메뉴 건너뛰기




Volumn 767, Issue , 2013, Pages 17-46

Erratum to: Structure and Mechanisms of SF1 DNA Helicases (Advances in Experimental Medicine and Biology), 10.1007/978-1-4614-5037-5_2;Structure and mechanisms of SF1 DNA helicases

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; DDA HELICASE; DOUBLE STRANDED DNA; HELICASE; NUCLEIC ACID BINDING PROTEIN; NUCLEOSIDE TRIPHOSPHATE; PCRA HELICASE; RECB HELICASE; RECBCD HELICASE; RECD HELICASE; RECD2 HELICASE; REP HELICASE; RNA POLYMERASE; RRM3 HELICASE; SF1 HELICASE; SF2 DNA HELICASE; SINGLE STRANDED DNA; UNCLASSIFIED DRUG; UVRD HELICASE; ADENOSINE TRIPHOSPHATASE; DNA HELICASE; PRCA HELICASE; SUPERFAMILY 1 DNA HELICASE; UNCLASSIFIED ENZYME;

EID: 84873632859     PISSN: 00652598     EISSN: 22148019     Source Type: Book Series    
DOI: 10.1007/978-1-4614-5037-5_14     Document Type: Erratum
Times cited : (61)

References (244)
  • 2
    • 0037294467 scopus 로고    scopus 로고
    • Helicase mechanisms and the coupling of helicases within macromolecular machines. Part II: Integration of helicases into cellular processes
    • Delagoutte E, von Hippel PH. Helicase mechanisms and the coupling of helicases within macromolecular machines. Part II: integration of helicases into cellular processes. Q Rev Biophys. 2003;36:1-69.
    • (2003) Q Rev Biophys , vol.36 , pp. 1-69
    • Delagoutte, E.1    Von Hippel, P.H.2
  • 4
    • 0026569419 scopus 로고
    • D-E-A-D protein family of putative RNA helicases
    • Schmid SR, Linder P. D-E-A-D protein family of putative RNA helicases. Mol Microbiol. 1992;6:283-91.
    • (1992) Mol Microbiol , vol.6 , pp. 283-291
    • Schmid, S.R.1    Linder, P.2
  • 5
    • 0027950513 scopus 로고
    • DNA helicases: Enzymes with essential roles in all aspects of DNA metabolism
    • Matson SW, Bean DW, George JW. DNA helicases: enzymes with essential roles in all aspects of DNA metabolism. Bioessays. 1994;16:13-22.
    • (1994) Bioessays , vol.16 , pp. 13-22
    • Matson, S.W.1    Bean, D.W.2    George, J.W.3
  • 6
    • 0032489015 scopus 로고    scopus 로고
    • The cell as a collection of protein machines: Preparing the next generation of molecular biologists
    • Alberts B. The cell as a collection of protein machines: preparing the next generation of molecular biologists. Cell. 1998;92:291-4.
    • (1998) Cell , vol.92 , pp. 291-294
    • Alberts, B.1
  • 8
    • 0037781588 scopus 로고    scopus 로고
    • Helicases of the DEAD-box family involved in translation initiation
    • Linder P, Yeast RNA. helicases of the DEAD-box family involved in translation initiation. Biol Cell. 2003;95:157-67.
    • (2003) Biol Cell , vol.95 , pp. 157-167
    • Linder, P.1    Yeast, R.N.A.2
  • 9
  • 10
    • 20444380748 scopus 로고    scopus 로고
    • Initiation of DNA replication requires the RECQL4 protein mutated in Rothmund-Thomson syndrome
    • Sangrithi MN, Bernal JA, Madine M, Philpott A, Lee J, Dunphy WG, et al. Initiation of DNA replication requires the RECQL4 protein mutated in Rothmund-Thomson syndrome. Cell. 2005;121:887-98.
    • (2005) Cell , vol.121 , pp. 887-898
    • Sangrithi, M.N.1    Bernal, J.A.2    Madine, M.3    Philpott, A.4    Lee, J.5    Dunphy, W.G.6
  • 12
    • 33745471225 scopus 로고    scopus 로고
    • The N-terminal noncatalytic region of Xenopus RecQ4 is required for chromatin binding of DNA polymerase alpha in the initiation of DNA replication
    • Matsuno K, Kumano M, Kubota Y, Hashimoto Y, Takisawa H. The N-terminal noncatalytic region of Xenopus RecQ4 is required for chromatin binding of DNA polymerase alpha in the initiation of DNA replication. Mol Cell Biol. 2006;26:4843-52.
    • (2006) Mol Cell Biol , vol.26 , pp. 4843-4852
    • Matsuno, K.1    Kumano, M.2    Kubota, Y.3    Hashimoto, Y.4    Takisawa, H.5
  • 13
    • 36849013079 scopus 로고    scopus 로고
    • RECQL5/Recql5 helicase regulates homologous recombination and suppresses tumor formation via disruption of Rad51 presynaptic fi laments
    • Hu Y, Raynard S, Sehorn MG, Lu X, Bussen W, Zheng L, et al. RECQL5/Recql5 helicase regulates homologous recombination and suppresses tumor formation via disruption of Rad51 presynaptic fi laments. Genes Dev. 2007;21:3073-84.
    • (2007) Genes Dev , vol.21 , pp. 3073-3084
    • Hu, Y.1    Raynard, S.2    Sehorn, M.G.3    Lu, X.4    Bussen, W.5    Zheng, L.6
  • 14
    • 0028564949 scopus 로고
    • Mismatch repair, genetic stability, and cancer
    • Modrich P. Mismatch repair, genetic stability, and cancer. Science. 1994;266:1959-60.
    • (1994) Science , vol.266 , pp. 1959-1960
    • Modrich, P.1
  • 15
    • 0028606403 scopus 로고
    • Mechanisms of DNA excision repair
    • Sancar A. Mechanisms of DNA excision repair. Science. 1994;266:1954-6.
    • (1994) Science , vol.266 , pp. 1954-1956
    • Sancar, A.1
  • 16
    • 34548700369 scopus 로고    scopus 로고
    • Nucleotide excision repair and its connection with cancer and ageing
    • Andressoo JO, Hoeijmakers JH, de Waard H. Nucleotide excision repair and its connection with cancer and ageing. Adv Exp Med Biol. 2005;570:45-83.
    • (2005) Adv Exp Med Biol , vol.570 , pp. 45-83
    • Andressoo, J.O.1    Hoeijmakers, J.H.2    De Waard, H.3
  • 17
    • 45449093552 scopus 로고    scopus 로고
    • The role of Cockayne syndrome group B (CSB) protein in base excision repair and aging
    • Stevnsner T, Muftuoglu M, Aamann MD, Bohr VA. The role of Cockayne syndrome group B (CSB) protein in base excision repair and aging. Mech Ageing Dev. 2008;129:441-8.
    • (2008) Mech Ageing Dev , vol.129 , pp. 441-448
    • Stevnsner, T.1    Muftuoglu, M.2    Aamann, M.D.3    Bohr, V.A.4
  • 18
    • 0030861685 scopus 로고    scopus 로고
    • DNA helicases in inherited human disorders
    • Ellis NA. DNA helicases in inherited human disorders. Curr Opin Genet Dev. 1997;7:354-63.
    • (1997) Curr Opin Genet Dev , vol.7 , pp. 354-363
    • Ellis, N.A.1
  • 19
    • 24044532209 scopus 로고    scopus 로고
    • Transcription-coupled repair and premature ageing
    • Andressoo JO, Hoeijmakers JH. Transcription-coupled repair and premature ageing. Mutat Res. 1997;577:179-94.
    • (1997) Mutat Res , vol.577 , pp. 179-194
    • Andressoo, J.O.1    Hoeijmakers, J.H.2
  • 20
    • 38049075962 scopus 로고    scopus 로고
    • Human premature aging DNA repair and RecQ helicases
    • Brosh Jr RM, Bohr VA. Human premature aging, DNA repair and RecQ helicases. Nucleic Acids Res. 2007;35:7527-44.
    • (2007) Nucleic Acids Res , vol.35 , pp. 7527-7544
    • Brosh Jr., R.M.1    Bohr, V.A.2
  • 21
    • 45449110194 scopus 로고    scopus 로고
    • Homologous recombination and maintenance of genome integrity: Cancer and aging through the prism of human RecQ helicases
    • Ouyang KJ, Woo LL, Ellis NA. Homologous recombination and maintenance of genome integrity: cancer and aging through the prism of human RecQ helicases. Mech Ageing Dev. 2008;129:425-40.
    • (2008) Mech Ageing Dev , vol.129 , pp. 425-440
    • Ouyang, K.J.1    Woo, L.L.2    Ellis, N.A.3
  • 22
    • 0028831333 scopus 로고
    • Bloom's syndrome
    • German J. Bloom's syndrome. Dermatol Clin. 1995;13:7-18.
    • (1995) Dermatol Clin , vol.13 , pp. 7-18
    • German, J.1
  • 23
    • 0032545515 scopus 로고    scopus 로고
    • Werner syndrome protein. I. DNA helicase and dna exonuclease reside on the same polypeptide
    • Shen JC, Gray MD, Oshima J, Kamath-Loeb AS, Fry M, Loeb LA. Werner syndrome protein. I. DNA helicase and dna exonuclease reside on the same polypeptide. J Biol Chem. 1998;273:34139-44.
    • (1998) J Biol Chem , vol.273 , pp. 34139-34144
    • Shen, J.C.1    Gray, M.D.2    Oshima, J.3    Kamath-Loeb, A.S.4    Fry, M.5    Loeb, L.A.6
  • 24
    • 0031255159 scopus 로고    scopus 로고
    • Mutations in transcriptional regulator ATRX establish the functional signi fi cance of a PHD-like domain
    • Gibbons RJ, Bachoo S, Picketts DJ, Aftimos S, Asenbauer B, Bergoffen J, et al. Mutations in transcriptional regulator ATRX establish the functional signi fi cance of a PHD-like domain. Nat Genet. 1997;17:146-8.
    • (1997) Nat Genet , vol.17 , pp. 146-148
    • Gibbons, R.J.1    Bachoo, S.2    Picketts, D.J.3    Aftimos, S.4    Asenbauer, B.5    Bergoffen, J.6
  • 25
    • 0035871341 scopus 로고    scopus 로고
    • Loss of Werner syndrome protein function promotes aberrant mitotic recombination
    • Prince PR, Emond MJ, Monnat Jr RJ. Loss of Werner syndrome protein function promotes aberrant mitotic recombination. Genes Dev. 2001;15:933-8.
    • (2001) Genes Dev , vol.15 , pp. 933-938
    • Prince, P.R.1    Emond, M.J.2    Monnat Jr., R.J.3
  • 27
    • 0037364415 scopus 로고    scopus 로고
    • RecQ helicases: Caretakers of the genome
    • Hickson ID. RecQ helicases: caretakers of the genome. Nat Rev Cancer. 2003;3:169-78.
    • (2003) Nat Rev Cancer , vol.3 , pp. 169-178
    • Hickson, I.D.1
  • 28
    • 33748744378 scopus 로고    scopus 로고
    • Mechanisms of RecQ helicases in pathways of DNA metabolism and maintenance of genomic stability
    • Sharma S, Doherty KM, Brosh Jr RM. Mechanisms of RecQ helicases in pathways of DNA metabolism and maintenance of genomic stability. Biochem J. 2006;398:319-37.
    • (2006) Biochem J , vol.398 , pp. 319-337
    • Sharma, S.1    Doherty, K.M.2    Brosh Jr., R.M.3
  • 29
    • 58149235463 scopus 로고    scopus 로고
    • Werner syndrome, aging and cancer
    • Ozgenc A, Loeb LA. Werner syndrome, aging and cancer. Genome Dyn. 2006;1:206-17.
    • (2006) Genome Dyn , vol.1 , pp. 206-217
    • Ozgenc, A.1    Loeb, L.A.2
  • 32
    • 2442658908 scopus 로고    scopus 로고
    • DNA/RNA helicase gene mutations in a form of juvenile amyotrophic lateral sclerosis (ALS4)
    • Chen YZ, Bennett CL, Huynh HM, Blair IP, Puls I, Irobi J, et al. DNA/RNA helicase gene mutations in a form of juvenile amyotrophic lateral sclerosis (ALS4). Am J Hum Genet. 2004;74:1128-35.
    • (2004) Am J Hum Genet , vol.74 , pp. 1128-1135
    • Chen, Y.Z.1    Bennett, C.L.2    Huynh, H.M.3    Blair, I.P.4    Puls, I.5    Irobi, J.6
  • 33
    • 10744230604 scopus 로고    scopus 로고
    • Senataxin, the ortholog of a yeast RNA helicase, is mutant in ataxia-ocular apraxia 2
    • Moreira MC, Klur S, Watanabe M, Nemeth AH, Le Ber I, Moniz JC, et al. Senataxin, the ortholog of a yeast RNA helicase, is mutant in ataxia-ocular apraxia 2. Nat Genet. 2004;36:225-7.
    • (2004) Nat Genet , vol.36 , pp. 225-227
    • Moreira, M.C.1    Klur, S.2    Watanabe, M.3    Nemeth, A.H.4    Le Ber, I.5    Moniz, J.C.6
  • 34
    • 63149150048 scopus 로고    scopus 로고
    • IGHMBP2 is a ribosome-associated helicase inactive in the neuromuscular disorder distal SMA type 1 (DSMA1)
    • Guenther UP, Handoko L, Laggerbauer B, Jablonka S, Chari A, Alzheimer M, et al. IGHMBP2 is a ribosome-associated helicase inactive in the neuromuscular disorder distal SMA type 1 (DSMA1). Hum Mol Genet. 2009;18:1288-300.
