메뉴 건너뛰기




Volumn 6, Issue , 2015, Pages

Identifying and quantifying two ligand-binding sites while imaging native human membrane receptors by AFM

Author keywords

[No Author keywords available]

Indexed keywords

NITRILOTRIACETIC ACID; POLYHISTIDINE TAG; PROTEINASE ACTIVATED RECEPTOR; PROTEOLIPOSOME; LIGAND; PROTEIN BINDING; PROTEINASE ACTIVATED RECEPTOR 1;

EID: 84946924432     PISSN: None     EISSN: 20411723     Source Type: Journal    
DOI: 10.1038/ncomms9857     Document Type: Article
Times cited : (68)

References (45)
  • 1
    • 84873685831 scopus 로고    scopus 로고
    • Molecular signatures of G-protein-coupled receptors
    • Venkatakrishnan, A. J. et al. Molecular signatures of G-protein-coupled receptors. Nature 494, 185-194 (2013).
    • (2013) Nature , vol.494 , pp. 185-194
    • Venkatakrishnan, A.J.1
  • 2
    • 74049133619 scopus 로고    scopus 로고
    • Subcellular targeting strategies for drug design and delivery
    • Rajendran, L., Knolker, H. J. & Simons, K. Subcellular targeting strategies for drug design and delivery. Nat. Rev. Drug Discov. 9, 29-42 (2010).
    • (2010) Nat. Rev. Drug Discov. , vol.9 , pp. 29-42
    • Rajendran, L.1    Knolker, H.J.2    Simons, K.3
  • 3
    • 34447633368 scopus 로고    scopus 로고
    • Conformational complexity of G-protein-coupled receptors
    • Kobilka, B. K. & Deupi, X. Conformational complexity of G-protein-coupled receptors. Trends Pharmacol. Sci. 28, 397-406 (2007).
    • (2007) Trends Pharmacol. Sci. , vol.28 , pp. 397-406
    • Kobilka, B.K.1    Deupi, X.2
  • 4
    • 0033121032 scopus 로고    scopus 로고
    • Spatially resolved force spectroscopy of biological surfaces using the atomic force microscope
    • Heinz, W. F. & Hoh, J. H. Spatially resolved force spectroscopy of biological surfaces using the atomic force microscope. Trends Biotechnol. 17, 143-150 (1999).
    • (1999) Trends Biotechnol. , vol.17 , pp. 143-150
    • Heinz, W.F.1    Hoh, J.H.2
  • 5
    • 84883412119 scopus 로고    scopus 로고
    • Multiparametric imaging of biological systems by force-distance curve-based AFM
    • Dufrene, Y. F., Martinez-Martin, D., Medalsy, I., Alsteens, D. & Muller, D. J. Multiparametric imaging of biological systems by force-distance curve-based AFM. Nat. Methods 10, 847-854 (2013).
    • (2013) Nat. Methods , vol.10 , pp. 847-854
    • Dufrene, Y.F.1    Martinez-Martin, D.2    Medalsy, I.3    Alsteens, D.4    Muller, D.J.5
  • 7
    • 33646021951 scopus 로고    scopus 로고
    • Detection and localization of single molecular recognition events using atomic force microscopy
    • Hinterdorfer, P. & Dufrene, Y. F. Detection and localization of single molecular recognition events using atomic force microscopy. Nat. Methods 3, 347-355 (2006).
    • (2006) Nat. Methods , vol.3 , pp. 347-355
    • Hinterdorfer, P.1    Dufrene, Y.F.2
  • 8
    • 43449133266 scopus 로고    scopus 로고
    • Atomic force microscopy as a multifunctional molecular toolbox in nanobiotechnology
    • Muller, D. J. & Dufrene, Y. F. Atomic force microscopy as a multifunctional molecular toolbox in nanobiotechnology. Nat. Nanotechnol. 3, 261-269 (2008).
    • (2008) Nat. Nanotechnol. , vol.3 , pp. 261-269
    • Muller, D.J.1    Dufrene, Y.F.2
  • 9
    • 83455198342 scopus 로고    scopus 로고
    • Imaging and quantifying chemical and physical properties of native proteins at molecular resolution by force-volume AFM
    • Medalsy, I., Hensen, U. & Muller, D. J. Imaging and quantifying chemical and physical properties of native proteins at molecular resolution by force-volume AFM. Angew. Chem. Int. Ed. 50, 12103-12108 (2011).
