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Volumn 422, Issue 6933, 2003, Pages 759-765

Molecular motors

Author keywords

[No Author keywords available]

Indexed keywords

CYTOLOGY; DISEASE CONTROL; MOLECULAR DYNAMICS;

EID: 0037452091     PISSN: 00280836     EISSN: None     Source Type: Journal    
DOI: 10.1038/nature01601     Document Type: Review
Times cited : (931)

References (101)
  • 2
    • 0030267349 scopus 로고    scopus 로고
    • Switches, latches, and amplifiers: Common themes of G proteins and molecular motors
    • Vale, R. D. Switches, latches, and amplifiers: common themes of G proteins and molecular motors. J. Cell Biol. 135, 291-302 (1996).
    • (1996) J. Cell Biol. , vol.135 , pp. 291-302
    • Vale, R.D.1
  • 4
    • 0035355208 scopus 로고    scopus 로고
    • A structural pathway for activation of the kinesin motor ATPase
    • Yun, M., Zhang, X., Park, C. G., Park, H. W. & Endow, S. A. A structural pathway for activation of the kinesin motor ATPase. EMBO J. 20, 2611-2618 (2000).
    • (2000) EMBO J. , vol.20 , pp. 2611-2618
    • Yun, M.1    Zhang, X.2    Park, C.G.3    Park, H.W.4    Endow, S.A.5
  • 5
    • 0035092686 scopus 로고    scopus 로고
    • A myosin 11 mutation uncouples ATPase activity from motility and shortens step size
    • Murphy, C. T., Rock, R. S. & Spudich, J. A. A myosin 11 mutation uncouples ATPase activity from motility and shortens step size. Nature Cell Biol. 3, 311-315 (2002).
    • (2002) Nature Cell Biol. , vol.3 , pp. 311-315
    • Murphy, C.T.1    Rock, R.S.2    Spudich, J.A.3
  • 6
    • 0032883413 scopus 로고    scopus 로고
    • Structural mechanism of muscle contraction
    • Geeves M. A. & Holmes, K. C. Structural mechanism of muscle contraction. Annu. Rev. Biochem. 68, 687-728 (1999).
    • (1999) Annu. Rev. Biochem. , vol.68 , pp. 687-728
    • Geeves, M.A.1    Holmes, K.C.2
  • 8
    • 0035344213 scopus 로고    scopus 로고
    • The myosin swinging cross-bridge model
    • Spudich, J. A. The myosin swinging cross-bridge model. Nature Rev. Mol. Cell Biol. 2, 387-392 (2001).
    • (2001) Nature Rev. Mol. Cell Biol. , vol.2 , pp. 387-392
    • Spudich, J.A.1
  • 9
    • 0035123582 scopus 로고    scopus 로고
    • Single-molecule tracking of myosins with genetically engineered amplifier domains
    • Ruff, C., Furch, M., Brenner, B., Manstein, D. J. & Meyhofer, E. Single-molecule tracking of myosins with genetically engineered amplifier domains. Nature Struct. Biol. 8, 226-229 (2001).
    • (2001) Nature Struct. Biol. , vol.8 , pp. 226-229
    • Ruff, C.1    Furch, M.2    Brenner, B.3    Manstein, D.J.4    Meyhofer, E.5
  • 10
    • 0037033787 scopus 로고    scopus 로고
    • Secretory vesicle transport velocity in living cells depends on the myosin-V lever arm length
    • Schott, D. H., Collins, R. N. & Bretscher, A. Secretory vesicle transport velocity in living cells depends on the myosin-V lever arm length. J. Cell Biol. 156, 35-39 (2002).
    • (2002) J. Cell Biol. , vol.156 , pp. 35-39
    • Schott, D.H.1    Collins, R.N.2    Bretscher, A.3
  • 11
    • 0033576727 scopus 로고    scopus 로고
    • A structural change in the kinesin motor protein that drives motility
    • Rice, S. et al. A structural change in the kinesin motor protein that drives motility. Nature 402, 778-784 (1999).
    • (1999) Nature , vol.402 , pp. 778-784
    • Rice, S.1
  • 12
    • 0034695259 scopus 로고    scopus 로고
    • 15 A resolution model of the monomeric kinesin motor, KFA
    • Kikkawa, M., Okada, Y. & Hirokawa, N. 15 A resolution model of the monomeric kinesin motor, KFA. Cell 100, 241-252 (2000).
    • (2000) Cell , vol.100 , pp. 241-252
    • Kikkawa, M.1    Okada, Y.2    Hirokawa, N.3
  • 13
    • 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
  • 14
    • 0034001336 scopus 로고    scopus 로고
    • Functional elements within the dynein microtubule-binding domain
    • Koonce, M. P. & Tikhonenko, I. Functional elements within the dynein microtubule-binding domain. Mol. Biol. Cell 11, 523-529 (2000).
    • (2000) Mol. Biol. Cell , vol.11 , pp. 523-529
    • Koonce, M.P.1    Tikhonenko, I.2
  • 16
    • 0029156511 scopus 로고
    • Highly processive microtubule-stimulated ATP hydrolysis by dimeric kinesin head domains
    • Hackney, D. D. Highly processive microtubule-stimulated ATP hydrolysis by dimeric kinesin head domains. Nature 377, 448-450 (1995).
