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Volumn 210, Issue 3, 2006, Pages 318-333

Squid (Loligo pealei) giant fiber system: A model for studying neurodegeneration and dementia?

Author keywords

[No Author keywords available]

Indexed keywords

CYTOSKELETON PROTEIN; NEUROFILAMENT PROTEIN; PHOSPHATASE; PHOSPHOTRANSFERASE;

EID: 33745700919     PISSN: 00063185     EISSN: None     Source Type: Journal    
DOI: 10.2307/4134568     Document Type: Review
Times cited : (18)

References (90)
  • 2
    • 0343435077 scopus 로고
    • Electrophysiology and biophysics of the squid giant axon
    • D.L. Gilbert, W.J. Adelman, and J.M. Arnold eds. Plenum Press, New York
    • Adelman, W. J., and D. L. Gilbert. 1990. Electrophysiology and biophysics of the squid giant axon, Pp. 93-132 in Squid as Experimental Animals, D.L. Gilbert, W.J. Adelman, and J.M. Arnold eds. Plenum Press, New York.
    • (1990) Squid As Experimental Animals , pp. 93-132
    • Adelman, W.J.1    Gilbert, D.L.2
  • 3
    • 0037390202 scopus 로고    scopus 로고
    • Neurofilaments and neurological disease
    • Al-Chalabi, A., and C. C. J. Miller. 2003. Neurofilaments and neurological disease. BioEssays 25: 346-355.
    • (2003) BioEssays , vol.25 , pp. 346-355
    • Al-Chalabi, A.1    Miller, C.C.J.2
  • 4
    • 0023761334 scopus 로고
    • Methods to distinguish various types of protein phosphatase activity
    • Brautigan, D. L., and C. L. Shriner. 1988. Methods to distinguish various types of protein phosphatase activity. Methods Enzymol. 159: 339-346.
    • (1988) Methods Enzymol. , vol.159 , pp. 339-346
    • Brautigan, D.L.1    Shriner, C.L.2
  • 5
    • 0023446949 scopus 로고
    • p13sucl acts in the fission yeast cell division cycle as a component of the p34cdc2 protein kinase
    • Brizuela, L., G. Draetta, and D. Beach. 1987. p13sucl acts in the fission yeast cell division cycle as a component of the p34cdc2 protein kinase. EMBO J. 6: 3507-3514.
    • (1987) EMBO J. , vol.6 , pp. 3507-3514
    • Brizuela, L.1    Draetta, G.2    Beach, D.3
  • 6
    • 0001370783 scopus 로고
    • The cytoskeleton of the squid giant axon
    • D.L. Gilbert, W. J. Adelman, and J. M. Arnold, eds. Plenum Press, New York
    • Brown, A., and R. J. Lasek. 1990. The cytoskeleton of the squid giant axon, Pp. 235-302 in Squid as Experimental Animals, D.L. Gilbert, W. J. Adelman, and J. M. Arnold, eds. Plenum Press, New York.
    • (1990) Squid As Experimental Animals , pp. 235-302
    • Brown, A.1    Lasek, R.J.2
  • 7
    • 3943102116 scopus 로고    scopus 로고
    • Unraveling the mechanisms involved in motor neuron degeneration in ALS
    • Bruijn, L. I., T. M. Miller, and D. W. Cleveland. 2004. Unraveling the mechanisms involved in motor neuron degeneration in ALS. Annu. Rev. Neurosci. 27: 723-749.
    • (2004) Annu. Rev. Neurosci. , vol.27 , pp. 723-749
    • Bruijn, L.I.1    Miller, T.M.2    Cleveland, D.W.3
  • 9
    • 15244352198 scopus 로고    scopus 로고
    • Emerging role for ERK as a key regulator of neuronal apoptosis
    • Cheung, E. C., and R. S. Slack. 2004. Emerging role for ERK as a key regulator of neuronal apoptosis. Sci STKE 2004: PE45.
    • (2004) Sci STKE , vol.2004
    • Cheung, E.C.1    Slack, R.S.2
  • 10
    • 0141642203 scopus 로고    scopus 로고
    • Wild-type nonneuronal cells extend survival of SOD1 mutant motor neurons in ALS mice
    • Clement, A. M., M. D. Nguyen, E. A. Roberts, M. L. Garcia, S. Boillee, et al. 2003. Wild-type nonneuronal cells extend survival of SOD1 mutant motor neurons in ALS mice. Science 302: 113-117.
    • (2003) Science , vol.302 , pp. 113-117
    • Clement, A.M.1    Nguyen, M.D.2    Roberts, E.A.3    Garcia, M.L.4    Boillee, S.5
  • 11
    • 0034383949 scopus 로고    scopus 로고
    • The regulation of protein function by multisite phosphorylation - A 25-year update
    • Cohen, P. 2000. The regulation of protein function by multisite phosphorylation-a 25-year update. Trends Biochem. Sci. 25: 596-601.
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 596-601
    • Cohen, P.1
  • 12
    • 0023372926 scopus 로고
    • Biochemical and immunocytochemical characterization and distribution of phosphorylated and nonphosphorylated subunits of neurofilaments in squid giant axon and stellate ganglion
    • Cohen, R. S., H. C. Pant, S. House, and H. Gainer. 1987. Biochemical and immunocytochemical characterization and distribution of phosphorylated and nonphosphorylated subunits of neurofilaments in squid giant axon and stellate ganglion. J. Neurosci. 7: 2056-2074.
