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Volumn 475, Issue C, 2010, Pages 591-623

Analysis of Single Nucleic Acid Molecules with Protein Nanopores

Author keywords

[No Author keywords available]

Indexed keywords

DOUBLE STRANDED DNA; NUCLEIC ACID; POTASSIUM CHLORIDE; SINGLE STRANDED DNA; SINGLE STRANDED RNA; PROTEIN;

EID: 77954602645     PISSN: 00766879     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S0076-6879(10)75022-9     Document Type: Chapter
Times cited : (108)

References (83)
  • 1
    • 0032762996 scopus 로고    scopus 로고
    • Microsecond time-scale discrimination among polycytidylic acid, polyadenylic acid and polyuridylic acid as homopolymers or as segments within single RNA molecules
    • Akeson M., Branton D., Kasianowicz J.J., Brandin E., Deamer D.W. Microsecond time-scale discrimination among polycytidylic acid, polyadenylic acid and polyuridylic acid as homopolymers or as segments within single RNA molecules. Biophys. J. 1999, 77:3227-3233.
    • (1999) Biophys. J. , vol.77 , pp. 3227-3233
    • Akeson, M.1    Branton, D.2    Kasianowicz, J.J.3    Brandin, E.4    Deamer, D.W.5
  • 2
    • 14844290867 scopus 로고    scopus 로고
    • Recognizing a single base in an individual DNA strand: A step toward nanopore DNA sequencing
    • Ashkenasy N., Sánchez-Quesada J., Bayley H., Ghadiri M.R. Recognizing a single base in an individual DNA strand: A step toward nanopore DNA sequencing. Angew. Chem. Int. Ed. Engl. 2005, 44:1401-1404.
    • (2005) Angew. Chem. Int. Ed. Engl. , vol.44 , pp. 1401-1404
    • Ashkenasy, N.1    Sánchez-Quesada, J.2    Bayley, H.3    Ghadiri, M.R.4
  • 3
    • 35648976000 scopus 로고    scopus 로고
    • Stochastic detection of motor protein-RNA complexes by single-channel current recording
    • Astier Y., Kainov D.E., Bayley H., Tuma R., Howorka S. Stochastic detection of motor protein-RNA complexes by single-channel current recording. ChemPhysChem 2007, 8:2189-2194.
    • (2007) ChemPhysChem , vol.8 , pp. 2189-2194
    • Astier, Y.1    Kainov, D.E.2    Bayley, H.3    Tuma, R.4    Howorka, S.5
  • 4
    • 33751414735 scopus 로고    scopus 로고
    • Sequencing single molecules of DNA
    • Bayley H. Sequencing single molecules of DNA. Curr. Opin. Chem. Biol. 2006, 10:628-637.
    • (2006) Curr. Opin. Chem. Biol. , vol.10 , pp. 628-637
    • Bayley, H.1
  • 5
    • 0035855827 scopus 로고    scopus 로고
    • Stochastic sensors inspired by biology
    • Bayley H., Cremer P.S. Stochastic sensors inspired by biology. Nature 2001, 413:226-230.
    • (2001) Nature , vol.413 , pp. 226-230
    • Bayley, H.1    Cremer, P.S.2
  • 7
    • 44349108149 scopus 로고    scopus 로고
    • Single-molecule covalent chemistry in a protein nanoreactor
    • Springer, Heidelberg, R. Rigler, H. Vogel (Eds.)
    • Bayley H., Luchian T., Shin S.-H., Steffensen M.B. Single-molecule covalent chemistry in a protein nanoreactor. Single Molecules and Nanotechnology 2008, 251-277. Springer, Heidelberg. R. Rigler, H. Vogel (Eds.).
    • (2008) Single Molecules and Nanotechnology , pp. 251-277
    • Bayley, H.1    Luchian, T.2    Shin, S.-H.3    Steffensen, M.B.4
  • 8
    • 0000067560 scopus 로고
    • Current noise reveals protonation kinetics and number of ionizable sites in an open protein ion channel
    • Bezrukov S.M., Kasianowicz J.J. Current noise reveals protonation kinetics and number of ionizable sites in an open protein ion channel. Phys. Rev. Lett. 1993, 70:2352-2355.