    • (1995) Nature , vol.377 , pp. 448-450
    • Hackney, D.D.1
  • 17
    • 0036469037 scopus 로고    scopus 로고
    • Distinguishing inchworm and hand-over-hand processive kinesin movement by neck rotation measurements
    • Hua, W., Chung, J. & Gelles, J. Distinguishing inchworm and hand-over-hand processive kinesin movement by neck rotation measurements. Science 295, 844-848 (2002).
    • (2002) Science , vol.295 , pp. 844-848
    • Hua, W.1    Chung, J.2    Gelles, J.3
  • 18
    • 0031471243 scopus 로고    scopus 로고
    • The crystal structure of dimeric kinesin and implications for microtubuledependent motility
    • Kozielski, F. et al. The crystal structure of dimeric kinesin and implications for microtubuledependent motility. Cell 1191, 985-994 (1997).
    • (1997) Cell , vol.1191 , pp. 985-994
    • Kozielski, F.1
  • 19
    • 0035890334 scopus 로고    scopus 로고
    • Unusual properties of the fungal conventional kinesin neck domain from Neurospora crassa
    • Kallipolitou, A. et al. Unusual properties of the fungal conventional kinesin neck domain from Neurospora crassa. EMBO J. 20, 6226-6235 (2001).
    • (2001) EMBO J. , vol.20 , pp. 6226-6235
    • Kallipolitou, A.1
  • 20
    • 0034722388 scopus 로고    scopus 로고
    • Controlling kinesin by reversible disulfide cross-linking. Identifying the motility-producing conformational change
    • Tomishige, M. & Vale, R. D. Controlling kinesin by reversible disulfide cross-linking. Identifying the motility-producing conformational change. J. Cell Biol. 151, 1081-1092 (2000).
    • (2000) J. Cell Biol. , vol.151 , pp. 1081-1092
    • Tomishige, M.1    Vale, R.D.2
  • 21
    • 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
  • 24
    • 0035923504 scopus 로고    scopus 로고
    • Myosin VI is a processive motor with a large step size
    • Rock, R. S. et al. Myosin VI is a processive motor with a large step size. Proc. Natl Acad. Sci. USA 98, 13655-13659 (2001).
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 13655-13659
    • Rock, R.S.1
  • 25
    • 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
  • 26
    • 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
  • 27
    • 0036222522 scopus 로고    scopus 로고
    • Myosin Xb is a single-headed minus-end-directed processive motor
    • Inoue, A., Saito, J., Ikebe, R. & Ikebe, M. Myosin Xb is a single-headed minus-end-directed processive motor. Nature Cell Biol. 4, 302-306 (2002).
    • (2002) Nature Cell Biol. , vol.4 , pp. 302-306
    • Inoue, A.1    Saito, J.2    Ikebe, R.3    Ikebe, M.4
  • 28
    • 0033527027 scopus 로고    scopus 로고
    • Inner-arm dynein c of Chlamydomonas flagella is a single-headed processive motor
    • Sakakibara, H., Kojima, H., Saka,i Y., Katayama, E. & Oiwa, K. Inner-arm dynein c of Chlamydomonas flagella is a single-headed processive motor. Nature 400, 586-590 (1999).
    • (1999) Nature , vol.400 , pp. 586-590
    • Sakakibara, H.1    Kojima, H.2    Saka, I.Y.3    Katayama, E.4    Oiwa, K.5
  • 29
    • 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
  • 30
    • 0034722373 scopus 로고    scopus 로고
    • Engineering the processive run length of the kinesin motor
    • Thorn, K. S., Ubersax, J. A. & Vale, R. D. Engineering the processive run length of the kinesin motor. J. Cell Biol. 151, 1093-1100 (2000).
    • (2000) J. Cell Biol. , vol.151 , pp. 1093-1100
    • Thorn, K.S.1    Ubersax, J.A.2    Vale, R.D.3
  • 31
    • 0035903699 scopus 로고    scopus 로고
    • KIF1D is a fast non-processive kinesin that demonstrates novel K-loop-dependent mechanochemistry
    • Rogers, K. R. et al. KIF1D is a fast non-processive kinesin that demonstrates novel K-loop-dependent mechanochemistry. EMBO J. 20, 5101-5113 (2001).
    • (2001) EMBO J. , vol.20 , pp. 5101-5113
    • Rogers, K.R.1
  • 32
    • 0037183926 scopus 로고    scopus 로고
    • Conversion of Unc104/KIF1A kinesin into a processive motor after dimerization
    • Tomishige, M., Klopfenstein, D. R. & Vale, R. D. Conversion of Unc104/KIF1A kinesin into a processive motor after dimerization. Science 297, 2263-2267 (2002).
    • (2002) Science , vol.297 , pp. 2263-2267
    • Tomishige, M.1    Klopfenstein, D.R.2    Vale, R.D.3
  • 33
    • 0032558718 scopus 로고    scopus 로고
    • Direction determination in the minus-end-directed kinesin motor ncd
    • Sablin, E. P. et al. Direction determination in the minus-end-directed kinesin motor ncd. Nature 395, 813-816 (1998).
