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Volumn 10, Issue 12, 2015, Pages 1881-1897

New approach to develop ultra-high inhibitory drug using the power function of the stoichiometry of the targeted nanomachine or biocomplex

Author keywords

binomial distribution; bionanotechnology; drug target; hexameric ATPase; nanobiotechnology; nanomotor; phi29 viral assembly

Indexed keywords

ARTICLE; BACILLUS PHAGE PHI29; BINOMIAL DISTRIBUTION; COPY NUMBER VARIATION; DNA PACKAGING; DRUG INHIBITION; DRUG SYNTHESIS; IN VITRO STUDY; NONHUMAN; PRIORITY JOURNAL; STOICHIOMETRY; VIRION; VIRUS INHIBITION; VIRUS REPLICATION; ALGORITHM; ANTAGONISTS AND INHIBITORS; CHEMICAL MODEL; CHEMISTRY; COMPUTER SIMULATION; DRUG DESIGN; PROTEIN TERTIARY STRUCTURE; VIRUS ASSEMBLY;

EID: 84936972846     PISSN: 17435889     EISSN: 17486963     Source Type: Journal    
DOI: 10.2217/nnm.15.37     Document Type: Article
Times cited : (13)

References (109)
  • 1
    • 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, et al. Common mechanisms of DNA translocation motors in bacteria and viruses using one-way revolution mechanism without rotation. Biotechnol. Adv. 32, 853-872 (2014).
    • (2014) Biotechnol. Adv. , vol.32 , pp. 853-872
    • Guo, P.1    Zhao, Z.2    Haak, J.3
  • 3
    • 34248340401 scopus 로고    scopus 로고
    • Viral nanomotors for packaging of dsDNA and dsRNA
    • Guo PX, Lee TJ. Viral nanomotors for packaging of dsDNA and dsRNA. Mol. Microbiol. 64, 886-903 (2007).
    • (2007) Mol. Microbiol. , vol.64 , pp. 886-903
    • Guo, P.X.1    Lee, T.J.2
  • 4
    • 85027930977 scopus 로고    scopus 로고
    • Popping the cork: Mechanisms of phage genome ejection
    • Molineux IJ, Panja D. Popping the cork: mechanisms of phage genome ejection. Nat. Rev. Microbiol. 11(3), 194-204 (2013).
    • (2013) Nat. Rev. Microbiol. , vol.11 , Issue.3 , pp. 194-204
    • Molineux, I.J.1    Panja, D.2
  • 5
    • 0346147005 scopus 로고    scopus 로고
    • Biochemistry of mechanoenzymes: Biological motors for nanotechnology
    • Lee BS, Lee SC, Holliday LS. Biochemistry of mechanoenzymes: biological motors for nanotechnology. Biomed. Microdevices 5(4), 269-280 (2003).
    • (2003) Biomed. Microdevices , vol.5 , Issue.4 , pp. 269-280
    • Lee, B.S.1    Lee, S.C.2    Holliday, L.S.3
  • 7
    • 34249302620 scopus 로고    scopus 로고
    • Exosome-mediated transfer of mRNAs and microRNAs is a novel mechanism of genetic exchange between cells
    • Valadi H, Ekstrom K, Bossios A, Sjostrand M, Lee JJ, Lotvall JO. Exosome-mediated transfer of mRNAs and microRNAs is a novel mechanism of genetic exchange between cells. Nat. Cell Biol. 9(6), 654-659 (2007).
    • (2007) Nat. Cell Biol. , vol.9 , Issue.6 , pp. 654-659
    • Valadi, H.1    Ekstrom, K.2    Bossios, A.3    Sjostrand, M.4    Lee, J.J.5    Lotvall, J.O.6
  • 8
    • 84897080142 scopus 로고    scopus 로고
    • Cancer becomes wasteful: Emerging roles of exosomes (dagger) in cell-fate determination
    • Wendler F, Bota-Rabassedas N, Franch-Marro X. Cancer becomes wasteful: emerging roles of exosomes (dagger) in cell-fate determination. J. Extracell. Vesicles 2(22390), 1-9 (2013).
    • (2013) J. Extracell. Vesicles , vol.2 , Issue.1-9 , pp. 22390
    • Wendler, F.1    Bota-Rabassedas, N.2    Franch-Marro, X.3
  • 9
    • 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. Role of channel lysines and push through a one-way valve mechanism of viral DNA packaging motor. Biophys. J. 102, 127-135 (2012).
    • (2012) Biophys. J. , vol.102 , pp. 127-135
    • Fang, H.1    Jing, P.2    Haque, F.3    Guo, P.4
  • 10
    • 84862878463 scopus 로고    scopus 로고
    • Push through one-way valve mechanism of viral DNA packaging
    • Zhang H, Schwartz C, De Donatis GM, Guo P. Push through one-way valve mechanism of viral DNA packaging. Adv. Virus Res. 83, 415-465 (2012).
    • (2012) Adv. Virus Res. , vol.83 , pp. 415-465
    • Zhang, H.1    Schwartz, C.2    De Donatis, G.M.3    Guo, P.4
  • 11
    • 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 One-way traffic of a viral motor channel for double-stranded DNA translocation. Nano Lett. 10, 3620-3627 (2010).
    • (2010) Nano Lett. , vol.10 , pp. 3620-3627
    • Jing, P.1    Haque, F.2    Shu, D.3    Montemagno, C.4    Guo, P.5
  • 12
    • 0030465241 scopus 로고    scopus 로고
    • Characterization of individual polynucleotide molecules using a membrane channel
    • Kasianowicz JJ, Brandin E, Branton D, Deamer DW. Characterization of individual polynucleotide molecules using a membrane channel. Proc. Natl Acad. Sci. USA 93(24), 13770-13773 (1996).