    • (2009) Hum Mol Genet , vol.18 , pp. 1288-1300
    • Guenther, U.P.1    Handoko, L.2    Laggerbauer, B.3    Jablonka, S.4    Chari, A.5    Alzheimer, M.6
  • 35
    • 17944374029 scopus 로고    scopus 로고
    • Mutations in the gene encoding immunoglobulin mu-binding protein 2 cause spinal muscular atrophy with respiratory distress type 1
    • Grohmann K, Schuelke M, Diers A, Hoffmann K, Lucke B, Adams C, et al. Mutations in the gene encoding immunoglobulin mu-binding protein 2 cause spinal muscular atrophy with respiratory distress type 1. Nat Genet. 2001;29:75-7.
    • (2001) Nat Genet , vol.29 , pp. 75-77
    • Grohmann, K.1    Schuelke, M.2    Diers, A.3    Hoffmann, K.4    Lucke, B.5    Adams, C.6
  • 36
    • 65349085023 scopus 로고    scopus 로고
    • Hitting the bull's eye: Novel directed cancer therapy through helicase-targeted synthetic lethality
    • Aggarwal M, Brosh Jr RM. Hitting the bull's eye: novel directed cancer therapy through helicase-targeted synthetic lethality. J Cell Biochem. 2009;106:758-63.
    • (2009) J Cell Biochem , vol.106 , pp. 758-763
    • Aggarwal, M.1    Brosh Jr., R.M.2
  • 37
    • 0033215473 scopus 로고    scopus 로고
    • Replication of herpes simplex virus DNA
    • Lehman IR, Boehmer PE. Replication of herpes simplex virus DNA. J Biol Chem. 1999;274:28059-62.
    • (1999) J Biol Chem , vol.274 , pp. 28059-28062
    • Lehman, I.R.1    Boehmer, P.E.2
  • 38
    • 0037315768 scopus 로고    scopus 로고
    • Novel agents and strategies to treat herpes simplex virus infections
    • Kleymann G. Novel agents and strategies to treat herpes simplex virus infections. Expert Opin Investig Drugs. 2003;12:165-83.
    • (2003) Expert Opin Investig Drugs , vol.12 , pp. 165-183
    • Kleymann, G.1
  • 39
    • 0345293206 scopus 로고    scopus 로고
    • New antiviral drugs that target herpesvirus helicase primase enzymes
    • Kleymann G. New antiviral drugs that target herpesvirus helicase primase enzymes. Herpes. 2003;10:46-52.
    • (2003) Herpes , vol.10 , pp. 46-52
    • Kleymann, G.1
  • 40
    • 0028817781 scopus 로고
    • C-terminal domain of the hepatitis C virus NS3 protein contains an RNA helicase activity
    • Kim DW, Gwack Y, Han JH, Choe J. C-terminal domain of the hepatitis C virus NS3 protein contains an RNA helicase activity. Biochem Biophys Res Commun. 1995;215:160-6.
    • (1995) Biochem Biophys Res Commun , vol.215 , pp. 160-166
    • Kim, D.W.1    Gwack, Y.2    Han, J.H.3    Choe, J.4
  • 41
    • 0037300878 scopus 로고    scopus 로고
    • New therapies on the horizon for hepatitis C: Are we close?
    • xi
    • De FR, Rice CM. New therapies on the horizon for hepatitis C: are we close? Clin Liver Dis. 2003;7:211-42, xi.
    • (2003) Clin Liver Dis , vol.7 , pp. 211-242
    • De, F.R.1    Rice, C.M.2
  • 42
    • 0034444554 scopus 로고    scopus 로고
    • Essential role for the Legionella pneumophila rep helicase homologue in intracellular infection of mammalian cells
    • Harb OS, Abu KY. Essential role for the Legionella pneumophila rep helicase homologue in intracellular infection of mammalian cells. Infect Immun. 2000;68:6970-8.
    • (2000) Infect Immun , vol.68 , pp. 6970-6978
    • Harb, O.S.1    Abu, K.Y.2
  • 43
    • 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
  • 45
    • 42449141601 scopus 로고    scopus 로고
    • Non-hexameric DNA helicases and translocases: Mechanisms and regulation
    • Lohman TM, Tomko EJ, Wu CG. Non-hexameric DNA helicases and translocases: mechanisms and regulation. Nat Rev Mol Cell Biol. 2008;9:391-401.
    • (2008) Nat Rev Mol Cell Biol , vol.9 , pp. 391-401
    • Lohman, T.M.1    Tomko, E.J.2    Wu, C.G.3
  • 46
    • 0024344173 scopus 로고
    • Two related superfamilies of putative helicases involved in replication, recombination, repair and expression of DNA and RNA genomes
    • Gorbalenya AE, Koonin EV, Donchenko AP, Blinov VM. Two related superfamilies of putative helicases involved in replication, recombination, repair and expression of DNA and RNA genomes. Nucleic Acids Res. 1989;17:4713-30.
    • (1989) Nucleic Acids Res , vol.17 , pp. 4713-4730
    • Gorbalenya, A.E.1    Koonin, E.V.2    Donchenko, A.P.3    Blinov, V.M.4
  • 47
    • 0027182114 scopus 로고
    • Helicases: Amino acid sequence comparisons and structurefunction relationships
    • Gorbalenya AE, Koonin EV. Helicases: amino acid sequence comparisons and structurefunction relationships. Curr Opin Struct Biol. 1993;3:419-29.
    • (1993) Curr Opin Struct Biol , vol.3 , pp. 419-429
    • Gorbalenya, A.E.1    Koonin, E.V.2
  • 48
    • 0036211179 scopus 로고    scopus 로고
    • Modularity and specialization in superfamily 1 and 2 helicases
    • Singleton MR, Wigley DB. Modularity and specialization in superfamily 1 and 2 helicases. J Bacteriol. 2002;184:1819-26.
    • (2002) J Bacteriol , vol.184 , pp. 1819-1826
    • Singleton, M.R.1    Wigley, D.B.2
  • 49
    • 0345492316 scopus 로고    scopus 로고
    • Macromolecular complexes that unwind nucleic acids
    • von Hippel PH, Delagoutte E. Macromolecular complexes that unwind nucleic acids. Bioessays. 2003;25:1168-77.
    • (2003) Bioessays , vol.25 , pp. 1168-1177
    • Von Hippel, P.H.1    Delagoutte, E.2
  • 50
    • 0035997356 scopus 로고    scopus 로고
    • ATP-dependent nucleosome remodeling
    • Becker PB, Horz W. ATP-dependent nucleosome remodeling. Annu Rev Biochem. 2002;71:247-73.
    • (2002) Annu Rev Biochem , vol.71 , pp. 247-273
    • Becker, P.B.1    Horz, W.2
  • 51
    • 0344198456 scopus 로고    scopus 로고
    • Chromatin remodeling by ATP-dependent molecular machines
    • Lusser A, Kadonaga JT. Chromatin remodeling by ATP-dependent molecular machines. Bioessays. 2003;25:1192-200.
    • (2003) Bioessays , vol.25 , pp. 1192-1200
    • Lusser, A.1    Kadonaga, J.T.2
  • 52
    • 27144460601 scopus 로고    scopus 로고
    • The human Rothmund-Thomson syndrome gene product, RECQL4, localizes to distinct nuclear foci that coincide with proteins involved in the maintenance of genome stability
    • Petkovic M, Dietschy T, Freire R, Jiao R, Stagljar I. The human Rothmund-Thomson syndrome gene product, RECQL4, localizes to distinct nuclear foci that coincide with proteins involved in the maintenance of genome stability. J Cell Sci. 2005;118:4261-9.
    • (2005) J Cell Sci , vol.118 , pp. 4261-4269
    • Petkovic, M.1    Dietschy, T.2    Freire, R.3    Jiao, R.4    Stagljar, I.5
  • 53
    • 40249083431 scopus 로고    scopus 로고
    • Human RECQ1 is a DNA damage responsive protein required for genotoxic stress resistance and suppression of sister chromatid exchanges
    • Sharma S, Brosh Jr RM. Human RECQ1 is a DNA damage responsive protein required for genotoxic stress resistance and suppression of sister chromatid exchanges. PLoS One. 2007;2:e1297.
    • (2007) PLoS One , vol.2
    • Sharma, S.1    Brosh Jr., R.M.2
  • 54
    • 77956379478 scopus 로고    scopus 로고
    • The chromatinremodeling factor CHD4 coordinates signaling and repair after DNA damage
    • Larsen DH, Poinsignon C, Gudjonsson T, Dinant C, Payne MR, Hari FJ, et al. The chromatinremodeling factor CHD4 coordinates signaling and repair after DNA damage. J Cell Biol. 2010;190:731-40.
    • (2010) J Cell Biol , Issue.190 , pp. 731-740
    • Larsen, D.H.1    Poinsignon, C.2    Gudjonsson, T.3    Dinant, C.4    Payne, M.R.5    Hari, F.J.6
  • 55
    • 33744927719 scopus 로고    scopus 로고
    • A double Holliday junction dissolvasome comprising BLM, topoisomerase IIIalpha, and BLAP75
    • Raynard S, Bussen W, Sung P. A double Holliday junction dissolvasome comprising BLM, topoisomerase IIIalpha, and BLAP75. J Biol Chem. 2006;281:13861-4.
    • (2006) J Biol Chem , vol.281 , pp. 13861-13864
    • Raynard, S.1    Bussen, W.2    Sung, P.3
  • 56
    • 33645242115 scopus 로고    scopus 로고
    • BLAP75/RMI1 promotes the BLMdependent dissolution of homologous recombination intermediates
    • Wu L, Bachrati CZ, Ou J, Xu C, Yin J, Chang M, et al. BLAP75/RMI1 promotes the BLMdependent dissolution of homologous recombination intermediates. Proc Natl Acad Sci U S A. 2006;103:4068-73.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 4068-4073
    • Wu, L.1    Bachrati, C.Z.2    Ou, J.3    Xu, C.4    Yin, J.5    Chang, M.6
  • 58
    • 54349114671 scopus 로고    scopus 로고
    • BLAP18/RMI2, a novel OB-fold-containing protein, is an essential component of the Bloom helicase-double Holliday junction dissolvasome
    • Singh TR, Ali AM, Busygina V, Raynard S, Fan Q, Du CH, et al. BLAP18/RMI2, a novel OB-fold-containing protein, is an essential component of the Bloom helicase-double Holliday junction dissolvasome. Genes Dev. 2008;22:2856-68.
    • (2008) Genes Dev , vol.22 , pp. 2856-2868
    • Singh, T.R.1    Ali, A.M.2    Busygina, V.3    Raynard, S.4    Fan, Q.5    Du, C.H.6
  • 59
    • 50649118135 scopus 로고    scopus 로고
    • RECQ1 possesses DNA branch migration activity
    • Bugreev DV, Brosh Jr RM, Mazin AV. RECQ1 possesses DNA branch migration activity. J Biol Chem. 2008;283:20231-42.
    • (2008) J Biol Chem , vol.283 , pp. 20231-20242
    • Bugreev, D.V.1    Brosh Jr., R.M.2    Mazin, A.V.3
  • 60
    • 79953147386 scopus 로고    scopus 로고
    • RTEL1: An essential helicase for telomere maintenance and the regulation of homologous recombination
    • Uringa EJ, Youds JL, Lisaingo K, Lansdorp PM, Boulton SJ. RTEL1: an essential helicase for telomere maintenance and the regulation of homologous recombination. Nucleic Acids Res. 2011;39:1647-55.
    • (2011) Nucleic Acids Res , vol.39 , pp. 1647-1655
    • Uringa, E.J.1    Youds, J.L.2    Lisaingo, K.3    Lansdorp, P.M.4    Boulton, S.J.5
  • 61
    • 0031807390 scopus 로고    scopus 로고
    • Comparison of the human and murine ATRX gene identi fi es highly conserved, functionally important domains
    • Picketts DJ, Tastan AO, Higgs DR, Gibbons RJ. Comparison of the human and murine ATRX gene identi fi es highly conserved, functionally important domains. Mamm Genome. 1998;9:400-3.
    • (1998) Mamm Genome , vol.9 , pp. 400-403
    • Picketts, D.J.1    Tastan, A.O.2    Higgs, D.R.3    Gibbons, R.J.4
  • 62
    • 0033598808 scopus 로고    scopus 로고
    • Chromatin modification by DNA tracking
    • Travers A. Chromatin modification by DNA tracking. Proc Natl Acad Sci USA. 1999;96:13634-7.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 13634-13637
    • Travers, A.1
  • 63
    • 0037334946 scopus 로고    scopus 로고
    • Rad54 protein possesses chromatin-remodeling activity stimulated by the Rad51-ssDNA nucleoprotein fi lament
    • Alexeev A, Mazin A, Kowalczykowski SC. Rad54 protein possesses chromatin-remodeling activity stimulated by the Rad51-ssDNA nucleoprotein fi lament. Nat Struct Biol. 2003;10:182-6.
    • (2003) Nat Struct Biol , vol.10 , pp. 182-186
    • Alexeev, A.1    Mazin, A.2    Kowalczykowski, S.C.3
  • 65
    • 70350351130 scopus 로고    scopus 로고
    • BLM helicase stimulates the ATPase and chromatin-remodeling activities of RAD54
    • Srivastava V, Modi P, Tripathi V, Mudgal R, De S, Sengupta S. BLM helicase stimulates the ATPase and chromatin-remodeling activities of RAD54. J Cell Sci. 2009;122:3093-103.
    • (2009) J Cell Sci , vol.122 , pp. 3093-3103
    • Srivastava, V.1    Modi, P.2    Tripathi, V.3    Mudgal, R.4    De S Sengupta, S.5
  • 66
    • 0026465665 scopus 로고
    • ERCC6, a member of a subfamily of putative helicases, is involved in Cockayne's syndrome and preferential repair of active genes
    • Troelstra C, van Gool A, de Wit J, Vermeulen W, Bootsma D, Hoeijmakers JH. ERCC6, a member of a subfamily of putative helicases, is involved in Cockayne's syndrome and preferential repair of active genes. Cell. 1992;71:939-53.
