메뉴 건너뛰기




Volumn 21, Issue 1, 2013, Pages 1189-1202

Single-molecule fluorescence imaging of processive myosin with enhanced background suppression using linear zero-mode waveguides (ZMWs) and convex lens induced confinement (CLIC)

Author keywords

[No Author keywords available]

Indexed keywords

FLUORESCENCE; FLUOROPHORES; LINEAR MOTORS; MOLECULES; REFRACTIVE INDEX; WAVEGUIDES;

EID: 84872713972     PISSN: None     EISSN: 10944087     Source Type: Journal    
DOI: 10.1364/OE.21.001189     Document Type: Article
Times cited : (40)

References (35)
  • 1
    • 58849085113 scopus 로고    scopus 로고
    • Simultaneous measurement of nucleotide occupancy and mechanical displacement in myosin-V, a processive molecular motor
    • T. Komori, S. Nishikawa, T. Ariga, A. H. Iwane, and T. Yanagida, "Simultaneous measurement of nucleotide occupancy and mechanical displacement in myosin-V, a processive molecular motor," Biophys. J. 96(1), L04-L06 (2009).
    • (2009) Biophys. J , vol.96 , Issue.1
    • Komori, T.1    Nishikawa, S.2    Ariga, T.3    Iwane, A.H.4    Yanagida, T.5
  • 2
    • 34447628890 scopus 로고    scopus 로고
    • Coupling of rotation and catalysis in F(1)-ATPase revealed by single-molecule imaging and manipulation
    • K. Adachi, K. Oiwa, T. Nishizaka, S. Furuike, H. Noji, H. Itoh, M. Yoshida, and K. Kinosita, Jr., "Coupling of rotation and catalysis in F(1)-ATPase revealed by single-molecule imaging and manipulation," Cell 130(2), 309-321 (2007).
    • (2007) Cell , vol.130 , Issue.2 , pp. 309-321
    • Adachi, K.1    Oiwa, K.2    Nishizaka, T.3    Furuike, S.4    Noji, H.5    Itoh, H.6    Yoshida, M.7    Kinosita Jr., K.8
  • 3
    • 0037474152 scopus 로고    scopus 로고
    • Zero-mode waveguides for single-molecule analysis at high concentrations
    • M. J. Levene, J. Korlach, S. W. Turner, M. Foquet, H. G. Craighead, and W. W. Webb, "Zero-mode waveguides for single-molecule analysis at high concentrations," Science 299(5607), 682-686 (2003).
    • (2003) Science , vol.299 , Issue.5607 , pp. 682-686
    • Levene, M.J.1    Korlach, J.2    Turner, S.W.3    Foquet, M.4    Craighead, H.G.5    Webb, W.W.6
  • 4
    • 0035819204 scopus 로고    scopus 로고
    • Immobilization in Surface-Tethered Lipid Vesicles as a New Tool for Single Biomolecule Spectroscopy
    • E. Boukobza, A. Sonnenfeld, and G. Haran, "Immobilization in Surface-Tethered Lipid Vesicles as a New Tool for Single Biomolecule Spectroscopy," J. Phys. Chem. B 105(48), 12165-12170 (2001).
    • (2001) J. Phys. Chem , vol.B 105 , Issue.48 , pp. 12165-12170
    • Boukobza, E.1    Sonnenfeld, A.2    Haran, G.3
  • 5
    • 67649976792 scopus 로고    scopus 로고
    • Droplets for ultrasmall-volume analysis
    • D. T. Chiu, R. M. Lorenz, and G. D. M. Jeffries, "Droplets for ultrasmall-volume analysis," Anal. Chem. 81(13), 5111-5118 (2009).
    • (2009) Anal. Chem , vol.81 , Issue.13 , pp. 5111-5118
    • Chiu, D.T.1    Lorenz, R.M.2    Jeffries, G.D.M.3
  • 6
    • 77957090469 scopus 로고    scopus 로고
    • Nanovesicle trapping for studying weak protein interactions by single-molecule FRET
