메뉴 건너뛰기




Volumn 33, Issue 1, 2010, Pages 27-37

Post-transcriptional control of neurofilaments: New roles in development, regeneration and neurodegenerative disease

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA INTERNEXIN; BETA TUBULIN; ELONGATION FACTOR 1ALPHA; GLYCERALDEHYDE 3 PHOSPHATE DEHYDROGENASE; HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN; HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN K; MESSENGER RNA; NEUROFILAMENT M PROTEIN; NEUROFILAMENT PROTEIN; NEUROMODULIN; PERIPHERIN; PROTEIN P21; VIMENTIN;

EID: 73449137883     PISSN: 01662236     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tins.2009.10.002     Document Type: Review
Times cited : (80)

References (109)
  • 1
    • 0034308278 scopus 로고    scopus 로고
    • The 'ins' and 'outs' of intermediate filament organization
    • Coulombe P.A., et al. The 'ins' and 'outs' of intermediate filament organization. Trends Cell Biol. 10 (2000) 420-428
    • (2000) Trends Cell Biol. , vol.10 , pp. 420-428
    • Coulombe, P.A.1
  • 2
    • 53749093269 scopus 로고    scopus 로고
    • Review of the multiple aspects of neurofilament functions and their possible contribution to neurodegeneration
    • Perrot R., et al. Review of the multiple aspects of neurofilament functions and their possible contribution to neurodegeneration. Mol. Neurobiol. 38 (2008) 27-65
    • (2008) Mol. Neurobiol. , vol.38 , pp. 27-65
    • Perrot, R.1
  • 3
    • 0035894849 scopus 로고    scopus 로고
    • Loss of neurofilaments alters axonal growth dynamics
    • Walker K.L., et al. Loss of neurofilaments alters axonal growth dynamics. J. Neurosci. 21 (2001) 9655-9666
    • (2001) J. Neurosci. , vol.21 , pp. 9655-9666
    • Walker, K.L.1
  • 4
    • 39149108125 scopus 로고    scopus 로고
    • Intermediate filaments: versatile building blocks of cell structure
    • Goldman R.D., et al. Intermediate filaments: versatile building blocks of cell structure. Curr. Opin. Cell Biol. 20 (2008) 28-34
    • (2008) Curr. Opin. Cell Biol. , vol.20 , pp. 28-34
    • Goldman, R.D.1
  • 5
    • 23844538993 scopus 로고    scopus 로고
    • The pathobiology of amyotrophic lateral sclerosis: a proteinopathy? J
    • Strong M.J., et al. The pathobiology of amyotrophic lateral sclerosis: a proteinopathy? J. Neuropathol. Exp. Neurol. 64 (2005) 649-664
    • (2005) Neuropathol. Exp. Neurol. , vol.64 , pp. 649-664
    • Strong, M.J.1
  • 6
    • 33751243629 scopus 로고    scopus 로고
    • Neuronal intermediate filaments and ALS: a new look at an old question
    • Xiao S., et al. Neuronal intermediate filaments and ALS: a new look at an old question. Biochim. Biophys. Acta 1762 (2006) 1001-1012
    • (2006) Biochim. Biophys. Acta , vol.1762 , pp. 1001-1012
    • Xiao, S.1
  • 7
    • 34547817056 scopus 로고    scopus 로고
    • The complex relation between genotype and phenotype in motor neuron disease
    • Cañete-Soler R., and Schlaepfer W.W. The complex relation between genotype and phenotype in motor neuron disease. Ann. Neurol. 62 (2007) 8-14
    • (2007) Ann. Neurol. , vol.62 , pp. 8-14
    • Cañete-Soler, R.1    Schlaepfer, W.W.2
  • 8
    • 0028116467 scopus 로고
    • A mutant neurofilament subunit causes massive, selective motor neuron death: implications for the pathogenesis of human motor neuron disease
    • Lee M.K., et al. A mutant neurofilament subunit causes massive, selective motor neuron death: implications for the pathogenesis of human motor neuron disease. Neuron 13 (1994) 975-988
    • (1994) Neuron , vol.13 , pp. 975-988
    • Lee, M.K.1
  • 9
    • 0033812601 scopus 로고    scopus 로고
    • Plasticin, a type III neuronal intermediate filament protein, assembles as an obligate heteropolymer: implications for axonal flexibility
    • Asch W.S., and Schechter N. Plasticin, a type III neuronal intermediate filament protein, assembles as an obligate heteropolymer: implications for axonal flexibility. J. Neurochem. 75 (2000) 1475-1486
    • (2000) J. Neurochem. , vol.75 , pp. 1475-1486
    • Asch, W.S.1    Schechter, N.2
  • 10
    • 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 Liem R.K. Assembly of type IV neuronal intermediate filaments in nonneuronal cells in the absence of preexisting cytoplasmic intermediate filaments. J. Cell Biol. 122 (1993) 1323-1335
    • (1993) J. Cell Biol. , vol.122 , pp. 1323-1335
    • Ching, G.Y.1    Liem, R.K.2
  • 11
    • 0027293898 scopus 로고
    • Neurofilaments are obligate heteropolymers in vivo
    • Lee M.K., et al. Neurofilaments are obligate heteropolymers in vivo. J. Cell Biol. 122 (1993) 1337-1350
    • (1993) J. Cell Biol. , vol.122 , pp. 1337-1350
    • Lee, M.K.1
  • 12
    • 0032570802 scopus 로고    scopus 로고
