메뉴 건너뛰기




Volumn 3, Issue 23, 2012, Pages 3532-3537

In vitro enzyme comparative kinetics: Unwinding of surface-bound DNA nanostructures by RecQ and RecQ1

Author keywords

[No Author keywords available]

Indexed keywords

AFM; ATP HYDROLYSIS; CELLULAR PROCESS; DNA MONOLAYERS; DNA NANOSTRUCTURES; DOUBLE STRANDED DNA; EXPERIMENTAL CONDITIONS; HEIGHT VARIATION; HELICASES; IN-VITRO; KINETIC BEHAVIOR; NANOGRAFTING; REACTION MECHANISM; SURFACE BOUNDS;

EID: 84870803245     PISSN: None     EISSN: 19487185     Source Type: Journal    
DOI: 10.1021/jz3018682     Document Type: Article
Times cited : (5)

References (30)
  • 1
    • 79951703153 scopus 로고    scopus 로고
    • Genome-Wide Comprehensive Analysis of Human Helicases
    • Umate, P.; Tuteja, R.; Tuteja, R.. Genome-Wide Comprehensive Analysis of Human Helicases Comm. & Integr. Biol. 2011, 4, 118-137
    • (2011) Comm. & Integr. Biol. , vol.4 , pp. 118-137
    • Umate, P.1    Tuteja, R.2    Tuteja, R.3
  • 2
    • 76749101923 scopus 로고    scopus 로고
    • Distinct Roles of RECQ1 in the Maintenance of Genomic Stability
    • Wu, Y.; Brosh, R. M. Distinct Roles of RECQ1 in the Maintenance of Genomic Stability DNA Repair. 2010, 9, 315-324
    • (2010) DNA Repair. , vol.9 , pp. 315-324
    • Wu, Y.1    Brosh, R.M.2
  • 3
    • 33947418105 scopus 로고    scopus 로고
    • Biochemical, Biophysical, and Proteomic Approaches to Study DNA Helicases
    • Vindigni, A. Biochemical, Biophysical, And Proteomic Approaches to Study DNA Helicases Mol. BioSyst. 2007, 3, 266-274
    • (2007) Mol. BioSyst. , vol.3 , pp. 266-274
    • Vindigni, A.1
  • 6
    • 0032736140 scopus 로고    scopus 로고
    • Rothmund-Thomson Syndrome Responsible Gene, RECQL4: Genomic Structure and Products
    • Kitao, S.; Lindor, N. M.; Shiratori, M.; Furuichi, Y.; Shimamoto, A. Rothmund-Thomson Syndrome Responsible Gene, RECQL4: Genomic Structure and Products Genomics. 1999, 61, 268-276
    • (1999) Genomics. , vol.61 , pp. 268-276
    • Kitao, S.1    Lindor, N.M.2    Shiratori, M.3    Furuichi, Y.4    Shimamoto, A.5
  • 7
    • 33645814832 scopus 로고    scopus 로고
    • Single Nucleotide Polymorphisms of RecQ1, RAD54L, and ATM Genes Are Associated with Reduced Survival of Pancreatic Cancer
    • Li, D.; Frazier, M.; Evans, D. B.; Hess, K. R.; Crane, C. H.; Jiao, L.; Abbruzzese, J. L. Single Nucleotide Polymorphisms of RecQ1, RAD54L, and ATM Genes Are Associated with Reduced Survival of Pancreatic Cancer J Clin Oncol 2006, 24, 1720-1728
    • (2006) J Clin Oncol , vol.24 , pp. 1720-1728
    • Li, D.1    Frazier, M.2    Evans, D.B.3    Hess, K.R.4    Crane, C.H.5    Jiao, L.6    Abbruzzese, J.L.7
  • 12
    • 77953024275 scopus 로고    scopus 로고
    • Probing the Structural Basis of RecQ Helicase Function
    • Vindigni, A.; Marino, F.; Gileadi, O. Probing the Structural Basis of RecQ Helicase Function Biophys. Chem. 2010, 149, 67-77
    • (2010) Biophys. Chem. , vol.149 , pp. 67-77
    • Vindigni, A.1    Marino, F.2    Gileadi, O.3
  • 14
    • 2342487313 scopus 로고    scopus 로고
    • Analysis of the Unwinding Activity of the Dimeric RECQ1 Helicase in the Presence of Human Replication Protein A
