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Volumn 143, Issue 1, 1998, Pages 1-4

Gene targeting studies begin to reveal the function of neurofilament proteins

Author keywords

[No Author keywords available]

Indexed keywords

NEUROFILAMENT PROTEIN;

EID: 0032487437     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.143.1.1     Document Type: Review
Times cited : (53)

References (36)
  • 1
    • 0025788760 scopus 로고
    • Neurofilament reassembly in vitro: Biochemical, morphological and immuno-electron microscopic studies employing monoclonal antibodies to defined epitopes
    • Balin, J.B., E.A. Clark, J.Q. Trojanowski, and V.M.-Y. Lee. 1991. Neurofilament reassembly in vitro: biochemical, morphological and immuno-electron microscopic studies employing monoclonal antibodies to defined epitopes. Brain Res. 556:181-195.
    • (1991) Brain Res. , vol.556 , pp. 181-195
    • Balin, J.B.1    Clark, E.A.2    Trojanowski, J.Q.3    Lee, V.M.-Y.4
  • 2
    • 0027220073 scopus 로고
    • Assembly of type IV neuronal intermediate filaments in nonneuronal cells in the absence of preexisting cytoplasmic intermediate filaments
    • Ching, G.Y., and R.K.H. Liem. 1993. Assembly of type IV neuronal intermediate filaments in nonneuronal cells in the absence of preexisting cytoplasmic intermediate filaments. J. Cell Biol. 122:1323-1335.
    • (1993) J. Cell Biol. , vol.122 , pp. 1323-1335
    • Ching, G.Y.1    Liem, R.K.H.2
  • 3
    • 0027465098 scopus 로고
    • Progressive neuropathy in transgenic mice expressing the human neurofilament gene: A mouse model of amyotrophic lateral sclerosis
    • Côté, F., J.F. Collard, and J.P. Julien. 1993. Progressive neuropathy in transgenic mice expressing the human neurofilament gene: a mouse model of amyotrophic lateral sclerosis. Cell. 73:35-46.
    • (1993) Cell , vol.73 , pp. 35-46
    • Côté, F.1    Collard, J.F.2    Julien, J.P.3
  • 4
    • 0026580004 scopus 로고
    • Local modulation of neurofilament phosphorylation, axonal caliber, and slow axonal transport by myelinating Schwann cells
    • de Waegh, S.M., V.M.-Y. Lee, and S. Brady. 1992. Local modulation of neurofilament phosphorylation, axonal caliber, and slow axonal transport by myelinating Schwann cells. Cell. 68:451-468.
    • (1992) Cell , vol.68 , pp. 451-468
    • De Waegh, S.M.1    Lee, V.M.-Y.2    Brady, S.3
  • 5
    • 0028261670 scopus 로고
    • Neurofilament-deficient axons and perikaryal aggregates in viable transgenic mice expressing a neurofilament β-galactosidase fusion protein
    • Eyer, J., and A. Peterson. 1994. Neurofilament-deficient axons and perikaryal aggregates in viable transgenic mice expressing a neurofilament β-galactosidase fusion protein. Neuron. 12:389-405.
    • (1994) Neuron. , vol.12 , pp. 389-405
    • Eyer, J.1    Peterson, A.2
  • 6
    • 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, P. Bosco, C. Kang, A. Goourov, P.-H. Tu, V.M.-Y. Lee, and R.A. Lazzarini. 1998a. 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, V.L.2    Bosco, P.3    Kang, C.4    Goourov, A.5    Tu, P.-H.6    Lee, V.M.-Y.7    Lazzarini, R.A.8
  • 8
    • 0001420783 scopus 로고
    • Axon diameters in relation to the spike dimensions and the conduction velocity in mammalian A fibers
    • Gasser, H.S., and H. Grundfest. 1939. Axon diameters in relation to the spike dimensions and the conduction velocity in mammalian A fibers. Am. J. Physiol. 127:393-414.
    • (1939) Am. J. Physiol. , vol.127 , pp. 393-414
    • Gasser, H.S.1    Grundfest, H.2
  • 9
    • 0019888431 scopus 로고
    • Self-assembly in vitro of the 68000 molecular weight component of the mammalian neurofilament triplet proteins into intermediate sized filaments