    • (1987) J. Neurosci. , vol.7 , pp. 2056-2074
    • Cohen, R.S.1    Pant, H.C.2    House, S.3    Gainer, H.4
  • 13
    • 0032483016 scopus 로고    scopus 로고
    • Protective effect of neurofilament heavy gene overexpression in motor neuron disease induced by mutant superoxide dismutase
    • Couillard-Despres, S., Q. Zhu, P. C. Wong, D. L. Price, D. W. Cleveland, and J. P. Julien. 1998. Protective effect of neurofilament heavy gene overexpression in motor neuron disease induced by mutant superoxide dismutase. Proc. Natl. Acad. Sci. USA 95: 9626-9630.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 9626-9630
    • Couillard-Despres, S.1    Zhu, Q.2    Wong, P.C.3    Price, D.L.4    Cleveland, D.W.5    Julien, J.P.6
  • 14
    • 0026580004 scopus 로고
    • Local modulation of neurofilament phosphorylation, axonal caliber, and slow axonal transport by myelinating Schwann cells
    • de Waegh, S. M., V. M. Lee, and S. T. Brady. 1992. Local modulation of neurofilament phosphorylation, axonal caliber, and slow axonal transport by myelinating Schwann cells. Cell 68: 451-463.
    • (1992) Cell , vol.68 , pp. 451-463
    • De Waegh, S.M.1    Lee, V.M.2    Brady, S.T.3
  • 15
    • 0026606341 scopus 로고
    • Association of cyclic-AMP-dependent protein kinase with neurofilaments
    • Dosemeci, A., and H. C. Pant. 1992. Association of cyclic-AMP-dependent protein kinase with neurofilaments. Biochem. J. 282: 477-481.
    • (1992) Biochem. J. , vol.282 , pp. 477-481
    • Dosemeci, A.1    Pant, H.C.2
  • 16
    • 0025029764 scopus 로고
    • Characterization of neurofilament-associated protein kinase activities from bovine spinal cord
    • Dosemeci, A., C. C. Floyd, and H. C. Pant. 1990. Characterization of neurofilament-associated protein kinase activities from bovine spinal cord. Cell Mol. Neurobiol. 10: 369-382.
    • (1990) Cell Mol. Neurobiol. , vol.10 , pp. 369-382
    • Dosemeci, A.1    Floyd, C.C.2    Pant, H.C.3
  • 17
    • 0023658309 scopus 로고
    • Identification of p34 and p13 human homologues of the cell cycle regulators of fission yeast encoded by cdc2 and sucl
    • Draetta, G., L. Brizuela, J. Potashkin, and D. Beach. 1987. Identification of p34 and p13 human homologues of the cell cycle regulators of fission yeast encoded by cdc2 and sucl. Cell 50: 319-325.
    • (1987) Cell , vol.50 , pp. 319-325
    • Draetta, G.1    Brizuela, L.2    Potashkin, J.3    Beach, D.4
  • 18
    • 0032482231 scopus 로고    scopus 로고
    • Absence of the mid-sized neurofilament subunit decreases axonal calibers, levels of light neurofilament (NF-L), and neurofilament content
    • Elder, G. A., V. L. Friedrich, Jr., P. Bosco, C. Kang, A. Gourov, P. H. Tu, V. M. Lee, and R. A. Lazzarini. 1998. Absence of the mid-sized neurofilament subunit decreases axonal calibers, levels of light neurofilament (NF-L), and neurofilament content. J. Cell Biol. 141: 727-739.
    • (1998) J. Cell Biol. , vol.141 , pp. 727-739
    • Elder, G.A.1    Friedrich Jr., V.L.2    Bosco, P.3    Kang, C.4    Gourov, A.5    Tu, P.H.6    Lee, V.M.7    Lazzarini, R.A.8
  • 19
    • 0028598882 scopus 로고
    • Tyrosine- versus serine-phosphorylation leads to conformational changes in a synthetic tau peptide
    • Fabian, H., L. Otvos, Jr., G. I. Szendrei, E. Lang, and H. H. Manisch. 1994. Tyrosine- versus serine-phosphorylation leads to conformational changes in a synthetic tau peptide. J. Biomol. Struct. Dyn. 12: 573-579.
    • (1994) J. Biomol. Struct. Dyn. , vol.12 , pp. 573-579
    • Fabian, H.1    Otvos Jr., L.2    Szendrei, G.I.3    Lang, E.4    Manisch, H.H.5
  • 20
    • 0030219389 scopus 로고    scopus 로고
    • More on target with protein phosphorylation: Conferring specificity by location
    • Faux, M. C., and J. D. Scott. 1996. More on target with protein phosphorylation: conferring specificity by location. Trends Biol. Sci. 21: 312-315.
    • (1996) Trends Biol. Sci. , vol.21 , pp. 312-315
    • Faux, M.C.1    Scott, J.D.2
  • 21
    • 0029053322 scopus 로고
    • Lesions of the vertical lobe impair visual discrimination learning by observation in Octopus vulgaris
    • Fiorito, G., and R. Chichery. 1995. Lesions of the vertical lobe impair visual discrimination learning by observation in Octopus vulgaris. Neurosci. Lett. 192: 117-120.
    • (1995) Neurosci. Lett. , vol.192 , pp. 117-120
    • Fiorito, G.1    Chichery, R.2
  • 22
    • 0026546002 scopus 로고
    • Observational learning in Octopus vulgaris
    • Fiorito, G., and P. Scotto. 1992. Observational learning in Octopus vulgaris. Science 256: 545-547.
    • (1992) Science , vol.256 , pp. 545-547
    • Fiorito, G.1    Scotto, P.2
  • 23
    • 0025150563 scopus 로고
    • Problem solving ability of Octopus vulgaris Lamarck (Mollusca, Cephalopoda)
    • Fiorito, G., C. von Planta, and P. Scotto. 1990. Problem solving ability of Octopus vulgaris Lamarck (Mollusca, Cephalopoda). Behav. Neural Biol. 53: 217-230.