    • Neurofilament (NF) assembly; divergent characteristics of human and rodent NF-L subunits
    • Carter J., et al. Neurofilament (NF) assembly; divergent characteristics of human and rodent NF-L subunits. J. Biol. Chem. 273 (1999) 5101-5108
    • (1999) J. Biol. Chem. , vol.273 , pp. 5101-5108
    • Carter, J.1
  • 13
    • 0023374805 scopus 로고
    • Properties of highly viscous gels formed by neurofilaments in vitro: a possible consequence of a specific inter-filament cross-bridging
    • Leterrier J.F., and Eyer J. Properties of highly viscous gels formed by neurofilaments in vitro: a possible consequence of a specific inter-filament cross-bridging. Biochem. J. 245 (1987) 93-101
    • (1987) Biochem. J. , vol.245 , pp. 93-101
    • Leterrier, J.F.1    Eyer, J.2
  • 14
    • 0022238110 scopus 로고
    • Characterization of mammalian neurofilament triplet proteins: subunit stoichiometry and morphology of native and reconstituted filaments
    • Scott D., et al. Characterization of mammalian neurofilament triplet proteins: subunit stoichiometry and morphology of native and reconstituted filaments. J. Biol. Chem. 260 (1985) 10736-10747
    • (1985) J. Biol. Chem. , vol.260 , pp. 10736-10747
    • Scott, D.1
  • 15
    • 61449150382 scopus 로고    scopus 로고
    • Age related and hypothyroidism related changes on the stoichiometry of neurofilament subunits in the developing rat brain
    • Chinnakkaruppan A., et al. Age related and hypothyroidism related changes on the stoichiometry of neurofilament subunits in the developing rat brain. Int. J. Dev. Neurosci. 27 (2009) 257-261
    • (2009) Int. J. Dev. Neurosci. , vol.27 , pp. 257-261
    • Chinnakkaruppan, A.1
  • 16
    • 0029670953 scopus 로고    scopus 로고
    • Alpha-internexin is the only neuronal intermediate filament expressed in developing cerebellar granule neurons
    • Chien C.-L., et al. Alpha-internexin is the only neuronal intermediate filament expressed in developing cerebellar granule neurons. J. Neurobiol. 29 (1996) 304-318
    • (1996) J. Neurobiol. , vol.29 , pp. 304-318
    • Chien, C.-L.1
  • 17
    • 0025941533 scopus 로고
    • NF-L and peripherin immunoreactivities define distinct classes of rat sensory ganglion cells
    • Goldstein M.E., et al. NF-L and peripherin immunoreactivities define distinct classes of rat sensory ganglion cells. J. Neurosci. Res. 30 (1991) 92-104
    • (1991) J. Neurosci. Res. , vol.30 , pp. 92-104
    • Goldstein, M.E.1
  • 18
    • 0026639603 scopus 로고
    • Identification and developmental expression of a novel low molecular weight neuronal intermediate filament protein in Xenopus laevis
    • Charnas L.R., et al. Identification and developmental expression of a novel low molecular weight neuronal intermediate filament protein in Xenopus laevis. J. Neurosci. 12 (1992) 3010-3024
    • (1992) J. Neurosci. , vol.12 , pp. 3010-3024
    • Charnas, L.R.1
  • 19
    • 0348011603 scopus 로고    scopus 로고
    • Functions of intermediate filaments in neuronal development and disease
    • Lariviére R.C., and Julien J.-P. Functions of intermediate filaments in neuronal development and disease. J. Neurobiol. 58 (2004) 131-148
    • (2004) J. Neurobiol. , vol.58 , pp. 131-148
    • Lariviére, R.C.1    Julien, J.-P.2
  • 20
    • 3943102116 scopus 로고    scopus 로고
    • Unraveling the mechanisms involved in motor neuron degeneration in ALS
    • Brujin L.I., et al. Unraveling the mechanisms involved in motor neuron degeneration in ALS. Annu. Rev. Neurosci. 27 (2004) 723-749
    • (2004) Annu. Rev. Neurosci. , vol.27 , pp. 723-749
    • Brujin, L.I.1
  • 21
    • 0034326239 scopus 로고    scopus 로고
    • Cytoskeletal abnormalities in amyotrophic lateral sclerosis: beneficial or detrimental effects
    • Julien J., and Beaulieu J. Cytoskeletal abnormalities in amyotrophic lateral sclerosis: beneficial or detrimental effects. J. Neurol. Sci. 180 (2000) 7-14
    • (2000) J. Neurol. Sci. , vol.180 , pp. 7-14
    • Julien, J.1    Beaulieu, J.2
  • 22
    • 73449121821 scopus 로고    scopus 로고
    • Neuronal intermediate filaments and neurodegenerative diseases
    • Paramio J.M. (Ed), Landes Bioscience
    • Ching G.Y., and Liem R.K.H. Neuronal intermediate filaments and neurodegenerative diseases. In: Paramio J.M. (Ed). Intermediate Filaments (2006), Landes Bioscience 35-51
    • (2006) Intermediate Filaments , pp. 35-51
    • Ching, G.Y.1    Liem, R.K.H.2
  • 23
    • 34249653116 scopus 로고    scopus 로고
    • Post-transcriptional control of neurofilaments in development and disease
    • Thyagarajan A., et al. Post-transcriptional control of neurofilaments in development and disease. Exp. Cell Res. 313 (2007) 2088-2097
    • (2007) Exp. Cell Res. , vol.313 , pp. 2088-2097
    • Thyagarajan, A.1
  • 24
