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Volumn 6, Issue 3, 2015, Pages 331-337

Nanopore-based sensors for ligand-receptor lead optimization

Author keywords

[No Author keywords available]

Indexed keywords

MOLECULAR DYNAMICS; MOLECULES; PROTEINS; SCREENING;

EID: 84922573368     PISSN: None     EISSN: 19487185     Source Type: Journal    
DOI: 10.1021/jz5025614     Document Type: Article
Times cited : (5)

References (41)
  • 2
    • 78049403279 scopus 로고    scopus 로고
    • Ligand binding assays at equilibrium: Validation and interpretation
    • Hulme, E. C.; Trevethick, M. A. Ligand binding assays at equilibrium: validation and interpretation. Br. J. Pharmacol. 2010, 161, 1219-1237.
    • (2010) Br. J. Pharmacol. , vol.161 , pp. 1219-1237
    • Hulme, E.C.1    Trevethick, M.A.2
  • 3
    • 0034650726 scopus 로고    scopus 로고
    • Exact analysis of competition ligand binding by displacement isothermal titration calorimetry
    • Sigurskjold, B. W. Exact analysis of competition ligand binding by displacement isothermal titration calorimetry. Anal. Biochem. 2000, 277, 260-266.
    • (2000) Anal. Biochem. , vol.277 , pp. 260-266
    • Sigurskjold, B.W.1
  • 4
    • 34250641961 scopus 로고    scopus 로고
    • Isothermal titration calorimetry to determine association constants for high-affinity ligands
    • Velazquez-Campoy, A.; Freire, E. Isothermal titration calorimetry to determine association constants for high-affinity ligands. Nat. Protoc. 2006, 1, 186-191.
    • (2006) Nat. Protoc. , vol.1 , pp. 186-191
    • Velazquez-Campoy, A.1    Freire, E.2
  • 5
    • 0025281866 scopus 로고
    • Study of strong to ultratight protein interactions using differential scanning calorimetry
    • Brandts, J. F.; Lin, L. N. Study of strong to ultratight protein interactions using differential scanning calorimetry. Biochemistry 1990, 29, 6927-6940.
    • (1990) Biochemistry , vol.29 , pp. 6927-6940
    • Brandts, J.F.1    Lin, L.N.2
  • 6
    • 0028922835 scopus 로고
    • Determination of receptor-ligand kinetic and equilibrium binding constants using surface plasmon resonance: Application to the lck SH2 domain and phosphotyrosyl peptides
    • Morelock, M.; Ingraham, R.; Betageri, R.; Jakes, S. Determination of receptor-ligand kinetic and equilibrium binding constants using surface plasmon resonance: application to the lck SH2 domain and phosphotyrosyl peptides. J. Med. Chem. 1995, 38, 1309-1318.
    • (1995) J. Med. Chem. , vol.38 , pp. 1309-1318
    • Morelock, M.1    Ingraham, R.2    Betageri, R.3    Jakes, S.4
  • 7
    • 84908568253 scopus 로고    scopus 로고
    • Surface plasmon resonance - More than a screening technology: Insights in the binding mode of σ70: Core RNAP inhibitors
    • Hüsecken, K.; Hinsberger, S.; Elgaher, W. A.; Haupenthal, J.; Hartmann, R. W. Surface plasmon resonance - more than a screening technology: insights in the binding mode of σ70: core RNAP inhibitors. Future Med. Chem. 2014, 6, 1551-1565.
    • (2014) Future Med. Chem. , vol.6 , pp. 1551-1565
    • Hüsecken, K.1    Hinsberger, S.2    Elgaher, W.A.3    Haupenthal, J.4    Hartmann, R.W.5
  • 8
    • 77954346685 scopus 로고    scopus 로고
    • Ligand-receptor binding affinities from saturation transfer difference (STD) NMR spectroscopy: The binding isotherm of STD initial growth rates
    • Angulo, J.; Enríquez-Navas, P. M.; Nieto, P. M. Ligand-receptor binding affinities from saturation transfer difference (STD) NMR spectroscopy: the binding isotherm of STD initial growth rates. Chem. - Eur. J. 2010, 16, 7803-7812.
    • (2010) Chem. - Eur. J. , vol.16 , pp. 7803-7812
    • Angulo, J.1    Enríquez-Navas, P.M.2    Nieto, P.M.3
  • 9
    • 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. U.S.A. 1996, 93, 13770-13773.
    • (1996) Proc. Natl. Acad. Sci. U.S.A. , vol.93 , pp. 13770-13773