    • (2011) Angew. Chem. Int. Ed. , vol.50 , pp. 12103-12108
    • Medalsy, I.1    Hensen, U.2    Muller, D.J.3
  • 10
    • 84870893219 scopus 로고    scopus 로고
    • High-resolution imaging of chemical and biological sites on living cells using peak force tapping atomic force microscopy
    • Alsteens, D. et al. High-resolution imaging of chemical and biological sites on living cells using peak force tapping atomic force microscopy. Langmuir 28, 16738-16744 (2012).
    • (2012) Langmuir , vol.28 , pp. 16738-16744
    • Alsteens, D.1
  • 11
    • 84887849212 scopus 로고    scopus 로고
    • Quantitative imaging of the electrostatic field and potential generated by a transmembrane protein pore at subnanometer resolution
    • Pfreundschuh, M., Hensen, U. & Muller, D. J. Quantitative imaging of the electrostatic field and potential generated by a transmembrane protein pore at subnanometer resolution. Nano Lett. 13, 5585-5593 (2013).
    • (2013) Nano Lett. , vol.13 , pp. 5585-5593
    • Pfreundschuh, M.1    Hensen, U.2    Muller, D.J.3
  • 12
    • 84900506601 scopus 로고    scopus 로고
    • Localizing chemical groups while imaging single native proteins by high-resolution atomic force microscopy
    • Pfreundschuh, M., Alsteens, D., Hilbert, M., Steinmetz, M. O. & Muller, D. J. Localizing chemical groups while imaging single native proteins by high-resolution atomic force microscopy. Nano Lett. 14, 2957-2964 (2014).
    • (2014) Nano Lett. , vol.14 , pp. 2957-2964
    • Pfreundschuh, M.1    Alsteens, D.2    Hilbert, M.3    Steinmetz, M.O.4    Muller, D.J.5
  • 13
    • 84940504317 scopus 로고    scopus 로고
    • Imaging G protein-coupled receptors while quantifying their ligand-binding free-energy landscape
    • Alsteens, D. et al. Imaging G protein-coupled receptors while quantifying their ligand-binding free-energy landscape. Nat. Methods 12, 845-851 (2015).
    • (2015) Nat. Methods , vol.12 , pp. 845-851
    • Alsteens, D.1
  • 14
    • 78650547219 scopus 로고    scopus 로고
    • Force-induced formation and propagation of adhesion nanodomains in living fungal cells
    • Alsteens, D., Garcia, M. C., Lipke, P. N. & Dufrene, Y. F. Force-induced formation and propagation of adhesion nanodomains in living fungal cells. Proc. Natl Acad. Sci. USA 107, 20744-20749 (2010).
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , pp. 20744-20749
    • Alsteens, D.1    Garcia, M.C.2    Lipke, P.N.3    Dufrene, Y.F.4
  • 15
    • 33645535034 scopus 로고    scopus 로고
    • G protein-coupled receptor rhodopsin
    • Palczewski, K. G protein-coupled receptor rhodopsin. Annu. Rev. Biochem. 75, 743-767 (2006).
    • (2006) Annu. Rev. Biochem. , vol.75 , pp. 743-767
    • Palczewski, K.1
  • 16
    • 66249144426 scopus 로고    scopus 로고
    • The structure and function of G-protein-coupled receptors
    • Rosenbaum, D. M., Rasmussen, S. G. & Kobilka, B. K. The structure and function of G-protein-coupled receptors. Nature 459, 356-363 (2009).
    • (2009) Nature , vol.459 , pp. 356-363
    • Rosenbaum, D.M.1    Rasmussen, S.G.2    Kobilka, B.K.3
  • 17
    • 84864221004 scopus 로고    scopus 로고
    • A new era of GPCR structural and chemical biology
    • Granier, S. & Kobilka, B. A new era of GPCR structural and chemical biology. Nat. Chem. Biol. 8, 670-673 (2012).
    • (2012) Nat. Chem. Biol. , vol.8 , pp. 670-673
    • Granier, S.1    Kobilka, B.2
  • 18
    • 77958039571 scopus 로고    scopus 로고
    • Energy landscapes as a tool to integrate GPCR structure, dynamics, and function
    • Deupi, X. & Kobilka, B. K. Energy landscapes as a tool to integrate GPCR structure, dynamics, and function. Physiology (Bethesda) 25, 293-303 (2010).