    • J. J. Benítez, A. M. Keller, and P. Chen, "Nanovesicle trapping for studying weak protein interactions by single-molecule FRET," Methods Enzymol. 472, 41-60 (2010).
    • (2010) Methods Enzymol , vol.472 , Issue.41
    • Benítez, J.J.1    Keller, A.M.2    Chen, P.3
  • 7
    • 70350052649 scopus 로고    scopus 로고
    • Single molecule nanocontainers made porous using a bacterial toxin
    • B. Okumus, S. Arslan, S. M. Fengler, S. Myong, and T. Ha, "Single molecule nanocontainers made porous using a bacterial toxin," J. Am. Chem. Soc. 131(41), 14844-14849 (2009).
    • (2009) J. Am. Chem. Soc , vol.131 , Issue.41 , pp. 14844-14849
    • Okumus, B.1    Arslan, S.2    Fengler, S.M.3    Myong, S.4    Ha, T.5
  • 8
    • 84867081368 scopus 로고    scopus 로고
    • A general approach to break the concentration barrier in single-molecule imaging
    • A. B. Loveland, S. Habuchi, J. C. Walter, and A. M. van Oijen, "A general approach to break the concentration barrier in single-molecule imaging," Nat. Methods 9(10), 987-992 (2012).
    • (2012) Nat. Methods 9 , vol.10 , pp. 987-992
    • Loveland, A.B.1    Habuchi, S.2    Walter, J.C.3    Van Oijen, A.M.4
  • 10
    • 51349088578 scopus 로고    scopus 로고
    • Direct observation of the mechanochemical coupling in myosin Va during processive movement
    • T. Sakamoto, M. R. Webb, E. Forgacs, H. D. White, and J. R. Sellers, "Direct observation of the mechanochemical coupling in myosin Va during processive movement," Nature 455(7209), 128-132 (2008).
    • (2008) Nature , vol.455 , Issue.7209 , pp. 128-132
    • Sakamoto, T.1    Webb, M.R.2    Forgacs, E.3    White, H.D.4    Sellers, J.R.5
  • 11
    • 0035943690 scopus 로고    scopus 로고
    • Kinetic mechanism and regulation of myosin VI
    • E. M. De La Cruz, E. M. Ostap, and H. L. Sweeney, "Kinetic mechanism and regulation of myosin VI," J. Biol. Chem. 276(34), 32373-32381 (2001).
    • (2001) J. Biol. Chem , vol.276 , Issue.34 , pp. 32373-32381
    • De La Cruz, E.M.1    Ostap, E.M.2    Sweeney, H.L.3
  • 12
    • 34247571461 scopus 로고    scopus 로고
    • Kinesin motor mechanics: Binding, stepping, tracking, gating, and limping
    • S. M. Block, "Kinesin motor mechanics: binding, stepping, tracking, gating, and limping," Biophys. J. 92(9), 2986-2995 (2007).
    • (2007) Biophys. J , vol.92 , Issue.9 , pp. 2986-2995
    • Block, S.M.1
  • 14
    • 84855828496 scopus 로고    scopus 로고
    • Cytoplasmic dynein moves through uncoordinated stepping of the AAA+ ring domains
    • M. A. DeWitt, A. Y. Chang, P. A. Combs, and A. Yildiz, "Cytoplasmic dynein moves through uncoordinated stepping of the AAA+ ring domains," Science 335(6065), 221-225 (2012).
    • (2012) Science , vol.6065 , pp. 221-225
    • Dewitt, M.A.1    Chang, A.Y.2    Combs, P.A.3    Yildiz, A.4
  • 16
    • 0032559298 scopus 로고    scopus 로고
    • Simultaneous observation of individual ATPase and mechanical events by a single myosin molecule during interaction with actin
    • A. Ishijima, H. Kojima, T. Funatsu, M. Tokunaga, H. Higuchi, H. Tanaka, and T. Yanagida, "Simultaneous observation of individual ATPase and mechanical events by a single myosin molecule during interaction with actin," Cell 92(2), 161-171 (1998).
