메뉴 건너뛰기




Volumn 31, Issue 4, 2002, Pages 257-267

How to get from A to B: Strategies for analysing protein motion on DNA

Author keywords

Diffusion; DNA; Restriction enzyme; Translocation

Indexed keywords

DNA; DNA BINDING PROTEIN;

EID: 0036656143     PISSN: 01757571     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00249-002-0224-4     Document Type: Article
Times cited : (67)

References (69)
  • 1
    • 0031031958 scopus 로고    scopus 로고
    • Kinetic measurement of the step size of DNA unwinding by Escherichia coli UvrD helicase
    • Ali JA, Lohman TM (1997) Kinetic measurement of the step size of DNA unwinding by Escherichia coli UvrD helicase. Science 275:377-380
    • (1997) Science , vol.275 , pp. 377-380
    • Ali, J.A.1    Lohman, T.M.2
  • 2
    • 0025622722 scopus 로고
    • Stable DNA loops in vivo and in vitro: Roles in gene regulation at a distance and in biophysical characterization of DNA
    • Bellomy GR, Record MT Jr (1989) Stable DNA loops in vivo and in vitro: roles in gene regulation at a distance and in biophysical characterization of DNA. Prog Nucleic Acid Res Mol Biol 39:81-128
    • (1989) Prog Nucleic Acid Res Mol Biol , vol.39 , pp. 81-128
    • Bellomy, G.R.1    Record M.T., Jr.2
  • 4
    • 0001973959 scopus 로고
    • On diffusion-controlled dissociation
    • Berg OG (1978) On diffusion-controlled dissociation. Chem Phys 31:47-57
    • (1978) Chem Phys , vol.31 , pp. 47-57
    • Berg, O.G.1
  • 5
    • 0019887628 scopus 로고
    • Diffusion-driven mechanisms of protein translocation on nucleic acids. 1. Models and theory
    • Berg OG, Winter RB, von Hippel PH (1981) Diffusion-driven mechanisms of protein translocation on nucleic acids. 1. Models and theory. Biochemistry 20:6929-6948
    • (1981) Biochemistry , vol.20 , pp. 6929-6948
    • Berg, O.G.1    Winter, R.B.2    Von Hippel, P.H.3
  • 6
    • 0033918211 scopus 로고    scopus 로고
    • Translocation-independent dimerization of the EcoKI endonuclease visualized by atomic force microscopy
    • Berge T, Ellis DJ, Dryden DTF, Edwardson JM, Henderson RM (2000) Translocation-independent dimerization of the EcoKI endonuclease visualized by atomic force microscopy. Biophys J 79:479-484
    • (2000) Biophys J , vol.79 , pp. 479-484
    • Berge, T.1    Ellis, D.J.2    Dryden, D.T.F.3    Edwardson, J.M.4    Henderson, R.M.5
  • 7
    • 0034682407 scopus 로고    scopus 로고
    • Translocation step size and mechanism of the RecBC DNA helicase
    • Bianco PR, Kowalczykowski SC (2000) Translocation step size and mechanism of the RecBC DNA helicase. Nature 405:368-372
    • (2000) Nature , vol.405 , pp. 368-372
    • Bianco, P.R.1    Kowalczykowski, S.C.2
  • 9
    • 0033546302 scopus 로고    scopus 로고
    • Facilitated target location on DNA by individual Escherichia coli RNA polymerase molecules observed with the scanning force microscope operating in liquid
    • Bustamante C, Guthold M, Zhu X, Yang X (1999) Facilitated target location on DNA by individual Escherichia coli RNA polymerase molecules observed with the scanning force microscope operating in liquid. J Biol Chem 274:16665-16668
    • (1999) J Biol Chem , vol.274 , pp. 16665-16668
    • Bustamante, C.1    Guthold, M.2    Zhu, X.3    Yang, X.4
  • 10
    • 0033546210 scopus 로고    scopus 로고
    • The organization of replication and transcription
    • Cook PR (1999) The organization of replication and transcription. Science 284:1790-1795
    • (1999) Science , vol.284 , pp. 1790-1795
    • Cook, P.R.1
  • 11
    • 0022447082 scopus 로고
    • Role of DNA topology in Mu transposition: Mechanism of sensing the relative orientation of two DNA segments
    • Craigie R, Mizuuchi K (1986) Role of DNA topology in Mu transposition: mechanism of sensing the relative orientation of two DNA segments. Cell 45:793-800