    • Geisler, N., and K. Weber. 1981. Self-assembly in vitro of the 68000 molecular weight component of the mammalian neurofilament triplet proteins into intermediate sized filaments. J. Mol. Biol. 151:565-571.
    • (1981) J. Mol. Biol. , vol.151 , pp. 565-571
    • Geisler, N.1    Weber, K.2
  • 10
    • 0023158848 scopus 로고
    • Posttranslational modification of neurofilament polypeptides in rabbit retina
    • Glicksman, M.A., D. Soppert, and M.B. Willard 1987. Posttranslational modification of neurofilament polypeptides in rabbit retina. J. Neurobiol. 18:167-196.
    • (1987) J. Neurobiol. , vol.18 , pp. 167-196
    • Glicksman, M.A.1    Soppert, D.2    Willard, M.B.3
  • 11
    • 0020326774 scopus 로고
    • Cross-linker system between neurofilaments, microtubules, and membranous organelles in frog axons revealed by the quick-freeze, deep-etching method
    • Hirokawa, N. 1982. Cross-linker system between neurofilaments, microtubules, and membranous organelles in frog axons revealed by the quick-freeze, deep-etching method. J. Cell Biol. 94:129-142.
    • (1982) J. Cell Biol. , vol.94 , pp. 129-142
    • Hirokawa, N.1
  • 12
    • 0021261943 scopus 로고
    • Organization of mammalian neurofilament polypeptides within the neuronal cytoskeleton
    • Hirokawa, N., M.A. Glicksman, and M.B. Willard. 1984. Organization of mammalian neurofilament polypeptides within the neuronal cytoskeleton. J. Cell Biol. 98:1523-1536.
    • (1984) J. Cell Biol. , vol.98 , pp. 1523-1536
    • Hirokawa, N.1    Glicksman, M.A.2    Willard, M.B.3
  • 13
    • 0023689454 scopus 로고
    • Structure of the peripheral domains of neurofilaments revealed by low angle rotary shadowing
    • Hisanaga, S., and N. Hirokawa. 1988. Structure of the peripheral domains of neurofilaments revealed by low angle rotary shadowing. J. Mol. Biol. 20: 297-305.
    • (1988) J. Mol. Biol. , vol.20 , pp. 297-305
    • Hisanaga, S.1    Hirokawa, N.2
  • 14
    • 0016541063 scopus 로고
    • The slow component of axonal transport. Identification of major astructural polypeptides of the axon and their generality among mammalian neurons
    • Huffman, P.N., and R.J. Lasek. 1975. The slow component of axonal transport. Identification of major astructural polypeptides of the axon and their generality among mammalian neurons. J. Cell Biol. 66:351-366.
    • (1975) J. Cell Biol. , vol.66 , pp. 351-366
    • Huffman, P.N.1    Lasek, R.J.2
  • 16
    • 0002203136 scopus 로고
    • Structure and expression of neurofilament genes
    • R.D. Burgoyne, editor. Wiley Liss, Inc., New York
    • Julien, J.P., and F. Grosveld. 1991. Structure and expression of neurofilament genes. In Neuronal Cytoskeleton. R.D. Burgoyne, editor. Wiley Liss, Inc., New York. 215-231.
    • (1991) Neuronal Cytoskeleton , pp. 215-231
    • Julien, J.P.1    Grosveld, F.2
  • 17
    • 0027293898 scopus 로고
    • Neurofilaments are obligate heteropolymers in vivo
    • Lee, M.K., Z. Xu, P.C. Wong, and D.W. Cleveland. 1993. Neurofilaments are obligate heteropolymers in vivo. J. Cell Biol. 122:1337-1350.
    • (1993) J. Cell Biol. , vol.122 , pp. 1337-1350
    • Lee, M.K.1    Xu, Z.2    Wong, P.C.3    Cleveland, D.W.4
  • 19
    • 0020488844 scopus 로고
    • Purification of individual components of the neurofilament triplet: Filament assembly from the 70000 dalton subunit
    • Liem, R.K.H., and S.B. Hutchison. 1982. Purification of individual components of the neurofilament triplet: filament assembly from the 70000 dalton subunit. Biochemistry. 21:3221-3226.
    • (1982) Biochemistry , vol.21 , pp. 3221-3226
    • Liem, R.K.H.1    Hutchison, S.B.2
  • 21
    • 0027486263 scopus 로고