    • Cui, S.; Arosio, D.; Doherty, K. M.; Brosh, R. M., Jr.; Falaschi, A.; Vindigni, A. Analysis of the Unwinding Activity of the Dimeric RECQ1 Helicase in the Presence of Human Replication Protein A Nucleic Acids Res. 2004, 32, 2158-2170
    • (2004) Nucleic Acids Res. , vol.32 , pp. 2158-2170
    • Cui, S.1    Arosio, D.2    Doherty, K.M.3    Brosh Jr., R.M.4    Falaschi, A.5    Vindigni, A.6
  • 15
    • 33745216451 scopus 로고    scopus 로고
    • Analysis of the DNA Unwinding Activity of RecQ Family Helicases
    • Bachrati, C. Z.; Hickson, I. D. Analysis of the DNA Unwinding Activity of RecQ Family Helicases Methods Enzymol. 2006, 409, 86-100
    • (2006) Methods Enzymol. , vol.409 , pp. 86-100
    • Bachrati, C.Z.1    Hickson, I.D.2
  • 17
    • 33744951869 scopus 로고    scopus 로고
    • Escherichia coli RecQ Is a Rapid, Efficient and Monomeric Helicase
    • Zhang, X.-D.; Dou, S.-X.; Xie, P.; Hu, J.-S.; Wang, P.-Y; Xi, X. G. Escherichia coli RecQ Is a Rapid, Efficient and Monomeric Helicase J. Biol. Chem. 2006, 281, 12655-12663
    • (2006) J. Biol. Chem. , vol.281 , pp. 12655-12663
    • Zhang, X.-D.1    Dou, S.-X.2    Xie, P.3    Hu, J.-S.4    Wang, P.-Y.5    Xi, X.G.6
  • 18
    • 84859397679 scopus 로고    scopus 로고
    • Translocation of E. coli RecQ Helicase on Single-Stranded DNA
    • Rad, B.; Kowalczykowski, S. C. Translocation of E. coli RecQ Helicase on Single-Stranded DNA Biochemistry. 2012, 51, 2921-2929
    • (2012) Biochemistry. , vol.51 , pp. 2921-2929
    • Rad, B.1    Kowalczykowski, S.C.2
  • 19
    • 84857137035 scopus 로고    scopus 로고
    • Efficient Coupling of ATP Hydrolysis to Translocation by RecQ Helicase
    • Rad, B.; Kowalczykowski, S. C. Efficient Coupling of ATP Hydrolysis to Translocation by RecQ Helicase Proc. Natl. Acad. Sci., U. S. A. 2012, 109, 1443-1448
    • (2012) Proc. Natl. Acad. Sci., U. S. A. , vol.109 , pp. 1443-1448
    • Rad, B.1    Kowalczykowski, S.C.2
  • 20
    • 1342346600 scopus 로고    scopus 로고
    • The DNA Binding Properties of the Escherichia coli RecQ Helicase
    • Dou, S. X.; Wang, P. Y.; Xu, H. Q.; Xi, X. G. The DNA Binding Properties of the Escherichia coli RecQ Helicase J. Biol. Chem. 2004, 279, 6354-6363
    • (2004) J. Biol. Chem. , vol.279 , pp. 6354-6363
    • Dou, S.X.1    Wang, P.Y.2    Xu, H.Q.3    Xi, X.G.4
  • 21
    • 77951247935 scopus 로고    scopus 로고
    • Multiple Escherichia coli RecQ Helicase Monomers Cooperate to Unwind Long DNA Substrates
    • Li, N.; Henry, E.; Guiot, E.; Rigolet, P.; Brochon, J. C.; Xi, X. G.; Deprez, E. Multiple Escherichia coli RecQ Helicase Monomers Cooperate to Unwind Long DNA Substrates J. Biol. Chem. 2010, 285, 6922-6936
    • (2010) J. Biol. Chem. , vol.285 , pp. 6922-6936
    • Li, N.1    Henry, E.2    Guiot, E.3    Rigolet, P.4    Brochon, J.C.5    Xi, X.G.6    Deprez, E.7
  • 22
    • 0035808456 scopus 로고    scopus 로고
    • Biochemical Characterization of the DNA Helicase Activity of the Escherichia coli RecQ Helicase