    • 0025335775 scopus 로고
    • Ontogeny of the neuronal intermediate filament protein, peripherin, in the mouse embryo
    • Troy C.M., et al. Ontogeny of the neuronal intermediate filament protein, peripherin, in the mouse embryo. Neuroscience 36 (1990) 217-237
    • (1990) Neuroscience , vol.36 , pp. 217-237
    • Troy, C.M.1
  • 25
    • 0034738706 scopus 로고    scopus 로고
    • Xenopus laevis peripherin (XIF3) is expressed in radial glia and proliferating neural epithelial cells as well as in neurons
    • Gervasi C., et al. Xenopus laevis peripherin (XIF3) is expressed in radial glia and proliferating neural epithelial cells as well as in neurons. J. Comp. Neurol. 423 (2000) 512-531
    • (2000) J. Comp. Neurol. , vol.423 , pp. 512-531
    • Gervasi, C.1
  • 26
    • 0032487414 scopus 로고    scopus 로고
    • Restricted expression of the neuronal intermediate filament protein plasticin during zebrafish development
    • Canger A.K., et al. Restricted expression of the neuronal intermediate filament protein plasticin during zebrafish development. J. Comp. Neurol. 399 (1998) 561-572
    • (1998) J. Comp. Neurol. , vol.399 , pp. 561-572
    • Canger, A.K.1
  • 27
    • 0035041241 scopus 로고    scopus 로고
    • Differential expression and localization of neuronal intermediate filament proteins within newly developing neurites in dissociated cultures of Xenopus laevis embryonic spinal cord
    • Undamatla J., and Szaro B.G. Differential expression and localization of neuronal intermediate filament proteins within newly developing neurites in dissociated cultures of Xenopus laevis embryonic spinal cord. Cell Motil. Cytoskel. 49 (2001) 16-32
    • (2001) Cell Motil. Cytoskel. , vol.49 , pp. 16-32
    • Undamatla, J.1    Szaro, B.G.2
  • 28
    • 0025129067 scopus 로고
    • Simultaneous up-regulation of neurofilament proteins during the postnatal development of the rat nervous system
    • Schlaepfer W.W., and Bruce J. Simultaneous up-regulation of neurofilament proteins during the postnatal development of the rat nervous system. J. Neurosci. Res. 25 (1990) 39-49
    • (1990) J. Neurosci. Res. , vol.25 , pp. 39-49
    • Schlaepfer, W.W.1    Bruce, J.2
  • 29
    • 0030569605 scopus 로고    scopus 로고
    • Role of vimentin in early stages of neuritogenesis in cultured hippocampal neurons
    • Boyne L.J., et al. Role of vimentin in early stages of neuritogenesis in cultured hippocampal neurons. Int. J. Dev. Neurosci. 14 (1996) 739-748
    • (1996) Int. J. Dev. Neurosci. , vol.14 , pp. 739-748
    • Boyne, L.J.1
  • 30
    • 0344875476 scopus 로고    scopus 로고
    • A role for intermediate filaments in determining and maintaining the shape of nerve cells
    • Helfand B.T., et al. A role for intermediate filaments in determining and maintaining the shape of nerve cells. Mol. Biol. Cell 14 (2003) 5069-5081
    • (2003) Mol. Biol. Cell , vol.14 , pp. 5069-5081
    • Helfand, B.T.1
  • 31
    • 4744358511 scopus 로고    scopus 로고
    • Reexpression of vimentin in differentiated neuroblastoma cells enhances elongation of axonal neurites
    • Dubey M., et al. Reexpression of vimentin in differentiated neuroblastoma cells enhances elongation of axonal neurites. J. Neurosci. Res. 78 (2004) 245-249
    • (2004) J. Neurosci. Res. , vol.78 , pp. 245-249
    • Dubey, M.1
  • 33
    • 0033396551 scopus 로고    scopus 로고
    • Gefiltin in zebrafish embryos: sequential gene expression of two neurofilament proteins in retinal ganglion cells
    • Leake D., et al. Gefiltin in zebrafish embryos: sequential gene expression of two neurofilament proteins in retinal ganglion cells. Differentiation 65 (1999) 181-189
    • (1999) Differentiation , vol.65 , pp. 181-189
    • Leake, D.1
  • 34
    • 33749177577 scopus 로고    scopus 로고
    • Alpha-internexin is structurally and functionally associated with the neurofilament triplet proteins in the mature CNS
    • Yuan A., et al. Alpha-internexin is structurally and functionally associated with the neurofilament triplet proteins in the mature CNS. J. Neurosci. 26 (2006) 10006-10019
    • (2006) J. Neurosci. , vol.26 , pp. 10006-10019
    • Yuan, A.1
  • 35
    • 10744228738 scopus 로고    scopus 로고
    • NF-M is an essential target for the myelin-directed "outside-in" signaling cascade that mediates radial axonal growth
    • Garcia M.L., et al. NF-M is an essential target for the myelin-directed "outside-in" signaling cascade that mediates radial axonal growth. J. Cell Biol. 163 (2003) 1011-1020
    • (2003) J. Cell Biol. , vol.163 , pp. 1011-1020
    • Garcia, M.L.1
  • 36
    • 34249704868 scopus 로고    scopus 로고
    • Neurofilaments: phosphorylation and signal transduction
    • Paramio J.M. (Ed), Springer Science and Business Media
