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Volumn 122, Issue 6, 1993, Pages 1337-1350

Neurofilaments are obligate heteropolymers in vivo

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PROTEIN SUBUNIT;

EID: 0027293898     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.122.6.1337     Document Type: Article
Times cited : (316)

References (56)
  • 1
    • 0023545331 scopus 로고
    • The expression of mutant epidermal keratin cDNAs in simple epithelial and squamous cell carcinoma lines
    • Albers, K., and E. Fuchs. 1987. The expression of mutant epidermal keratin cDNAs in simple epithelial and squamous cell carcinoma lines. J. Cell Biol. 105:791-806.
    • (1987) J. Cell Biol. , vol.105 , pp. 791-806
    • Albers, K.1    Fuchs, E.2
  • 2
    • 0024512061 scopus 로고
    • Domain- and sequence-specific phosphorylation of vimentin induces disassembly of the filament structure
    • Ando, S., K. Tanabe, Y. Gonda, C. Sato, and M. Inagaki. 1989. Domain- and sequence-specific phosphorylation of vimentin induces disassembly of the filament structure. Biochemistry. 28:2974-2979.
    • (1989) Biochemistry , vol.28 , pp. 2974-2979
    • Ando, S.1    Tanabe, K.2    Gonda, Y.3    Sato, C.4    Inagaki, M.5
  • 3
    • 0025718837 scopus 로고
    • Intermediate filaments formed de nove rom tail-less cytokeratins in the cytoplasm and in the nucleus
    • Bader, B. L., T. M. Magin, M. Freudenmann, S. Stumpp, and W. W. Franke. 1991. Intermediate filaments formed de nove rom tail-less cytokeratins in the cytoplasm and in the nucleus. J. Cell Biol. 115:1293-1307.
    • (1991) J. Cell Biol. , vol.115 , pp. 1293-1307
    • Bader, B.L.1    Magin, T.M.2    Freudenmann, M.3    Stumpp, S.4    Franke, W.W.5
  • 4
    • 0025887292 scopus 로고
    • Individual neurofilament subunits reassembled in vitro exhibit unique biochemical, morphological and immunological properties
    • Balin, B. J., and V. M.-Y. Lee. 1991. Individual neurofilament subunits reassembled in vitro exhibit unique biochemical, morphological and immunological properties. Brain Res. 556:196-208.
    • (1991) Brain Res. , vol.556 , pp. 196-208
    • Balin, B.J.1    Lee, V.M.-Y.2
  • 5
    • 0022550636 scopus 로고
    • Chemical crosslinking analyzes of ox neurofilaments
    • Carden, M.S., and Eagles, P.A.M. 1986. Chemical crosslinking analyzes of ox neurofilaments. Biochem. J. 234:587-591.
    • (1986) Biochem. J. , vol.234 , pp. 587-591
    • Carden, M.S.1    Eagles, P.A.M.2
  • 6
    • 0025514319 scopus 로고
    • Transfected NF-H coassembles with vimentin in nonphosphorylated form
    • Chin, S. S., and R. K. H. Liem. 1990. Transfected NF-H coassembles with vimentin in nonphosphorylated form. J. Neurosci. 10:3714-3726.
    • (1990) J. Neurosci. , vol.10 , pp. 3714-3726
    • Chin, S.S.1    Liem, R.K.H.2
  • 7
    • 0025828675 scopus 로고
    • Effects of truncated neurofilament proteins on the endogenous intermediate filaments in transfected fibroblasts
    • Chin, S. S., P. Macioce, and R. K. H. Liem. 1991. Effects of truncated neurofilament proteins on the endogenous intermediate filaments in transfected fibroblasts. J. Cell Sci. 99:335-350.
