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Volumn 111, Issue 21, 1998, Pages 3221-3234

Transport of ER vesicles on actin filaments in neurons by myosin V

Author keywords

Actin filament; Axonal transport; ER transport; Myosin V; Organelle vesicle movement; Squid giant axon

Indexed keywords

ISOMERASE; MYOSIN;

EID: 0031784059     PISSN: 00219533     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (181)

References (76)
  • 1
    • 0019849712 scopus 로고
    • Video-enhanced contrast differential interference contrast (AVEC-DIC) microscopy: A new method capable of analyzing microtubule-related motility in the reticulopodial network of Allogromia laticollaris
    • Allen, R. D., Allen, N. S. and Travis, J. L. (1981). Video-enhanced contrast differential interference contrast (AVEC-DIC) microscopy: A new method capable of analyzing microtubule-related motility in the reticulopodial network of Allogromia laticollaris. Cell Motil. Cytoskel. 1, 291-302.
    • (1981) Cell Motil. Cytoskel. , vol.1 , pp. 291-302
    • Allen, R.D.1    Allen, N.S.2    Travis, J.L.3
  • 2
    • 0021952113 scopus 로고
    • Gliding movements of and bidirectional transport along single native microtubules from squid axoplasm: Evidence for an active role of microtubules in cytoplasmic transport
    • Allen, R. D., Weiss, D. G., Hayden, J. H., Brown, D. T., Fujiwake, H. and Simpson, M. (1985). Gliding movements of and bidirectional transport along single native microtubules from squid axoplasm: Evidence for an active role of microtubules in cytoplasmic transport. J. Cell Biol. 100, 1736-1752.
    • (1985) J. Cell Biol. , vol.100 , pp. 1736-1752
    • Allen, R.D.1    Weiss, D.G.2    Hayden, J.H.3    Brown, D.T.4    Fujiwake, H.5    Simpson, M.6
  • 3
  • 4
    • 0030861056 scopus 로고    scopus 로고
    • Dimerization of the highly conserved light chain shared by dynein and myosin V
    • Benashski, S. E., Harrison, A., Patel-King, R. S. and King, S. M. (1997). Dimerization of the highly conserved light chain shared by dynein and myosin V. J. Biol. Chem. 272, 20929-20935.
    • (1997) J. Biol. Chem. , vol.272 , pp. 20929-20935
    • Benashski, S.E.1    Harrison, A.2    Patel-King, R.S.3    King, S.M.4
  • 5
    • 0029914986 scopus 로고    scopus 로고
    • Asymmetric accumulation of Ash 1p in postanaphase nuclei depends on a myosin and restricts yeast mating-type switching to mother cells
    • Bobola, N., Jansen, R. P., Shin, T. H. and Nasmyth, K. (1996) Asymmetric accumulation of Ash 1p in postanaphase nuclei depends on a myosin and restricts yeast mating-type switching to mother cells. Cell 84, 699-709.
    • (1996) Cell , vol.84 , pp. 699-709
    • Bobola, N.1    Jansen, R.P.2    Shin, T.H.3    Nasmyth, K.4
  • 6
    • 0025021497 scopus 로고
    • A monoclonal antibody against kinesin inhibits both anterograde and retrograde fast axonal transport in squid axoplasm
    • Brady, S. T., Pfister, K. K. and Bloom, G. S. (1990). A monoclonal antibody against kinesin inhibits both anterograde and retrograde fast axonal transport in squid axoplasm. Proc. Nat. Acad. Sci. USA 87, 1061-1065.
    • (1990) Proc. Nat. Acad. Sci. USA , vol.87 , pp. 1061-1065
    • Brady, S.T.1    Pfister, K.K.2    Bloom, G.S.3
  • 12
    • 0020575985 scopus 로고
    • The axoplasmic reticulum within myelinated axons is not transported rapidly
    • Ellisman, M. H. and Lindsey, J. D. (1983). The axoplasmic reticulum within myelinated axons is not transported rapidly. Neurocytol 12, 393-411.