    • Kesavapany S., et al. Neurofilaments: phosphorylation and signal transduction. In: Paramio J.M. (Ed). Intermediate Filaments (2006), Springer Science and Business Media 52-73
    • (2006) Intermediate Filaments , pp. 52-73
    • Kesavapany, S.1
  • 37
    • 0023912713 scopus 로고
    • mRNA levels of all three neurofilament proteins decline following nerve transection
    • Goldstein M.E., et al. mRNA levels of all three neurofilament proteins decline following nerve transection. Brain Res. 427 (1988) 287-291
    • (1988) Brain Res. , vol.427 , pp. 287-291
    • Goldstein, M.E.1
  • 38
    • 0024313983 scopus 로고
    • Axotomy-induced changes in the expression of a type III neuronal intermediate filament
    • Oblinger M.M., et al. Axotomy-induced changes in the expression of a type III neuronal intermediate filament. J. Neurosci. 9 (1989) 3766-3775
    • (1989) J. Neurosci. , vol.9 , pp. 3766-3775
    • Oblinger, M.M.1
  • 39
    • 0037096372 scopus 로고    scopus 로고
    • Axonally transported peripheral signals regulate alpha-internexin expression in regenerating motoneurons
    • McGraw T.S., et al. Axonally transported peripheral signals regulate alpha-internexin expression in regenerating motoneurons. J. Neurosci. 22 (2002) 4955-4963
    • (2002) J. Neurosci. , vol.22 , pp. 4955-4963
    • McGraw, T.S.1
  • 40
    • 0025946116 scopus 로고
    • Corticospinal neurons exhibit a novel pattern of cytoskeletal gene expression after injury
    • Mikucki S.A., and Oblinger M.M. Corticospinal neurons exhibit a novel pattern of cytoskeletal gene expression after injury. J. Neurosci. Res. 30 (1991) 213-225
    • (1991) J. Neurosci. Res. , vol.30 , pp. 213-225
    • Mikucki, S.A.1    Oblinger, M.M.2
  • 41
    • 0038248923 scopus 로고    scopus 로고
    • Increased expression of multiple neurofilament mRNAs during regeneration of vertebrate central nervous system axons
    • Gervasi C., et al. Increased expression of multiple neurofilament mRNAs during regeneration of vertebrate central nervous system axons. J. Comp. Neurol. 461 (2003) 262-275
    • (2003) J. Comp. Neurol. , vol.461 , pp. 262-275
    • Gervasi, C.1
  • 42
    • 0031841161 scopus 로고    scopus 로고
    • Cloning of zebrafish neurofilament cDNAs for plasticin and gefiltin: increased mRNA expression in ganglion cells after optic nerve injury
    • Asch W.S., et al. Cloning of zebrafish neurofilament cDNAs for plasticin and gefiltin: increased mRNA expression in ganglion cells after optic nerve injury. J. Neurochem. 71 (1998) 20-32
    • (1998) J. Neurochem. , vol.71 , pp. 20-32
    • Asch, W.S.1
  • 43
    • 0030994563 scopus 로고    scopus 로고
    • Recovery of neurofilament expression selectively in regenerating reticulospinal neurons
    • Jacobs A.J., et al. Recovery of neurofilament expression selectively in regenerating reticulospinal neurons. J. Neurosci. 17 (1997) 5206-5220
    • (1997) J. Neurosci. , vol.17 , pp. 5206-5220
    • Jacobs, A.J.1
  • 44
    • 0026458240 scopus 로고
    • Axo-glial interactions at the dorsal root transitional zone regulate neurofilament protein synthesis in axotomized sensory neurons
    • Liuzzi F.J., and Tedeschi B. Axo-glial interactions at the dorsal root transitional zone regulate neurofilament protein synthesis in axotomized sensory neurons. J. Neurosci. 12 (1992) 4783-4792
    • (1992) J. Neurosci. , vol.12 , pp. 4783-4792
    • Liuzzi, F.J.1    Tedeschi, B.2
  • 45
    • 0029007246 scopus 로고
    • The optic tract and tectal ablation influence the composition of neurofilaments in regenerating optic axons of Xenopus laevis
    • Zhao Y., and Szaro B.G. The optic tract and tectal ablation influence the composition of neurofilaments in regenerating optic axons of Xenopus laevis. J. Neurosci. 15 (1995) 4629-4640
    • (1995) J. Neurosci. , vol.15 , pp. 4629-4640
    • Zhao, Y.1    Szaro, B.G.2
  • 46
    • 0035808841 scopus 로고    scopus 로고
    • Evidence that regenerating optic axons maintain long-term growth in the lizard Ctenophorus ornatus: growth-associated protein-43 and gefiltin expression
    • Rodger J., et al. Evidence that regenerating optic axons maintain long-term growth in the lizard Ctenophorus ornatus: growth-associated protein-43 and gefiltin expression. Neuroscience 102 (2001) 647-654
    • (2001) Neuroscience , vol.102 , pp. 647-654
    • Rodger, J.1
  • 47
    • 0942287654 scopus 로고    scopus 로고
    • Morphological and biochemical changes of neurofilaments in aged rat sciatic nerve axons
    • Hisanaga S.-I., et al. Morphological and biochemical changes of neurofilaments in aged rat sciatic nerve axons. J. Neurochem. 88 (2004) 735-745
    • (2004) J. Neurochem. , vol.88 , pp. 735-745
    • Hisanaga, S.-I.1
  • 48
    • 9644268929 scopus 로고    scopus 로고