    • (1998) Nature , vol.395 , pp. 813-816
    • Sablin, E.P.1
  • 34
    • 0001089368 scopus 로고    scopus 로고
    • Determinants of molecular motor directionality
    • Endow, S. A. Determinants of molecular motor directionality. Nature Cell Biol. 1, E163-E167 (1999).
    • (1999) Nature Cell Biol. , vol.1
    • Endow, S.A.1
  • 35
    • 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
  • 36
    • 0033619258 scopus 로고    scopus 로고
    • Myosin VI is an actin-based motor that moves backwards
    • Wells, A. L. et al. Myosin VI is an actin-based motor that moves backwards. Nature 401, 505-508 (1999).
    • (1999) Nature , vol.401 , pp. 505-508
    • Wells, A.L.1
  • 37
    • 0035939958 scopus 로고    scopus 로고
    • The core of the motor domain determines the direction of myosin movement
    • Homma, K., Yoshimura, M., Saito, J., Ikebe, R. & Ikebe, M. The core of the motor domain determines the direction of myosin movement. Nature 412, 831-834 (2001).
    • (2001) Nature , vol.412 , pp. 831-834
    • Homma, K.1    Yoshimura, M.2    Saito, J.3    Ikebe, R.4    Ikebe, M.5
  • 40
    • 0036284131 scopus 로고    scopus 로고
    • An automated two-dimensional optical force clamp for single molecule studies
    • Lang, M. J., Asbury, C. L., Shaevitz, J. W. & Block, S. M. An automated two-dimensional optical force clamp for single molecule studies. Biophys. J. 83, 491-501 (2002).
    • (2002) Biophys. J. , vol.83 , pp. 491-501
    • Lang, M.J.1    Asbury, C.L.2    Shaevitz, J.W.3    Block, S.M.4
  • 41
    • 0037044779 scopus 로고    scopus 로고
    • Dynamics of myoc (myosin-1β) lipid binding and dissociation
    • Tang, N., Lin, T. & Ostap, E. M. Dynamics of myoc (myosin-1β) lipid binding and dissociation. J. Biol. Chem. (2002).
    • (2002) J. Biol. Chem.
    • Tang, N.1    Lin, T.2    Ostap, E.M.3
  • 42
    • 0037013148 scopus 로고    scopus 로고
    • Role of phosphatidylinositol(4,5)bisphosphate organization in membrane transport by the Unc104 kinesin motor
    • Klopfenstein, D. R., Tomishige, M., Stuurman, N. & Vale, R. D. Role of phosphatidylinositol(4,5)bisphosphate organization in membrane transport by the Unc104 kinesin motor. Cell 109, 347-358 (2002).
    • (2002) Cell , vol.109 , pp. 347-358
    • Klopfenstein, D.R.1    Tomishige, M.2    Stuurman, N.3    Vale, R.D.4
  • 43
    • 0035818998 scopus 로고    scopus 로고
    • Kinesin-mediated axonal transport of a membrane compartment containing βsecretase and presenilin-1 requires APP
    • Kamal, A. et al. Kinesin-mediated axonal transport of a membrane compartment containing βsecretase and presenilin-1 requires APP. Nature 414, 643-648 (2001).
    • (2001) Nature , vol.414 , pp. 643-648
    • Kamal, A.1
  • 44
    • 0033603239 scopus 로고    scopus 로고
    • Rhodopsin's carboxy-terminal cytoplasmic tail acts as a membrane receptor for cytoplasmic dynein by binding to the dynein light chain Tctex-1
    • Tai, A. W., Chuang, J. Z., Bode, C., Wolfrum, U. & Sung, C. H. Rhodopsin's carboxy-terminal cytoplasmic tail acts as a membrane receptor for cytoplasmic dynein by binding to the dynein light chain Tctex-1. Cell 97, 877-887 (1999).
    • (1999) Cell , vol.97 , pp. 877-887
    • Tai, A.W.1    Chuang, J.Z.2    Bode, C.3    Wolfrum, U.4    Sung, C.H.5
  • 45
    • 0033712055 scopus 로고    scopus 로고
    • Kinesin-dependent axonal transport is mediated by the sunday driver (SYD) protein
    • Bowman, A. B. et al. Kinesin-dependent axonal transport is mediated by the sunday driver (SYD) protein. Cell 10, 583-594 (2000).
    • (2000) Cell , vol.10 , pp. 583-594
    • Bowman, A.B.1
  • 46
    • 0035809914 scopus 로고    scopus 로고
    • Cargo of kinesin identified as JIP scaffolding proteins and associated signaling molecules
    • Verhey, K. J. et al. Cargo of kinesin identified as JIP scaffolding proteins and associated signaling molecules. J. Cell Biol. 152, 959-970 (2001).
    • (2001) J. Cell Biol. , vol.152 , pp. 959-970
    • Verhey, K.J.1
  • 47
    • 0033730445 scopus 로고    scopus 로고
    • Moving on to the cargo problem of microtubule-dependent motors in neurons
    • Terada, S. & Hirokawa, N. Moving on to the cargo problem of microtubule-dependent motors in neurons. Curr. Opin. Neurobiol. 10, 566-573 (2000).