    • (1983) Neurocytol , vol.12 , pp. 393-411
    • Ellisman, M.H.1    Lindsey, J.D.2
  • 13
    • 0029151640 scopus 로고
    • Requirement for Drosophila cytoplasmic tropomyosin in oskar mRNA localization
    • Erdelyi, M., Michon, A. M., Guichet, A., Glotzer, J. B. and Ephrussi, A. (1995). Requirement for Drosophila cytoplasmic tropomyosin in oskar mRNA localization. Nature 377, 524-527.
    • (1995) Nature , vol.377 , pp. 524-527
    • Erdelyi, M.1    Michon, A.M.2    Guichet, A.3    Glotzer, J.B.4    Ephrussi, A.5
  • 14
    • 0026642525 scopus 로고
    • Biochemical and immunological characterization of p190-calmodulin complex from vertebrate brain: A novel calmodulin-binding myosin
    • Espindola, F. S., Espreafico, E. M., Coelho, M. V., Martins, A. R., Costa, F. R., Mooseker, M. S. and Larson, R. E. (1992). Biochemical and immunological characterization of p190-calmodulin complex from vertebrate brain: a novel calmodulin-binding myosin. J. Cell Biol. 118, 359-368.
    • (1992) J. Cell Biol. , vol.118 , pp. 359-368
    • Espindola, F.S.1    Espreafico, E.M.2    Coelho, M.V.3    Martins, A.R.4    Costa, F.R.5    Mooseker, M.S.6    Larson, R.E.7
  • 16
    • 0027068050 scopus 로고
    • Primary structure and cellular localization of chicken brain myosin-V (p190), an unconventional myosin with calmodulin light chains
    • Espreafico, E. M., Cheney, R. E., Matteoli, M., Nascimento, A. A., De Camilli, P. V., Larson, R. E. and Mooseker, M. S. (1992). Primary structure and cellular localization of chicken brain myosin-V (p190), an unconventional myosin with calmodulin light chains. J Cell Biol. 119, 1541-1557.
    • (1992) J Cell Biol. , vol.119 , pp. 1541-1557
    • Espreafico, E.M.1    Cheney, R.E.2    Matteoli, M.3    Nascimento, A.A.4    De Camilli, P.V.5    Larson, R.E.6    Mooseker, M.S.7
  • 17
    • 0031049775 scopus 로고    scopus 로고
    • Subcellular localization of myosin V in nerve growth cones and outgrowth from dilute-lethal neurons
    • Evans, L. L., Hammer, J. and Bridgman, P. C. (1997). Subcellular localization of myosin V in nerve growth cones and outgrowth from dilute-lethal neurons. J. Cell Sci. 110, 439-449.
    • (1997) J. Cell Sci. , vol.110 , pp. 439-449
    • Evans, L.L.1    Hammer, J.2    Bridgman, P.C.3
  • 18
    • 0031819385 scopus 로고    scopus 로고
    • Vesicle-associated brain myosin-V can be activated to catalyze actin-based transport
    • Evans, L. L., Lee, A. J., Bridgemen, P. C. and Mooseker, M. S. (1998). Vesicle-associated brain myosin-V can be activated to catalyze actin-based transport. J. Cell Sci. 111, 2055-2066.
    • (1998) J. Cell Sci. , vol.111 , pp. 2055-2066
    • Evans, L.L.1    Lee, A.J.2    Bridgemen, P.C.3    Mooseker, M.S.4
  • 19
    • 0028985886 scopus 로고
    • Pathway of processive ATP hydrolysis by kinesin
    • Gilbert, S. P., Webb, M. R., Brune, M. and Johnson, K. A. (1995). Pathway of processive ATP hydrolysis by kinesin. Nature 373, 671-676.
