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Volumn 1, Issue 3, 2012, Pages 220-231

Ndel1-derived peptides modulate bidirectional transport of injected beads in the squid giant axon

Author keywords

Anterograde transport; Cytoplasmic dynein; Kinesin; Microtubules; Retrograde transport

Indexed keywords


EID: 84964596705     PISSN: None     EISSN: 20466390     Source Type: Journal    
DOI: 10.1242/bio.2012307     Document Type: Article
Times cited : (11)

References (87)
  • 2
    • 75749098711 scopus 로고    scopus 로고
    • Oppositepolarity motors activate one another to trigger cargo transport in live cells
    • Ally, S., Larson, A. G., Barlan, K., Rice, S. E. and Gelfand, V. I. (2009). Oppositepolarity motors activate one another to trigger cargo transport in live cells. J. Cell Biol. 187, 1071-1082.
    • (2009) J. Cell Biol. , vol.187 , pp. 1071-1082
    • Ally, S.1    Larson, A.G.2    Barlan, K.3    Rice, S.E.4    Gelfand, V.I.5
  • 3
    • 0005541930 scopus 로고    scopus 로고
    • Association of actin filaments with axonal microtubule tracts
    • Bearer, E. L. and Reese, T. S. (1999). Association of actin filaments with axonal microtubule tracts. J. Neurocytol. 28, 85-98.
    • (1999) J. Neurocytol. , vol.28 , pp. 85-98
    • Bearer, E.L.1    Reese, T.S.2
  • 4
    • 0034608952 scopus 로고    scopus 로고
    • Retrograde axonal transport of herpes simplex virus: Evidence for a single mechanism and a role for tegument
    • Bearer, E. L., Breakefield, X. O., Schuback, D., Reese, T. S. and LaVail, J. H. (2000). Retrograde axonal transport of herpes simplex virus: evidence for a single mechanism and a role for tegument. Proc. Natl. Acad. Sci. USA 97, 8146-8150.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 8146-8150
    • Bearer, E.L.1    Breakefield, X.O.2    Schuback, D.3    Reese, T.S.4    LaVail, J.H.5
  • 5
    • 33846199544 scopus 로고    scopus 로고
    • Dynactin enhances the processivity of kinesin-2
    • Berezuk, M. A. and Schroer, T. A. (2007). Dynactin enhances the processivity of kinesin-2. Traffic 8, 124-129.
    • (2007) Traffic , vol.8 , pp. 124-129
    • Berezuk, M.A.1    Schroer, T.A.2
  • 6
    • 0030612145 scopus 로고    scopus 로고
    • Phosphorylation by p34cdc2 protein kinase regulates binding of the kinesin-related motor HsEg5 to the dynactin subunit p150
    • Blangy, A., Arnaud, L. and Nigg, E. A. (1997). Phosphorylation by p34cdc2 protein kinase regulates binding of the kinesin-related motor HsEg5 to the dynactin subunit p150. J. Biol. Chem. 272, 19,418-19,424.
    • (1997) J. Biol. Chem. , vol.272 , pp. 19418-19424
    • Blangy, A.1    Arnaud, L.2    Nigg, E.A.3
  • 8
    • 0020419627 scopus 로고
    • Fast axonal transport in extruded axoplasm from squid giant axon
    • Brady, S. T., Lasek, R. J. and Allen, R. D. (1982). Fast axonal transport in extruded axoplasm from squid giant axon. Science 218, 1129-1131.
    • (1982) Science , vol.218 , pp. 1129-1131
    • Brady, S.T.1    Lasek, R.J.2    Allen, R.D.3
  • 9
    • 0021894565 scopus 로고
    • Video microscopy of fast axonal transport in extruded axoplasm: A new model for study of molecular mechanisms
    • Brady, S. T., Lasek, R. J. and Allen, R. D. (1985). Video microscopy of fast axonal transport in extruded axoplasm: a new model for study of molecular mechanisms. Cell Motil. 5, 81-101.
    • (1985) Cell Motil. , vol.5 , pp. 81-101
    • Brady, S.T.1    Lasek, R.J.2    Allen, R.D.3
  • 10
    • 33751020569 scopus 로고    scopus 로고
    • Axonal transport and neurodegenerative disease
    • Chevalier-Larsen, E. and Holzbaur, E. L. (2006). Axonal transport and neurodegenerative disease. Biochim. Biophys. Acta 1762, 1094-1108.