    • (1998) Cell , vol.92 , Issue.2 , pp. 161-171
    • Ishijima, A.1    Kojima, H.2    Funatsu, T.3    Tokunaga, M.4    Higuchi, H.5    Tanaka, H.6    Yanagida, T.7
  • 17
    • 0031560940 scopus 로고    scopus 로고
    • Single molecule imaging of fluorophores and enzymatic reactions achieved by objective-type total internal reflection fluorescence microscopy
    • M. Tokunaga, K. Kitamura, K. Saito, A. H. Iwane, and T. Yanagida, "Single molecule imaging of fluorophores and enzymatic reactions achieved by objective-type total internal reflection fluorescence microscopy," Biochem. Biophys. Res. Commun. 235(1), 47-53 (1997).
    • (1997) Biochem. Biophys. Res. Commun , vol.235 , Issue.1 , pp. 47-53
    • Tokunaga, M.1    Kitamura, K.2    Saito, K.3    Iwane, A.H.4    Yanagida, T.5
  • 19
    • 46849085956 scopus 로고    scopus 로고
    • Measurement system for simultaneous observation of myosin v chemical and mechanical events
    • T. Komori, S. Nishikawa, T. Ariga, A. H. Iwane, and T. Yanagida, "Measurement system for simultaneous observation of myosin V chemical and mechanical events," Biosystems 93(1-2), 48-57 (2008).
    • (2008) Biosystems , vol.93 , Issue.1-2 , pp. 48-57
    • Komori, T.1    Nishikawa, S.2    Ariga, T.3    Iwane, A.H.4    Yanagida, T.5
  • 20
    • 78751687016 scopus 로고    scopus 로고
    • Detailed tuning of structure and intramolecular communication are dispensable for processive motion of myosin VI
    • M. W. Elting, Z. Bryant, J. C. Liao, and J. A. Spudich, "Detailed tuning of structure and intramolecular communication are dispensable for processive motion of myosin VI," Biophys. J. 100(2), 430-439 (2011).
    • (2011) Biophys. J , vol.100 , Issue.2 , pp. 430-439
    • Elting, M.W.1    Bryant, Z.2    Liao, J.C.3    Spudich, J.A.4
  • 21
    • 34249997015 scopus 로고    scopus 로고
    • How myosin VI coordinates its heads during processive movement
    • H. L. Sweeney, H. Park, A. B. Zong, Z. Yang, P. R. Selvin, and S. S. Rosenfeld, "How myosin VI coordinates its heads during processive movement," EMBO J. 26(11), 2682-2692 (2007).
    • (2007) EMBO J , vol.26 , Issue.11 , pp. 2682-2692
    • Sweeney, H.L.1    Park, H.2    Zong, A.B.3    Yang, Z.4    Selvin, P.R.5    Rosenfeld, S.S.6
  • 23
    • 77952393147 scopus 로고    scopus 로고
    • Contribution of the myosin VI tail domain to processive stepping and intramolecular tension sensing
    • A. R. Dunn, P. Chuan, Z. Bryant, and J. A. Spudich, "Contribution of the myosin VI tail domain to processive stepping and intramolecular tension sensing," Proc. Natl. Acad. Sci. U.S.A. 107(17), 7746-7750 (2010).
    • (2010) Proc. Natl. Acad. Sci. U.S.A , vol.107 , Issue.17 , pp. 7746-7750
    • Dunn, A.R.1    Chuan, P.2    Bryant, Z.3    Spudich, J.A.4
  • 25
    • 77951107295 scopus 로고    scopus 로고
    • Real-time tRNA transit on single translating ribosomes at codon resolution
    • S. Uemura, C. E. Aitken, J. Korlach, B. A. Flusberg, S. W. Turner, and J. D. Puglisi, "Real-time tRNA transit on single translating ribosomes at codon resolution," Nature 464(7291), 1012-1017 (2010).
    • (2010) Nature , vol.464 , Issue.7291 , pp. 1012-1017