    • (1995) Nature , vol.373 , pp. 671-676
    • Gilbert, S.P.1    Webb, M.R.2    Brune, M.3    Johnson, K.A.4
  • 20
    • 0028902506 scopus 로고
    • The role of Myo2, a yeast class V myosin, in vesicular transport
    • Govindan, B., Bowser, R. and Novick, P. (1995). The role of Myo2, a yeast class V myosin, in vesicular transport. J. Cell Biol. 128, 1055-1068.
    • (1995) J. Cell Biol. , vol.128 , pp. 1055-1068
    • Govindan, B.1    Bowser, R.2    Novick, P.3
  • 21
    • 0028216280 scopus 로고
    • Identification of MYO4, a second class V myosin gene in yeast
    • Haarer, B. K., Petzold, A., Lillie, S. H. and Brown, S. S. (1994). Identification of MYO4, a second class V myosin gene in yeast. J. Cell Sci., 107, 1055-1064.
    • (1994) J. Cell Sci. , vol.107 , pp. 1055-1064
    • Haarer, B.K.1    Petzold, A.2    Lillie, S.H.3    Brown, S.S.4
  • 22
    • 0029156511 scopus 로고
    • Highly processive microtubule-stimulated ATP hydrolysis by dimeric kinesin head domains
    • Hackney, D. D. (1995). Highly processive microtubule-stimulated ATP hydrolysis by dimeric kinesin head domains. Nature 377, 448-450.
    • (1995) Nature , vol.377 , pp. 448-450
    • Hackney, D.D.1
  • 23
    • 0030470182 scopus 로고    scopus 로고
    • Actin and myosin function in directed vacuole movement during cell division in Saccharomyces cerevisiae
    • Hill, K. L., Catlett, N. L. and Weisman, L. S. (1996). Actin and myosin function in directed vacuole movement during cell division in Saccharomyces cerevisiae. J. Cell Biol. 135, 1535-1549.
    • (1996) J. Cell Biol. , vol.135 , pp. 1535-1549
    • Hill, K.L.1    Catlett, N.L.2    Weisman, L.S.3
  • 24
    • 0018896912 scopus 로고
    • The neuroplasmic network in Loligo and Hermissenda neurons
    • Hodge, A. J. and Adelman, W. J. Jr (1980). The neuroplasmic network in Loligo and Hermissenda neurons. J. Ultrastruct. Res. 70, 220-241.
    • (1980) J. Ultrastruct. Res. , vol.70 , pp. 220-241
    • Hodge, A.J.1    Adelman Jr., W.J.2
  • 25
    • 0030773824 scopus 로고    scopus 로고
    • Molecular motors: Structural adaptations to cellular functions
    • Howard, J. (1997). Molecular motors: structural adaptations to cellular functions. Nature 389, 561-567.
    • (1997) Nature , vol.389 , pp. 561-567
    • Howard, J.1
  • 27
    • 0025801365 scopus 로고
    • The Saccharomyces cerevisiae MYO2 gene encodes an essential myosin for vectorial transport of vesicles
    • Johnston, G. C., Prendergast, J. A. and Singer, R. A. (1991) The Saccharomyces cerevisiae MYO2 gene encodes an essential myosin for vectorial transport of vesicles. J. Cell Biol. 113, 539-551.
    • (1991) J. Cell Biol. , vol.113 , pp. 539-551
    • Johnston, G.C.1    Prendergast, J.A.2    Singer, R.A.3
  • 28
    • 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, 722-725.
    • (1992) Nature , vol.356 , pp. 722-725
    • Kuznetsov, S.A.1    Langford, G.M.2    Weiss, D.G.3
  • 30
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 31
    • 0028093376 scopus 로고
    • Movement of axoplasmic organelles on actin filaments assembled on acrosomal processes: Evidence for a barbed-end-directed organelle motor
    • Langford, G. M., Kuznetsov, S. A., Johnson, D., Cohen, D. L. and Weiss, D. G. (1994). Movement of axoplasmic organelles on actin filaments assembled on acrosomal processes: evidence for a barbed-end-directed organelle motor. J. Cell Sci. 107, 2291-2298.
    • (1994) J. Cell Sci. , vol.107 , pp. 2291-2298
    • Langford, G.M.1    Kuznetsov, S.A.2    Johnson, D.3    Cohen, D.L.4    Weiss, D.G.5
  • 32
    • 0028942256 scopus 로고
    • Actin- and microtubule-dependent organelle motors: Interrelationships between the two motility systems
    • Langford, G. M. (1995). Actin-and microtubule-dependent organelle motors: interrelationships between the two motility systems. Curr. Opin. Cell Biol. 7, 82-88.
    • (1995) Curr. Opin. Cell Biol. , vol.7 , pp. 82-88
    • Langford, G.M.1
  • 33
    • 0032212657 scopus 로고    scopus 로고
    • Myosin V in the brain: Mutations lead to neurological defects
    • in press
    • Langford, G. M. and Molyneaux, B. J. (1998). Myosin V in the brain: mutations lead to neurological defects. Brain Res. Rev. (in press).
    • (1998) Brain Res. Rev.
    • Langford, G.M.1    Molyneaux, B.J.2
  • 34
    • 0030091263 scopus 로고    scopus 로고
    • Myosin-V: A class of unconventional molecular motors
    • Larson, R. E. (1996). Myosin-V: a class of unconventional molecular motors. Braz. J. Med. Biol. Res. 29, 309-318.
    • (1996) Braz. J. Med. Biol. Res. , vol.29 , pp. 309-318
    • Larson, R.E.1
  • 36
    • 0030875775 scopus 로고    scopus 로고
    • Mating type switching in yeast controlled by asymmetric localization of ASH1 mRNA
    • Long, R. M., Singer, R. H., Meng, X., Gonzalez, I., Nasmyth, K. and Jansen, R. P. (1997). Mating type switching in yeast controlled by asymmetric localization of ASH1 mRNA. Science 277, 383-387.
    • (1997) Science , vol.277 , pp. 383-387
    • Long, R.M.1    Singer, R.H.2    Meng, X.3    Gonzalez, I.4    Nasmyth, K.5    Jansen, R.P.6
  • 37
    • 0028141914 scopus 로고
    • ERcalcistorin/protein disulfide isomerase (PDI). Sequence determination and expression of a cDNA clone encoding a calcium storage protein with PDI activity from endoplasmic reticulum of the sea urchin egg
    • Lucero, H. A, Lebeche, D. and kaminer, B. (1994). ERcalcistorin/protein disulfide isomerase (PDI). Sequence determination and expression of a cDNA clone encoding a calcium storage protein with PDI activity from endoplasmic reticulum of the sea urchin egg. J. Biol. Chem. 269, 23112-23119.
    • (1994) J. Biol. Chem. , vol.269 , pp. 23112-23119
    • Lucero, H.A.1    Lebeche, D.2    Kaminer, B.3
  • 38
    • 0032540349 scopus 로고    scopus 로고
    • ERcalcistorin/protein disulfide isomerase acts as a calcium storage protein in the endoplasmic reticulum of a living cell
    • Lucero, H. A., Lebeche, D. and Kaminer, B. (1998). ERcalcistorin/protein disulfide isomerase acts as a calcium storage protein in the endoplasmic reticulum of a living cell. J. Biol. Chem. 273, 9857-9863.
    • (1998) J. Biol. Chem. , vol.273 , pp. 9857-9863
    • Lucero, H.A.1    Lebeche, D.2    Kaminer, B.3
  • 39
    • 0018817283 scopus 로고
    • Preparation of Fab fragments from IgGs of different animal species
    • Mage, M. G. (1980). Preparation of Fab fragments from IgGs of different animal species. Meth. Enzymol. 70, 142-150.
    • (1980) Meth. Enzymol. , vol.70 , pp. 142-150
    • Mage, M.G.1
  • 40
    • 0025967015 scopus 로고
    • Novel myosin heavy chain encoded by murine dilute coat color locus
    • Mercer, J. A., Seperack, P. K., Strobel, M. C., Copeland, N. G. and Jenkins, N. A. (1991). Novel myosin heavy chain encoded by murine dilute coat color locus. Nature 349, 709-713.