    • (1991) J. Cell Sci. , vol.99 , pp. 335-350
    • Chin, S.S.1    Macioce, P.2    Liem, R.K.H.3
  • 8
    • 0005175316 scopus 로고
    • Phosphosphorylation and disassembly of intermediate filaments in mitotic cells
    • Chou, C.-H., E. Rosevear, and R. D. Goldman. 1990. Phosphosphorylation and disassembly of intermediate filaments in mitotic cells. Proc. Natl. Acad. Sci. USA. 86:1885-1889.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 1885-1889
    • Chou, C.-H.1    Rosevear, E.2    Goldman, R.D.3
  • 10
    • 0027465098 scopus 로고
    • Prograssive neuronopathy in transgenic mice expressing the human neurofilament heavy gene: A mouse model of amyotrophic lateral sclerosis
    • Côté, F., J.-F. Collard, and J.-P. Julien. 1993. Prograssive neuronopathy in transgenic mice expressing the human neurofilament heavy 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
  • 11
    • 0027328373 scopus 로고
    • Glycosylation of mammalian neurofilaments: Local-ization of multiple O-linked N-acetylglucosamine moieties on neurofilament polypeptides L and M
    • Dong, D. L.-Y., Z.-S. Xu, M. R. Chevrier, R. J. Cotter, D. W. Cleveland, and G. W. Hart. 1993. Glycosylation of mammalian neurofilaments: Local-ization of multiple O-linked N-acetylglucosamine moieties on neurofilament polypeptides L and M. J. Biol. Chem. 268:16679-16687.
    • (1993) J. Biol. Chem. , vol.268 , pp. 16679-16687
    • Dong, D.L.-Y.1    Xu, Z.-S.2    Chevrier, M.R.3    Cotter, R.J.4    Cleveland, D.W.5    Hart, G.W.6
  • 12
    • 0026706734 scopus 로고
    • Assembly of tail-less mutant of the intermediate protein, vimentin, in vitro and in vivo
    • Eckelt, A., H. Herrmann, and W. Franke. 1992. Assembly of tail-less mutant of the intermediate protein, vimentin, in vitro and in vivo. Eur. J. Cell Biol. 58:319-330.
    • (1992) Eur. J. Cell Biol. , vol.58 , pp. 319-330
    • Eckelt, A.1    Herrmann, H.2    Franke, W.3
  • 13
    • 0024526186 scopus 로고
    • Phosphorylation of vimentin in mitotically selected cells. in vitro cAMP-independent kinase and calcium stimulated phosphatase activity
    • Evans, R. M. 1989. Phosphorylation of vimentin in mitotically selected cells. In vitro cAMP-independent kinase and calcium stimulated phosphatase activity. J. Cell Biol. 108:67-78.
    • (1989) J. Cell Biol. , vol.108 , pp. 67-78
    • Evans, R.M.1
  • 14
    • 0022340978 scopus 로고
    • Isolation of monoclonal antibodies specific for human c-myc proto-oncogene product
    • Evan, G. I., G. K. Lewis, G. Ramsay, and J. M. Bishop. 1985. Isolation of monoclonal antibodies specific for human c-myc proto-oncogene product. Mol. Cell Biol. 5:3610-3616.
    • (1985) Mol. Cell Biol. , vol.5 , pp. 3610-3616
    • Evan, G.I.1    Lewis, G.K.2    Ramsay, G.3    Bishop, J.M.4
  • 15
    • 0025181698 scopus 로고
    • The predicted amino acid sequence of α-internexin is that of a novel neuronal intermediate filament protein
    • Fliegner, K. H., G. Y. Ching, and R. K. H. Liem. 1990. The predicted amino acid sequence of α-internexin is that of a novel neuronal intermediate filament protein. EMBO (Eur. Mol. Biol. Organ.) J. 9:749-755.
    • (1990) EMBO (Eur. Mol. Biol. Organ.) J. , vol.9 , pp. 749-755
    • Fliegner, K.H.1    Ching, G.Y.2    Liem, R.K.H.3
  • 16
    • 0021359297 scopus 로고
    • Formation of 10 nm fiaments from 150 kDa neurofilament protein in vitro
    • Gardner, E. E., D. Dahl, and A. Bignami. 1984. Formation of 10 nm fiaments from 150 kDa neurofilament protein in vitro. J. Neurosci. Res. 11:145-155.
