    • Baker, J.E.1    Brust-Mascher, I.2    Ramachandran, S.3    LaConte, L.E.4    Thomas, D.D.5
  • 207
    • 84964077108 scopus 로고    scopus 로고
    • Direct real-time detection of the structural and biochemical events in the myosin power stroke
    • Muretta JM, Rohde JA, Johnsrud DO, Cornea S, Thomas DD. 2015. Direct real-time detection of the structural and biochemical events in the myosin power stroke. Proc Natl Acad Sci U S A 112:14272-14277. http://dx.doi.org/10.1073/pnas.1514859112.
    • (2015) Proc Natl Acad Sci U S A , vol.112 , pp. 14272-14277
    • Muretta, J.M.1    Rohde, J.A.2    Johnsrud, D.O.3    Cornea, S.4    Thomas, D.D.5
  • 208
    • 84947969124 scopus 로고    scopus 로고
    • Direct measurements of the coordination of lever arm swing and the catalytic cycle in myosin V
    • Trivedi DV, Muretta JR, Swenson AM, Davis JP, Thomas DD, Yengo CM. 2015. Direct measurements of the coordination of lever arm swing and the catalytic cycle in myosin V. Proc Natl Acad Sci U S A 112:14593-14598. http://dx.doi.org/10.1073/pnas.1517566112.
    • (2015) Proc Natl Acad Sci U S A , vol.112 , pp. 14593-14598
    • Trivedi, D.V.1    Muretta, J.R.2    Swenson, A.M.3    Davis, J.P.4    Thomas, D.D.5    Yengo, C.M.6
  • 210
    • 84925533369 scopus 로고    scopus 로고
    • Structure of human cytoplasmic dynein-2 primed for its power stroke
    • Schmidt H, Zalyte R, Urnavicius L, Carter AP. 2015. Structure of human cytoplasmic dynein-2 primed for its power stroke. Nature 518:435-438. http://dx.doi.org/10.1038/nature14023.
    • (2015) Nature , vol.518 , pp. 435-438
    • Schmidt, H.1    Zalyte, R.2    Urnavicius, L.3    Carter, A.P.4
  • 211
    • 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
  • 212
    • 84874531575 scopus 로고    scopus 로고
    • Solid-state and biological nanopore for real-time sensing of single chemical and sequencing of DNA
    • Haque F, Li J, Wu H-C, Liang X-J, Guo P. 2013. Solid-state and biological nanopore for real-time sensing of single chemical and sequencing of DNA. Nano Today 8:56-74. http://dx.doi.org/10.1016/j.nantod.2012.12.008.
    • (2013) Nano Today , vol.8 , pp. 56-74
    • Haque, F.1    Li, J.2    Wu, H.-C.3    Liang, X.-J.4    Guo, P.5
  • 213
    • 84860360735 scopus 로고    scopus 로고
    • Real-time sensing and discrimination of single chemicals using the channel of phi29 DNA packaging nanomotor
    • Haque F, Lunn J, Fang H, Smithrud D, Guo P. 2012. Real-time sensing and discrimination of single chemicals using the channel of phi29 DNA packaging nanomotor. ACS Nano 6:3251-3261. http://dx.doi.org/10.1021/nn3001615.
    • (2012) ACS Nano , vol.6 , pp. 3251-3261
    • Haque, F.1    Lunn, J.2    Fang, H.3    Smithrud, D.4    Guo, P.5
  • 214
    • 84888863270 scopus 로고    scopus 로고
    • Engineered nanopore of phi29 DNA-packaging motor for real-time detection of single colon cancer specific antibody in serum
    • Wang S, Haque F, Rychahou PG, Evers BM, Guo P. 2013. Engineered nanopore of phi29 DNA-packaging motor for real-time detection of single colon cancer specific antibody in serum. ACS Nano 7:9814-9822. http://dx.doi.org/10.1021/nn404435v.
    • (2013) ACS Nano , vol.7 , pp. 9814-9822
    • Wang, S.1    Haque, F.2    Rychahou, P.G.3    Evers, B.M.4    Guo, P.5
  • 215
    • 11144220854 scopus 로고    scopus 로고
    • A vesicle bioreactor as a step toward an artificial cell assembly
    • Noireaux V, Libchaber A. 2004. A vesicle bioreactor as a step toward an artificial cell assembly. Proc Natl Acad Sci U S A 101:17669-17674. http://dx.doi.org/10.1073/pnas.0408236101.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 17669-17674
    • Noireaux, V.1    Libchaber, A.2
  • 216
    • 84906666242 scopus 로고    scopus 로고
    • Nanoshuttles propelled by motor proteins sequentially assemble molecular cargo in a microfluidic device
    • Steuerwald D, Fruh SM, Griss R, Lovchik RD, Vogel V. 2014. Nanoshuttles propelled by motor proteins sequentially assemble molecular cargo in a microfluidic device. Lab Chip 14:3729-3738. http://dx.doi.org/10.1039/C4LC00385C.