    • (1991) Nature , vol.349 , pp. 709-713
    • Mercer, J.A.1    Seperack, P.K.2    Strobel, M.C.3    Copeland, N.G.4    Jenkins, N.A.5
  • 41
    • 0032559349 scopus 로고    scopus 로고
    • Unconventional myosins in cell movement, membrane traffic, and signal transduction
    • Mermall, V., Post, P. L. and Mooseker, M. S. (1998). Unconventional myosins in cell movement, membrane traffic, and signal transduction. Science 279, 527-533.
    • (1998) Science , vol.279 , pp. 527-533
    • Mermall, V.1    Post, P.L.2    Mooseker, M.S.3
  • 42
    • 0020670628 scopus 로고
    • Neurofilamentous network and filamenouus matrix preserved and isolated by different techniques from squid giant axon
    • Metuzals, J., Hodge, A. J,. Lasek, R. J. and Kaiserman-Abramof, I. R. (1983). Neurofilamentous network and filamenouus matrix preserved and isolated by different techniques from squid giant axon. Cell Tissue Res. 228, 415-432.
    • (1983) Cell Tissue Res. , vol.228 , pp. 415-432
    • Metuzals, J.1    Hodge, A.J.2    Lasek, R.J.3    Kaiserman-Abramof, I.R.4
  • 43
    • 0030886832 scopus 로고    scopus 로고
    • Organization of the cortical endoplasmic reticulum in the squid giant axon
    • Metuzals, J., Chang, D., Hammar, K. and Reese, T. S. (1997). Organization of the cortical endoplasmic reticulum in the squid giant axon. J. Neurocytol. 26, 529-539.
    • (1997) J. Neurocytol. , vol.26 , pp. 529-539
    • Metuzals, J.1    Chang, D.2    Hammar, K.3    Reese, T.S.4
  • 45
    • 0031258017 scopus 로고    scopus 로고
    • Characterization of antibodies to the head and tail domains of squid brain myosin V
    • Molyneaux, B. J. and Langford, G. M. (1997). Characterization of antibodies to the head and tail domains of squid brain myosin V. Biol. Bull. 193, 222-223.
    • (1997) Biol. Bull. , vol.193 , pp. 222-223
    • Molyneaux, B.J.1    Langford, G.M.2
  • 46
    • 77957091724 scopus 로고
    • Rapid separation of proteins and peptides using conventional silica-based supports: Identification of 2-D gel proteins following in-gel proteolysis
    • (ed. J. W. Crabb). Academic Press, San Diego
    • Moritz, R. L., Eddes, J., Hong, J., Reid, G. E. and Simpson, R. J. (1995). Rapid separation of proteins and peptides using conventional silica-based supports: identification of 2-D gel proteins following in-gel proteolysis. In Techniques in Protein Chemistry VI (ed. J. W. Crabb). pp 311-319. Academic Press, San Diego.
    • (1995) Techniques in Protein Chemistry VI , pp. 311-319
    • Moritz, R.L.1    Eddes, J.2    Hong, J.3    Reid, G.E.4    Simpson, R.J.5
  • 47
    • 0020026984 scopus 로고
    • Stable polymers of the axonal cytoskeleton: The axoplasmic ghost
    • Morris, J. R. and Lasek, R. J. (1982). Stable polymers of the axonal cytoskeleton: the axoplasmic ghost. J. Cell Biol. 92, 192-198.
    • (1982) J. Cell Biol. , vol.92 , pp. 192-198
    • Morris, J.R.1    Lasek, R.J.2
  • 48
    • 0021244966 scopus 로고
    • Monomer-polymer equilibria in the axon: Direct measurement of tubulin and actin as polymer and monomer in axoplasm
    • Morris, J. R. and Lasek, R. J. (1984). Monomer-polymer equilibria in the axon: direct measurement of tubulin and actin as polymer and monomer in axoplasm. J. Cell Biol. 98, 2064-2076.