    • (1984) J. Neurosci. Res. , vol.11 , pp. 145-155
    • Gardner, E.E.1    Dahl, D.2    Bignami, A.3
  • 17
    • 0019888431 scopus 로고
    • Self-assembly in vitro of 68,000 molecular weight component of the mammalian neurofilament triplet proteins into intermediate size filaments
    • Giesler, N., and K. Weber. 1981. Self-assembly in vitro of 68,000 molecular weight component of the mammalian neurofilament triplet proteins into intermediate size filaments. J. Mol. Biol. 151:565-571.
    • (1981) J. Mol. Biol. , vol.151 , pp. 565-571
    • Giesler, N.1    Weber, K.2
  • 18
    • 0025107358 scopus 로고
    • Assembly properties of dominant and recessive mutationa in the small mouse neurofilament (NF-L) subunit
    • Gill, S. R., P. C. Wong, M. J. Monteiro, and D. W. Cleveland. 1990. Assembly properties of dominant and recessive mutationa in the small mouse neurofilament (NF-L) subunit. J. Cell Biol. 111:2005-2019.
    • (1990) J. Cell Biol. , vol.111 , pp. 2005-2019
    • Gill, S.R.1    Wong, P.C.2    Monteiro, M.J.3    Cleveland, D.W.4
  • 19
    • 0015847039 scopus 로고
    • A new technique for the assay of infectivity of human adenovirus 5 DNA
    • Graham, R., and A. J. van der Eb. 1973. A new technique for the assay of infectivity of human adenovirus 5 DNA. Virology. 52:456-467.
    • (1973) Virology , vol.52 , pp. 456-467
    • Graham, R.1    Van Der Eb, A.J.2
  • 20
    • 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
  • 21
    • 0025220189 scopus 로고
    • Effects of phosphorylation of neurofilament L protein on filamentous structure
    • Hisanaga, S.-I., Y. Gonda, M. Inagaki, A. Ikai, and N. Hirokawa. 1990. Effects of phosphorylation of neurofilament L protein on filamentous structure. Cell Regul. 1:237-248.
    • (1990) Cell Regul. , vol.1 , pp. 237-248
    • Hisanaga, S.-I.1    Gonda, Y.2    Inagaki, M.3    Ikai, A.4    Hirokawa, N.5
  • 22
    • 0023689454 scopus 로고
    • Structure of the peripheral domains of neurofilaments revealed by low angle rotary shadowing
    • Hisanaga, S.-I., 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.-I.1    Hirokawa, N.2
  • 23
    • 0023239962 scopus 로고
    • Site-specific phosphorylation induces disassembly of vimentin filaments in vitro
    • Inagaki, M., Y. Nishi, K. Nishizawa, M. Matsuyama, and C. Sato. 1989. Site-specific phosphorylation induces disassembly of vimentin filaments in vitro. Nature (Lond.) 328:649-652.
    • (1989) Nature (Lond.) , vol.328 , pp. 649-652
    • Inagaki, M.1    Nishi, Y.2    Nishizawa, K.3    Matsuyama, M.4    Sato, C.5
  • 25
    • 0022339650 scopus 로고
    • Intermediate filament forming ability of desmin derivatives lacking either the amino-terminal 67 or the carboxyl-terminal 27 residues
    • Kaufmann, E., K. Weber, and N. Geisler. 1985. Intermediate filament forming ability of desmin derivatives lacking either the amino-terminal 67 or the carboxyl-terminal 27 residues. J. Mol. Biol. 185:733-742.
