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Volumn 12, Issue 3, 2011, Pages 163-176

Moving into the cell: Single-molecule studies of molecular motors in complex environments

Author keywords

[No Author keywords available]

Indexed keywords

GREEN FLUORESCENT PROTEIN; KINESIN 1; MOLECULAR MOTOR; MYOSIN II; MYOSIN V; QUANTUM DOT;

EID: 79951971261     PISSN: 14710072     EISSN: 14710080     Source Type: Journal    
DOI: 10.1038/nrm3062     Document Type: Review
Times cited : (162)

References (187)
  • 2
    • 70349437416 scopus 로고    scopus 로고
    • Kinesin superfamily motor proteins and intracellular transport
    • Hirokawa, N., Noda, Y., Tanaka, Y. & Niwa, S. Kinesin superfamily motor proteins and intracellular transport. Nature Rev. Mol. Cell Biol. 10, 682-696 (2009).
    • (2009) Nature Rev. Mol. Cell Biol. , vol.10 , pp. 682-696
    • Hirokawa, N.1    Noda, Y.2    Tanaka, Y.3    Niwa, S.4
  • 3
    • 70450228589 scopus 로고    scopus 로고
    • Regulators of the cytoplasmic dynein motor
    • Kardon, J. R. & Vale, R. D. Regulators of the cytoplasmic dynein motor. Nature Rev. Mol. Cell Biol. 10, 854-865 (2009).
    • (2009) Nature Rev. Mol. Cell Biol. , vol.10 , pp. 854-865
    • Kardon, J.R.1    Vale, R.D.2
  • 4
    • 75149128079 scopus 로고    scopus 로고
    • Myosin VI: An innovative motor that challenged the swinging lever arm hypothesis
    • Spudich, J. A. & Sivaramakrishnan, S. Myosin VI: an innovative motor that challenged the swinging lever arm hypothesis. Nature Rev. Mol. Cell Biol. 11, 128-137 (2010).
    • (2010) Nature Rev. Mol. Cell Biol. , vol.11 , pp. 128-137
    • Spudich, J.A.1    Sivaramakrishnan, S.2
  • 5
    • 70350446761 scopus 로고    scopus 로고
    • Traffic control: Regulation of kinesin motors
    • Verhey, K. J. & Hammond, J. W. Traffic control: regulation of kinesin motors. Nature Rev. Mol. Cell Biol. 10, 765-777 (2009).
    • (2009) Nature Rev. Mol. Cell Biol. , vol.10 , pp. 765-777
    • Verhey, K.J.1    Hammond, J.W.2
  • 7
    • 0036150882 scopus 로고    scopus 로고
    • Kinesin: Switch I & II and the motor mechanism
    • Kull, F. J. & Endow, S. A. Kinesin: switch I & II and the motor mechanism. J. Cell Sci. 115, 15-23 (2002).
    • (2002) J. Cell Sci. , vol.115 , pp. 15-23
    • Kull, F.J.1    Endow, S.A.2
  • 8
    • 26844566272 scopus 로고    scopus 로고
    • Fibrous Proteins: Muscle and Molecular Motors, Elsevier Academic Press Inc., San Diego
    • Geeves, M. A. & Holmes, K. C. in Advances in Protein Chemistry Vol. 71 (Fibrous Proteins: Muscle and Molecular Motors) 161-193 (Elsevier Academic Press Inc., San Diego, 2005).
    • (2005) Advances in Protein Chemistry , vol.71 , pp. 161-193
    • Geeves, M.A.1    Holmes, K.C.2
  • 9
    • 39949083937 scopus 로고    scopus 로고
    • The role of microtubules in processive kinesin movement
    • Kikkawa, M. The role of microtubules in processive kinesin movement. Trends Cell Biol. 18, 128-135 (2008).
    • (2008) Trends Cell Biol. , vol.18 , pp. 128-135
    • Kikkawa, M.1
  • 10
    • 0033576727 scopus 로고    scopus 로고
    • A structural change in the kinesin motor protein that drives motility
    • A classic study that provides evidence for the kinesin neck linker conformational change by using electron paramagnetic resonance, FRET, kinetics and electron microscopy
    • Rice, S. et al. A structural change in the kinesin motor protein that drives motility. Nature 402, 778-784 (1999). A classic study that provides evidence for the kinesin neck linker conformational change by using electron paramagnetic resonance, FRET, kinetics and electron microscopy.
    • (1999) Nature , vol.402 , pp. 778-784
    • Rice, S.1
  • 11
    • 0027194702 scopus 로고
    • Three-dimensional structure of myosin subfragment-1: A molecular motor
    • Presented the first X-ray crystallography structure of a myosin motor domain, which strongly advanced our understanding of motor function
    • Rayment, I. et al. Three-dimensional structure of myosin subfragment-1: a molecular motor. Science 261, 50-58 (1993). Presented the first X-ray crystallography structure of a myosin motor domain, which strongly advanced our understanding of motor function.
    • (1993) Science , vol.261 , pp. 50-58
    • Rayment, I.1
  • 12
    • 0027220271 scopus 로고
    • Three-dimensional atomic model of F-actin decorated with Dictyostelium myosin S1
    • Schröder, R. R. et al. Three-dimensional atomic model of F-actin decorated with Dictyostelium myosin S1. Nature 364, 171-174 (1993).
    • (1993) Nature , vol.364 , pp. 171-174
    • Schröder, R.R.1
  • 13
    • 0032483563 scopus 로고    scopus 로고
    • Crystal structure of a vertebrate smooth muscle myosin motor domain and its complex with the essential light chain: Visualization of the pre-power stroke state
    • Dominguez, R., Freyzon, Y., Trybus, K. M. & Cohen, C. Crystal structure of a vertebrate smooth muscle myosin motor domain and its complex with the essential light chain: visualization of the pre-power stroke state. Cell 94, 559-571 (1998).
    • (1998) Cell , vol.94 , pp. 559-571
    • Dominguez, R.1    Freyzon, Y.2    Trybus, K.M.3    Cohen, C.4
  • 14
    • 1642340974 scopus 로고    scopus 로고
    • Atomic structure of scallop myosin subfragment S1 complexed with MgADP: A novel conformation of the myosin head
    • Houdusse, A., Kalbokis, V. N., Himmel, D., Szent-Gyorgyi, A. G. & Cohen, C. Atomic structure of scallop myosin subfragment S1 complexed with MgADP: a novel conformation of the myosin head. Cell 97, 459-470 (1999).
    • (1999) Cell , vol.97 , pp. 459-470
    • Houdusse, A.1    Kalbokis, V.N.2    Himmel, D.3    Szent-Gyorgyi, A.G.4    Cohen, C.5
  • 15
    • 0037164812 scopus 로고    scopus 로고
    • The prepower stroke conformation of myosin V
    • Burgess, S. et al. The prepower stroke conformation of myosin V. J. Cell Biol. 159, 983-991 (2002).
    • (2002) J. Cell Biol. , vol.159 , pp. 983-991
    • Burgess, S.1
  • 16
    • 0034660532 scopus 로고    scopus 로고
    • Two-headed binding of a processive myosin to F-actin
    • Walker, M. L. et al. Two-headed binding of a processive myosin to F-actin. Nature 405, 804-807 (2000).
    • (2000) Nature , vol.405 , pp. 804-807
    • Walker, M.L.1
  • 17
    • 77952934976 scopus 로고    scopus 로고
    • Structural and functional insights into the myosin motor mechanism
    • Sweeney, H. L. & Houdusse, A. Structural and functional insights into the myosin motor mechanism. Annu. Rev. Biophys. 39, 539-57 (2010).
    • (2010) Annu. Rev. Biophys. , vol.39 , pp. 539-557
    • Sweeney, H.L.1    Houdusse, A.2
  • 18
    • 0028261701 scopus 로고
    • Single myosin molecule mechanics-piconewton forces and nanometer steps
    • Describes the three-bead single-molecule assay for myosin for the first time and is also the first report of myosin power strokes and single-molecule forces
    • Finer, J. T., Simmons, R. M. & Spudich, J. A. Single myosin molecule mechanics-piconewton forces and nanometer steps. Nature 368, 113-119 (1994). Describes the three-bead single-molecule assay for myosin for the first time and is also the first report of myosin power strokes and single-molecule forces.
    • (1994) Nature , vol.368 , pp. 113-119
    • Finer, J.T.1    Simmons, R.M.2    Spudich, J.A.3
  • 19
    • 61849174756 scopus 로고    scopus 로고
    • Biothermodynamics Part A, Eds Johnson, M. L., Holt, J. M. & Ackers, G. K Elsevier Academic Press Inc., San Diego
    • De La Cruz, E. M. & Ostap, E. M. in Methods in Enzymology Vol. 455, (Biothermodynamics Part A) (Eds Johnson, M. L., Holt, J. M. & Ackers, G. K) 157-192 (Elsevier Academic Press Inc., San Diego, 2009).
    • (2009) Methods in Enzymology , vol.455 , pp. 157-192
    • De La Cruz, E.M.1    Ostap, E.M.2
  • 20
    • 13444292382 scopus 로고    scopus 로고
    • Dynamics of actomyosin interactions in relation to the cross-bridge cycle
    • Zeng, W. et al. Dynamics of actomyosin interactions in relation to the cross-bridge cycle. Phil. Trans. R. Soc. B 359, 1843-1855 (2004).
    • (2004) Phil. Trans. R. Soc. B , vol.359 , pp. 1843-1855
    • Zeng, W.1
  • 21
    • 26844579689 scopus 로고    scopus 로고
    • Fibrous Proteins: Muscle and Molecular Motors, Elsevier Academic Press Inc., San Diego
    • Marx, A., Muller, J. & Mandelkow, E. in Advances in Protein Chemistry Vol. 71 (Fibrous Proteins: Muscle and Molecular Motors) 299-344 (Elsevier Academic Press Inc., San Diego, 2005).
