메뉴 건너뛰기




Volumn 104, Issue 12, 2013, Pages 2651-2661

Single-molecule motility: Statistical analysis and the effects of track length on quantification of processive motion

Author keywords

[No Author keywords available]

Indexed keywords

KINESIN;

EID: 84879200496     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2013.05.022     Document Type: Article
Times cited : (17)

References (36)
  • 1
    • 17844385071 scopus 로고    scopus 로고
    • Differential labeling of myosin v heads with quantum dots allows direct visualization of hand-over-hand processivity
    • D.M. Warshaw, and G.G. Kennedy K.M. Trybus Differential labeling of myosin V heads with quantum dots allows direct visualization of hand-over-hand processivity Biophys. J. 88 2005 L30 L32
    • (2005) Biophys. J. , vol.88
    • Warshaw, D.M.1    Kennedy, G.G.2    Trybus, K.M.3
  • 2
    • 77953135927 scopus 로고    scopus 로고
    • Neck linker length determines the degree of processivity in kinesin-1 and kinesin-2 motors
    • S. Shastry, and W.O. Hancock Neck linker length determines the degree of processivity in kinesin-1 and kinesin-2 motors Curr. Biol. 20 2010 939 943
    • (2010) Curr. Biol. , vol.20 , pp. 939-943
    • Shastry, S.1    Hancock, W.O.2
  • 3
    • 80053654615 scopus 로고    scopus 로고
    • Interhead tension determines processivity across diverse N-terminal kinesins
    • S. Shastry, and W.O. Hancock Interhead tension determines processivity across diverse N-terminal kinesins Proc. Natl. Acad. Sci. USA 108 2011 16253 16258
    • (2011) Proc. Natl. Acad. Sci. USA , vol.108 , pp. 16253-16258
    • Shastry, S.1    Hancock, W.O.2
  • 4
    • 39749165656 scopus 로고    scopus 로고
    • Differential regulation of dynein and kinesin motor proteins by Tau
    • R. Dixit, and J.L. Ross E.L. Holzbaur Differential regulation of dynein and kinesin motor proteins by Tau Science 319 2008 1086 1089
    • (2008) Science , vol.319 , pp. 1086-1089
    • Dixit, R.1    Ross, J.L.2    Holzbaur, E.L.3
  • 5
    • 83355163345 scopus 로고    scopus 로고
    • The nucleotide-binding state of microtubules modulates kinesin processivity and the ability of Tau to inhibit kinesin-mediated transport
    • D.P. McVicker, L.R. Chrin, and C.L. Berger The nucleotide-binding state of microtubules modulates kinesin processivity and the ability of Tau to inhibit kinesin-mediated transport J. Biol. Chem. 286 2011 42873 42880
    • (2011) J. Biol. Chem. , vol.286 , pp. 42873-42880
    • McVicker, D.P.1    Chrin, L.R.2    Berger, C.L.3
  • 7
    • 0023066791 scopus 로고
    • Preferred microtubules for vesicle transport in lobster axons
    • R.H. Miller, R.J. Lasek, and M.J. Katz Preferred microtubules for vesicle transport in lobster axons Science 235 1987 220 222
    • (1987) Science , vol.235 , pp. 220-222
    • Miller, R.H.1    Lasek, R.J.2    Katz, M.J.3
  • 8
    • 79961105234 scopus 로고    scopus 로고
    • Preferential binding of a kinesin-1 motor to GTP-tubulin-rich microtubules underlies polarized vesicle transport
    • T. Nakata, and S. Niwa N. Hirokawa Preferential binding of a kinesin-1 motor to GTP-tubulin-rich microtubules underlies polarized vesicle transport J. Cell Biol. 194 2011 245 255
    • (2011) J. Cell Biol. , vol.194 , pp. 245-255
    • Nakata, T.1    Niwa, S.2    Hirokawa, N.3
  • 9
    • 70350501513 scopus 로고    scopus 로고
    • Single molecule imaging reveals differences in microtubule track selection between kinesin motors
    • D. Cai, and D.P. McEwen K.J. Verhey Single molecule imaging reveals differences in microtubule track selection between kinesin motors PLoS Biol. 7 2009 e1000216
    • (2009) PLoS Biol. , vol.7 , pp. 1000216
    • Cai, D.1    McEwen, D.P.2    Verhey, K.J.3
  • 10
    • 33750618516 scopus 로고    scopus 로고
    • Microtubule acetylation promotes kinesin-1 binding and transport
    • N.A. Reed, and D. Cai K.J. Verhey Microtubule acetylation promotes kinesin-1 binding and transport Curr. Biol. 16 2006 2166 2172
    • (2006) Curr. Biol. , vol.16 , pp. 2166-2172
    • Reed, N.A.1    Cai, D.2    Verhey, K.J.3
  • 11
    • 67349200776 scopus 로고    scopus 로고
    • Tubulin tyrosination navigates the kinesin-1 motor domain to axons