    • (1986) Cell , vol.45 , pp. 793-800
    • Craigie, R.1    Mizuuchi, K.2
  • 12
    • 0032212129 scopus 로고    scopus 로고
    • EcoKI with an amino acid substitution in any one of seven DEAD-box motifs has impaired ATPase and endonuclease activities
    • Davies GP, Powell LM, Webb JL, Cooper LP, Murray NE (1998) EcoKI with an amino acid substitution in any one of seven DEAD-box motifs has impaired ATPase and endonuclease activities Nucleic Acids Res 26:1775-1782
    • (1998) Nucleic Acids Res , vol.26 , pp. 1775-1782
    • Davies, G.P.1    Powell, L.M.2    Webb, J.L.3    Cooper, L.P.4    Murray, N.E.5
  • 13
    • 0033214565 scopus 로고    scopus 로고
    • The DNA translcoation and ATPase activities of restriction-deficient mutants of EcoKI
    • Davies GP, Kemp P, Molineux IJ, Murray NE (1999) The DNA translcoation and ATPase activities of restriction-deficient mutants of EcoKI. J Mol Biol 292:787-796
    • (1999) J Mol Biol , vol.292 , pp. 787-796
    • Davies, G.P.1    Kemp, P.2    Molineux, I.J.3    Murray, N.E.4
  • 14
    • 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 (2000) Demonstration of unidirectional single-stranded DNA translocation by PcrA helicase: measurement of step size and translocation speed. Biochemistry 39:205-212
    • (2000) Biochemistry , vol.39 , pp. 205-212
    • Dillingham, M.S.1    Wigley, D.B.2    Webb, M.R.3
  • 17
    • 0032932374 scopus 로고    scopus 로고
    • Direct observation of DNA translocation and cleavage by the EcoKI endonuclease using atomic force microscopy
    • Ellis DJ, Dryden DTF, Berge T, Edwardson JM, Henderson RM (1999) Direct observation of DNA translocation and cleavage by the EcoKI endonuclease using atomic force microscopy. Nat Struct Biol 6:15-17
    • (1999) Nat Struct Biol , vol.6 , pp. 15-17
    • Ellis, D.J.1    Dryden, D.T.F.2    Berge, T.3    Edwardson, J.M.4    Henderson, R.M.5
  • 18
    • 0034595208 scopus 로고    scopus 로고
    • Measuring motion on DNA by the type I restriction endonuclease EcoR124I using triplex displacement
    • Firman K, Szczelkun MD (2000) Measuring motion on DNA by the type I restriction endonuclease EcoR124I using triplex displacement. EMBO J 19:2094-2102
    • (2000) EMBO J , vol.19 , pp. 2094-2102
    • Firman, K.1    Szczelkun, M.D.2
  • 19
    • 0033607255 scopus 로고    scopus 로고
    • Translocation and specific cleavage of bacteriophage T7 in vivo by EcoKI
    • Garcia LR, Molineux IJ (1999) Translocation and specific cleavage of bacteriophage T7 in vivo by EcoKI. Proc Natl Acad Sci USA 96:12430-12435
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 12430-12435
    • Garcia, L.R.1    Molineux, I.J.2
  • 20
    • 0033980541 scopus 로고    scopus 로고
    • RuvAB-mediated branch migration does not involve extensive DNA opening within the RuvB hexamer
    • George H, Kuraoka I, Nauman DA, Kobertz WR, Wood RD, West SC (2000) RuvAB-mediated branch migration does not involve extensive DNA opening within the RuvB hexamer. Curr Biol 10:103-106
    • (2000) Curr Biol , vol.10 , pp. 103-106
    • George, H.1    Kuraoka, I.2    Nauman, D.A.3    Kobertz, W.R.4    Wood, R.D.5    West, S.C.6
  • 21
    • 0025995309 scopus 로고
    • Endonuclease (R) subunits of type-I and type-III restriction-modification enzymes contain a helicase-like domain
    • Gorbalenya AE, Koonin EV (1991) Endonuclease (R) subunits of type-I and type-III restriction-modification enzymes contain a helicase-like domain. FEBS Lett 291:277-281
    • (1991) FEBS Lett , vol.291 , pp. 277-281
    • Gorbalenya, A.E.1    Koonin, E.V.2
  • 24
    • 0030721538 scopus 로고    scopus 로고
    • Transposition and site-specific recombination: Adapting DNA cut-and-paste mechanisms to a variety of DNA rearrangements