    • (1990) Behav. Neural Biol. , vol.53 , pp. 217-230
    • Fiorito, G.1    Von Planta, C.2    Scotto, P.3
  • 24
    • 0025906420 scopus 로고
    • Principal neurofilament-associated protein kinase in squid axoplasm is related to casein kinase I
    • Floyd, C. C., P. Grant, P. E. Gallant, and H. C. Pant 1991. Principal neurofilament-associated protein kinase in squid axoplasm is related to casein kinase I. J. Biol. Chem. 266: 4987-4994.
    • (1991) J. Biol. Chem. , vol.266 , pp. 4987-4994
    • Floyd, C.C.1    Grant, P.2    Gallant, P.E.3    Pant, H.C.4
  • 25
    • 0033613238 scopus 로고    scopus 로고
    • Slow transport of unpolymerized tubulin and polymerized neurofilament in the squid giant axon
    • Galbraith, J. A., T. S. Reese, M. L. Schlief, and P. E. Gallant. 1999. Slow transport of unpolymerized tubulin and polymerized neurofilament in the squid giant axon. Proc. Natl. Acad. Sci. USA 96: 11589-11594.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 11589-11594
    • Galbraith, J.A.1    Reese, T.S.2    Schlief, M.L.3    Gallant, P.E.4
  • 26
    • 0031452245 scopus 로고    scopus 로고
    • Study of proline-directed protein kinases involved in phosphorylation of the heavy neurofilament subunit
    • Giasson, B. I., and W. E. Mushynski. 1997. Study of proline-directed protein kinases involved in phosphorylation of the heavy neurofilament subunit. J. Neurosci. 17: 9466-9472.
    • (1997) J. Neurosci. , vol.17 , pp. 9466-9472
    • Giasson, B.I.1    Mushynski, W.E.2
  • 28
    • 0033614777 scopus 로고    scopus 로고
    • Filamentous nerve cell inclusions in neurodegenerative diseases: Tauopathies and alpha-synucleinopathies
    • Goedert, M. 1999. Filamentous nerve cell inclusions in neurodegenerative diseases: tauopathies and alpha-synucleinopathies. Philos. Trans. R. Soc. Lond. B Biol. Sci. 354: 1101-1118.
    • (1999) Philos. Trans. R. Soc. Lond. B Biol. Sci. , vol.354 , pp. 1101-1118
    • Goedert, M.1
  • 29
    • 0025953405 scopus 로고
    • Use of vanadate as protein-phosphotyrosine phosphatase inhibitor
    • Gordon, J. A. 1991. Use of vanadate as protein-phosphotyrosine phosphatase inhibitor. Methods Enzymol. 20: 477-482.
    • (1991) Methods Enzymol. , vol.20 , pp. 477-482
    • Gordon, J.A.1
  • 30
    • 1342281018 scopus 로고    scopus 로고
    • Topographic regulation of phosphorylation in giant neurons of the squid, Loligo pealei: Role of phosphatases
    • Grant, P., and H. C. Pant. 2004. Topographic regulation of phosphorylation in giant neurons of the squid, Loligo pealei: role of phosphatases. J. Neurobiol. 58: 514-528.
    • (2004) J. Neurobiol. , vol.58 , pp. 514-528
    • Grant, P.1    Pant, H.C.2
  • 31
    • 0032976041 scopus 로고    scopus 로고
    • Topographic regulation of cytoskeletal protein phosphorylation by multimeric complexes in the squid giant fiber system
    • Grant, P., M. Diggins, and H. C. Pant. 1999. Topographic regulation of cytoskeletal protein phosphorylation by multimeric complexes in the squid giant fiber system. J. Neurobiol. 40: 89-102.
    • (1999) J. Neurobiol. , vol.40 , pp. 89-102
    • Grant, P.1    Diggins, M.2    Pant, H.C.3
  • 32
    • 0029936770 scopus 로고    scopus 로고
    • Differential cellular phosphorylation of neurofilament heavy side-arms by glycogen synthase kinase-3 and cyclin-dependent kinase-5
    • Guidato, S., L. H. Tsai, J. Woodgett, and C. C. Miller. 1996. Differential cellular phosphorylation of neurofilament heavy side-arms by glycogen synthase kinase-3 and cyclin-dependent kinase-5. J. Neurochem. 66: 1698-1706.
    • (1996) J. Neurochem. , vol.66 , pp. 1698-1706
    • Guidato, S.1    Tsai, L.H.2    Woodgett, J.3    Miller, C.C.4
  • 33
    • 0033841994 scopus 로고    scopus 로고
    • The single neurofilament subunit of the lamprey forms filaments and regulates axonal caliber and neuronal size in vivo
    • Hall, G. F., B. Chu, S. Lee, Y. Liu, and J. Yao. 2000. The single neurofilament subunit of the lamprey forms filaments and regulates axonal caliber and neuronal size in vivo. Cell Motil. Cytoskelet. 46: 166-182.
    • (2000) Cell Motil. Cytoskelet. , vol.46 , pp. 166-182
    • Hall, G.F.1    Chu, B.2    Lee, S.3    Liu, Y.4    Yao, J.5
  • 34
    • 0035139540 scopus 로고    scopus 로고
    • Staging of neurofibrillary degeneration caused by human tau overexpression in a unique cellular model of human tauopathy
    • Hall, G. H., V. M.-Y. Lee, G. Lee, and J. Yao. 2001. Staging of neurofibrillary degeneration caused by human tau overexpression in a unique cellular model of human tauopathy. Am. J. Pathol. 158: 235-246.
    • (2001) Am. J. Pathol. , vol.158 , pp. 235-246
    • Hall, G.H.1    Lee, V.M.-Y.2    Lee, G.3    Yao, J.4
  • 35
    • 0025280187 scopus 로고
    • Molecular architecture of the neurofilament. II. Reassembly process of neurofilament L protein in vitro
    • Hisanaga, S., and N. Hirokawa. 1990. Molecular architecture of the neurofilament. II. Reassembly process of neurofilament L protein in vitro. J. Mol. Biol. 211: 871-882.