    • (1992) Cell , vol.71 , pp. 939-953
    • Troelstra, C.1    Van Gool, A.2    De Wit, J.3    Vermeulen, W.4    Bootsma, D.5    Hoeijmakers, J.H.6
  • 67
    • 0031013308 scopus 로고    scopus 로고
    • Open complex formation around a lesion during nucleotide excision repair provides a structure for cleavage by human XPG protein
    • Evans E, Fellows J, Coffer A, Wood RD. Open complex formation around a lesion during nucleotide excision repair provides a structure for cleavage by human XPG protein. EMBO J. 1997;16:625-38.
    • (1997) EMBO J , vol.16 , pp. 625-638
    • Evans, E.1    Fellows, J.2    Coffer, A.3    Wood, R.D.4
  • 68
    • 0032143062 scopus 로고    scopus 로고
    • Unraveling the role of helicases in transcription
    • Eisen A, Lucchesi JC. Unraveling the role of helicases in transcription. Bioessays. 1998;20:634-41.
    • (1998) Bioessays , vol.20 , pp. 634-641
    • Eisen, A.1    Lucchesi, J.C.2
  • 70
    • 33749134437 scopus 로고    scopus 로고
    • DExD/H box RNA helicases: Multifunctional proteins with important roles in transcriptional regulation
    • Fuller-Pace FV. DExD/H box RNA helicases: multifunctional proteins with important roles in transcriptional regulation. Nucleic Acids Res. 2008;34:4206-15.
    • (2008) Nucleic Acids Res , vol.34 , pp. 4206-4215
    • Fuller-Pace, F.V.1
  • 71
    • 47249100637 scopus 로고    scopus 로고
    • A RECQ5-RNA polymerase II association identi fi ed by targeted proteomic analysis of human chromatin
    • Aygun O, Svejstrup J, Liu Y. A RECQ5-RNA polymerase II association identi fi ed by targeted proteomic analysis of human chromatin. Proc Natl Acad Sci U S A. 2008;105:8580-4.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 8580-8584
    • Aygun, O.1    Svejstrup, J.2    Liu, Y.3
  • 72
    • 48249140331 scopus 로고    scopus 로고
    • Association of human DNA helicase RecQ5beta with RNA polymerase II and its possible role in transcription
    • Izumikawa K, Yanagida M, Hayano T, Tachikawa H, Komatsu W, Shimamoto A, et al. Association of human DNA helicase RecQ5beta with RNA polymerase II and its possible role in transcription. Biochem J. 2008;413:505-16.
    • (2008) Biochem J , vol.413 , pp. 505-516
    • Izumikawa, K.1    Yanagida, M.2    Hayano, T.3    Tachikawa, H.4    Komatsu, W.5    Shimamoto, A.6
  • 74
    • 0242407470 scopus 로고    scopus 로고
    • Purification and characterization of the PcrA helicase of Bacillus anthracis
    • Naqvi A, Tinsley E, Khan SA. Purification and characterization of the PcrA helicase of Bacillus anthracis. J Bacteriol. 2003;185:6633-9.
    • (2003) J Bacteriol , vol.185 , pp. 6633-6639
    • Naqvi, A.1    Tinsley, E.2    Khan, S.A.3
  • 75
    • 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;32:1439-47.
    • (2004) Nucleic Acids Res , vol.32 , pp. 1439-1447
    • Constantinesco, F.1    Forterre, P.2    Koonin, E.V.3    Aravind, L.4    Elie, C.5
  • 76
    • 0033428970 scopus 로고    scopus 로고
    • Helicase motifs: The engine that powers DNA unwinding
    • Hall MC, Matson SW. Helicase motifs: the engine that powers DNA unwinding. Mol Microbiol. 1999;34:867-77.
    • (1999) Mol Microbiol , vol.34 , pp. 867-877
    • Hall, M.C.1    Matson, S.W.2
  • 77
    • 2442676334 scopus 로고    scopus 로고
    • Prokaryotic and eukaryotic DNA helicases. Essential molecular motor proteins for cellular machinery
    • Tuteja N, Tuteja R. Prokaryotic and eukaryotic DNA helicases. Essential molecular motor proteins for cellular machinery. Eur J Biochem. 2004;271:1835-48.
    • (2004) Eur J Biochem , vol.271 , pp. 1835-1848
    • Tuteja, N.1    Tuteja, R.2
  • 78
    • 0026597376 scopus 로고
    • Escherichia coli DNA helicases: Mechanisms of DNA unwinding
    • Lohman TM. Escherichia coli DNA helicases: mechanisms of DNA unwinding. Mol Microbiol. 1992;6:5-14.
    • (1992) Mol Microbiol , vol.6 , pp. 5-14
    • Lohman, T.M.1
  • 79
    • 2442706340 scopus 로고    scopus 로고
    • Unraveling DNA helicases. Motif, structure, mechanism and function
    • Tuteja N, Tuteja R. Unraveling DNA helicases. Motif, structure, mechanism and function. Eur J Biochem. 2004;271:1849-63.
    • (2004) Eur J Biochem , vol.271 , pp. 1849-1863
    • Tuteja, N.1    Tuteja, R.2
  • 81
    • 1642325936 scopus 로고    scopus 로고
    • Evolutionary history and higher order classification of AAA+ ATPases
    • Iyer LM, Leipe DD, Koonin EV, Aravind L. Evolutionary history and higher order classification of AAA+ ATPases. J Struct Biol. 2004;146:11-31.
    • (2004) J Struct Biol , vol.146 , pp. 11-31
    • Iyer, L.M.1    Leipe, D.D.2    Koonin, E.V.3    Aravind, L.4
  • 82
    • 0030897821 scopus 로고    scopus 로고
    • Virus-encoded RNA helicases
    • Kadare G, Haenni AL. Virus-encoded RNA helicases. J Virol. 1997;71:2583-90.
    • (1997) J Virol , vol.71 , pp. 2583-2590
    • Kadare, G.1    Haenni, A.L.2
  • 83
    • 33344473656 scopus 로고    scopus 로고
    • The DEAD-box protein family of RNA helicases
    • Cordin O, Banroques J, Tanner NK, Linder P. The DEAD-box protein family of RNA helicases. Gene. 2006;367:17-37.
    • (2006) Gene , vol.367 , pp. 17-37
    • Cordin, O.1    Banroques, J.2    Tanner, N.K.3    Linder, P.4
  • 84
    • 34347385000 scopus 로고    scopus 로고
    • RNA helicases-one fold for many functions
    • Jankowsky E, Fairman ME. RNA helicases-one fold for many functions. Curr Opin Struct Biol. 2007;17:316-24.
    • (2007) Curr Opin Struct Biol , vol.17 , pp. 316-324
    • Jankowsky, E.1    Fairman, M.E.2
  • 85
    • 48249113056 scopus 로고    scopus 로고
    • Translocation and unwinding mechanisms of RNA and DNA helicases
    • Pyle AM. Translocation and unwinding mechanisms of RNA and DNA helicases. Annu Rev Biophys. 2008;37:317-36.
    • (2008) Annu Rev Biophys , vol.37 , pp. 317-336
    • Pyle, A.M.1
  • 88
    • 0030740262 scopus 로고    scopus 로고
    • Major domain swiveling revealed by the crystal structures of complexes of E. coli Rep helicase bound to single-stranded DNA and ADP
    • Korolev S, Hsieh J, Gauss GH, Lohman TM, Waksman G. Major domain swiveling revealed by the crystal structures of complexes of E. coli Rep helicase bound to single-stranded DNA and ADP. Cell. 1997;90:635-47.
    • (1997) Cell , vol.90 , pp. 635-647
    • Korolev, S.1    Hsieh, J.2    Gauss, G.H.3    Lohman, T.M.4    Waksman, G.5
  • 89
    • 0033515425 scopus 로고    scopus 로고
    • Crystal structures of complexes of PcrA DNA helicase with a DNA substrate indicate an inchworm mechanism
    • Velankar SS, Soultanas P, Dillingham MS, Subramanya HS, Wigley DB. Crystal structures of complexes of PcrA DNA helicase with a DNA substrate indicate an inchworm mechanism. Cell. 1999;97:75-84.
    • (1999) Cell , vol.97 , pp. 75-84
    • Velankar, S.S.1    Soultanas, P.2    Dillingham, M.S.3    Subramanya, H.S.4    Wigley, D.B.5
  • 90
    • 0034679815 scopus 로고    scopus 로고
    • Uncoupling DNA translocation and helicase activity in PcrA: Direct evidence for an active mechanism
    • Soultanas P, Dillingham MS, Wiley P, Webb MR, Wigley DB. Uncoupling DNA translocation and helicase activity in PcrA: direct evidence for an active mechanism. EMBO J. 2000;19:3799-810.
    • (2000) EMBO J , vol.19 , pp. 3799-3810
    • Soultanas, P.1    Dillingham, M.S.2    Wiley, P.3    Webb, M.R.4    Wigley, D.B.5
  • 91
    • 0034635172 scopus 로고    scopus 로고
    • Demonstration of unidirectional single-stranded DNA translocation by PcrA helicase: Measurement of step size and translocation speed
    • Dillingham MS, Wigley DB, Webb MR. Demonstration of unidirectional single-stranded DNA translocation by PcrA helicase: measurement of step size and translocation speed. Biochemistry. 2000;39:205-12.
    • (2000) Biochemistry , vol.39 , pp. 205-212
    • Dillingham, M.S.1    Wigley, D.B.2    Webb, M.R.3
  • 92
    • 34247602963 scopus 로고    scopus 로고
    • A nonuniform stepping mechanism for E. coli UvrD monomer translocation along single-stranded DNA
    • Tomko EJ, Fischer CJ, Niedziela-Majka A, Lohman TM. A nonuniform stepping mechanism for E. coli UvrD monomer translocation along single-stranded DNA. Mol Cell. 2007;26:335-47.
    • (2007) Mol Cell , vol.26 , pp. 335-347
    • Tomko, E.J.1    Fischer, C.J.2    Niedziela-Majka, A.3    Lohman, T.M.4
  • 93
    • 49949083837 scopus 로고    scopus 로고
    • DNA binding to RecD: Role of the 1B domain in SF1B helicase activity
    • Saikrishnan K, Grif fi ths SP, Cook N, Court R, Wigley DB. DNA binding to RecD: role of the 1B domain in SF1B helicase activity. EMBO J. 2008;27:2222-9.
    • (2008) EMBO J , vol.27 , pp. 2222-2229
    • Saikrishnan, K.1    Griffiths, S.P.2    Cook, N.3    Court, R.4    Wigley, D.B.5
  • 94
    • 66149148295 scopus 로고    scopus 로고
    • Mechanistic basis of 5 ¢ -3 ¢ translocation in SF1B helicases
    • Saikrishnan K, Powell B, Cook NJ, Webb MR, Wigley DB. Mechanistic basis of 5 ¢ -3 ¢ translocation in SF1B helicases. Cell. 2009;137:849-59.
    • (2009) Cell , vol.137 , pp. 849-859
    • Saikrishnan, K.1    Powell, B.2    Cook, N.J.3    Webb, M.R.4    Wigley, D.B.5
  • 95
    • 0023705613 scopus 로고
    • A novel superfamily of nucleoside triphosphate-binding motif containing proteins which are probably involved in duplex unwinding in DNA and RNA replication and recombination
    • Gorbalenya AE, Koonin EV, Donchenko AP, Blinov VM. A novel superfamily of nucleoside triphosphate-binding motif containing proteins which are probably involved in duplex unwinding in DNA and RNA replication and recombination. FEBS Lett. 1988;235:16-24.
    • (1988) FEBS Lett , vol.235 , pp. 16-24
    • Gorbalenya, A.E.1    Koonin, E.V.2    Donchenko, A.P.3    Blinov, V.M.4
  • 97
    • 0024278568 scopus 로고
    • A new superfamily of replicative proteins
    • Hodgman TC. A new superfamily of replicative proteins. Nature. 1988;333:22-3.
    • (1988) Nature , vol.333 , pp. 22-23
    • Hodgman, T.C.1
  • 98
    • 0026748738 scopus 로고
    • Conserved sequence motifs in the initiator proteins for rolling circle DNA replication encoded by diverse replicons from eubacteria, eucaryotes and archaebacteria
    • Ilyina TV, Koonin EV. Conserved sequence motifs in the initiator proteins for rolling circle DNA replication encoded by diverse replicons from eubacteria, eucaryotes and archaebacteria. Nucleic Acids Res. 1992;20:3279-85.
    • (1992) Nucleic Acids Res , vol.20 , pp. 3279-3285
    • Ilyina, T.V.1    Koonin, E.V.2
  • 99
    • 0031911760 scopus 로고    scopus 로고
    • Comparisons between the structures of HCV and Rep helicases reveal structural similarities between SF1 and SF2 super-families of helicases
    • Korolev S, Yao N, Lohman TM, Weber PC, Waksman G. Comparisons between the structures of HCV and Rep helicases reveal structural similarities between SF1 and SF2 super-families of helicases. Protein Sci. 1998;7:605-10.
    • (1998) Protein Sci , vol.7 , pp. 605-610
    • Korolev, S.1    Yao, N.2    Lohman, T.M.3    Weber, P.C.4    Waksman, G.5
  • 100
    • 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, Grif fi th JP, Dwyer MD, Thomson JA, Murcko MA, et al. Hepatitis C virus NS3 RNA helicase domain with a bound oligonucleotide: the crystal structure provides insights into the mode of unwinding. Structure. 1998;6:89-100.
    • (1998) Structure , vol.6 , 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
  • 101
    • 0043199343 scopus 로고    scopus 로고
    • The newly identi fi ed Q motif of DEAD box helicases is involved in adenine recognition
    • Tanner NK. The newly identi fi ed Q motif of DEAD box helicases is involved in adenine recognition. Cell Cycle. 2003;2:18-9.