    • Hallet B, Sherratt DJ (1997) Transposition and site-specific recombination: adapting DNA cut-and-paste mechanisms to a variety of DNA rearrangements. FEMS Microbiol Rev 21:157-178
    • (1997) FEMS Microbiol Rev , vol.21 , pp. 157-178
    • Hallet, B.1    Sherratt, D.J.2
  • 26
    • 0020160863 scopus 로고
    • Involvement of outside sequences in the major kinetic path by which EcoRI endonuclease locates and leaves its recognition sequence
    • Jack WE, Terry BJ, Modrich P (1982) Involvement of outside sequences in the major kinetic path by which EcoRI endonuclease locates and leaves its recognition sequence. Proc Natl Acad Sci USA 79:4010-4014
    • (1982) Proc Natl Acad Sci USA , vol.79 , pp. 4010-4014
    • Jack, W.E.1    Terry, B.J.2    Modrich, P.3
  • 27
    • 0034719392 scopus 로고    scopus 로고
    • The DExH protein NPH-II is a processive and directional motor for unwinding RNA
    • Jankowsky E, Gross CH, Shuman S, Pyle AM (2000) The DExH protein NPH-II is a processive and directional motor for unwinding RNA. Nature 403:447-451
    • (2000) Nature , vol.403 , pp. 447-451
    • Jankowsky, E.1    Gross, C.H.2    Shuman, S.3    Pyle, A.M.4
  • 28
    • 0034723157 scopus 로고    scopus 로고
    • DNA supercoiling during ATP-dependent DNA translocation by the type I restriction enzyme EcoAI
    • Janscak P, Bickle TA (2000) DNA supercoiling during ATP-dependent DNA translocation by the type I restriction enzyme EcoAI. J Mol Biol 295:1089-1099
    • (2000) J Mol Biol , vol.295 , pp. 1089-1099
    • Janscak, P.1    Bickle, T.A.2
  • 29
    • 0032190284 scopus 로고    scopus 로고
    • Analysis of the subunit assembly of the type IC restriction-modification enzyme EcoR124I
    • Janscak P, Dryden DT, Firman K (1998) Analysis of the subunit assembly of the type IC restriction-modification enzyme EcoR124I. Nucleic Acids Res 26:4439-4445
    • (1998) Nucleic Acids Res , vol.26 , pp. 4439-4445
    • Janscak, P.1    Dryden, D.T.2    Firman, K.3
  • 30
    • 0032562139 scopus 로고    scopus 로고
    • Kinetic characterisation of linear diffusion of the restriction endonuclease EcoRV on DNA
    • Jeltsch A, Pingoud A (1998) Kinetic characterisation of linear diffusion of the restriction endonuclease EcoRV on DNA. Biochemistry 37:2160-2169
    • (1998) Biochemistry , vol.37 , pp. 2160-2169
    • Jeltsch, A.1    Pingoud, A.2
  • 31
    • 0028782732 scopus 로고
    • Pausing of the restriction endonuclease EcoRI during linear diffusion on DNA
    • Jeltsch A, Alves J, Wolfes H, Maass G, Pingoud A (1994) Pausing of the restriction endonuclease EcoRI during linear diffusion on DNA. Biochemistry 34:10215-10219
    • (1994) Biochemistry , vol.34 , pp. 10215-10219
    • Jeltsch, A.1    Alves, J.2    Wolfes, H.3    Maass, G.4    Pingoud, A.5
  • 32
    • 0029790522 scopus 로고    scopus 로고
    • Linear diffusion of the restriction endonuclease EcoRV on DNA is essential for the in vivo function of the enzyme
    • Jeltsch A, Wenz C, Stahl F, Pingoud A (1996) Linear diffusion of the restriction endonuclease EcoRV on DNA is essential for the in vivo function of the enzyme. EMBO J 15:5104-5111
    • (1996) EMBO J , vol.15 , pp. 5104-5111
    • Jeltsch, A.1    Wenz, C.2    Stahl, F.3    Pingoud, A.4
  • 35
    • 0034649621 scopus 로고    scopus 로고
    • Rapid exchange of histone H1.1 on chromatin in living human cells
    • Lever MA, Th'ng JP, Sun X, Hendzel MJ (2000) Rapid exchange of histone H1.1 on chromatin in living human cells. Nature 408:873-876
    • (2000) Nature , vol.408 , pp. 873-876
    • Lever, M.A.1    Th'ng, J.P.2    Sun, X.3    Hendzel, M.J.4
  • 36
    • 0020490965 scopus 로고
    • Sequence specificity of exonuclease III from E. coli
    • Linxweiler W, Horz W (1982) Sequence specificity of exonuclease III from E. coli. Nucleic Acids Res 10:4845-4859
    • (1982) Nucleic Acids Res , vol.10 , pp. 4845-4859
    • Linxweiler, W.1    Horz, W.2
  • 37
    • 0023433855 scopus 로고
    • Supercoiling of the DNA template during transcription
    • Liu LF, Wang JC (1987) Supercoiling of the DNA template during transcription. Proc Natl Acad Sci USA 84:7024-7027
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 7024-7027
    • Liu, L.F.1    Wang, J.C.2
  • 38
    • 0022573212 scopus 로고
    • Kinetics of protein-nucleic acid interactions: Use of salt effects to probe mechanisms of interactions
    • Lohman TM (1986) Kinetics of protein-nucleic acid interactions: use of salt effects to probe mechanisms of interactions. CRC Crit Rev Biochem 19:191-245
    • (1986) CRC Crit Rev Biochem , vol.19 , pp. 191-245
    • Lohman, T.M.1
  • 39
    • 0029893874 scopus 로고    scopus 로고
    • Mechanisms of helicase-catalyzed DNA unwinding
    • Lohman TM, Bjornson KP (1996) Mechanisms of helicase-catalyzed DNA unwinding. Annu Rev Biochem 65:169-214
    • (1996) Annu Rev Biochem , vol.65 , pp. 169-214
    • Lohman, T.M.1    Bjornson, K.P.2
  • 40
    • 85081158488 scopus 로고    scopus 로고
    • Analysis of DNA looping interactions by type II restriction enzymes that require two copies of their recognition sites
    • Milsom SE, Halford SE, Embleton ML, Szczelkun MD (2001) Analysis of DNA looping interactions by type II restriction enzymes that require two copies of their recognition sites. J Mol Biol 31:517-528
    • (2001) J Mol Biol , vol.31 , pp. 517-528
    • Milsom, S.E.1    Halford, S.E.2    Embleton, M.L.3    Szczelkun, M.D.4
  • 41
    • 0035793376 scopus 로고    scopus 로고
    • Protein dynamics: Implications for nuclear architecture and gene expression
    • Misteli T (2001) Protein dynamics: implications for nuclear architecture and gene expression. Science 291:843-847
    • (2001) Science , vol.291 , pp. 843-847
    • Misteli, T.1
  • 42
    • 0034649663 scopus 로고    scopus 로고
    • Dynamic binding of histone H1 to chromatin in living cells
    • Misteli T, Gunjan A, Hock R, Bustin M, Brown DT (2000) Dynamic binding of histone H1 to chromatin in living cells. Nature 408:877-881
    • (2000) Nature , vol.408 , pp. 877-881
    • Misteli, T.1    Gunjan, A.2    Hock, R.3    Bustin, M.4    Brown, D.T.5
  • 43
    • 0034130457 scopus 로고    scopus 로고
    • Type I restriction systems: Sophisticated molecular machines
    • Murray NE (2000) Type I restriction systems: sophisticated molecular machines. Microbiol Mol Biol Rev 64:412-434
    • (2000) Microbiol Mol Biol Rev , vol.64 , pp. 412-434
    • Murray, N.E.1
  • 44
    • 0025707019 scopus 로고
    • Template supercoiling by a chimera of yeast GAL4 protein and phage T7 RNA polymerase
    • Ostrander EA, Benedetti P, Wang JC (1990) Template supercoiling by a chimera of yeast GAL4 protein and phage T7 RNA polymerase. Science 14:1261-1265
    • (1990) Science , vol.14 , pp. 1261-1265
    • Ostrander, E.A.1    Benedetti, P.2    Wang, J.C.3
  • 46
    • 0016302334 scopus 로고
    • Diffusion controlled reaction rates in spheroidal geometry. Application to repressor-operator association and membrane bound enzymes
    • Richter PH, Eigen M (1974) Diffusion controlled reaction rates in spheroidal geometry. Application to repressor-operator association and membrane bound enzymes. Biophys Chem 2:255-263
    • (1974) Biophys Chem , vol.2 , pp. 255-263
    • Richter, P.H.1    Eigen, M.2
  • 47
    • 0014945567 scopus 로고
    • The lac repressor-operator interaction. III. Kinetic studies
    • Riggs AD, Bourgeois S, Cohn M (1970) The lac repressor-operator interaction. III. Kinetic studies. J Mol Biol 53: 401-417
    • (1970) J Mol Biol , vol.53 , pp. 401-417
    • Riggs, A.D.1    Bourgeois, S.2    Cohn, M.3
  • 48
    • 0033485539 scopus 로고    scopus 로고
    • Quantitative comparison of DNA looping in vitro and in vivo: Chromatin increases effective DNA flexibility at short distances
    • Ringrose L, Chabanis S, Angrand PO, Woodroofe C, Stewart AF (1999) Quantitative comparison of DNA looping in vitro and in vivo: chromatin increases effective DNA flexibility at short distances. EMBO J 18:6630-6641
    • (1999) EMBO J , vol.18 , pp. 6630-6641
    • Ringrose, L.1    Chabanis, S.2    Angrand, P.O.3    Woodroofe, C.4    Stewart, A.F.5
  • 49
    • 0002598414 scopus 로고
    • Type II restriction endonucleases
    • Linn SM, Lloyd RS, Roberts RJ (eds). Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Roberts RJ, Halford SE (1993) Type II restriction endonucleases. In: Linn SM, Lloyd RS, Roberts RJ (eds) Nucleases. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY, pp 35-88
    • (1993) Nucleases , pp. 35-88
    • Roberts, R.J.1    Halford, S.E.2
  • 50
    • 0026673415 scopus 로고
    • Processivity of the DNA helicase activity of Escherichia coli recBCD enzyme
    • Roman LJ, Eggleston AK, Kowalczykowski SC (1992) Processivity of the DNA helicase activity of Escherichia coli recBCD enzyme. J Biol Chem 267:4207-4214
    • (1992) J Biol Chem , vol.267 , pp. 4207-4214
    • Roman, L.J.1    Eggleston, A.K.2    Kowalczykowski, S.C.3
  • 51
    • 0032986554 scopus 로고    scopus 로고
    • One-dimensional diffusion of proteins along DNA
    • Shimamoto N (1999) One-dimensional diffusion of proteins along DNA. J Biol Chem 274:15293-15296
    • (1999) J Biol Chem , vol.274 , pp. 15293-15296
    • Shimamoto, N.1
  • 52
    • 0016350386 scopus 로고
    • Model for wandering restriction enzymes
    • Shulman MJ (1974) Model for wandering restriction enzymes. Nature 252:76-78
    • (1974) Nature , vol.252 , pp. 76-78
    • Shulman, M.J.1
  • 53
    • 0035812836 scopus 로고    scopus 로고
    • Structural analysis of DNA replication fork reversal by RecG
    • in press
    • Singleton MR, Scaife S, Wigley DB (2001) Structural analysis of DNA replication fork reversal by RecG. Cell (in press)
    • (2001) Cell
    • Singleton, M.R.1    Scaife, S.2    Wigley, D.B.3
  • 54
    • 0035150184 scopus 로고    scopus 로고
    • Unwinding the "Gordian knot" of helicase action
    • Soultanas P, Wigley DB (2001) Unwinding the "Gordian knot" of helicase action. Trends Biochem Sci. 26:47-54
    • (2001) Trends Biochem Sci , vol.26 , pp. 47-54
    • Soultanas, P.1    Wigley, D.B.2
  • 55
    • 0034387984 scopus 로고    scopus 로고
    • Oneand three-dimensional pathways for proteins to reach specific DNA sites
    • Stanford NP, Szczelkun MD, Marko JF, Halford SE (2000) Oneand three-dimensional pathways for proteins to reach specific DNA sites. EMBO J 19:6546-6557
    • (2000) EMBO J , vol.19 , pp. 6546-6557
    • Stanford, N.P.1    Szczelkun, M.D.2    Marko, J.F.3    Halford, S.E.4
  • 56
    • 0023732866 scopus 로고
    • Model for how type I restriction enzymes select cleavage sites in DNA
    • Studier FW, Bandyopadhyay PK (1988) Model for how type I restriction enzymes select cleavage sites in DNA. Proc Natl Acad Sci USA 85: 4677-4681
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 4677-4681
    • Studier, F.W.1    Bandyopadhyay, P.K.2
  • 57
    • 0034458482 scopus 로고    scopus 로고
    • How do proteins move along DNA? Lessons from type-I and type-III restriction endonucleases
    • Szczelkun MD (2000) How do proteins move along DNA? Lessons from type-I and type-III restriction endonucleases. Essays Biochem 35:131-143
    • (2000) Essays Biochem , vol.35 , pp. 131-143
    • Szczelkun, M.D.1
  • 58
    • 0037065729 scopus 로고    scopus 로고
    • Kinetic models of translocation, head-on collision and DNA cleavage by type I restriction endonucleases
    • Szczelkun MD (2002) Kinetic models of translocation, head-on collision and DNA cleavage by type I restriction endonucleases. Biochemistry 41:2067-2074
    • (2002) Biochemistry , vol.41 , pp. 2067-2074
    • Szczelkun, M.D.1
  • 59
    • 0029978713 scopus 로고    scopus 로고
    • Recombination by resolvase to analyse DNA communications by the SfiI restriction endonuclease
    • Szczelkun MD, Halford SE (1996) Recombination by resolvase to analyse DNA communications by the SfiI restriction endonuclease. EMBO J 15:1460-1469
    • (1996) EMBO J , vol.15 , pp. 1460-1469
    • Szczelkun, M.D.1    Halford, S.E.2
  • 60
    • 0029910629 scopus 로고    scopus 로고
    • Repercussions of DNA tracking by the type IC restriction endonuclease EcoR124I on linear, circular and catenated substrates
    • Szczelkun MD, Dillingham MS, Janscak P, Firman K, Halford SE (1996) Repercussions of DNA tracking by the type IC restriction endonuclease EcoR124I on linear, circular and catenated substrates. EMBO J 15:6335-6347
    • (1996) EMBO J , vol.15 , pp. 6335-6347
    • Szczelkun, M.D.1    Dillingham, M.S.2    Janscak, P.3    Firman, K.4    Halford, S.E.5
  • 61
    • 0022381905 scopus 로고
    • Facilitated diffusion during catalysis by EcoRI endonuclease
    • Terry BJ, Jack WE, Modrich P (1985) Facilitated diffusion during catalysis by EcoRI endonuclease. J Biol Chem 260:13130-13137
    • (1985) J Biol Chem , vol.260 , pp. 13130-13137
    • Terry, B.J.1    Jack, W.E.2    Modrich, P.3
  • 62
    • 0031008221 scopus 로고    scopus 로고
    • Basic mechanisms of transcript elongation and its regulation
    • Uptain SM, Kane CM, Chamberlin MJ (1997) Basic mechanisms of transcript elongation and its regulation. Annu Rev Biochem 66:117-172
    • (1997) Annu Rev Biochem , vol.66 , pp. 117-172
    • Uptain, S.M.1    Kane, C.M.2    Chamberlin, M.J.3
  • 64
    • 0024531901 scopus 로고
    • Facilitated target location in biological systems
    • von Hippel PH, Berg OG (1989) Facilitated target location in biological systems. J Biol Chem 264:675-678
    • (1989) J Biol Chem , vol.264 , pp. 675-678
    • Von Hippel, P.H.1    Berg, O.G.2
  • 66
    • 0029965714 scopus 로고    scopus 로고
    • Restriction by EcoKI is enhanced by co-operative interactions between target sequences and is dependent on DEAD box motifs
    • Webb JL, King G, Ternet D, Titheradge AJB, Murray NE (1996) Restriction by EcoKI is enhanced by co-operative interactions between target sequences and is dependent on DEAD box motifs. EMBO J 15:2003-2009
    • (1996) EMBO J , vol.15 , pp. 2003-2009
    • Webb, J.L.1    King, G.2    Ternet, D.3    Titheradge, A.J.B.4    Murray, N.E.5
  • 67
    • 0019867850 scopus 로고
    • Diffusion-driven mechanisms of protein translocation on nucleic acids. 3. The Escherichia coli lac repressor-operator interaction: Kinetic measurements and conclusions
    • Winter RB, Berg OG, von Hippel PH (1981) Diffusion-driven mechanisms of protein translocation on nucleic acids. 3. The Escherichia coli lac repressor-operator interaction: kinetic measurements and conclusions. Biochemistry 20:6961-6977
    • (1981) Biochemistry , vol.20 , pp. 6961-6977
    • Winter, R.B.1    Berg, O.G.2    Von Hippel, P.H.3
  • 69
    • 0029160260 scopus 로고
    • T7 RNA polymerase bypass of large gaps on the template strand reveals a critical role of the nontemplate strand in elongation
    • Zhou W, Reines D, Doetsch PW (1995) T7 RNA polymerase bypass of large gaps on the template strand reveals a critical role of the nontemplate strand in elongation. Cell 82:577-585
    • (1995) Cell , vol.82 , pp. 577-585
    • Zhou, W.1    Reines, D.2    Doetsch, P.W.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.