    • (2014) Lab Chip , vol.14 , pp. 3729-3738
    • Steuerwald, D.1    Fruh, S.M.2    Griss, R.3    Lovchik, R.D.4    Vogel, V.5
  • 217
    • 0030465241 scopus 로고    scopus 로고
    • Characterization of individual polynucleotide molecules using a membrane channel
    • Kasianowicz JJ, Brandin E, Branton D, Deamer DW. 1996. Characterization of individual polynucleotide molecules using a membrane channel. Proc Natl Acad SciUSA 93:13770-13773. http://dx.doi.org/10.1073/pnas.93.24.13770.
    • (1996) Proc Natl Acad SciUSA , vol.93 , pp. 13770-13773
    • Kasianowicz, J.J.1    Brandin, E.2    Branton, D.3    Deamer, D.W.4
  • 220
    • 84952333338 scopus 로고    scopus 로고
    • Supramolecular photochemistry applied to artificial photosynthesis and molecular logic devices
    • Gust D. 2015. Supramolecular photochemistry applied to artificial photosynthesis and molecular logic devices. Faraday Discuss http://dx.doi.org/10.1039/C5FD00142K.
    • (2015) Faraday Discuss
    • Gust, D.1
  • 221
    • 77953303738 scopus 로고    scopus 로고
    • Optical recognition of converted DNA nucleotides for single-molecule DNA sequencing using nanopore arrays
    • McNally B, Singer A, Yu Z, Sun Y, Weng Z, Meller A. 2010. Optical recognition of converted DNA nucleotides for single-molecule DNA sequencing using nanopore arrays. Nano Lett 10:2237-2244. http://dx.doi.org/10.1021/nl1012147.
    • (2010) Nano Lett , vol.10 , pp. 2237-2244
    • McNally, B.1    Singer, A.2    Yu, Z.3    Sun, Y.4    Weng, Z.5    Meller, A.6
  • 222
    • 1242265462 scopus 로고    scopus 로고
    • Membrane surface dynamics of DNA-threaded nanopores revealed by simultaneous single-molecule optical and ensemble electrical recording
    • Chandler EL, Smith AL, Burden LM, Kasianowicz JJ, Burden DL. 2004. Membrane surface dynamics of DNA-threaded nanopores revealed by simultaneous single-molecule optical and ensemble electrical recording. Langmuir 20:898-905. http://dx.doi.org/10.1021/la 035728i.
    • (2004) Langmuir , vol.20 , pp. 898-905
    • Chandler, E.L.1    Smith, A.L.2    Burden, L.M.3    Kasianowicz, J.J.4    Burden, D.L.5
  • 223
    • 80455154991 scopus 로고    scopus 로고
    • Thermodynamically stable RNA three-way junctions for constructing multifuntional nanoparticles for delivery of therapeutics
    • Shu D, Shu Y, Haque F, Abdelmawla S, Guo P. 2011. Thermodynamically stable RNA three-way junctions for constructing multifuntional nanoparticles for delivery of therapeutics. Nat Nanotechnol 6:658-667. http://dx.doi.org/10.1038/nnano. 2011.105.
    • (2011) Nat Nanotechnol , vol.6 , pp. 658-667
    • Shu, D.1    Shu, Y.2    Haque, F.3    Abdelmawla, S.4    Guo, P.5
  • 224
    • 84865784936 scopus 로고    scopus 로고
    • Ultrastable synergistic tetravalent RNA nanoparticles for targeting to cancers
    • Haque F, Shu D, Shu Y, Shlyakhtenko L, Rychahou P, Evers M, Guo P. 2012. Ultrastable synergistic tetravalent RNA nanoparticles for targeting to cancers. Nano Today 7:245-257. http://dx.doi.org/10.1016/j.nantod.2012.06.010.
    • (2012) Nano Today , vol.7 , pp. 245-257
    • Haque, F.1    Shu, D.2    Shu, Y.3    Shlyakhtenko, L.4    Rychahou, P.5    Evers, M.6    Guo, P.7
  • 225
    • 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
  • 226
    • 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 10:1881-1897. http://dx.doi.org/10.2217/nnm.15.37.
    • (2015) Nanomedicine , vol.10 , pp. 1881-1897
    • Shu, D.1    Pi, F.2    Wang, C.3    Zhang, P.4    Guo, P.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.