    • (2005) Advances in Protein Chemistry , vol.71 , pp. 299-344
    • Marx, A.1    Muller, J.2    Mandelkow, E.3
  • 24
    • 33645531531 scopus 로고    scopus 로고
    • Structure of the MTIP-MyoA complex, a key component of the malaria parasite invasion motor
    • Bosch, J. et al. Structure of the MTIP-MyoA complex, a key component of the malaria parasite invasion motor. Proc. Natl Acad. Sci. USA 103, 4852-4857 (2006).
    • (2006) Proc. Natl Acad. Sci. USA , vol.103 , pp. 4852-4857
    • Bosch, J.1
  • 27
    • 0025052483 scopus 로고
    • Molecular structure of F-actin and location of surface binding sites
    • Milligan, R. A., Whittaker, M. & Safer, D. Molecular structure of F-actin and location of surface binding sites. Nature 348, 217-221 (1990).
    • (1990) Nature , vol.348 , pp. 217-221
    • Milligan, R.A.1    Whittaker, M.2    Safer, D.3
  • 28
    • 0027226230 scopus 로고
    • Structure of the actin-myosin complex and its implications for muscle-contraction
    • Rayment, I. et al. Structure of the actin-myosin complex and its implications for muscle-contraction. Science 261, 58-65 (1993).
    • (1993) Science , vol.261 , pp. 58-65
    • Rayment, I.1
  • 29
    • 0025868445 scopus 로고
    • Microtubule dynamics and microtubule caps: A time-resolved cryo-electron microscopy study
    • Mandelkow, E. M., Mandelkow, E. & Milligan, R. A. Microtubule dynamics and microtubule caps: a time-resolved cryo-electron microscopy study. J. Cell Biol. 114, 977-991 (1991).
    • (1991) J. Cell Biol. , vol.114 , pp. 977-991
    • Mandelkow, E.M.1    Mandelkow, E.2    Milligan, R.A.3
  • 30
    • 0029795642 scopus 로고    scopus 로고
    • Three-dimensional cryoelectron microscopy of dimeric kinesin and ncd motor domains on microtubules
    • Hirose, K., Lockhart, A., Cross, R. A. & Amos, L. A. Three-dimensional cryoelectron microscopy of dimeric kinesin and ncd motor domains on microtubules. Proc. Natl Acad. Sci. USA 93, 9539-9544 (1996).
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 9539-9544
    • Hirose, K.1    Lockhart, A.2    Cross, R.A.3    Amos, L.A.4
  • 32
    • 64049086564 scopus 로고    scopus 로고
    • 9-Ångström structure of a microtubule-bound mitotic motor
    • Bodey, A. J., Kikkawa, M. & Moores, C. A. 9-Ångström structure of a microtubule-bound mitotic motor. J. Mol. Biol. 388, 218-224 (2009).
    • (2009) J. Mol. Biol. , vol.388 , pp. 218-224
    • Bodey, A.J.1    Kikkawa, M.2    Moores, C.A.3
  • 33
    • 33746152398 scopus 로고    scopus 로고
    • The cargo-binding domain regulates structure and activity of myosin 5
    • Thirumurugan, K., Sakamoto, T., Hammer, J. A., Sellers, J. R. & Knight, P. J. The cargo-binding domain regulates structure and activity of myosin 5. Nature 442, 212-215 (2006).
    • (2006) Nature , vol.442 , pp. 212-215
    • Thirumurugan, K.1    Sakamoto, T.2    Hammer, J.A.3    Sellers, J.R.4    Knight, P.J.5
  • 34
    • 33746129173 scopus 로고    scopus 로고
    • Three-dimensional structure of the myosin V inhibited state by cryoelectron tomography
    • Liu, J., Taylor, D. W., Krementsova, E. B., Trybus, K. M. & Taylor, K. A. Three-dimensional structure of the myosin V inhibited state by cryoelectron tomography. Nature 442, 208-211 (2006).
    • (2006) Nature , vol.442 , pp. 208-211
    • Liu, J.1    Taylor, D.W.2    Krementsova, E.B.3    Trybus, K.M.4    Taylor, K.A.5
  • 35
    • 0344198646 scopus 로고    scopus 로고
    • Distinct conformations of the kinesin Unc104 neck regulate a monomer to dimer motor transition
    • Al-Bassam, J. et al. Distinct conformations of the kinesin Unc104 neck regulate a monomer to dimer motor transition. J. Cell Biol. 163, 743-753 (2003).
    • (2003) J. Cell Biol. , vol.163 , pp. 743-753
    • Al-Bassam, J.1
  • 36
    • 0033591331 scopus 로고    scopus 로고
    • Formation of the compact confomer of kinesin requires a COOH-terminal heavy chain domain and inhibits microtubule-stimulated ATPase activity
    • Stock, M. F. et al. Formation of the compact confomer of kinesin requires a COOH-terminal heavy chain domain and inhibits microtubule-stimulated ATPase activity. J. Biol. Chem. 274, 14617-14623 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 14617-14623
    • Stock, M.F.1
  • 37
    • 48249153389 scopus 로고    scopus 로고
    • The Kinesin-1 motor protein is regulated by a direct interaction of its head and tail
    • Dietrich, K. A. et al. The Kinesin-1 motor protein is regulated by a direct interaction of its head and tail. Proc. Natl Acad. Sci. USA 105, 8938-8943 (2008).
    • (2008) Proc. Natl Acad. Sci. USA , vol.105 , pp. 8938-8943
    • Dietrich, K.A.1
  • 38
    • 14844330221 scopus 로고    scopus 로고
    • Structural studies by electron tomography: From cells to molecules
    • Lucic, V., Forster, F. & Baumeister, W. Structural studies by electron tomography: from cells to molecules. Annu. Rev. Biochem. 74, 833-865 (2005).
    • (2005) Annu. Rev. Biochem. , vol.74 , pp. 833-865
    • Lucic, V.1    Forster, F.2    Baumeister, W.3
  • 39
    • 0020586332 scopus 로고
    • Movement of myosincoated fluorescent beads on actin cables in vitro
    • Sheetz, M. P. & Spudich, J. A. Movement of myosincoated fluorescent beads on actin cables in vitro. Nature 303, 31-35 (1983).
    • (1983) Nature , vol.303 , pp. 31-35
    • Sheetz, M.P.1    Spudich, J.A.2
  • 40
    • 0023919181 scopus 로고
    • Force measurements by micromanipulation of a single actin filament by glass needles
    • Kishino, A. & Yanagida, T. Force measurements by micromanipulation of a single actin filament by glass needles. Nature 334, 74-76 (1988).
    • (1988) Nature , vol.334 , pp. 74-76
    • Kishino, A.1    Yanagida, T.2
  • 41
    • 0021261156 scopus 로고
    • Direct observation of motion of single F-actin filaments in the presence of myosin
    • Yanagida, T., Nakase, M., Nishiyama, K. & Oosawa, F. Direct observation of motion of single F-actin filaments in the presence of myosin. Nature 307, 58-60 (1984).
    • (1984) Nature , vol.307 , pp. 58-60
    • Yanagida, T.1    Nakase, M.2    Nishiyama, K.3    Oosawa, F.4
  • 42
    • 0001675681 scopus 로고
    • Fluorescent actin-filaments move on myosin fixed to a glass surface
    • Kron, S. J. & Spudich, J. A. Fluorescent actin-filaments move on myosin fixed to a glass surface Proc. Natl Acad. Sci. USA 83, 6272-6276 (1986).
    • (1986) Proc. Natl Acad. Sci. USA , vol.83 , pp. 6272-6276
    • Kron, S.J.1    Spudich, J.A.2
  • 43
    • 0028803118 scopus 로고
    • Movement and force produced by a single myosin head
    • A careful study of power strokes of single myosin dimers, which properly takes into account thermal fluctuations and gives the most accurate estimate of power-stroke amplitude
    • Molloy, J. E., Burns, J. E., Kendrick-Jones, J., Tregear, R. T. & White, D. C. S. Movement and force produced by a single myosin head. Nature 378, 209-212 (1995). A careful study of power strokes of single myosin dimers, which properly takes into account thermal fluctuations and gives the most accurate estimate of power-stroke amplitude.
    • (1995) Nature , vol.378 , pp. 209-212
    • Molloy, J.E.1    Burns, J.E.2    Kendrick-Jones, J.3    Tregear, R.T.4    White, D.C.S.5
  • 44
    • 18744364420 scopus 로고    scopus 로고
    • Microscopic evidence for a minus-end-directed power stroke in the kinesin motor ncd
    • Wendt, T. G. et al. Microscopic evidence for a minus-end-directed power stroke in the kinesin motor ncd. EMBO J. 21, 5969-5978 (2002).
    • (2002) EMBO J. , vol.21 , pp. 5969-5978
    • Wendt, T.G.1
  • 46
    • 0034710696 scopus 로고    scopus 로고
    • A mutant of the motor protein kinesin that moves in both directions on microtubules
    • Endow, S. A. & Higuchi, H. A mutant of the motor protein kinesin that moves in both directions on microtubules. Nature 406, 913-916 (2000).
    • (2000) Nature , vol.406 , pp. 913-916
    • Endow, S.A.1    Higuchi, H.2
  • 47
    • 0027453868 scopus 로고
    • Direct observation of kinesin stepping by optical trapping interferometry
    • The first report on the steps and stall forces of single kinesin motors, which were measured by optical trapping
    • Svoboda, K., Schmidt, C. F., Schnapp, B. J. & Block, S. M. Direct observation of kinesin stepping by optical trapping interferometry. Nature 365, 721-727 (1993). The first report on the steps and stall forces of single kinesin motors, which were measured by optical trapping.