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , Issue.24 , pp. 13770-13773
    • Kasianowicz, J.J.1    Brandin, E.2    Branton, D.3    Deamer, D.W.4
  • 14
    • 70449556810 scopus 로고    scopus 로고
    • Translocation of doublestranded DNA through membrane-Adapted phi29 motor protein nanopores
    • Wendell D, Jing P, Geng J, et al. Translocation of doublestranded DNA through membrane-Adapted phi29 motor protein nanopores. Nat. Nanotechnol. 4, 765-772 (2009).
    • (2009) Nat. Nanotechnol. , vol.4 , pp. 765-772
    • Wendell, D.1    Jing, P.2    Geng, J.3
  • 15
    • 79952271938 scopus 로고    scopus 로고
    • Dynamics of unfolded protein transport through an aerolysin pore
    • Pastoriza-Gallego M, Rabah L, Gibrat G, et al. Dynamics of unfolded protein transport through an aerolysin pore. J. Am. Chem. Soc. 133(9), 2923-2931 (2011).
    • (2011) J. Am. Chem. Soc. , vol.133 , Issue.9 , pp. 2923-2931
    • Pastoriza-Gallego, M.1    Rabah, L.2    Gibrat, G.3
  • 16
    • 85015540432 scopus 로고
    • How chaperonins monitor their protein charges
    • Ezzell C. How chaperonins monitor their protein charges. J. NIH Res. 6, 31-34 (1994).
    • (1994) J. NIH Res. , vol.6 , pp. 31-34
    • Ezzell, C.1
  • 17
    • 0041885325 scopus 로고    scopus 로고
    • Proliferating cell nuclear antigen (PCNA): A dancer with many partners
    • Maga G, Hubscher U. Proliferating cell nuclear antigen (PCNA): a dancer with many partners. J. Cell Sci. 116(Pt 15), 3051-3060 (2003).
    • (2003) J. Cell Sci. , vol.116 , pp. 3051-3060
    • Maga, G.1    Hubscher, U.2
  • 18
    • 0028200647 scopus 로고
    • The in vitro ATPases of bacteriophage ? Terminase and its large subunit, gene product A
    • Rubinchik S, Parris W, Gold M. The in vitro ATPases of bacteriophage ? terminase and its large subunit, gene product A. J. Biol. Chem. 269, 13586-13593 (1994).
    • (1994) J. Biol. Chem. , vol.269 , pp. 13586-13593
    • Rubinchik, S.1    Parris, W.2    Gold, M.3
  • 19
    • 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. The ATPase of the phi29 DNA-packaging motor is a member of the hexameric AAA+ superfamily. Virology 443, 20-27 (2013).
    • (2013) Virology , vol.443 , pp. 20-27
    • Schwartz, C.1    De Donatis, G.M.2    Fang, H.3    Guo, P.4
  • 20
    • 84892585316 scopus 로고    scopus 로고
    • Icosahedral bacteriophage PhiX174 forms a tail for DNA transport during infection
    • Sun L, Young LN, Zhang X, et al. Icosahedral bacteriophage PhiX174 forms a tail for DNA transport during infection. Nature 505(7483), 432-435 (2014).
    • (2014) Nature , vol.505 , Issue.7483 , pp. 432-435
    • Sun, L.1    Young, L.N.2    Zhang, X.3
  • 21
    • 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 HC, Liang XJ, Guo P. Solid-state and biological nanopore for real-Time sensing of single chemical and sequencing of DNA. Nano Today 8, 56-74 (2013).
    • (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
  • 22
    • 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. Real-Time sensing and discrimination of single chemicals using the channel of Phi29 DNA packaging nanomotor. ACS Nano 6, 3251-3261 (2012).
    • (2012) ACS Nano , vol.6 , pp. 3251-3261
    • Haque, F.1    Lunn, J.2    Fang, H.3    Smithrud, D.4    Guo, P.5
  • 23
    • 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. Engineered nanopore of Phi29 DNA-packaging motor for real-Time detection of single colon cancer specific antibody in serum. ACS Nano 7, 9814-9822 (2013).
    • (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
  • 25
    • 0034711368 scopus 로고    scopus 로고
    • Nanoelectromechanical systems
    • Craighead HG. Nanoelectromechanical systems. Science 290, 1532-1536 (2000).
    • (2000) Science , vol.290 , pp. 1532-1536
    • Craighead, H.G.1
  • 27
    • 84876585976 scopus 로고    scopus 로고
    • Channel size conversion of Phi29 DNA-packaging nanomotor for discrimination of single-And double-stranded nucleic acids
    • Geng J, Wang S, Fang H, Guo P. Channel size conversion of Phi29 DNA-packaging nanomotor for discrimination of single-And double-stranded nucleic acids. ACS Nano 7(4), 3315-3323 (2013).
    • (2013) ACS Nano , vol.7 , Issue.4 , pp. 3315-3323
    • Geng, J.1    Wang, S.2    Fang, H.3    Guo, P.4
  • 28
    • 77953303738 scopus 로고    scopus 로고
    • Optical recognition of converted DNA nucleotides for singlemolecule DNA sequencing using nanopore arrays
    • McNally B, Singer A, Yu Z, Sun Y, Weng Z, Meller A Optical Recognition of Converted DNA Nucleotides for Singlemolecule DNA Sequencing Using Nanopore Arrays. Nano Lett. 10(6), 2237-2244 (2010).
    • (2010) Nano Lett. , vol.10 , Issue.6 , pp. 2237-2244
    • McNally, B.1    Singer, A.2    Yu, Z.3    Sun, Y.4    Weng, Z.5    Meller, A.6
  • 29
    • 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. Membrane surface dynamics of DNA-Threaded nanopores revealed by simultaneous single-molecule optical and ensemble electrical recording. Langmuir 20(3), 898-905 (2004).
    • (2004) Langmuir , vol.20 , Issue.3 , pp. 898-905
    • Chandler, E.L.1    Smith, A.L.2    Burden, L.M.3    Kasianowicz, J.J.4    Burden, D.L.5
  • 30
    • 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. Thermodynamically stable RNA three-way junctions for constructing multifuntional nanoparticles for delivery of therapeutics. Nat. Nanotechnol. 6, 658-667 (2011).
    • (2011) Nat. Nanotechnol. , vol.6 , pp. 658-667
    • Shu, D.1    Shu, Y.2    Haque, F.3    Abdelmawla, S.4    Guo, P.5
  • 31
    • 84865784936 scopus 로고    scopus 로고
    • Ultrastable synergistic tetravalent RNA nanoparticles for targeting to cancers
    • Haque F, Shu D, Shu Y, et al. Ultrastable synergistic tetravalent RNA nanoparticles for targeting to cancers. Nano Today 7, 245-257 (2012).
    • (2012) Nano Today , vol.7 , pp. 245-257
    • Haque, F.1    Shu, D.2    Shu, Y.3
  • 32
    • 78049300491 scopus 로고    scopus 로고
    • FtsK DNA translocase: The fast motor that knows where its going
    • Crozat E, Grainge I. FtsK DNA translocase: the fast motor that knows where its going. Chembiochem. 11, 2232-2243 (2010).
    • (2010) Chembiochem. , vol.11 , pp. 2232-2243
    • Crozat, E.1    Grainge, I.2
  • 33
    • 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. Revolution rather than rotation of AAA+ hexameric phi29 nanomotor for viral dsDNA packaging without coiling. Virology 443, 28-39 (2013).
    • (2013) Virology , vol.443 , pp. 28-39
    • Schwartz, C.1    De Donatis, G.M.2    Zhang, H.3    Fang, H.4    Guo, P.5
  • 35
    • 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. Discovery of a new motion mechanism of biomotors similar to the earth revolving around the sun without rotation. Virology 446, 133-143 (2013).
    • (2013) Virology , vol.446 , pp. 133-143
    • Guo, P.1    Schwartz, C.2    Haak, J.3    Zhao, Z.4
  • 36
    • 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, et al. Finding of widespread viral and bacterial revolution dsDNA translocation motors distinct from rotation motors by channel chirality and size. Cell Biosci. 4, 30 (2014).
    • (2014) Cell Biosci. , vol.4 , Issue.30
    • De-Donatis, G.1    Zhao, Z.2    Wang, S.3
  • 38
    • 84871010618 scopus 로고    scopus 로고
    • Prevalence of and viral outcomes associated with primary HIV-1 drug resistance
    • Buskin SE, Zhang S, Thibault CS. Prevalence of and viral outcomes associated with primary HIV-1 drug resistance. Open AIDS J. 6, 181-187 (2012).
    • (2012) Open AIDS J. , vol.6 , pp. 181-187
    • Buskin, S.E.1    Zhang, S.2    Thibault, C.S.3
  • 40
    • 84895109493 scopus 로고    scopus 로고
    • Bedaquiline-The first ATP synthase inhibitor against multi drug resistant tuberculosis
    • Lakshmanan M, Xavier AS. Bedaquiline-The first ATP synthase inhibitor against multi drug resistant tuberculosis. J. Young Pharm. 5(4), 112-115 (2013).
    • (2013) J. Young Pharm. , vol.5 , Issue.4 , pp. 112-115
    • Lakshmanan, M.1    Xavier, A.S.2
  • 41
    • 38349155799 scopus 로고    scopus 로고
    • Trastuzumab signaling in ErbB2-overexpressing inflammatory breast cancer correlates with X-linked inhibitor of apoptosis protein expression
    • Aird KM, Ding XY, Baras A, et al. Trastuzumab signaling in ErbB2-overexpressing inflammatory breast cancer correlates with X-linked inhibitor of apoptosis protein expression. Mol. Cancer Ther. 7(1), 38-47 (2008).
    • (2008) Mol. Cancer Ther. , vol.7 , Issue.1 , pp. 38-47
    • Aird, K.M.1    Ding, X.Y.2    Baras, A.3
  • 42
    • 0036090950 scopus 로고    scopus 로고
    • Down regulation of bcl2 expression in invasive ductal carcinomas is both estrogenand progesterone-receptor dependent and associated with poor prognostic factors
    • Park SH, Kim H, Song BJ. Down regulation of bcl2 expression in invasive ductal carcinomas is both estrogenand progesterone-receptor dependent and associated with poor prognostic factors. Pathol. Oncol. Res. 8(1), 26-30 (2002).
    • (2002) Pathol. Oncol. Res. , vol.8 , Issue.1 , pp. 26-30
    • Park, S.H.1    Kim, H.2    Song, B.J.3
  • 43
    • 77954243341 scopus 로고    scopus 로고
    • Targeted delivery of RNAi therapeutics with endogenous and exogenous ligand-based mechanisms
    • Akinc A, Querbes W, De S, et al. Targeted delivery of RNAi therapeutics with endogenous and exogenous ligand-based mechanisms. Mol. Ther. 18(7), 1357-1364 (2010).
    • (2010) Mol. Ther. , vol.18 , Issue.7 , pp. 1357-1364
    • Akinc, A.1    Querbes, W.2    De, S.3
  • 45
    • 79960925147 scopus 로고    scopus 로고
    • Targeted drug delivery to tumors: Myths, reality and possibility
    • Bae YH, Park K. Targeted drug delivery to tumors: myths, reality and possibility. J. Control Release 153(3), 198-205 (2011).
    • (2011) J. Control Release , vol.153 , Issue.3 , pp. 198-205
    • Bae, Y.H.1    Park, K.2
  • 46
    • 84865436732 scopus 로고    scopus 로고
    • Uniqueness, advantages, challenges, solutions, and perspectives in therapeutics applying RNA nanotechnology
    • Guo P, Haque F, Hallahan B, Reif R, Li H. Uniqueness, advantages, challenges, solutions, and perspectives in therapeutics applying RNA nanotechnology. Nucleic Acid Ther. 22(4), 226-245 (2012).
    • (2012) Nucleic Acid Ther. , vol.22 , Issue.4 , pp. 226-245
    • Guo, P.1    Haque, F.2    Hallahan, B.3    Reif, R.4    Li, H.5
  • 47
    • 0033290332 scopus 로고    scopus 로고
    • HIV's potent cocktail
    • Lusky K. HIV's potent cocktail. Contemp. Longterm Care 22(12), 59 (1999).
    • (1999) Contemp. Longterm Care , vol.22 , Issue.12 , pp. 59
    • Lusky, K.1
  • 48
    • 84899730819 scopus 로고    scopus 로고
    • MiR-17-5p downregulation contributes to paclitaxel resistance of lung cancer cells through altering Beclin1 expression
    • Chatterjee A, Chattopadhyay D, Chakrabarti G. miR-17-5p downregulation contributes to paclitaxel resistance of lung cancer cells through altering Beclin1 expression. PLoS ONE 9(4), e95716 (2014).
    • (2014) PLoS ONE , vol.9 , Issue.4 , pp. e95716
    • Chatterjee, A.1    Chattopadhyay, D.2    Chakrabarti, G.3
  • 49
    • 84882449121 scopus 로고    scopus 로고
    • Combining T-cell immunotherapy and anti-Androgen therapy for prostate cancer
    • Sanchez C, Chan R, Bajgain P, et al. Combining T-cell immunotherapy and anti-Androgen therapy for prostate cancer. Prostate Cancer Prostatic Dis. 16(2), 123-131 (2013).
    • (2013) Prostate Cancer Prostatic Dis. , vol.16 , Issue.2 , pp. 123-131
    • Sanchez, C.1    Chan, R.2    Bajgain, P.3
  • 50
    • 77955920848 scopus 로고    scopus 로고
    • Synergistic growth inhibition of anaplastic large cell lymphoma cells by combining cellular ALK gene silencing and a low dose of the kinase inhibitor U0126
    • Ito M, Zhao N, Zeng Z, Chang CC, Zu Y. Synergistic growth inhibition of anaplastic large cell lymphoma cells by combining cellular ALK gene silencing and a low dose of the kinase inhibitor U0126. Cancer Gene Ther. 17(9), 633-644 (2010).
    • (2010) Cancer Gene Ther. , vol.17 , Issue.9 , pp. 633-644
    • Ito, M.1    Zhao, N.2    Zeng, Z.3    Chang, C.C.4    Zu, Y.5
  • 51
    • 84912150523 scopus 로고    scopus 로고
    • Binomial distribution for quantification of protein subunits in biological nanoassemblies and functional nanomachines
    • Fang H, Zhang P, Huang LP, et al. Binomial distribution for quantification of protein subunits in biological nanoassemblies and functional nanomachines. Nanomedicine 10(7), 1433-1440 (2014).
    • (2014) Nanomedicine , vol.10 , Issue.7 , pp. 1433-1440
    • Fang, H.1    Zhang, P.2    Huang, L.P.3
  • 52
    • 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. Inter-RNA interaction of phage phi29 pRNA to form a hexameric complex for viral DNA transportation. Mol. Cell. 2, 149-155 (1998).
    • (1998) Mol. Cell. , vol.2 , pp. 149-155
    • Guo, P.1    Zhang, C.2    Chen, C.3    Trottier, M.4    Garver, K.5
  • 53
    • 33947213307 scopus 로고    scopus 로고
    • Experimental test of connector rotation during DNA packaging into bacteriophage phi29 capsids
    • Hugel T, Michaelis J, Hetherington CL, et al. Experimental test of connector rotation during DNA packaging into bacteriophage phi29 capsids. PloS Biol. 5, 558-567 (2007).
    • (2007) PloS Biol. , vol.5 , pp. 558-567
    • Hugel, T.1    Michaelis, J.2    Hetherington, C.L.3
  • 54
    • 19444373849 scopus 로고    scopus 로고
    • Binding of pRNA to the N-Terminal 14 amino acids of connector protein of bacterial phage phi29
    • Xiao F, Moll D, Guo S, Guo P. Binding of pRNA to the N-Terminal 14 amino acids of connector protein of bacterial phage phi29. Nucleic Acids Res. 33, 2640-2649 (2005).
    • (2005) Nucleic Acids Res. , vol.33 , pp. 2640-2649
    • Xiao, F.1    Moll, D.2    Guo, S.3    Guo, P.4
  • 55
    • 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. Prohead and DNA-gp3-dependent ATPase activity of the DNA packaging protein gp16 of bacteriophage phi29. J. Mol. Biol. 197, 229-236 (1987).
    • (1987) J. Mol. Biol. , vol.197 , pp. 229-236
    • Guo, P.1    Peterson, C.2    Anderson, D.3
  • 56
    • 0031060162 scopus 로고    scopus 로고
    • Approaches to determine stoichiometry of viral assembly components
    • Trottier M, Guo P. Approaches to determine stoichiometry of viral assembly components. J. Virol. 71, 487-494 (1997).
    • (1997) J. Virol. , vol.71 , pp. 487-494
    • Trottier, M.1    Guo, P.2
  • 57
    • 0023660929 scopus 로고
    • Initiation events in in vitro packaging of bacteriophage phi29 DNA-gp3
    • Guo P, Peterson C, Anderson D. Initiation events in in vitro packaging of bacteriophage phi29 DNA-gp3. J. Mol. Biol. 197, 219-228 (1987).
    • (1987) J. Mol. Biol. , vol.197 , pp. 219-228
    • Guo, P.1    Peterson, C.2    Anderson, D.3
  • 58
    • 84878292282 scopus 로고    scopus 로고
    • Mechanism of one-way traffic of hexameric phi29 DNA packaging motor with four electropositive relaying layers facilitating antiparallel revolution
    • Zhao Z, Khisamutdinov E, Schwartz C, Guo P. Mechanism of one-way traffic of hexameric phi29 DNA packaging motor with four electropositive relaying layers facilitating antiparallel revolution. ACS Nano 7, 4082-4092 (2013).
    • (2013) ACS Nano , vol.7 , pp. 4082-4092
    • Zhao, Z.1    Khisamutdinov, E.2    Schwartz, C.3    Guo, P.4
  • 60
    • 57349086349 scopus 로고    scopus 로고
    • RCSB PDB. www.rcsb.org/pdb
    • RCSB PDB.
  • 61
    • 79952816898 scopus 로고    scopus 로고
    • Structure and mechanism of the hexameric MecA-ClpC molecular machine
    • Wang F, Mei Z, Qi Y, et al. Structure and mechanism of the hexameric MecA-ClpC molecular machine. Nature 471, 331-335 (2011).
    • (2011) Nature , vol.471 , pp. 331-335
    • Wang, F.1    Mei, Z.2    Qi, Y.3
  • 62
    • 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. Two classes of nucleic acid translocation motors: rotation and revolution without rotation. Cell Biosci. 4(1), 54 (2014).
    • (2014) Cell Biosci. , vol.4 , Issue.1 , pp. 54
    • Guo, P.1    Grainge, I.2    Zhao, Z.3    Vieweger, M.4
  • 63
    • 80051707836 scopus 로고    scopus 로고
    • The DNA-packaging nanomotor of tailed bacteriophages
    • Casjens SR. The DNA-packaging nanomotor of tailed bacteriophages. Nat. Rev. Microbiol. 9(9), 647-657 (2011).
    • (2011) Nat. Rev. Microbiol. , vol.9 , Issue.9 , pp. 647-657
    • Casjens, S.R.1
  • 66
    • 0022444512 scopus 로고
    • A defined system for in vitro packaging of DNA-gp3 of the Bacillus subtilis bacteriophage phi29
    • Guo P, Grimes S, Anderson D. A defined system for in vitro packaging of DNA-gp3 of the Bacillus subtilis bacteriophage phi29. Proc. Natl Acad. Sci. USA 83, 3505-3509 (1986).
    • (1986) Proc. Natl Acad. Sci. USA , vol.83 , pp. 3505-3509
    • Guo, P.1    Grimes, S.2    Anderson, D.3
  • 67
    • 0028361637 scopus 로고
    • The proximate 5 and 3 ends of the 120-base viral RNA (pRNA) are crucial for the packaging of bacteriophage ?d29 DNA
    • Zhang CL, Lee C-S, Guo P. The proximate 5 and 3 ends of the 120-base viral RNA (pRNA) are crucial for the packaging of bacteriophage ?d29 DNA. Virology 201, 77-85 (1994).
    • (1994) Virology , vol.201 , pp. 77-85
    • Zhang, C.L.1    Lee, C.-S.2    Guo, P.3
  • 68
    • 2342493879 scopus 로고    scopus 로고
    • Construction of phi29 DNA-packaging RNA (pRNA) monomers, dimers and trimers with variable sizes and shapes as potential parts for nano-devices
    • Shu D, Huang L, Hoeprich S, Guo P. Construction of phi29 DNA-packaging RNA (pRNA) monomers, dimers and trimers with variable sizes and shapes as potential parts for nano-devices. J. Nanosci. Nanotechnol. 3, 295-302 (2003).
    • (2003) J. Nanosci. Nanotechnol. , vol.3 , pp. 295-302
    • Shu, D.1    Huang, L.2    Hoeprich, S.3    Guo, P.4
  • 69
    • 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. A highly sensitive system for the assay of in vitro viral assembly of bacteriophage phi29 of Bacillus subtilis. Virology 202, 1039-1042 (1994).
    • (1994) Virology , vol.202 , pp. 1039-1042
    • Lee, C.S.1    Guo, P.2
  • 70
    • 0029655643 scopus 로고    scopus 로고
    • Complete inhibition of virion assembly in vivo with mutant pRNA essential for phage phi29 DNA packaging
    • Trottier M, Zhang CL, Guo P. Complete inhibition of virion assembly in vivo with mutant pRNA essential for phage phi29 DNA packaging. J. Virol. 70, 55-61 (1996).
    • (1996) J. Virol. , vol.70 , pp. 55-61
    • Trottier, M.1    Zhang, C.L.2    Guo, P.3
  • 71
    • 0030896203 scopus 로고    scopus 로고
    • Sequential action of six virus-encoded DNA-packaging RNAs during phage phi29 genomic DNA translocation
    • Chen C, Guo P. Sequential action of six virus-encoded DNA-packaging RNAs during phage phi29 genomic DNA translocation. J. Virol. 71(5), 3864-3871 (1997).
    • (1997) J. Virol. , vol.71 , Issue.5 , pp. 3864-3871
    • Chen, C.1    Guo, P.2
  • 72
    • 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. Sequential hydrolysis of ATP molecules bound in interacting catalytic sites of Escherichia coli transcription termination protein Rho. J. Biol. Chem. 273(41), 26477-26486 (1998).
    • (1998) J. Biol. Chem. , vol.273 , Issue.41 , pp. 26477-26486
    • Stitt, B.L.1    Xu, Y.2
  • 73
    • 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. Tenascin-C hexabrachion assembly is a sequential two-step process initiated by coiled-coil alpha-helices. J. Biol. Chem. 273(17), 10602-10608 (1998).
    • (1998) J. Biol. Chem. , vol.273 , Issue.17 , pp. 10602-10608
    • Kammerer, R.A.1    Schulthess, T.2    Landwehr, R.3    Lustig, A.4    Fischer, D.5    Engel, J.6
  • 74
    • 20744434561 scopus 로고    scopus 로고
    • Cooperative mechanism of RNA packaging motor
    • Lisal J, Tuma R. Cooperative mechanism of RNA packaging motor. J. Biol. Chem. 280, 23157-23164 (2005).
    • (2005) J. Biol. Chem. , vol.280 , pp. 23157-23164
    • Lisal, J.1    Tuma, R.2
  • 75
    • 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, et al. Detailed characterization of the cooperative mechanism of Ca(2+) binding and catalytic activation in the Ca(2+) transport (SERCA) ATPase. Biochemistry 39(30), 8758-8767 (2000).
    • (2000) Biochemistry , vol.39 , Issue.30 , pp. 8758-8767
    • Zhang, Z.1    Lewis, D.2    Strock, C.3
  • 76
    • 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. Ordered and cooperative binding of opposing globular domains of calmodulin to the plasma membrane Ca-ATPase. J. Biol. Chem. 275(3), 1731-1738 (2000).
    • (2000) J. Biol. Chem. , vol.275 , Issue.3 , pp. 1731-1738
    • Sun, H.1    Squier, T.C.2
  • 77
    • 0025316679 scopus 로고
    • Kinetic analysis of cooperative interactions induced by Mn2+ binding to the chloroplast H(+)-ATPase
    • Hiller R, Carmeli C. Kinetic analysis of cooperative interactions induced by Mn2+ binding to the chloroplast H(+)-ATPase. Biochemistry 29(26), 6186-6192 (1990).
    • (1990) Biochemistry , vol.29 , Issue.26 , pp. 6186-6192
    • Hiller, R.1    Carmeli, C.2
  • 78
    • 0020410192 scopus 로고
    • Cooperative behavior of smooth muscle myosin
    • Persechini A, Hartshorne DJ. Cooperative behavior of smooth muscle myosin. Fed. Proc. 41(12), 2868-2872 (1982).
    • (1982) Fed. Proc. , vol.41 , Issue.12 , pp. 2868-2872
    • Persechini, A.1    Hartshorne, D.J.2
  • 79
    • 0029039737 scopus 로고
    • Sequential interactions of structural proteins in phage phi29 procapsid assembly
    • Lee CS, Guo P. Sequential interactions of structural proteins in phage phi29 procapsid assembly. J. Virol. 69, 5024-5032 (1995).
    • (1995) J. Virol. , vol.69 , pp. 5024-5032
    • Lee, C.S.1    Guo, P.2
  • 80
    • 0002107186 scopus 로고
    • Control mechanisms in dsDNA bacteriophage assembly
    • Calendar R (Eds). Plenum Publishing Corp., NY, USA
    • Casjens S, Hendrix R. Control mechanisms in dsDNA bacteriophage assembly. In: The Bacteriophages Vol. 1. Calendar R (Eds). Plenum Publishing Corp., NY, USA, 15-92 (1988).
    • (1988) The Bacteriophages , vol.1 , pp. 15-92
    • Casjens, S.1    Hendrix, R.2
  • 81
    • 84865988896 scopus 로고    scopus 로고
    • Sequence-dependent synergistic inhibition of human glioma cell lines by combined temozolomide and miR-21 inhibitor gene therapy
    • Qian X, Ren Y, Shi Z, et al. Sequence-dependent synergistic inhibition of human glioma cell lines by combined temozolomide and miR-21 inhibitor gene therapy. Mol. Pharm. 9(9), 2636-2645 (2012).
    • (2012) Mol. Pharm. , vol.9 , Issue.9 , pp. 2636-2645
    • Qian, X.1    Ren, Y.2    Shi, Z.3
  • 82
    • 34748878999 scopus 로고    scopus 로고
    • Instrumentation and metrology for single RNA counting in biological complexes or nanoparticles by a single molecule dual-view system
    • Zhang H, Shu D, Huang F, Guo P. Instrumentation and metrology for single RNA counting in biological complexes or nanoparticles by a single molecule dual-view system. RNA 13, 1793-1802 (2007).
    • (2007) RNA , vol.13 , pp. 1793-1802
    • Zhang, H.1    Shu, D.2    Huang, F.3    Guo, P.4
  • 83
    • 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. New approaches to stoichiometry determination and mechanism investigation on RNA involved in intermediate reactions. Nucleic Acids Symp. Ser. 36, 190-193 (1997).
    • (1997) Nucleic Acids Symp. Ser. , vol.36 , pp. 190-193
    • Chen, C.1    Trottier, M.2    Guo, P.3
  • 84
    • 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. Counting of six pRNAs of phi29 DNA-packaging motor with customized single molecule dual-view system. EMBO J. 26, 527-537 (2007).
    • (2007) EMBO J. , vol.26 , pp. 527-537
    • Shu, D.1    Zhang, H.2    Jin, J.3    Guo, P.4
  • 85
    • 84878025754 scopus 로고    scopus 로고
    • Fabrication of 14 different RNA nanoparticles for specific tumor targeting without accumulation in normal organs
    • Shu Y, Haque F, Shu D, et al. Fabrication of 14 different RNA nanoparticles for specific tumor targeting without accumulation in normal organs. RNA 19, 766-777 (2013).
    • (2013) RNA , vol.19 , pp. 766-777
    • Shu, Y.1    Haque, F.2    Shu, D.3
  • 86
    • 84883203978 scopus 로고    scopus 로고
    • Fabrication of pRNA nanoparticles to deliver therapeutic RNAs and bioactive compounds into tumor cells
    • Shu Y, Shu D, Haque F, Guo P. Fabrication of pRNA nanoparticles to deliver therapeutic RNAs and bioactive compounds into tumor cells. Nat. Protoc. 8(9), 1635-1659 (2013).
    • (2013) Nat. Protoc. , vol.8 , Issue.9 , pp. 1635-1659
    • Shu, Y.1    Shu, D.2    Haque, F.3    Guo, P.4
  • 87
    • 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, et al. Crystal structure of 3WJ core revealing divalent ion-promoted thermostability and assembly of the Phi29 hexameric motor pRNA. RNA 19, 1226-1237 (2013).
    • (2013) RNA , vol.19 , pp. 1226-1237
    • Zhang, H.1    Endrizzi, J.A.2    Shu, Y.3
  • 88
    • 35348840808 scopus 로고    scopus 로고
    • In vivo hexamerization and characterization of the Arabidopsis AAA ATPase CDC48A complex using forster resonance energy transferfluorescence lifetime imaging microscopy and fluorescence correlation spectroscopy
    • Aker J, Hesselink R, Engel R, et al. In vivo hexamerization and characterization of the Arabidopsis AAA ATPase CDC48A complex using forster resonance energy transferfluorescence lifetime imaging microscopy and fluorescence correlation spectroscopy. Plant Physiology 145(2), 339-350 (2007).
    • (2007) Plant Physiology , vol.145 , Issue.2 , pp. 339-350
    • Aker, J.1    Hesselink, R.2    Engel, R.3
  • 89
    • 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. EM single particle analysis of the ATP-dependent BchI complex of magnesium chelatase: an AAA(+) hexamer. J. Struct. Biol. 146(1-2), 227-233 (2004).
    • (2004) J. Struct. Biol. , vol.146 , Issue.1-2 , pp. 227-233
    • Willows, R.D.1    Hansson, A.2    Birch, D.3    Al-Karadaghi, S.4    Hansson, M.5
  • 90
    • 0036308842 scopus 로고    scopus 로고
    • The hexameric ring structure of the Escherichia coli RuvB branch migration protein
    • Chen YJ, Yu X, Egelman EH. The hexameric ring structure of the Escherichia coli RuvB branch migration protein. J. Mol. Biol. 319(3), 587-591 (2002).
    • (2002) J. Mol. Biol. , vol.319 , Issue.3 , pp. 587-591
    • Chen, Y.J.1    Yu, X.2    Egelman, E.H.3
  • 91
    • 84880576754 scopus 로고    scopus 로고
    • The structure of the NTPase that powers DNA packaging into sulfolobus turreted icosahedral virus 2
    • Happonen LJ, Oksanen E, Liljeroos L, Goldman A, Kajander T, Butcher SJ. The structure of the NTPase that powers DNA packaging into sulfolobus turreted icosahedral virus 2. J. Virol. 87, 8388-8398 (2013).
    • (2013) J. Virol. , vol.87 , pp. 8388-8398
    • Happonen, L.J.1    Oksanen, E.2    Liljeroos, L.3    Goldman, A.4    Kajander, T.5    Butcher, S.J.6
  • 92
    • 65149084160 scopus 로고    scopus 로고
    • The AAA+ superfamily of functionally diverse proteins
    • Snider J, Thibault G, Houry WA. The AAA+ superfamily of functionally diverse proteins. Genome Biol. 9(4), 216-216 (2008).
    • (2008) Genome Biol. , vol.9 , Issue.4 , pp. 216-216
    • Snider, J.1    Thibault, G.2    Houry, W.A.3
  • 93
    • 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. 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 (2012).
    • (2012) Nucleic Acids Res. , vol.40 , pp. 2577-2586
    • Schwartz, C.1    Fang, H.2    Huang, L.3    Guo, P.4
  • 94
    • 0000916475 scopus 로고    scopus 로고
    • DNA-packaging pRNA as target for complete inhibition of viral assembly in vitro and in vivo
    • Trottier M, Garver K, Zhang C, Guo P. DNA-packaging pRNA as target for complete inhibition of viral assembly in vitro and in vivo. Nucleic Acids Symp. Ser. 36, 187-189 (1997).
    • (1997) Nucleic Acids Symp. Ser. , vol.36 , pp. 187-189
    • Trottier, M.1    Garver, K.2    Zhang, C.3    Guo, P.4
  • 95
    • 0032981057 scopus 로고    scopus 로고
    • Sequence requirement for handin-hand interaction in formation of pRNA dimers and hexamers to gear phi29 DNA translocation motor
    • Chen C, Zhang C, Guo P. Sequence requirement for handin-hand interaction in formation of pRNA dimers and hexamers to gear phi29 DNA translocation motor. RNA 5, 805-818 (1999).
    • (1999) RNA , vol.5 , pp. 805-818
    • Chen, C.1    Zhang, C.2    Guo, P.3
  • 96
    • 0028966682 scopus 로고
    • Circularly permuted viral pRNA active and specific in the packaging of bacteriophage Phi29 DNA
    • Zhang CL, Trottier M, Guo PX. Circularly permuted viral pRNA active and specific in the packaging of bacteriophage Phi29 DNA. Virology 207, 442-451 (1995).
    • (1995) Virology , vol.207 , pp. 442-451
    • Zhang, C.L.1    Trottier, M.2    Guo, P.X.3
  • 97
    • 0032111970 scopus 로고    scopus 로고
    • Function of hexameric RNA in packaging of bacteriophage phi29 DNA in vitro
    • Zhang F, Lemieux S, Wu X, et al. Function of hexameric RNA in packaging of bacteriophage phi29 DNA in vitro. Mol. Cell 2, 141-147 (1998).