    • Phylogenetically conserved binding of specific KH domain proteins to the 3′ untranslated region of the vertebrate middle neurofilament mRNA
    • Thyagarajan A., and Szaro B.G. Phylogenetically conserved binding of specific KH domain proteins to the 3′ untranslated region of the vertebrate middle neurofilament mRNA. J. Biol. Chem. 279 (2004) 49680-49688
    • (2004) J. Biol. Chem. , vol.279 , pp. 49680-49688
    • Thyagarajan, A.1    Szaro, B.G.2
  • 49
    • 0025787346 scopus 로고
    • Squid low molecular weight neurofilament proteins are a novel class of neurofilament protein
    • Szaro B.G., et al. Squid low molecular weight neurofilament proteins are a novel class of neurofilament protein. J. Biol. Chem. 266 (1991) 15035-15041
    • (1991) J. Biol. Chem. , vol.266 , pp. 15035-15041
    • Szaro, B.G.1
  • 50
    • 0026648109 scopus 로고
    • A high-molecular-weight squid neurofilament protein contains a lamin-like rod domain and a tail domain of Lys-Ser-Pro repeats
    • Way J., et al. A high-molecular-weight squid neurofilament protein contains a lamin-like rod domain and a tail domain of Lys-Ser-Pro repeats. Proc. Natl. Acad. Sci. U. S. A. 89 (1992) 6963-6967
    • (1992) Proc. Natl. Acad. Sci. U. S. A. , vol.89 , pp. 6963-6967
    • Way, J.1
  • 51
    • 0030564999 scopus 로고    scopus 로고
    • Medium weight neurofilament mRNA in goldfish Mauthner axoplasm
    • Weiner O.D., et al. Medium weight neurofilament mRNA in goldfish Mauthner axoplasm. Neurosci. Lett. 213 (1996) 83-86
    • (1996) Neurosci. Lett. , vol.213 , pp. 83-86
    • Weiner, O.D.1
  • 52
    • 0033770070 scopus 로고    scopus 로고
    • Neurofilament mRNAs are present and translated in the normal and severed sciatic nerve
    • Sotelo-Silveira J.R., et al. Neurofilament mRNAs are present and translated in the normal and severed sciatic nerve. J. Neurosci. Res. 62 (2000) 65-74
    • (2000) J. Neurosci. Res. , vol.62 , pp. 65-74
    • Sotelo-Silveira, J.R.1
  • 53
    • 33745841571 scopus 로고    scopus 로고
    • RNA trafficking in axons
    • Sotelo-Silveira J.R., et al. RNA trafficking in axons. Traffic 7 (2006) 508-515
    • (2006) Traffic , vol.7 , pp. 508-515
    • Sotelo-Silveira, J.R.1
  • 54
    • 68249124086 scopus 로고    scopus 로고
    • Axonal mRNAs: characterisation and role in the growth and regeneration of dorsal root ganglion axons and growth cones
    • Vogelaar C.F., et al. Axonal mRNAs: characterisation and role in the growth and regeneration of dorsal root ganglion axons and growth cones. Mol. Cell. Neurosci. 42 (2009) 102-115
    • (2009) Mol. Cell. Neurosci. , vol.42 , pp. 102-115
    • Vogelaar, C.F.1
  • 55
    • 0027183092 scopus 로고
    • Neurofilament proteins are synthesized in nerve endings from squid brain
    • Crispino M., et al. Neurofilament proteins are synthesized in nerve endings from squid brain. J. Neurochem. 61 (1993) 1144-1146
    • (1993) J. Neurochem. , vol.61 , pp. 1144-1146
    • Crispino, M.1
  • 56
    • 0033104147 scopus 로고    scopus 로고
    • Protein-synthesizing machinery in the axon compartment
    • Koenig E., and Giuditta A. Protein-synthesizing machinery in the axon compartment. Neuroscience 89 (1999) 5-15
    • (1999) Neuroscience , vol.89 , pp. 5-15
    • Koenig, E.1    Giuditta, A.2
  • 57
    • 34547439282 scopus 로고    scopus 로고
    • Ribosomal distributions in axons of mammalian myelinated fibers
    • Kun A., et al. Ribosomal distributions in axons of mammalian myelinated fibers. J. Neurosci. Res. 85 (2007) 2087-2098
    • (2007) J. Neurosci. Res. , vol.85 , pp. 2087-2098
    • Kun, A.1
  • 58
    • 34548857945 scopus 로고    scopus 로고
    • Extracellular stimuli specifically regulate localized levels of individual neuronal mRNAs
    • Willis D.E., et al. Extracellular stimuli specifically regulate localized levels of individual neuronal mRNAs. J. Cell Biol. 178 (2007) 965-980
    • (2007) J. Cell Biol. , vol.178 , pp. 965-980
    • Willis, D.E.1
  • 59
    • 33644508655 scopus 로고    scopus 로고
    • Assembling an intermediate filament network by dynamic cotranslation
    • Chang L., et al. Assembling an intermediate filament network by dynamic cotranslation. J. Cell Biol. 172 (2006) 747-758
    • (2006) J. Cell Biol. , vol.172 , pp. 747-758
    • Chang, L.1
  • 60
    • 0026476009 scopus 로고
    • Actinomycin prevents the destabilization of neurofilament mRNA in primary sensory neurons
    • Schwartz M.L., et al. Actinomycin prevents the destabilization of neurofilament mRNA in primary sensory neurons. J. Biol. Chem. 267 (1992) 24596-24600
    • (1992) J. Biol. Chem. , vol.267 , pp. 24596-24600
    • Schwartz, M.L.1
  • 61
    • 0027506094 scopus 로고
    • Different post transcriptional controls for the human neurofilament light and heavy genes in transgenic mice