    • (2000) Curr. Opin. Neurobiol. , vol.10 , pp. 566-573
    • Terada, S.1    Hirokawa, N.2
  • 48
    • 0036226156 scopus 로고    scopus 로고
    • Identification of an organelle receptor for myosin-Va
    • Wu, X. S. et al. Identification of an organelle receptor for myosin-Va. Nature Cell Biol. 4, 271-278 (2002).
    • (2002) Nature Cell Biol. , vol.4 , pp. 271-278
    • Wu, X.S.1
  • 49
    • 0036468368 scopus 로고    scopus 로고
    • Rabs grab motors: Defining the connections between Rab GTPases and motor proteins
    • Hammer, J. A. III & Wu, X. S. Rabs grab motors: defining the connections between Rab GTPases and motor proteins. Curr. Opin. Cell Biol. 14, 69-75 (2002).
    • (2002) Curr. Opin. Cell Biol. , vol.14 , pp. 69-75
    • Hammer J.A. III1    Wu, X.S.2
  • 50
    • 0031947483 scopus 로고    scopus 로고
    • The role of the dynactin complex in intracellular motility
    • Holleran, E. A., Karki, S. & Holzbaur, E. L. The role of the dynactin complex in intracellular motility. Int. Rev. Cytol. 18, 69-109 (1998).
    • (1998) Int. Rev. Cytol. , vol.18 , pp. 69-109
    • Holleran, E.A.1    Karki, S.2    Holzbaur, E.L.3
  • 51
    • 0035104723 scopus 로고    scopus 로고
    • Dynactin-dependent, dynein-driven vesicle transport in the absence of membrane proteins: A role for spectrin and acidic phospholipids
    • Muresan, V. et al. Dynactin-dependent, dynein-driven vesicle transport in the absence of membrane proteins: a role for spectrin and acidic phospholipids. Mol. Cell 7, 173-183 (2001).
    • (2001) Mol. Cell , vol.7 , pp. 173-183
    • Muresan, V.1
  • 52
    • 0035902995 scopus 로고    scopus 로고
    • Cell cycle regulation of myosin-V by calcium/calmodulin-dependent protein kinase II
    • Karcher, R. L. et al. Cell cycle regulation of myosin-V by calcium/calmodulin-dependent protein kinase II. Science 293, 1317-1320 (2001).
    • (2001) Science , vol.293 , pp. 1317-1320
    • Karcher, R.L.1
  • 53
    • 0035844158 scopus 로고    scopus 로고
    • Phosphorylation by cdc2-cyclinB-1 kinase releases cytoplasmic dynein from membranes
    • Addinall, S. G. et al. Phosphorylation by cdc2-cyclinB-1 kinase releases cytoplasmic dynein from membranes. J. Biol. Chem. 276, 15939-15944 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 15939-15944
    • Addinall, S.G.1
  • 54
    • 0036469290 scopus 로고    scopus 로고
    • Glycogen synthase kinase 3 phosphorylates kinesin light chains and negatively regulates kinesin-based motility
    • Morfini, G., Szebenyi, G., Elluru, R., Ratner, N. & Brady, S. T. Glycogen synthase kinase 3 phosphorylates kinesin light chains and negatively regulates kinesin-based motility. EMBO J. 21, 281-293 (2002).
    • (2002) EMBO J. , vol.21 , pp. 281-293
    • Morfini, G.1    Szebenyi, G.2    Elluru, R.3    Ratner, N.4    Brady, S.T.5
  • 55
    • 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. & Howard, J. Kinesin's tail domain is an inhibitory regulator of the motor domain. Nature Cell Biol. 1, 289-292 (1999).
    • (1999) Nature Cell Biol. , vol.1 , pp. 289-292
    • Coy, D.L.1    Hancock, W.O.2    Wagenbach, M.3    Howard, J.4
  • 56
    • 0033195492 scopus 로고    scopus 로고
    • Single-molecule analysis of kinesin motility reveals regulation by the cargo-binding tail domain
    • Friedman, D. S. & Vale, R. D. Single-molecule analysis of kinesin motility reveals regulation by the cargo-binding tail domain. Nature Cell Biol. 1, 293-297 (1999).
    • (1999) Nature Cell Biol. , vol.1 , pp. 293-297
    • Friedman, D.S.1    Vale, R.D.2
  • 57
    • 0033771938 scopus 로고    scopus 로고
    • Cargo binding and regulatory sites in the tail of fungal conventional kinesin
    • Seiler, S. et al. Cargo binding and regulatory sites in the tail of fungal conventional kinesin. Nature Cell Biol. 2, 333-338 (2000).
    • (2000) Nature Cell Biol. , vol.2 , pp. 333-338
    • Seiler, S.1
  • 58
    • 0033771901 scopus 로고    scopus 로고
    • Kinesin's IAK tail domain inhibits initial microtubule-stimulated ADP release
    • Hackney, D. D. & Stock, M. F. Kinesin's IAK tail domain inhibits initial microtubule-stimulated ADP release. Nature Cell Biol. 2, 257-260 (2000).