    • (1990) J. Mol. Biol. , vol.211 , pp. 871-882
    • Hisanaga, S.1    Hirokawa, N.2
  • 36
    • 0018896912 scopus 로고
    • The neuroplasmic network in Loligo and Hermissenda neurons
    • Hodge, A. J., and W. J. Adelman, 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
  • 37
    • 0035116914 scopus 로고    scopus 로고
    • Characterization of the phosphorylation sites of the squid (Loligo pealei) high-molecular-weight neurofilament protein from giant axon axoplasm
    • Jaffe, H., P. Sharma, P. Grant, and H. Pant. 2001. Characterization of the phosphorylation sites of the squid (Loligo pealei) high-molecular-weight neurofilament protein from giant axon axoplasm. J. Neurochem. 76: 1022-1031.
    • (2001) J. Neurochem. , vol.76 , pp. 1022-1031
    • Jaffe, H.1    Sharma, P.2    Grant, P.3    Pant, H.4
  • 38
    • 0029993727 scopus 로고    scopus 로고
    • Active and inactive protein kinases: Structural basis for regulation
    • Johnson, L. N., M. E. Noble, and D. J. Owen. 1996. Active and inactive protein kinases: structural basis for regulation. Cell 85: 149-158.
    • (1996) Cell , vol.85 , pp. 149-158
    • Johnson, L.N.1    Noble, M.E.2    Owen, D.J.3
  • 40
    • 0033810408 scopus 로고    scopus 로고
    • Hypophosphorylated neurofilament subunits undergo axonal transport more rapidly than more extensively phosphorylated subunits in situ
    • Jung, C., J. T. Yabe, S. Lee, and T. B. Shea. 2000a. Hypophosphorylated neurofilament subunits undergo axonal transport more rapidly than more extensively phosphorylated subunits in situ. Cell Motil. Cytoskelet. 47: 120-129.
    • (2000) Cell Motil. Cytoskelet. , vol.47 , pp. 120-129
    • Jung, C.1    Yabe, J.T.2    Lee, S.3    Shea, T.B.4
  • 41
    • 0033977488 scopus 로고    scopus 로고
    • C-terminal phosphorylation of the high molecular weight neurofilament subunit correlates with decreased neurofilament axonal transport velocity
    • Jung, C., J. T. Yabe, and T. B. Shea. 2000b. C-terminal phosphorylation of the high molecular weight neurofilament subunit correlates with decreased neurofilament axonal transport velocity. Brain Res. 856: 12-19.
    • (2000) Brain Res. , vol.856 , pp. 12-19
    • Jung, C.1    Yabe, J.T.2    Shea, T.B.3
  • 42
    • 0034096201 scopus 로고    scopus 로고
    • Protein phosphatases and the regulation of mitogen-activated protein kinase signalling
    • Keyse, S. M. 2000. Protein phosphatases and the regulation of mitogen-activated protein kinase signalling. Curr. Opin. Cell Biol. 12: 186-192.
    • (2000) Curr. Opin. Cell Biol. , vol.12 , pp. 186-192
    • Keyse, S.M.1
  • 43
    • 0029887701 scopus 로고    scopus 로고
    • Coordination of three signaling enzymes by AKAP79, a mammalian scaffold protein
    • Klauck, T. M., M. C. Faux, K. Labudda, L. K. Langeberg, S. Jaken, and J. D. Scott. 1996. Coordination of three signaling enzymes by AKAP79, a mammalian scaffold protein. Science 271: 1589-1592.
    • (1996) Science , vol.271 , pp. 1589-1592
    • Klauck, T.M.1    Faux, M.C.2    Labudda, K.3    Langeberg, L.K.4    Jaken, S.5    Scott, J.D.6
  • 44
    • 10944273982 scopus 로고    scopus 로고
    • Phosphorylated tau and the neurodegenerative foldopathies
    • Kosik, K. S., and H. Shimura. 2005. Phosphorylated tau and the neurodegenerative foldopathies. Biochim. Biophys. Acta 1739: 298-310.
    • (2005) Biochim. Biophys. Acta , vol.1739 , pp. 298-310
    • Kosik, K.S.1    Shimura, H.2
  • 45
    • 0030723127 scopus 로고    scopus 로고
    • Casein kinase 1 is tightly associated with paired-helical filaments isolated from Alzheimer's disease brain
    • Kuret, J., G. S. Johnson, D. Cha, E. R. Christenson, A. J. DeMaggio, and M. F. Hoekstra. 1997. Casein kinase 1 is tightly associated with paired-helical filaments isolated from Alzheimer's disease brain. J. Neurochem. 69: 2506-2515.
    • (1997) J. Neurochem. , vol.69 , pp. 2506-2515
    • Kuret, J.1    Johnson, G.S.2    Cha, D.3    Christenson, E.R.4    DeMaggio, A.J.5    Hoekstra, M.F.6
  • 46
    • 0028894984 scopus 로고
    • Disruption of the cytoskeleton in Alzheimer's disease
    • Lee, V. M. 1995. Disruption of the cytoskeleton in Alzheimer's disease. Curr. Opin. Neurobiol. 5: 663-668.
    • (1995) Curr. Opin. Neurobiol. , vol.5 , pp. 663-668
    • Lee, V.M.1
  • 47
    • 0033563176 scopus 로고    scopus 로고
    • Activation of mitogen-activated protein kinases (Erk1 and Erk2) cascade results in phosphorylation of NF-M tail domains in transfected NIH 3T3 cells
    • Li, B.-S., Veeranna, P. Grant, and H. C. Pant 1999. Activation of mitogen-activated protein kinases (Erk1 and Erk2) cascade results in phosphorylation of NF-M tail domains in transfected NIH 3T3 cells. Eur. J. Biochem. 262: 211-217.
    • (1999) Eur. J. Biochem. , vol.262 , pp. 211-217
    • Li, B.-S.1    Veeranna2    Grant, P.3    Pant, H.C.4
  • 48
    • 0025170679 scopus 로고
    • Visualization of differential neurofilament phosphorylation in the pre- and postsynaptic axoplasm of the squid giant synapse: An electron spectroscopic study
    • Martin, R., K. Schilling, W. Fritz, and A. Giuditta. 1990. Visualization of differential neurofilament phosphorylation in the pre- and postsynaptic axoplasm of the squid giant synapse: an electron spectroscopic study. Neuroscience 37: 553-562.
    • (1990) Neuroscience , vol.37 , pp. 553-562
    • Martin, R.1    Schilling, K.2    Fritz, W.3    Giuditta, A.4
  • 49
    • 0014633643 scopus 로고
    • Spatial patterns of threadlike elements in the axoplasm of the giant nerve fiber of the squid (Loligo pealii L.) as disclosed by differential interference microscopy and by electron microscopy
    • Metuzals, J., and C. S. Izzard. 1969. Spatial patterns of threadlike elements in the axoplasm of the giant nerve fiber of the squid (Loligo pealii L.) as disclosed by differential interference microscopy and by electron microscopy. J. Cell Biol. 43: 456-479.
    • (1969) J. Cell Biol. , vol.43 , pp. 456-479
    • Metuzals, J.1    Izzard, C.S.2
  • 51
    • 3042634127 scopus 로고    scopus 로고
    • A novel CDK5-dependent pathway for regulating GSK3 activity and kinesin-driven motility in neurons
    • Morfini, G., G. Szebenyi, H. Brown, H. C. Pant, G. Pigino, S. DeBoer, U. Beffert, and S. T. Brady. 2004. A novel CDK5-dependent pathway for regulating GSK3 activity and kinesin-driven motility in neurons. EMBO J. 23: 2235-2245.
    • (2004) EMBO J. , vol.23 , pp. 2235-2245
    • Morfini, G.1    Szebenyi, G.2    Brown, H.3    Pant, H.C.4    Pigino, G.5    Deboer, S.6    Beffert, U.7    Brady, S.T.8
  • 52
    • 17744368458 scopus 로고    scopus 로고
    • Deregulation of Cdk5 in a mouse model of ALS: Toxicity alleviated by perikaryal neurofilament inclusions
    • Nguyen, M. D., R. C. Lariviere, and J. P. Julien. 2001. Deregulation of Cdk5 in a mouse model of ALS: toxicity alleviated by perikaryal neurofilament inclusions. Neuron 30: 135-147.
    • (2001) Neuron , vol.30 , pp. 135-147
    • Nguyen, M.D.1    Lariviere, R.C.2    Julien, J.P.3
  • 53
    • 0023148301 scopus 로고
    • Posttranslational modification of neurofilament proteins by phosphate during axoplasmic transport in retinal ganglion cell neurons
    • Nixon, R. A., S. E. Lewis, and C. A. Marotta. 1987. Posttranslational modification of neurofilament proteins by phosphate during axoplasmic transport in retinal ganglion cell neurons. J. Neurosci. 7: 1145-158.
    • (1987) J. Neurosci. , vol.7 , pp. 1145-1158
    • Nixon, R.A.1    Lewis, S.E.2    Marotta, C.A.3
  • 54
    • 0024545532 scopus 로고
    • Early posttranslational modifications of the three neurofilament subunits in mouse retinal ganglion cells: Neuronal sites and time course in relation to subunit polymerization and axonal transport
    • Nixon, R. A., S. E. Lewis, D. Dahl, C. A. Marotta, and U. C. Drager. 1989. Early posttranslational modifications of the three neurofilament subunits in mouse retinal ganglion cells: neuronal sites and time course in relation to subunit polymerization and axonal transport. Brain Res. Mol. Brain Res. 5: 93-108.
    • (1989) Brain Res. Mol. Brain Res. , vol.5 , pp. 93-108
    • Nixon, R.A.1    Lewis, S.E.2    Dahl, D.3    Marotta, C.A.4    Drager, U.C.5
  • 56
    • 0023025498 scopus 로고
    • Characterization of a cyclic nucleotide- and calcium-independent neurofilament protein kinase activity in axoplasm from the squid giant axon
    • Pant, H. C., P. E. Gallant, and H. Gainer. 1986. Characterization of a cyclic nucleotide- and calcium-independent neurofilament protein kinase activity in axoplasm from the squid giant axon. J. Biol. Chem. 261: 2968-2977.
    • (1986) J. Biol. Chem. , vol.261 , pp. 2968-2977
    • Pant, H.C.1    Gallant, P.E.2    Gainer, H.3
  • 57
    • 77957083031 scopus 로고    scopus 로고
    • Regulation of axonal neurofilament phosphorylation
    • Pant, H. C., Veeranna, and P. Grant. 2000. Regulation of axonal neurofilament phosphorylation. Curr. Top. Cell. Regul. 36: 133-150.
    • (2000) Curr. Top. Cell. Regul. , vol.36 , pp. 133-150
    • Pant, H.C.1    Veeranna2    Grant, P.3
  • 58
    • 0033540060 scopus 로고    scopus 로고
    • Conversion of p35 to p25 deregulates Cdk5 activity and promotes neurodegeneration
    • Patrick, G. N., L. Zukerberg, M. Nikolic, S. de la Monte, P. Dikkes, and L. H. Tsai. 1999. Conversion of p35 to p25 deregulates Cdk5 activity and promotes neurodegeneration. Nature 402: 615-622.
    • (1999) Nature , vol.402 , pp. 615-622
    • Patrick, G.N.1    Zukerberg, L.2    Nikolic, M.3    De La Monte, S.4    Dikkes, P.5    Tsai, L.H.6
  • 59
    • 0034474025 scopus 로고    scopus 로고
    • Fast transport of neurofilament protein along microtubules in squid axoplasm
    • Prahlad, V., B. T. Helfand, G. M. Langford, R. D. Vale, and R. D. Goldman. 2000. Fast transport of neurofilament protein along microtubules in squid axoplasm. J. Cell. Sci. 113: 3939-3946.