    • (2006) Biochim. Biophys. Acta , vol.1762 , pp. 1094-1108
    • Chevalier-Larsen, E.1    Holzbaur, E.L.2
  • 11
    • 49149112606 scopus 로고    scopus 로고
    • Huntingtin phosphorylation acts as a molecular switch for anterograde/retrograde transport in neurons
    • Colin, E., Zala, D., Liot, G., Rangone, H., Borrell-Pages, M., Li, X. J., Saudou, F. and Humbert, S. (2008). Huntingtin phosphorylation acts as a molecular switch for anterograde/retrograde transport in neurons. EMBO J. 27, 2124-2134.
    • (2008) EMBO J. , vol.27 , pp. 2124-2134
    • Colin, E.1    Zala, D.2    Liot, G.3    Rangone, H.4    Borrell-Pages, M.5    Li, X.J.6    Saudou, F.7    Humbert, S.8
  • 12
    • 0033193864 scopus 로고    scopus 로고
    • Kinesin's tail domain is an inhibitory regulator of the motor domain
    • Coy, D. L., Hancock, W. O., Wagenbach, M. and Howard, J. (1999). Kinesin's tail domain is an inhibitory regulator of the motor domain. Nat. Cell Biol. 1, 288-292.
    • (1999) Nat. Cell Biol. , vol.1 , pp. 288-292
    • Coy, D.L.1    Hancock, W.O.2    Wagenbach, M.3    Howard, J.4
  • 14
    • 53849136570 scopus 로고    scopus 로고
    • Kinesin-3 is an organelle motor in the squid giant axon
    • DeGiorgis, J. A., Petukhova, T. A., Evans, T. A. and Reese, T. S. (2008). Kinesin-3 is an organelle motor in the squid giant axon. Traffic 9, 1867-1877.
    • (2008) Traffic , vol.9 , pp. 1867-1877
    • DeGiorgis, J.A.1    Petukhova, T.A.2    Evans, T.A.3    Reese, T.S.4
  • 15
    • 80054764482 scopus 로고    scopus 로고
    • Identification of molecular motors in the Woods Hole squid, Loligo pealei: An expressed sequence tag approach
    • Degiorgis, J. A., Cavaliere, K. R. and Burbach, J. P. (2011). Identification of molecular motors in the Woods Hole squid, Loligo pealei: an expressed sequence tag approach. Cytoskeleton 68, 566-577.
    • (2011) Cytoskeleton , vol.68 , pp. 566-577
    • Degiorgis, J.A.1    Cavaliere, K.R.2    Burbach, J.P.3
  • 16
    • 35948969808 scopus 로고    scopus 로고
    • The structure of the coiled-coil domain of Ndel1 and the basis of its interaction with Lis1, the causal protein of Miller-Dieker lissencephaly
    • Derewenda, U., Tarricone, C., Choi, W. C., Cooper, D. R., Lukasik, S., Perrina, F., Tripathy, A., Kim, M. H., Cafiso, D. S., Musacchio, A. et al. (2007). The structure of the coiled-coil domain of Ndel1 and the basis of its interaction with Lis1, the causal protein of Miller-Dieker lissencephaly. Structure 15, 1467-1481.
    • (2007) Structure , vol.15 , pp. 1467-1481
    • Derewenda, U.1    Tarricone, C.2    Choi, W.C.3    Cooper, D.R.4    Lukasik, S.5    Perrina, F.6    Tripathy, A.7    Kim, M.H.8    Cafiso, D.S.9    Musacchio, A.10
  • 17
    • 39749165656 scopus 로고    scopus 로고
    • Differential regulation of dynein and kinesin motor proteins by tau
    • Dixit, R., Ross, J. L., Goldman, Y. E. and Holzbaur, E. L. (2008). Differential regulation of dynein and kinesin motor proteins by tau. Science 319, 1086-1089.
    • (2008) Science , vol.319 , pp. 1086-1089
    • Dixit, R.1    Ross, J.L.2    Goldman, Y.E.3    Holzbaur, E.L.4
  • 18
    • 34047175919 scopus 로고    scopus 로고
    • Histone deacetylase 6 inhibition compensates for the transport deficit in Huntington's disease by increasing tubulin acetylation
    • Dompierre, J. P., Godin, J. D., Charrin, B. C., Cordelieres, F. P., King, S. J., Humbert, S. and Saudou, F. (2007). Histone deacetylase 6 inhibition compensates for the transport deficit in Huntington's disease by increasing tubulin acetylation. J. Neurosci. 27, 3571-3583.
    • (2007) J. Neurosci. , vol.27 , pp. 3571-3583
    • Dompierre, J.P.1    Godin, J.D.2    Charrin, B.C.3    Cordelieres, F.P.4    King, S.J.5    Humbert, S.6    Saudou, F.7
  • 19
    • 33749398995 scopus 로고    scopus 로고
    • The genetics of axonal transport and axonal transport disorders
    • Duncan, J. E. and Goldstein, L. S. (2006). The genetics of axonal transport and axonal transport disorders. PLoS Genet. 2, e124.