    • (1993) Nature , vol.365 , pp. 721-727
    • Svoboda, K.1    Schmidt, C.F.2    Schnapp, B.J.3    Block, S.M.4
  • 48
    • 0033527043 scopus 로고    scopus 로고
    • Myosin-V is a processive actin-based motor
    • Mehta, A. D. et al. Myosin-V is a processive actin-based motor. Nature 400, 590-593 (1999).
    • (1999) Nature , vol.400 , pp. 590-593
    • Mehta, A.D.1
  • 49
    • 0034646431 scopus 로고    scopus 로고
    • Processive movement of single 22S dynein molecules occurs only at low ATP concentrations
    • Hirakawa, E., Higuchi, H. & Toyoshima, Y. Y. Processive movement of single 22S dynein molecules occurs only at low ATP concentrations. Proc. Natl Acad. Sci. USA 97, 2533-2537 (2000).
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 2533-2537
    • Hirakawa, E.1    Higuchi, H.2    Toyoshima, Y.Y.3
  • 50
    • 33746253688 scopus 로고    scopus 로고
    • Single-molecule analysis of dynein processivity and stepping behavior
    • A landmark paper using quantum dots to perform single-molecule experiments with dimeric dynein, and showing processive stepping behaviour
    • Reck-Peterson, S. L. et al. Single-molecule analysis of dynein processivity and stepping behavior. Cell 126, 335-348 (2006). A landmark paper using quantum dots to perform single-molecule experiments with dimeric dynein, and showing processive stepping behaviour.
    • (2006) Cell , vol.126 , pp. 335-348
    • Reck-Peterson, S.L.1
  • 52
    • 50649121477 scopus 로고    scopus 로고
    • Advances in single-molecule fluorescence methods for molecular biology
    • Joo, C., Balci, H., Ishitsuka, Y., Buranachai, C. & Ha, T. Advances in single-molecule fluorescence methods for molecular biology. Annu. Rev. Biochem. 77, 51-76 (2008).
    • (2008) Annu. Rev. Biochem. , vol.77 , pp. 51-76
    • Joo, C.1    Balci, H.2    Ishitsuka, Y.3    Buranachai, C.4    Ha, T.5
  • 55
    • 34247571461 scopus 로고    scopus 로고
    • Kinesin motor mechanics: Binding, stepping, tracking, gating, and limping
    • Block, S. M. Kinesin motor mechanics: binding, stepping, tracking, gating, and limping. Biophys. J. 92, 2986-2995 (2007).
    • (2007) Biophys. J. , vol.92 , pp. 2986-2995
    • Block, S.M.1
  • 56
    • 60749121148 scopus 로고    scopus 로고
    • Walking the walk: How kinesin and dynein coordinate their steps
    • Gennerich, A. & Vale, R. D. Walking the walk: how kinesin and dynein coordinate their steps. Curr. Opin. Cell Biol. 21, 59-67 (2009).
    • (2009) Curr. Opin. Cell Biol. , vol.21 , pp. 59-67
    • Gennerich, A.1    Vale, R.D.2
  • 58
    • 1542299042 scopus 로고    scopus 로고
    • The mechanism of myosin VI translocation an its load-induced anchoring
    • Altman, D., Sweeney, H. L. & Spudich, J. A. The mechanism of myosin VI translocation an its load-induced anchoring. Cell 116, 737-749 (2004).
    • (2004) Cell , vol.116 , pp. 737-749
    • Altman, D.1    Sweeney, H.L.2    Spudich, J.A.3
  • 59
    • 36249009069 scopus 로고    scopus 로고
    • Force-induced bidirectional stepping of cytoplasmic dynein
    • Showed, in a single-molecule assay, that the processive myosin V motor takes a step in two phases and, further, that it needs a thermal fluctuation to reach its next binding site
    • Gennerich, A., Carter, A. P., Reck-Peterson, S. L. & Vale, R. D. Force-induced bidirectional stepping of cytoplasmic dynein. Cell 131, 952-965 (2007). Showed, in a single-molecule assay, that the processive myosin V motor takes a step in two phases and, further, that it needs a thermal fluctuation to reach its next binding site.
    • (2007) Cell , vol.131 , pp. 952-965
    • Gennerich, A.1    Carter, A.P.2    Reck-Peterson, S.L.3    Vale, R.D.4
  • 60
    • 0028362896 scopus 로고
    • Force and velocity measured for single kinesin molecules
    • Svoboda, K. & Block, S. M. Force and velocity measured for single kinesin molecules. Cell 77, 773-784 (1994).
    • (1994) Cell , vol.77 , pp. 773-784
    • Svoboda, K.1    Block, S.M.2
  • 62
    • 0030744142 scopus 로고    scopus 로고
    • Kinesin hydrolyses one ATP per 8-nm step
    • A landmark paper that proves, from the statistical analysis of single-molecule data, that kinesin uses one ATP molecule per 8 nm step
    • Schnitzer, M. J. & Block, S. M. Kinesin hydrolyses one ATP per 8-nm step. Nature 388, 386-390 (1997). A landmark paper that proves, from the statistical analysis of single-molecule data, that kinesin uses one ATP molecule per 8 nm step.
    • (1997) Nature , vol.388 , pp. 386-390
    • Schnitzer, M.J.1    Block, S.M.2
  • 63
    • 51349088578 scopus 로고    scopus 로고
    • Direct observation of the mechanochemical coupling in myosin Va during processive movement
    • Sakamoto, T., Webb, M. R., Forgacs, E., White, H. D. & Sellers, J. R. Direct observation of the mechanochemical coupling in myosin Va during processive movement. Nature 455, 128-132 (2008).
    • (2008) Nature , vol.455 , pp. 128-132
    • Sakamoto, T.1    Webb, M.R.2    Forgacs, E.3    White, H.D.4    Sellers, J.R.5
  • 64
    • 0033535556 scopus 로고    scopus 로고
    • The motor protein myosin-I produces its working stroke in two steps
    • Veigel, C. et al. The motor protein myosin-I produces its working stroke in two steps. Nature 398, 530-533 (1999).
    • (1999) Nature , vol.398 , pp. 530-533
    • Veigel, C.1
  • 66
    • 34848923743 scopus 로고    scopus 로고
    • Myosin V stepping mechanism
    • Cappello, G. et al. Myosin V stepping mechanism. Proc. Natl Acad. Sci. USA 104, 15328-15333 (2007).
    • (2007) Proc. Natl Acad. Sci. USA , vol.104 , pp. 15328-15333
    • Cappello, G.1
  • 67
    • 77951978236 scopus 로고    scopus 로고
    • Direct observation of the myosin-Va power stroke and its reversal
    • The first direct evidence that the myosin power stroke can be physically reversed, which has important implications for motor regulation in cells
    • Sellers, J. R. & Veigel, C. Direct observation of the myosin-Va power stroke and its reversal. Nature Struct. Mol. Biol. 17, 590-595 (2010). The first direct evidence that the myosin power stroke can be physically reversed, which has important implications for motor regulation in cells.
    • (2010) Nature Struct. Mol. Biol. , vol.17 , pp. 590-595
    • Sellers, J.R.1    Veigel, C.2
  • 68
    • 26944449015 scopus 로고    scopus 로고
    • Load-dependent kinetics of myosin-V can explain its high processivity
    • Veigel, C., Schmitz, S., Wang, F. & Sellers, J. R. Load-dependent kinetics of myosin-V can explain its high processivity. Nature Cell Biol. 7, 861-869 (2005).
    • (2005) Nature Cell Biol. , vol.7 , pp. 861-869
    • Veigel, C.1    Schmitz, S.2    Wang, F.3    Sellers, J.R.4
  • 69
    • 0242609969 scopus 로고    scopus 로고
    • Load-dependent kinetics of force production by smooth muscle myosin measured with optical tweezers
    • Veigel, C., Molloy, J. E., Schmitz, S. & Kendrick-Jones, J. Load-dependent kinetics of force production by smooth muscle myosin measured with optical tweezers. Nature Cell Biol. 5, 980-986 (2003).
    • (2003) Nature Cell Biol. , vol.5 , pp. 980-986
    • Veigel, C.1    Molloy, J.E.2    Schmitz, S.3    Kendrick-Jones, J.4
  • 70
    • 62049083505 scopus 로고    scopus 로고
    • Helix sliding in the stalk coiled coil of dynein couples ATPase and microtubule binding
    • Kon, T. et al. Helix sliding in the stalk coiled coil of dynein couples ATPase and microtubule binding. Nature Struct. Mol. Biol. 16, 325-333 (2009).
    • (2009) Nature Struct. Mol. Biol. , vol.16 , pp. 325-333
    • Kon, T.1
  • 71
    • 0347623370 scopus 로고    scopus 로고
    • Kinesin moves by an asymmetric hand-over-hand mechanism
    • Asbury, C. L., Fehr, A. N. & Block, S. M. Kinesin moves by an asymmetric hand-over-hand mechanism. Science 302, 2130-2134 (2003).
    • (2003) Science , vol.302 , pp. 2130-2134
    • Asbury, C.L.1    Fehr, A.N.2    Block, S.M.3
  • 72
    • 0037832404 scopus 로고    scopus 로고
    • Myosin V walks hand-over-hand: Single fluorophore imaging with 1.5-nm localization
    • Yildiz, A. et al. Myosin V walks hand-over-hand: single fluorophore imaging with 1.5-nm localization. Science 300, 2061-2065 (2003).
    • (2003) Science , vol.300 , pp. 2061-2065
    • Yildiz, A.1
  • 74
    • 17844385071 scopus 로고    scopus 로고
    • Differential labeling of myosin V heads with quantum dots allows direct visualization of hand-over-hand processivity
    • Warshaw, D. M. et al. Differential labeling of myosin V heads with quantum dots allows direct visualization of hand-over-hand processivity. Biophys. J. 88, L30-L32 (2005).
