메뉴 건너뛰기




Volumn 20, Issue 7, 2012, Pages 1189-1200

The T4 phage SF1B helicase Dda is structurally optimized to perform DNA strand separation

Author keywords

[No Author keywords available]

Indexed keywords

DOUBLE STRANDED DNA; HELICASE; HELICASE DDA; PROTEIN SH3; SINGLE STRANDED DNA; UNCLASSIFIED DRUG;

EID: 84863504414     PISSN: 09692126     EISSN: 18784186     Source Type: Journal    
DOI: 10.1016/j.str.2012.04.013     Document Type: Article
Times cited : (36)

References (61)
  • 2
    • 65349085023 scopus 로고    scopus 로고
    • Hitting the bull's eye: Novel directed cancer therapy through helicase-targeted synthetic lethality
    • M. Aggarwal, and R.M. Brosh Jr. Hitting the bull's eye: novel directed cancer therapy through helicase-targeted synthetic lethality J. Cell. Biochem. 106 2009 758 763
    • (2009) J. Cell. Biochem. , vol.106 , pp. 758-763
    • Aggarwal, M.1    Brosh, Jr.R.M.2
  • 3
    • 0020806166 scopus 로고
    • Properties of the T4 bacteriophage DNA replication apparatus: The T4 dda DNA helicase is required to pass a bound RNA polymerase molecule
    • P. Bedinger, M. Hochstrasser, C.V. Jongeneel, and B.M. Alberts Properties of the T4 bacteriophage DNA replication apparatus: the T4 dda DNA helicase is required to pass a bound RNA polymerase molecule Cell 34 1983 115 123
    • (1983) Cell , vol.34 , pp. 115-123
    • Bedinger, P.1    Hochstrasser, M.2    Jongeneel, C.V.3    Alberts, B.M.4
  • 4
    • 0016432255 scopus 로고
    • Characterization of a bacteriophage T4 mutant lacking DNA-dependent ATPase
    • M.T. Behme, and K. Ebisuzaki Characterization of a bacteriophage T4 mutant lacking DNA-dependent ATPase J. Virol. 15 1975 50 54
    • (1975) J. Virol. , vol.15 , pp. 50-54
    • Behme, M.T.1    Ebisuzaki, K.2
  • 6
    • 64849109616 scopus 로고    scopus 로고
    • Development and evaluation of a structural model for SF1B helicase Dda
    • L.P. Blair, A.J. Tackett, and K.D. Raney Development and evaluation of a structural model for SF1B helicase Dda Biochemistry 48 2009 2321 2329
    • (2009) Biochemistry , vol.48 , pp. 2321-2329
    • Blair, L.P.1    Tackett, A.J.2    Raney, K.D.3
  • 7
    • 76749129611 scopus 로고    scopus 로고
    • Unwinding the functions of the Pif1 family helicases
    • M.L. Bochman, N. Sabouri, and V.A. Zakian Unwinding the functions of the Pif1 family helicases DNA Repair (Amst.) 9 2010 237 249
    • (2010) DNA Repair (Amst.) , vol.9 , pp. 237-249
    • Bochman, M.L.1    Sabouri, N.2    Zakian, V.A.3
  • 8
    • 56449090762 scopus 로고    scopus 로고
    • Rising from the RecQ-age: The role of human RecQ helicases in genome maintenance
    • V.A. Bohr Rising from the RecQ-age: the role of human RecQ helicases in genome maintenance Trends Biochem. Sci. 33 2008 609 620
    • (2008) Trends Biochem. Sci. , vol.33 , pp. 609-620
    • Bohr, V.A.1
  • 9
    • 77952984351 scopus 로고    scopus 로고
    • Characterization of the helicase activity and anti-telomerase properties of yeast Pif1p in vitro
    • J.B. Boulé, and V.A. Zakian Characterization of the helicase activity and anti-telomerase properties of yeast Pif1p in vitro Methods Mol. Biol. 587 2010 359 376
    • (2010) Methods Mol. Biol. , vol.587 , pp. 359-376
    • Boulé, J.B.1    Zakian, V.A.2
  • 10
    • 27744445335 scopus 로고    scopus 로고
    • The yeast Pif1p helicase removes telomerase from telomeric DNA
    • DOI 10.1038/nature04091, PII N04091
    • J.B. Boulé, L.R. Vega, and V.A. Zakian The yeast Pif1p helicase removes telomerase from telomeric DNA Nature 438 2005 57 61 (Pubitemid 41599817)
    • (2005) Nature , vol.438 , Issue.7064 , pp. 57-61