    • (2003) Cell Cycle , vol.2 , pp. 18-19
    • Tanner, N.K.1
  • 102
    • 0141865522 scopus 로고    scopus 로고
    • High-resolution structure of the E. coli RecQ helicase catalytic core
    • Bernstein DA, Zittel MC, Keck JL. High-resolution structure of the E. coli RecQ helicase catalytic core. EMBO J. 2003;22:4910-21.
    • (2003) EMBO J , vol.22 , pp. 4910-4921
    • Bernstein, D.A.1    Zittel, M.C.2    Keck, J.L.3
  • 104
    • 18844457346 scopus 로고    scopus 로고
    • X-ray structures of the Sulfolobus solfataricus SWI2/SNF2 ATPase core and its complex with DNA
    • Durr H, Korner C, Muller M, Hickmann V, Hopfner KP. X-ray structures of the Sulfolobus solfataricus SWI2/SNF2 ATPase core and its complex with DNA. Cell. 2005;121:363-73.
    • (2005) Cell , vol.121 , pp. 363-373
    • Durr, H.1    Korner, C.2    Muller, M.3    Hickmann, V.4    Hopfner, K.P.5
  • 105
    • 0024415732 scopus 로고
    • A lysine substitution in the ATP-binding site of eucaryotic initiation factor 4A abrogates nucleotide-binding activity
    • Rozen F, Pelletier J, Trachsel H, Sonenberg N. A lysine substitution in the ATP-binding site of eucaryotic initiation factor 4A abrogates nucleotide-binding activity. Mol Cell Biol. 1989;9:4061-3.
    • (1989) Mol Cell Biol , vol.9 , pp. 4061-4063
    • Rozen, F.1    Pelletier, J.2    Trachsel, H.3    Sonenberg, N.4
  • 106
    • 0034857262 scopus 로고    scopus 로고
    • DExD/H box RNA helicases: From generic motors to speci fi c dissociation functions
    • Tanner NK, Linder P. DExD/H box RNA helicases: from generic motors to speci fi c dissociation functions. Mol Cell. 2001;8:251-62.
    • (2001) Mol Cell , vol.8 , pp. 251-262
    • Tanner, N.K.1    Linder, P.2
  • 107
    • 0001607723 scopus 로고
    • Distantly related sequences in the alpha- and beta-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold
    • Walker JE, Saraste M, Runswick MJ, Gay NJ. Distantly related sequences in the alpha- and beta-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold. EMBO J. 1982;1:945-51.
    • (1982) EMBO J , vol.1 , pp. 945-951
    • Walker, J.E.1    Saraste, M.2    Runswick, M.J.3    Gay, N.J.4
  • 108
    • 0020364657 scopus 로고
    • Bacteriophage T4 gene 41 protein, required for the synthesis of RNA primers, is also a DNA helicase
    • Venkatesan M, Silver LL, Nossal NG. Bacteriophage T4 gene 41 protein, required for the synthesis of RNA primers, is also a DNA helicase. J Biol Chem. 1982;257:12426-34.
    • (1982) J Biol Chem , vol.257 , pp. 12426-12434
    • Venkatesan, M.1    Silver, L.L.2    Nossal, N.G.3
  • 109
    • 0026584599 scopus 로고
    • Structure of the recA protein-ADP complex
    • Story RM, Steitz TA. Structure of the recA protein-ADP complex. Nature. 1992; 355:374-6.
    • (1992) Nature , vol.355 , pp. 374-376
    • Story, R.M.1    Steitz, T.A.2
  • 110
    • 0026680746 scopus 로고
    • Mutational analysis of a DEAD box RNA helicase: The mammalian translation initiation factor eIF-4A
    • Pause A, Sonenberg N. Mutational analysis of a DEAD box RNA helicase: the mammalian translation initiation factor eIF-4A. EMBO J. 1992;11:2643-54.
    • (1992) EMBO J , vol.11 , pp. 2643-2654
    • Pause, A.1    Sonenberg, N.2
  • 111
    • 0029620994 scopus 로고
    • Mutations in motif II of Escherichia coli DNA helicase II render the enzyme nonfunctional in both mismatch repair and excision repair with differential effects on the unwinding reaction
    • Brosh Jr RM, Matson SW. Mutations in motif II of Escherichia coli DNA helicase II render the enzyme nonfunctional in both mismatch repair and excision repair with differential effects on the unwinding reaction. J Bacteriol. 1995;177:5612-21.
    • (1995) J Bacteriol , vol.177 , pp. 5612-5621
    • Brosh Jr., R.M.1    Matson, S.W.2
  • 112
    • 0029791449 scopus 로고    scopus 로고
    • Genetic and biochemical characterization of mutations in the ATPase and helicase regions of the Upf1 protein
    • Weng Y, Czaplinski K, Peltz SW. Genetic and biochemical characterization of mutations in the ATPase and helicase regions of the Upf1 protein. Mol Cell Biol. 1996;16:5477-90.
    • (1996) Mol Cell Biol , vol.16 , pp. 5477-5490
    • Weng, Y.1    Czaplinski, K.2    Peltz, S.W.3
  • 113
    • 0031054522 scopus 로고    scopus 로고
    • Biochemical analyses of mutations in the HSV-1 helicase-primase that alter ATP hydrolysis, DNA unwinding, and coupling between hydrolysis and unwinding
    • Graves-Woodward KL, Gottlieb J, Challberg MD, Weller SK. Biochemical analyses of mutations in the HSV-1 helicase-primase that alter ATP hydrolysis, DNA unwinding, and coupling between hydrolysis and unwinding. J Biol Chem. 1997;272:4623-30.
    • (1997) J Biol Chem , vol.272 , pp. 4623-4630
    • Graves-Woodward, K.L.1    Gottlieb, J.2    Challberg, M.D.3    Weller, S.K.4
  • 114
    • 15444357274 scopus 로고    scopus 로고
    • A point mutation in Escherichia coli DNA helicase II renders the enzyme nonfunctional in two DNA repair pathways. Evidence for initiation of unwinding from a nick in vivo
    • Brosh Jr RM, Matson SW. A point mutation in Escherichia coli DNA helicase II renders the enzyme nonfunctional in two DNA repair pathways. Evidence for initiation of unwinding from a nick in vivo. J Biol Chem. 1997;272:572-9.
    • (1997) J Biol Chem , vol.272 , pp. 572-579
    • Brosh Jr., R.M.1    Matson, S.W.2
  • 115
    • 10144248959 scopus 로고    scopus 로고
    • A partially functional DNA helicase II mutant defective in forming stable binary complexes with ATP and DNA. A role for helicase motif III
    • Brosh Jr RM, Matson SW. A partially functional DNA helicase II mutant defective in forming stable binary complexes with ATP and DNA. A role for helicase motif III. J Biol Chem. 1996;271:25360-8.
    • (1996) J Biol Chem , vol.271 , pp. 25360-25368
    • Brosh Jr., R.M.1    Matson, S.W.2
  • 116
    • 0029666257 scopus 로고    scopus 로고
    • Replacement of gly815 in helicase motif v alters the single-stranded DNA-dependent ATPase activity of the herpes simplex virus type 1 helicaseprimase
    • Graves-Woodward KL, Weller SK. Replacement of gly815 in helicase motif V alters the single-stranded DNA-dependent ATPase activity of the herpes simplex virus type 1 helicaseprimase. J Biol Chem. 1996;271:13629-35.
    • (1996) J Biol Chem , vol.271 , pp. 13629-13635
    • Graves-Woodward, K.L.1    Weller, S.K.2
  • 117
    • 0032571396 scopus 로고    scopus 로고
    • Site-directed mutations in motif VI of Escherichia coli DNA helicase II result in multiple biochemical defects: Evidence for the involvement of motif VI in the coupling of ATPase and DNA binding activities via conformational changes
    • Hall MC, Ozsoy AZ, Matson SW. Site-directed mutations in motif VI of Escherichia coli DNA helicase II result in multiple biochemical defects: evidence for the involvement of motif VI in the coupling of ATPase and DNA binding activities via conformational changes. J Mol Biol. 1998;277:257-71.
    • (1998) J Mol Biol , vol.277 , pp. 257-271
    • Hall, M.C.1    Ozsoy, A.Z.2    Matson, S.W.3
  • 118
    • 43249100378 scopus 로고    scopus 로고
    • A conserved phenylalanine of motif IV in superfamily 2 helicases is required for cooperative ATP-dependent binding of RNA substrates in DEAD-box proteins
    • Banroques J, Cordin O, Doere M, Linder P, Tanner NK. A conserved phenylalanine of motif IV in superfamily 2 helicases is required for cooperative, ATP-dependent binding of RNA substrates in DEAD-box proteins. Mol Cell Biol. 2008;28:3359-71.
    • (2008) Mol Cell Biol , vol.28 , pp. 3359-3371
    • Banroques, J.1    Cordin, O.2    Doere, M.3    Linder, P.4    Tanner, N.K.5
  • 119
    • 0035816217 scopus 로고    scopus 로고
    • E. coli Rep oligomers are required to initiate DNA unwinding in vitro
    • Cheng W, Hsieh J, Brendza KM, Lohman TM. E. coli Rep oligomers are required to initiate DNA unwinding in vitro. J Mol Biol. 2001;310:327-50.
    • (2001) J Mol Biol , vol.310 , pp. 327-350
    • Cheng, W.1    Hsieh, J.2    Brendza, K.M.3    Lohman, T.M.4
  • 120
    • 0037057630 scopus 로고    scopus 로고
    • Initiation and re-initiation of DNA unwinding by the Escherichia coli Rep helicase
    • Ha T, Rasnik I, Cheng W, Babcock HP, Gauss GH, Lohman TM, et al. Initiation and re-initiation of DNA unwinding by the Escherichia coli Rep helicase. Nature. 2002;419:638-41.
    • (2002) Nature , vol.419 , pp. 638-641
    • Ha, T.1    Rasnik, I.2    Cheng, W.3    Babcock, H.P.4    Gauss, G.H.5    Lohman, T.M.6
  • 121
    • 0041355282 scopus 로고    scopus 로고
    • Kinetic mechanism for formation of the active, dimeric UvrD helicase-DNA complex
    • Maluf NK, Ali JA, Lohman TM. Kinetic mechanism for formation of the active, dimeric UvrD helicase-DNA complex. J Biol Chem. 2003;278:31930-40.
    • (2003) J Biol Chem , vol.278 , pp. 31930-31940
    • Maluf, N.K.1    Ali, J.A.2    Lohman, T.M.3
  • 122
    • 33845657428 scopus 로고    scopus 로고
    • UvrD helicase unwinds DNA bone base pair at a time by a two-part power stroke
    • Lee JY, Yang W. UvrD helicase unwinds DNA bone base pair at a time by a two-part power stroke. Cell. 2006;127:1349-60.
    • (2006) Cell , vol.127 , pp. 1349-1360
    • Lee, J.Y.1    Yang, W.2
  • 124
    • 33646017369 scopus 로고    scopus 로고
    • Structural basis for RNA unwinding by the DEAD-box protein Drosophila Vasa
    • Sengoku T, Nureki O, Nakamura A, Kobayashi S, Yokoyama S. Structural basis for RNA unwinding by the DEAD-box protein Drosophila Vasa. Cell. 2006;125:287-300.
    • (2006) Cell , vol.125 , pp. 287-300
    • Sengoku, T.1    Nureki, O.2    Nakamura, A.3    Kobayashi, S.4    Yokoyama, S.5
  • 125
    • 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;14:647-52.
    • (2007) Nat Struct Mol Biol , vol.14 , pp. 647-652
    • Buttner, K.1    Nehring, S.2    Hopfner, K.P.3
  • 126
    • 0035812836 scopus 로고    scopus 로고
    • Structural analysis of DNA replication fork reversal by RecG
    • Singleton MR, Scaife S, Wigley DB. Structural analysis of DNA replication fork reversal by RecG. Cell. 2001;107:79-89.
    • (2001) Cell , vol.107 , pp. 79-89
    • Singleton, M.R.1    Scaife, S.2    Wigley, D.B.3
  • 130
    • 0242582359 scopus 로고    scopus 로고
    • Two novel conserved motifs in the hepatitis C virus NS3 protein critical for helicase action
    • Lam AM, Keeney D, Frick DN. Two novel conserved motifs in the hepatitis C virus NS3 protein critical for helicase action. J Biol Chem. 2003;278:44514-24.
    • (2003) J Biol Chem , vol.278 , pp. 44514-44524
    • Lam, A.M.1    Keeney, D.2    Frick, D.N.3
  • 131
    • 0031031958 scopus 로고    scopus 로고
    • Kinetic measurement of the step size of DNA unwinding by Escherichia coli UvrD helicase
    • Ali JA, Lohman TM. Kinetic measurement of the step size of DNA unwinding by Escherichia coli UvrD helicase. Science. 1997;275:377-80.
    • (1997) Science , vol.275 , pp. 377-380
    • Ali, J.A.1    Lohman, T.M.2
  • 132
    • 0026546001 scopus 로고
    • Allosteric effects of nucleotide cofactors on Escherichia coli Rep helicase- DNA binding
    • Wong I, Lohman TM. Allosteric effects of nucleotide cofactors on Escherichia coli Rep helicase- DNA binding. Science. 1992;256:350-5.
    • (1992) Science , vol.256 , pp. 350-355
    • Wong, I.1    Lohman, T.M.2
  • 134
    • 0033527761 scopus 로고    scopus 로고
    • An oligomeric form of E. coli UvrD is required for optimal helicase activity
    • Ali JA, Maluf NK, Lohman TM. An oligomeric form of E. coli UvrD is required for optimal helicase activity. J Mol Biol. 1999;293:815-34.
    • (1999) J Mol Biol , vol.293 , pp. 815-834
    • Ali, J.A.1    Maluf, N.K.2    Lohman, T.M.3
  • 135
    • 0037474547 scopus 로고    scopus 로고
    • A dimer of Escherichia coli UvrD is the active form of the helicase in vitro
    • Maluf NK, Fischer CJ, Lohman TM. A dimer of Escherichia coli UvrD is the active form of the helicase in vitro. J Mol Biol. 2003;325:913-35.