    • (2005) Biophys. J. , vol.88
    • Warshaw, D.M.1
  • 75
    • 69949092035 scopus 로고    scopus 로고
    • Direct observation of the binding state of the kinesin head to the microtubule
    • Guydosh, N. R. & Block, S. M. Direct observation of the binding state of the kinesin head to the microtubule. Nature 461, 125-128 (2009).
    • (2009) Nature , vol.461 , pp. 125-128
    • Guydosh, N.R.1    Block, S.M.2
  • 77
    • 19644377414 scopus 로고    scopus 로고
    • Mechanics of the kinesin step
    • Carter, N. J. & Cross, R. A. Mechanics of the kinesin step. Nature 435, 308-312 (2005).
    • (2005) Nature , vol.435 , pp. 308-312
    • Carter, N.J.1    Cross, R.A.2
  • 78
    • 50649125304 scopus 로고    scopus 로고
    • Structure and mechanics of membrane proteins
    • Engel, A. & Gaub, H. E. Structure and mechanics of membrane proteins. Annu. Rev. Biochem. 77, 127-148 (2008).
    • (2008) Annu. Rev. Biochem. , vol.77 , pp. 127-148
    • Engel, A.1    Gaub, H.E.2
  • 80
    • 4143107868 scopus 로고    scopus 로고
    • Resolving the molecular structure of microtubules under physiological conditions with scanning force microscopy
    • Schaap, I. A. T., de Pablo, P. J. & Schmidt, C. F. Resolving the molecular structure of microtubules under physiological conditions with scanning force microscopy. Eur. Biophys. J. 33, 462-467 (2004).
    • (2004) Eur. Biophys. J. , vol.33 , pp. 462-467
    • Schaap, I.A.T.1    De Pablo, P.J.2    Schmidt, C.F.3
  • 81
    • 33746784797 scopus 로고    scopus 로고
    • Elastic response, buckling, and instability of microtubules under radial indentation
    • Schaap, I. A. T., Carrasco, C., de Pablo, P. J., MacKintosh, F. C. & Schmidt, C. F. Elastic response, buckling, and instability of microtubules under radial indentation. Biophys. J. 91, 1521-1531 (2006).
    • (2006) Biophys. J. , vol.91 , pp. 1521-1531
    • Schaap, I.A.T.1    Carrasco, C.2    De Pablo, P.J.3    MacKintosh, F.C.4    Schmidt, C.F.5
  • 82
    • 34249008806 scopus 로고    scopus 로고
    • Tau protein binding forms a 1 nm thick layer along protofilaments without affecting the radial elasticity of microtubules
    • Schaap, I. A. T., Hoffmann, B., Carrasco, C., Merkel, R. & Schmidt, C. F. Tau protein binding forms a 1 nm thick layer along protofilaments without affecting the radial elasticity of microtubules. J. Struct. Biol. 158, 282-292 (2007).
    • (2007) J. Struct. Biol. , vol.158 , pp. 282-292
    • Schaap, I.A.T.1    Hoffmann, B.2    Carrasco, C.3    Merkel, R.4    Schmidt, C.F.5
  • 83
    • 43149090623 scopus 로고    scopus 로고
    • Cytoskeletal filaments and their associated proteins studied with atomic force microscopy
    • Schaap, I. A. T. et al. Cytoskeletal filaments and their associated proteins studied with atomic force microscopy. Biophys. J. (Suppl) 309A (2007).
    • (2007) Biophys. J. , Issue.SUPPL.
    • Schaap, I.A.T.1
  • 84
    • 78149285270 scopus 로고    scopus 로고
    • Video imaging of walking myosin V by high-speed atomic force microscopy
    • Kodera, N., Yamamoto, D., Ishikawa, R. & Ando, T. Video imaging of walking myosin V by high-speed atomic force microscopy. Nature 468, 72-76 (2010).
    • (2010) Nature , vol.468 , pp. 72-76
    • Kodera, N.1    Yamamoto, D.2    Ishikawa, R.3    Ando, T.4
  • 85
    • 34548457759 scopus 로고    scopus 로고
    • Tip-sample distance control using photothermal actuation of a small cantilever for highspeed atomic force microscopy
    • Yamashita, H. et al. Tip-sample distance control using photothermal actuation of a small cantilever for highspeed atomic force microscopy. Rev. Sci. Instr. 78, 083702 (2007).
    • (2007) Rev. Sci. Instr. , vol.78 , pp. 083702
    • Yamashita, H.1
  • 86
    • 67650762824 scopus 로고    scopus 로고
    • Super-resolution fluorescence microscopy
    • Huang, B., Bates, M. & Zhuang, X. W. Super-resolution fluorescence microscopy. Annu. Rev. Biochem. 78, 993-1016 (2009).
    • (2009) Annu. Rev. Biochem. , vol.78 , pp. 993-1016
    • Huang, B.1    Bates, M.2    Zhuang, X.W.3
  • 87
    • 0021717324 scopus 로고
    • Detection of single microtubules in living cells - Particle transport can occur in both directions along the same microtubule
    • Hayden, J. H. & Allen, R. D. Detection of single microtubules in living cells - particle transport can occur in both directions along the same microtubule. J. Cell Biol. 99, 1785-1793 (1984).
    • (1984) J. Cell Biol. , vol.99 , pp. 1785-1793
    • Hayden, J.H.1    Allen, R.D.2
  • 88
    • 0022019741 scopus 로고
    • Single microtubules from squid axoplams support bidirectional movement of organelles
    • Schnapp, B. J., Vale, R. D., Sheetz, M. P. & Reese, T. S. Single microtubules from squid axoplams support bidirectional movement of organelles. Cell 40, 455-462 (1985).
    • (1985) Cell , vol.40 , pp. 455-462
    • Schnapp, B.J.1    Vale, R.D.2    Sheetz, M.P.3    Reese, T.S.4
  • 89
    • 34250969819 scopus 로고
    • The demonstration of bacterial flagella by means of the phase microscope
    • Burcik, E. & Plankenhorn, B. The demonstration of bacterial flagella by means of the phase microscope. Arch. Mikrobiol. 19, 435-437 (1953).
    • (1953) Arch. Mikrobiol. , vol.19 , pp. 435-437
    • Burcik, E.1    Plankenhorn, B.2
  • 90
    • 0022492523 scopus 로고
    • Visualization of the dynamic instability of individual microtubules by dark-field microscopy
    • Horio, T. & Hotani, H. Visualization of the dynamic instability of individual microtubules by dark-field microscopy. Nature 321, 605-607 (1986).
    • (1986) Nature , vol.321 , pp. 605-607
    • Horio, T.1    Hotani, H.2
  • 91
    • 79951986650 scopus 로고
    • Individual actin-filaments visualized by DIC (Nomarski) microscopy
    • Stemmer, A. Individual actin-filaments visualized by DIC (Nomarski) microscopy. Biol. Bull. 183, 360-361 (1992).
    • (1992) Biol. Bull. , vol.183 , pp. 360-361
    • Stemmer, A.1
  • 92
    • 0037474152 scopus 로고    scopus 로고
    • Zero-mode waveguides for single-molecule analysis at high concentrations
    • Levene, M. J. et al. Zero-mode waveguides for single-molecule analysis at high concentrations. Science 299, 682-686 (2003).
    • (2003) Science , vol.299 , pp. 682-686
    • Levene, M.J.1
  • 95
    • 33847680889 scopus 로고    scopus 로고
    • Dynamics of the unbound head during myosin V processive translocation
    • Dunn, A. R. & Spudich, J. A. Dynamics of the unbound head during myosin V processive translocation. Nature Struct. Mol. Biol. 14, 246-248 (2007).
    • (2007) Nature Struct. Mol. Biol. , vol.14 , pp. 246-248
    • Dunn, A.R.1    Spudich, J.A.2
  • 96
    • 0033953433 scopus 로고    scopus 로고
    • Single-target molecule detection with nonbleaching multicolor optical immunolabels
    • Schultz, S., Smith, D. R., Mock, J. J. & Schultz, D. A. Single-target molecule detection with nonbleaching multicolor optical immunolabels. Proc. Natl Acad. Sci. USA 97, 996-1001 (2000).
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 996-1001
    • Schultz, S.1    Smith, D.R.2    Mock, J.J.3    Schultz, D.A.4
  • 97
    • 0020659058 scopus 로고
    • Total internal reflection fluorescent microscopy
    • Axelrod, D., Thompson, N. L. & Burghardt, T. P. Total internal reflection fluorescent microscopy. J. Microsc. 129, 19-28 (1983).
    • (1983) J. Microsc. , vol.129 , pp. 19-28
    • Axelrod, D.1    Thompson, N.L.2    Burghardt, T.P.3
  • 98
    • 0037804221 scopus 로고    scopus 로고
    • Myosin motors walk the walk
    • Molloy, J. E. & Veigel, C. Myosin motors walk the walk. Science 300, 2045-2046 (2003).
    • (2003) Science , vol.300 , pp. 2045-2046
    • Molloy, J.E.1    Veigel, C.2
  • 99
    • 13444292841 scopus 로고    scopus 로고
    • Single molecule high-resolution colocalization of Cy3 and Cy5 attached to macromolecules measures intramolecular distances through time
    • Churchman, L. S., Okten, Z., Rock, R. S., Dawson, J. F. & Spudich, J. A. Single molecule high-resolution colocalization of Cy3 and Cy5 attached to macromolecules measures intramolecular distances through time. Proc. Natl Acad. Sci. USA 102, 1419-1423 (2005).
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , pp. 1419-1423
    • Churchman, L.S.1    Okten, Z.2    Rock, R.S.3    Dawson, J.F.4    Spudich, J.A.5
  • 100
    • 77956634165 scopus 로고    scopus 로고
    • Switch between large hand-over-hand and small inchworm-like steps in myosin VI
    • Nishikawa, S. et al. Switch between large hand-over-hand and small inchworm-like steps in myosin VI. Cell 142, 879-888 (2010).