    • (2000) J. Cell. Sci. , vol.113 , pp. 3939-3946
    • Prahlad, V.1    Helfand, B.T.2    Langford, G.M.3    Vale, R.D.4    Goldman, R.D.5
  • 60
    • 0032487499 scopus 로고    scopus 로고
    • Neurofilament-dependent radial growth of motor axons and axonal organization of neurofilaments does not require the neurofilament heavy subunit (NF-H) or its phosphorylation
    • Rao, M. V., M. K. Houseweart, T. L. Williamson, T. O. Crawford, J. Folmer and D. W. Cleveland. 1998. Neurofilament-dependent radial growth of motor axons and axonal organization of neurofilaments does not require the neurofilament heavy subunit (NF-H) or its phosphorylation J. Cell Biol. 143: 171-181.
    • (1998) J. Cell Biol. , vol.143 , pp. 171-181
    • Rao, M.V.1    Houseweart, M.K.2    Williamson, T.L.3    Crawford, T.O.4    Folmer, J.5    Cleveland, D.W.6
  • 61
    • 0037135978 scopus 로고    scopus 로고
    • Gene replacement in mice reveals that the heavily phosphorylated tail of neurofilament heavy subunit does not affect axonal caliber or the transit of cargoes in slow axonal transport
    • Rao, M. V., M. L. Garcia, Y. Miyazaki, T. Gotow, A. Yuan, S. Mattina, C. M. Ward, N. A. Calcutt, Y. Uchiyama, R. A. Nixon, and D. W. Cleveland. 2002. Gene replacement in mice reveals that the heavily phosphorylated tail of neurofilament heavy subunit does not affect axonal caliber or the transit of cargoes in slow axonal transport. J. Cell Biol. 158: 681-693.
    • (2002) J. Cell Biol. , vol.158 , pp. 681-693
    • Rao, M.V.1    Garcia, M.L.2    Miyazaki, Y.3    Gotow, T.4    Yuan, A.5    Mattina, S.6    Ward, C.M.7    Calcutt, N.A.8    Uchiyama, Y.9    Nixon, R.A.10    Cleveland, D.W.11
  • 62
    • 0026321413 scopus 로고
    • Multisite and hierarchal protein phosphorylation
    • Roach, P. J. 1991. Multisite and hierarchal protein phosphorylation. J. Biol. Chem. 266: 14139-14142.
    • (1991) J. Biol. Chem. , vol.266 , pp. 14139-14142
    • Roach, P.J.1
  • 63
    • 0030898417 scopus 로고    scopus 로고
    • Mitogen-activated protein kinase pathways
    • Robinson, M. J., and M. H. Cobb. 1997. Mitogen-activated protein kinase pathways. Curr. Opin. Cell Biol. 9: 180-186.
    • (1997) Curr. Opin. Cell Biol. , vol.9 , pp. 180-186
    • Robinson, M.J.1    Cobb, M.H.2
  • 65
    • 0034722377 scopus 로고    scopus 로고
    • Local control of neurofilament accumulation during radial growth of myelinating axons in vivo: Selective role of site-specific phosphorylation
    • Sanchez, I., L. Hassinger, R. K. Sihag, D. W. Cleveland, P. Mohan, and R. A. Nixon. 2000. Local control of neurofilament accumulation during radial growth of myelinating axons in vivo: selective role of site-specific phosphorylation. J. Cell Biol. 151: 1013-1024.
    • (2000) J. Cell Biol. , vol.151 , pp. 1013-1024
    • Sanchez, I.1    Hassinger, L.2    Sihag, R.K.3    Cleveland, D.W.4    Mohan, P.5    Nixon, R.A.6
  • 66
  • 68
    • 0024531851 scopus 로고
    • In vivo phosphorylation of distinct domains of the 70-kilodalton neurofilament subunit involves different protein kinases
    • Sihag, R. K., and R. A. Nixon. 1989. In vivo phosphorylation of distinct domains of the 70-kilodalton neurofilament subunit involves different protein kinases. J. Biol. Chem. 264: 457-464.
    • (1989) J. Biol. Chem. , vol.264 , pp. 457-464
    • Sihag, R.K.1    Nixon, R.A.2
  • 69
    • 0025257205 scopus 로고
    • Phosphorylation of the aminoterminal head domain of the middle molecular mass 145-kDa subunit of neurofilaments: Evidence for regulation by second messenger-dependent protein kinases
    • Sihag, R. K., and R. A. Nixon. 1990. Phosphorylation of the aminoterminal head domain of the middle molecular mass 145-kDa subunit of neurofilaments: evidence for regulation by second messenger-dependent protein kinases. J. Biol. Chem. 265: 4166-4171.
    • (1990) J. Biol. Chem. , vol.265 , pp. 4166-4171
    • Sihag, R.K.1    Nixon, R.A.2
  • 70
    • 0025950711 scopus 로고
    • Identification of Ser-55 as a major protein kinase a phosphorylation site on the 70-kDa subunit of neurofilaments: Early turnover during axonal transport
    • Sihag, R. K., and R. A. Nixon. 1991. Identification of Ser-55 as a major protein kinase A phosphorylation site on the 70-kDa subunit of neurofilaments: early turnover during axonal transport. J. Biol. Chem. 266: 18861-18867.
    • (1991) J. Biol. Chem. , vol.266 , pp. 18861-18867
    • Sihag, R.K.1    Nixon, R.A.2
  • 71
    • 0023916538 scopus 로고
    • Phosphorylation of neurofilament proteins by protein kinase C
    • Sihag, R. K., A. Y. Jeng, and R. A. Nixon. 1988. Phosphorylation of neurofilament proteins by protein kinase C. FEBS Lett. 233: 181-185.