    • (1993) Phys. Rev. Lett. , vol.70 , pp. 2352-2355
    • Bezrukov, S.M.1    Kasianowicz, J.J.2
  • 9
    • 77955095800 scopus 로고
    • Staphylococcal α-toxin: Oligomerization of hydrophilic monomers to form amphiphilic hexamers induced through contact with deoxycholate micelles
    • Bhakdi S., Füssle R., Tranum-Jensen J. Staphylococcal α-toxin: Oligomerization of hydrophilic monomers to form amphiphilic hexamers induced through contact with deoxycholate micelles. Proc. Natl. Acad. Sci. USA 1981, 78:5475-5479.
    • (1981) Proc. Natl. Acad. Sci. USA , vol.78 , pp. 5475-5479
    • Bhakdi, S.1    Füssle, R.2    Tranum-Jensen, J.3
  • 12
    • 36049035070 scopus 로고    scopus 로고
    • Ionic current blockades from DNA and RNA molecules in the alpha-hemolysin nanopore
    • Butler T.Z., Gundlach J.H., Troll M. Ionic current blockades from DNA and RNA molecules in the alpha-hemolysin nanopore. Biophys. J. 2007, 93:3229-3240.
    • (2007) Biophys. J. , vol.93 , pp. 3229-3240
    • Butler, T.Z.1    Gundlach, J.H.2    Troll, M.3
  • 14
    • 0031404458 scopus 로고    scopus 로고
    • Spontaneous oligomerization of a staphylococcal α-hemolysin conformationally constrained by removal of residues that form the transmembrane β barrel
    • Cheley S., Malghani M.S., Song L., Hobaugh M., Gouaux J.E., Yang J., Bayley H. Spontaneous oligomerization of a staphylococcal α-hemolysin conformationally constrained by removal of residues that form the transmembrane β barrel. Protein Eng. 1997, 10:1433-1443.
    • (1997) Protein Eng. , vol.10 , pp. 1433-1443
    • Cheley, S.1    Malghani, M.S.2    Song, L.3    Hobaugh, M.4    Gouaux, J.E.5    Yang, J.6    Bayley, H.7
  • 15
    • 0032993061 scopus 로고    scopus 로고
    • A functional protein pore with a "retro" transmembrane domain
    • Cheley S., Braha O., Lu X., Conlan S., Bayley H. A functional protein pore with a "retro" transmembrane domain. Protein Sci. 1999, 8:1257-1267.
    • (1999) Protein Sci. , vol.8 , pp. 1257-1267
    • Cheley, S.1    Braha, O.2    Lu, X.3    Conlan, S.4    Bayley, H.5
  • 16
    • 0035989992 scopus 로고    scopus 로고
    • Stochastic sensing of nanomolar inositol 1,4,5-trisphosphate with an engineered pore
    • Cheley S., Gu L.-Q., Bayley H. Stochastic sensing of nanomolar inositol 1,4,5-trisphosphate with an engineered pore. Chem. Biol. 2002, 9:829-838.
    • (2002) Chem. Biol. , vol.9 , pp. 829-838
    • Cheley, S.1    Gu, L.-Q.2    Bayley, H.3
  • 17
    • 0026654006 scopus 로고
    • Solubilization in formamide protects RNA from degradation
    • Chomczynski P. Solubilization in formamide protects RNA from degradation. Nucleic Acids Res. 1992, 20:3791-3792.
    • (1992) Nucleic Acids Res. , vol.20 , pp. 3791-3792
    • Chomczynski, P.1
  • 18
  • 19
    • 38349169632 scopus 로고    scopus 로고
    • A single-molecule nanopore device detects DNA polymerase activity with single-nucleotide resolution
    • Cockroft S.L., Chu J., Amorin M., Ghadiri M.R. A single-molecule nanopore device detects DNA polymerase activity with single-nucleotide resolution. J. Am. Chem. Soc. 2008, 130:818-820.