    • (2010) Cell , vol.142 , pp. 879-888
    • Nishikawa, S.1
  • 101
    • 34948867142 scopus 로고    scopus 로고
    • Myosin-V makes two brownian 90° rotations per 36-nm step
    • Komori, Y., Iwane, A. H. & Yanagida, T. Myosin-V makes two brownian 90° rotations per 36-nm step. Nature Struct. Mol. Biol. 14, 968-973 (2007).
    • (2007) Nature Struct. Mol. Biol. , vol.14 , pp. 968-973
    • Komori, Y.1    Iwane, A.H.2    Yanagida, T.3
  • 102
    • 2342582682 scopus 로고    scopus 로고
    • Single-molecule high-resolution imaging with photobleaching
    • Gordon, M. P., Ha, T. & Selvin, P. R. Single-molecule high-resolution imaging with photobleaching. Proc. Natl Acad. Sci. USA 101, 6462-6465 (2004).
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 6462-6465
    • Gordon, M.P.1    Ha, T.2    Selvin, P.R.3
  • 103
    • 3843104585 scopus 로고    scopus 로고
    • Nanometer-localized multiple single-molecule fluorescence microscopy
    • Qu, X. H., Wu, D., Mets, L. & Scherer, N. F. Nanometer-localized multiple single-molecule fluorescence microscopy. Proc. Natl Acad. Sci. USA 101, 11298-11303 (2004).
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 11298-11303
    • Qu, X.H.1    Wu, D.2    Mets, L.3    Scherer, N.F.4
  • 104
    • 23244444140 scopus 로고    scopus 로고
    • Interhead distance measurements in myosin VI via SHRImP support a simplified hand-over-hand model
    • Balci, H., Ha, T., Sweeney, H. L. & Selvin, P. R. Interhead distance measurements in myosin VI via SHRImP support a simplified hand-over-hand model. Biophys. J. 89, 413-417 (2005).
    • (2005) Biophys. J. , vol.89 , pp. 413-417
    • Balci, H.1    Ha, T.2    Sweeney, H.L.3    Selvin, P.R.4
  • 105
    • 36749068925 scopus 로고    scopus 로고
    • How kinesin waits between steps
    • An important study that applied single-molecule FRET to analyse the relative position of the two heads of a kinesin motor during processive movement
    • Mori, T., Vale, R. D. & Tomishige, M. How kinesin waits between steps. Nature 450, 750-754 (2007). An important study that applied single-molecule FRET to analyse the relative position of the two heads of a kinesin motor during processive movement.
    • (2007) Nature , vol.450 , pp. 750-754
    • Mori, T.1    Vale, R.D.2    Tomishige, M.3
  • 106
    • 0012112253 scopus 로고    scopus 로고
    • Orientational imaging of single molecules by annular illumination
    • Sick, B., Hecht, B. & Novotny, L. Orientational imaging of single molecules by annular illumination. Phys. Rev. Lett. 85, 4482-4485 (2000).
    • (2000) Phys. Rev. Lett. , vol.85 , pp. 4482-4485
    • Sick, B.1    Hecht, B.2    Novotny, L.3
  • 107
    • 33646237832 scopus 로고    scopus 로고
    • Defocused orientation and position imaging (DOPI) of myosin V
    • Toprak, E. et al. Defocused orientation and position imaging (DOPI) of myosin V. Proc. Natl Acad. Sci. USA 103, 6495-6499 (2006).
    • (2006) Proc. Natl Acad. Sci. USA , vol.103 , pp. 6495-6499
    • Toprak, E.1
  • 108
    • 0034995132 scopus 로고    scopus 로고
    • ADP-induced rocking of the kinesin motor domain revealed by single-molecule fluorescence polarization microscopy
    • Sosa, H., Peterman, E. J. G., Moerner, W. E. & Goldstein, L. S. B. ADP-induced rocking of the kinesin motor domain revealed by single-molecule fluorescence polarization microscopy. Nature Struct. Biol. 8, 540-544 (2001).
    • (2001) Nature Struct. Biol. , vol.8 , pp. 540-544
    • Sosa, H.1    Peterman, E.J.G.2    Moerner, W.E.3    Goldstein, L.S.B.4
  • 109
    • 0033615015 scopus 로고    scopus 로고
    • Dynamic measurement of myosin light-chain-domain tilt and twist in muscle contraction
    • Corrie, J. E. T. et al. Dynamic measurement of myosin light-chain-domain tilt and twist in muscle contraction. Nature 400, 425-430 (1999).
    • (1999) Nature , vol.400 , pp. 425-430
    • Corrie, J.E.T.1
  • 110
    • 0037468838 scopus 로고    scopus 로고
    • Three-dimensional structural dynamics of myosin V by single-molecule fluorescence polarization
    • Forkey, J. N., Quinlan, M. E., Shaw, M. A., Corrie, J. E. T. & Goldman, Y. E. Three-dimensional structural dynamics of myosin V by single-molecule fluorescence polarization. Nature 422, 399-404 (2003).
    • (2003) Nature , vol.422 , pp. 399-404
    • Forkey, J.N.1    Quinlan, M.E.2    Shaw, M.A.3    Corrie, J.E.T.4    Goldman, Y.E.5
  • 111
    • 34249948276 scopus 로고    scopus 로고
    • Myosin V walks by lever action and Brownian motion
    • Shiroguchi, K. & Kinosita, K. Myosin V walks by lever action and Brownian motion. Science 316, 1208-1212 (2007).
    • (2007) Science , vol.316 , pp. 1208-1212
    • Shiroguchi, K.1    Kinosita, K.2
  • 112
    • 8544226261 scopus 로고    scopus 로고
    • A series of related nucleotide analogues that aids optimization of fluorescence signals in probing the mechanism of P-loop ATPases, such as actomyosin
    • Webb, M. R., Reid, G. P., Munasinghe, V. R. N. & Corrie, J. E. T. A series of related nucleotide analogues that aids optimization of fluorescence signals in probing the mechanism of P-loop ATPases, such as actomyosin. Biochemistry 43, 14463-14471 (2004).
    • (2004) Biochemistry , vol.43 , pp. 14463-14471
    • Webb, M.R.1    Reid, G.P.2    Munasinghe, V.R.N.3    Corrie, J.E.T.4
  • 113
    • 0032559298 scopus 로고    scopus 로고
    • Simultaneous observation of individual ATPase and mechanical events by a single myosin molecule during interaction with actin
    • Ishijima, A. et al. Simultaneous observation of individual ATPase and mechanical events by a single myosin molecule during interaction with actin. Cell 92, 161-171 (1998).
    • (1998) Cell , vol.92 , pp. 161-171
    • Ishijima, A.1
  • 114
    • 2642522184 scopus 로고    scopus 로고
    • Combining optical trapping and single-molecule fluorescence spectroscopy: Enhanced photobleaching of fluorophores
    • van Dijk, M. A., Kapitein, L. C., van Mameren, J., Schmidt, C. F. & Peterman, E. J. G. Combining optical trapping and single-molecule fluorescence spectroscopy: enhanced photobleaching of fluorophores. J. Phys. Chem. B 108, 6479-6484 (2004).
    • (2004) J. Phys. Chem. B , vol.108 , pp. 6479-6484
    • Van Dijk, M.A.1    Kapitein, L.C.2    Van Mameren, J.3    Schmidt, C.F.4    Peterman, E.J.G.5
  • 115
    • 17444366080 scopus 로고    scopus 로고
    • Simultaneous, coincident optical trapping and single-molecule fluorescence
    • Lang, M. J., Fordyce, P. M., Engh, A. M., Neuman, K. C. & Block, S. M. Simultaneous, coincident optical trapping and single-molecule fluorescence. Nature Methods 1, 133-139 (2004).
    • (2004) Nature Methods , vol.1 , pp. 133-139
    • Lang, M.J.1    Fordyce, P.M.2    Engh, A.M.3    Neuman, K.C.4    Block, S.M.5
  • 116
    • 33746702015 scopus 로고    scopus 로고
    • Interlaced optical force-fluorescence measurements for single molecule biophysics
    • Brau, R. R., Tarsa, P. B., Ferrer, J. M., Lee, P. & Lang, M. J. Interlaced optical force-fluorescence measurements for single molecule biophysics. Biophys. J. 91, 1069-1077 (2006).
    • (2006) Biophys. J. , vol.91 , pp. 1069-1077
    • Brau, R.R.1    Tarsa, P.B.2    Ferrer, J.M.3    Lee, P.4    Lang, M.J.5
  • 117
    • 0037119610 scopus 로고    scopus 로고
    • Photothermal imaging of nanometer-sized metal particles among scatterers
    • Boyer, D., Tamarat, P., Maali, A., Lounis, B. & Orrit, M. Photothermal imaging of nanometer-sized metal particles among scatterers. Science 297, 1160-1163 (2002).
    • (2002) Science , vol.297 , pp. 1160-1163
    • Boyer, D.1    Tamarat, P.2    Maali, A.3    Lounis, B.4    Orrit, M.5
  • 118
    • 33947697260 scopus 로고    scopus 로고
    • Automatic detection of single fluorophores in live cells
    • Mashanov, G. I. & Molloy, J. E. Automatic detection of single fluorophores in live cells. Biophys. J. 92, 2199-2211 (2007).
    • (2007) Biophys. J. , vol.92 , pp. 2199-2211
    • Mashanov, G.I.1    Molloy, J.E.2
  • 119
    • 77952215650 scopus 로고    scopus 로고
    • Optimized localization analysis for single-molecule tracking and super-resolution microscopy
    • Mortensen, K. I., Churchman, L. S., Spudich, J. A. & Flyvbjerg, H. Optimized localization analysis for single-molecule tracking and super-resolution microscopy. Nature Methods 7, 377-381 (2010).