    • Harmon, F. G.; Kowalczykowski, S. C. Biochemical Characterization of the DNA Helicase Activity of the Escherichia coli RecQ Helicase J. Biol. Chem. 2001, 276, 232-243
    • (2001) J. Biol. Chem. , vol.276 , pp. 232-243
    • Harmon, F.G.1    Kowalczykowski, S.C.2
  • 23
    • 0242380624 scopus 로고    scopus 로고
    • Simultaneously Monitoring DNA Binding and Helicase-Catalyzed DNA Unwinding by Fluorescence Polarization
    • Xu, H. Q.; Zhang, A. H.; Auclair, C.; Xi, X. G. Simultaneously Monitoring DNA Binding and Helicase-Catalyzed DNA Unwinding by Fluorescence Polarization Nucleic Acids Res. 2003, 31, e70
    • (2003) Nucleic Acids Res. , vol.31 , pp. 70
    • Xu, H.Q.1    Zhang, A.H.2    Auclair, C.3    Xi, X.G.4
  • 25
    • 77954008225 scopus 로고    scopus 로고
    • Monitoring Helicase-Catalyzed DNA Unwinding by Fluorescence Anisotropy and Fluorescence Cross-Correlation Spectroscopy
    • Xi, X. G.; Deprez, E. Monitoring Helicase-Catalyzed DNA Unwinding by Fluorescence Anisotropy and Fluorescence Cross-Correlation Spectroscopy Methods 2010, 51, 289-294
    • (2010) Methods , vol.51 , pp. 289-294
    • Xi, X.G.1    Deprez, E.2
  • 26
    • 33749132155 scopus 로고    scopus 로고
    • Sit down, Relax and Unwind: Structural Insights into RecQ Helicase Mechanisms
    • Killoran, M. P.; Keck, J. L. Sit down, Relax and Unwind: Structural Insights into RecQ Helicase Mechanisms Nucleic Acid Res. 2006, 34, 4098-4105
    • (2006) Nucleic Acid Res. , vol.34 , pp. 4098-4105
    • Killoran, M.P.1    Keck, J.L.2
  • 27
    • 0040292131 scopus 로고    scopus 로고
    • Probing Resistance to Protein Adsorption of Oligo(ethylene glycol)-Terminated Self-Assembled Monolayers by Scanning Force Microscopy
    • Feldman, K.; Hahner, G.; Spencer, N. D.; Harder, P.; Grunze, M. Probing Resistance to Protein Adsorption of Oligo(ethylene glycol)-Terminated Self-Assembled Monolayers by Scanning Force Microscopy J. Am. Chem. Sâ©oc. 1999, 121, 10134-10141
    • (1999) J. Am. Chem. Sâ©oc. , vol.121 , pp. 10134-10141
    • Feldman, K.1    Hahner, G.2    Spencer, N.D.3    Harder, P.4    Grunze, M.5
  • 28
    • 0036447339 scopus 로고    scopus 로고
    • DNA Unwinding Step-Size of E. coli RecBCD Helicase Determined from Single Turnover Chemical Quenched-Flow Kinetic Studies
    • Lucius, A. L.; Vindigni, A.; Gregorian, R.; Ali, J. A.; Taylor, A. F.; Smith, G. R.; Lohman, T. M. DNA Unwinding Step-Size of E. coli RecBCD Helicase Determined from Single Turnover Chemical Quenched-Flow Kinetic Studies J. Mol. Biol. 2002, 324, 409-428
    • (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    Lohman, T.M.7
  • 29
    • 61649088104 scopus 로고    scopus 로고
    • Control of Steric Hindrance on Restriction Enzyme Reactions with Surface-Bound DNA Nanostructures
    • Castronovo, M.; Radovic, S.; Grunwald, C.; Casalis, L.; Morgante, M.; Scoles, G. Control of Steric Hindrance on Restriction Enzyme Reactions with Surface-Bound DNA Nanostructures Nano Lett. 2008, 8, 4140-4145
    • (2008) Nano Lett. , vol.8 , pp. 4140-4145
    • Castronovo, M.1    Radovic, S.2    Grunwald, C.3    Casalis, L.4    Morgante, M.5    Scoles, G.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.