    • Beaudet L., et al. Different post transcriptional controls for the human neurofilament light and heavy genes in transgenic mice. Mol. Brain Res. 18 (1993) 23-31
    • (1993) Mol. Brain Res. , vol.18 , pp. 23-31
    • Beaudet, L.1
  • 62
    • 44449098839 scopus 로고    scopus 로고
    • Dynamic endogenous association of neurofilament mRNAs with K-homology domain ribonucleoproteins in developing cerebral cortex
    • Thyagarajan A., and Szaro B.G. Dynamic endogenous association of neurofilament mRNAs with K-homology domain ribonucleoproteins in developing cerebral cortex. Brain Res. 1189 (2008) 33-42
    • (2008) Brain Res. , vol.1189 , pp. 33-42
    • Thyagarajan, A.1    Szaro, B.G.2
  • 63
    • 0029067504 scopus 로고
    • Transcriptional and post-transcriptional mechanisms regulating neurofilament and tubulin gene expression during normal development of the rat brain
    • Moskowitz P.F., and Oblinger M.M. Transcriptional and post-transcriptional mechanisms regulating neurofilament and tubulin gene expression during normal development of the rat brain. Mol. Brain Res. 30 (1995) 211-222
    • (1995) Mol. Brain Res. , vol.30 , pp. 211-222
    • Moskowitz, P.F.1    Oblinger, M.M.2
  • 64
    • 41949133239 scopus 로고    scopus 로고
    • Dynamic regulation of middle neurofilament (NF-M) RNA pools during optic nerve regeneration
    • Ananthakrishnan L., et al. Dynamic regulation of middle neurofilament (NF-M) RNA pools during optic nerve regeneration. Neuroscience 153 (2008) 144-153
    • (2008) Neuroscience , vol.153 , pp. 144-153
    • Ananthakrishnan, L.1
  • 65
    • 58149295962 scopus 로고    scopus 로고
    • Transcriptional and translational dynamics of light neurofilament subunit RNAs during Xenopus laevis optic nerve regeneration
    • Ananthakrishnan L., and Szaro B.G. Transcriptional and translational dynamics of light neurofilament subunit RNAs during Xenopus laevis optic nerve regeneration. Brain Res. 1250 (2009) 27-40
    • (2009) Brain Res. , vol.1250 , pp. 27-40
    • Ananthakrishnan, L.1    Szaro, B.G.2
  • 66
    • 0021895471 scopus 로고
    • The transneuronal induction of sprouting and synapse formation in intact mouse muscles
    • Rotshenker S., and Tal M. The transneuronal induction of sprouting and synapse formation in intact mouse muscles. J. Physiol. 360 (1985) 387-396
    • (1985) J. Physiol. , vol.360 , pp. 387-396
    • Rotshenker, S.1    Tal, M.2
  • 67
    • 0033763630 scopus 로고    scopus 로고
    • Characterization of neuronal intermediate filament protein expression in cervical spinal motor neurons in sporadic amyotrophic lateral sclerosis (ALS)
    • Wong N., et al. Characterization of neuronal intermediate filament protein expression in cervical spinal motor neurons in sporadic amyotrophic lateral sclerosis (ALS). J. Neuropathol. Exp. Neurol. 59 (2000) 972-982
    • (2000) J. Neuropathol. Exp. Neurol. , vol.59 , pp. 972-982
    • Wong, N.1
  • 68
    • 0036723914 scopus 로고    scopus 로고
    • Selective loss of neurofilament expression in Cu/Zn superoxide dismutase (SOD1) linked amyotrophic lateral sclerosis
    • Menzies F.M., et al. Selective loss of neurofilament expression in Cu/Zn superoxide dismutase (SOD1) linked amyotrophic lateral sclerosis. J. Neurochem. 82 (2002) 1118-1128
    • (2002) J. Neurochem. , vol.82 , pp. 1118-1128
    • Menzies, F.M.1
  • 69
    • 1542616991 scopus 로고    scopus 로고
    • Intermediate filament steady-state mRNA levels in amyotrophic lateral sclerosis
    • Strong M.J., et al. Intermediate filament steady-state mRNA levels in amyotrophic lateral sclerosis. Biochem. Biophys. Res. Commun. 316 (2004) 317-322
    • (2004) Biochem. Biophys. Res. Commun. , vol.316 , pp. 317-322
    • Strong, M.J.1
  • 70
    • 0038374249 scopus 로고    scopus 로고
    • Selective loss of trans-acting instability determinants of neurofilament mRNA in amyotrophic lateral sclerosis spinal cord
    • Ge W.W., et al. Selective loss of trans-acting instability determinants of neurofilament mRNA in amyotrophic lateral sclerosis spinal cord. J. Biol. Chem. 278 (2003) 26558-26563
    • (2003) J. Biol. Chem. , vol.278 , pp. 26558-26563
    • Ge, W.W.1
  • 71
    • 34249751076 scopus 로고    scopus 로고
    • TDP43 is a human low molecular weight neurofilament (hNFL) mRNA-binding protein
    • Strong M.J., et al. TDP43 is a human low molecular weight neurofilament (hNFL) mRNA-binding protein. Mol. Cell. Neurosci. 35 (2007) 320-327
    • (2007) Mol. Cell. Neurosci. , vol.35 , pp. 320-327
    • Strong, M.J.1
  • 72
    • 33845900214 scopus 로고    scopus 로고
    • 14-3-3 protein binds to the low molecular weight neurofilament (NFL) mRNA 3′UTR