    • (2010) Nature Methods , vol.7 , pp. 377-381
    • Mortensen, K.I.1    Churchman, L.S.2    Spudich, J.A.3    Flyvbjerg, H.4
  • 120
    • 33646950699 scopus 로고    scopus 로고
    • The depolymerizing kinesin MCAK uses lattice diffusion to rapidly target microtubule ends
    • Describes a single-molecule fluorescence assay that showed that the microtubule-depolymerizing Kinesin-13 MCAK (mitotic centromere-associated kinesin; also known as KIF2C) uses 1D diffusion to reach the microtubule ends
    • Helenius, J., Brouhard, G., Kalaidzidis, Y., Diez, S. & Howard, J. The depolymerizing kinesin MCAK uses lattice diffusion to rapidly target microtubule ends. Nature 441, 115-119 (2006). Describes a single-molecule fluorescence assay that showed that the microtubule-depolymerizing Kinesin-13 MCAK (mitotic centromere-associated kinesin; also known as KIF2C) uses 1D diffusion to reach the microtubule ends.
    • (2006) Nature , vol.441 , pp. 115-119
    • Helenius, J.1    Brouhard, G.2    Kalaidzidis, Y.3    Diez, S.4    Howard, J.5
  • 121
    • 0033582814 scopus 로고    scopus 로고
    • A processive single-headed motor: Kinesin superfamily protein KIF1A
    • Okada, Y. & Hirokawa, N. A processive single-headed motor: kinesin superfamily protein KIF1A. Science 283, 1152-1157 (1999).
    • (1999) Science , vol.283 , pp. 1152-1157
    • Okada, Y.1    Hirokawa, N.2
  • 122
    • 0034681137 scopus 로고    scopus 로고
    • Mechanism of the single-headed processivity: Diffusional anchoring between the K-loop of kinesin and the C terminus of tubulin
    • Okada, Y. & Hirokawa, N. Mechanism of the single-headed processivity: diffusional anchoring between the K-loop of kinesin and the C terminus of tubulin. Proc. Natl Acad. Sci. USA 97, 640-645 (2000).
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 640-645
    • Okada, Y.1    Hirokawa, N.2
  • 123
    • 70350425612 scopus 로고    scopus 로고
    • Diffusive movement of processive Kinesin-1 on microtubules
    • Lu, H. L., Ali, M. Y., Bookwalter, C. S., Warshaw, D. M. & Trybus, K. M. Diffusive movement of processive Kinesin-1 on microtubules. Traffic 10, 1429-1438 (2009).
    • (2009) Traffic , vol.10 , pp. 1429-1438
    • Lu, H.L.1    Ali, M.Y.2    Bookwalter, C.S.3    Warshaw, D.M.4    Trybus, K.M.5
  • 124
    • 34047262039 scopus 로고    scopus 로고
    • Myosin Va maneuvers through actin intersections and diffuses along microtubules
    • Ali, M. Y. et al. Myosin Va maneuvers through actin intersections and diffuses along microtubules. Proc. Natl Acad. Sci. USA 104, 4332-4336 (2007).
    • (2007) Proc. Natl Acad. Sci. USA , vol.104 , pp. 4332-4336
    • Ali, M.Y.1
  • 126
    • 70149111601 scopus 로고    scopus 로고
    • Kinesin-8 motors act cooperatively to mediate length-dependent microtubule depolymerization
    • Varga, V., Leduc, C., Bormuth, V., Diez, S. & Howard, J. Kinesin-8 motors act cooperatively to mediate length-dependent microtubule depolymerization. Cell 138, 1174-1183 (2009).
    • (2009) Cell , vol.138 , pp. 1174-1183
    • Varga, V.1    Leduc, C.2    Bormuth, V.3    Diez, S.4    Howard, J.5
  • 127
    • 55249101931 scopus 로고    scopus 로고
    • Microtubule-driven multimerization recruits ase1p onto overlapping microtubules
    • Kapitein, L. C. et al. Microtubule-driven multimerization recruits ase1p onto overlapping microtubules. Curr. Biol. 18, 1713-1717 (2008).
    • (2008) Curr. Biol. , vol.18 , pp. 1713-1717
    • Kapitein, L.C.1
  • 128
    • 18344371892 scopus 로고    scopus 로고
    • The bipolar mitotic kinesin Eg5 moves on both microtubules that it crosslinks
    • Kapitein, L. C. et al. The bipolar mitotic kinesin Eg5 moves on both microtubules that it crosslinks. Nature 435, 114-118 (2005).
    • (2005) Nature , vol.435 , pp. 114-118
    • Kapitein, L.C.1
  • 129
    • 57649086182 scopus 로고    scopus 로고
    • The homotetrameric Kinesin-5 KLP61F preferentially crosslinks microtubules into antiparallel orientations
    • van den Wildenberg, S. et al. The homotetrameric Kinesin-5 KLP61F preferentially crosslinks microtubules into antiparallel orientations. Curr. Biol. 18, 1860-1864 (2008).
    • (2008) Curr. Biol. , vol.18 , pp. 1860-1864
    • Van Den Wildenberg, S.1
  • 130
    • 33747624954 scopus 로고    scopus 로고
    • Allosteric inhibition of Kinesin-5 modulates its processive directional motility
    • Kwok, B. H. et al. Allosteric inhibition of Kinesin-5 modulates its processive directional motility. Nature Chem. Biol. 2, 480-485 (2006).
    • (2006) Nature Chem. Biol. , vol.2 , pp. 480-485
    • Kwok, B.H.1
  • 131
    • 77953081400 scopus 로고    scopus 로고
    • The effect of monastrol on the processive motility of a dimeric Kinesin-5 head/Kinesin-1 stalk chimera
    • Lakämper, S. et al. The effect of monastrol on the processive motility of a dimeric Kinesin-5 head/Kinesin-1 stalk chimera. J. Mol. Biol. 399, 1-8 (2010).
    • (2010) J. Mol. Biol. , vol.399 , pp. 1-8
    • Lakämper, S.1
  • 132
    • 49749107045 scopus 로고    scopus 로고
    • Microtubule cross-linking triggers the directional motility of Kinesin-5
    • Single-molecule fluorescence was used here to observe the cargo-dependent switching on and off of a bipolar mitotic kinesin motor
    • Kapitein, L. C. et al. Microtubule cross-linking triggers the directional motility of Kinesin-5. J. Cell Biol. 182, 421-428 (2008). Single-molecule fluorescence was used here to observe the cargo-dependent switching on and off of a bipolar mitotic kinesin motor.
    • (2008) J. Cell Biol. , vol.182 , pp. 421-428
    • Kapitein, L.C.1
  • 133
    • 0035033890 scopus 로고    scopus 로고
    • Autofluorescent proteins in single-molecule research: Applications to live cell imaging microscopy
    • Harms, G. S., Cognet, L., Lommerse, P. H. M., Blab, G. A. & Schmidt, T. Autofluorescent proteins in single-molecule research: applications to live cell imaging microscopy. Biophys. J. 80, 2396-2408 (2001).
    • (2001) Biophys. J. , vol.80 , pp. 2396-2408
    • Harms, G.S.1    Cognet, L.2    Lommerse, P.H.M.3    Blab, G.A.4    Schmidt, T.5
  • 134
  • 135
    • 2442595175 scopus 로고    scopus 로고
    • The spatial and temporal dynamics of pleckstrin homology domain binding at the plasma membrane measured by imaging single molecules in live mouse myoblasts
    • Mashanov, G. I., Tacon, D., Peckham, M. & Molloy, J. E. The spatial and temporal dynamics of pleckstrin homology domain binding at the plasma membrane measured by imaging single molecules in live mouse myoblasts. J. Biol. Chem. 279, 15274-15280 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 15274-15280
    • Mashanov, G.I.1    Tacon, D.2    Peckham, M.3    Molloy, J.E.4
  • 136
    • 20344382542 scopus 로고    scopus 로고
    • Kinesin and dynein move a peroxisome in vivo: A tug-of-war or coordinated movement?
    • Kural, C. et al. Kinesin and dynein move a peroxisome in vivo: a tug-of-war or coordinated movement? Science 308, 1469-1472 (2005).
    • (2005) Science , vol.308 , pp. 1469-1472
    • Kural, C.1
  • 137
    • 30344436982 scopus 로고    scopus 로고
    • Observation of individual microtubule motor steps in living cells with endocytosed quantum dots
    • Nan, X. L., Sims, P. A., Chen, P. & Xie, X. S. Observation of individual microtubule motor steps in living cells with endocytosed quantum dots. J. Phys. Chem. B 109, 24220-24224 (2005).
    • (2005) J. Phys. Chem. B , vol.109 , pp. 24220-24224
    • Nan, X.L.1    Sims, P.A.2    Chen, P.3    Xie, X.S.4
  • 138
    • 34547477550 scopus 로고    scopus 로고
    • Detection of fractional steps in cargo movement by the collective operation of Kinesin-1 motors
    • Leduc, C., Ruhnow, F., Howard, J. & Diez, S. Detection of fractional steps in cargo movement by the collective operation of Kinesin-1 motors. Proc. Natl Acad. Sci. USA 104, 10847-10852 (2007).
    • (2007) Proc. Natl Acad. Sci. USA , vol.104 , pp. 10847-10852
    • Leduc, C.1    Ruhnow, F.2    Howard, J.3    Diez, S.4
  • 139
    • 68049143191 scopus 로고    scopus 로고
    • Velocity, processivity, and individual steps of single myosin V molecules in live cells
    • Pierobon, P. et al. Velocity, processivity, and individual steps of single myosin V molecules in live cells. Biophys. J. 96, 4268-4275 (2009).