    • Uemura, S.1    Aitken, C.E.2    Korlach, J.3    Flusberg, B.A.4    Turner, S.W.5    Puglisi, J.D.6
  • 26
    • 77954630782 scopus 로고    scopus 로고
    • Convex lens-induced confinement for imaging single molecules
    • S. R. Leslie, A. P. Fields, and A. E. Cohen, "Convex lens-induced confinement for imaging single molecules," Anal. Chem. 82(14), 6224-6229 (2010).
    • (2010) Anal. Chem , vol.82 , Issue.14 , pp. 6224-6229
    • Leslie, S.R.1    Fields, A.P.2    Cohen, A.E.3
  • 27
    • 13444292841 scopus 로고    scopus 로고
    • Single molecule high-resolution colocalization of Cy3 and Cy5 attached to macromolecules measures intramolecular distances through time
    • L. S. Churchman, Z. Okten, R. S. Rock, J. F. Dawson, and J. A. Spudich, "Single molecule high-resolution colocalization of Cy3 and Cy5 attached to macromolecules measures intramolecular distances through time," Proc. Natl. Acad. Sci. U.S.A. 102(5), 1419-1423 (2005).
    • (2005) Proc. Natl. Acad. Sci. U.S.A , vol.102 , Issue.5 , pp. 1419-1423
    • Churchman, L.S.1    Okten, Z.2    Rock, R.S.3    Dawson, J.F.4    Spudich, J.A.5
  • 28
    • 69749119729 scopus 로고    scopus 로고
    • Engineered myosin VI motors reveal minimal structural determinants of directionality and processivity
    • J.-C. Liao, M. W. Elting, S. L. Delp, J. A. Spudich, and Z. Bryant, "Engineered myosin VI motors reveal minimal structural determinants of directionality and processivity," J. Mol. Biol. 392(4), 862-867 (2009).
    • (2009) J. Mol. Biol , vol.392 , Issue.4 , pp. 862-867
    • Liao, J.-C.1    Elting, M.W.2    Delp, S.L.3    Spudich, J.A.4    Bryant, Z.5
  • 29
    • 0020001703 scopus 로고
    • Purification of muscle actin
    • J. D. Pardee and J. A. Spudich, "Purification of muscle actin," Methods Cell Biol. 24, 271-289 (1982).
    • (1982) Methods Cell Biol , vol.24 , pp. 271-289
    • Pardee, J.D.1    Spudich, J.A.2
  • 32
    • 0026647697 scopus 로고
    • The nucleation-release model of actin filament dynamics in cell motility
    • J. A. Theriot and T. J. Mitchison, "The nucleation-release model of actin filament dynamics in cell motility," Trends Cell Biol. 2(8), 219-222 (1992).
    • (1992) Trends Cell Biol , vol.2 , Issue.8 , pp. 219-222
    • Theriot, J.A.1    Mitchison, T.J.2
  • 33
  • 34
    • 0036713779 scopus 로고    scopus 로고
    • Microscopic analysis of polymerization dynamics with individual actin filaments
    • I. Fujiwara, S. Takahashi, H. Tadakuma, T. Funatsu, and S. Ishiwata, "Microscopic analysis of polymerization dynamics with individual actin filaments," Nat. Cell Biol. 4(9), 666-673 (2002).
    • (2002) Nat. Cell Biol , vol.4 , Issue.9 , pp. 666-673
    • Fujiwara, I.1    Takahashi, S.2    Tadakuma, H.3    Funatsu, T.4    Ishiwata, S.5
  • 35
    • 33845619142 scopus 로고    scopus 로고
    • The bacterial actin-like cytoskeleton
    • R. Carballido-López, "The bacterial actin-like cytoskeleton," Microbiol. Mol. Biol. Rev. 70(4), 888-909 (2006).
    • (2006) Microbiol. Mol. Biol. Rev , vol.70 , Issue.4 , pp. 888-909
    • Carballido-López, R.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.