    • Ge W.W., et al. 14-3-3 protein binds to the low molecular weight neurofilament (NFL) mRNA 3′UTR. Mol. Cell. Neurosci. 34 (2007) 80-87
    • (2007) Mol. Cell. Neurosci. , vol.34 , pp. 80-87
    • Ge, W.W.1
  • 73
    • 12844269876 scopus 로고    scopus 로고
    • Mutant copper/zinc superoxide dismutase binds to and destabilizes human low molecular weight neurofilament mRNA
    • Ge W.W., et al. Mutant copper/zinc superoxide dismutase binds to and destabilizes human low molecular weight neurofilament mRNA. J. Biol. Chem. 280 (2005) 118-124
    • (2005) J. Biol. Chem. , vol.280 , pp. 118-124
    • Ge, W.W.1
  • 74
    • 27444439730 scopus 로고    scopus 로고
    • Temporal profiles of neuronal degeneration, glial proliferation, and cell death in hNFL+/+ and NFL-/- mice
    • McLean J.R., et al. Temporal profiles of neuronal degeneration, glial proliferation, and cell death in hNFL+/+ and NFL-/- mice. Glia 52 (2005) 59-69
    • (2005) Glia , vol.52 , pp. 59-69
    • McLean, J.R.1
  • 75
    • 0036759174 scopus 로고    scopus 로고
    • Untranslated element in neurofilament mRNA has neuropathic effect on motor neurons of transgenic mice
    • Nie Z., et al. Untranslated element in neurofilament mRNA has neuropathic effect on motor neurons of transgenic mice. J. Neurosci. 22 (2002) 7662-7770
    • (2002) J. Neurosci. , vol.22 , pp. 7662-7770
    • Nie, Z.1
  • 76
    • 0035943731 scopus 로고    scopus 로고
    • p190RhoGEF binds to a destabilizing element in the 3′UTR of NF-L mRNA and alters the stability of the transcript
    • Cañete-Soler R., et al. p190RhoGEF binds to a destabilizing element in the 3′UTR of NF-L mRNA and alters the stability of the transcript. J. Biol. Chem. 276 (2001) 32046-32050
    • (2001) J. Biol. Chem. , vol.276 , pp. 32046-32050
    • Cañete-Soler, R.1
  • 77
    • 18244397436 scopus 로고    scopus 로고
    • Aldolases A and C are ribonucleolytic components of a neuronal complex that regulates the stability of the light neurofilament mRNA
    • Cañete-Soler R., et al. Aldolases A and C are ribonucleolytic components of a neuronal complex that regulates the stability of the light neurofilament mRNA. J. Neurosci. 25 (2005) 4353-4364
    • (2005) J. Neurosci. , vol.25 , pp. 4353-4364
    • Cañete-Soler, R.1
  • 78
    • 27744597388 scopus 로고    scopus 로고
    • RNA-binding protein is involved in aggregation of light neurofilament protein and is implicated in the pathogenesis of motor neuron degeneration
    • Lin H., et al. RNA-binding protein is involved in aggregation of light neurofilament protein and is implicated in the pathogenesis of motor neuron degeneration. Hum. Mol. Genet. 14 (2005) 3643-3659
    • (2005) Hum. Mol. Genet. , vol.14 , pp. 3643-3659
    • Lin, H.1
  • 79
    • 71049162268 scopus 로고    scopus 로고
    • Human low molecular weight neurofilament (NFL) mRNA interacts with a predicted p190RhoGEF homologue (RGNEF)
    • Volkening K., et al. Human low molecular weight neurofilament (NFL) mRNA interacts with a predicted p190RhoGEF homologue (RGNEF). Amyotroph. Lateral Scler. Jun 1 (2009) 1-7
    • (2009) Amyotroph. Lateral Scler. Jun , vol.1 , pp. 1-7
    • Volkening, K.1
  • 80
    • 33847421038 scopus 로고    scopus 로고
    • Coregulation of light neurofilament mRNA by poly(A)-binding protein and aldolase C: implications for neurodegeneration
    • Stefanizzi I., and Cañete-Soler R. Coregulation of light neurofilament mRNA by poly(A)-binding protein and aldolase C: implications for neurodegeneration. Brain Res. 1139 (2007) 15-28
    • (2007) Brain Res. , vol.1139 , pp. 15-28
    • Stefanizzi, I.1    Cañete-Soler, R.2
  • 81
    • 63849138722 scopus 로고    scopus 로고
    • Potential application of RNAi for understanding and therapy of neurodegenerative diseases
    • Schwartz E.I. Potential application of RNAi for understanding and therapy of neurodegenerative diseases. Front. Biosci. 14 (2009) 297-320
    • (2009) Front. Biosci. , vol.14 , pp. 297-320
    • Schwartz, E.I.1
  • 82
    • 67349159137 scopus 로고    scopus 로고
    • Five siRNAs targeting SNPs may provide therapy for three-quarters of Huntington's disease patients
    • Pfister E.L., et al. Five siRNAs targeting SNPs may provide therapy for three-quarters of Huntington's disease patients. Curr. Biol. 19 (2009) 774-778
    • (2009) Curr. Biol. , vol.19 , pp. 774-778
    • Pfister, E.L.1
  • 83
    • 0033557936 scopus 로고    scopus 로고
    • ELAV tumor antigen, Hel-N1, increases translation of neurofilament M mRNA and induces formation of neurites in teratocarcinoma cells
    • Antic D., et al. ELAV tumor antigen, Hel-N1, increases translation of neurofilament M mRNA and induces formation of neurites in teratocarcinoma cells. Genes Dev. 13 (1999) 449-461
    • (1999) Genes Dev. , vol.13 , pp. 449-461