    • (2010) Physiology (Bethesda) , vol.25 , pp. 293-303
    • Deupi, X.1    Kobilka, B.K.2
  • 19
    • 0034648757 scopus 로고    scopus 로고
    • Thrombin signalling and protease-activated receptors
    • Coughlin, S. R. Thrombin signalling and protease-activated receptors. Nature 407, 258-264 (2000).
    • (2000) Nature , vol.407 , pp. 258-264
    • Coughlin, S.R.1
  • 20
    • 79955584619 scopus 로고    scopus 로고
    • Structure, function and pathophysiology of protease activated receptors
    • Adams, M. N. et al. Structure, function and pathophysiology of protease activated receptors. Pharmacol. Ther. 130, 248-282 (2011).
    • (2011) Pharmacol. Ther. , vol.130 , pp. 248-282
    • Adams, M.N.1
  • 21
    • 84895156496 scopus 로고    scopus 로고
    • Biased signalling and proteinase-activated receptors (PARs): Targeting inflammatory disease
    • Hollenberg, M. D. et al. Biased signalling and proteinase-activated receptors (PARs): targeting inflammatory disease. Br. J. Pharmacol. 171, 1180-1194 (2014).
    • (2014) Br. J. Pharmacol. , vol.171 , pp. 1180-1194
    • Hollenberg, M.D.1
  • 22
    • 28344436780 scopus 로고    scopus 로고
    • Protease-activated receptors in hemostasis, thrombosis and vascular biology
    • Coughlin, S. R. Protease-activated receptors in hemostasis, thrombosis and vascular biology. J. Thromb. Haemost. 3, 1800-1814 (2005).
    • (2005) J. Thromb. Haemost. , vol.3 , pp. 1800-1814
    • Coughlin, S.R.1
  • 23
    • 33947314576 scopus 로고    scopus 로고
    • Regulation of receptor trafficking by GRKs and arrestins
    • Moore, C. A., Milano, S. K. & Benovic, J. L. Regulation of receptor trafficking by GRKs and arrestins. Annu. Rev. Physiol. 69, 451-482 (2007).
    • (2007) Annu. Rev. Physiol. , vol.69 , pp. 451-482
    • Moore, C.A.1    Milano, S.K.2    Benovic, J.L.3
  • 24
    • 22944441978 scopus 로고    scopus 로고
    • High-affinity adaptors for switchable recognition of histidine-tagged proteins
    • Lata, S., Reichel, A., Brock, R., Tampe, R. & Piehler, J. High-affinity adaptors for switchable recognition of histidine-tagged proteins. J. Am. Chem. Soc. 127, 10205-10215 (2005).
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 10205-10215
    • Lata, S.1    Reichel, A.2    Brock, R.3    Tampe, R.4    Piehler, J.5
  • 25
    • 0026775223 scopus 로고
    • Structure-function relationships in the activation of platelet thrombin receptors by receptor-derived peptides
    • Vassallo, Jr R. R., Kieber-Emmons, T., Cichowski, K. & Brass, L. F. Structure-function relationships in the activation of platelet thrombin receptors by receptor-derived peptides. J. Biol. Chem. 267, 6081-6085 (1992).
    • (1992) J. Biol. Chem. , vol.267 , pp. 6081-6085
    • Vassallo, R.R.1    Kieber-Emmons, T.2    Cichowski, K.3    Brass, L.F.4
  • 26
    • 0029758276 scopus 로고    scopus 로고
    • Development of potent thrombin receptor antagonist peptides
    • Bernatowicz, M. S. et al. Development of potent thrombin receptor antagonist peptides. J. Med. Chem. 39, 4879-4887 (1996).
    • (1996) J. Med. Chem. , vol.39 , pp. 4879-4887
    • Bernatowicz, M.S.1
  • 27
    • 41049093662 scopus 로고    scopus 로고
    • Chemical modifications of AFM tips for the study of molecular recognition events
    • Barattin, R. & Voyer, N. Chemical modifications of AFM tips for the study of molecular recognition events. Chem. Commun. (Camb.) 13, 1513-1532 (2008).