    • (2003) J Mol Biol , vol.325 , pp. 913-935
    • Maluf, N.K.1    Fischer, C.J.2    Lohman, T.M.3
  • 136
    • 84861998735 scopus 로고    scopus 로고
    • Dda helicase tightly couples translocation on single-stranded dna to unwinding of duplex DNA: Dda is an optimally active helicase
    • Byrd AK, Matlock DL, Bagchi D, Aarattuthodiyil S, Harrison D, Croquette V, et al. Dda helicase tightly couples translocation on single-stranded dna to unwinding of duplex DNA: Dda is an optimally active helicase. J Mol Biol. 2012;420(3):141-54.
    • (2012) J Mol Biol , vol.420 , Issue.3 , pp. 141-154
    • Byrd, A.K.1    Matlock, D.L.2    Bagchi, D.3    Aarattuthodiyil, S.4    Harrison, D.5    Croquette, V.6
  • 137
    • 77749322591 scopus 로고    scopus 로고
    • Stepwise translocation of nucleic acid motors
    • Myong S, Ha T. Stepwise translocation of nucleic acid motors. Curr Opin Struct Biol. 2010;20:121-7.
    • (2010) Curr Opin Struct Biol , vol.20 , pp. 121-127
    • Myong, S.1    Ha, T.2
  • 138
    • 84861374075 scopus 로고    scopus 로고
    • Single-molecule views of protein movement on singlestranded DNA
    • Ha T, Kozlov AG, Lohman TM. Single-molecule views of protein movement on singlestranded DNA. Annu Rev Biophys. 2012;41:295-319.
    • (2012) Annu Rev Biophys , vol.41 , pp. 295-319
    • Ha, T.1    Kozlov, A.G.2    Lohman, T.M.3
  • 140
    • 0035905807 scopus 로고    scopus 로고
    • Chi-sequence recognition and DNA translocation by single RecBCD helicase/nuclease molecules
    • Dohoney KM, Gelles J. Chi-sequence recognition and DNA translocation by single RecBCD helicase/nuclease molecules. Nature. 2001;409:370-4.
    • (2001) Nature , vol.409 , pp. 370-374
    • Dohoney, K.M.1    Gelles, J.2
  • 141
    • 0141540814 scopus 로고    scopus 로고
    • A molecular throttle: The recombination hotspot chi controls DNA translocation by the RecBCD helicase
    • Spies M, Bianco PR, Dillingham MS, Handa N, Baskin RJ, Kowalczykowski SC. A molecular throttle: the recombination hotspot chi controls DNA translocation by the RecBCD helicase. Cell. 2003;114:647-54.
    • (2003) Cell , vol.114 , pp. 647-654
    • Spies, M.1    Bianco, P.R.2    Dillingham, M.S.3    Handa, N.4    Baskin, R.J.5    Kowalczykowski, S.C.6
  • 142
    • 36049052525 scopus 로고    scopus 로고
    • RecBCD enzyme switches lead motor subunits in response to [chi] recognition
    • Spies M, Amitani I, Baskin RJ, Kowalczykowski SC. RecBCD enzyme switches lead motor subunits in response to [chi] recognition. Cell. 2007;131:694-705.
    • (2007) Cell , vol.131 , pp. 694-705
    • Spies, M.1    Amitani, I.2    Baskin, R.J.3    Kowalczykowski, S.C.4
  • 143
    • 33749135460 scopus 로고    scopus 로고
    • Unraveling helicase mechanisms one molecule at a time
    • Rasnik I, Myong S, Ha T. Unraveling helicase mechanisms one molecule at a time. Nucleic Acids Res. 2006;34:4225-31.
    • (2006) Nucleic Acids Res , vol.34 , pp. 4225-4231
    • Rasnik, I.1    Myong, S.2    Ha, T.3
  • 144
    • 77955605175 scopus 로고    scopus 로고
    • PcrA helicase dismantles RecA fi laments by reeling in DNA in uniform steps
    • Park J, Myong S, Niedziela-Majka A, Lee KS, Yu J, Lohman TM, et al. PcrA helicase dismantles RecA fi laments by reeling in DNA in uniform steps. Cell. 2010;142:544-55.
    • (2010) Cell , vol.142 , pp. 544-555
    • Park, J.1    Myong, S.2    Niedziela-Majka, A.3    Lee, K.S.4    Yu, J.5    Lohman, T.M.6
  • 145
    • 34848840105 scopus 로고    scopus 로고
    • Bacillus stearothermophilus PcrA monomer is a single-stranded DNA translocase but not a processive helicase in vitro
    • Niedziela-Majka A, Chesnik MA, Tomko EJ, Lohman TM. Bacillus stearothermophilus PcrA monomer is a single-stranded DNA translocase but not a processive helicase in vitro. J Biol Chem. 2007;282:27076-85.
    • (2007) J Biol Chem , vol.282 , pp. 27076-27085
    • Niedziela-Majka, A.1    Chesnik, M.A.2    Tomko, E.J.3    Lohman, T.M.4
  • 146
    • 67649637509 scopus 로고    scopus 로고
    • Srs2 disassembles Rad51 fi laments by a protein-protein interaction triggering ATP turnover and dissociation of Rad51 from DNA
    • Antony E, Tomko Q, Xiao L, Krejci L, Lohman TM, Ellengerger T. Srs2 disassembles Rad51 fi laments by a protein-protein interaction triggering ATP turnover and dissociation of Rad51 from DNA. Mol Cell. 2009;35:105-15.
    • (2009) Mol Cell , vol.35 , pp. 105-115
    • Antony, E.1    Tomko, Q.2    Xiao, L.3    Krejci, L.4    Lohman, T.M.5    Ellengerger, T.6
  • 147
    • 27644514163 scopus 로고    scopus 로고
    • Repetitive shuttling of a motor protein on DNA
    • Myong S, Rasnik I, Joo C, Lohman TM, Ha T. Repetitive shuttling of a motor protein on DNA. Nature. 2005;437:1321-5.
    • (2005) Nature , vol.437 , pp. 1321-1325
    • Myong, S.1    Rasnik, I.2    Joo, C.3    Lohman, T.M.4    Ha, T.5
  • 148
    • 0037673941 scopus 로고    scopus 로고
    • DNA helicase Srs2 disrupts the Rad51 presynaptic fi lament
    • Krejci L, Van KS, Li Y, Villemain J, Reddy MS, Klein H, et al. DNA helicase Srs2 disrupts the Rad51 presynaptic fi lament. Nature. 2003;423:305-9.
    • (2003) Nature , vol.423 , pp. 305-309
    • Krejci, L.1    Van Ks Li, Y.2    Villemain, J.3    Reddy, M.S.4    Klein, H.5
  • 149
    • 0037673943 scopus 로고    scopus 로고
    • The Srs2 helicase prevents recombination by disrupting Rad51 nucleoprotein fi laments
    • Veaute X, Jeusset J, Soustelle C, Kowalczykowski SC, Le CE, Fabre F. The Srs2 helicase prevents recombination by disrupting Rad51 nucleoprotein fi laments. Nature. 2003;423:309-12.
    • (2003) Nature , vol.423 , pp. 309-312
    • Veaute, X.1    Jeusset, J.2    Soustelle, C.3    Kowalczykowski, S.C.4    Le Fabre, C.E.F.5
  • 150
    • 13244252309 scopus 로고    scopus 로고
    • UvrD helicase, unlike Rep helicase, dismantles RecA nucleoprotein fi laments in Escherichia coli
    • Veaute X, Delmas S, Selva M, Jeusset J, Le CE, Matic I, et al. UvrD helicase, unlike Rep helicase, dismantles RecA nucleoprotein fi laments in Escherichia coli. EMBO J. 2005;24:180-9.
    • (2005) EMBO J , vol.24 , pp. 180-189
    • Veaute, X.1    Delmas, S.2    Selva, M.3    Jeusset, J.4    Le Matic, C.E.I.5
  • 151
    • 80052449840 scopus 로고    scopus 로고
    • Single-molecule nanopositioning: Structural transitions of a helicase-DNA complex during ATP hydrolysis
    • Balci H, Arslan S, Myong S, Lohman TM, Ha T. Single-molecule nanopositioning: structural transitions of a helicase-DNA complex during ATP hydrolysis. Biophys J. 2011; 101:976-84.
    • (2011) Biophys J , vol.101 , pp. 976-984
    • Balci, H.1    Arslan, S.2    Myong, S.3    Lohman, T.M.4    Ha, T.5
  • 152
    • 4143071283 scopus 로고    scopus 로고
    • Single-molecule three-color FRET
    • Hohng S, Joo C, Ha T. Single-molecule three-color FRET. Biophys J. 2004;87:1328-37.
    • (2004) Biophys J , vol.87 , pp. 1328-1337
    • Hohng, S.1    Joo, C.2    Ha, T.3
  • 153
    • 13444291091 scopus 로고    scopus 로고
    • Three-color single-molecule fl uorescence resonance energy transfer
    • Clamme JP, Deniz AA. Three-color single-molecule fl uorescence resonance energy transfer. Chemphyschem. 2005;6:74-7.
    • (2005) Chemphyschem , vol.6 , pp. 74-77
    • Clamme, J.P.1    Deniz, A.A.2
  • 156
    • 9244235535 scopus 로고    scopus 로고
    • Mechanism of ATP-dependent translocation of E. coli UvrD monomers along single-stranded DNA
    • Fischer CJ, Maluf NK, Lohman TM. Mechanism of ATP-dependent translocation of E. coli UvrD monomers along single-stranded DNA. J Mol Biol. 2004;344:1287-309.
    • (2004) J Mol Biol , vol.344 , pp. 1287-1309
    • Fischer, C.J.1    Maluf, N.K.2    Lohman, T.M.3
  • 157
    • 0037080166 scopus 로고    scopus 로고
    • Direct measurement of single-stranded DNA translocation by PcrA helicase using the fl uorescent base analogue 2-aminopurine
    • Dillingham MS, Wigley DB, Webb MR. Direct measurement of single-stranded DNA translocation by PcrA helicase using the fl uorescent base analogue 2-aminopurine. Biochemistry. 2002;41:643-51.
    • (2002) Biochemistry , vol.41 , pp. 643-651
    • Dillingham, M.S.1    Wigley, D.B.2    Webb, M.R.3
  • 158
    • 0037069390 scopus 로고    scopus 로고
    • Pre-steady-state DNA unwinding by bacteriophage T4 Dda helicase reveals a monomeric molecular motor
    • Nanduri B, Byrd AK, Eoff RL, Tackett AJ, Raney KD. Pre-steady-state DNA unwinding by bacteriophage T4 Dda helicase reveals a monomeric molecular motor. Proc Natl Acad Sci U S A. 2002;99:14722-7.
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 14722-14727
    • Nanduri, B.1    Byrd, A.K.2    Eoff, R.L.3    Tackett, A.J.4    Raney, K.D.5
  • 159
    • 33845980606 scopus 로고    scopus 로고
    • DNA unwinding by Escherichia coli DNA helicase i (TraI) provides evidence for a processive monomeric molecular motor
    • Sikora B, Eoff RL, Matson SW, Raney KD. DNA unwinding by Escherichia coli DNA helicase I (TraI) provides evidence for a processive monomeric molecular motor. J Biol Chem. 2006;281:36110-6.
    • (2006) J Biol Chem , vol.281 , pp. 36110-36116
    • Sikora, B.1    Eoff, R.L.2    Matson, S.W.3    Raney, K.D.4
  • 160
    • 34447266733 scopus 로고    scopus 로고
    • Directional loading and stimulation of PcrA helicase by the replication initiator protein RepD
    • Zhang W, Dillingham MS, Thomas CD, Allen S, Roberts CJ, Soultanas P. Directional loading and stimulation of PcrA helicase by the replication initiator protein RepD. J Mol Biol. 2007;371:336-48.
    • (2007) J Mol Biol , vol.371 , pp. 336-348
    • Zhang, W.1    Dillingham, M.S.2    Thomas, C.D.3    Allen, S.4    Roberts, C.J.5    Soultanas, P.6
  • 161
    • 0026054936 scopus 로고
    • DNA-induced dimerization of the Escherichia coli Rep helicase
    • Chao KL, Lohman TM. DNA-induced dimerization of the Escherichia coli Rep helicase. J Mol Biol. 1991;221:1165-81.
    • (1991) J Mol Biol , vol.221 , pp. 1165-1181
    • Chao, K.L.1    Lohman, T.M.2
  • 162
    • 0026646192 scopus 로고
    • DNA-induced dimerization of the Escherichia coli rep helicase. Allosteric effects of single-stranded and duplex DNA
    • Wong I, Chao KL, Bujalowski W, Lohman TM. DNA-induced dimerization of the Escherichia coli rep helicase. Allosteric effects of single-stranded and duplex DNA. J Biol Chem. 1992;267:7596-610.
    • (1992) J Biol Chem , vol.267 , pp. 7596-7610
    • Wong, I.1    Chao, K.L.2    Bujalowski, W.3    Lohman, T.M.4
  • 163
    • 0027172508 scopus 로고
    • Escherichia coli rep helicase unwinds DNA by an active mechanism
    • Amaratunga M, Lohman TM. Escherichia coli rep helicase unwinds DNA by an active mechanism. Biochemistry. 1993;32:6815-20.
    • (1993) Biochemistry , vol.32 , pp. 6815-6820
    • Amaratunga, M.1    Lohman, T.M.2
  • 164
    • 0028138413 scopus 로고
    • Single-turnover kinetics of helicasecatalyzed DNA unwinding monitored continuously by fl uorescence energy transfer
    • Bjornson KP, Amaratunga M, Moore KJ, Lohman TM. Single-turnover kinetics of helicasecatalyzed DNA unwinding monitored continuously by fl uorescence energy transfer. Biochemistry. 1994;33:14306-16.