    • (2009) Biophys. J. , vol.96 , pp. 4268-4275
    • Pierobon, P.1
  • 140
    • 68949125193 scopus 로고    scopus 로고
    • Random walk of processive, quantum dot-labeled myosin Va molecules within the actin cortex of COS-7 Cells
    • References 139 and 140 are landmark papers reporting the single-molecule observation of quantum-dot-labelled myosin V in cells
    • Nelson, S. R., Ali, M. Y., Trybus, K. M. & Warshaw, D. M. Random walk of processive, quantum dot-labeled myosin Va molecules within the actin cortex of COS-7 Cells. Biophys. J. 97, 509-518 (2009). References 139 and 140 are landmark papers reporting the single-molecule observation of quantum-dot-labelled myosin V in cells.
    • (2009) Biophys. J. , vol.97 , pp. 509-518
    • Nelson, S.R.1    Ali, M.Y.2    Trybus, K.M.3    Warshaw, D.M.4
  • 141
    • 34250372604 scopus 로고    scopus 로고
    • Tracking single kinesin molecules in the cytoplasm of mammalian cells
    • Cai, D. W., Verhey, K. J. & Meyhofer, E. Tracking single kinesin molecules in the cytoplasm of mammalian cells. Biophys. J. 92, 4137-4144 (2007).
    • (2007) Biophys. J. , vol.92 , pp. 4137-4144
    • Cai, D.W.1    Verhey, K.J.2    Meyhofer, E.3
  • 143
    • 0034909695 scopus 로고    scopus 로고
    • Analysis of single-molecule mechanical recordings: Application to acto-myosin interactions
    • Knight, A. E., Veigel, C., Chambers, C. & Molloy, J. E. Analysis of single-molecule mechanical recordings: application to acto-myosin interactions. Prog. Biophys. Mol. Biol. 77, 45-72 (2001).
    • (2001) Prog. Biophys. Mol. Biol. , vol.77 , pp. 45-72
    • Knight, A.E.1    Veigel, C.2    Chambers, C.3    Molloy, J.E.4
  • 144
    • 0036660188 scopus 로고    scopus 로고
    • Lights, action: Optical tweezers
    • Molloy, J. E. & Padgett, M. J. Lights, action: optical tweezers. Contemp. Phys. 43, 241-258 (2002).
    • (2002) Contemp. Phys. , vol.43 , pp. 241-258
    • Molloy, J.E.1    Padgett, M.J.2
  • 145
    • 0029976424 scopus 로고    scopus 로고
    • Quantitative measurements of force and displacement using an optical trap
    • Simmons, R. M., Finer, J. T., Chu, S. & Spudich, J. A. Quantitative measurements of force and displacement using an optical trap. Biophys. J. 70, 1813-1822 (1996).
    • (1996) Biophys. J. , vol.70 , pp. 1813-1822
    • Simmons, R.M.1    Finer, J.T.2    Chu, S.3    Spudich, J.A.4
  • 147
    • 0030878880 scopus 로고    scopus 로고
    • Detection of single-molecule interactions using correlated thermal diffusion
    • Mehta, A. D., Finer, J. T. & Spudich, J. A. Detection of single-molecule interactions using correlated thermal diffusion. Proc. Natl Acad. Sci. USA 94, 7927-7931 (1997).
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 7927-7931
    • Mehta, A.D.1    Finer, J.T.2    Spudich, J.A.3
  • 148
    • 65249184511 scopus 로고    scopus 로고
    • Leveraging single protein polymers to measure flexural rigidity
    • van Mameren, J., Vermeulen, K. C., Gittes, F. & Schmidt, C. F. Leveraging single protein polymers to measure flexural rigidity. J. Phys. Chem. B 113, 3837-3844 (2009).
    • (2009) J. Phys. Chem. B , vol.113 , pp. 3837-3844
    • Van Mameren, J.1    Vermeulen, K.C.2    Gittes, F.3    Schmidt, C.F.4
  • 149
    • 0031656226 scopus 로고    scopus 로고
    • The stiffness of rabbit skeletal actomyosin cross-bridges determined with an optical tweezers transducer
    • Veigel, C., Bartoo, M. L., White, D. C. S., Sparrow, J. C. & Molloy, J. E. The stiffness of rabbit skeletal actomyosin cross-bridges determined with an optical tweezers transducer. Biophys. J. 75, 1424-1438 (1998).
    • (1998) Biophys. J. , vol.75 , pp. 1424-1438
    • Veigel, C.1    Bartoo, M.L.2    White, D.C.S.3    Sparrow, J.C.4    Molloy, J.E.5
  • 151
    • 33645758327 scopus 로고    scopus 로고
    • Force generation in single conventional actomyosin complexes under high dynamic load
    • Takagi, Y., Homsher, E. E., Goldman, Y. E. & Shuman, H. Force generation in single conventional actomyosin complexes under high dynamic load. Biophys. J. 90, 1295-1307 (2006).
    • (2006) Biophys. J. , vol.90 , pp. 1295-1307
    • Takagi, Y.1    Homsher, E.E.2    Goldman, Y.E.3    Shuman, H.4
  • 152
    • 0027472356 scopus 로고
    • Micromanipulation by multiple optical traps created by a single fast scanning trap integrated with the bilateral confocal scanning laser microscope
    • Visscher, K., Brakenhoff, G. J. & Krol, J. J. Micromanipulation by multiple optical traps created by a single fast scanning trap integrated with the bilateral confocal scanning laser microscope. Cytometry 14, 105-114 (1993).
    • (1993) Cytometry , vol.14 , pp. 105-114
    • Visscher, K.1    Brakenhoff, G.J.2    Krol, J.J.3
  • 153
    • 41549169619 scopus 로고    scopus 로고
    • Precision steering of an optical trap by electro-optic deflection
    • Valentine, M. T. et al. Precision steering of an optical trap by electro-optic deflection. Opt. Lett. 33, 599-601 (2008).
    • (2008) Opt. Lett. , vol.33 , pp. 599-601
    • Valentine, M.T.1
  • 154
    • 0033536183 scopus 로고    scopus 로고
    • Single kinesin molecules studied with a molecular force clamp
    • The application of a single-molecule force clamp in an optical trap assay made it possible for these authors to study the force-dependence of the kinesin cycle with unprecedented accuracy
    • Visscher, K., Schnitzer, M. J. & Block, S. M. Single kinesin molecules studied with a molecular force clamp. Nature 400, 184-189 (1999). The application of a single-molecule force clamp in an optical trap assay made it possible for these authors to study the force-dependence of the kinesin cycle with unprecedented accuracy.
    • (1999) Nature , vol.400 , pp. 184-189
    • Visscher, K.1    Schnitzer, M.J.2    Block, S.M.3
  • 155
    • 33744987629 scopus 로고    scopus 로고
    • Individual dimers of the mitotic kinesin motor Eg5 step processively and support substantial loads in vitro
    • Valentine, M. T., Fordyce, P. M., Krzysiak, T. C., Gilbert, S. P. & Block, S. M. Individual dimers of the mitotic kinesin motor Eg5 step processively and support substantial loads in vitro. Nature Cell Biol. 8, 470-476 (2006).
    • (2006) Nature Cell Biol. , vol.8 , pp. 470-476
    • Valentine, M.T.1    Fordyce, P.M.2    Krzysiak, T.C.3    Gilbert, S.P.4    Block, S.M.5
  • 156
  • 157
    • 0034662912 scopus 로고    scopus 로고
    • Myosin-V stepping kinetics: A molecular model for processivity
    • Rief, M. et al. Myosin-V stepping kinetics: a molecular model for processivity. Proc. Natl Acad. Sci. USA 97, 9482-9486 (2000).
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 9482-9486
    • Rief, M.1
  • 158
    • 0032582494 scopus 로고    scopus 로고
    • Force and velocity measured for single molecules of RNA polymerase
    • Wang, M. D. et al. Force and velocity measured for single molecules of RNA polymerase. Science 282, 902-907 (1998).
    • (1998) Science , vol.282 , pp. 902-907
    • Wang, M.D.1
  • 161
    • 38849204944 scopus 로고    scopus 로고
    • Direct observation of hierarchical folding in single riboswitch aptamers
    • Greenleaf, W. J., Frieda, K. L., Foster, D. A. N., Woodside, M. T. & Block, S. M. Direct observation of hierarchical folding in single riboswitch aptamers. Science 319, 630-633 (2008).
    • (2008) Science , vol.319 , pp. 630-633
    • Greenleaf, W.J.1    Frieda, K.L.2    Foster, D.A.N.3    Woodside, M.T.4    Block, S.M.5
  • 162
    • 33750970551 scopus 로고    scopus 로고
    • Direct measurement of the full, sequence-dependent folding landscape of a nucleic acid
    • Woodside, M. T. et al. Direct measurement of the full, sequence-dependent folding landscape of a nucleic acid. Science 314, 1001-1004 (2006).
    • (2006) Science , vol.314 , pp. 1001-1004
    • Woodside, M.T.1
  • 163
    • 0031930529 scopus 로고    scopus 로고
    • Thermal noise limitations on micromechanical experiments
    • Gittes, F. & Schmidt, C. F. Thermal noise limitations on micromechanical experiments. Eur. Biophys. J. 27, 75-81 (1998).
    • (1998) Eur. Biophys. J. , vol.27 , pp. 75-81
    • Gittes, F.1    Schmidt, C.F.2
  • 164
    • 0031961707 scopus 로고    scopus 로고
    • Laser Tweezers in Cell Biology, Ed. M. P. Sheetz, Academic Press Inc., San Diego, A basic introduction to the analysis of single-molecule optical-trap data and a discussion of relevant noise sources
    • Gittes, F. & Schmidt, C. F. in Methods in Cell Biology, Vol. 55 (Laser Tweezers in Cell Biology) (Ed. M. P. Sheetz) 129-156 (Academic Press Inc., San Diego, 1998). A basic introduction to the analysis of single-molecule optical-trap data and a discussion of relevant noise sources.