    • (2006) PLoS Genet. , vol.2 , pp. e124
    • Duncan, J.E.1    Goldstein, L.S.2
  • 20
    • 79951710366 scopus 로고    scopus 로고
    • Stable kinesin and dynein assemblies drive the axonal transport of mammalian prion protein vesicles
    • Encalada, S. E., Szpankowski, L., Xia, C. and Goldstein, L. S. (2011). Stable kinesin and dynein assemblies drive the axonal transport of mammalian prion protein vesicles. Cell 144, 551-565.
    • (2011) Cell , vol.144 , pp. 551-565
    • Encalada, S.E.1    Szpankowski, L.2    Xia, C.3    Goldstein, L.S.4
  • 22
    • 5144222593 scopus 로고    scopus 로고
    • Mitotic spindle regulation by Nde1 controls cerebral cortical size
    • Feng, Y. and Walsh, C. A. (2004). Mitotic spindle regulation by Nde1 controls cerebral cortical size. Neuron 44, 279-293.
    • (2004) Neuron , vol.44 , pp. 279-293
    • Feng, Y.1    Walsh, C.A.2
  • 23
    • 0034517593 scopus 로고    scopus 로고
    • LIS1 regulates CNS lamination by interacting with mNudE, a central component of the centrosome
    • Feng, Y., Olson, E. C., Stukenberg, P. T., Flanagan, L. A., Kirschner, M. W. and Walsh, C. A. (2000). LIS1 regulates CNS lamination by interacting with mNudE, a central component of the centrosome. Neuron 28, 665-679.
    • (2000) Neuron , vol.28 , pp. 665-679
    • Feng, Y.1    Olson, E.C.2    Stukenberg, P.T.3    Flanagan, L.A.4    Kirschner, M.W.5    Walsh, C.A.6
  • 24
    • 0037447054 scopus 로고    scopus 로고
    • Dynactin: Coordinating motors with opposite inclinations
    • Gross, S. P. (2003). Dynactin: coordinating motors with opposite inclinations. Curr. Biol. 13, R320-R322.
    • (2003) Curr. Biol. , vol.13 , pp. R320-R322
    • Gross, S.P.1
  • 25
    • 9244243320 scopus 로고    scopus 로고
    • Hither and yon: A review of bi-directional microtubule-based transport
    • Gross, S. P. (2004). Hither and yon: a review of bi-directional microtubule-based transport. Phys. Biol. 1, R1-R11.
    • (2004) Phys. Biol. , vol.1 , pp. R1-R11
    • Gross, S.P.1
  • 26
    • 0037128208 scopus 로고    scopus 로고
    • Coordination of opposite-polarity microtubule motors
    • Gross, S. P., Welte, M. A., Block, S. M. and Wieschaus, E. F. (2002). Coordination of opposite-polarity microtubule motors. J. Cell Biol. 156, 715-724.
    • (2002) J. Cell Biol. , vol.156 , pp. 715-724
    • Gross, S.P.1    Welte, M.A.2    Block, S.M.3    Wieschaus, E.F.4
  • 27
    • 75749090448 scopus 로고    scopus 로고
    • Coordination and collective properties of molecular motors: Theory
    • Guerin, T., Prost, J., Martin, P. and Joanny, J. F. (2010). Coordination and collective properties of molecular motors: theory. Curr. Opin. Cell Biol. 22, 14-20.
    • (2010) Curr. Opin. Cell Biol. , vol.22 , pp. 14-20
    • Guerin, T.1    Prost, J.2    Martin, P.3    Joanny, J.F.4
  • 29
    • 77951206786 scopus 로고    scopus 로고
    • Motor coordination via a tug-of-war mechanism drives bidirectional vesicle transport
    • Hendricks, A. G., Perlson, E., Ross, J. L., Schroeder, H. W., 3rd, Tokito, M. and Holzbaur, E. L. (2010). Motor coordination via a tug-of-war mechanism drives bidirectional vesicle transport. Curr. Biol. 20, 697-702.
    • (2010) Curr. Biol. , vol.20 , pp. 697-702
    • Hendricks, A.G.1    Perlson, E.2    Ross, J.L.3    Schroeder, H.W.4    Tokito, M.5    Holzbaur, E.L.6
  • 30
    • 33746911579 scopus 로고    scopus 로고
    • P78/MCRS1 forms a complex with centrosomal protein Nde1 and is essential for cell viability
    • Hirohashi, Y., Wang, Q., Liu, Q., Du, X., Zhang, H., Sato, N. and Greene, M. I. (2006a). p78/MCRS1 forms a complex with centrosomal protein Nde1 and is essential for cell viability. Oncogene 25, 4937-4946.
    • (2006) Oncogene , vol.25 , pp. 4937-4946
    • Hirohashi, Y.1    Wang, Q.2    Liu, Q.3    Du, X.4    Zhang, H.5    Sato, N.6    Greene, M.I.7
  • 32
    • 2342561865 scopus 로고    scopus 로고
    • Motor neurons rely on motor proteins
    • Holzbaur, E. L. (2004). Motor neurons rely on motor proteins. Trends Cell Biol. 14, 233-240.
    • (2004) Trends Cell Biol. , vol.14 , pp. 233-240
    • Holzbaur, E.L.1
  • 33
    • 75749123506 scopus 로고    scopus 로고
    • Coordination of molecular motors: From in vitro assays to intracellular dynamics
    • Holzbaur, E. L. and Goldman, Y. E. (2010). Coordination of molecular motors: from in vitro assays to intracellular dynamics. Curr. Opin. Cell Biol. 22, 4-13.
    • (2010) Curr. Opin. Cell Biol. , vol.22 , pp. 4-13
    • Holzbaur, E.L.1    Goldman, Y.E.2
  • 34
    • 0024463944 scopus 로고
    • Movement of microtubules by single kinesin molecules
    • Howard, J., Hudspeth, A. J. and Vale, R. D. (1989). Movement of microtubules by single kinesin molecules. Nature 342, 154-158.
    • (1989) Nature , vol.342 , pp. 154-158
    • Howard, J.1    Hudspeth, A.J.2    Vale, R.D.3
  • 36
    • 70450228589 scopus 로고    scopus 로고
    • Regulators of the cytoplasmic dynein motor
    • Kardon, J. R. and Vale, R. D. (2009). Regulators of the cytoplasmic dynein motor. Nat. Rev. Mol. Cell Biol. 10, 854-865.
    • (2009) Nat. Rev. Mol. Cell Biol. , vol.10 , pp. 854-865
    • Kardon, J.R.1    Vale, R.D.2
  • 37
    • 0033789351 scopus 로고    scopus 로고
    • Dynactin increases the processivity of the cytoplasmic dynein motor
    • King, S. J. and Schroer, T. A. (2000). Dynactin increases the processivity of the cytoplasmic dynein motor. Nat. Cell Biol. 2, 20-24.
    • (2000) Nat. Cell Biol. , vol.2 , pp. 20-24
    • King, S.J.1    Schroer, T.A.2
  • 38
    • 0036227869 scopus 로고    scopus 로고
    • Subunit organization in cytoplasmic dynein subcomplexes
    • King, S. J., Bonilla, M., Rodgers, M. E. and Schroer, T. A. (2002). Subunit organization in cytoplasmic dynein subcomplexes. Protein Sci. 11, 1239-1250.
    • (2002) Protein Sci. , vol.11 , pp. 1239-1250
    • King, S.J.1    Bonilla, M.2    Rodgers, M.E.3    Schroer, T.A.4
  • 39
    • 0026534466 scopus 로고
    • Actin-dependent organelle movement in squid axoplasm
    • Kuznetsov, S. A., Langford, G. M. and Weiss, D. G. (1992). Actin-dependent organelle movement in squid axoplasm. Nature 356, 722-755.
    • (1992) Nature , vol.356 , pp. 722-755
    • Kuznetsov, S.A.1    Langford, G.M.2    Weiss, D.G.3
  • 40
    • 33644507718 scopus 로고    scopus 로고
    • Cytoplasmic dynein/dynactin function and dysfunction in motor neurons
    • Levy, J. R. and Holzbaur, E. L. (2006). Cytoplasmic dynein/dynactin function and dysfunction in motor neurons. Int. J. Dev. Neurosci. 24, 103-111.
    • (2006) Int. J. Dev. Neurosci. , vol.24 , pp. 103-111
    • Levy, J.R.1    Holzbaur, E.L.2
  • 41
    • 1242285142 scopus 로고    scopus 로고
    • Nudel functions in membrane traffic mainly through association with Lis1 and cytoplasmic dynein
    • Liang, Y., Yu, W., Li, Y., Yang, Z., Yan, X., Huang, Q. and Zhu, X. (2004). Nudel functions in membrane traffic mainly through association with Lis1 and cytoplasmic dynein. J. Cell Biol. 164, 557-566.