    • (2008) Chem. Commun. (Camb.) , vol.13 , pp. 1513-1532
    • Barattin, R.1    Voyer, N.2
  • 28
    • 84855268688 scopus 로고    scopus 로고
    • Probing binding pocket of serotonin transporter by single molecular force spectroscopy on living cells
    • Wildling, L. et al. Probing binding pocket of serotonin transporter by single molecular force spectroscopy on living cells. J. Biol. Chem. 287, 105-113 (2012).
    • (2012) J. Biol. Chem. , vol.287 , pp. 105-113
    • Wildling, L.1
  • 29
    • 84859054318 scopus 로고    scopus 로고
    • Pulling tethers from pore-spanning bilayers: Towards simultaneous determination of local bending modulus and lateral tension of membranes
    • Kocun, M. & Janshoff, A. Pulling tethers from pore-spanning bilayers: towards simultaneous determination of local bending modulus and lateral tension of membranes. Small 8, 847-851 (2012).
    • (2012) Small , vol.8 , pp. 847-851
    • Kocun, M.1    Janshoff, A.2
  • 30
    • 0028309424 scopus 로고
    • Adhesion forces between individual ligand-receptor pairs
    • Florin, E.-L., Moy, V. T. & Gaub, H. E. Adhesion forces between individual ligand-receptor pairs. Science 264, 415-417 (1994).
    • (1994) Science , vol.264 , pp. 415-417
    • Florin, E.-L.1    Moy, V.T.2    Gaub, H.E.3
  • 31
    • 34249936024 scopus 로고    scopus 로고
    • Forces and bond dynamics in cell adhesion
    • Evans, E. A. & Calderwood, D. A. Forces and bond dynamics in cell adhesion. Science 316, 1148-1153 (2007).
    • (2007) Science , vol.316 , pp. 1148-1153
    • Evans, E.A.1    Calderwood, D.A.2
  • 33
    • 65949083762 scopus 로고    scopus 로고
    • Force probing surfaces of living cells to molecular resolution
    • Muller, D. J., Helenius, J., Alsteens, D. & Dufrene, Y. F. Force probing surfaces of living cells to molecular resolution. Nat. Chem. Biol. 5, 383-390 (2009).
    • (2009) Nat. Chem. Biol. , vol.5 , pp. 383-390
    • Muller, D.J.1    Helenius, J.2    Alsteens, D.3    Dufrene, Y.F.4
  • 34
    • 84870896671 scopus 로고    scopus 로고
    • Cholesterol increases kinetic, energetic, and mechanical stability of the human beta2-adrenergic receptor
    • Zocher, M., Zhang, C., Rasmussen, S. G., Kobilka, B. K. & Muller, D. J. Cholesterol increases kinetic, energetic, and mechanical stability of the human beta2-adrenergic receptor. Proc. Natl Acad. Sci. USA 109, E3463-E3472 (2012).
    • (2012) Proc. Natl Acad. Sci. USA , vol.109 , pp. E3463-E3472
    • Zocher, M.1    Zhang, C.2    Rasmussen, S.G.3    Kobilka, B.K.4    Muller, D.J.5
  • 35
    • 44249115874 scopus 로고    scopus 로고
    • Self-assembled monolayers containing terminal mono-, bis-, and tris-nitrilotriacetic acid groups: Characterization and application
    • Valiokas, R. et al. Self-assembled monolayers containing terminal mono-, bis-, and tris-nitrilotriacetic acid groups: characterization and application. Langmuir 24, 4959-4967 (2008).
    • (2008) Langmuir , vol.24 , pp. 4959-4967
    • Valiokas, R.1
  • 36
    • 69249203735 scopus 로고    scopus 로고
    • Detection of metal binding sites on functional S-layer nanoarrays using single molecule force spectroscopy
    • Tang, J. et al. Detection of metal binding sites on functional S-layer nanoarrays using single molecule force spectroscopy. J. Struct. Biol. 168, 217-222 (2009).
    • (2009) J. Struct. Biol. , vol.168 , pp. 217-222
    • Tang, J.1
  • 37
    • 84890642916 scopus 로고    scopus 로고
    • Multiparametric atomic force microscopy imaging of single bacteriophages extruding from living bacteria
    • Alsteens, D., Trabelsi, H., Soumillion, P. & Dufrene, Y. F. Multiparametric atomic force microscopy imaging of single bacteriophages extruding from living bacteria. Nat. Commun. 4, 2926 (2013).