    • Interaction of the tail domain of high molecular weight subunits of neurofilaments with the COOH-terminal region of tubulin and its regulation by the Tau protein kinase II
    • Miyasaka, H., S. Okabe, K. Ishiguro, T. Uchida, and N. Hirokawa. 1993. Interaction of the tail domain of high molecular weight subunits of neurofilaments with the COOH-terminal region of tubulin and its regulation by the Tau protein kinase II. J. Biol. Chem. 268:22695-22702.
    • (1993) J. Biol. Chem. , vol.268 , pp. 22695-22702
    • Miyasaka, H.1    Okabe, S.2    Ishiguro, K.3    Uchida, T.4    Hirokawa, N.5
  • 22
    • 0025852343 scopus 로고
    • Antibody labelling of bovine neurofilaments: Implications on the structure of neurofilament side-arms
    • Mulligan, L., B.J. Balin, V.M.-Y. Lee, and W. Ip. 1991. Antibody labelling of bovine neurofilaments: implications on the structure of neurofilament side-arms. J. Struct. Biol. 106:1445-1460.
    • (1991) J. Struct. Biol. , vol.106 , pp. 1445-1460
    • Mulligan, L.1    Balin, B.J.2    Lee, V.M.-Y.3    Ip, W.4
  • 23
    • 0023357815 scopus 로고
    • The human mid-sized neurofilament subunit: A repeated protein sequence and the relationship of its gene to the intermediate filament gene family
    • Myers, M.W., R.A. Lazzarini, V.M. Schlalpfer, and D.L. Nelson 1987. The human mid-sized neurofilament subunit: a repeated protein sequence and the relationship of its gene to the intermediate filament gene family. EMBO (Eur. Mol. Biol. Organ.) J. 6:1617-1626.
    • (1987) EMBO (Eur. Mol. Biol. Organ.) J. , vol.6 , pp. 1617-1626
    • Myers, M.W.1    Lazzarini, R.A.2    Schlalpfer, V.M.3    Nelson, D.L.4
  • 24
    • 0028900588 scopus 로고
    • Two distinct functions of the carboxyl-terminal domain of NF-M upon neurofilament assembly: Cross-bridge formation and longitudinal elongation of filaments
    • Nakagawa, T., J.C. Chen, Z. Zhang, Y. Kanai, and N. Hirokawa. 1995. Two distinct functions of the carboxyl-terminal domain of NF-M upon neurofilament assembly: cross-bridge formation and longitudinal elongation of filaments. J. Cell Biol. 129:411-429.
    • (1995) J. Cell Biol. , vol.129 , pp. 411-429
    • Nakagawa, T.1    Chen, J.C.2    Zhang, Z.3    Kanai, Y.4    Hirokawa, N.5
  • 25
    • 0027931132 scopus 로고
    • Phosphorylation of carboxyl terminus domains of neurofilament proteins in retinal ganglion cell neurons in vivo: Influences on regional neurofilament accumulation, interfilament spacing, and axon caliber
    • Nixon, R.A., P.A. Paskevich, P.R.K. Sihag, and C.Y. Thayer. 1994. Phosphorylation of carboxyl terminus domains of neurofilament proteins in retinal ganglion cell neurons in vivo: influences on regional neurofilament accumulation, interfilament spacing, and axon caliber. J. Cell Biol. 126:1031-1046.
    • (1994) J. Cell Biol. , vol.126 , pp. 1031-1046
    • Nixon, R.A.1    Paskevich, P.A.2    Sihag, P.R.K.3    Thayer, C.Y.4
  • 26
    • 0027530064 scopus 로고
    • Neurofilament deficiency in quail caused by nonsense mutation in neurofilament-L gene
    • Ohara, O., Y. Gahara, T. Miyake, H. Teraoka, and T.K. Itamura. 1993. Neurofilament deficiency in quail caused by nonsense mutation in neurofilament-L gene. J. Cell Biol. 121:387-395.
    • (1993) J. Cell Biol. , vol.121 , pp. 387-395
    • Ohara, O.1    Gahara, Y.2    Miyake, T.3    Teraoka, H.4    Itamura, T.K.5
  • 27
    • 0032487499 scopus 로고    scopus 로고
    • Neurofilament-dependent radial growth of motor axons and axonal organization of neurofilaments does not require 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 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
  • 28
    • 0019968002 scopus 로고
    • Differential expression of neurofilament triplet proteins in brain development