    • (1984) J. Cell Biol. , vol.98 , pp. 2064-2076
    • Morris, J.R.1    Lasek, R.J.2
  • 49
    • 0032498607 scopus 로고    scopus 로고
    • Visualization of the dynamics of synaptic vesicle and plasma membrane proteins in living axons
    • Nakata, T., Terada, S. and Hirokawa, N. (1998). Visualization of the dynamics of synaptic vesicle and plasma membrane proteins in living axons. J. Cell Biol. 140, 659-674.
    • (1998) J. Cell Biol. , vol.140 , pp. 659-674
    • Nakata, T.1    Terada, S.2    Hirokawa, N.3
  • 51
    • 0030822624 scopus 로고    scopus 로고
    • Subcellular localization of myosin-V in the B16 melanoma cells, a wild-type cell line fron the dilute gene
    • Nascimento, A. A. C., Amaral, R. G., Bizario, J. C. S., Larson, R. E. and Espreafico, E. M. (1997). Subcellular localization of myosin-V in the B16 melanoma cells, a wild-type cell line fron the dilute gene. Mol. Biol. Cell 8, 1971-1978.
    • (1997) Mol. Biol. Cell , vol.8 , pp. 1971-1978
    • Nascimento, A.A.C.1    Amaral, R.G.2    Bizario, J.C.S.3    Larson, R.E.4    Espreafico, E.M.5
  • 52
    • 0029987840 scopus 로고    scopus 로고
    • Overlapping functions of myosin-I isoforms?
    • Ostap, E. M. and Pollard, T. D. (1996). Overlapping functions of myosin-I isoforms? J. Cell Biol. 133, 221-224.
    • (1996) J. Cell Biol. , vol.133 , pp. 221-224
    • Ostap, E.M.1    Pollard, T.D.2
  • 53
    • 0020146091 scopus 로고
    • Mechanism of K+-induced actin assembly
    • Pardee, J. D. and Spudich, J. A. (1982). Mechanism of K+-induced actin assembly. J. Cell Biol. 93, 648-654.
    • (1982) J. Cell Biol. , vol.93 , pp. 648-654
    • Pardee, J.D.1    Spudich, J.A.2
  • 54
    • 0029035839 scopus 로고
    • AF-6/cno: Neither a kinesin nor a myosin, but a bit of both
    • Ponting, C. P. (1995). AF-6/cno: neither a kinesin nor a myosin, but a bit of both. Trends Biochem. Sci. 20, 265-266.
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 265-266
    • Ponting, C.P.1
  • 56
    • 0030921711 scopus 로고    scopus 로고
    • 2+-dependent interaction with the synaptobrevin-synaptophysin complex
    • 2+-dependent interaction with the synaptobrevin-synaptophysin complex. J. Cell Biol. 137, 1589-1601.
    • (1997) J. Cell Biol. , vol.137 , pp. 1589-1601
    • Prekeris, R.1    Terrian, D.M.2
  • 57
    • 0029955902 scopus 로고    scopus 로고
    • Cultured melanocytes from dilute mutant mice exhibit dendritic morphology and altered melanosome distribution
    • Provance, D. W. Jr, Wei, M., Ipe, N. and Mercer, J. A. (1996). Cultured melanocytes from dilute mutant mice exhibit dendritic morphology and altered melanosome distribution. Proc. Nat. Acad. Sci. USA 93, 14554-14558.
    • (1996) Proc. Nat. Acad. Sci. USA , vol.93 , pp. 14554-14558
    • Provance Jr., D.W.1    Wei, M.2    Ipe, N.3    Mercer, J.A.4
  • 58
    • 0031013414 scopus 로고    scopus 로고
    • Targeting of chitin synthase 3 to polarized growth sites in yeast requires Chs5p and Myo2p
    • Santos, B. and Snyder, M. (1997). Targeting of chitin synthase 3 to polarized growth sites in yeast requires Chs5p and Myo2p. J. Cell Biol. 136, 95-110.