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 818-820
    • Cockroft, S.L.1    Chu, J.2    Amorin, M.3    Ghadiri, M.R.4
  • 20
    • 0036797062 scopus 로고    scopus 로고
    • Characterization of nucleic acids by nanopore analysis
    • Deamer D.W., Branton D. Characterization of nucleic acids by nanopore analysis. Acc. Chem. Res. 2002, 35:817-825.
    • (2002) Acc. Chem. Res. , vol.35 , pp. 817-825
    • Deamer, D.W.1    Branton, D.2
  • 21
    • 34248351114 scopus 로고    scopus 로고
    • Solid-state nanopores
    • Dekker C. Solid-state nanopores. Nat. Nanotechnol. 2007, 2:209-215.
    • (2007) Nat. Nanotechnol. , vol.2 , pp. 209-215
    • Dekker, C.1
  • 22
    • 34250356054 scopus 로고    scopus 로고
    • Extracting kinetics from single-molecule force spectroscopy: Nanopore unzipping of DNA hairpins
    • Dudko O.K., Mathe J., Szabo A., Meller A., Hummer G. Extracting kinetics from single-molecule force spectroscopy: Nanopore unzipping of DNA hairpins. Biophys. J. 2007, 92:4188-4195.
    • (2007) Biophys. J. , vol.92 , pp. 4188-4195
    • Dudko, O.K.1    Mathe, J.2    Szabo, A.3    Meller, A.4    Hummer, G.5
  • 24
    • 0033798636 scopus 로고    scopus 로고
    • Interaction of the non-covalent molecular adapter, b-cyclodextrin, with the staphylococcal α-hemolysin pore
    • Gu L.Q., Bayley H. Interaction of the non-covalent molecular adapter, b-cyclodextrin, with the staphylococcal α-hemolysin pore. Biophys. J. 2000, 79:1967-1975.
    • (2000) Biophys. J. , vol.79 , pp. 1967-1975
    • Gu, L.Q.1    Bayley, H.2
  • 25
    • 0035169385 scopus 로고    scopus 로고
    • Prolonged residence time of a noncovalent molecular adapter, β-cyclodextrin, within the lumen of mutant α-hemolysin pores
    • Gu L.Q., Cheley S., Bayley H. Prolonged residence time of a noncovalent molecular adapter, β-cyclodextrin, within the lumen of mutant α-hemolysin pores. J. Gen. Physiol. 2001, 118:481-494.
    • (2001) J. Gen. Physiol. , vol.118 , pp. 481-494
    • Gu, L.Q.1    Cheley, S.2    Bayley, H.3
  • 28
    • 18644374474 scopus 로고    scopus 로고
    • Direct introduction of single protein channels and pores into lipid bilayers
    • Holden M.A., Bayley H. Direct introduction of single protein channels and pores into lipid bilayers. J. Am. Chem. Soc. 2005, 127:6502-6503.
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 6502-6503
    • Holden, M.A.1    Bayley, H.2
  • 29
    • 33646869929 scopus 로고    scopus 로고
    • Direct transfer of membrane proteins from bacteria to planar bilayers for rapid screening by single-channel recording
    • Holden M.A., Jayasinghe L., Daltrop O., Mason A., Bayley H. Direct transfer of membrane proteins from bacteria to planar bilayers for rapid screening by single-channel recording. Nat. Chem. Biol. 2006, 2:314-318.
    • (2006) Nat. Chem. Biol. , vol.2 , pp. 314-318
    • Holden, M.A.1    Jayasinghe, L.2    Daltrop, O.3    Mason, A.4    Bayley, H.5
  • 31
    • 0034930381 scopus 로고    scopus 로고
    • Sequence-specific detection of individual DNA strands using engineered nanopores
    • Howorka S., Cheley S., Bayley H. Sequence-specific detection of individual DNA strands using engineered nanopores. Nat. Biotechnol. 2001, 19:636-639.