    • (1988) FEBS Lett. , vol.233 , pp. 181-185
    • Sihag, R.K.1    Jeng, A.Y.2    Nixon, R.A.3
  • 72
    • 0002918293 scopus 로고
    • Monoclonal antibodies distinguish phosphorylated and non-phosphorylated forms of neurofilaments in situ
    • Sternberger, L. A., and N. H. Sternberger. 1983. Monoclonal antibodies distinguish phosphorylated and non-phosphorylated forms of neurofilaments in situ. Proc. Natl. Acad. Sci. USA 80: 6126-6130.
    • (1983) Proc. Natl. Acad. Sci. USA , vol.80 , pp. 6126-6130
    • Sternberger, L.A.1    Sternberger, N.H.2
  • 75
    • 17544370807 scopus 로고    scopus 로고
    • Phosphorylation of the high molecular weight neurofilament protein (NF-H) by Cdk5 and p35
    • Sun, D., C. L. Leung, and R. K. H. Liem. 1996. Phosphorylation of the high molecular weight neurofilament protein (NF-H) by Cdk5 and p35. J. Biol. Chem. 271: 14245-14251.
    • (1996) J. Biol. Chem. , vol.271 , pp. 14245-14251
    • Sun, D.1    Leung, C.L.2    Liem, R.K.H.3
  • 76
    • 0025787346 scopus 로고
    • Squid low molecular weight neurofilament proteins are a novel class of neurofilament protein. A nuclear lamin-like core and multiple distinct proteins formed by alternative RNA processing
    • Szaro, B. G., H. C. Pant, J. Way, and J. Battey. 1991. Squid low molecular weight neurofilament proteins are a novel class of neurofilament protein. A nuclear lamin-like core and multiple distinct proteins formed by alternative RNA processing. J. Biol. Chem. 266: 15035-15041.
    • (1991) J. Biol. Chem. , vol.266 , pp. 15035-15041
    • Szaro, B.G.1    Pant, H.C.2    Way, J.3    Battey, J.4
  • 77
    • 0028981152 scopus 로고
    • P13sucl associates with a cdc2-like kinase in a multimeric cytoskeletal complex in squid axoplasm
    • Takahashi, M., N. Amin, P. Grant, and H. C. Pant. 1995. P13sucl associates with a cdc2-like kinase in a multimeric cytoskeletal complex in squid axoplasm. J. Neurosci. 15: 6222-6229.
    • (1995) J. Neurosci. , vol.15 , pp. 6222-6229
    • Takahashi, M.1    Amin, N.2    Grant, P.3    Pant, H.C.4
  • 78
    • 0025289033 scopus 로고
    • Characterization of the distinctive neurofilament subunits of the soma and axon initial segments in the squid stellate ganglion
    • Tytell, M., H. C. Pant, H. Gainer, and W. D. Hill. 1990. Characterization of the distinctive neurofilament subunits of the soma and axon initial segments in the squid stellate ganglion. J. Neurosci. Res. 25: 153-161.
    • (1990) J. Neurosci. Res. , vol.25 , pp. 153-161
    • Tytell, M.1    Pant, H.C.2    Gainer, H.3    Hill, W.D.4
  • 79
    • 0022557170 scopus 로고
    • Association of calcium/calmodulin-dependent kinase with cytoskeletal preparations: Phosphorylation of tubulin, neurofilament, and microtubule associated proteins
    • Vallano, M. L., J. R. Goldenring, R. S. Lasher, and R. J. DeLorenzo. 1986. Association of calcium/calmodulin-dependent kinase with cytoskeletal preparations: phosphorylation of tubulin, neurofilament, and microtubule associated proteins. Ann. N. Y. Acad. Sci. 466: 357-374.
    • (1986) Ann. N. Y. Acad. Sci. , vol.466 , pp. 357-374
    • Vallano, M.L.1    Goldenring, J.R.2    Lasher, R.S.3    Delorenzo, R.J.4
  • 80
    • 0032100631 scopus 로고    scopus 로고
    • Mitogen-activated protein kinases (Erk1,2) phosphorylate Lys-Ser-Pro (KSP) repeats in neurofilament proteins NF-H and NF-M
    • Veeranna, N. D. Amin, N. G. Ahn, H. Jalle, C. A. Winters, P. Grant, and H. C. Pant. 1998. Mitogen-activated protein kinases (Erk1,2) phosphorylate Lys-Ser-Pro (KSP) repeats in neurofilament proteins NF-H and NF-M. J. Neurosci. 18: 4008-4021.
    • (1998) J. Neurosci. , vol.18 , pp. 4008-4021
    • Veeranna1    Amin, N.D.2    Ahn, N.G.3    Jalle, H.4    Winters, C.A.5    Grant, P.6    Pant, H.C.7
  • 81
    • 0034728574 scopus 로고    scopus 로고
    • Cdk5 and MAPK are associated with complexes of cytoskeletal proteins in rat brain
    • Veeranna, K. T. Shetty, M. Takahashi, P. Grant, and H. C. Pant. 2000. Cdk5 and MAPK are associated with complexes of cytoskeletal proteins in rat brain. Brain Res. Mol. Brain Res. 76: 229-236.
    • (2000) Brain Res. Mol. Brain Res. , vol.76 , pp. 229-236
    • Veeranna1    Shetty, K.T.2    Takahashi, M.3    Grant, P.4    Pant, H.C.5
  • 82
    • 0033776708 scopus 로고    scopus 로고
    • Rapid movement of axonal neurofilaments interrupted by prolonged pauses
    • Wang, L., C. L. Ho, D. Sun, R. K. Liem, and A. Brown. 2000. Rapid movement of axonal neurofilaments interrupted by prolonged pauses. Nat. Cell Biol. 2: 137-141.