    • (1994) Biochemistry , vol.33 , pp. 14306-14316
    • Bjornson, K.P.1    Amaratunga, M.2    Moore, K.J.3    Lohman, T.M.4
  • 165
    • 0030025650 scopus 로고    scopus 로고
    • Kinetic mechanism of DNA binding and DNAinduced dimerization of the Escherichia coli Rep helicase
    • Bjornson KP, Moore KJ, Lohman TM. Kinetic mechanism of DNA binding and DNAinduced dimerization of the Escherichia coli Rep helicase. Biochemistry. 1996;35:2268-82.
    • (1996) Biochemistry , vol.35 , pp. 2268-2282
    • Bjornson, K.P.1    Moore, K.J.2    Lohman, T.M.3
  • 166
    • 77957259274 scopus 로고    scopus 로고
    • DNA binding induces dimerization of Saccharomyces cerevisiae Pif1
    • Barranco-Medina S, Galletto R. DNA binding induces dimerization of Saccharomyces cerevisiae Pif1. Biochemistry. 2010;49(39):8445-54.
    • (2010) Biochemistry , vol.49 , Issue.39 , pp. 8445-8454
    • Barranco-Medina, S.1    Galletto, R.2
  • 167
    • 0742324525 scopus 로고    scopus 로고
    • DNA-binding orientation and domain conformation of the E. coli rep helicase monomer bound to a partial duplex junction: Singlemolecule studies of fl uorescently labeled enzymes
    • Rasnik I, Myong S, Cheng W, Lohman TM, Ha T. DNA-binding orientation and domain conformation of the E. coli rep helicase monomer bound to a partial duplex junction: singlemolecule studies of fl uorescently labeled enzymes. J Mol Biol. 2004;336:395-408.
    • (2004) J Mol Biol , vol.336 , pp. 395-408
    • Rasnik, I.1    Myong, S.2    Cheng, W.3    Lohman, T.M.4    Ha, T.5
  • 168
    • 33750467618 scopus 로고    scopus 로고
    • The absence of Top3 reveals an interaction between the Sgs1 and Pif1 DNA helicases in Saccharomyces cerevisiae
    • Wagner M, Price G, Rothstein R. The absence of Top3 reveals an interaction between the Sgs1 and Pif1 DNA helicases in Saccharomyces cerevisiae. Genetics. 2006;174:555-73.
    • (2006) Genetics , vol.174 , pp. 555-573
    • Wagner, M.1    Price, G.2    Rothstein, R.3
  • 169
    • 79951572633 scopus 로고    scopus 로고
    • Localization of an accessory helicase at the replisome is critical in sustaining ef fi cient genome duplication
    • Atkinson J, Gupta MK, Rudolph CJ, Bell H, Lloyd RG, McGlynn P. Localization of an accessory helicase at the replisome is critical in sustaining ef fi cient genome duplication. Nucleic Acids Res. 2011;39(3):949-57.
    • (2011) Nucleic Acids Res , vol.39 , Issue.3 , pp. 949-957
    • Atkinson, J.1    Gupta, M.K.2    Rudolph, C.J.3    Bell, H.4    Lloyd, R.G.5    McGlynn, P.6
  • 170
    • 1542677230 scopus 로고    scopus 로고
    • TWINKLE Has 5 ¢ -> 3 ¢ DNA helicase activity and is speci fi cally stimulated by mitochondrial single-stranded DNA-binding protein
    • Korhonen JA, Gaspari M, Falkenberg M. TWINKLE Has 5 ¢ -> 3 ¢ DNA helicase activity and is speci fi cally stimulated by mitochondrial single-stranded DNA-binding protein. J Biol Chem. 2003;278:48627-32.
    • (2003) J Biol Chem , vol.278 , pp. 48627-48632
    • Korhonen, J.A.1    Gaspari, M.2    Falkenberg, M.3
  • 171
    • 13444282478 scopus 로고    scopus 로고
    • PriA helicase and SSB interact physically and functionally
    • Cadman CJ, McGlynn P. PriA helicase and SSB interact physically and functionally. Nucleic Acids Res. 2004;32:6378-87.
    • (2004) Nucleic Acids Res , vol.32 , pp. 6378-6387
    • Cadman, C.J.1    McGlynn, P.2
  • 172
    • 34547121734 scopus 로고    scopus 로고
    • A central role for SSB in Escherichia coli RecQ DNA helicase function
    • Shereda RD, Bernstein DA, Keck JL. A central role for SSB in Escherichia coli RecQ DNA helicase function. J Biol Chem. 2007;282:19247-58.
    • (2007) J Biol Chem , vol.282 , pp. 19247-19258
    • Shereda, R.D.1    Bernstein, D.A.2    Keck, J.L.3
  • 173
    • 38049029649 scopus 로고    scopus 로고
    • Single strand binding proteins increase the processivity of DNA unwinding by the hepatitis C virus helicase
    • Rajagopal V, Patel SS. Single strand binding proteins increase the processivity of DNA unwinding by the hepatitis C virus helicase. J Mol Biol. 2008;376:69-79.
    • (2008) J Mol Biol , vol.376 , pp. 69-79
    • Rajagopal, V.1    Patel, S.S.2
  • 174
    • 71749098999 scopus 로고    scopus 로고
    • Replication protein A stimulates the Werner syndrome protein branch migration activity
    • Sowd G, Wang H, Pretto D, Chazin WJ, Opresko PL. Replication protein A stimulates the Werner syndrome protein branch migration activity. J Biol Chem. 2009;284:34682-91.
    • (2009) J Biol Chem , vol.284 , pp. 34682-34691
    • Sowd, G.1    Wang, H.2    Pretto, D.3    Chazin, W.J.4    Opresko, P.L.5
  • 175
    • 0017332435 scopus 로고
    • A mechanism of duplex DNA replication revealed by enzymatic studies of phage phi X174: Catalytic strand separation in advance of replication
    • Scott JF, Eisenberg S, Bertsch LL, Kornberg A. A mechanism of duplex DNA replication revealed by enzymatic studies of phage phi X174: catalytic strand separation in advance of replication. Proc Natl Acad Sci U S A. 1977;74:193-7.
    • (1977) Proc Natl Acad Sci U S A , vol.74 , pp. 193-197
    • Scott, J.F.1    Eisenberg, S.2    Bertsch, L.L.3    Kornberg, A.4
  • 176
    • 0017669060 scopus 로고
    • PhiX174 cistron A protein is a multifunctional enzyme in DNA replication
    • Eisenberg S, Grif fi th J, Kornberg A. phiX174 cistron A protein is a multifunctional enzyme in DNA replication. Proc Natl Acad Sci U S A. 1977;74:3198-202.
    • (1977) Proc Natl Acad Sci U S A , vol.74 , pp. 3198-3202
    • Eisenberg, S.1    Griffith, J.2    Kornberg, A.3
  • 177
    • 0018353521 scopus 로고
    • Enzyme-catalyzed DNA unwinding: Studies on Escherichia coli rep protein
    • Yarranton GT, Gefter ML. Enzyme-catalyzed DNA unwinding: studies on Escherichia coli rep protein. Proc Natl Acad Sci U S A. 1979;76:1658-62.
    • (1979) Proc Natl Acad Sci U S A , vol.76 , pp. 1658-1662
    • Yarranton, G.T.1    Gefter, M.L.2
  • 178
    • 0020693235 scopus 로고
    • Studies on the phi X174 gene A protein-mediated termination of leading strand DNA synthesis
    • Reinberg D, Zipursky SL, Weisbeek P, Brown D, Hurwitz J. Studies on the phi X174 gene A protein-mediated termination of leading strand DNA synthesis. J Biol Chem. 1983;258:529-37.
    • (1983) J Biol Chem , vol.258 , pp. 529-537
    • Reinberg, D.1    Zipursky, S.L.2    Weisbeek, P.3    Brown, D.4    Hurwitz, J.5
  • 180
    • 67650066482 scopus 로고    scopus 로고
    • PcrA helicase tightly couples ATP hydrolysis to unwinding double-stranded DNA, modulated by the initiator protein for plasmid replication, RepD
    • Slatter AF, Thomas CD, Webb MR. PcrA helicase tightly couples ATP hydrolysis to unwinding double-stranded DNA, modulated by the initiator protein for plasmid replication, RepD. Biochemistry. 2009;48(27):6326-34.
    • (2009) Biochemistry , vol.48 , Issue.27 , pp. 6326-6334
    • Slatter, A.F.1    Thomas, C.D.2    Webb, M.R.3
  • 181
    • 36148937572 scopus 로고    scopus 로고
    • RecBCD: The supercar of DNA repair
    • Wigley DB. RecBCD: the supercar of DNA repair. Cell. 2007;131:651-3.
    • (2007) Cell , vol.131 , pp. 651-653
    • Wigley, D.B.1
  • 182
    • 0037698985 scopus 로고    scopus 로고
    • RecBCD enzyme is a DNA helicase with fast and slow motors of opposite polarity
    • Taylor AF, Smith GR. RecBCD enzyme is a DNA helicase with fast and slow motors of opposite polarity. Nature. 2003;423:889-93.
    • (2003) Nature , vol.423 , pp. 889-893
    • Taylor, A.F.1    Smith, G.R.2
  • 183
    • 0026673415 scopus 로고
    • Processivity of the DNA helicase activity of Escherichia coli recBCD enzyme
    • Roman LJ, Eggleston AK, Kowalczykowski SC. Processivity of the DNA helicase activity of Escherichia coli recBCD enzyme. J Biol Chem. 1992;267:4207-14.
    • (1992) J Biol Chem , vol.267 , pp. 4207-4214
    • Roman, L.J.1    Eggleston, A.K.2    Kowalczykowski, S.C.3
  • 184
    • 0016198522 scopus 로고
    • Rec-mediated recombinational hot spot activity in bacteriophage lambda. II. A mutation which causes hot spot activity
    • Lam ST, Stahl MM, McMilin KD, Stahl FW. Rec-mediated recombinational hot spot activity in bacteriophage lambda. II. A mutation which causes hot spot activity. Genetics. 1974;77:425-33.
    • (1974) Genetics , vol.77 , pp. 425-433
    • Lam, S.T.1    Stahl, M.M.2    McMilin, K.D.3    Stahl, F.W.4
  • 185
    • 0030969429 scopus 로고    scopus 로고
    • The recombination hot spot chi is a regulatory element that switches the polarity of DNA degradation by the RecBCD enzyme
    • Anderson DG, Kowalczykowski SC. The recombination hot spot chi is a regulatory element that switches the polarity of DNA degradation by the RecBCD enzyme. Genes Dev. 1997;11:571-81.
    • (1997) Genes Dev , vol.11 , pp. 571-581
    • Anderson, D.G.1    Kowalczykowski, S.C.2
  • 186
    • 0026646152 scopus 로고
    • The RecB subunit of the Escherichia coli RecBCD enzyme couples ATP hydrolysis to DNA unwinding
    • Boehmer PE, Emmerson PT. The RecB subunit of the Escherichia coli RecBCD enzyme couples ATP hydrolysis to DNA unwinding. J Biol Chem. 1992;267:4981-7.
    • (1992) J Biol Chem , vol.267 , pp. 4981-4987
    • Boehmer, P.E.1    Emmerson, P.T.2
  • 187
    • 0034682407 scopus 로고    scopus 로고
    • Translocation step size and mechanism of the RecBC DNA helicase
    • Bianco PR, Kowalczykowski SC. Translocation step size and mechanism of the RecBC DNA helicase. Nature. 2000;405:368-72.
    • (2000) Nature , vol.405 , pp. 368-372
    • Bianco, P.R.1    Kowalczykowski, S.C.2
  • 188
    • 23944518444 scopus 로고    scopus 로고
    • An inactivated nuclease-like domain in RecC with novel function: Implications for evolution
    • Rigden DJ. An inactivated nuclease-like domain in RecC with novel function: implications for evolution. BMC Struct Biol. 2005;5:9.
    • (2005) BMC Struct Biol , vol.5 , pp. 9
    • Rigden, D.J.1
  • 189
    • 33645094195 scopus 로고    scopus 로고
    • In fl uence of chromatin and single strand binding proteins on the activity of an archaeal MCM
    • Marsh VL, McGeoch AT, Bell SD. In fl uence of chromatin and single strand binding proteins on the activity of an archaeal MCM. J Mol Biol. 2006;357:1345-50.
    • (2006) J Mol Biol , vol.357 , pp. 1345-1350
    • Marsh, V.L.1    McGeoch, A.T.2    Bell, S.D.3
  • 190
    • 70449633073 scopus 로고    scopus 로고
    • Rep provides a second motor at the replisome to promote duplication of protein-bound DNA
    • Guy CP, Atkinson J, Gupta MK, Mahdi A, Gwynn EJ, Rudolph CJ, et al. Rep provides a second motor at the replisome to promote duplication of protein-bound DNA. Mol Cell. 2009;36:654-66.
    • (2009) Mol Cell , vol.36 , pp. 654-666
    • Guy, C.P.1    Atkinson, J.2    Gupta, M.K.3    Mahdi, A.4    Gwynn, E.J.5    Rudolph, C.J.6
  • 191
    • 0034528196 scopus 로고    scopus 로고
    • Characterization of the enzymatic properties of the yeast dna2 helicase/endonuclease suggests a new model for Okazaki fragment processing
    • Bae SH, Seo YS. Characterization of the enzymatic properties of the yeast dna2 helicase/endonuclease suggests a new model for Okazaki fragment processing. J Biol Chem. 2000;275:38022-31.
    • (2000) J Biol Chem , vol.275 , pp. 38022-38031
    • Bae, S.H.1    Seo, Y.S.2
  • 192
    • 77956525557 scopus 로고    scopus 로고
    • Components of the secondary pathway stimulate the primary pathway of eukaryotic Okazaki fragment processing
    • Henry RA, Balakrishnan L, Ying-Lin ST, Campbell JL, Bambara RA. Components of the secondary pathway stimulate the primary pathway of eukaryotic Okazaki fragment processing. J Biol Chem. 2010;285:28496-505.