    • (1985) J. Mol. Biol. , vol.185 , pp. 733-742
    • Kaufmann, E.1    Weber, K.2    Geisler, N.3
  • 26
    • 0000704627 scopus 로고
    • Transfection of DNA into eukaryotic cells
    • F. Ausubel, R. Brent, R. Kingston, D. Moore, J. Seidman, J. Smith, and K. Struhl, editors. John Wiley and Sons Inc., New York
    • Kingston, R. E. 1990. Transfection of DNA into eukaryotic cells. In Current Protocols in Molecular Biology. F. Ausubel, R. Brent, R. Kingston, D. Moore, J. Seidman, J. Smith, and K. Struhl, editors. John Wiley and Sons Inc., New York.
    • (1990) Current Protocols in Molecular Biology
    • Kingston, R.E.1
  • 27
    • 0024544011 scopus 로고
    • Protein kinase C phosphorylation of desmin at four serine residues within the non-α-helical head domain
    • Kitamura, S., S. Ando, M. Shibata, K. Tanabe, C. Sato, and M. Inagaki. 1989. Protein kinase C phosphorylation of desmin at four serine residues within the non-α-helical head domain. J. Biol. Chem. 264:5674-5678.
    • (1989) J. Biol. Chem. , vol.264 , pp. 5674-5678
    • Kitamura, S.1    Ando, S.2    Shibata, M.3    Tanabe, K.4    Sato, C.5    Inagaki, M.6
  • 28
    • 0025881180 scopus 로고
    • A potential role for the COOH-terminal domain in the lateral packing of type III intermediate filaments
    • Kouklis, P. D., T. Papamarcaki, A. Merdes, and S. D. Georgatos. 1991. A potential role for the COOH-terminal domain in the lateral packing of type III intermediate filaments. J. Cell Biol. 114:773-786.
    • (1991) J. Cell Biol. , vol.114 , pp. 773-786
    • Kouklis, P.D.1    Papamarcaki, T.2    Merdes, A.3    Georgatos, S.D.4
  • 29
    • 0014949207 scopus 로고
    • Cleavage structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. 1970. Cleavage structural proteins during the assembly of the head of bacteriophage T4. Nature (Lond.). 227:680-685.
    • (1970) Nature (Lond.) , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 31
    • 0020488844 scopus 로고
    • Purification of individual components of the neurfilament triplet: Filament assembly from the 70,000 dalton subunit
    • Liem, R. K. H., and S. B. Hutchinson. 1982. Purification of individual components of the neurfilament triplet: filament assembly from the 70,000 dalton subunit. Biochemistry. 21:3221-3226.
    • (1982) Biochemistry , vol.21 , pp. 3221-3226
    • Liem, R.K.H.1    Hutchinson, S.B.2
  • 32
    • 0023425413 scopus 로고
    • In vivo microtubules are copolymers of available β-tubulin isotypes: Localization of each of the six vertebrate β-tubulin isotypes using polyclonal antibodies elicited by synthetic peptide antigens
    • Lopata, M. A., and D. W. Cleveland. 1987. In vivo microtubules are copolymers of available β-tubulin isotypes: localization of each of the six vertebrate β-tubulin isotypes using polyclonal antibodies elicited by synthetic peptide antigens. J. Cell Biol. 105:1707-1720.
    • (1987) J. Cell Biol. , vol.105 , pp. 1707-1720
    • Lopata, M.A.1    Cleveland, D.W.2
  • 33
    • 0021770787 scopus 로고
    • High level transient expression of a chloramphenicol acetyl transferase gene by DEAE-dextran mediated DNA transfection coupled with dimethylsulfoxide or glycerol shock treatment
    • Lopata, M. A., D. W. Cleveland, and B. Sollner-Webb. 1984. High level transient expression of a chloramphenicol acetyl transferase gene by DEAE-dextran mediated DNA transfection coupled with dimethylsulfoxide or glycerol shock treatment. Nucleic Acids Res. 12:5707-5717.