    • (2004) J. Cell Biol. , vol.164 , pp. 557-566
    • Liang, Y.1    Yu, W.2    Li, Y.3    Yang, Z.4    Yan, X.5    Huang, Q.6    Zhu, X.7
  • 42
    • 2342640469 scopus 로고    scopus 로고
    • A direct interaction between cytoplasmic dynein and kinesin i may coordinate motor activity
    • Ligon, L. A., Tokito, M., Finklestein, J. M., Grossman, F. E. and Holzbaur, E. L. (2004). A direct interaction between cytoplasmic dynein and kinesin I may coordinate motor activity. J. Biol. Chem. 279, 19,201-19,208.
    • (2004) J. Biol. Chem. , vol.279 , pp. 19201-19208
    • Ligon, L.A.1    Tokito, M.2    Finklestein, J.M.3    Grossman, F.E.4    Holzbaur, E.L.5
  • 43
    • 0036538577 scopus 로고    scopus 로고
    • Cytoplasmic dynein-associated structures move bidirectionally in vivo
    • Ma, S. and Chisholm, R. L. (2002). Cytoplasmic dynein-associated structures move bidirectionally in vivo. J. Cell Sci. 115, 1453-1460.
    • (2002) J. Cell Sci. , vol.115 , pp. 1453-1460
    • Ma, S.1    Chisholm, R.L.2
  • 44
    • 5444273804 scopus 로고    scopus 로고
    • MARK/PAR1 kinase is a regulator of microtubule-dependent transport in axons
    • Mandelkow, E. M., Thies, E., Trinczek, B., Biernat, J. and Mandelkow, E. (2004). MARK/PAR1 kinase is a regulator of microtubule-dependent transport in axons. J. Cell Biol. 167, 99-110.
    • (2004) J. Cell Biol. , vol.167 , pp. 99-110
    • Mandelkow, E.M.1    Thies, E.2    Trinczek, B.3    Biernat, J.4    Mandelkow, E.5
  • 45
    • 59349119386 scopus 로고    scopus 로고
    • Large-scale profiling of protein palmitoylation in mammalian cells
    • Martin, B. R. and Cravatt, B. F. (2009). Large-scale profiling of protein palmitoylation in mammalian cells. Nat. Methods 6, 135-138.
    • (2009) Nat. Methods , vol.6 , pp. 135-138
    • Martin, B.R.1    Cravatt, B.F.2
  • 46
    • 0032741064 scopus 로고    scopus 로고
    • Cytoplasmic dynein, the dynactin complex, and kinesin are interdependent and essential for fast axonal transport
    • Martin, M., Iyadurai, S. J., Gassman, A., Gindhart, J. G., Jr, Hays, T. S. and Saxton, W. M. (1999). Cytoplasmic dynein, the dynactin complex, and kinesin are interdependent and essential for fast axonal transport. Mol. Biol. Cell 10, 3717-3728.
    • (1999) Mol. Biol. Cell , vol.10 , pp. 3717-3728
    • Martin, M.1    Iyadurai, S.J.2    Gassman, A.3    Gindhart, J.G.4    Hays, T.S.5    Saxton, W.M.6
  • 47
    • 77951701022 scopus 로고    scopus 로고
    • LIS1 and NudE induce a persistent dynein force-producing state
    • McKenney, R. J., Vershinin, M., Kunwar, A., Vallee, R. B. and Gross, S. P. (2010). LIS1 and NudE induce a persistent dynein force-producing state. Cell 141, 304-314.
    • (2010) Cell , vol.141 , pp. 304-314
    • McKenney, R.J.1    Vershinin, M.2    Kunwar, A.3    Vallee, R.B.4    Gross, S.P.5
  • 49
    • 42449124179 scopus 로고    scopus 로고
    • Tug-of-war as a cooperative mechanism for bidirectional cargo transport by molecular motors
    • Muller, M. J., Klumpp, S. and Lipowsky, R. (2008). Tug-of-war as a cooperative mechanism for bidirectional cargo transport by molecular motors. Proc. Natl. Acad. Sci. USA 105, 4609-4614.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 4609-4614
    • Muller, M.J.1    Klumpp, S.2    Lipowsky, R.3
  • 50
    • 77952961423 scopus 로고    scopus 로고
    • Bidirectional transport by molecular motors: Enhanced processivity and response to external forces
    • Muller, M. J., Klumpp, S. and Lipowsky, R. (2010). Bidirectional transport by molecular motors: enhanced processivity and response to external forces. Biophys. J. 98, 2610-2618.
    • (2010) Biophys. J. , vol.98 , pp. 2610-2618
    • Muller, M.J.1    Klumpp, S.2    Lipowsky, R.3
  • 51
    • 34548363870 scopus 로고    scopus 로고
    • Intermediate chain subunit as a probe for cytoplasmic dynein function: Biochemical analyses and live cell imaging in PC12 cells
    • Myers, K. R., Lo, K. W., Lye, R. J., Kogoy, J. M., Soura, V., Hafezparast, M. and Pfister, K. K. (2007). Intermediate chain subunit as a probe for cytoplasmic dynein function: biochemical analyses and live cell imaging in PC12 cells. J. Neurosci. Res. 85, 2640-2647.
    • (2007) J. Neurosci. Res. , vol.85 , pp. 2640-2647
    • Myers, K.R.1    Lo, K.W.2    Lye, R.J.3    Kogoy, J.M.4    Soura, V.5    Hafezparast, M.6    Pfister, K.K.7
  • 52
    • 0034520636 scopus 로고    scopus 로고
    • NUDEL is a novel Cdk5 substrate that associates with LIS1 and cytoplasmic dynein
    • Niethammer, M., Smith, D. S., Ayala, R., Peng, J., Ko, J., Lee, M. S., Morabito, M. and Tsai, L. H. (2000). NUDEL is a novel Cdk5 substrate that associates with LIS1 and cytoplasmic dynein. Neuron 28, 697-711.
    • (2000) Neuron , vol.28 , pp. 697-711
    • Niethammer, M.1    Smith, D.S.2    Ayala, R.3    Peng, J.4    Ko, J.5    Lee, M.S.6    Morabito, M.7    Tsai, L.H.8
  • 54
    • 68549121208 scopus 로고    scopus 로고
    • A switch in retrograde signaling from survival to stress in rapid-onset neurodegeneration
    • Perlson, E., Jeong, G. B., Ross, J. L., Dixit, R., Wallace, K. E., Kalb, R. G. and Holzbaur, E. L. (2009). A switch in retrograde signaling from survival to stress in rapid-onset neurodegeneration. J. Neurosci. 29, 9903-9917.
    • (2009) J. Neurosci. , vol.29 , pp. 9903-9917
    • Perlson, E.1    Jeong, G.B.2    Ross, J.L.3    Dixit, R.4    Wallace, K.E.5    Kalb, R.G.6    Holzbaur, E.L.7
  • 57
    • 0030933293 scopus 로고    scopus 로고
    • Regulated bidirectional motility of melanophore pigment granules along microtubules in vitro
    • Rogers, S. L., Tint, I. S., Fanapour, P. C. and Gelfand, V. I. (1997). Regulated bidirectional motility of melanophore pigment granules along microtubules in vitro. Proc. Natl. Acad. Sci. USA 94, 3720-3725.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 3720-3725
    • Rogers, S.L.1    Tint, I.S.2    Fanapour, P.C.3    Gelfand, V.I.4
  • 59
    • 2542424286 scopus 로고    scopus 로고
    • Fast anterograde transport of herpes simplex virus: Role for the amyloid precursor protein of Alzheimer's disease
    • Satpute-Krishnan, P., DeGiorgis, J. A. and Bearer, E. L. (2003). Fast anterograde transport of herpes simplex virus: role for the amyloid precursor protein of Alzheimer's disease. Aging Cell 2, 305-318.
    • (2003) Aging Cell , vol.2 , pp. 305-318
    • Satpute-Krishnan, P.1    DeGiorgis, J.A.2    Bearer, E.L.3
  • 61
    • 0006163872 scopus 로고
    • Dynein is the motor for retrograde axonal transport of organelles
    • Schnapp, B. J. and Reese, T. S. (1989). Dynein is the motor for retrograde axonal transport of organelles. Proc. Natl. Acad. Sci. USA 86, 1548-1552.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 1548-1552
    • Schnapp, B.J.1    Reese, T.S.2
  • 63
    • 79955651488 scopus 로고    scopus 로고
    • Mechanistic logic underlying the axonal transport of cytosolic proteins
    • Scott, D. A., Das, U., Tang, Y. and Roy, S. (2011). Mechanistic logic underlying the axonal transport of cytosolic proteins. Neuron 70, 441-454.
    • (2011) Neuron , vol.70 , pp. 441-454
    • Scott, D.A.1    Das, U.2    Tang, Y.3    Roy, S.4
  • 64
    • 0037119947 scopus 로고    scopus 로고
    • Single-molecule investigation of the interference between kinesin, tau and MAP2c
    • Seitz, A., Kojima, H., Oiwa, K., Mandelkow, E. M., Song, Y. H. and Mandelkow, E. (2002). Single-molecule investigation of the interference between kinesin, tau and MAP2c. EMBO J. 21, 4896-4905.
