메뉴 건너뛰기




Volumn 7, Issue 4, 2013, Pages 3341-3350

Erratum: Sampling a biomarker of the human immunodeficiency virus across a synthetic nanopore (ACS Nano (2013) 7 DOI: 10.1021/nn400125c);Sampling a biomarker of the human immunodeficiency virus across a synthetic nanopore

Author keywords

biosensors; chemical kinetics; nanobiotechnology; protein RNA interactions; single channel electrical recordings; single molecule detection

Indexed keywords

BINDING ENERGY; BIOMARKERS; BIOMEDICAL ENGINEERING; BIOSENSORS; CHEMICAL DETECTION; DISSOCIATION; NANOBIOTECHNOLOGY; NANOPORES; PROTEINS; REACTION KINETICS; RNA; SILICON NITRIDE; VIRUSES;

EID: 84876546704     PISSN: 19360851     EISSN: 1936086X     Source Type: Journal    
DOI: 10.1021/nn401345w     Document Type: Erratum
Times cited : (61)

References (67)
  • 1
    • 0034050876 scopus 로고    scopus 로고
    • Ion Channels as Molecular Coulter Counters to Probe Metabolite Transport
    • Bezrukov, S. M. Ion Channels as Molecular Coulter Counters To Probe Metabolite Transport J. Membr. Biol. 2000, 174, 1-13
    • (2000) J. Membr. Biol. , vol.174 , pp. 1-13
    • Bezrukov, S.M.1
  • 2
    • 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
  • 3
    • 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
  • 4
    • 42149194233 scopus 로고    scopus 로고
    • Squeezing a Single Polypeptide through a Nanopore
    • Movileanu, L. Squeezing a Single Polypeptide through a Nanopore Soft Matter 2008, 4, 925-931
    • (2008) Soft Matter , vol.4 , pp. 925-931
    • Movileanu, L.1
  • 6
    • 65549134365 scopus 로고    scopus 로고
    • Interrogating Single Proteins through Nanopores: Challenges and Opportunities
    • Movileanu, L. Interrogating Single Proteins through Nanopores: Challenges and Opportunities Trends Biotechnol. 2009, 27, 333-341
    • (2009) Trends Biotechnol. , vol.27 , pp. 333-341
    • Movileanu, L.1
  • 7
    • 77249128977 scopus 로고    scopus 로고
    • Single Molecule Sensing by Nanopores and Nanopore Devices
    • Gu, L. Q.; Shim, J. W. Single Molecule Sensing by Nanopores and Nanopore Devices Analyst 2010, 135, 441-451
    • (2010) Analyst , vol.135 , pp. 441-451
    • Gu, L.Q.1    Shim, J.W.2
  • 11
    • 41149181242 scopus 로고    scopus 로고
    • Controlling a Single Protein in a Nanopore through Electrostatic Traps
    • Mohammad, M. M.; Prakash, S.; Matouschek, A.; Movileanu, L. Controlling a Single Protein in a Nanopore through Electrostatic Traps J. Am. Chem. Soc. 2008, 130, 4081-4088
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 4081-4088
    • Mohammad, M.M.1    Prakash, S.2    Matouschek, A.3    Movileanu, L.4
  • 12
    • 45849114386 scopus 로고    scopus 로고
    • Excursion of a Single Polypeptide into a Protein Pore: Simple Physics, but Complicated Biology
    • Mohammad, M. M.; Movileanu, L. Excursion of a Single Polypeptide into a Protein Pore: Simple Physics, but Complicated Biology Eur. Biophys. J. 2008, 37, 913-925
    • (2008) Eur. Biophys. J. , vol.37 , pp. 913-925
    • Mohammad, M.M.1    Movileanu, L.2
  • 15
    • 77951040294 scopus 로고    scopus 로고
    • Unraveling Single-Stranded DNA in a Solid-State Nanopore
    • Kowalczyk, S. W.; Tuijtel, M. W.; Donkers, S. P.; Dekker, C. Unraveling Single-Stranded DNA in a Solid-State Nanopore Nano Lett. 2010, 10, 1414-1420
    • (2010) Nano Lett. , vol.10 , pp. 1414-1420
    • Kowalczyk, S.W.1    Tuijtel, M.W.2    Donkers, S.P.3    Dekker, C.4
  • 21
    • 84859583528 scopus 로고    scopus 로고
    • Stochastic Sensing of Proteins with Receptor-Modified Solid-State Nanopores
    • Wei, R.; Gatterdam, V.; Wieneke, R.; Tampe, R.; Rant, U. Stochastic Sensing of Proteins with Receptor-Modified Solid-State Nanopores Nat. Nanotechnol. 2012, 7, 257-263
    • (2012) Nat. Nanotechnol. , vol.7 , pp. 257-263
    • Wei, R.1    Gatterdam, V.2    Wieneke, R.3    Tampe, R.4    Rant, U.5
  • 22
    • 50249133095 scopus 로고    scopus 로고
    • Encapsulating a Single G-Quadruplex Aptamer in a Protein Nanocavity
    • Shim, J. W.; Gu, L. Q. Encapsulating a Single G-Quadruplex Aptamer in a Protein Nanocavity J. Phys. Chem. B 2008, 112, 8354-8360
    • (2008) J. Phys. Chem. B , vol.112 , pp. 8354-8360
    • Shim, J.W.1    Gu, L.Q.2
  • 23
    • 63349095582 scopus 로고    scopus 로고
    • Single-Molecule Detection of Folding and Unfolding of the G-Quadruplex Aptamer in a Nanopore Nanocavity
    • Shim, J. W.; Tan, Q.; Gu, L. Q. Single-Molecule Detection of Folding and Unfolding of the G-Quadruplex Aptamer in a Nanopore Nanocavity Nucleic Acids Res. 2009, 37, 972-982
    • (2009) Nucleic Acids Res. , vol.37 , pp. 972-982
    • Shim, J.W.1    Tan, Q.2    Gu, L.Q.3
  • 24
    • 68849091326 scopus 로고    scopus 로고
    • Capturing Single Molecules of Immunoglobulin and Ricin with an Aptamer-Encoded Glass Nanopore
    • Ding, S.; Gao, C.; Gu, L. Q. Capturing Single Molecules of Immunoglobulin and Ricin with an Aptamer-Encoded Glass Nanopore Anal. Chem. 2009, 81, 6649-6655
    • (2009) Anal. Chem. , vol.81 , pp. 6649-6655
    • Ding, S.1    Gao, C.2    Gu, L.Q.3
  • 25
  • 27
  • 28
    • 84866309637 scopus 로고    scopus 로고
    • An Engineered ClyA Nanopore Detects Folded Target Proteins by Selective External Association and Pore Entry
    • Soskine, M.; Biesemans, A.; Moeyaert, B.; Cheley, S.; Bayley, H.; Maglia, G. An Engineered ClyA Nanopore Detects Folded Target Proteins by Selective External Association and Pore Entry Nano Lett. 2012, 12, 4895-4900
    • (2012) Nano Lett. , vol.12 , pp. 4895-4900
    • Soskine, M.1    Biesemans, A.2    Moeyaert, B.3    Cheley, S.4    Bayley, H.5    Maglia, G.6
  • 32
    • 77955377302 scopus 로고    scopus 로고
    • Single-Molecule Observation of Protein Adsorption onto an Inorganic Surface
    • Niedzwiecki, D. J.; Grazul, J.; Movileanu, L. Single-Molecule Observation of Protein Adsorption onto an Inorganic Surface J. Am. Chem. Soc. 2010, 132, 10816-10822
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 10816-10822
    • Niedzwiecki, D.J.1    Grazul, J.2    Movileanu, L.3
  • 33
    • 2242469712 scopus 로고    scopus 로고
    • Structure of the HIV-1 Nucleocapsid Protein Bound to the SL3 Ψ-RNA Recognition Element
    • De Guzman, R. N.; Wu, Z. R.; Stalling, C. C.; Pappalardo, L.; Borer, P. N.; Summers, M. F. Structure of the HIV-1 Nucleocapsid Protein Bound to the SL3 Ψ-RNA Recognition Element Science 1998, 279, 384-388
    • (1998) Science , vol.279 , pp. 384-388
    • De Guzman, R.N.1    Wu, Z.R.2    Stalling, C.C.3    Pappalardo, L.4    Borer, P.N.5    Summers, M.F.6
  • 34
    • 0025295654 scopus 로고
    • Retroviral RNA Packaging: Sequence Requirements and Implications
    • Linial, M. L.; Miller, A. D. Retroviral RNA Packaging: Sequence Requirements and Implications Curr. Top. Microbiol. Immunol. 1990, 157, 125-152
    • (1990) Curr. Top. Microbiol. Immunol. , vol.157 , pp. 125-152
    • Linial, M.L.1    Miller, A.D.2
  • 35
    • 77951674873 scopus 로고    scopus 로고
    • Effects of the Nature and Concentration of Salt on the Interaction of the HIV-1 Nucleocapsid Protein with SL3 RNA
    • Athavale, S. S.; Ouyang, W.; McPike, M. P.; Hudson, B. S.; Borer, P. N. Effects of the Nature and Concentration of Salt on the Interaction of the HIV-1 Nucleocapsid Protein with SL3 RNA Biochemistry 2010, 49, 3525-3533
    • (2010) Biochemistry , vol.49 , pp. 3525-3533
    • Athavale, S.S.1    Ouyang, W.2    McPike, M.P.3    Hudson, B.S.4    Borer, P.N.5
  • 36
    • 0037168488 scopus 로고    scopus 로고
    • Affinities of the Nucleocapsid Protein for Variants of SL3 RNA in HIV-1
    • Paoletti, A. C.; Shubsda, M. F.; Hudson, B. S.; Borer, P. N. Affinities of the Nucleocapsid Protein for Variants of SL3 RNA in HIV-1 Biochemistry 2002, 41, 15423-15428
    • (2002) Biochemistry , vol.41 , pp. 15423-15428
    • Paoletti, A.C.1    Shubsda, M.F.2    Hudson, B.S.3    Borer, P.N.4
  • 37
    • 0025647651 scopus 로고
    • Solid Phase Synthesis of the Retroviral Nucleocapsid Protein NCp10 of Moloney Murine Leukaemia Virus and Related "zinc-Fingers" in Free SH Forms. Influence of Zinc Chelation on Structural and Biochemical Properties
    • Cornille, F.; Mely, Y.; Ficheux, D.; Savignol, I.; Gerard, D.; Darlix, J. L.; Fournie-Zaluski, M. C.; Roques, B. P. Solid Phase Synthesis of the Retroviral Nucleocapsid Protein NCp10 of Moloney Murine Leukaemia Virus and Related "Zinc-Fingers" in Free SH Forms. Influence of Zinc Chelation on Structural and Biochemical Properties Int. J. Pept. Protein Res. 1990, 36, 551-558
    • (1990) Int. J. Pept. Protein Res. , vol.36 , pp. 551-558
    • Cornille, F.1    Mely, Y.2    Ficheux, D.3    Savignol, I.4    Gerard, D.5    Darlix, J.L.6    Fournie-Zaluski, M.C.7    Roques, B.P.8
  • 38
    • 0033593039 scopus 로고    scopus 로고
    • Nucleic Acid Sequence Discrimination by the HIV-1 Nucleocapsid Protein NCp7: A Fluorescence Study
    • Vuilleumier, C.; Bombarda, E.; Morellet, N.; Gerard, D.; Roques, B. P.; Mely, Y. Nucleic Acid Sequence Discrimination by the HIV-1 Nucleocapsid Protein NCp7: A Fluorescence Study Biochemistry 1999, 38, 16816-16825
    • (1999) Biochemistry , vol.38 , pp. 16816-16825
    • Vuilleumier, C.1    Bombarda, E.2    Morellet, N.3    Gerard, D.4    Roques, B.P.5    Mely, Y.6
  • 39
    • 0027077686 scopus 로고
    • Nucleocapsid Zinc Fingers Detected in Retroviruses: EXAFS Studies of Intact Viruses and the Solution-State Structure of the Nucleocapsid Protein from HIV-1
    • Summers, M. F.; Henderson, L. E.; Chance, M. R.; Bess, J. W., Jr.; South, T. L.; Blake, P. R.; Sagi, I.; Perez-Alvarado, G.; Sowder, R. C., III; Hare, D. R. Nucleocapsid Zinc Fingers Detected in Retroviruses: EXAFS Studies of Intact Viruses and the Solution-State Structure of the Nucleocapsid Protein from HIV-1 Protein Sci. 1992, 1, 563-574
    • (1992) Protein Sci. , vol.1 , pp. 563-574
    • Summers, M.F.1    Henderson, L.E.2    Chance, M.R.3    Bess, Jr.J.W.4    South, T.L.5    Blake, P.R.6    Sagi, I.7    Perez-Alvarado, G.8    Hare, D.R.9
  • 40
    • 0037161291 scopus 로고    scopus 로고
    • Affinities of Packaging Domain Loops in HIV-1 RNA for the Nucleocapsid Protein
    • Shubsda, M. F.; Paoletti, A. C.; Hudson, B. S.; Borer, P. N. Affinities of Packaging Domain Loops in HIV-1 RNA for the Nucleocapsid Protein Biochemistry 2002, 41, 5276-5282
    • (2002) Biochemistry , vol.41 , pp. 5276-5282
    • Shubsda, M.F.1    Paoletti, A.C.2    Hudson, B.S.3    Borer, P.N.4
  • 41
    • 84876559360 scopus 로고    scopus 로고
    • NMR Analysis of Structural Features of the HIV-1 Nucleocapsid Protein in Response to Mutation and Interaction with RNA and Drug Candidates. Ph.D. Dissertation, Syracuse University.
    • Yang, L. NMR Analysis of Structural Features of the HIV-1 Nucleocapsid Protein in Response to Mutation and Interaction with RNA and Drug Candidates. Ph.D. Dissertation, Syracuse University, 2008.
    • (2008)
    • Yang, L.1
  • 42
    • 35148840942 scopus 로고    scopus 로고
    • Functional Aptamers and Aptazymes in Biotechnology, Diagnostics, and Therapy
    • Famulok, M.; Hartig, J. S.; Mayer, G. Functional Aptamers and Aptazymes in Biotechnology, Diagnostics, and Therapy Chem. Rev. 2007, 107, 3715-3743
    • (2007) Chem. Rev. , vol.107 , pp. 3715-3743
    • Famulok, M.1    Hartig, J.S.2    Mayer, G.3
  • 46
    • 76649116514 scopus 로고    scopus 로고
    • Electrostatic Focusing of Unlabelled DNA into Nanoscale Pores Using a Salt Gradient
    • Wanunu, M.; Morrison, W.; Rabin, Y.; Grosberg, A. Y.; Meller, A. Electrostatic Focusing of Unlabelled DNA into Nanoscale Pores Using a Salt Gradient Nat. Nanotechnol. 2010, 5, 160-165
    • (2010) Nat. Nanotechnol. , vol.5 , pp. 160-165
    • Wanunu, M.1    Morrison, W.2    Rabin, Y.3    Grosberg, A.Y.4    Meller, A.5
  • 47
    • 0041843734 scopus 로고    scopus 로고
    • Partitioning of Individual Flexible Polymers into a Nanoscopic Protein Pore
    • Movileanu, L.; Cheley, S.; Bayley, H. Partitioning of Individual Flexible Polymers into a Nanoscopic Protein Pore Biophys. J. 2003, 85, 897-910
    • (2003) Biophys. J. , vol.85 , pp. 897-910
    • Movileanu, L.1    Cheley, S.2    Bayley, H.3
  • 48
    • 36148943499 scopus 로고    scopus 로고
    • Catalyzing the Translocation of Polypeptides through Attractive Interactions
    • Wolfe, A. J.; Mohammad, M. M.; Cheley, S.; Bayley, H.; Movileanu, L. Catalyzing the Translocation of Polypeptides through Attractive Interactions J. Am. Chem. Soc. 2007, 129, 14034-14041
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 14034-14041
    • Wolfe, A.J.1    Mohammad, M.M.2    Cheley, S.3    Bayley, H.4    Movileanu, L.5
  • 50
    • 78149459196 scopus 로고    scopus 로고
    • Facilitated Translocation of Polypeptides through a Single Nanopore
    • Bikwemu, R.; Wolfe, A. J.; Xing, X.; Movileanu, L. Facilitated Translocation of Polypeptides through a Single Nanopore J. Phys.: Condens. Matter 2010, 22, 454117
    • (2010) J. Phys.: Condens. Matter , vol.22 , pp. 454117
    • Bikwemu, R.1    Wolfe, A.J.2    Xing, X.3    Movileanu, L.4
  • 51
    • 0042820036 scopus 로고    scopus 로고
    • Direct Mass Spectrometric Determination of the Stoichiometry and Binding Affinity of the Complexes between Nucleocapsid Protein and RNA Stem-Loop Hairpins of the HIV-1 Ψ-Recognition Element
    • Hagan, N.; Fabris, D. Direct Mass Spectrometric Determination of the Stoichiometry and Binding Affinity of the Complexes between Nucleocapsid Protein and RNA Stem-Loop Hairpins of the HIV-1 Ψ-Recognition Element Biochemistry 2003, 42, 10736-10745
    • (2003) Biochemistry , vol.42 , pp. 10736-10745
    • Hagan, N.1    Fabris, D.2
  • 52
    • 70350649035 scopus 로고    scopus 로고
    • Single-Molecule Bonds Characterized by Solid-State Nanopore Force Spectroscopy
    • Tabard-Cossa, V.; Wiggin, M.; Trivedi, D.; Jetha, N. N.; Dwyer, J. R.; Marziali, A. Single-Molecule Bonds Characterized by Solid-State Nanopore Force Spectroscopy ACS Nano 2009, 3, 3009-3014
    • (2009) ACS Nano , vol.3 , pp. 3009-3014
    • Tabard-Cossa, V.1    Wiggin, M.2    Trivedi, D.3    Jetha, N.N.4    Dwyer, J.R.5    Marziali, A.6
  • 53
    • 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
  • 54
    • 34347230598 scopus 로고
    • Effects of Entropic Barriers on Polymer Dynamics
    • Muthukumar, M.; Baumgartner, A. Effects of Entropic Barriers on Polymer Dynamics Macromolecules 1989, 22, 1937-1941
    • (1989) Macromolecules , vol.22 , pp. 1937-1941
    • Muthukumar, M.1    Baumgartner, A.2
  • 55
    • 84869424814 scopus 로고    scopus 로고
    • Inspection of the Engineered FhuA Δc/Δ4L Protein Nanopore by Polymer Exclusion
    • Niedzwiecki, D. J.; Mohammad, M. M.; Movileanu, L. Inspection of the Engineered FhuA ΔC/Δ4L Protein Nanopore by Polymer Exclusion Biophys. J. 2012, 103, 2115-2124
    • (2012) Biophys. J. , vol.103 , pp. 2115-2124
    • Niedzwiecki, D.J.1    Mohammad, M.M.2    Movileanu, L.3
  • 56
    • 0346734135 scopus 로고    scopus 로고
    • Electroosmotic Enhancement of the Binding of a Neutral Molecule to a Transmembrane Pore
    • Gu, L. Q.; Cheley, S.; Bayley, H. Electroosmotic Enhancement of the Binding of a Neutral Molecule to a Transmembrane Pore Proc. Natl. Acad. Sci. U.S.A. 2003, 100, 15498-15503
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 15498-15503
    • Gu, L.Q.1    Cheley, S.2    Bayley, H.3
  • 57
    • 34247644060 scopus 로고    scopus 로고
    • Polymer Capture by Electro-osmotic Flow of Oppositely Charged Nanopores
    • Wong, C. T.; Muthukumar, M. Polymer Capture by Electro-osmotic Flow of Oppositely Charged Nanopores J. Chem. Phys. 2007, 126, 164903
    • (2007) J. Chem. Phys. , vol.126 , pp. 164903
    • Wong, C.T.1    Muthukumar, M.2
  • 60
    • 45249104680 scopus 로고    scopus 로고
    • Label-Free Detection of Single Protein Molecules and Protein-Protein Interactions Using Synthetic Nanopores
    • Han, A.; Creus, M.; Schurmann, G.; Linder, V.; Ward, T. R.; de Rooij, N. F.; Staufer, U. Label-Free Detection of Single Protein Molecules and Protein-Protein Interactions Using Synthetic Nanopores Anal. Chem. 2008, 80, 4651-4658
    • (2008) Anal. Chem. , vol.80 , pp. 4651-4658
    • Han, A.1    Creus, M.2    Schurmann, G.3    Linder, V.4    Ward, T.R.5    De Rooij, N.F.6    Staufer, U.7
  • 61
    • 72449183574 scopus 로고    scopus 로고
    • Multichannel Simultaneous Measurements of Single-Molecule Translocation in α-Hemolysin Nanopore Array
    • Osaki, T.; Suzuki, H.; Le, P. B.; Takeuchi, S. Multichannel Simultaneous Measurements of Single-Molecule Translocation in α-Hemolysin Nanopore Array Anal. Chem. 2009, 81, 9866-9870
    • (2009) Anal. Chem. , vol.81 , pp. 9866-9870
    • Osaki, T.1    Suzuki, H.2    Le, P.B.3    Takeuchi, S.4
  • 63
    • 84870516750 scopus 로고    scopus 로고
    • DNA Sequencing and Bar-Coding Using Solid-State Nanopores
    • Atas, E.; Singer, A.; Meller, A. DNA Sequencing and Bar-Coding Using Solid-State Nanopores Electrophoresis 2012, 33, 3437-3447
    • (2012) Electrophoresis , vol.33 , pp. 3437-3447
    • Atas, E.1    Singer, A.2    Meller, A.3
  • 66
    • 78149415469 scopus 로고    scopus 로고
    • Rapid Electronic Detection of Probe-Specific MicroRNAs Using Thin Nanopore Sensors
    • Wanunu, M.; Dadosh, T.; Ray, V.; Jin, J.; McReynolds, L.; Drndic, M. Rapid Electronic Detection of Probe-Specific MicroRNAs Using Thin Nanopore Sensors Nat. Nanotechnol. 2010, 5, 807-814
    • (2010) Nat. Nanotechnol. , vol.5 , pp. 807-814
    • Wanunu, M.1    Dadosh, T.2    Ray, V.3    Jin, J.4    McReynolds, L.5    Drndic, M.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.