    • (2010) J Biol Chem , Issue.285 , pp. 28496-28505
    • Henry, R.A.1    Balakrishnan, L.2    Ying-Lin, S.T.3    Campbell, J.L.4    Bambara, R.A.5
  • 193
    • 0036606186 scopus 로고    scopus 로고
    • Saccharomyces Rrm3p a 5 ¢ to 3 ¢ DNA helicase that promotes replication fork progression through telomeric and subtelomeric DNA
    • Ivessa AS, Zhou JQ, Schulz VP, Monson EK, Zakian VA. Saccharomyces Rrm3p, a 5 ¢ to 3 ¢ DNA helicase that promotes replication fork progression through telomeric and subtelomeric DNA. Genes Dev. 2002;16:1383-96.
    • (2002) Genes Dev , vol.16 , pp. 1383-1396
    • Ivessa, A.S.1    Zhou, J.Q.2    Schulz, V.P.3    Monson, E.K.4    Zakian, V.A.5
  • 194
    • 33751237066 scopus 로고    scopus 로고
    • The S. cerevisiae Rrm3p DNA helicase moves with the replication fork and affects replication of all yeast chromosomes
    • Azvolinsky AS, Dunaway S, Torres JZ, Bessler JB, Zakian VA. The S. cerevisiae Rrm3p DNA helicase moves with the replication fork and affects replication of all yeast chromosomes. Genes Dev. 2006;20:3104-16.
    • (2006) Genes Dev , vol.20 , pp. 3104-3116
    • Azvolinsky, A.S.1    Dunaway, S.2    Torres, J.Z.3    Bessler, J.B.4    Zakian, V.A.5
  • 195
    • 84857748099 scopus 로고    scopus 로고
    • Recognition of SUMO-modi fi ed PCNA requires tandem receptor motifs in Srs2
    • Armstrong AA, Mohideen F, Lima CD. Recognition of SUMO-modi fi ed PCNA requires tandem receptor motifs in Srs2. Nature. 2012;483:59-63.
    • (2012) Nature , vol.483 , pp. 59-63
    • Armstrong, A.A.1    Mohideen, F.2    Lima, C.D.3
  • 196
    • 0028178792 scopus 로고
    • The Saccharomyces PIF1 DNA helicase inhibits telomere elongation and de novo telomere formation
    • Schulz VP, Zakian VA. The Saccharomyces PIF1 DNA helicase inhibits telomere elongation and de novo telomere formation. Cell. 1994;76:145-55.
    • (1994) Cell , vol.76 , pp. 145-155
    • Schulz, V.P.1    Zakian, V.A.2
  • 197
  • 198
    • 27744445335 scopus 로고    scopus 로고
    • The yeast Pif1p helicase removes telomerase from telomeric DNA
    • Boule JB, Vega LR, Zakian VA. The yeast Pif1p helicase removes telomerase from telomeric DNA. Nature. 2005;438:57-61.
    • (2005) Nature , vol.438 , pp. 57-61
    • Boule, J.B.1    Vega, L.R.2    Zakian, V.A.3
  • 199
    • 0021709778 scopus 로고
    • Effects of the bacteriophage T4 dda protein on DNA synthesis catalyzed by puri fi ed T4 replication proteins
    • Jongeneel CV, Bedinger P, Alberts BM. Effects of the bacteriophage T4 dda protein on DNA synthesis catalyzed by puri fi ed T4 replication proteins. J Biol Chem. 1984;259:12933-8.
    • (1984) J Biol Chem , vol.259 , pp. 12933-12938
    • Jongeneel, C.V.1    Bedinger, P.2    Alberts, B.M.3
  • 201
    • 0025230540 scopus 로고
    • Puri fi ed Escherichia coli F-factor TraY protein binds oriT
    • Lahue EE, Matson SW. Puri fi ed Escherichia coli F-factor TraY protein binds oriT. J Bacteriol. 1990;172:1385-91.
    • (1990) J Bacteriol , vol.172 , pp. 1385-1391
    • Lahue, E.E.1    Matson, S.W.2
  • 202
    • 0024720526 scopus 로고
    • Staphylococcus aureus chromosomal mutations that decrease ef fi ciency of Rep utilization in replication of pT181 and related plasmids
    • Iordanescu S, Bargonetti J. Staphylococcus aureus chromosomal mutations that decrease ef fi ciency of Rep utilization in replication of pT181 and related plasmids. J Bacteriol. 1989;171:4501-3.
    • (1989) J Bacteriol , vol.171 , pp. 4501-4503
    • Iordanescu, S.1    Bargonetti, J.2
  • 203
    • 0026073154 scopus 로고
    • Association of DNA helicase and primase activities with a subassembly of the herpes simplex virus 1 helicase-primase composed of the UL5 and UL52 gene products
    • Dodson MS, Lehman IR. Association of DNA helicase and primase activities with a subassembly of the herpes simplex virus 1 helicase-primase composed of the UL5 and UL52 gene products. Proc Natl Acad Sci U S A. 1991;88:1105-9.
    • (1991) Proc Natl Acad Sci U S A , vol.88 , pp. 1105-1109
    • Dodson, M.S.1    Lehman, I.R.2
  • 204
    • 0026089250 scopus 로고
    • The hyper-gene conversion hpr5-1 mutation of Saccharomyces cerevisiae is an allele of the SRS2/RADH gene
    • Rong L, Palladino F, Aguilera A, Klein HL. The hyper-gene conversion hpr5-1 mutation of Saccharomyces cerevisiae is an allele of the SRS2/RADH gene. Genetics. 1991;127:75-85.
    • (1991) Genetics , vol.127 , pp. 75-85
    • Rong, L.1    Palladino, F.2    Aguilera, A.3    Klein, H.L.4
  • 205
    • 0028325764 scopus 로고
    • DNA helicase requirements for DNA replication during bacteriophage T4 infection
    • Gauss P, Park K, Spencer TE, Hacker KJ. DNA helicase requirements for DNA replication during bacteriophage T4 infection. J Bacteriol. 1994;176:1667-72.
    • (1994) J Bacteriol , vol.176 , pp. 1667-1672
    • Gauss, P.1    Park, K.2    Spencer, T.E.3    Hacker, K.J.4
  • 206
    • 0030298002 scopus 로고    scopus 로고
    • ATP hydrolysis stimulates binding and release of single stranded DNA from alternating subunits of the dimeric E. coli Rep helicase: Implications for ATP-driven helicase translocation
    • Bjornson KP, Wong I, Lohman TM. ATP hydrolysis stimulates binding and release of single stranded DNA from alternating subunits of the dimeric E. coli Rep helicase: implications for ATP-driven helicase translocation. J Mol Biol. 1996;263:411-22.
    • (1996) J Mol Biol , vol.263 , pp. 411-422
    • Bjornson, K.P.1    Wong, I.2    Lohman, T.M.3
  • 207
    • 0031000629 scopus 로고    scopus 로고
    • A yeast replicative helicase, Dna2 helicase, interacts with yeast FEN-1 nuclease in carrying out its essential function
    • Budd ME, Campbell JL. A yeast replicative helicase, Dna2 helicase, interacts with yeast FEN-1 nuclease in carrying out its essential function. Mol Cell Biol. 1997;17:2136-42.
    • (1997) Mol Cell Biol , vol.17 , pp. 2136-2142
    • Budd, M.E.1    Campbell, J.L.2
  • 208
    • 0032102956 scopus 로고    scopus 로고
    • Characterisation of Bacillus stearothermophilus PcrA helicase: Evidence against an active rolling mechanism
    • Bird LE, Brannigan JA, Subramanya HS, Wigley DB. Characterisation of Bacillus stearothermophilus PcrA helicase: evidence against an active rolling mechanism. Nucleic Acids Res. 1998;26:2686-93.
    • (1998) Nucleic Acids Res , vol.26 , pp. 2686-2693
    • Bird, L.E.1    Brannigan, J.A.2    Subramanya, H.S.3    Wigley, D.B.4
  • 209
    • 0032502779 scopus 로고    scopus 로고
    • Mismatch- MutS-MutL-, and helicase II-dependent unwinding from the single-strand break of an incised heteroduplex
    • Dao V, Modrich P. Mismatch-, MutS-, MutL-, and helicase II-dependent unwinding from the single-strand break of an incised heteroduplex. J Biol Chem. 1998;273:9202-7.
    • (1998) J Biol Chem , vol.273 , pp. 9202-9207
    • Dao, V.1    Modrich, P.2
  • 210
    • 0031854048 scopus 로고    scopus 로고
    • PcrA is an essential DNA helicase of Bacillus subtilis ful fi lling functions both in repair and rolling-circle replication
    • Petit MA, Dervyn E, Rose M, Entian KD, McGovern S, Ehrlich SD, et al. PcrA is an essential DNA helicase of Bacillus subtilis ful fi lling functions both in repair and rolling-circle replication. Mol Microbiol. 1998;29:261-73.
    • (1998) Mol Microbiol , vol.29 , pp. 261-273
    • Petit, M.A.1    Dervyn, E.2    Rose, M.3    Entian, K.D.4    McGovern, S.5    Ehrlich, S.D.6
  • 211
    • 0033958431 scopus 로고    scopus 로고
    • UvrD-dependent replication of rolling-circle plasmids in Escherichia coli
    • Bruand C, Ehrlich SD. UvrD-dependent replication of rolling-circle plasmids in Escherichia coli. Mol Microbiol. 2000;35:204-10.
    • (2000) Mol Microbiol , vol.35 , pp. 204-210
    • Bruand, C.1    Ehrlich, S.D.2
  • 212
    • 0034681257 scopus 로고    scopus 로고
    • The Saccharomyces Pif1p DNA helicase and the highly related Rrm3p have opposite effects on replication fork progression in ribosomal DNA
    • Ivessa AS, Zhou JQ, Zakian VA. The Saccharomyces Pif1p DNA helicase and the highly related Rrm3p have opposite effects on replication fork progression in ribosomal DNA. Cell. 2000;100:479-89.
    • (2000) Cell , vol.100 , pp. 479-489
    • Ivessa, A.S.1    Zhou, J.Q.2    Zakian, V.A.3
  • 213
    • 0035878952 scopus 로고    scopus 로고
    • Involvement of Schizosaccharomyces pombe Srs2 in cellular responses to DNA damage
    • Wang SW, Goodwin A, Hickson ID, Norbury CJ. Involvement of Schizosaccharomyces pombe Srs2 in cellular responses to DNA damage. Nucleic Acids Res. 2001;29:2963-72.
    • (2001) Nucleic Acids Res , vol.29 , pp. 2963-2972
    • Wang, S.W.1    Goodwin, A.2    Hickson, I.D.3    Norbury, C.J.4
  • 214
    • 0036258214 scopus 로고    scopus 로고
    • Dynamic localization of an Okazaki fragment processing protein suggests a novel role in telomere replication
    • Choe W, Budd M, Imamura O, Hoopes L, Campbell JL. Dynamic localization of an Okazaki fragment processing protein suggests a novel role in telomere replication. Mol Cell Biol. 2002;22:4202-17.
    • (2002) Mol Cell Biol , vol.22 , pp. 4202-4217
    • Choe, W.1    Budd, M.2    Imamura, O.3    Hoopes, L.4    Campbell, J.L.5
  • 215
    • 1542344026 scopus 로고    scopus 로고
    • The transcriptome of prematurely aging yeast cells is similar to that of telomerase-de fi cient cells
    • Lesur I, Campbell JL. The transcriptome of prematurely aging yeast cells is similar to that of telomerase-de fi cient cells. Mol Biol Cell. 2004;15:1297-312.
    • (2004) Mol Biol Cell , vol.15 , pp. 1297-1312
    • Lesur, I.1    Campbell, J.L.2
  • 216
    • 2942718760 scopus 로고    scopus 로고
    • Regulation of murine telomere length by Rtel: An essential gene encoding a helicase-like protein
    • Ding H, Schertzer M, Wu X, Gertsenstein M, Selig S, Kammori M, et al. Regulation of murine telomere length by Rtel: an essential gene encoding a helicase-like protein. Cell. 2004;117:873-86.
    • (2004) Cell , vol.117 , pp. 873-886
    • Ding, H.1    Schertzer, M.2    Wu, X.3    Gertsenstein, M.4    Selig, S.5    Kammori, M.6
  • 217
    • 2942637828 scopus 로고    scopus 로고
    • The Werner syndrome helicase and exonuclease cooperate to resolve telomeric D loops in a manner regulated by TRF1 and TRF2
    • Opresko PL, Otterlei M, Graakjaer J, Bruheim P, Dawut L, Kolvraa S, et al. The Werner syndrome helicase and exonuclease cooperate to resolve telomeric D loops in a manner regulated by TRF1 and TRF2. Mol Cell. 2004;14:763-74.
    • (2004) Mol Cell , vol.14 , pp. 763-774
    • Opresko, P.L.1    Otterlei, M.2    Graakjaer, J.3    Bruheim, P.4    Dawut, L.5    Kolvraa, S.6
  • 218
    • 33645215616 scopus 로고    scopus 로고
    • Evidence suggesting that Pif1 helicase functions in DNA replication with the Dna2 helicase/nuclease and DNA polymerase delta
    • Budd ME, Reis CC, Smith S, Myung K, Campbell JL. Evidence suggesting that Pif1 helicase functions in DNA replication with the Dna2 helicase/nuclease and DNA polymerase delta. Mol Cell Biol. 2006;26:2490-500.
    • (2006) Mol Cell Biol , vol.26 , pp. 2490-2500
    • Budd, M.E.1    Reis, C.C.2    Smith, S.3    Myung, K.4    Campbell, J.L.5
  • 219
    • 56049111594 scopus 로고    scopus 로고
    • Identification of the Xenopus DNA2 protein as a major nuclease for the 5 ¢ ->3 ¢ strand-speci fi c processing of DNA ends
    • Liao S, Toczylowski T, Yan H. Identification of the Xenopus DNA2 protein as a major nuclease for the 5 ¢ ->3 ¢ strand-speci fi c processing of DNA ends. Nucleic Acids Res. 2008;36:6091-100.