    • (1984) Nucleic Acids Res. , vol.12 , pp. 5707-5717
    • Lopata, M.A.1    Cleveland, D.W.2    Sollner-Webb, B.3
  • 34
    • 0025073744 scopus 로고
    • Retrovirus-mediated transgenic keratin expression in cultured fibroblasts: Specific domain functions in keratin stabilization and filament formation
    • Lu, X., and E. B. Lane. 1990. Retrovirus-mediated transgenic keratin expression in cultured fibroblasts: Specific domain functions in keratin stabilization and filament formation. Cell. 62:681-696.
    • (1990) Cell , vol.62 , pp. 681-696
    • Lu, X.1    Lane, E.B.2
  • 35
    • 0024578553 scopus 로고
    • Expression of NF-L and NF-M in fibroblasts reveals coassembly of neurofilament and vimentin subunits
    • Monteiro, M. J., and D. W. Cleveland. 1990. Expression of NF-L and NF-M in fibroblasts reveals coassembly of neurofilament and vimentin subunits. J. Cell Biol. 108:579-593.
    • (1990) J. Cell Biol. , vol.108 , pp. 579-593
    • Monteiro, M.J.1    Cleveland, D.W.2
  • 36
    • 0025852343 scopus 로고
    • Antibody labeling of bovine neurofilaments: Implication on the structure of neurofilament side-arms
    • Mulligan, L., Balin, B.J., Lee. V.M.-Y., and Ip, W. 1991. Antibody labeling of bovine neurofilaments: implication on the structure of neurofilament side-arms. J. Struct. Biol. 106:145-160.
    • (1991) J. Struct. Biol. , vol.106 , pp. 145-160
    • Mulligan, L.1    Balin, B.J.2    Lee, V.M.-Y.3    Ip, W.4
  • 37
    • 0023357815 scopus 로고
    • The human mid size neurfilament subunit: A repeated protein sequence and the relation ship of its gene to the intermediate filament gene family
    • Myers, M. W., R. A. Lazzarini, V. M. Y. Lee, W. W. Schlaepfer, and D. L. Nelson. 1987. The human mid size neurfilament subunit: a repeated protein sequence and the relation ship 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    Lee, V.M.Y.3    Schlaepfer, W.W.4    Nelson, D.L.5
  • 38
    • 0026764101 scopus 로고
    • Dynamics of neuronal intermediate filaments: A developmental perspective
    • Nixon, R. A., and T. B. Shea. 1992. Dynamics of neuronal intermediate filaments: a developmental perspective. Cell Motil. Cytoskeleton. 22:81-91.
    • (1992) Cell Motil. Cytoskeleton , vol.22 , pp. 81-91
    • Nixon, R.A.1    Shea, T.B.2
  • 39
    • 0025370462 scopus 로고
    • In vitro disassembly of nuclear lamina and M-phase-specific phosphorylation of lamins by cdc2 kinase
    • Peter, M., J. Nakagawa. M. Doree, J. C. Ley, and R. D. Goldman. 1990 In vitro disassembly of nuclear lamina and M-phase-specific phosphorylation of lamins by cdc2 kinase. Cell. 61:591-602.
    • (1990) Cell , vol.61 , pp. 591-602
    • Peter, M.1    Nakagawa, J.2    Doree, M.3    Ley, J.C.4    Goldman, R.D.5
  • 44
    • 0025339874 scopus 로고
    • Regulated expression of vimentin cDNA in the presence and absence of preexisting vimentin filament network
    • Sarria, A., S. Nordeen, and R. Evans. 1990. Regulated expression of vimentin cDNA in the presence and absence of preexisting vimentin filament network. J. Cell Biol. 111:553-565.
    • (1990) J. Cell Biol. , vol.111 , pp. 553-565
    • Sarria, A.1    Nordeen, S.2    Evans, R.3
  • 45
    • 0023777868 scopus 로고
    • The largest murine neurofilament protein (NF-H): Repeated phosphorylation sites
    • Shneidman, P. S., M. J. Carden, J. F. Lees, and R. A. Lazzarini. 1988. The largest murine neurofilament protein (NF-H): Repeated phosphorylation sites. Mol. Brain Res. 4:217-231.