    • (2001) Nat. Biotechnol. , vol.19 , pp. 636-639
    • Howorka, S.1    Cheley, S.2    Bayley, H.3
  • 32
    • 0034738622 scopus 로고    scopus 로고
    • Order-disorder transition in bilayers of diphytanoyl phosphatidylcholine
    • Hung W.C., Chen F.Y., Huang H.W. Order-disorder transition in bilayers of diphytanoyl phosphatidylcholine. Biochim. Biophys. Acta 2000, 1467:198-206.
    • (2000) Biochim. Biophys. Acta , vol.1467 , pp. 198-206
    • Hung, W.C.1    Chen, F.Y.2    Huang, H.W.3
  • 33
    • 77952269618 scopus 로고    scopus 로고
    • Urea facilitates the translocation of single-stranded DNA and RNA through the α-hemolysin nanopore
    • Japrung D., Henricus M., Li Q., Maglia G., Bayley H. Urea facilitates the translocation of single-stranded DNA and RNA through the α-hemolysin nanopore. Biophys. J. 2010, 98:1856-1863.
    • (2010) Biophys. J. , vol.98 , pp. 1856-1863
    • Japrung, D.1    Henricus, M.2    Li, Q.3    Maglia, G.4    Bayley, H.5
  • 34
    • 0027247995 scopus 로고
    • Membrane area and electrical capacitance
    • Kado R.T. Membrane area and electrical capacitance. Methods Enzymol. 1993, 221:273-299.
    • (1993) Methods Enzymol. , vol.221 , pp. 273-299
    • Kado, R.T.1
  • 35
    • 0031313776 scopus 로고    scopus 로고
    • Novel DNA detection system of flow injection analysis (2). The distinctive properties of a novel system employing PNA (peptide nucleic acid) as a probe for specific DNA detection
    • Kai E., Sawata S., Ikebukuro K., Iida T., Honda T., Karube I. Novel DNA detection system of flow injection analysis (2). The distinctive properties of a novel system employing PNA (peptide nucleic acid) as a probe for specific DNA detection. Nucleic Acids Symp. Ser. 1997, 321-322.
    • (1997) Nucleic Acids Symp. Ser. , pp. 321-322
    • Kai, E.1    Sawata, S.2    Ikebukuro, K.3    Iida, T.4    Honda, T.5    Karube, I.6
  • 36
    • 16244372752 scopus 로고    scopus 로고
    • Single protein pores containing molecular adapters at high temperatures
    • Kang X., Gu L.-Q., Cheley S., Bayley H. Single protein pores containing molecular adapters at high temperatures. Angew. Chem. Int. Ed. Engl. 2005, 44:1495-1499.
    • (2005) Angew. Chem. Int. Ed. Engl. , vol.44 , pp. 1495-1499
    • Kang, X.1    Gu, L.-Q.2    Cheley, S.3    Bayley, H.4
  • 37
    • 0030465241 scopus 로고    scopus 로고
    • Characterization of individual polynucleotide molecules using a membrane channel
    • Kasianowicz J.J., Brandin E., Branton D., Deamer D.W. Characterization of individual polynucleotide molecules using a membrane channel. Proc. Natl. Acad. Sci. USA 1996, 93:13770-13773.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 13770-13773
    • Kasianowicz, J.J.1    Brandin, E.2    Branton, D.3    Deamer, D.W.4
  • 38
    • 60849133617 scopus 로고    scopus 로고
    • Controlling the translocation of single-stranded DNA through alpha-hemolysin ion channels using viscosity
    • Kawano R., Schibel A.E., Cauley C., White H.S. Controlling the translocation of single-stranded DNA through alpha-hemolysin ion channels using viscosity. Langmuir 2009, 25:1233-1237.
    • (2009) Langmuir , vol.25 , pp. 1233-1237
    • Kawano, R.1    Schibel, A.E.2    Cauley, C.3    White, H.S.4
  • 41
    • 0015236713 scopus 로고
    • Freezing and melting of lipid bilayers and the mode of action of nonactin, valinomycin, and gramidicin
    • Krasne S., Eisenman G., Szabo G. Freezing and melting of lipid bilayers and the mode of action of nonactin, valinomycin, and gramidicin. Science 1971, 174:412-415.
    • (1971) Science , vol.174 , pp. 412-415
    • Krasne, S.1    Eisenman, G.2    Szabo, G.3
  • 42
    • 0018386941 scopus 로고
    • Physicochemical characterization of 1,2-diphytanoyl-sn-glycero-3-phosphocholine in model membrane systems
    • Lindsey H., Petersen N.O., Chan S.I. Physicochemical characterization of 1,2-diphytanoyl-sn-glycero-3-phosphocholine in model membrane systems. Biochim. Biophys. Acta 1979, 555:147-167.
    • (1979) Biochim. Biophys. Acta , vol.555 , pp. 147-167
    • Lindsey, H.1    Petersen, N.O.2    Chan, S.I.3
  • 43
    • 58149402384 scopus 로고    scopus 로고
    • Enhanced translocation of single DNA molecules through α-hemolysin nanopores by manipulation of internal charge
    • Maglia G., Rincon Restrepo M., Mikhailova E., Bayley H. Enhanced translocation of single DNA molecules through α-hemolysin nanopores by manipulation of internal charge. Proc. Natl. Acad. Sci. USA 2008, 105:19720-19725.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 19720-19725
    • Maglia, G.1    Rincon Restrepo, M.2    Mikhailova, E.3    Bayley, H.4
  • 45
    • 72849121810 scopus 로고    scopus 로고
    • DNA strands from denatured duplexes are translocated through engineered protein nanopores at alkaline pH
    • Maglia M., Henricus M., Wyss R., Li Q., Cheley S., Bayley H. DNA strands from denatured duplexes are translocated through engineered protein nanopores at alkaline pH. Nano Lett. 2009, 9:3831-3836.
    • (2009) Nano Lett. , vol.9 , pp. 3831-3836
    • Maglia, M.1    Henricus, M.2    Wyss, R.3    Li, Q.4    Cheley, S.5    Bayley, H.6
  • 47
    • 0141819130 scopus 로고    scopus 로고
    • Microfabricated teflon membranes for low-noise recordings of ion channels in planar lipid bilayers
    • Mayer M., Kriebel J.K., Tosteson M.T., Whitesides G.M. Microfabricated teflon membranes for low-noise recordings of ion channels in planar lipid bilayers. Biophys. J. 2003, 85:2684-2695.
    • (2003) Biophys. J. , vol.85 , pp. 2684-2695
    • Mayer, M.1    Kriebel, J.K.2    Tosteson, M.T.3    Whitesides, G.M.4
  • 48
    • 0037855911 scopus 로고    scopus 로고
    • Dynamics of polynucleotide transport through nanometre-scale pores
    • Meller A. Dynamics of polynucleotide transport through nanometre-scale pores. J. Phys.: Condens. Matter 2003, 15:R581-R607.
    • (2003) J. Phys.: Condens. Matter , vol.15
    • Meller, A.1
  • 49
    • 0036674122 scopus 로고    scopus 로고
    • Single molecule measurements of DNA transport through a nanopore
    • Meller A., Branton D. Single molecule measurements of DNA transport through a nanopore. Electrophoresis 2002, 23:2583-2591.
    • (2002) Electrophoresis , vol.23 , pp. 2583-2591
    • Meller, A.1    Branton, D.2
  • 51
    • 0035831563 scopus 로고    scopus 로고
    • Voltage-driven DNA translocations through a nanopore
    • Meller A., Nivon L., Branton D. Voltage-driven DNA translocations through a nanopore. Phys. Rev. Lett. 2001, 86:3435-3438.
    • (2001) Phys. Rev. Lett. , vol.86 , pp. 3435-3438
    • Meller, A.1    Nivon, L.2    Branton, D.3
  • 52
    • 0036081266 scopus 로고    scopus 로고
    • Properties of Bacillus cereus hemolysin II: A heptameric transmembrane pore
    • Miles G., Bayley H., Cheley S. Properties of Bacillus cereus hemolysin II: A heptameric transmembrane pore. Protein Sci. 2002, 11:1813-1824.
    • (2002) Protein Sci. , vol.11 , pp. 1813-1824
    • Miles, G.1    Bayley, H.2    Cheley, S.3
  • 53
    • 0004068272 scopus 로고
    • Plenum, New York, C. Miller (Ed.)
    • Ion Channel Reconstitution 1986, Plenum, New York. C. Miller (Ed.).
    • (1986) Ion Channel Reconstitution
  • 54
    • 49649084921 scopus 로고    scopus 로고
    • Chemical tags facilitate the sensing of individual DNA strands with nanopores
    • Mitchell N., Howorka S. Chemical tags facilitate the sensing of individual DNA strands with nanopores. Angew. Chem. Int. Ed. Engl. 2008, 47:5565-5568.
    • (2008) Angew. Chem. Int. Ed. Engl. , vol.47 , pp. 5565-5568
    • Mitchell, N.1    Howorka, S.2
  • 55
    • 0015459562 scopus 로고
    • Formation of bimolecular membranes from lipid monolayers and study of their electrical properties
    • Montal M., Mueller P. Formation of bimolecular membranes from lipid monolayers and study of their electrical properties. Proc. Natl. Acad. Sci. USA 1972, 69:3561-3566.
    • (1972) Proc. Natl. Acad. Sci. USA , vol.69 , pp. 3561-3566
    • Montal, M.1    Mueller, P.2
  • 57
    • 0036672773 scopus 로고    scopus 로고
    • Evaluation of nanopores as candidates for electronic analyte detection
    • Nakane J., Akeson M., Marziali A. Evaluation of nanopores as candidates for electronic analyte detection. Electrophoresis 2002, 23:2592-2601.
    • (2002) Electrophoresis , vol.23 , pp. 2592-2601
    • Nakane, J.1    Akeson, M.2    Marziali, A.3
  • 58
    • 3042736845 scopus 로고    scopus 로고
    • A nanosensor for transmembrane capture and identification of single nucleic acid molecules
    • Nakane J., Wiggin M., Marziali A. A nanosensor for transmembrane capture and identification of single nucleic acid molecules. Biophys. J. 2004, 87:615-621.
    • (2004) Biophys. J. , vol.87 , pp. 615-621
    • Nakane, J.1    Wiggin, M.2    Marziali, A.3
  • 59
    • 0023974755 scopus 로고
    • Planar bilayer membranes made from phospholipid monolayers form by a thinning process
    • Niles W.D., Levis R.A., Cohen F.S. Planar bilayer membranes made from phospholipid monolayers form by a thinning process. Biophys. J. 1988, 53:327-335.
    • (1988) Biophys. J. , vol.53 , pp. 327-335
    • Niles, W.D.1    Levis, R.A.2    Cohen, F.S.3
  • 61
    • 79051469797 scopus 로고    scopus 로고
    • Effect of screening on the transport of polyelectrolytes through nanopores
    • (1-5)
    • Oukhaled G., Bacri L., Mathé J., Pelta J., Auvray L. Effect of screening on the transport of polyelectrolytes through nanopores. Europhys. Lett. 2008, 82:48003. (1-5).
    • (2008) Europhys. Lett. , vol.82 , pp. 48003
    • Oukhaled, G.1    Bacri, L.2    Mathé, J.3    Pelta, J.4    Auvray, L.5
  • 62
    • 0029814699 scopus 로고    scopus 로고
    • Rapid preparation of single stranded DNA from PCR products by streptavidin induced electrophoretic mobility shift
    • Pagratis N.C. Rapid preparation of single stranded DNA from PCR products by streptavidin induced electrophoretic mobility shift. Nucleic Acids Res. 1996, 24:3645-3646.
    • (1996) Nucleic Acids Res. , vol.24 , pp. 3645-3646
    • Pagratis, N.C.1
  • 63
    • 65549111370 scopus 로고    scopus 로고
    • Reverse DNA translocation through a solid-state nanopore by magnetic tweezers
    • Peng H., Ling X.S. Reverse DNA translocation through a solid-state nanopore by magnetic tweezers. Nanotechnology 2009, 20:185101.
    • (2009) Nanotechnology , vol.20 , pp. 185101
    • Peng, H.1    Ling, X.S.2
  • 65
    • 66249083118 scopus 로고    scopus 로고
    • Emerging roles for lipids in shaping membrane-protein function
    • Phillips R., Ursell T., Wiggins P., Sens P. Emerging roles for lipids in shaping membrane-protein function. Nature 2009, 459:379-385.
    • (2009) Nature , vol.459 , pp. 379-385
    • Phillips, R.1    Ursell, T.2    Wiggins, P.3    Sens, P.4
  • 66
    • 54549099396 scopus 로고    scopus 로고
    • Nucleotide identification and orientation discrimination of DNA homopolymers immobilized in a protein nanopore
    • Purnell R.F., Mehta K.K., Schmidt J.J. Nucleotide identification and orientation discrimination of DNA homopolymers immobilized in a protein nanopore. Nano Lett. 2008, 9:3029-3034.
    • (2008) Nano Lett. , vol.9 , pp. 3029-3034
    • Purnell, R.F.1    Mehta, K.K.2    Schmidt, J.J.3
  • 67
    • 70349527955 scopus 로고    scopus 로고
    • Discrimination of single base substitutions in a DNA strand immobilized in a biological nanopore
    • Purnell R.F., Schmidt J.J. Discrimination of single base substitutions in a DNA strand immobilized in a biological nanopore. ACS Nano 2009, 3:2533-2538.
    • (2009) ACS Nano , vol.3 , pp. 2533-2538
    • Purnell, R.F.1    Schmidt, J.J.2
  • 69
    • 33947105421 scopus 로고    scopus 로고
    • Nanopore sequencing technology: Nanopore preparations
    • Rhee M., Burns M.A. Nanopore sequencing technology: Nanopore preparations. Trends Biotechnol. 2007, 25:174-181.
    • (2007) Trends Biotechnol. , vol.25 , pp. 174-181
    • Rhee, M.1    Burns, M.A.2
  • 70
    • 84942547356 scopus 로고    scopus 로고
    • Controlled translocation of single DNA molecules through engineered protein nanopores. In preparation
    • Rincon-Restrepo, M., Mikhailova, E., Bayley, H., and Maglia, G. Controlled translocation of single DNA molecules through engineered protein nanopores. In preparation.
    • Rincon-Restrepo, M.1    Mikhailova, E.2    Bayley, H.3    Maglia, G.4
  • 72
    • 0027324923 scopus 로고
    • Direct sequencing of single primer PCR products: A rapid method to achieve short chromosomal walks
    • Screaton G.R., Bangham C.R., Bell J.I. Direct sequencing of single primer PCR products: A rapid method to achieve short chromosomal walks. Nucleic Acids Res. 1993, 21:2263-2264.
    • (1993) Nucleic Acids Res. , vol.21 , pp. 2263-2264
    • Screaton, G.R.1    Bangham, C.R.2    Bell, J.I.3
  • 73
    • 34548821873 scopus 로고    scopus 로고
    • Developing synthetic conical nanopores for biosensing applications
    • Sexton L.T., Horne L.P., Martin C.R. Developing synthetic conical nanopores for biosensing applications. Mol. BioSyst. 2007, 3:667-685.
    • (2007) Mol. BioSyst. , vol.3 , pp. 667-685
    • Sexton, L.T.1    Horne, L.P.2    Martin, C.R.3
  • 74
    • 0027517912 scopus 로고
    • Preventing errors when estimating single channel properties from the analysis of current fluctuations
    • Silberberg S.D., Magleby K.L. Preventing errors when estimating single channel properties from the analysis of current fluctuations. Biophys. J. 1993, 65:1570-1584.
    • (1993) Biophys. J. , vol.65 , pp. 1570-1584
    • Silberberg, S.D.1    Magleby, K.L.2
  • 75
    • 0030447720 scopus 로고    scopus 로고
    • Structure of staphylococcal α-hemolysin, a heptameric transmembrane pore
    • Song L., Hobaugh M.R., Shustak C., Cheley S., Bayley H., Gouaux J.E. Structure of staphylococcal α-hemolysin, a heptameric transmembrane pore. Science 1996, 274:1859-1865.
    • (1996) Science , vol.274 , pp. 1859-1865
    • Song, L.1    Hobaugh, M.R.2    Shustak, C.3    Cheley, S.4    Bayley, H.5    Gouaux, J.E.6
  • 76
    • 66049132042 scopus 로고    scopus 로고
    • Single nucleotide discrimination in immobilized DNA oligonucleotides with a biological nanopore
    • Stoddart D., Heron A., Mikhailova E., Maglia G., Bayley H. Single nucleotide discrimination in immobilized DNA oligonucleotides with a biological nanopore. Proc. Natl. Acad. Sci. USA 2009, 106:7702-7707.
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 7702-7707
    • Stoddart, D.1    Heron, A.2    Mikhailova, E.3    Maglia, G.4    Bayley, H.5
  • 77
    • 74549164354 scopus 로고    scopus 로고
    • Multiple base-recognition sites in a biological nanopore-Two heads are better than one
    • Stoddart D., Maglia G., Mikhailova E., Heron A., Bayley H. Multiple base-recognition sites in a biological nanopore-Two heads are better than one. Angew. Chem. Int. Ed. 2010, 49:556-559.
    • (2010) Angew. Chem. Int. Ed. , vol.49 , pp. 556-559
    • Stoddart, D.1    Maglia, G.2    Mikhailova, E.3    Heron, A.4    Bayley, H.5
  • 78
    • 0021844629 scopus 로고
    • Secondary structure and assembly mechanism of an oligomeric channel protein
    • Tobkes N., Wallace B.A., Bayley H. Secondary structure and assembly mechanism of an oligomeric channel protein. Biochemistry 1985, 24:1915-1920.
    • (1985) Biochemistry , vol.24 , pp. 1915-1920
    • Tobkes, N.1    Wallace, B.A.2    Bayley, H.3
  • 79
    • 0035107270 scopus 로고    scopus 로고
    • Rapid discrimination among individual DNA hairpin molecules at single-nucleotide resolution using an ion channel
    • Vercoutere W., Winters-Hilt S., Olsen H., Deamer D., Haussler D., Akeson M. Rapid discrimination among individual DNA hairpin molecules at single-nucleotide resolution using an ion channel. Nat. Biotechnol. 2001, 19:248-252.
    • (2001) Nat. Biotechnol. , vol.19 , pp. 248-252
    • Vercoutere, W.1    Winters-Hilt, S.2    Olsen, H.3    Deamer, D.4    Haussler, D.5    Akeson, M.6
  • 80
    • 0016664317 scopus 로고
    • Phase transitions in planar bilayer membranes
    • White S. Phase transitions in planar bilayer membranes. Biophys. J. 1975, 15:95-117.
    • (1975) Biophys. J. , vol.15 , pp. 95-117
    • White, S.1
  • 82
    • 0017064880 scopus 로고
    • Formation of planar bilayer membranes from lipid monolayers. A critique
    • White S.H., Petersen D.C., Simon S., Yafuso M. Formation of planar bilayer membranes from lipid monolayers. A critique. Biophys. J. 1976, 16:481-489.
    • (1976) Biophys. J. , vol.16 , pp. 481-489
    • White, S.H.1    Petersen, D.C.2    Simon, S.3    Yafuso, M.4
  • 83
    • 0025062857 scopus 로고
    • Optimizing planar lipid bilayer single-channel recordings for high resolution with rapid voltage steps
    • Wonderlin W.F., Finkel A., French R.J. Optimizing planar lipid bilayer single-channel recordings for high resolution with rapid voltage steps. Biophys. J. 1990, 58:289-294.
    • (1990) Biophys. J. , vol.58 , pp. 289-294
    • Wonderlin, W.F.1    Finkel, A.2    French, R.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.