    • Kasianowicz, J.J.1    Brandin, E.2    Branton, D.3    Deamer, D.W.4
  • 11
    • 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
  • 12
    • 84908441398 scopus 로고    scopus 로고
    • Polymer translocation: The first two decades and the recent diversification
    • Palyulin, V. V.; Ala-Nissila, T.; Metzler, R. Polymer translocation: the first two decades and the recent diversification. Soft Matter 2014, 10, 9016-9037.
    • (2014) Soft Matter , vol.10 , pp. 9016-9037
    • Palyulin, V.V.1    Ala-Nissila, T.2    Metzler, R.3
  • 17
    • 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
  • 18
    • 78650005633 scopus 로고    scopus 로고
    • Hybrid pore formation by directed insertion of α-haemolysin into solid-state nanopores
    • Hall, A.; Scott, A.; Rotem, D.; Mehta, K.; Bayley, H.; Dekker, C. Hybrid pore formation by directed insertion of α-haemolysin into solid-state nanopores. Nat. Nanotechnol. 2010, 5, 874-877.
    • (2010) Nat. Nanotechnol. , vol.5 , pp. 874-877
    • Hall, A.1    Scott, A.2    Rotem, D.3    Mehta, K.4    Bayley, H.5    Dekker, C.6
  • 19
    • 4644236471 scopus 로고    scopus 로고
    • Hydrophobic collapse in multidomain protein folding
    • Zhou, R.; Huang, X.; Margulis, C.; Berne, B. Hydrophobic collapse in multidomain protein folding. Science 2004, 305, 1605.
    • (2004) Science , vol.305 , pp. 1605
    • Zhou, R.1    Huang, X.2    Margulis, C.3    Berne, B.4
  • 20
    • 24344448662 scopus 로고    scopus 로고
    • Observation of a dewetting transition in the collapse of the melittin tetramer
    • Liu, P.; Huang, X.; Zhou, R.; Berne, B. Observation of a dewetting transition in the collapse of the melittin tetramer. Nature 2005, 437, 159-162.
    • (2005) Nature , vol.437 , pp. 159-162
    • Liu, P.1    Huang, X.2    Zhou, R.3    Berne, B.4
  • 22
    • 56749160319 scopus 로고    scopus 로고
    • DNA attraction in monovalent and divalent electrolytes
    • Luan, B.; Aksimentiev, A. DNA attraction in monovalent and divalent electrolytes. J. Am. Chem. Soc. 2008, 130, 15754-15755.
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 15754-15755
    • Luan, B.1    Aksimentiev, A.2
  • 23
    • 21244462347 scopus 로고    scopus 로고
    • The breakdown of continuum models for mechanical contacts
    • Luan, B.; Robbins, M. O. The breakdown of continuum models for mechanical contacts. Nature 2005, 435, 929-932.
    • (2005) Nature , vol.435 , pp. 929-932
    • Luan, B.1    Robbins, M.O.2
  • 25
    • 70849127936 scopus 로고    scopus 로고
    • Watermediated signal multiplication with Y-shaped carbon nanotubes
    • Tu, Y.; Xiu, P.; Wan, R.; Hu, J.; Zhou, R.; Fang, H. Watermediated signal multiplication with Y-shaped carbon nanotubes. Proc. Natl. Acad. Sci. U.S.A. 2009, 106, 18120-18124.
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 18120-18124
    • Tu, Y.1    Xiu, P.2    Wan, R.3    Hu, J.4    Zhou, R.5    Fang, H.6
  • 27
    • 27344436659 scopus 로고    scopus 로고
    • Scalable molecular dynamics with NAMD
    • Phillips, J. C.; et al. Scalable molecular dynamics with NAMD. J. Comput. Chem. 2005, 26, 1781.
    • (2005) J. Comput. Chem. , vol.26 , pp. 1781
    • Phillips, J.C.1
  • 29
    • 0000036869 scopus 로고    scopus 로고
    • Simulation of activation free energies in molecular systems
    • Neria, E.; Fischer, S.; Karplus, M. Simulation of activation free energies in molecular systems. J. Chem. Phys. 1996, 105, 1902.
    • (1996) J. Chem. Phys. , vol.105 , pp. 1902
    • Neria, E.1    Fischer, S.2    Karplus, M.3
  • 30
    • 0001655657 scopus 로고
    • Finite representation of an infinite bulk system: Solvent boundary potential for computer simulations
    • Beglov, D.; Roux, B. Finite representation of an infinite bulk system: solvent boundary potential for computer simulations. J. Chem. Phys. 1994, 100, 9050-9063.