    • Antic, D.1
  • 84
    • 2942623743 scopus 로고    scopus 로고
    • hnRNP K: one protein multiple processes
    • Bomsztyk K., et al. hnRNP K: one protein multiple processes. BioEssays 26 (2004) 629-638
    • (2004) BioEssays , vol.26 , pp. 629-638
    • Bomsztyk, K.1
  • 85
    • 58149109750 scopus 로고    scopus 로고
    • A crucial role for hnRNP K in axon development in Xenopus laevis
    • Liu Y., et al. A crucial role for hnRNP K in axon development in Xenopus laevis. Development 135 (2008) 3125-3135
    • (2008) Development , vol.135 , pp. 3125-3135
    • Liu, Y.1
  • 86
    • 16844370540 scopus 로고    scopus 로고
    • Involvement of Hu and heterogeneous nuclear ribonucleoprotein K in neuronal differentiation through p21 mRNA post-transcriptional regulation
    • Yano M., et al. Involvement of Hu and heterogeneous nuclear ribonucleoprotein K in neuronal differentiation through p21 mRNA post-transcriptional regulation. J. Biol. Chem. 280 (2005) 12690-12699
    • (2005) J. Biol. Chem. , vol.280 , pp. 12690-12699
    • Yano, M.1
  • 87
    • 0030842963 scopus 로고    scopus 로고
    • Identification of two proteins that bind to a pyrimidine-rich sequence in the 3′-untranslated region of GAP-43 mRNA
    • Irwin N., et al. Identification of two proteins that bind to a pyrimidine-rich sequence in the 3′-untranslated region of GAP-43 mRNA. Nucleic Acids Res. 25 (1997) 1281-1288
    • (1997) Nucleic Acids Res. , vol.25 , pp. 1281-1288
    • Irwin, N.1
  • 88
    • 0035951373 scopus 로고    scopus 로고
    • Lipoxygenase mRNA silencing in erythroid differentiation: the 3′UTR regulatory complex controls 60S ribosomal subunit joining
    • Ostareck D.H., et al. Lipoxygenase mRNA silencing in erythroid differentiation: the 3′UTR regulatory complex controls 60S ribosomal subunit joining. Cell 104 (2001) 281-290
    • (2001) Cell , vol.104 , pp. 281-290
    • Ostareck, D.H.1
  • 89
    • 0035095885 scopus 로고    scopus 로고
    • ERK phosphorylation drives cytoplasmic accumulation of hnRNP K and inhibition of mRNA translation
    • Habelhah H., et al. ERK phosphorylation drives cytoplasmic accumulation of hnRNP K and inhibition of mRNA translation. Nat. Cell Biol. 3 (2001) 325-330
    • (2001) Nat. Cell Biol. , vol.3 , pp. 325-330
    • Habelhah, H.1
  • 90
    • 24644502657 scopus 로고    scopus 로고
    • From birth to death: the complex lives of eukaryotic mRNAs
    • Moore M.J. From birth to death: the complex lives of eukaryotic mRNAs. Science 309 (2005) 1514-1518
    • (2005) Science , vol.309 , pp. 1514-1518
    • Moore, M.J.1
  • 91
    • 1942467797 scopus 로고    scopus 로고
    • Molecular insights into mental retardation: multiple functions for the Fragile X mental retardation protein?
    • Zalfa F., and Bagni C. Molecular insights into mental retardation: multiple functions for the Fragile X mental retardation protein?. Curr. Issues Mol. Biol. 6 (2004) 73-88
    • (2004) Curr. Issues Mol. Biol. , vol.6 , pp. 73-88
    • Zalfa, F.1    Bagni, C.2
  • 92
    • 46549085203 scopus 로고    scopus 로고
    • Function and regulation of local axonal translation
    • Lin A.C., and Holt C.E. Function and regulation of local axonal translation. Curr. Opin. Neurobiol. 18 (2008) 60-68
    • (2008) Curr. Opin. Neurobiol. , vol.18 , pp. 60-68
    • Lin, A.C.1    Holt, C.E.2
  • 93
    • 0036289532 scopus 로고    scopus 로고
    • Eukaryotic mRNPs may represent posttranscriptional operons
    • Keene J.D., and Tenenbaum S.A. Eukaryotic mRNPs may represent posttranscriptional operons. Mol. Cell 9 (2002) 1161-1167
    • (2002) Mol. Cell , vol.9 , pp. 1161-1167
    • Keene, J.D.1    Tenenbaum, S.A.2
  • 94
    • 34848901958 scopus 로고    scopus 로고
    • Axonal neurofilaments control multiple fiber properties but do not influence structure or spacing of nodes of Ranvier
    • Perrot R., et al. Axonal neurofilaments control multiple fiber properties but do not influence structure or spacing of nodes of Ranvier. J. Neurosci. 27 (2007) 9573-9584
    • (2007) J. Neurosci. , vol.27 , pp. 9573-9584
    • Perrot, R.1
  • 95
    • 3943078618 scopus 로고    scopus 로고
    • Intermediate filaments: molecular structure, assembly mechanism, and integration into functionally distinct intracellular scaffolds
    • Herrmann H., and Aebi U. Intermediate filaments: molecular structure, assembly mechanism, and integration into functionally distinct intracellular scaffolds. Annu. Rev. Biochem. 73 (2004) 749-789
    • (2004) Annu. Rev. Biochem. , vol.73 , pp. 749-789
    • Herrmann, H.1    Aebi, U.2
  • 96
    • 34250880140 scopus 로고    scopus 로고
    • Intermediate filaments: from cell architecture to nanomechanics
    • Herrmann H., et al. Intermediate filaments: from cell architecture to nanomechanics. