메뉴 건너뛰기




Volumn 4, Issue 1, 2014, Pages

Nanobiomotors of archaeal DNA repair machineries: Current research status and application potential

Author keywords

Archaea; DNA repair; Helicase; Nanobiomotor; RecA fold

Indexed keywords


EID: 84902947823     PISSN: None     EISSN: 20453701     Source Type: Journal    
DOI: 10.1186/2045-3701-4-32     Document Type: Review
Times cited : (9)

References (89)
  • 1
    • 84867422454 scopus 로고    scopus 로고
    • Proof of concept for next-generation nanoparticle drugs in humans
    • Sheridan C. Proof of concept for next-generation nanoparticle drugs in humans. Nat Biotechnol 2012, 30(6):471-473.
    • (2012) Nat Biotechnol , vol.30 , Issue.6 , pp. 471-473
    • Sheridan, C.1
  • 2
    • 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 2013, 8(9):1635-1659.
    • (2013) Nat Protoc , vol.8 , Issue.9 , pp. 1635-1659
    • Shu, Y.1    Shu, D.2    Haque, F.3    Guo, P.4
  • 3
    • 0025300402 scopus 로고
    • Towards a natural system of organisms: proposal for the domains Archaea, Bacteria, and Eucarya
    • Woese CR, Kandler O, Wheelis ML. Towards a natural system of organisms: proposal for the domains Archaea, Bacteria, and Eucarya. Proc Natl Acad Sci U S A 1990, 87(12):4576-4579.
    • (1990) Proc Natl Acad Sci U S A , vol.87 , Issue.12 , pp. 4576-4579
    • Woese, C.R.1    Kandler, O.2    Wheelis, M.L.3
  • 4
    • 27844542206 scopus 로고    scopus 로고
    • Archaeal DNA replication and repair
    • Kelman Z, White MF. Archaeal DNA replication and repair. Curr Opin Microbiol 2005, 8(6):669-676.
    • (2005) Curr Opin Microbiol , vol.8 , Issue.6 , pp. 669-676
    • Kelman, Z.1    White, M.F.2
  • 5
    • 0032102006 scopus 로고    scopus 로고
    • Transcription and translation in Archaea: a mosaic of eukaryal and bacterial features
    • Bell SD, Jackson SP. Transcription and translation in Archaea: a mosaic of eukaryal and bacterial features. Trends Microbiol 1998, 6(6):222-228.
    • (1998) Trends Microbiol , vol.6 , Issue.6 , pp. 222-228
    • Bell, S.D.1    Jackson, S.P.2
  • 6
    • 79551489593 scopus 로고    scopus 로고
    • Homologous recombination in the archaea: the means justify the ends
    • White MF. Homologous recombination in the archaea: the means justify the ends. Biochem Soc Trans 2011, 39(1):15-19.
    • (2011) Biochem Soc Trans , vol.39 , Issue.1 , pp. 15-19
    • White, M.F.1
  • 8
    • 77951248354 scopus 로고    scopus 로고
    • The XBP-Bax1 helicase-nuclease complex unwinds and cleaves DNA: implications for eukaryal and archaeal nucleotide excision repair
    • Rouillon C, White MF. The XBP-Bax1 helicase-nuclease complex unwinds and cleaves DNA: implications for eukaryal and archaeal nucleotide excision repair. J Biol Chem 2010, 285(14):11013-11022.
    • (2010) J Biol Chem , vol.285 , Issue.14 , pp. 11013-11022
    • Rouillon, C.1    White, M.F.2
  • 9
    • 78650579621 scopus 로고    scopus 로고
    • Genetic analysis of DNA repair in the hyperthermophilic archaeon. Thermococcus kodakaraensis
    • Fujikane R, Ishino S, Ishino Y, Forterre P. Genetic analysis of DNA repair in the hyperthermophilic archaeon. Thermococcus kodakaraensis. Genes Genet Syst 2010, 85(4):243-257.
    • (2010) Genes Genet Syst , vol.85 , Issue.4 , pp. 243-257
    • Fujikane, R.1    Ishino, S.2    Ishino, Y.3    Forterre, P.4
  • 10
    • 84873108850 scopus 로고    scopus 로고
    • Genetic manipulation in Sulfolobus islandicus and functional analysis of DNA repair genes
    • Zhang C, Tian B, Li S, Ao X, Dalgaard K, Gokce S, Liang Y, She Q. Genetic manipulation in Sulfolobus islandicus and functional analysis of DNA repair genes. Biochem Soc Trans 2013, 41(1):405-410.
    • (2013) Biochem Soc Trans , vol.41 , Issue.1 , pp. 405-410
    • Zhang, C.1    Tian, B.2    Li, S.3    Ao, X.4    Dalgaard, K.5    Gokce, S.6    Liang, Y.7    She, Q.8
  • 11
    • 84861457511 scopus 로고    scopus 로고
    • TFIIH: when transcription met DNA repair
    • Compe E, Egly JM. TFIIH: when transcription met DNA repair. Nat Rev Mol Cell Biol 2012, 13(6):343-354.
    • (2012) Nat Rev Mol Cell Biol , vol.13 , Issue.6 , pp. 343-354
    • Compe, E.1    Egly, J.M.2
  • 13
    • 53649104599 scopus 로고    scopus 로고
    • Sae2, Exo1 and Sgs1 collaborate in DNA double-strand break processing
    • Mimitou EP, Symington LS. Sae2, Exo1 and Sgs1 collaborate in DNA double-strand break processing. Nature 2008, 455(7214):770-774.
    • (2008) Nature , vol.455 , Issue.7214 , pp. 770-774
    • Mimitou, E.P.1    Symington, L.S.2
  • 17
    • 59749105974 scopus 로고    scopus 로고
    • RecA family proteins in archaea: RadA and its cousins
    • Haldenby S, White MF, Allers T. RecA family proteins in archaea: RadA and its cousins. Biochem Soc Trans 2009, 37(Pt 1):102-107.
    • (2009) Biochem Soc Trans , vol.37 , Issue.PART 1 , pp. 102-107
    • Haldenby, S.1    White, M.F.2    Allers, T.3
  • 18
    • 38049173021 scopus 로고    scopus 로고
    • Homologous recombination in DNA repair and DNA damage tolerance
    • Li X, Heyer WD. Homologous recombination in DNA repair and DNA damage tolerance. Cell Res 2008, 18(1):99-113.
    • (2008) Cell Res , vol.18 , Issue.1 , pp. 99-113
    • Li, X.1    Heyer, W.D.2
  • 19
    • 33644631729 scopus 로고    scopus 로고
    • Mechanisms of maintaining genetic stability by homologous recombination
    • Ishino Y, Nishino T, Morikawa K. Mechanisms of maintaining genetic stability by homologous recombination. Chem Rev 2006, 106(2):324-339.
    • (2006) Chem Rev , vol.106 , Issue.2 , pp. 324-339
    • Ishino, Y.1    Nishino, T.2    Morikawa, K.3
  • 21
    • 84872486501 scopus 로고    scopus 로고
    • Distinct functions of human RECQ helicases WRN and BLM in replication fork recovery and progression after hydroxyurea-induced stalling
    • Sidorova JM, Kehrli K, Mao F, Monnat R. Distinct functions of human RECQ helicases WRN and BLM in replication fork recovery and progression after hydroxyurea-induced stalling. DNA Repair (Amst) 2013, 12(2):128-139.
    • (2013) DNA Repair (Amst) , vol.12 , Issue.2 , pp. 128-139
    • Sidorova, J.M.1    Kehrli, K.2    Mao, F.3    Monnat, R.4
  • 22
    • 16844380971 scopus 로고    scopus 로고
    • Identification of a novel helicase activity unwinding branched DNAs from the hyperthermophilic archaeon. Pyrococcus furiosus
    • Fujikane R, Komori K, Shinagawa H, Ishino Y. Identification of a novel helicase activity unwinding branched DNAs from the hyperthermophilic archaeon. Pyrococcus furiosus. J Biol Chem 2005, 280(13):12351-12358.
    • (2005) J Biol Chem , vol.280 , Issue.13 , pp. 12351-12358
    • Fujikane, R.1    Komori, K.2    Shinagawa, H.3    Ishino, Y.4
  • 23
    • 41949135245 scopus 로고    scopus 로고
    • Hjm/Hel308A DNA helicase from Sulfolobus tokodaii promotes replication fork regression and interacts with Hjc endonuclease in vitro
    • Li Z, Lu S, Hou G, Ma X, Sheng D, Ni J, Shen Y. Hjm/Hel308A DNA helicase from Sulfolobus tokodaii promotes replication fork regression and interacts with Hjc endonuclease in vitro. J Bacteriol 2008, 190(8):3006-3017.
    • (2008) J Bacteriol , vol.190 , Issue.8 , pp. 3006-3017
    • Li, Z.1    Lu, S.2    Hou, G.3    Ma, X.4    Sheng, D.5    Ni, J.6    Shen, Y.7
  • 25
    • 33645988522 scopus 로고    scopus 로고
    • Conserved XPB core structure and motifs for DNA unwinding: implications for pathway selection of transcription or excision repair
    • Fan L, Arvai AS, Cooper PK, Iwai S, Hanaoka F, Tainer JA. Conserved XPB core structure and motifs for DNA unwinding: implications for pathway selection of transcription or excision repair. Mol Cell 2006, 22(1):27-37.
    • (2006) Mol Cell , vol.22 , Issue.1 , pp. 27-37
    • Fan, L.1    Arvai, A.S.2    Cooper, P.K.3    Iwai, S.4    Hanaoka, F.5    Tainer, J.A.6
  • 26
    • 44149094083 scopus 로고    scopus 로고
    • XPD helicase structures and activities: insights into the cancer and aging phenotypes from XPD mutations
    • Fan L, Fuss JO, Cheng QJ, Arvai AS, Hammel M, Roberts VA, Cooper PK, Tainer JA. XPD helicase structures and activities: insights into the cancer and aging phenotypes from XPD mutations. Cell 2008, 133(5):789-800.
    • (2008) Cell , vol.133 , Issue.5 , pp. 789-800
    • Fan, L.1    Fuss, J.O.2    Cheng, Q.J.3    Arvai, A.S.4    Hammel, M.5    Roberts, V.A.6    Cooper, P.K.7    Tainer, J.A.8
  • 27
    • 34548638261 scopus 로고    scopus 로고
    • Structure and mechanism of helicases and nucleic acid translocases
    • Singleton MR, Dillingham MS, Wigley DB. Structure and mechanism of helicases and nucleic acid translocases. Annu Rev Biochem 2007, 76:23-50.
    • (2007) Annu Rev Biochem , vol.76 , pp. 23-50
    • Singleton, M.R.1    Dillingham, M.S.2    Wigley, D.B.3
  • 28
    • 78751572692 scopus 로고    scopus 로고
    • The evolution and mechanisms of nucleotide excision repair proteins
    • Rouillon C, White MF. The evolution and mechanisms of nucleotide excision repair proteins. Res Microbiol 2011, 162(1):19-26.
    • (2011) Res Microbiol , vol.162 , Issue.1 , pp. 19-26
    • Rouillon, C.1    White, M.F.2
  • 29
    • 0032518490 scopus 로고    scopus 로고
    • Hepatitis C virus NS3 RNA helicase domain with a bound oligonucleotide: the crystal structure provides insights into the mode of unwinding
    • Kim JL, Morgenstern KA, Griffith JP, Dwyer MD, Thomson JA, Murcko MA, Lin C, Caron PR. Hepatitis C virus NS3 RNA helicase domain with a bound oligonucleotide: the crystal structure provides insights into the mode of unwinding. Structure 1998, 6(1):89-100.
    • (1998) Structure , vol.6 , Issue.1 , pp. 89-100
    • Kim, J.L.1    Morgenstern, K.A.2    Griffith, J.P.3    Dwyer, M.D.4    Thomson, J.A.5    Murcko, M.A.6    Lin, C.7    Caron, P.R.8
  • 30
    • 79960377998 scopus 로고    scopus 로고
    • XPB and XPD helicases in TFIIH orchestrate DNA duplex opening and damage verification to coordinate repair with transcription and cell cycle via CAK kinase
    • Fuss JO, Tainer JA. XPB and XPD helicases in TFIIH orchestrate DNA duplex opening and damage verification to coordinate repair with transcription and cell cycle via CAK kinase. DNA Repair (Amst) 2011, 10(7):697-713.
    • (2011) DNA Repair (Amst) , vol.10 , Issue.7 , pp. 697-713
    • Fuss, J.O.1    Tainer, J.A.2
  • 31
    • 84857195289 scopus 로고    scopus 로고
    • Functional and structural studies of the nucleotide excision repair helicase XPD suggest a polarity for DNA translocation
    • Kuper J, Wolski SC, Michels G, Kisker C. Functional and structural studies of the nucleotide excision repair helicase XPD suggest a polarity for DNA translocation. EMBO J 2012, 31(2):494-502.
    • (2012) EMBO J , vol.31 , Issue.2 , pp. 494-502
    • Kuper, J.1    Wolski, S.C.2    Michels, G.3    Kisker, C.4
  • 32
    • 21444447661 scopus 로고    scopus 로고
    • Archaeal Hel308 helicase targets replication forks in vivo and in vitro and unwinds lagging strands
    • Guy CP, Bolt EL. Archaeal Hel308 helicase targets replication forks in vivo and in vitro and unwinds lagging strands. Nucleic Acids Res 2005, 33(11):3678-3690.
    • (2005) Nucleic Acids Res , vol.33 , Issue.11 , pp. 3678-3690
    • Guy, C.P.1    Bolt, E.L.2
  • 33
    • 84855826963 scopus 로고    scopus 로고
    • Dissection of the functional domains of an archaeal Holliday junction helicase
    • Hong Y, Chu M, Li Y, Ni J, Sheng D, Hou G, She Q, Shen Y. Dissection of the functional domains of an archaeal Holliday junction helicase. DNA Repair (Amst) 2012, 11(2):102-111.
    • (2012) DNA Repair (Amst) , vol.11 , Issue.2 , pp. 102-111
    • Hong, Y.1    Chu, M.2    Li, Y.3    Ni, J.4    Sheng, D.5    Hou, G.6    She, Q.7    Shen, Y.8
  • 34
    • 34447132375 scopus 로고    scopus 로고
    • Structural basis for DNA duplex separation by a superfamily-2 helicase
    • Buttner K, Nehring S, Hopfner KP. Structural basis for DNA duplex separation by a superfamily-2 helicase. Nat Struct Mol Biol 2007, 14(7):647-652.
    • (2007) Nat Struct Mol Biol , vol.14 , Issue.7 , pp. 647-652
    • Buttner, K.1    Nehring, S.2    Hopfner, K.P.3
  • 37
    • 2442670846 scopus 로고    scopus 로고
    • A bipolar DNA helicase gene, herA, clusters with rad50, mre11 and nurA genes in thermophilic archaea
    • Constantinesco F, Forterre P, Koonin EV, Aravind L, Elie C. A bipolar DNA helicase gene, herA, clusters with rad50, mre11 and nurA genes in thermophilic archaea. Nucleic Acids Res 2004, 32(4):1439-1447.
    • (2004) Nucleic Acids Res , vol.32 , Issue.4 , pp. 1439-1447
    • Constantinesco, F.1    Forterre, P.2    Koonin, E.V.3    Aravind, L.4    Elie, C.5
  • 38
    • 39149101784 scopus 로고    scopus 로고
    • Archaeal DNA helicase HerA interacts with Mre11 homologue and unwinds blunt-ended double-stranded DNA and recombination intermediates
    • Zhang S, Wei T, Hou G, Zhang C, Liang P, Ni J, Sheng D, Shen Y. Archaeal DNA helicase HerA interacts with Mre11 homologue and unwinds blunt-ended double-stranded DNA and recombination intermediates. DNA Repair (Amst) 2008, 7(3):380-391.
    • (2008) DNA Repair (Amst) , vol.7 , Issue.3 , pp. 380-391
    • Zhang, S.1    Wei, T.2    Hou, G.3    Zhang, C.4    Liang, P.5    Ni, J.6    Sheng, D.7    Shen, Y.8
  • 39
    • 53549093050 scopus 로고    scopus 로고
    • The P. furiosus mre11/rad50 complex promotes 5' strand resection at a DNA double-strand break
    • Hopkins BB, Paull TT. The P. furiosus mre11/rad50 complex promotes 5' strand resection at a DNA double-strand break. Cell 2008, 135(2):250-260.
    • (2008) Cell , vol.135 , Issue.2 , pp. 250-260
    • Hopkins, B.B.1    Paull, T.T.2
  • 40
    • 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. 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 2004, 32(17):5260-5279.
    • (2004) Nucleic Acids Res , vol.32 , Issue.17 , pp. 5260-5279
    • Iyer, L.M.1    Makarova, K.S.2    Koonin, E.V.3    Aravind, L.4
  • 42
    • 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 2013, 7(5):4082-4092.
    • (2013) ACS Nano , vol.7 , Issue.5 , pp. 4082-4092
    • Zhao, Z.1    Khisamutdinov, E.2    Schwartz, C.3    Guo, P.4
  • 43
    • 84902925332 scopus 로고    scopus 로고
    • Viral and cellular SOS-related motor proteins: dsDNA translocation mechanisms with divergent functions
    • in press
    • Wolfe A, Phipps K, Tao WT. Viral and cellular SOS-related motor proteins: dsDNA translocation mechanisms with divergent functions. Cell Biosci 2014, in press.
    • (2014) Cell Biosci
    • Wolfe, A.1    Phipps, K.2    Tao, W.T.3
  • 44
    • 84901951285 scopus 로고    scopus 로고
    • Common mechanisms of DNA translocation motors in bacteria and viruses using one-way revolution mechanism without rotation
    • in press
    • Guo P, Zhao Z, Haak J, Wang S, Weitao T. Common mechanisms of DNA translocation motors in bacteria and viruses using one-way revolution mechanism without rotation. Biotechnol Adv 2014, in press.
    • (2014) Biotechnol Adv
    • Guo, P.1    Zhao, Z.2    Haak, J.3    Wang, S.4    Weitao, T.5
  • 45
    • 84899892055 scopus 로고    scopus 로고
    • Biophysical Studies Reveal New Evidence for One-Way Revolution Mechanism of Bacteriophage phi29 DNA Packaging Motor
    • Guo P. Biophysical Studies Reveal New Evidence for One-Way Revolution Mechanism of Bacteriophage phi29 DNA Packaging Motor. Biophys J 2014, 106(8):1837-1838.
    • (2014) Biophys J , vol.106 , Issue.8 , pp. 1837-1838
    • Guo, P.1
  • 46
    • 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. Double-stranded DNA translocation: structure and mechanism of hexameric FtsK. Mol Cell 2006, 23(4):457-469.
    • (2006) Mol Cell , vol.23 , Issue.4 , pp. 457-469
    • Massey, T.H.1    Mercogliano, C.P.2    Yates, J.3    Sherratt, D.J.4    Lowe, J.5
  • 47
    • 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. Molecular mechanism of sequence-directed DNA loading and translocation by FtsK. Mol Cell 2008, 31(4):498-509.
    • (2008) Mol Cell , vol.31 , Issue.4 , pp. 498-509
    • Lowe, J.1    Ellonen, A.2    Allen, M.D.3    Atkinson, C.4    Sherratt, D.J.5    Grainge, I.6
  • 48
    • 78049300491 scopus 로고    scopus 로고
    • FtsK DNA translocase: the fast motor that knows where it's going
    • Crozat E, Grainge I. FtsK DNA translocase: the fast motor that knows where it's going. Chembiochem 2010, 11(16):2232-2243.
    • (2010) Chembiochem , vol.11 , Issue.16 , pp. 2232-2243
    • Crozat, E.1    Grainge, I.2
  • 49
    • 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 2010, 10(9):3620-3627.
    • (2010) Nano Lett , vol.10 , Issue.9 , pp. 3620-3627
    • Jing, P.1    Haque, F.2    Shu, D.3    Montemagno, C.4    Guo, P.5
  • 50
    • 84855423787 scopus 로고    scopus 로고
    • Role of channel lysines and the "push through a one-way valve" mechanism of the viral DNA packaging motor
    • Fang H, Jing P, Haque F, Guo P. Role of channel lysines and the "push through a one-way valve" mechanism of the viral DNA packaging motor. Biophys J 2012, 102(1):127-135.
    • (2012) Biophys J , vol.102 , Issue.1 , pp. 127-135
    • Fang, H.1    Jing, P.2    Haque, F.3    Guo, P.4
  • 51
    • 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 2013, 443(1):28-39.
    • (2013) Virology , vol.443 , Issue.1 , pp. 28-39
    • Schwartz, C.1    De Donatis, G.M.2    Zhang, H.3    Fang, H.4    Guo, P.5
  • 52
    • 84880948085 scopus 로고    scopus 로고
    • Ultrastable pRNA hexameric ring gearing hexameric phi29 DNA-packaging motor by revolving without rotating and coiling
    • Schwartz C, Guo P. Ultrastable pRNA hexameric ring gearing hexameric phi29 DNA-packaging motor by revolving without rotating and coiling. Curr Opin Biotechnol 2013, 24(4):581-590.
    • (2013) Curr Opin Biotechnol , vol.24 , Issue.4 , pp. 581-590
    • Schwartz, C.1    Guo, P.2
  • 53
    • 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 2013, 443(1):20-27.
    • (2013) Virology , vol.443 , Issue.1 , pp. 20-27
    • Schwartz, C.1    De Donatis, G.M.2    Fang, H.3    Guo, P.4
  • 54
    • 84896522348 scopus 로고    scopus 로고
    • Elastic properties and heterogeneous stiffness of the phi29 motor connector channel
    • Kumar R, Grubmuller H. Elastic properties and heterogeneous stiffness of the phi29 motor connector channel. Biophys J 2014, 106(6):1338-1348.
    • (2014) Biophys J , vol.106 , Issue.6 , pp. 1338-1348
    • Kumar, R.1    Grubmuller, H.2
  • 55
    • 84902546969 scopus 로고    scopus 로고
    • Finding of widespread viral and bacterial revolution dsDNA translocation motors distinct from rotation motors by channel chirality and size
    • in press
    • De-Donatis GM, Zhao Z, Wang S, Huang LP, Schwartz C, Tsodikov OV, Zhang H, Haque F, Guo P. Finding of widespread viral and bacterial revolution dsDNA translocation motors distinct from rotation motors by channel chirality and size. Cell Biosci 2014, in press.
    • (2014) Cell Biosci
    • De-Donatis, G.M.1    Zhao, Z.2    Wang, S.3    Huang, L.P.4    Schwartz, C.5    Tsodikov, O.V.6    Zhang, H.7    Haque, F.8    Guo, P.9
  • 56
    • 16844376846 scopus 로고    scopus 로고
    • Bacterial virus phi29 DNA-packaging motor and its potential applications in gene therapy and nanotechnology
    • Guo P. Bacterial virus phi29 DNA-packaging motor and its potential applications in gene therapy and nanotechnology. Methods Mol Biol 2005, 300:285-324.
    • (2005) Methods Mol Biol , vol.300 , pp. 285-324
    • Guo, P.1
  • 58
    • 0032079749 scopus 로고    scopus 로고
    • RadA protein is an archaeal RecA protein homolog that catalyzes DNA strand exchange
    • Seitz EM, Brockman JP, Sandler SJ, Clark AJ, Kowalczykowski SC. RadA protein is an archaeal RecA protein homolog that catalyzes DNA strand exchange. Genes Dev 1998, 12(9):1248-1253.
    • (1998) Genes Dev , vol.12 , Issue.9 , pp. 1248-1253
    • Seitz, E.M.1    Brockman, J.P.2    Sandler, S.J.3    Clark, A.J.4    Kowalczykowski, S.C.5
  • 59
    • 0034721873 scopus 로고    scopus 로고
    • Domain analysis of an archaeal RadA protein for the strand exchange activity
    • Komori K, Miyata T, Daiyasu H, Toh H, Shinagawa H, Ishino a Y. Domain analysis of an archaeal RadA protein for the strand exchange activity. J Biol Chem 2000, 275(43):33791-33797.
    • (2000) J Biol Chem , vol.275 , Issue.43 , pp. 33791-33797
    • Komori, K.1    Miyata, T.2    Daiyasu, H.3    Toh, H.4    Shinagawa, H.5    Ishino a, Y.6
  • 60
    • 0026500416 scopus 로고
    • The structure of the E. coli recA protein monomer and polymer
    • Story RM, Weber IT, Steitz TA. The structure of the E. coli recA protein monomer and polymer. Nature 1992, 355(6358):318-325.
    • (1992) Nature , vol.355 , Issue.6358 , pp. 318-325
    • Story, R.M.1    Weber, I.T.2    Steitz, T.A.3
  • 61
    • 4143068081 scopus 로고    scopus 로고
    • Crystal structure of archaeal recombinase RADA: a snapshot of its extended conformation
    • Wu Y, He Y, Moya IA, Qian X, Luo Y. Crystal structure of archaeal recombinase RADA: a snapshot of its extended conformation. Mol Cell 2004, 15(3):423-435.
    • (2004) Mol Cell , vol.15 , Issue.3 , pp. 423-435
    • Wu, Y.1    He, Y.2    Moya, I.A.3    Qian, X.4    Luo, Y.5
  • 64
    • 14844355639 scopus 로고    scopus 로고
    • Conformational flexibility revealed by the crystal structure of a crenarchaeal RadA
    • Ariza A, Richard DJ, White MF, Bond CS. Conformational flexibility revealed by the crystal structure of a crenarchaeal RadA. Nucleic Acids Res 2005, 33(5):1465-1473.
    • (2005) Nucleic Acids Res , vol.33 , Issue.5 , pp. 1465-1473
    • Ariza, A.1    Richard, D.J.2    White, M.F.3    Bond, C.S.4
  • 65
    • 27144526413 scopus 로고    scopus 로고
    • Crystal structure of Methanococcus voltae RadA in complex with ADP: hydrolysis-induced conformational change
    • Qian X, Wu Y, He Y, Luo Y. Crystal structure of Methanococcus voltae RadA in complex with ADP: hydrolysis-induced conformational change. Biochemistry 2005, 44(42):13753-13761.
    • (2005) Biochemistry , vol.44 , Issue.42 , pp. 13753-13761
    • Qian, X.1    Wu, Y.2    He, Y.3    Luo, Y.4
  • 66
    • 84877840212 scopus 로고    scopus 로고
    • An archaeal RadA paralog influences presynaptic filament formation
    • Graham WJ, Rolfsmeier ML, Haseltine CA. An archaeal RadA paralog influences presynaptic filament formation. DNA Repair (Amst) 2013, 12(6):403-413.
    • (2013) DNA Repair (Amst) , vol.12 , Issue.6 , pp. 403-413
    • Graham, W.J.1    Rolfsmeier, M.L.2    Haseltine, C.A.3
  • 67
    • 44349162159 scopus 로고    scopus 로고
    • Mechanism of homologous recombination from the RecA-ssDNA/dsDNA structures
    • Chen Z, Yang H, Pavletich NP. Mechanism of homologous recombination from the RecA-ssDNA/dsDNA structures. Nature 2008, 453(7194):489-484.
    • (2008) Nature , vol.453 , Issue.7194 , pp. 489-1484
    • Chen, Z.1    Yang, H.2    Pavletich, N.P.3
  • 68
    • 3042791448 scopus 로고    scopus 로고
    • Ca2+ activates human homologous recombination protein Rad51 by modulating its ATPase activity
    • Bugreev DV, Mazin AV. Ca2+ activates human homologous recombination protein Rad51 by modulating its ATPase activity. Proc Natl Acad Sci U S A 2004, 101(27):9988-9993.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , Issue.27 , pp. 9988-9993
    • Bugreev, D.V.1    Mazin, A.V.2
  • 69
    • 22844432495 scopus 로고    scopus 로고
    • Activation of human meiosis-specific recombinase Dmc1 by Ca2+
    • Bugreev DV, Golub EI, Stasiak AZ, Stasiak A, Mazin AV. Activation of human meiosis-specific recombinase Dmc1 by Ca2+. J Biol Chem 2005, 280(29):26886-26895.
    • (2005) J Biol Chem , vol.280 , Issue.29 , pp. 26886-26895
    • Bugreev, D.V.1    Golub, E.I.2    Stasiak, A.Z.3    Stasiak, A.4    Mazin, A.V.5
  • 70
    • 28844505344 scopus 로고    scopus 로고
    • Calcium ion promotes yeast Dmc1 activity via formation of long and fine helical filaments with single-stranded DNA
    • Lee MH, Chang YC, Hong EL, Grubb J, Chang CS, Bishop DK, Wang TF. Calcium ion promotes yeast Dmc1 activity via formation of long and fine helical filaments with single-stranded DNA. J Biol Chem 2005, 280(49):40980-40984.
    • (2005) J Biol Chem , vol.280 , Issue.49 , pp. 40980-40984
    • Lee, M.H.1    Chang, Y.C.2    Hong, E.L.3    Grubb, J.4    Chang, C.S.5    Bishop, D.K.6    Wang, T.F.7
  • 72
    • 33845968081 scopus 로고    scopus 로고
    • Calcium stiffens archaeal Rad51 recombinase from Methanococcus voltae for homologous recombination
    • Qian X, He Y, Ma X, Fodje MN, Grochulski P, Luo Y. Calcium stiffens archaeal Rad51 recombinase from Methanococcus voltae for homologous recombination. J Biol Chem 2006, 281(51):39380-39387.
    • (2006) J Biol Chem , vol.281 , Issue.51 , pp. 39380-39387
    • Qian, X.1    He, Y.2    Ma, X.3    Fodje, M.N.4    Grochulski, P.5    Luo, Y.6
  • 73
    • 12844272179 scopus 로고    scopus 로고
    • Crystal structure of an ATPase-active form of Rad51 homolog from Methanococcus voltae. Insights into potassium dependence
    • Wu Y, Qian X, He Y, Moya IA, Luo Y. Crystal structure of an ATPase-active form of Rad51 homolog from Methanococcus voltae. Insights into potassium dependence. J Biol Chem 2005, 280(1):722-728.
    • (2005) J Biol Chem , vol.280 , Issue.1 , pp. 722-728
    • Wu, Y.1    Qian, X.2    He, Y.3    Moya, I.A.4    Luo, Y.5
  • 74
    • 34247869930 scopus 로고    scopus 로고
    • Crystal structure of the left-handed archaeal RadA helical filament: identification of a functional motif for controlling quaternary structures and enzymatic functions of RecA family proteins
    • Chen LT, Ko TP, Chang YC, Lin KA, Chang CS, Wang AH, Wang TF. Crystal structure of the left-handed archaeal RadA helical filament: identification of a functional motif for controlling quaternary structures and enzymatic functions of RecA family proteins. Nucleic Acids Res 2007, 35(6):1787-1801.
    • (2007) Nucleic Acids Res , vol.35 , Issue.6 , pp. 1787-1801
    • Chen, L.T.1    Ko, T.P.2    Chang, Y.C.3    Lin, K.A.4    Chang, C.S.5    Wang, A.H.6    Wang, T.F.7
  • 75
    • 38049046713 scopus 로고    scopus 로고
    • Right or left turn? RecA family protein filaments promote homologous recombination through clockwise axial rotation
    • Wang TF, Chen LT, Wang AH. Right or left turn? RecA family protein filaments promote homologous recombination through clockwise axial rotation. Bioessays 2008, 30(1):48-56.
    • (2008) Bioessays , vol.30 , Issue.1 , pp. 48-56
    • Wang, T.F.1    Chen, L.T.2    Wang, A.H.3
  • 76
    • 38049024946 scopus 로고    scopus 로고
    • Structural and functional analyses of five conserved positively charged residues in the L1 and N-terminal DNA binding motifs of archaeal RADA protein
    • Chen LT, Ko TP, Chang YW, Lin KA, Wang AH, Wang TF. Structural and functional analyses of five conserved positively charged residues in the L1 and N-terminal DNA binding motifs of archaeal RADA protein. PLoS One 2007, 2(9):e858.
    • (2007) PLoS One , vol.2 , Issue.9
    • Chen, L.T.1    Ko, T.P.2    Chang, Y.W.3    Lin, K.A.4    Wang, A.H.5    Wang, T.F.6
  • 78
    • 20444447742 scopus 로고    scopus 로고
    • Structure of RadB recombinase from a hyperthermophilic archaeon, Thermococcus kodakaraensis KOD1: an implication for the formation of a near-7-fold helical assembly
    • Akiba T, Ishii N, Rashid N, Morikawa M, Imanaka T, Harata K. Structure of RadB recombinase from a hyperthermophilic archaeon, Thermococcus kodakaraensis KOD1: an implication for the formation of a near-7-fold helical assembly. Nucleic Acids Res 2005, 33(10):3412-3423.