    • (1997) J. Cell Biol. , vol.136 , pp. 95-110
    • Santos, B.1    Snyder, M.2
  • 59
    • 0027078786 scopus 로고
    • Endolasmic reticulum: A dynamic patchwork of spccialized subregions
    • Sitia, R. and Meldolesi, J. (1992). Endolasmic reticulum: a dynamic patchwork of spccialized subregions. Mol. Biol. Cell 3, 1067-1072.
    • (1992) Mol. Biol. Cell , vol.3 , pp. 1067-1072
    • Sitia, R.1    Meldolesi, J.2
  • 60
    • 0030295320 scopus 로고    scopus 로고
    • Immunogold localization of the intermediate chain within the protein complex of cytoplasmic dynein
    • Steffen, W., Hodgkinson, J. L. and Wiche, G. (1996). Immunogold localization of the intermediate chain within the protein complex of cytoplasmic dynein. J. Struct. Biol. 117, 227-235.
    • (1996) J. Struct. Biol. , vol.117 , pp. 227-235
    • Steffen, W.1    Hodgkinson, J.L.2    Wiche, G.3
  • 61
    • 0030473355 scopus 로고    scopus 로고
    • Localization of myosin on tubulovesicular organelles in the squid giant axon by immuno-EM
    • Tabb, J. S., Harmon, K. O., DePina, A. S. and Langford, G. M. (1996). Localization of myosin on tubulovesicular organelles in the squid giant axon by immuno-EM. Biol. Bull. 191, 274-275.
    • (1996) Biol. Bull. , vol.191 , pp. 274-275
    • Tabb, J.S.1    Harmon, K.O.2    DePina, A.S.3    Langford, G.M.4
  • 63
    • 0030930836 scopus 로고    scopus 로고
    • Actin-dependent localization of an RNA encoding a cell-fate determinant in yeast
    • Takizawa, P. A., Sil, A., Swedlow, J. R., Herskowitz, I. and Vale, R. D. (1997). Actin-dependent localization of an RNA encoding a cell-fate determinant in yeast. Nature 389, 90-93.
    • (1997) Nature , vol.389 , pp. 90-93
    • Takizawa, P.A.1    Sil, A.2    Swedlow, J.R.3    Herskowitz, I.4    Vale, R.D.5
  • 64
    • 0027736954 scopus 로고
    • Imaging endoplasmic reticulum in living sea urchin eggs
    • Terasaki, M. and Jaffe, L. A. (1993). Imaging endoplasmic reticulum in living sea urchin eggs. Meth. Cell Biol. 38, 211-220.
    • (1993) Meth. Cell Biol. , vol.38 , pp. 211-220
    • Terasaki, M.1    Jaffe, L.A.2
  • 65
    • 0021748350 scopus 로고
    • Localization of endoplasmic reticulum in living and glutaraldehyde-fixed cells with fluorescent dyes
    • Terasaki, M., Song, J., Wong, J. R., Weiss, M. J. and Chen, L. B. (1984). Localization of endoplasmic reticulum in living and glutaraldehyde-fixed cells with fluorescent dyes. Cell 38, 101-108.
    • (1984) Cell , vol.38 , pp. 101-108
    • Terasaki, M.1    Song, J.2    Wong, J.R.3    Weiss, M.J.4    Chen, L.B.5
  • 66
    • 0031106858 scopus 로고    scopus 로고
    • Unconventional myosins: New frontiers in actin-based motors
    • Titus, M. A. (1997). Unconventional myosins: new frontiers in actin-based motors. Trends Cell Biol 7, 119-123.
    • (1997) Trends Cell Biol , vol.7 , pp. 119-123
    • Titus, M.A.1
  • 67
    • 0018869198 scopus 로고
    • The movement of membranous organelles in axons. Electron microscopic identification of anterogradely and retrogradely transported organelles
    • Tsukita, S. and Ishikawa, H. (1980). The movement of membranous organelles in axons. Electron microscopic identification of anterogradely and retrogradely transported organelles. J. Cell Biol 84, 513-530.