    • (2008) Nucleic Acids Res , vol.36 , pp. 6091-6100
    • Liao, S.1    Toczylowski, T.2    Yan, H.3
  • 220
    • 55549146815 scopus 로고    scopus 로고
    • Pif1 helicase directs eukaryotic Okazaki fragments toward the two-nuclease cleavage pathway for primer removal
    • Rossi ML, Pike JE, Wang W, Burgers PM, Campbell JL, Bambara RA. Pif1 helicase directs eukaryotic Okazaki fragments toward the two-nuclease cleavage pathway for primer removal. J Biol Chem. 2008;283:27483-93.
    • (2008) J Biol Chem , vol.283 , pp. 27483-27493
    • Rossi, M.L.1    Pike, J.E.2    Wang, W.3    Burgers, P.M.4    Campbell, J.L.5    Bambara, R.A.6
  • 221
    • 61349135721 scopus 로고    scopus 로고
    • FANCJ is a structure-speci fi c DNA helicase associated with the maintenance of genomic G/C tracts
    • London TB, Barber LJ, Mosedale G, Kelly GP, Balasubramanian S, Hickson ID, et al. FANCJ is a structure-speci fi c DNA helicase associated with the maintenance of genomic G/C tracts. J Biol Chem. 2008;283:36132-9.
    • (2008) J Biol Chem , vol.283 , pp. 36132-36139
    • London, T.B.1    Barber, L.J.2    Mosedale, G.3    Kelly, G.P.4    Balasubramanian, S.5    Hickson, I.D.6
  • 222
    • 44949114282 scopus 로고    scopus 로고
    • FANCJ helicase defective in Fanconia anemia and breast cancer unwinds G-quadruplex DNA to defend genomic stability
    • Wu Y, Shin-ya K, Brosh Jr RM. FANCJ helicase defective in Fanconia anemia and breast cancer unwinds G-quadruplex DNA to defend genomic stability. Mol Cell Biol. 2008;28:4116-28.
    • (2008) Mol Cell Biol , vol.28 , pp. 4116-4128
    • Wu, Y.1    Shin-Ya, K.2    Brosh Jr., R.M.3
  • 223
    • 69949122831 scopus 로고    scopus 로고
    • Pif1 helicase lengthens some Okazaki fragment fl aps necessitating Dna2 nuclease/helicase action in the two-nuclease processing pathway
    • Pike JE, Burgers PM, Campbell JL, Bambara RA. Pif1 helicase lengthens some Okazaki fragment fl aps necessitating Dna2 nuclease/helicase action in the two-nuclease processing pathway. J Biol Chem. 2009;284:25170-80.
    • (2009) J Biol Chem , vol.284 , pp. 25170-25180
    • Pike, J.E.1    Burgers, P.M.2    Campbell, J.L.3    Bambara, R.A.4
  • 224
    • 71449125359 scopus 로고    scopus 로고
    • Telomeric D-loops containing 8-oxo-2 ¢ - deoxyguanosine are preferred substrates for Werner and Bloom syndrome helicases and are bound by POT1
    • Ghosh A, Rossi ML, Aulds J, Croteau D, Bohr VA. Telomeric D-loops containing 8-oxo-2 ¢ - deoxyguanosine are preferred substrates for Werner and Bloom syndrome helicases and are bound by POT1. J Biol Chem. 2009;284:31074-84.
    • (2009) J Biol Chem , vol.284 , pp. 31074-31084
    • Ghosh, A.1    Rossi, M.L.2    Aulds, J.3    Croteau, D.4    Bohr, V.A.5
  • 225
    • 63249130106 scopus 로고    scopus 로고
    • Polymerase dynamics at the eukaryotic DNA replication fork
    • Burgers PM. Polymerase dynamics at the eukaryotic DNA replication fork. J Biol Chem. 2009;284:4041-5.
    • (2009) J Biol Chem , vol.284 , pp. 4041-4045
    • Burgers, P.M.1
  • 226
    • 77955705802 scopus 로고    scopus 로고
    • WRN helicase unwinds Okazaki fragment-like hybrids in a reaction stimulated by the human DHX9 helicase
    • Chakraborty P, Grosse F. WRN helicase unwinds Okazaki fragment-like hybrids in a reaction stimulated by the human DHX9 helicase. Nucleic Acids Res. 2010;38:4722-30.
    • (2010) Nucleic Acids Res , vol.38 , pp. 4722-4730
    • Chakraborty, P.1    Grosse, F.2
  • 227
    • 0013778216 scopus 로고
    • The location of genes controlling radiation sensitivity in Escherichia coli
    • van de Putte P, van Sluis CA, van Dillewijn J, Rorsch A. The location of genes controlling radiation sensitivity in Escherichia coli. Mutat Res. 1965;2:97-110.
    • (1965) Mutat Res , vol.2 , pp. 97-110
    • Van De Putte, P.1    Van Sluis, C.A.2    Van Dillewijn, J.3    Rorsch, A.4
  • 228
    • 0014401726 scopus 로고
    • Studies on radiation-sensitive mutants of E. coli. I. Mutants defective in the repair synthesis
    • Ogawa H, Shimada K, Tomizawa J. Studies on radiation-sensitive mutants of E. coli. I. Mutants defective in the repair synthesis. Mol Gen Genet. 1968;101:227-44.
    • (1968) Mol Gen Genet , vol.101 , pp. 227-244
    • Ogawa, H.1    Shimada, K.2    Tomizawa, J.3
  • 229
    • 0019122884 scopus 로고
    • Hyper-recombination in uvrD mutants of Escherichia coli K-12
    • Arthur HM, Lloyd RG. Hyper-recombination in uvrD mutants of Escherichia coli K-12. Mol Gen Genet. 1980;180:185-91.
    • (1980) Mol Gen Genet , vol.180 , pp. 185-191
    • Arthur, H.M.1    Lloyd, R.G.2
  • 230
    • 0021750329 scopus 로고
    • Purification and characterization of the bacteriophage T4 dda protein. A DNA helicase that associates with the viral helix-destabilizing protein
    • Jongeneel CV, Formosa T, Alberts BM. Purification and characterization of the bacteriophage T4 dda protein. A DNA helicase that associates with the viral helix-destabilizing protein. J Biol Chem. 1984;259:12925-32.
    • (1984) J Biol Chem , vol.259 , pp. 12925-12932
    • Jongeneel, C.V.1    Formosa, T.2    Alberts, B.M.3
  • 232
    • 0032548445 scopus 로고    scopus 로고
    • Kinetic mechanism for the sequential binding of two single-stranded oligodeoxynucleotides to the Escherichia coli Rep helicase dimer
    • Bjornson KP, Hsieh J, Amaratunga M, Lohman TM. Kinetic mechanism for the sequential binding of two single-stranded oligodeoxynucleotides to the Escherichia coli Rep helicase dimer. Biochemistry. 1998;37:891-9.
    • (1998) Biochemistry , vol.37 , pp. 891-899
    • Bjornson, K.P.1    Hsieh, J.2    Amaratunga, M.3    Lohman, T.M.4
  • 233
    • 45549092030 scopus 로고    scopus 로고
    • Hepatitis C virus NS3 helicase forms oligomeric structures that exhibit optimal DNA unwinding activity in vitro
    • Sikora B, Chen Y, Lichti CF, Harrison MK, Jennings TA, Tang Y, et al. Hepatitis C virus NS3 helicase forms oligomeric structures that exhibit optimal DNA unwinding activity in vitro. J Biol Chem. 2008;283:11516-25.
    • (2008) J Biol Chem , vol.283 , pp. 11516-11525
    • Sikora, B.1    Chen, Y.2    Lichti, C.F.3    Harrison, M.K.4    Jennings, T.A.5    Tang, Y.6
  • 234
    • 84858706298 scopus 로고    scopus 로고
    • Single-stranded DNA translocation of E. coli UvrD monomer is tightly coupled to ATP hydrolysis
    • Tomko EJ, Fischer CJ, Lohman TM. Single-stranded DNA translocation of E. coli UvrD monomer is tightly coupled to ATP hydrolysis. J Mol Biol. 2012;418:32-46.
    • (2012) J Mol Biol , vol.418 , pp. 32-46
    • Tomko, E.J.1    Fischer, C.J.2    Lohman, T.M.3
  • 235
    • 2542430217 scopus 로고    scopus 로고
    • Fluorescence stopped- fl ow studies of single turnover kinetics of E. coli RecBCD helicase-catalyzed DNA unwinding
    • Lucius AL, Wong CJ, Lohman TM. Fluorescence stopped- fl ow studies of single turnover kinetics of E. coli RecBCD helicase-catalyzed DNA unwinding. J Mol Biol. 2004;339:731-50.
    • (2004) J Mol Biol , vol.339 , pp. 731-750
    • Lucius, A.L.1    Wong, C.J.2    Lohman, T.M.3
  • 236
    • 2542475076 scopus 로고    scopus 로고
    • Effects of temperature and ATP on the kinetic mechanism and kinetic step-size for E. coli RecBCD helicase-catalyzed DNA unwinding
    • Lucius AL, Lohman TM. Effects of temperature and ATP on the kinetic mechanism and kinetic step-size for E. coli RecBCD helicase-catalyzed DNA unwinding. J Mol Biol. 2004;339:751-71.
    • (2004) J Mol Biol , vol.339 , pp. 751-771
    • Lucius, A.L.1    Lohman, T.M.2
  • 237
    • 0036447339 scopus 로고    scopus 로고
    • DNA unwinding step-size of E. coli RecBCD helicase determined from single turnover chemical quenchedfl ow kinetic studies
    • Lucius AL, Vindigni A, Gregorian R, Ali JA, Taylor AF, Smith GR, et al. DNA unwinding step-size of E. coli RecBCD helicase determined from single turnover chemical quenchedfl ow kinetic studies. J Mol Biol. 2002;324:409-28.
    • (2002) J Mol Biol , vol.324 , pp. 409-428
    • Lucius, A.L.1    Vindigni, A.2    Gregorian, R.3    Ali, J.A.4    Taylor, A.F.5    Smith, G.R.6
  • 238
    • 50049092327 scopus 로고    scopus 로고
    • In fl uence of DNA end structure on the mechanism of initiation of DNA unwinding by the Escherichia coli RecBCD and RecBC helicases
    • Wu CG, Lohman TM. In fl uence of DNA end structure on the mechanism of initiation of DNA unwinding by the Escherichia coli RecBCD and RecBC helicases. J Mol Biol. 2008;382:312-26.
    • (2008) J Mol Biol , vol.382 , pp. 312-326
    • Wu, C.G.1    Lohman, T.M.2
  • 239
    • 27744469165 scopus 로고    scopus 로고
    • Bipolar DNA translocation contributes to highly processive DNA unwinding by RecBCD enzyme
    • Dillingham MS, Webb MR, Kowalczykowski SC. Bipolar DNA translocation contributes to highly processive DNA unwinding by RecBCD enzyme. J Biol Chem. 2005;280:37069-77.
    • (2005) J Biol Chem , vol.280 , pp. 37069-37077
    • Dillingham, M.S.1    Webb, M.R.2    Kowalczykowski, S.C.3
  • 240
    • 41849106909 scopus 로고    scopus 로고
    • Evidence for a functional dimeric form of the PcrA helicase in DNA unwinding
    • Yang Y, Dou SX, Ren H, Wang PY, Zhang XD, Qian M, et al. Evidence for a functional dimeric form of the PcrA helicase in DNA unwinding. Nucleic Acids Res. 2008;36:1976-89.
    • (2008) Nucleic Acids Res , vol.36 , pp. 1976-1989
    • Yang, Y.1    Dou, S.X.2    Ren, H.3    Wang, P.Y.4    Zhang, X.D.5    Qian, M.6
  • 241
    • 33644793170 scopus 로고    scopus 로고
    • Intermediates revealed in the kinetic mechanism for DNA unwinding by a monomeric helicase
    • Eoff RL, Raney KD. Intermediates revealed in the kinetic mechanism for DNA unwinding by a monomeric helicase. Nat Struct Mol Biol. 2006;13:242-9.
    • (2006) Nat Struct Mol Biol , vol.13 , pp. 242-249
    • Eoff, R.L.1    Raney, K.D.2
  • 242
    • 77952803647 scopus 로고    scopus 로고
    • Kinetic mechanism for DNA unwinding by multiple molecules of Dda helicase aligned on DNA
    • Eoff RL, Raney KD. Kinetic mechanism for DNA unwinding by multiple molecules of Dda helicase aligned on DNA. Biochemistry. 2010;49:4543-53.
    • (2010) Biochemistry , vol.49 , pp. 4543-4553
    • Eoff, R.L.1    Raney, K.D.2
  • 243
    • 0023850023 scopus 로고
    • Escherichia coli DNA helicase i catalyzes a unidirectional and highly processive unwinding reaction
    • Lahue EE, Matson SW. Escherichia coli DNA helicase I catalyzes a unidirectional and highly processive unwinding reaction. J Biol Chem. 1988;263:3208-15.
    • (1988) J Biol Chem , vol.263 , pp. 3208-3215
    • Lahue, E.E.1    Matson, S.W.2
  • 244
    • 77957785417 scopus 로고    scopus 로고
    • Escherichia coli RecBC helicase has two translocase activities controlled by a single ATPase motor
    • Wu CG, Bradford C, Lohman TM. Escherichia coli RecBC helicase has two translocase activities controlled by a single ATPase motor. Nat Struct Mol Biol. 2010;17(10):1210-7.
    • (2010) Nat Struct Mol Biol , vol.17 , Issue.10 , pp. 1210-1217
    • Wu, C.G.1    Bradford, C.2    Lohman, T.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.