    • (1994) J. Chem. Phys. , vol.100 , pp. 9050-9063
    • Beglov, D.1    Roux, B.2
  • 31
    • 33751266937 scopus 로고    scopus 로고
    • Water-silica force field for simulating nanodevices
    • Cruz-Chu, E. R.; Aksimentiev, A.; Schulten, K. Water-silica force field for simulating nanodevices. J. Phys. Chem. B 2006, 110, 21497-21508.
    • (2006) J. Phys. Chem. B , vol.110 , pp. 21497-21508
    • Cruz-Chu, E.R.1    Aksimentiev, A.2    Schulten, K.3
  • 32
    • 0041784950 scopus 로고    scopus 로고
    • All-atom empirical potential for molecular modeling and dynamics studies of proteins
    • MacKerell, A., Jr.; et al. All-atom empirical potential for molecular modeling and dynamics studies of proteins. J. Phys. Chem. B 1998, 102, 3586-3616.
    • (1998) J. Phys. Chem. B , vol.102 , pp. 3586-3616
    • MacKerell Jr.1    , A.2
  • 33
    • 84865988248 scopus 로고    scopus 로고
    • Nanopore-based sensors for detecting toxicity of a carbon nanotube to proteins
    • Luan, B.; Zhou, R. Nanopore-based sensors for detecting toxicity of a carbon nanotube to proteins. J. Phys. Chem. Lett. 2012, 3, 2337-2341.
    • (2012) J. Phys. Chem. Lett. , vol.3 , pp. 2337-2341
    • Luan, B.1    Zhou, R.2
  • 34
    • 22244445788 scopus 로고    scopus 로고
    • Imaging α-hemolysin with molecular dynamics: Ionic conductance, osmotic permeability and the electrostatic potential map
    • Aksimentiev, A.; Schulten, K. Imaging α-hemolysin with molecular dynamics: ionic conductance, osmotic permeability and the electrostatic potential map. Biophys. J. 2005, 88, 3745-3761.
    • (2005) Biophys. J. , vol.88 , pp. 3745-3761
    • Aksimentiev, A.1    Schulten, K.2
  • 35
    • 50849102996 scopus 로고    scopus 로고
    • Electro-osmotic screening of the DNA charge in a nanopore
    • Luan, B. Q.; Aksimentiev, A. Electro-osmotic screening of the DNA charge in a nanopore. Phys. Rev. E 2008, 78, 021912.
    • (2008) Phys. Rev. E , vol.78 , pp. 021912
    • Luan, B.Q.1    Aksimentiev, A.2
  • 36
    • 34250356054 scopus 로고    scopus 로고
    • Extracting kinetics from single-molecule force spectroscopy: Nanopore unzipping of DNA hairpins
    • Dudko, O. K.; Mathé, 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    Mathé, J.2    Szabo, A.3    Meller, A.4    Hummer, G.5
  • 37
    • 0018101150 scopus 로고
    • Models for the specific adhesion of cells to cells
    • Bell, G. I. Models for the specific adhesion of cells to cells. Science 1978, 200, 618-627.
    • (1978) Science , vol.200 , pp. 618-627
    • Bell, G.I.1
  • 38
    • 0035861991 scopus 로고    scopus 로고
    • Solution structures of the YAP65 WW domain and the variant L30 K in complex with the peptides GTPPPPYTVG, N-(n-octyl)-GPPPY and PLPPY and the application of peptide libraries reveal a minimal binding epitope
    • Pires, J. R.; Taha-Nejad, F.; Toepert, F.; Ast, T.; Hoffmüller, U.; Schneider-Mergener, J.; Kühne, R.; Macias, M. J.; Oschkinat, H. Solution structures of the YAP65 WW domain and the variant L30 K in complex with the peptides GTPPPPYTVG, N-(n-octyl)-GPPPY and PLPPY and the application of peptide libraries reveal a minimal binding epitope. J. Mol. Bio. 2001, 314, 1147-1156.
    • (2001) J. Mol. Bio. , vol.314 , pp. 1147-1156
    • Pires, J.R.1    Taha-Nejad, F.2    Toepert, F.3    Ast, T.4    Hoffmüller, U.5    Schneider-Mergener, J.6    Kühne, R.7    Macias, M.J.8    Oschkinat, H.9
  • 39
    • 84901250803 scopus 로고    scopus 로고
    • Automated Fabrication of 2-nm solid-state nanopores for nucleic acid analysis
    • Briggs, K.; Kwok, H.; Tabard-Cossa, V. Automated Fabrication of 2-nm solid-state nanopores for nucleic acid analysis. Small 2014, 10, 2077-2086.
    • (2014) Small , vol.10 , pp. 2077-2086
    • Briggs, K.1    Kwok, H.2    Tabard-Cossa, V.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.