    • (1998) Mol. Cell , vol.2 , pp. 141-147
    • Zhang, F.1    Lemieux, S.2    Wu, X.3
  • 98
    • 0032563227 scopus 로고    scopus 로고
    • Bacteriophage DNA packaging: RNA gears in a DNA transport machine (minireview)
    • Hendrix RW. Bacteriophage DNA packaging: RNA gears in a DNA transport machine (minireview). Cell 94, 147-150 (1998).
    • (1998) Cell , vol.94 , pp. 147-150
    • Hendrix, R.W.1
  • 99
    • 0036761372 scopus 로고    scopus 로고
    • Implication of the prohead RNA in phage phi29 DNA packaging
    • Bourassa N, Major F. Implication of the prohead RNA in phage phi29 DNA packaging. Biochimie 84, 945-951 (2002).
    • (2002) Biochimie , vol.84 , pp. 945-951
    • Bourassa, N.1    Major, F.2
  • 100
    • 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. Novel mechanism of hexamer ring assembly in protein/RNA interactions revealed by single molecule imaging. Nucleic Acids Res. 36, 6620-6632 (2008).
    • (2008) Nucleic Acids Res. , vol.36 , pp. 6620-6632
    • Xiao, F.1    Zhang, H.2    Guo, P.3
  • 101
    • 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. Grouping of ferritin and gold nanoparticles conjugated to pRNA of the Phage phi29 DNA-packaging motor. J. Nanosci. Nanotech. (JNN) 7, 3257-3267 (2007).
    • (2007) J. Nanosci. Nanotech. (JNN , vol.7 , pp. 3257-3267
    • Moll, D.1    Guo, P.2
  • 103
    • 77955866886 scopus 로고    scopus 로고
    • Assembly mechanism of the sixty-subunit nanoparticles via interaction of RNA with the reengineered protein connector of phi29 DNA-packaging motor
    • Xiao F, Demeler B, Guo P. Assembly mechanism of the sixty-subunit nanoparticles via interaction of RNA with the reengineered protein connector of phi29 DNA-packaging motor. ACS Nano. 4(6), 3293-3301 (2010).
    • (2010) ACS Nano. , vol.4 , Issue.6 , pp. 3293-3301
    • Xiao, F.1    Demeler, B.2    Guo, P.3
  • 104
    • 21644486473 scopus 로고    scopus 로고
    • The procapsid binding domain of phi29 packaging RNA has a modular architecture and requires 2-hydroxyl groups in packaging RNA interaction
    • Fang Y, Cai Q, Qin PZ. The procapsid binding domain of phi29 packaging RNA has a modular architecture and requires 2-hydroxyl groups in packaging RNA interaction. Biochemistry 44, 9348-9358 (2005).
    • (2005) Biochemistry , vol.44 , pp. 9348-9358
    • Fang, Y.1    Cai, Q.2    Qin, P.Z.3
  • 105
    • 0034625371 scopus 로고    scopus 로고
    • A dimer as a building block in assembling RNA: A hexamer that gears bacterial virus phi29 DNA-Translocating machinery
    • Chen C, Sheng S, Shao Z, Guo P. A dimer as a building block in assembling RNA: a hexamer that gears bacterial virus phi29 DNA-Translocating machinery. J. Biol. Chem. 275(23), 17510-17516 (2000).
    • (2000) J. Biol. Chem. , vol.275 , Issue.23 , pp. 17510-17516
    • Chen, C.1    Sheng, S.2    Shao, Z.3    Guo, P.4
  • 106
    • 0028978266 scopus 로고
    • Inhibition of phage phi29 assembly by antisense oligonucleotides targeting viral pRNA essential for DNA packaging
    • Zhang CL, Garver K, Guo P. Inhibition of phage phi29 assembly by antisense oligonucleotides targeting viral pRNA essential for DNA packaging. Virology 211, 568-576 (1995).
    • (1995) Virology , vol.211 , pp. 568-576
    • Zhang, C.L.1    Garver, K.2    Guo, P.3
  • 107
    • 35948947822 scopus 로고    scopus 로고
    • Aaa+ atpases achieving diversity of function with conserved machinery
    • White SR, Lauring B. AAA+ ATPases: achieving diversity of function with conserved machinery. Traffic 8(12), 1657-1667 (2007).
    • (2007) Traffic , vol.8 , Issue.12 , pp. 1657-1667
    • White, S.R.1    Lauring, B.2
  • 108
    • 1642325936 scopus 로고    scopus 로고
    • Evolutionary history and higher order classification of AAA plus ATPases
    • Iyer LM, Leipe DD, Koonin EV, Aravind L. Evolutionary history and higher order classification of AAA plus ATPases. J. Struct. Biol. 146(1-2), 11-31 (2004).
    • (2004) J. Struct. Biol. , vol.146 , Issue.1-2 , pp. 11-31
    • Iyer, L.M.1    Leipe, D.D.2    Koonin, E.V.3    Aravind, L.4
  • 109
    • 0035261353 scopus 로고    scopus 로고
    • Interplay between AAUAAA and the trans-splice site in processing of a Caenorhabditis elegans operon pre-mRNA
    • Liu Y, Huang T, MacMorris M, Blumenthal T. Interplay between AAUAAA and the trans-splice site in processing of a Caenorhabditis elegans operon pre-mRNA. RNA 7(2), 176-181 (2001).
    • (2001) RNA , vol.7 , Issue.2 , pp. 176-181
    • Liu, Y.1    Huang, T.2    MacMorris, M.3    Blumenthal, T.4


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