    • (1980) J. Cell Biol , vol.84 , pp. 513-530
    • Tsukita, S.1    Ishikawa, H.2
  • 68
    • 0029879228 scopus 로고    scopus 로고
    • Direct observation of single kinesin molecules moving along microtubules
    • Vale, R. D., Fanatsu, 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    Fanatsu, T.2    Pierce, D.W.3    Romberg, L.4    Harada, Y.5    Yanagida, T.6
  • 69
    • 0030267349 scopus 로고    scopus 로고
    • Switches, latches, and amplifiers: Common themes of G proteins and molecular motors
    • Vale, R. D. (1996). Switches, latches, and amplifiers: common themes of G proteins and molecular motors. J. Cell Biol. 135, 291-302.
    • (1996) J. Cell Biol. , vol.135 , pp. 291-302
    • Vale, R.D.1
  • 70
    • 0030930514 scopus 로고    scopus 로고
    • Sec2p mediates nucleotide exchange on Sec4p and is involved in polarized delivery of post-Golgi vesicles
    • Walch-Solimena, C., Collins, R. N. and Novick, P. J. (1997). Sec2p mediates nucleotide exchange on Sec4p and is involved in polarized delivery of post-Golgi vesicles. J. Cell Biol. 137, 1495-1509.
    • (1997) J. Cell Biol. , vol.137 , pp. 1495-1509
    • Walch-Solimena, C.1    Collins, R.N.2    Novick, P.J.3
  • 71
    • 0029750192 scopus 로고    scopus 로고
    • Function of myosin-V in filopodial extension of neuronal growth cones
    • Wang, F. S., Wolenski, J. S., Cheney, R. E., Mooseker, M. S. and Jay, D. G. (1996). Function of myosin-V in filopodial extension of neuronal growth cones. Science 273, 660-663.
    • (1996) Science , vol.273 , pp. 660-663
    • Wang, F.S.1    Wolenski, J.S.2    Cheney, R.E.3    Mooseker, M.S.4    Jay, D.G.5
  • 74
    • 0027917985 scopus 로고
    • In vitro motilities of the unconventional myosins, brush border myosin-I, and chick brain myosin-V exhibit assay-dependent differences in velocity
    • Wolenski, J. S., Cheney, R. E., Forscher, P. and Mooseker, M. S. (1993). In vitro motilities of the unconventional myosins, brush border myosin-I, and chick brain myosin-V exhibit assay-dependent differences in velocity. J. Exp. Zool. 267, 33-39.
    • (1993) J. Exp. Zool. , vol.267 , pp. 33-39
    • Wolenski, J.S.1    Cheney, R.E.2    Forscher, P.3    Mooseker, M.S.4
  • 75
    • 0028930479 scopus 로고
    • In vitro motility of immunoadsorbed brain myosin-V using a Limulus acrosomal process and optical tweezer-based assay
    • Wolenski, J. S., Cheney, R. E., Mooseker, M. S. and Forscher, P. (1995). In vitro motility of immunoadsorbed brain myosin-V using a Limulus acrosomal process and optical tweezer-based assay. J. Cell Sci. 108, 1489-1496.
    • (1995) J. Cell Sci. , vol.108 , pp. 1489-1496
    • Wolenski, J.S.1    Cheney, R.E.2    Mooseker, M.S.3    Forscher, P.4
  • 76
    • 0030964893 scopus 로고    scopus 로고
    • Myosin V associates with melanosomes in mouse melanocytes: Evidence that myosin V is an organelle motor
    • Wu, X., Bowers, B., Wei, Q., Kocher, B. and Hammer, J. A. III (1997). Myosin V associates with melanosomes in mouse melanocytes: evidence that myosin V is an organelle motor. J. Cell Sci. 110, 847-859.
    • (1997) J. Cell Sci. , vol.110 , pp. 847-859
    • Wu, X.1    Bowers, B.2    Wei, Q.3    Kocher, B.4    Hammer III, J.A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.