    • (2000) Nat. Cell Biol. , vol.2 , pp. 137-141
    • Wang, L.1    Ho, C.L.2    Sun, D.3    Liem, R.K.4    Brown, A.5
  • 83
    • 0026648109 scopus 로고
    • A high-molecular-weight squid neurofilament protein contains a lamin-like rod domain and a tail domain with Lys-Ser-Pro repeats
    • Way, J., M. R. Hellmich, H. Jaffe, B. Szaro, H. C. Pant, H. Gainer, and J. Battey. 1992. A high-molecular-weight squid neurofilament protein contains a lamin-like rod domain and a tail domain with Lys-Ser-Pro repeats. Proc. Natl. Acad. Sci. USA 89: 6963-6967.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 6963-6967
    • Way, J.1    Hellmich, M.R.2    Jaffe, H.3    Szaro, B.4    Pant, H.C.5    Gainer, H.6    Battey, J.7
  • 84
    • 0842268467 scopus 로고
    • Studying axoplasmic transport by video microscopy and using the squid giant axon as a model system
    • D. L. Gilbert, W. J. Adelman, and J. M. Arnold, eds. Plenum Press, New York
    • Weiss, D. G., M. A. Meyer, and G. M. Langford. 1990. Studying axoplasmic transport by video microscopy and using the squid giant axon as a model system. Pp. 303-321 in Squid as Experimental Animals, D. L. Gilbert, W. J. Adelman, and J. M. Arnold, eds. Plenum Press, New York.
    • (1990) Squid As Experimental Animals , pp. 303-321
    • Weiss, D.G.1    Meyer, M.A.2    Langford, G.M.3
  • 85
    • 0032694199 scopus 로고    scopus 로고
    • Kinesin-mediated transport of neurofilament protein oligomers in growing axons
    • Yabe, J. T., A. Pimenta, and T. B. Shea. 1999. Kinesin-mediated transport of neurofilament protein oligomers in growing axons. J. Cell Sci. 112 (Pt 21): 3799-3814.
    • (1999) J. Cell Sci. , vol.112 , Issue.PART 21 , pp. 3799-3814
    • Yabe, J.T.1    Pimenta, A.2    Shea, T.B.3
  • 86
    • 0035164218 scopus 로고    scopus 로고
    • The predominant form in which neurofilament subunits undergo axonal transport varies during axonal initiation, elongation, and maturation
    • Yabe, J. T., W. K. Chan, T. M. Chylinski, S. Lee, A. F. Pimenta, and T. B. Shea. 2001a. The predominant form in which neurofilament subunits undergo axonal transport varies during axonal initiation, elongation, and maturation. Cell Motil. Cytoskelet. 48: 61-83.
    • (2001) Cell Motil. Cytoskelet. , vol.48 , pp. 61-83
    • Yabe, J.T.1    Chan, W.K.2    Chylinski, T.M.3    Lee, S.4    Pimenta, A.F.5    Shea, T.B.6
  • 87
    • 0035313106 scopus 로고    scopus 로고
    • Neurofilaments consist o f distinct populations that can be distinguished by C-terminal phosphorylation, bundling, and axonal transport rate in growing xonal neurites
    • Yabe, J. T., T. Chylinski, F. S. Wang, A. Pimenta, S. D. Kattar, M. D. Linsley, W. K. Chan, and T. B. Shea. 2001b. Neurofilaments consist o f distinct populations that can be distinguished by C-terminal phosphorylation, bundling, and axonal transport rate in growing xonal neurites. J. Neurosci. 21: 2195-2205.
    • (2001) J. Neurosci. , vol.21 , pp. 2195-2205
    • Yabe, J.T.1    Chylinski, T.2    Wang, F.S.3    Pimenta, A.4    Kattar, S.D.5    Linsley, M.D.6    Chan, W.K.7    Shea, T.B.8
  • 88
    • 0000529165 scopus 로고
    • Fused neurons and synaptic contacts in the giant nerve fibres of cephalopods
    • Young, J. Z. 1939. Fused neurons and synaptic contacts in the giant nerve fibres of cephalopods. Philos. Trans. R. Soc. Lond. B Biol. Sci. 229: 465-503.
    • (1939) Philos. Trans. R. Soc. Lond. B Biol. Sci. , vol.229 , pp. 465-503
    • Young, J.Z.1
  • 89
    • 0037591990 scopus 로고    scopus 로고
    • Phosphorylation of the head domain of neurofilament protein (NF-M): A factor regulating topographic phosphorylation of NF-M tail domain KSP sites in neurons
    • Zheng, Y. L., B. S. Li, Veeranna, and H. C. Pant. 2003. Phosphorylation of the head domain of neurofilament protein (NF-M): a factor regulating topographic phosphorylation of NF-M tail domain KSP sites in neurons. J. Biol. Chem. 278: 24026-24032.
    • (2003) J. Biol. Chem. , vol.278 , pp. 24026-24032
    • Zheng, Y.L.1    Li, B.S.2    Veeranna3    Pant, H.C.4
  • 90
    • 0032487532 scopus 로고    scopus 로고
    • Disruption of the NF-H gene increases axonal microtubule content and velocity of neurofilament transport: Relief of axonopathy resulting from the toxin β,β′-iminodipropionitrile
    • Zhu, Q., M. Lindenbaum, F. Levavasseur, H. Jacomy, and J. P. Julien. 1998. Disruption of the NF-H gene increases axonal microtubule content and velocity of neurofilament transport: relief of axonopathy resulting from the toxin β,β′-iminodipropionitrile. J. Cell Biol. 143: 183-193.
    • (1998) J. Cell Biol. , vol.143 , pp. 183-193
    • Zhu, Q.1    Lindenbaum, M.2    Levavasseur, F.3    Jacomy, H.4    Julien, J.P.5


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