    • (2000) Nature Cell Biol. , vol.2 , pp. 257-260
    • Hackney, D.D.1    Stock, M.F.2
  • 59
    • 0033280225 scopus 로고    scopus 로고
    • Cooperation between microtubule- and actin-based motor proteins
    • Brown, S. S. Cooperation between microtubule- and actin-based motor proteins. Annu. Rev. Cell Dev. Biol. 15, 63-80 (1999).
    • (1999) Annu. Rev. Cell Dev. Biol. , vol.15 , pp. 63-80
    • Brown, S.S.1
  • 60
    • 0037018150 scopus 로고    scopus 로고
    • Interactions and regulation of molecular motors in Xenopus melanophores
    • Gross, S. P. et al. Interactions and regulation of molecular motors in Xenopus melanophores. J. Cell Biol. 156, 855-865 (2002).
    • (2002) J. Cell Biol. , vol.156 , pp. 855-865
    • Gross, S.P.1
  • 61
    • 0036226156 scopus 로고    scopus 로고
    • Identification of an organelle receptor for myosin-Va
    • Wu, X. S. et al. Identification of an organelle receptor for myosin-Va. Nature Cell Biol. 4, 271-278 (2002).
    • (2002) Nature Cell Biol. , vol.4 , pp. 271-278
    • Wu, X.S.1
  • 62
    • 0032872611 scopus 로고    scopus 로고
    • Myosin Va movements in normal and dilute-lethal axons provide support for a dual filament motor complex
    • Bridgman, P. C. Myosin Va movements in normal and dilute-lethal axons provide support for a dual filament motor complex. J. Cell Biol. 146, 1045-1060 (1999).
    • (1999) J. Cell Biol. , vol.146 , pp. 1045-1060
    • Bridgman, P.C.1
  • 63
    • 0033590558 scopus 로고    scopus 로고
    • Direct interaction of microtubule- and actin-based transport motors
    • Huang, I. D. et al. Direct interaction of microtubule- and actin-based transport motors. Nature 397, 267-270 (1999).
    • (1999) Nature , vol.397 , pp. 267-270
    • Huang, I.D.1
  • 64
    • 0035320036 scopus 로고    scopus 로고
    • mRNA localization: Message on the move
    • Jansen, R. P. mRNA localization: message on the move. Nature Rev. Mol. Cell Biol. 2, 247-256 (2001).
    • (2001) Nature Rev. Mol. Cell Biol. , vol.2 , pp. 247-256
    • Jansen, R.P.1
  • 65
    • 0034109216 scopus 로고    scopus 로고
    • Molecular insights into mRNA transport and local translation in the mammalian nervous system
    • Kiebler, M. A. & DesGroseillers, L. Molecular insights into mRNA transport and local translation in the mammalian nervous system. Neuron 25, 19-28 (2000).
    • (2000) Neuron , vol.25 , pp. 19-28
    • Kiebler, M.A.1    DesGroseillers, L.2
  • 66
    • 0034795562 scopus 로고    scopus 로고
    • Cytoskeleton-dependent transport and localization of mRNA
    • Stebbings, H. Cytoskeleton-dependent transport and localization of mRNA. Int. Rev. Cytol. 211, 1-31 (2001).
    • (2001) Int. Rev. Cytol. , vol.211 , pp. 1-31
    • Stebbings, H.1
  • 67
    • 0034703428 scopus 로고    scopus 로고
    • A function for kinesin I in the posterior transport of oskar mRNA and Staufen protein
    • Brendza, R. P., Serbus, L. R., Duffy, J. B. & Saxton, W. M. A function for kinesin I in the posterior transport of oskar mRNA and Staufen protein. Science 289, 2120-2122 (2000).
    • (2000) Science , vol.289 , pp. 2120-2122
    • Brendza, R.P.1    Serbus, L.R.2    Duffy, J.B.3    Saxton, W.M.4
  • 68
    • 0035854361 scopus 로고    scopus 로고
    • In vivo analysis of Drosophila bicoid mRNA localization reveals a novel microtubule-dependent axis specification pathway
    • Cha, B. J., Koppetsch, B. S. & Theurkauf, W. E. In vivo analysis of Drosophila bicoid mRNA localization reveals a novel microtubule-dependent axis specification pathway. Cell 106, 35-46 (2001).
    • (2001) Cell , vol.106 , pp. 35-46
    • Cha, B.J.1    Koppetsch, B.S.2    Theurkauf, W.E.3
  • 69
    • 0033787039 scopus 로고    scopus 로고
    • The molecular motor dynein is involved in targeting swallow and bicoid RNA to the anterior pole of Drosophila oocytes
    • Schnorrer, F., Bohmann, K. & Nüsslein-Volhard, C. The molecular motor dynein is involved in targeting swallow and bicoid RNA to the anterior pole of Drosophila oocytes. Nature Cell Biol. 2, 185-190 (2000).
    • (2000) Nature Cell Biol. , vol.2 , pp. 185-190
    • Schnorrer, F.1    Bohmann, K.2    Nüsslein-Volhard, C.3
  • 70
    • 0030656618 scopus 로고    scopus 로고
    • Mutation of an axonemal dynein affects left-right asymmetry in inversus viscerum mice
    • Supp, D. M., Witte, D. P., Potter, S. S. & Brueckner, M. Mutation of an axonemal dynein affects left-right asymmetry in inversus viscerum mice. Nature 389, 963-966 (1997).
    • (1997) Nature , vol.389 , pp. 963-966
    • Supp, D.M.1    Witte, D.P.2    Potter, S.S.3    Brueckner, M.4
  • 71
    • 0032428685 scopus 로고    scopus 로고
    • Randomization of left-right asymmetry due to loss of nodal cilia generating leftward flow of extraembryonicfluid in mice lacking KIF3B motor protein
    • Nonaka, S. et al. Randomization of left-right asymmetry due to loss of nodal cilia generating leftward flow of extraembryonicfluid in mice lacking KIF3B motor protein. Cell 95, 829-837 (1998).
    • (1998) Cell , vol.95 , pp. 829-837
    • Nonaka, S.1
  • 72
    • 0037019287 scopus 로고    scopus 로고
    • Determination of left-right patterning of the mouse embryo by artificial nodal flow
    • Nonaka, S., Shiratori, H., Saijoh, Y. & Hamada, H. Determination of left-right patterning of the mouse embryo by artificial nodal flow. Nature 418, 96-99 (2002).
    • (2002) Nature , vol.418 , pp. 96-99
    • Nonaka, S.1    Shiratori, H.2    Saijoh, Y.3    Hamada, H.4
  • 73
    • 0036000019 scopus 로고    scopus 로고
    • PLAC-24 is a cytoplasmic dynein-binding protein that is recruited to sites of cell-cell contact
    • Karki, S., Ligon, L. A., DeSantis, J., Tokito, M. & Holzbaur, E. L. PLAC-24 is a cytoplasmic dynein-binding protein that is recruited to sites of cell-cell contact. Mol. Biol. Cell 13, 1722-1734 (2002).
    • (2002) Mol. Biol. Cell , vol.13 , pp. 1722-1734
    • Karki, S.1    Ligon, L.A.2    DeSantis, J.3    Tokito, M.4    Holzbaur, E.L.5
  • 75
    • 0037182581 scopus 로고    scopus 로고
    • A requirement for cytoplasmic dynein and dynactin in intermediate filament network assembly and organization
    • Helfand, B. T., Mikami, A., Vallee, R. B. & Goldman, R. D. A requirement for cytoplasmic dynein and dynactin in intermediate filament network assembly and organization. J. Cell Biol. 157, 795-806 (2002).
    • (2002) J. Cell Biol. , vol.157 , pp. 795-806
    • Helfand, B.T.1    Mikami, A.2    Vallee, R.B.3    Goldman, R.D.4
  • 76
    • 0035510709 scopus 로고    scopus 로고
    • Kinesin, dynein and neurofilament transport
    • Shea, T. B. & Flanagan, L. A. Kinesin, dynein and neurofilament transport. Trends Neurosci. 24, 644-648 (2001).
    • (2001) Trends Neurosci. , vol.24 , pp. 644-648
    • Shea, T.B.1    Flanagan, L.A.2
  • 77
    • 0036226855 scopus 로고    scopus 로고
    • Identification of a link between the tumour suppressor APC and the kinesin superfamily
    • Jimbo, T. et al. Identification of a link between the tumour suppressor APC and the kinesin superfamily. Nature Cell Biol. 4, 323-327 (2002).
    • (2002) Nature Cell Biol. , vol.4 , pp. 323-327
    • Jimbo, T.1
  • 78
    • 0036796793 scopus 로고    scopus 로고
    • Glued is required for the formation and maintenance of a radial microtubule array anchored at the centrosome
    • Glued is required for the formation and maintenance of a radial microtubule array anchored at the centrosome. Mol. Biol. Cell 13, 3627-3645 (2002).
    • (2002) Mol. Biol. Cell , vol.13 , pp. 3627-3645
    • Askham, J.M.1    Vaughan, K.T.2    Goodson, H.V.3    Morrison, E.E.4
  • 79
    • 0032559641 scopus 로고    scopus 로고
    • A class VI unconventional myosin is associated with a homologue of a microtubule-binding protein, cytoplasmic linker protein-170, in neurons and at the posterior pole of Drosophila embryos
    • Lantz, V. A. & Miller, K. G. A class VI unconventional myosin is associated with a homologue of a microtubule-binding protein, cytoplasmic linker protein-170, in neurons and at the posterior pole of Drosophila embryos. J. Cell Biol. 140, 897-910 (1999).
    • (1999) J. Cell Biol. , vol.140 , pp. 897-910
    • Lantz, V.A.1    Miller, K.G.2
  • 80
    • 0037018147 scopus 로고    scopus 로고
    • CHOI a mammalian kinesin-like protein, interacts with F-actin and is involved in the terminal phase of cytokinesis
    • Kuriyama, R., Gustus, C., Terada, Y., Uetake, Y. & Matuliene, J. CHOI, a mammalian kinesin-like protein, interacts with F-actin and is involved in the terminal phase of cytokinesis. J. Cell Biol. 156, 783-790 (2002).