    • Shaw, G., and K. Weber. 1982. Differential expression of neurofilament triplet proteins in brain development. Nature. 298:296-299.
    • (1982) Nature , vol.298 , pp. 296-299
    • Shaw, G.1    Weber, K.2
  • 29
    • 0029052277 scopus 로고
    • Overexpression of the human NFM subunit in transgenic mice modifies the level of endogenous NFL and the phosphorylation state of NFH subunits
    • Tu, P.-H., G. Elder, R.A. Lazzarini, D. Nelson, J.Q. Trojanowski, and V.M.-Y. Lee. 1995. Overexpression of the human NFM subunit in transgenic mice modifies the level of endogenous NFL and the phosphorylation state of NFH subunits. J. Cell Biol. 129:1629-1640.
    • (1995) J. Cell Biol. , vol.129 , pp. 1629-1640
    • Tu, P.-H.1    Elder, G.2    Lazzarini, R.A.3    Nelson, D.4    Trojanowski, J.Q.5    Lee, V.M.-Y.6
  • 30
    • 0029124072 scopus 로고
    • Increasing neurofilament subunit NF-M expression reduces axonal NF-H, inhibits radial growth, and results in neurofilamentous accumulation in motor neurons
    • Wong, P.C., J. Marszalek, T.O. Crowford, Z. Xu, S.-T. Hsieh, J.W. Griffin, and D.W. Cleveland. 1995. Increasing neurofilament subunit NF-M expression reduces axonal NF-H, inhibits radial growth, and results in neurofilamentous accumulation in motor neurons. J. Cell Biol. 130:1413-1422.
    • (1995) J. Cell Biol. , vol.130 , pp. 1413-1422
    • Wong, P.C.1    Marszalek, J.2    Crowford, T.O.3    Xu, Z.4    Hsieh, S.-T.5    Griffin, J.W.6    Cleveland, D.W.7
  • 31
    • 0027410516 scopus 로고
    • Increased expression of neurofilament subunit NF-L produces morphological alterations that resemble the pathology of human motor neuron disease
    • Xu, Z.-S., L.C. Cork, J.W. Griffin, and D.W. Cleveland. 1993. Increased expression of neurofilament subunit NF-L produces morphological alterations that resemble the pathology of human motor neuron disease. Cell. 73:23-33.
    • (1993) Cell , vol.73 , pp. 23-33
    • Xu, Z.-S.1    Cork, L.C.2    Griffin, J.W.3    Cleveland, D.W.4
  • 33
    • 0025993428 scopus 로고
    • Hereditary hypotrophic axonopathy with neurofilament deficiency in a mutant strain of the Japanese quail
    • Yamasaki, H., C. Itakura, and M. Mizutani. 1991. Hereditary hypotrophic axonopathy with neurofilament deficiency in a mutant strain of the Japanese quail. Acta Neuropathol. 82:427-434.
    • (1991) Acta Neuropathol. , vol.82 , pp. 427-434
    • Yamasaki, H.1    Itakura, C.2    Mizutani, M.3
  • 34
    • 0030598838 scopus 로고    scopus 로고
    • An essential cytoskeletal linker protein connecting actin filaments to intermediate filaments
    • Yang, Y., J. Dowling, Q.-C. Yu, P. Kouklis, and D.W. Cleveland. 1996. An essential cytoskeletal linker protein connecting actin filaments to intermediate filaments. Cell. 86:655-665.
    • (1996) Cell , vol.86 , pp. 655-665
    • Yang, Y.1    Dowling, J.2    Yu, Q.-C.3    Kouklis, P.4    Cleveland, D.W.5
  • 35
    • 0031263931 scopus 로고    scopus 로고
    • Delayed maturation of regenerating myelinated axons in mice lacking neurofilaments
    • Zhu, Q., S. Couillard-Despres, and J.P. Julien. 1997. Delayed maturation of regenerating myelinated axons in mice lacking neurofilaments. Exp. Neurol. 148:299-316.
    • (1997) Exp. Neurol. , vol.148 , pp. 299-316
    • Zhu, Q.1    Couillard-Despres, S.2    Julien, J.P.3
  • 36
    • 0032487532 scopus 로고    scopus 로고
    • Disruption of the NF-H gene increases axonal microtubule content and velocity of neurofilament transport: Relief of axonopathy due to 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 due to 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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