    • Y. Konishi, and M. Setou Tubulin tyrosination navigates the kinesin-1 motor domain to axons Nat. Neurosci. 12 2009 559 567
    • (2009) Nat. Neurosci. , vol.12 , pp. 559-567
    • Konishi, Y.1    Setou, M.2
  • 12
    • 76649143069 scopus 로고    scopus 로고
    • Posttranslational modifications of tubulin and the polarized transport of kinesin-1 in neurons
    • J.W. Hammond, and C.F. Huang K.J. Verhey Posttranslational modifications of tubulin and the polarized transport of kinesin-1 in neurons Mol. Biol. Cell 21 2010 572 583
    • (2010) Mol. Biol. Cell , vol.21 , pp. 572-583
    • Hammond, J.W.1    Huang, C.F.2    Verhey, K.J.3
  • 13
    • 34250317264 scopus 로고    scopus 로고
    • Tau binding to microtubules does not directly affect microtubule-based vesicle motility
    • G. Morfini, and G. Pigino S.T. Brady Tau binding to microtubules does not directly affect microtubule-based vesicle motility J. Neurosci. Res. 85 2007 2620 2630
    • (2007) J. Neurosci. Res. , vol.85 , pp. 2620-2630
    • Morfini, G.1    Pigino, G.2    Brady, S.T.3
  • 14
    • 33746871112 scopus 로고    scopus 로고
    • Tracking individual kinesin motors in living cells using single quantum-dot imaging
    • S. Courty, and C. Luccardini M. Dahan Tracking individual kinesin motors in living cells using single quantum-dot imaging Nano Lett. 6 2006 1491 1495
    • (2006) Nano Lett. , vol.6 , pp. 1491-1495
    • Courty, S.1    Luccardini, C.2    Dahan, M.3
  • 15
    • 68949125193 scopus 로고    scopus 로고
    • Random walk of processive, quantum dot-labeled myosin Va molecules within the actin cortex of COS-7 cells
    • S.R. Nelson, and M.Y. Ali D.M. Warshaw Random walk of processive, quantum dot-labeled myosin Va molecules within the actin cortex of COS-7 cells Biophys. J. 97 2009 509 518
    • (2009) Biophys. J. , vol.97 , pp. 509-518
    • Nelson, S.R.1    Ali, M.Y.2    Warshaw, D.M.3
  • 16
    • 84922523364 scopus 로고    scopus 로고
    • Intracellular imaging of targeted proteins labeled with quantum dots
    • J. Yoo, and T. Kambara H. Higuchi Intracellular imaging of targeted proteins labeled with quantum dots Exp. Cell Res. 314 2008 3563 3569
    • (2008) Exp. Cell Res. , vol.314 , pp. 3563-3569
    • Yoo, J.1    Kambara, T.2    Higuchi, H.3
  • 17
    • 34250372604 scopus 로고    scopus 로고
    • Tracking single kinesin molecules in the cytoplasm of mammalian cells
    • D. Cai, K.J. Verhey, and E. Meyhöfer Tracking single kinesin molecules in the cytoplasm of mammalian cells Biophys. J. 92 2007 4137 4144
    • (2007) Biophys. J. , vol.92 , pp. 4137-4144
    • Cai, D.1    Verhey, K.J.2    Meyhöfer, E.3
  • 18
    • 0021894565 scopus 로고
    • Video microscopy of fast axonal transport in extruded axoplasm: A new model for study of molecular mechanisms
    • S.T. Brady, R.J. Lasek, and R.D. Allen Video microscopy of fast axonal transport in extruded axoplasm: a new model for study of molecular mechanisms Cell Motil. 5 1985 81 101
    • (1985) Cell Motil. , vol.5 , pp. 81-101
    • Brady, S.T.1    Lasek, R.J.2    Allen, R.D.3
  • 19
    • 60549086255 scopus 로고    scopus 로고
    • Imaging biological structures with fluorescence photoactivation localization microscopy
    • T.J. Gould, V.V. Verkhusha, and S.T. Hess Imaging biological structures with fluorescence photoactivation localization microscopy Nat. Protoc. 4 2009 291 308
    • (2009) Nat. Protoc. , vol.4 , pp. 291-308
    • Gould, T.J.1    Verkhusha, V.V.2    Hess, S.T.3
  • 20
    • 0028344617 scopus 로고
    • Changes in microtubule number and length during axon differentiation
    • W. Yu, and P.W. Baas Changes in microtubule number and length during axon differentiation J. Neurosci. 14 1994 2818 2829
    • (1994) J. Neurosci. , vol.14 , pp. 2818-2829
    • Yu, W.1    Baas, P.W.2
  • 22
    • 0343415156 scopus 로고    scopus 로고
    • The way things move: Looking under the hood of molecular motor proteins
    • R.D. Vale, and R.A. Milligan The way things move: looking under the hood of molecular motor proteins Science 288 2000 88 95
    • (2000) Science , vol.288 , pp. 88-95
    • Vale, R.D.1    Milligan, R.A.2
  • 24
    • 0025222347 scopus 로고
    • Bead movement by single kinesin molecules studied with optical tweezers
    • S.M. Block, L.S. Goldstein, and B.J. Schnapp Bead movement by single kinesin molecules studied with optical tweezers Nature 348 1990 348 352
    • (1990) Nature , vol.348 , pp. 348-352
    • Block, S.M.1    Goldstein, L.S.2    Schnapp, B.J.3
  • 25
    • 0029879228 scopus 로고    scopus 로고
    • Direct observation of single kinesin molecules moving along microtubules
    • R.D. Vale, and T. Funatsu T. Yanagida Direct observation of single kinesin molecules moving along microtubules Nature 380 1996 451 453
    • (1996) Nature , vol.380 , pp. 451-453
    • Vale, R.D.1    Funatsu, T.2    Yanagida, T.3
  • 27
    • 47749098361 scopus 로고    scopus 로고
    • A myosin motor that selects bundled actin for motility
    • S. Nagy, and B.L. Ricca R.S. Rock A myosin motor that selects bundled actin for motility Proc. Natl. Acad. Sci. USA 105 2008 9616 9620
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 9616-9620
    • Nagy, S.1    Ricca, B.L.2    Rock, R.S.3
  • 28
    • 84864746082 scopus 로고    scopus 로고
    • Tubulin acetylation alone does not affect kinesin-1 velocity and run length in vitro
    • W.J. Walter, and V. Beránek S. Diez Tubulin acetylation alone does not affect kinesin-1 velocity and run length in vitro PLoS ONE 7 2012 e42218
    • (2012) PLoS ONE , vol.7 , pp. 42218
    • Walter, W.J.1    Beránek, V.2    Diez, S.3
  • 30
    • 77954133346 scopus 로고    scopus 로고
    • Streamlined determination of processive run length and mechanochemical coupling of nucleic acid motor activities
    • M. Gyimesi, and K. Sarlós M. Kovács Streamlined determination of processive run length and mechanochemical coupling of nucleic acid motor activities Nucleic Acids Res. 38 2010 e102
    • (2010) Nucleic Acids Res. , vol.38 , pp. 102
    • Gyimesi, M.1    Sarlós, K.2    Kovács, M.3
  • 31
    • 77950857024 scopus 로고    scopus 로고
    • Engineering the length distribution of microtubules polymerized in vitro
    • Y. Jeune-Smith, and H. Hess Engineering the length distribution of microtubules polymerized in vitro Soft Matter 8 2010 1778 1784
    • (2010) Soft Matter , vol.8 , pp. 1778-1784
    • Jeune-Smith, Y.1    Hess, H.2
  • 32
    • 0000315224 scopus 로고
    • Physical aspects of the growth and regulation of microtubule structures
    • M. Dogterom, and S. Leibler Physical aspects of the growth and regulation of microtubule structures Phys. Rev. Lett. 70 1993 1347 1350
    • (1993) Phys. Rev. Lett. , vol.70 , pp. 1347-1350
    • Dogterom, M.1    Leibler, S.2
  • 33
    • 84865037917 scopus 로고    scopus 로고
    • Microtubule-severing enzymes at the cutting edge
    • D.J. Sharp, and J.L. Ross Microtubule-severing enzymes at the cutting edge J. Cell Sci. 125 2012 2561 2569
    • (2012) J. Cell Sci. , vol.125 , pp. 2561-2569
    • Sharp, D.J.1    Ross, J.L.2
  • 34
    • 39149138988 scopus 로고    scopus 로고
    • Cargo transport: Molecular motors navigate a complex cytoskeleton
    • J.L. Ross, M.Y. Ali, and D.M. Warshaw Cargo transport: molecular motors navigate a complex cytoskeleton Curr. Opin. Cell Biol. 20 2008 41 47
    • (2008) Curr. Opin. Cell Biol. , vol.20 , pp. 41-47
    • Ross, J.L.1    Ali, M.Y.2    Warshaw, D.M.3
  • 35
    • 43149106461 scopus 로고    scopus 로고
    • Differential trafficking of Kif5c on tyrosinated and detyrosinated microtubules in live cells
    • S. Dunn, and E.E. Morrison M. Peckham Differential trafficking of Kif5c on tyrosinated and detyrosinated microtubules in live cells J. Cell Sci. 121 2008 1085 1095
    • (2008) J. Cell Sci. , vol.121 , pp. 1085-1095
    • Dunn, S.1    Morrison, E.E.2    Peckham, M.3
  • 36
    • 43149117264 scopus 로고    scopus 로고
    • Kinesin and dynein-dynactin at intersecting microtubules: Motor density affects dynein function
    • J.L. Ross, and H. Shuman Y.E. Goldman Kinesin and dynein-dynactin at intersecting microtubules: motor density affects dynein function Biophys. J. 94 2008 3115 3125
    • (2008) Biophys. J. , vol.94 , pp. 3115-3125
    • Ross, J.L.1    Shuman, H.2    Goldman, Y.E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.