    • (2002) EMBO J. , vol.21 , pp. 4896-4905
    • Seitz, A.1    Kojima, H.2    Oiwa, K.3    Mandelkow, E.M.4    Song, Y.H.5    Mandelkow, E.6
  • 67
    • 57149145788 scopus 로고    scopus 로고
    • Consequences of motor copy number on the intracellular transport of kinesin-1-driven lipid droplets
    • Shubeita, G. T., Tran, S. L., Xu, J., Vershinin, M., Cermelli, S., Cotton, S. L., Welte, M. A. and Gross, S. P. (2008). Consequences of motor copy number on the intracellular transport of kinesin-1-driven lipid droplets. Cell 135, 1098-1107.
    • (2008) Cell , vol.135 , pp. 1098-1107
    • Shubeita, G.T.1    Tran, S.L.2    Xu, J.3    Vershinin, M.4    Cermelli, S.5    Cotton, S.L.6    Welte, M.A.7    Gross, S.P.8
  • 68
    • 34447127515 scopus 로고    scopus 로고
    • Potential role for phosphorylation in differential regulation of the assembly of dynein light chains
    • Song, Y., Benison, G., Nyarko, A., Hays, T. S. and Barbar, E. (2007). Potential role for phosphorylation in differential regulation of the assembly of dynein light chains. J. Biol. Chem. 282, 17,272-17,279.
    • (2007) J. Biol. Chem. , vol.282 , pp. 17272-17279
    • Song, Y.1    Benison, G.2    Nyarko, A.3    Hays, T.S.4    Barbar, E.5
  • 69
    • 34547958546 scopus 로고    scopus 로고
    • NudE and NudEL are required for mitotic progression and are involved in dynein recruitment to kinetochores
    • Stehman, S. A., Chen, Y., McKenney, R. J. and Vallee, R. B. (2007). NudE and NudEL are required for mitotic progression and are involved in dynein recruitment to kinetochores. J. Cell Biol. 178, 583-594.
    • (2007) J. Cell Biol. , vol.178 , pp. 583-594
    • Stehman, S.A.1    Chen, Y.2    McKenney, R.J.3    Vallee, R.B.4
  • 70
    • 33746355958 scopus 로고    scopus 로고
    • Axonal transport and Alzheimer's disease
    • Stokin, G. B. and Goldstein, L. S. (2006). Axonal transport and Alzheimer's disease. Annu. Rev. Biochem. 75, 607-627.
    • (2006) Annu. Rev. Biochem. , vol.75 , pp. 607-627
    • Stokin, G.B.1    Goldstein, L.S.2
  • 71
    • 0034730328 scopus 로고    scopus 로고
    • Oligomeric tubulin in large transporting complex is transported via kinesin in squid giant axons
    • Terada, S., Kinjo, M. and Hirokawa, N. (2000). Oligomeric tubulin in large transporting complex is transported via kinesin in squid giant axons. Cell 103, 141-155.
    • (2000) Cell , vol.103 , pp. 141-155
    • Terada, S.1    Kinjo, M.2    Hirokawa, N.3
  • 74
    • 0022385727 scopus 로고
    • Identification of a novel forcegenerating protein, kinesin, involved in microtubule-based motility
    • Vale, R. D., Reese, T. S. and Sheetz, M. P. (1985a). Identification of a novel forcegenerating protein, kinesin, involved in microtubule-based motility. Cell 42, 39-50.
    • (1985) Cell , vol.42 , pp. 39-50
    • Vale, R.D.1    Reese, T.S.2    Sheetz, M.P.3
  • 75
    • 0022294771 scopus 로고
    • Different axoplasmic proteins generate movement in opposite directions along microtubules in vitro
    • Vale, R. D., Schnapp, B. J., Mitchison, T., Steuer, E., Reese, T. S. and Sheetz, M. P. (1985b). Different axoplasmic proteins generate movement in opposite directions along microtubules in vitro. Cell 43, 623-632.
    • (1985) Cell , vol.43 , pp. 623-632
    • Vale, R.D.1    Schnapp, B.J.2    Mitchison, T.3    Steuer, E.4    Reese, T.S.5    Sheetz, M.P.6
  • 76
    • 0021849732 scopus 로고
    • Organelle, bead, and microtubule translocations promoted by soluble factors from the squid giant axon
    • Vale, R. D., Schnapp, B. J., Reese, T. S. and Sheetz, M. P. (1985c). Organelle, bead, and microtubule translocations promoted by soluble factors from the squid giant axon. Cell 40, 559-569.