    • Boule, J.-B.1    Vega, L.R.2    Zakian, V.A.3
  • 13
    • 34447132375 scopus 로고    scopus 로고
    • Structural basis for DNA duplex separation by a superfamily-2 helicase
    • DOI 10.1038/nsmb1246, PII NSMB1246
    • K. Büttner, S. Nehring, and K.P. Hopfner Structural basis for DNA duplex separation by a superfamily-2 helicase Nat. Struct. Mol. Biol. 14 2007 647 652 (Pubitemid 47037060)
    • (2007) Nature Structural and Molecular Biology , vol.14 , Issue.7 , pp. 647-652
    • Buttner, K.1    Nehring, S.2    Hopfner, K.-P.3
  • 14
    • 2542432027 scopus 로고    scopus 로고
    • Protein displacement by an assembly of helicase molecules aligned along single-stranded DNA
    • A.K. Byrd, and K.D. Raney Protein displacement by an assembly of helicase molecules aligned along single-stranded DNA Nat. Struct. Mol. Biol. 11 2004 531 538 (Pubitemid 38691920)
    • (2004) Nature Structural and Molecular Biology , vol.11 , Issue.6 , pp. 531-538
    • Byrd, A.K.1    Raney, K.D.2
  • 15
    • 33745176286 scopus 로고    scopus 로고
    • Displacement of a DNA binding protein by Dda helicase
    • DOI 10.1093/nar/gkl369
    • A.K. Byrd, and K.D. Raney Displacement of a DNA binding protein by Dda helicase Nucleic Acids Res. 34 2006 3020 3029 (Pubitemid 44540429)
    • (2006) Nucleic Acids Research , vol.34 , Issue.10 , pp. 3020-3029
    • Byrd, A.K.1    Raney, K.D.2
  • 16
    • 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
    • 10.1016/j.jmb.2012.04.007 Published online Apr 11, 2012
    • A.K. Byrd, D.L. Matlock, D. Bagchi, S. Aarattuthodiyil, D. Harrison, V. Croquette, and K.D. Raney Dda helicase tightly couples translocation on single-stranded DNA to unwinding of duplex DNA: Dda is an optimally active helicase J. Mol. Biol. 2012 10.1016/j.jmb.2012.04.007 Published online Apr 11, 2012
    • (2012) J. Mol. Biol.
    • Byrd, A.K.1    Matlock, D.L.2    Bagchi, D.3    Aarattuthodiyil, S.4    Harrison, D.5    Croquette, V.6    Raney, K.D.7
  • 17
    • 33947137756 scopus 로고    scopus 로고
    • The role of Pif1p, a DNA helicase in Saccharomyces cerevisiae, in maintaining mitochondrial DNA
    • DOI 10.1016/j.mito.2006.11.023, PII S1567724906002467
    • X. Cheng, S. Dunaway, and A.S. Ivessa The role of Pif1p, a DNA helicase in Saccharomyces cerevisiae, in maintaining mitochondrial DNA Mitochondrion 7 2007 211 222 (Pubitemid 46395200)
    • (2007) Mitochondrion , vol.7 , Issue.3 , pp. 211-222
    • Cheng, X.1    Dunaway, S.2    Ivessa, A.S.3
  • 18
    • 0037294467 scopus 로고    scopus 로고
    • Helicase mechanisms and the coupling of helicases within macromolecular machines Part II: Integration of helicases into cellular processes
    • DOI 10.1017/S0033583502003864
    • E. Delagoutte, and P.H. von Hippel Helicase mechanisms and the coupling of helicases within macromolecular machines. Part II: Integration of helicases into cellular processes Q. Rev. Biophys. 36 2003 1 69 (Pubitemid 36313959)
    • (2003) Quarterly Reviews of Biophysics , vol.36 , Issue.1 , pp. 1-69
    • Delagoutte, E.1    Von Hippel, P.H.2
  • 20
    • 0030861685 scopus 로고    scopus 로고
    • DNA helicases in inherited human disorders
    • DOI 10.1016/S0959-437X(97)80149-9
    • N.A. Ellis DNA helicases in inherited human disorders Curr. Opin. Genet. Dev. 7 1997 354 363 (Pubitemid 27292287)
    • (1997) Current Opinion in Genetics and Development , vol.7 , Issue.3 , pp. 354-363
    • Ellis, N.A.1
  • 22
    • 33644793170 scopus 로고    scopus 로고
    • Intermediates revealed in the kinetic mechanism for DNA unwinding by a monomeric helicase
    • DOI 10.1038/nsmb1055, PII N1055
    • R.L. Eoff, and K.D. Raney Intermediates revealed in the kinetic mechanism for DNA unwinding by a monomeric helicase Nat. Struct. Mol. Biol. 13 2006 242 249 (Pubitemid 43348510)
    • (2006) Nature Structural and Molecular Biology , vol.13 , Issue.3 , pp. 242-249
    • Eoff, R.L.1    Raney, K.D.2
  • 23
    • 77952803647 scopus 로고    scopus 로고
    • Kinetic mechanism for DNA unwinding by multiple molecules of Dda helicase aligned on DNA
    • R.L. Eoff, and K.D. Raney Kinetic mechanism for DNA unwinding by multiple molecules of Dda helicase aligned on DNA Biochemistry 49 2010 4543 4553
    • (2010) Biochemistry , vol.49 , pp. 4543-4553
    • Eoff, R.L.1    Raney, K.D.2
  • 24
    • 12144258604 scopus 로고    scopus 로고
    • Chemically modified DNA substrates implicate the importance of electrostatic interactions for DNA unwinding by Dda Helicase
    • DOI 10.1021/bi0484926
    • R.L. Eoff, T.L. Spurling, and K.D. Raney Chemically modified DNA substrates implicate the importance of electrostatic interactions for DNA unwinding by Dda helicase Biochemistry 44 2005 666 674 (Pubitemid 40105497)
    • (2005) Biochemistry , vol.44 , Issue.2 , pp. 666-674
    • Eoff, R.L.1    Spurling, T.L.2    Raney, K.D.3
  • 25
    • 0021646229 scopus 로고
    • The use of affinity chromatography to study proteins involved in bacteriophage T4 genetic recombination
    • T. Formosa, and B.M. Alberts The use of affinity chromatography to study proteins involved in bacteriophage T4 genetic recombination Cold Spring Harb. Symp. Quant. Biol. 49 1984 363 370 (Pubitemid 16195229)
    • (1984) Cold Spring Harbor Symposia on Quantitative Biology , vol.VOL. 49 , pp. 363-370
    • Formosa, T.1    Alberts, B.M.2
  • 26
    • 33846456636 scopus 로고    scopus 로고
    • The hepatitis C virus NS3 protein: A model RNA helicase and potential drug target
    • D.N. Frick The hepatitis C virus NS3 protein: a model RNA helicase and potential drug target Curr. Issues Mol. Biol. 9 2007 1 20 (Pubitemid 46139067)
    • (2007) Current Issues in Molecular Biology , vol.9 , Issue.1 , pp. 1-20
    • Frick, D.N.1
  • 27
    • 0028325764 scopus 로고
    • DNA helicase requirements for DNA replication during bacteriophage T4 infection
    • P. Gauss, K. Park, T.E. Spencer, and K.J. Hacker DNA helicase requirements for DNA replication during bacteriophage T4 infection J. Bacteriol. 176 1994 1667 1672 (Pubitemid 24100217)
    • (1994) Journal of Bacteriology , vol.176 , Issue.6 , pp. 1667-1672
    • Gauss, P.1    Park, K.2    Spencer, T.E.3    Hacker, K.J.4
  • 28
    • 0027182114 scopus 로고
    • Helicases - Amino-Acid-Sequence Comparisons and Structure-Function- Relationships
    • A.E. Gorbalenya, and E.V. Koonin Helicases - Amino-Acid-Sequence Comparisons and Structure-Function-Relationships Curr. Opin. Struct. Biol. 3 1993 419 429
    • (1993) Curr. Opin. Struct. Biol. , vol.3 , pp. 419-429
    • Gorbalenya, A.E.1    Koonin, E.V.2
  • 29
    • 3042721656 scopus 로고    scopus 로고
    • Cell cycle-dependent regulation of a human DNA helicase that localizes in DNA damage foci
    • DOI 10.1091/mbc.E04-03-0227
    • J. Gu, X. Xia, P. Yan, H. Liu, V.N. Podust, A.B. Reynolds, and E. Fanning Cell cycle-dependent regulation of a human DNA helicase that localizes in DNA damage foci Mol. Biol. Cell 15 2004 3320 3332 (Pubitemid 38850126)
    • (2004) Molecular Biology of the Cell , vol.15 , Issue.7 , pp. 3320-3332
    • Gu, J.1    Xia, X.2    Yan, P.3    Liu, H.4    Podust, V.N.5    Reynolds, A.B.6    Fanning, E.7
  • 30
    • 0026713735 scopus 로고
    • Overexpression, purification, sequence analysis, and characterization of the T4 bacteriophage dda DNA helicase
    • K.J. Hacker, and B.M. Alberts Overexpression, purification, sequence analysis, and characterization of the T4 bacteriophage dda DNA helicase J. Biol. Chem. 267 1992 20674 20681
    • (1992) J. Biol. Chem. , vol.267 , pp. 20674-20681
    • Hacker, K.J.1    Alberts, B.M.2
  • 31
    • 34347385000 scopus 로고    scopus 로고
    • RNA helicases - one fold for many functions
    • DOI 10.1016/j.sbi.2007.05.007, PII S0959440X07000723, Nucleic acids / Sequences and topology
    • E. Jankowsky, and M.E. Fairman RNA helicases - one fold for many functions Curr. Opin. Struct. Biol. 17 2007 316 324 (Pubitemid 47021361)
    • (2007) Current Opinion in Structural Biology , vol.17 , Issue.3 , pp. 316-324
    • Jankowsky, E.1    Fairman, M.E.2
  • 32
    • 60549105802 scopus 로고    scopus 로고
    • Global kinetic explorer: A new computer program for dynamic simulation and fitting of kinetic data
    • K.A. Johnson, Z.B. Simpson, and T. Blom Global kinetic explorer: a new computer program for dynamic simulation and fitting of kinetic data Anal. Biochem. 387 2009 20 29
    • (2009) Anal. Biochem. , vol.387 , pp. 20-29
    • Johnson, K.A.1    Simpson, Z.B.2    Blom, T.3
  • 33
    • 4143084041 scopus 로고    scopus 로고
    • UvsX recombinase and Dda helicase rescue stalled bacteriophage T4 DNA replication forks in vitro
    • DOI 10.1074/jbc.M403942200
    • F.A. Kadyrov, and J.W. Drake UvsX recombinase and Dda helicase rescue stalled bacteriophage T4 DNA replication forks in vitro J. Biol. Chem. 279 2004 35735 35740 (Pubitemid 39100578)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.34 , pp. 35735-35740
    • Kadyrov, F.A.1    Drake, J.W.2
  • 35
    • 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
    • J.L. Kim, K.A. Morgenstern, J.P. Griffith, M.D. Dwyer, J.A. Thomson, M.A. Murcko, C. Lin, and P.R. Caron Hepatitis C virus NS3 RNA helicase domain with a bound oligonucleotide: the crystal structure provides insights into the mode of unwinding Structure 6 1998 89 100 (Pubitemid 28084402)
    • (1998) Structure , vol.6 , Issue.1 , pp. 89-100
    • Kim, J.L.1    Morgenstern, K.A.2    Griffith, J.P.3    Dwyer, M.D.4    Thomson, J.A.5    Murcko, M.A.6    Lin, C.7    Caron, P.R.8
  • 36
    • 0030845843 scopus 로고    scopus 로고
    • Model building and refinement practice
    • DOI 10.1016/S0076-6879(97)77013-7
    • G.J. Kleywegt, and T.A. Jones Model building and refinement practice Methods Enzymol. 277 1997 208 230 (Pubitemid 27390923)
    • (1997) Methods in Enzymology , vol.277 , pp. 208-230
    • Kleywegt, G.J.1    Jones, T.A.2
  • 37
    • 0025786902 scopus 로고
    • Inhibition of protein-mediated homologous pairing by a DNA helicase
    • T. Kodadek Inhibition of protein-mediated homologous pairing by a DNA helicase J. Biol. Chem. 266 1991 9712 9718 (Pubitemid 21906715)
    • (1991) Journal of Biological Chemistry , vol.266 , Issue.15 , pp. 9712-9718
    • Kodadek, T.1
  • 38
    • 0023113724 scopus 로고
    • Stimulation of protein-directed strand exchange by a DNA helicase
    • DOI 10.1038/326312a0
    • T. Kodadek, and B.M. Alberts Stimulation of protein-directed strand exchange by a DNA helicase Nature 326 1987 312 314 (Pubitemid 17053759)
    • (1987) Nature , vol.326 , Issue.6110 , pp. 312-314
    • Kodadek, T.1    Alberts, B.M.2
  • 39
    • 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
    • DOI 10.1016/S0092-8674(00)80525-5
    • S. Korolev, J. Hsieh, G.H. Gauss, T.M. Lohman, and G. Waksman Major domain swiveling revealed by the crystal structures of complexes of E. coli Rep helicase bound to single-stranded DNA and ADP Cell 90 1997 635 647 (Pubitemid 27357956)
    • (1997) Cell , vol.90 , Issue.4 , pp. 635-647
    • Korolev, S.1    Hsieh, J.2    Gauss, G.H.3    Lohman, T.M.4    Waksman, G.5
  • 40
    • 0242582359 scopus 로고    scopus 로고
    • Two Novel Conserved Motifs in the Hepatitis C Virus NS3 Protein Critical for Helicase Action
    • DOI 10.1074/jbc.M306444200
    • A.M. Lam, D. Keeney, and D.N. Frick Two novel conserved motifs in the hepatitis C virus NS3 protein critical for helicase action J. Biol. Chem. 278 2003 44514 44524 (Pubitemid 37377204)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.45 , pp. 44514-44524
    • Lam, A.M.I.1    Keeney, D.2    Frick, D.N.3
  • 42
    • 33845657428 scopus 로고    scopus 로고
    • UvrD Helicase Unwinds DNA One Base Pair at a Time by a Two-Part Power Stroke
    • DOI 10.1016/j.cell.2006.10.049, PII S0092867406016011
    • J.Y. Lee, and W. Yang UvrD helicase unwinds DNA one base pair at a time by a two-part power stroke Cell 127 2006 1349 1360 (Pubitemid 44960421)
    • (2006) Cell , vol.127 , Issue.7 , pp. 1349-1360
    • Lee, J.Y.1    Yang, W.2
  • 43
    • 53249121029 scopus 로고    scopus 로고
    • Towards the design of antiviral inhibitors against flaviviruses: The case for the multifunctional NS3 protein from Dengue virus as a target
    • J. Lescar, D. Luo, T. Xu, A. Sampath, S.P. Lim, B. Canard, and S.G. Vasudevan Towards the design of antiviral inhibitors against flaviviruses: the case for the multifunctional NS3 protein from Dengue virus as a target Antiviral Res. 80 2008 94 101
    • (2008) Antiviral Res. , vol.80 , pp. 94-101
    • Lescar, J.1    Luo, D.2    Xu, T.3    Sampath, A.4    Lim, S.P.5    Canard, B.6    Vasudevan, S.G.7
  • 44
    • 42449141601 scopus 로고    scopus 로고
    • Non-hexameric DNA helicases and translocases: Mechanisms and regulation
    • DOI 10.1038/nrm2394, PII NRM2394
    • T.M. Lohman, E.J. Tomko, and C.G. Wu Non-hexameric DNA helicases and translocases: mechanisms and regulation Nat. Rev. Mol. Cell Biol. 9 2008 391 401 (Pubitemid 351574201)
    • (2008) Nature Reviews Molecular Cell Biology , vol.9 , Issue.5 , pp. 391-401
    • Lohman, T.M.1    Tomko, E.J.2    Wu, C.G.3
  • 46
    • 0033586732 scopus 로고    scopus 로고
    • DNA helicases displace streptavidin from biotin-labeled oligonucleotides
    • P.D. Morris, and K.D. Raney DNA helicases displace streptavidin from biotin-labeled oligonucleotides Biochemistry 38 1999 5164 5171
    • (1999) Biochemistry , vol.38 , pp. 5164-5171
    • Morris, P.D.1    Raney, K.D.2
  • 48
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • DOI 10.1016/S0076-6879(97)76066-X
    • Z. Otwinowski, and W. Minor Processing of X-ray diffraction data collected in oscillation mode Methods Enzymol. 276 1997 307 326 (Pubitemid 27085611)
    • (1997) Methods in Enzymology , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 49
    • 33745823112 scopus 로고    scopus 로고
    • Mechanisms of helicases
    • DOI 10.1074/jbc.R600008200
    • S.S. Patel, and I. Donmez Mechanisms of helicases J. Biol. Chem. 281 2006 18265 18268 (Pubitemid 44035481)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.27 , pp. 18265-18268
    • Patel, S.S.1    Donmez, I.2
  • 52
    • 0035980230 scopus 로고    scopus 로고
    • Structure of β-ketoacyl-[acyl carrier protein] reductase from Escherichia coli: Negative cooperativity and its structural basis
    • DOI 10.1021/bi010737g
    • A.C. Price, Y.M. Zhang, C.O. Rock, and S.W. White Structure of beta-ketoacyl-[acyl carrier protein] reductase from Escherichia coli: negative cooperativity and its structural basis Biochemistry 40 2001 12772 12781 (Pubitemid 33026624)
    • (2001) Biochemistry , vol.40 , Issue.43 , pp. 12772-12781
    • Price, A.C.1    Zhang, Y.-M.2    Rock, C.O.3    White, S.W.4
  • 53
    • 48249113056 scopus 로고    scopus 로고
    • Translocation and unwinding mechanisms of RNA and DNA helicases
    • A.M. Pyle Translocation and unwinding mechanisms of RNA and DNA helicases Annu Rev Biophys 37 2008 317 336
    • (2008) Annu Rev Biophys , vol.37 , pp. 317-336
    • Pyle, A.M.1
  • 54
    • 77952909625 scopus 로고    scopus 로고
    • The protease domain increases the translocation stepping efficiency of the hepatitis C virus NS3-4A helicase
    • V. Rajagopal, M. Gurjar, M.K. Levin, and S.S. Patel The protease domain increases the translocation stepping efficiency of the hepatitis C virus NS3-4A helicase J. Biol. Chem. 285 2010 17821 17832
    • (2010) J. Biol. Chem. , vol.285 , pp. 17821-17832
    • Rajagopal, V.1    Gurjar, M.2    Levin, M.K.3    Patel, S.S.4
  • 55
    • 49949083837 scopus 로고    scopus 로고
    • DNA binding to RecD: Role of the 1B domain in SF1B helicase activity
    • K. Saikrishnan, S.P. Griffiths, N. Cook, R. Court, and D.B. Wigley DNA binding to RecD: role of the 1B domain in SF1B helicase activity EMBO J. 27 2008 2222 2229
    • (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
  • 56
    • 66149148295 scopus 로고    scopus 로고
    • Mechanistic basis of 5′-3′ translocation in SF1B helicases
    • K. Saikrishnan, B. Powell, N.J. Cook, M.R. Webb, and D.B. Wigley Mechanistic basis of 5′-3′ translocation in SF1B helicases Cell 137 2009 849 859
    • (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
  • 57
    • 34548638261 scopus 로고    scopus 로고
    • Structure and mechanism of helicases and nucleic acid translocases
    • M.R. Singleton, M.S. Dillingham, and D.B. Wigley Structure and mechanism of helicases and nucleic acid translocases Annu. Rev. Biochem. 76 2007 23 50
    • (2007) Annu. Rev. Biochem. , vol.76 , pp. 23-50
    • Singleton, M.R.1    Dillingham, M.S.2    Wigley, D.B.3
  • 58
    • 45449093552 scopus 로고    scopus 로고
    • The role of Cockayne Syndrome group B (CSB) protein in base excision repair and aging
    • T. Stevnsner, M. Muftuoglu, M.D. Aamann, and V.A. Bohr The role of Cockayne Syndrome group B (CSB) protein in base excision repair and aging Mech. Ageing Dev. 129 2008 441 448
    • (2008) Mech. Ageing Dev. , vol.129 , pp. 441-448
    • Stevnsner, T.1    Muftuoglu, M.2    Aamann, M.D.3    Bohr, V.A.4
  • 60
    • 0033573066 scopus 로고    scopus 로고
    • Crystal structure of UvrB, a DNA helicase adapted for nucleotide excision repair
    • K. Theis, P.J. Chen, M. Skorvaga, B. Van Houten, and C. Kisker Crystal structure of UvrB, a DNA helicase adapted for nucleotide excision repair EMBO J. 18 1999 6899 6907 (Pubitemid 30000443)
    • (1999) EMBO Journal , vol.18 , Issue.24 , pp. 6899-6907
    • Theis, K.1    Chen, P.J.2    Skorvaga, M.3    Van Houten, B.4    Kisker, C.5
  • 61
    • 0033515425 scopus 로고    scopus 로고
    • Crystal structures of complexes of PcrA DNA helicase with a DNA substrate indicate an inchworm mechanism
    • S.S. Velankar, P. Soultanas, M.S. Dillingham, H.S. Subramanya, and D.B. Wigley Crystal structures of complexes of PcrA DNA helicase with a DNA substrate indicate an inchworm mechanism Cell 97 1999 75 84 (Pubitemid 29165891)
    • (1999) Cell , vol.97 , Issue.1 , pp. 75-84
    • Velankar, S.S.1    Soultanas, P.2    Dillingham, M.S.3    Subramanya, H.S.4    Wigley, D.B.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.