    • (1988) Mol. Brain Res. , vol.4 , pp. 217-231
    • Shneidman, P.S.1    Carden, M.J.2    Lees, J.F.3    Lazzarini, R.A.4
  • 46
    • 0025257205 scopus 로고
    • Phosphorylation of the amino terminal 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 amino terminal 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
  • 47
    • 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
  • 49
    • 0026781976 scopus 로고
    • Loss of epithelial markers and acquisition of vimentin expression in adriamycin- And vinblastin-resistant human breast cancer cell lines
    • Sommers, C. L., S. E. Heckford, J. M. Skerker, P. Worland, J. A. Torri, E. W. Thompson, S.W. Byers, and E. P. Gelmann. 1992. Loss of epithelial markers and acquisition of vimentin expression in adriamycin- and vinblastin-resistant human breast cancer cell lines. Cancer Res. 52:5190-5197.
    • (1992) Cancer Res. , vol.52 , pp. 5190-5197
    • Sommers, C.L.1    Heckford, S.E.2    Skerker, J.M.3    Worland, P.4    Torri, J.A.5    Thompson, E.W.6    Byers, S.W.7    Gelmann, E.P.8
  • 50
    • 0023951297 scopus 로고
    • Molecular and cell biology of intermediate filaments
    • Steinert, P. M., and D. R. Roop. 1988. Molecular and cell biology of intermediate filaments. Annu. Rev. Biochem. 57:593-625.
    • (1988) Annu. Rev. Biochem. , vol.57 , pp. 593-625
    • Steinert, P.M.1    Roop, D.R.2
  • 51
    • 0027550657 scopus 로고
    • Intermediate filament structure and assembly
    • Stewart, M. 1993. Intermediate filament structure and assembly. Cur. Opin. Cell Biol. 5:3-11.
    • (1993) Cur. Opin. Cell Biol. , vol.5 , pp. 3-11
    • Stewart, M.1
  • 52
    • 0019828628 scopus 로고
    • Antibody decoration of neurofilaments
    • Willard, M., and C. Simon. 1981. Antibody decoration of neurofilaments. J. Cell Biol. 89:198-205.
    • (1981) J. Cell Biol. , vol.89 , pp. 198-205
    • Willard, M.1    Simon, C.2
  • 53
    • 0025013886 scopus 로고
    • Characterization of dominant and recessive assembly-defective mutations in mouse neurofilament NF-M
    • Wong, P. C., and D. W. Cleveland. 1990. Characterization of dominant and recessive assembly-defective mutations in mouse neurofilament NF-M. J. Cell Biol. 111:1987-2003.
    • (1990) J. Cell Biol. , vol.111 , pp. 1987-2003
    • Wong, P.C.1    Cleveland, D.W.2
  • 54
    • 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. 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.2    Griffin, J.W.3    Cleveland, D.W.4
  • 55
    • 0025993428 scopus 로고
    • Hereditary hypertrophic axonopathy with neurofilament deficiency in a mutant strain of the Japanese quail
    • Yamasaki, H., C. Itakura, and M. Mizutani. 1991. Hereditary hypertrophic 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
  • 56
    • 0038437591 scopus 로고    scopus 로고
    • In vitro reconstitution of intermediate filaments from mammalian neurofilament triplet peptides
    • Zackroff, R. V., W. W. Idler, P. M. Steinert, and R. D. Goldman. In vitro reconstitution of intermediate filaments from mammalian neurofilament triplet peptides. Proc. Natl. Acad. Sci. USA. 79:754-757.
    • Proc. Natl. Acad. Sci. USA , vol.79 , pp. 754-757
    • Zackroff, R.V.1    Idler, W.W.2    Steinert, P.M.3    Goldman, R.D.4


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