    • (1985) Cell , vol.40 , pp. 559-569
    • Vale, R.D.1    Schnapp, B.J.2    Reese, T.S.3    Sheetz, M.P.4
  • 77
    • 0029879228 scopus 로고    scopus 로고
    • Direct observation of single kinesin molecules moving along microtubules
    • Vale, R. D., Funatsu, T., Pierce, D. W., Romberg, L., Harada, Y. and Yanagida, T. (1996). Direct observation of single kinesin molecules moving along microtubules. Nature 380, 451-453.
    • (1996) Nature , vol.380 , pp. 451-453
    • Vale, R.D.1    Funatsu, T.2    Pierce, D.W.3    Romberg, L.4    Harada, Y.5    Yanagida, T.6
  • 78
    • 0842333851 scopus 로고    scopus 로고
    • Dynein: An ancient motor protein involved in multiple modes of transport
    • Vallee, R. B., Williams, J. C., Varma, D. and Barnhart, L. E. (2004). Dynein: an ancient motor protein involved in multiple modes of transport. J. Neurobiol. 58, 189-200.
    • (2004) J. Neurobiol. , vol.58 , pp. 189-200
    • Vallee, R.B.1    Williams, J.C.2    Varma, D.3    Barnhart, L.E.4
  • 79
    • 0035854775 scopus 로고    scopus 로고
    • Cytoplasmic dynein intermediate chain phosphorylation regulates binding to dynactin
    • Vaughan, P. S., Leszyk, J. D. and Vaughan, K. T. (2001). Cytoplasmic dynein intermediate chain phosphorylation regulates binding to dynactin. J. Biol. Chem. 276, 26,171-26,179.
    • (2001) J. Biol. Chem. , vol.276 , pp. 26171-26179
    • Vaughan, P.S.1    Leszyk, J.D.2    Vaughan, K.T.3
  • 80
    • 61349169838 scopus 로고    scopus 로고
    • Fast fluorescence microscopy for imaging the dynamics of embryonic development
    • Vermot, J., Fraser, S. E. and Liebling, M. (2008). Fast fluorescence microscopy for imaging the dynamics of embryonic development. HFSP J. 2, 143-155.
    • (2008) HFSP J. , vol.2 , pp. 143-155
    • Vermot, J.1    Fraser, S.E.2    Liebling, M.3
  • 82
    • 43149098264 scopus 로고    scopus 로고
    • Tuning microtubule-based transport through filamentous MAPs: The problem of dynein
    • Vershinin, M., Xu, J., Razafsky, D. S., King, S. J. and Gross, S. P. (2008). Tuning microtubule-based transport through filamentous MAPs: the problem of dynein. Traffic 9, 882-892.
    • (2008) Traffic , vol.9 , pp. 882-892
    • Vershinin, M.1    Xu, J.2    Razafsky, D.S.3    King, S.J.4    Gross, S.P.5
  • 83
    • 78650941122 scopus 로고    scopus 로고
    • Identification of a novel dynein-binding domain in Nudel essential for spindle pole organization in Xenopus egg extracts
    • Wang, S. and Zheng, Y. (2010). Identification of a novel dynein-binding domain in Nudel essential for spindle pole organization in Xenopus egg extracts. J. Biol. Chem. 286, 587-593.
    • (2010) J. Biol. Chem. , vol.286 , pp. 587-593
    • Wang, S.1    Zheng, Y.2
  • 85
    • 0037315489 scopus 로고    scopus 로고
    • Human Nudel and NudE as regulators of cytoplasmic dynein in poleward protein transport along the mitotic spindle
    • Yan, X., Li, F., Liang, Y., Shen, Y., Zhao, X., Huang, Q. and Zhu, X. (2003). Human Nudel and NudE as regulators of cytoplasmic dynein in poleward protein transport along the mitotic spindle. Mol. Cell. Biol. 23, 1239-1250.
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 1239-1250
    • Yan, X.1    Li, F.2    Liang, Y.3    Shen, Y.4    Zhao, X.5    Huang, Q.6    Zhu, X.7
  • 86
    • 68549111211 scopus 로고    scopus 로고
    • Nudel promotes axonal lysosome clearance and endo-lysosome formation via dyneinmediated transport
    • Zhang, Q., Wang, F., Cao, J., Shen, Y., Huang, Q., Bao, L. and Zhu, X. (2009). Nudel promotes axonal lysosome clearance and endo-lysosome formation via dyneinmediated transport. Traffic 10, 1337-1349.
    • (2009) Traffic , vol.10 , pp. 1337-1349
    • Zhang, Q.1    Wang, F.2    Cao, J.3    Shen, Y.4    Huang, Q.5    Bao, L.6    Zhu, X.7


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