    • (2002) J. Cell Biol. , vol.156 , pp. 783-790
    • Kuriyama, R.1    Gustus, C.2    Terada, Y.3    Uetake, Y.4    Matuliene, J.5
  • 81
    • 0035422395 scopus 로고    scopus 로고
    • The Ras-like GTPase Gem is involved in cell shape remodelling and interacts with the novel kinesin-like protein KIF9
    • Piddini, E., Schmid, J. A., de Martin, R. & Dotti, C. G. The Ras-like GTPase Gem is involved in cell shape remodelling and interacts with the novel kinesin-like protein KIF9. EMBO J. 20, 4076-4087 (2001).
    • (2001) EMBO J. , vol.20 , pp. 4076-4087
    • Piddini, E.1    Schmid, J.A.2    De Martin, R.3    Dotti, C.G.4
  • 82
    • 0033661719 scopus 로고    scopus 로고
    • The light chain composition of chicken brain myosin-Va: Calmodulin, myosin-II essential light chains, and 8-kDa dynein light chain/PIN
    • Espindola, F. S. et al. The light chain composition of chicken brain myosin-Va: calmodulin, myosin-II essential light chains, and 8-kDa dynein light chain/PIN. Cell Motil. Cytoskel. 47, 269-281 (2000).
    • (2000) Cell Motil. Cytoskel. , vol.47 , pp. 269-281
    • Espindola, F.S.1
  • 83
    • 0034608071 scopus 로고    scopus 로고
    • Interaction of a kinesin-like calmodulin-binding protein with a protein kinase
    • Day, I. S., Miller, C., Golovkin, M. & Reddy, A. S. Interaction of a kinesin-like calmodulin-binding protein with a protein kinase. J. Biol. Chem. 275, 13737-13745 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 13737-13745
    • Day, I.S.1    Miller, C.2    Golovkin, M.3    Reddy, A.S.4
  • 84
    • 0034568928 scopus 로고    scopus 로고
    • Construction of centrosomes and spindle poles by molecular motordriven assembly of protein particles
    • Zimmerman, W. & Doxsey, S. J. Construction of centrosomes and spindle poles by molecular motordriven assembly of protein particles. Traffic 1, 927-934 (2000).
    • (2000) Traffic , vol.1 , pp. 927-934
    • Zimmerman, W.1    Doxsey, S.J.2
  • 85
    • 0342903325 scopus 로고    scopus 로고
    • Physical properties determining self-organization of motors and microtubules
    • Surrey, T., Nedelec, F., Leibler, S. & Karsenti, E. Physical properties determining self-organization of motors and microtubules. Science 292, 1167-1171 (2001).
    • (2001) Science , vol.292 , pp. 1167-1171
    • Surrey, T.1    Nedelec, F.2    Leibler, S.3    Karsenti, E.4
  • 86
    • 85047699197 scopus 로고    scopus 로고
    • Active fluidization of polymer networks through molecular motors
    • Humphrey, D., Duggan, C., Saha, D., Smith, D. & Käs, J. Active fluidization of polymer networks through molecular motors. Nature 416, 413-416 (2002).
    • (2002) Nature , vol.416 , pp. 413-416
    • Humphrey, D.1    Duggan, C.2    Saha, D.3    Smith, D.4    Käs, J.5
  • 88
    • 0035936792 scopus 로고    scopus 로고
    • The genetic basis for cardiomyopathy: From mutation identification to mechanistic paradigms
    • Seidman, J. G. & Seidman, C. The genetic basis for cardiomyopathy: from mutation identification to mechanistic paradigms. Cell 104, 557-567 (2001).
    • (2001) Cell , vol.104 , pp. 557-567
    • Seidman, J.G.1    Seidman, C.2
  • 89
    • 0034787514 scopus 로고    scopus 로고
    • The dilute locus and Griscelli syndrome: Gateways towards a better understanding of melanosome transport
    • Westbroek, W., Lambert, J. & Naeyaert, J. M. The dilute locus and Griscelli syndrome: gateways towards a better understanding of melanosome transport. Pigment Cell Res. 14, 320-327 (2001).
    • (2001) Pigment Cell Res. , vol.14 , pp. 320-327
    • Westbroek, W.1    Lambert, J.2    Naeyaert, J.M.3
  • 90
    • 0036359428 scopus 로고    scopus 로고
    • The genetics of deafness: A model for genomic and biological complexity
    • Avraham, K. B. The genetics of deafness: a model for genomic and biological complexity. Ernst Schering Res. Found. Workshop 36, 271-297 (2002).
    • (2002) Ernst Schering Res. Found. Workshop , vol.36 , pp. 271-297
    • Avraham, K.B.1
  • 91
    • 0034697971 scopus 로고    scopus 로고
    • Genetic evidence for selective transport of opsin and arrestin by kinesin-II in mammalian photoreceptors
    • Marszalek, J. R. et al. Genetic evidence for selective transport of opsin and arrestin by kinesin-II in mammalian photoreceptors. Cell 102, 175-187 (2000).