    • (2013) Nat. Commun. , vol.4 , pp. 2926
    • Alsteens, D.1    Trabelsi, H.2    Soumillion, P.3    Dufrene, Y.F.4
  • 38
    • 0032227720 scopus 로고    scopus 로고
    • Energy landscapes of biomolecular adhesion and receptor anchoring at interfaces explored with dynamic force spectroscopy
    • Evans, E. Energy landscapes of biomolecular adhesion and receptor anchoring at interfaces explored with dynamic force spectroscopy. Faraday Discuss. 111, 1-16 (1998).
    • (1998) Faraday Discuss , vol.111 , pp. 1-16
    • Evans, E.1
  • 39
    • 57349124448 scopus 로고    scopus 로고
    • Theory, analysis, and interpretation of single-molecule force spectroscopy experiments
    • Dudko, O. K., Hummer, G. & Szabo, A. Theory, analysis, and interpretation of single-molecule force spectroscopy experiments. Proc. Natl Acad. Sci. USA 105, 15755-15760 (2008).
    • (2008) Proc. Natl Acad. Sci. USA , vol.105 , pp. 15755-15760
    • Dudko, O.K.1    Hummer, G.2    Szabo, A.3
  • 40
    • 84865282672 scopus 로고    scopus 로고
    • Interpreting the widespread nonlinear force spectra of intermolecular bonds
    • Friddle, R. W., Noy, A. & De Yoreo, J. J. Interpreting the widespread nonlinear force spectra of intermolecular bonds. Proc. Natl Acad. Sci. USA 109, 13573-13578 (2012).
    • (2012) Proc. Natl Acad. Sci. USA , vol.109 , pp. 13573-13578
    • Friddle, R.W.1    Noy, A.2    De Yoreo, J.J.3
  • 41
    • 0031001349 scopus 로고    scopus 로고
    • Dynamic strength of molecular adhesion bonds
    • Evans, E. & Ritchie, K. Dynamic strength of molecular adhesion bonds. Biophys. J. 72, 1541-1555 (1997).
    • (1997) Biophys. J , vol.72 , pp. 1541-1555
    • Evans, E.1    Ritchie, K.2
  • 42
    • 33645004171 scopus 로고    scopus 로고
    • Intrinsic rates and activation free energies from single-molecule pulling experiments
    • Dudko, O. K., Hummer, G. & Szabo, A. Intrinsic rates and activation free energies from single-molecule pulling experiments. Phys. Rev. Lett. 96, 108101 (2006).
    • (2006) Phys. Rev. Lett. , vol.96
    • Dudko, O.K.1    Hummer, G.2    Szabo, A.3
  • 43
    • 84864853215 scopus 로고    scopus 로고
    • Ligand-specific interactions modulate kinetic, energetic, and mechanical properties of the human beta2 adrenergic receptor
    • Zocher, M., Fung, J. J., Kobilka, B. K. & Muller, D. J. Ligand-specific interactions modulate kinetic, energetic, and mechanical properties of the human beta2 adrenergic receptor. Structure 20, 1391-1402 (2012).
    • (2012) Structure , vol.20 , pp. 1391-1402
    • Zocher, M.1    Fung, J.J.2    Kobilka, B.K.3    Muller, D.J.4
  • 44
    • 79959234730 scopus 로고    scopus 로고
    • Linking of sensor molecules with amino groups to amino-functionalized AFM tips
    • Wildling, L. et al. Linking of sensor molecules with amino groups to amino-functionalized AFM tips. Bioconjug. Chem. 22, 1239-1248 (2011).
    • (2011) Bioconjug. Chem. , vol.22 , pp. 1239-1248
    • Wildling, L.1
  • 45
    • 24744472221 scopus 로고    scopus 로고
    • High-affinity chelator thiols for switchable and oriented immobilization of histidine-tagged proteins: A generic platform for protein chip technologies
    • Tinazli, A. et al. High-affinity chelator thiols for switchable and oriented immobilization of histidine-tagged proteins: a generic platform for protein chip technologies. Chemistry 11, 5249-5259 (2005).
    • (2005) Chemistry , vol.11 , pp. 5249-5259
    • Tinazli, A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.