    • (2005) Nucleic Acids Res , vol.33 , Issue.10 , pp. 3412-3423
    • Akiba, T.1    Ishii, N.2    Rashid, N.3    Morikawa, M.4    Imanaka, T.5    Harata, K.6
  • 79
    • 38049068811 scopus 로고    scopus 로고
    • The in vitro activity of a Rad55 homologue from Sulfolobus tokodaii, a candidate mediator in RadA-catalyzed homologous recombination
    • Sheng D, Zhu S, Wei T, Ni J, Shen Y. The in vitro activity of a Rad55 homologue from Sulfolobus tokodaii, a candidate mediator in RadA-catalyzed homologous recombination. Extremophiles 2008, 12(1):147-157.
    • (2008) Extremophiles , vol.12 , Issue.1 , pp. 147-157
    • Sheng, D.1    Zhu, S.2    Wei, T.3    Ni, J.4    Shen, Y.5
  • 80
    • 84862790777 scopus 로고    scopus 로고
    • Sulfolobus tokodaii RadA paralog, stRadC2, is involved in DNA recombination via interaction with RadA and Hjc
    • Wang L, Sheng D, Han W, Huang B, Zhu S, Ni J, Li J, Shen Y. Sulfolobus tokodaii RadA paralog, stRadC2, is involved in DNA recombination via interaction with RadA and Hjc. Sci China Life Sci 2012, 55(3):261-267.
    • (2012) Sci China Life Sci , vol.55 , Issue.3 , pp. 261-267
    • Wang, L.1    Sheng, D.2    Han, W.3    Huang, B.4    Zhu, S.5    Ni, J.6    Li, J.7    Shen, Y.8
  • 81
    • 84885955417 scopus 로고    scopus 로고
    • Knockouts of RecA-Like Proteins RadC1 and RadC2 Have Distinct Responses to DNA Damage Agents in Sulfolobus islandicus
    • Liang PJ, Han WY, Huang QH, Li YZ, Ni JF, She QX, Shen YL. Knockouts of RecA-Like Proteins RadC1 and RadC2 Have Distinct Responses to DNA Damage Agents in Sulfolobus islandicus. J Genet Genomics 2013, 40:533-541.
    • (2013) J Genet Genomics , vol.40 , pp. 533-541
    • Liang, P.J.1    Han, W.Y.2    Huang, Q.H.3    Li, Y.Z.4    Ni, J.F.5    She, Q.X.6    Shen, Y.L.7
  • 83
    • 66149160255 scopus 로고    scopus 로고
    • Crystal structure of KaiC-like protein PH0186 from hyperthermophilic archaea Pyrococcus horikoshii OT3
    • Kang HJ, Kubota K, Ming H, Miyazono K, Tanokura M. Crystal structure of KaiC-like protein PH0186 from hyperthermophilic archaea Pyrococcus horikoshii OT3. Proteins 2009, 75(4):1035-1039.
    • (2009) Proteins , vol.75 , Issue.4 , pp. 1035-1039
    • Kang, H.J.1    Kubota, K.2    Ming, H.3    Miyazono, K.4    Tanokura, M.5
  • 86
    • 79957936588 scopus 로고    scopus 로고
    • DNA nanotechnology. DNA nanotechnology grows up
    • 1143
    • Service RF. DNA nanotechnology. DNA nanotechnology grows up. Science 2011, 332(6034):1140-1141. 1143.
    • (2011) Science , vol.332 , Issue.6034 , pp. 1140-1141
    • Service, R.F.1
  • 87
    • 66149129286 scopus 로고    scopus 로고
    • From DNA nanotechnology to synthetic biology
    • Jungmann R, Renner S, Simmel FC. From DNA nanotechnology to synthetic biology. HFSP J 2008, 2(2):99-109.
    • (2008) HFSP J , vol.2 , Issue.2 , pp. 99-109
    • Jungmann, R.1    Renner, S.2    Simmel, F.C.3
  • 88
    • 80455154991 scopus 로고    scopus 로고
    • Thermodynamically stable RNA three-way junction for constructing multifunctional nanoparticles for delivery of therapeutics
    • Shu D, Shu Y, Haque F, Abdelmawla S, Guo P. Thermodynamically stable RNA three-way junction for constructing multifunctional nanoparticles for delivery of therapeutics. Nat Nanotechnol 2011, 6(10):658-667.
    • (2011) Nat Nanotechnol , vol.6 , Issue.10 , pp. 658-667
    • Shu, D.1    Shu, Y.2    Haque, F.3    Abdelmawla, S.4    Guo, P.5
  • 89
    • 84873352526 scopus 로고    scopus 로고
    • Incorporation of a viral DNA-packaging motor channel in lipid bilayers for real-time, single-molecule sensing of chemicals and double-stranded DNA
    • Haque F, Geng J, Montemagno C, Guo P. Incorporation of a viral DNA-packaging motor channel in lipid bilayers for real-time, single-molecule sensing of chemicals and double-stranded DNA. Nat Protoc 2013, 8(2):373-392.
    • (2013) Nat Protoc , vol.8 , Issue.2 , pp. 373-392
    • Haque, F.1    Geng, J.2    Montemagno, C.3    Guo, P.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.