    • (2000) Cell , vol.102 , pp. 175-187
    • Marszalek, J.R.1
  • 92
    • 0036479029 scopus 로고    scopus 로고
    • Mutations in DNAH5 cause primary ciliary dyskinesia and randomization of leftright asymmetry
    • Olbrich, H. et al. Mutations in DNAH5 cause primary ciliary dyskinesia and randomization of leftright asymmetry. Nature Genet. 30, 143-144 (2002).
    • (2002) Nature Genet. , vol.30 , pp. 143-144
    • Olbrich, H.1
  • 93
    • 0033609103 scopus 로고    scopus 로고
    • Situs inversus and embryonic ciliary morphogenesis defects in mouse mutants lacking the KIF3A subunit of kinesin-II
    • Marszalek, J. R., Ruiz-Lozano, P., Roberts, E., Chien, K. R. & Goldstein, L. S. Situs inversus and embryonic ciliary morphogenesis defects in mouse mutants lacking the KIF3A subunit of kinesin-II. Proc. Natl Acad. Sci. USA 96, 5043-5048 (1999).
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 5043-5048
    • Marszalek, J.R.1    Ruiz-Lozano, P.2    Roberts, E.3    Chien, K.R.4    Goldstein, L.S.5
  • 94
    • 0035916823 scopus 로고    scopus 로고
    • An autosomal recessive polycystic kidney disease gene homolog is involved in intraflagellar transport in C. elegans ciliated sensory neurons
    • Qin, H., Rosenbaum, J. L. & Barr, M. M. An autosomal recessive polycystic kidney disease gene homolog is involved in intraflagellar transport in C. elegans ciliated sensory neurons. Curr. Biol. 11, 457-461 (2001).
    • (2001) Curr. Biol. , vol.11 , pp. 457-461
    • Qin, H.1    Rosenbaum, J.L.2    Barr, M.M.3
  • 95
    • 0035312694 scopus 로고    scopus 로고
    • LIS1: Cellular function of a disease-causing gene
    • Vallee, R. B., Tai, C. & Faulkner, N. E. LIS1: cellular function of a disease-causing gene. Trends Cell Biol. 11, 155-160 (2001).
    • (2001) Trends Cell Biol. , vol.11 , pp. 155-160
    • Vallee, R.B.1    Tai, C.2    Faulkner, N.E.3
  • 96
    • 0035369084 scopus 로고    scopus 로고
    • Charcot-Marie-Tooth disease type 2A caused by mutation in a microtubule motor KIF1Bβ
    • Zhao, C. et al. Charcot-Marie-Tooth disease type 2A caused by mutation in a microtubule motor KIF1Bβ. Cell 105, 587-597 (2001).
    • (2001) Cell , vol.105 , pp. 587-597
    • Zhao, C.1
  • 97
    • 0035736471 scopus 로고    scopus 로고
    • Kinesin-dependent movement on microtubules precedes actin-based motility of vaccinia virus
    • Rietdorf, J. et al. Kinesin-dependent movement on microtubules precedes actin-based motility of vaccinia virus. Nature Cell Biol. 3, 992-1000 (2001).
    • (2001) Nature Cell Biol. , vol.3 , pp. 992-1000
    • Rietdorf, J.1
  • 98
    • 0036678882 scopus 로고    scopus 로고
    • Function of dynein and dynactin in herpes simplex virus capsid transport
    • Dohner, K. et al. Function of dynein and dynactin in herpes simplex virus capsid transport. Mol. Biol. Cell 13, 2795-2809 (2002).
    • (2002) Mol. Biol. Cell , vol.13 , pp. 2795-2809
    • Dohner, K.1
  • 99
    • 0035797887 scopus 로고    scopus 로고
    • Kif-C, a kinesin-like motor protein, mediates mouse macrophage resistance to anthrax lethal factor
    • Watters, J. W., Dewar, K., Lehoczky, J., Boyartchuk, V. & Dietrich, W. F. Kif-C, a kinesin-like motor protein, mediates mouse macrophage resistance to anthrax lethal factor. Curr. Biol. 11, 1503-1511 (2001).
    • (2001) Curr. Biol. , vol.11 , pp. 1503-1511
    • Watters, J.W.1    Dewar, K.2    Lehoczky, J.3    Boyartchuk, V.4    Dietrich, W.F.5
  • 100
    • 0035829720 scopus 로고    scopus 로고
    • Disruption of axonal transport and neuronal viability by amyloid precursor protein mutations in Drosophila
    • Gunawardena, S. & Goldstein, L. S. Disruption of axonal transport and neuronal viability by amyloid precursor protein mutations in Drosophila. Neuron 32, 389-401 (2001).
    • (2001) Neuron , vol.32 , pp. 389-401
    • Gunawardena, S.1    Goldstein, L.S.2
  • 101
    • 0037198698 scopus 로고    scopus 로고
    • Disruption of dynein/dynactin inhibits axonal transport in motor neurons causing late-onset progressive degeneration
    • LaMonte B. H. et al. Disruption of dynein/dynactin inhibits axonal transport in motor neurons causing late-onset progressive degeneration. Neuron 34, 715-727 (2002).
    • (2002) Neuron , vol.34 , pp. 715-727
    • LaMonte, B.H.1


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