    • (1998) Methods in Cell Biology , vol.55 , pp. 129-156
    • Gittes, F.1    Schmidt, C.F.2
  • 165
    • 0034757969 scopus 로고    scopus 로고
    • Hidden-Markov methods for the analysis of singlemolecule actomyosin displacement data: The variance-Hidden-Markov method
    • Smith, D. A., Steffen, W., Simmons, R. M. & Sleep, J. Hidden-Markov methods for the analysis of singlemolecule actomyosin displacement data: the variance-Hidden-Markov method. Biophys. J. 81, 2795-2816 (2001).
    • (2001) Biophys. J. , vol.81 , pp. 2795-2816
    • Smith, D.A.1    Steffen, W.2    Simmons, R.M.3    Sleep, J.4
  • 166
    • 30444437723 scopus 로고    scopus 로고
    • Two independent mechanical events in the interaction cycle of skeletal muscle myosin with actin
    • Capitanio, M. et al. Two independent mechanical events in the interaction cycle of skeletal muscle myosin with actin. Proc. Natl Acad. Sci. USA 103, 87-92 (2006).
    • (2006) Proc. Natl Acad. Sci. USA , vol.103 , pp. 87-92
    • Capitanio, M.1
  • 167
    • 44049094435 scopus 로고    scopus 로고
    • Single-molecule measurement of the stiffness of the rigor myosin head
    • Lewalle, A., Steffen, W., Stevenson, O., Ouyang, Z. Q. & Sleep, J. Single-molecule measurement of the stiffness of the rigor myosin head. Biophys. J. 94, 2160-2169 (2008).
    • (2008) Biophys. J. , vol.94 , pp. 2160-2169
    • Lewalle, A.1    Steffen, W.2    Stevenson, O.3    Ouyang, Z.Q.4    Sleep, J.5
  • 168
    • 2442609583 scopus 로고    scopus 로고
    • A monomeric myosin VI with a large working stroke
    • Lister, I. et al. A monomeric myosin VI with a large working stroke. EMBO J. 23, 1729-1738 (2004).
    • (2004) EMBO J. , vol.23 , pp. 1729-1738
    • Lister, I.1
  • 169
    • 46849089895 scopus 로고    scopus 로고
    • Myosin I can act as a molecular force sensor
    • Laakso, J. M., Lewis, J. H., Shuman, H. & Ostap, E. M. Myosin I can act as a molecular force sensor. Science 321, 133-136 (2008).
    • (2008) Science , vol.321 , pp. 133-136
    • Laakso, J.M.1    Lewis, J.H.2    Shuman, H.3    Ostap, E.M.4
  • 170
    • 77049091811 scopus 로고    scopus 로고
    • The lever arm effects a mechanical asymmetry of the myosin-V-actin bond
    • Gebhardt, J. C. M., Okten, Z. & Rief, M. The lever arm effects a mechanical asymmetry of the myosin-V-actin bond. Biophys. J. 98, 277-281 (2010).
    • (2010) Biophys. J. , vol.98 , pp. 277-281
    • Gebhardt, J.C.M.1    Okten, Z.2    Rief, M.3
  • 171
    • 77949874333 scopus 로고    scopus 로고
    • Robust processivity of myosin V under off-axis loads
    • Oguchi, Y. et al. Robust processivity of myosin V under off-axis loads. Nature Chem. Biol. 6, 300-305 (2010).
    • (2010) Nature Chem. Biol. , vol.6 , pp. 300-305
    • Oguchi, Y.1
  • 172
    • 0037390461 scopus 로고    scopus 로고
    • Loading direction regulates the affinity of ADP for kinesin
    • Uemura, S. & Ishiwata, S. Loading direction regulates the affinity of ADP for kinesin. Nature Struct. Biol. 10, 308-311 (2003).
    • (2003) Nature Struct. Biol. , vol.10 , pp. 308-311
    • Uemura, S.1    Ishiwata, S.2
  • 173
    • 0025251665 scopus 로고
    • Force generation of organelle transport measured in vivo by an infrared laser trap
    • Ashkin, A., Schutze, K., Dziedzic, J. M., Euteneuer, U. & Schliwa, M. Force generation of organelle transport measured in vivo by an infrared laser trap. Nature 348, 346-348 (1990).
    • (1990) Nature , vol.348 , pp. 346-348
    • Ashkin, A.1    Schutze, K.2    Dziedzic, J.M.3    Euteneuer, U.4    Schliwa, M.5
  • 174
    • 0032548920 scopus 로고    scopus 로고
    • Developmental regulation of vesicle transport in Drosophila embryos: Forces and kinetics
    • Welte, M. A., Gross, S. P., Postner, M., Block, S. M. & Wieschaus, E. F. Developmental regulation of vesicle transport in Drosophila embryos: forces and kinetics. Cell 92, 547-557 (1998).
    • (1998) Cell , vol.92 , pp. 547-557
    • Welte, M.A.1    Gross, S.P.2    Postner, M.3    Block, S.M.4    Wieschaus, E.F.5
  • 175
    • 57149145788 scopus 로고    scopus 로고
    • Consequences of motor copy number on the intracellular transport of Kinesin-1-driven lipid droplets
    • Shubeita, G. T. et al. Consequences of motor copy number on the intracellular transport of Kinesin-1-driven lipid droplets. Cell 135, 1098-1107 (2008).
    • (2008) Cell , vol.135 , pp. 1098-1107
    • Shubeita, G.T.1
  • 177
    • 62549122152 scopus 로고    scopus 로고
    • The reciprocal coordination and mechanics of molecular motors in living cells
    • Laib, J. A., Marin, J. A., Bloodgood, R. A. & Guilford, W. H. The reciprocal coordination and mechanics of molecular motors in living cells. Proc. Natl Acad. Sci. USA 106, 3190-3195 (2009).
    • (2009) Proc. Natl Acad. Sci. USA , vol.106 , pp. 3190-3195
    • Laib, J.A.1    Marin, J.A.2    Bloodgood, R.A.3    Guilford, W.H.4
  • 179
    • 33846625096 scopus 로고    scopus 로고
    • Nonequilibrium mechanics of active cytoskeletal networks
    • Mizuno, D., Tardin, C., Schmidt, C. F. & MacKintosh, F. C. Nonequilibrium mechanics of active cytoskeletal networks. Science 315, 370-373 (2007).
    • (2007) Science , vol.315 , pp. 370-373
    • Mizuno, D.1    Tardin, C.2    Schmidt, C.F.3    MacKintosh, F.C.4
  • 180
    • 0000534160 scopus 로고
    • Position measurement with a resolution and noise-limited instrument
    • Bobroff, N. Position measurement with a resolution and noise-limited instrument. Rev. Sci. Instr. 57, 1152-1157 (1986).
    • (1986) Rev. Sci. Instr. , vol.57 , pp. 1152-1157
    • Bobroff, N.1
  • 181
    • 0036231415 scopus 로고    scopus 로고
    • Precise nanometer localization analysis for individual fluorescent probes
    • A fundamental discussion of attainable accuracy in localizing single fluorescent molecules in a microscope
    • Thompson, R. E., Larson, D. R. & Webb, W. W. Precise nanometer localization analysis for individual fluorescent probes. Biophys. J. 82, 2775-2783 (2002). A fundamental discussion of attainable accuracy in localizing single fluorescent molecules in a microscope.
    • (2002) Biophys. J. , vol.82 , pp. 2775-2783
    • Thompson, R.E.1    Larson, D.R.2    Webb, W.W.3
  • 182
    • 49549091342 scopus 로고    scopus 로고
    • Protein modification for single molecule fluorescence microscopy
    • Dillingham, M. S. & Wallace, M. I. Protein modification for single molecule fluorescence microscopy. Org. Biomol. Chem. 6, 3031-3037 (2008).
    • (2008) Org. Biomol. Chem. , vol.6 , pp. 3031-3037
    • Dillingham, M.S.1    Wallace, M.I.2
  • 183
    • 33846499787 scopus 로고    scopus 로고
    • Characterization and application of single fluorescent nanodiamonds as cellular biomarkers
    • Fu, C. C. et al. Characterization and application of single fluorescent nanodiamonds as cellular biomarkers. Proc. Natl Acad. Sci. USA 104, 727-732 (2007).
    • (2007) Proc. Natl Acad. Sci. USA , vol.104 , pp. 727-732
    • Fu, C.C.1
  • 184
    • 68649095245 scopus 로고    scopus 로고
    • Fluorescence and spin properties of defects in single digit nanodiamonds
    • Tisler, J. et al. Fluorescence and spin properties of defects in single digit nanodiamonds. ACS Nano 3, 1959-1965 (2009).
    • (2009) ACS Nano , vol.3 , pp. 1959-1965
    • Tisler, J.1
  • 185
    • 0037147175 scopus 로고    scopus 로고
    • Structure-assigned optical spectra of single-walled carbon nanotubes
    • Bachilo, S. M. et al. Structure-assigned optical spectra of single-walled carbon nanotubes. Science 298, 2361-2366 (2002).
    • (2002) Science , vol.298 , pp. 2361-2366
    • Bachilo, S.M.1
  • 186
    • 0343415156 scopus 로고    scopus 로고
    • The way things move: Looking under the hood of molecular motor proteins
    • Vale, R. D. & Milligan, R. A. The way things move: looking under the hood of molecular motor proteins. Science 288, 88-95 (2000).
    • (2000) Science , vol.288 , pp. 88-95
    • Vale, R.D.1    Milligan, R.A.2
  • 187
    • 28844444610 scopus 로고    scopus 로고
    • High-speed atomic force microscopy for capturing dynamic behavior of protein molecules at work
    • Ando, T. et al. High-speed atomic force microscopy for capturing dynamic behavior of protein molecules at work. e-J. Surf. Sci. Nanotech. 3, 384-392 (2005).
    • (2005) e-J. Surf. Sci. Nanotech. , vol.3 , pp. 384-392
    • Ando, T.1


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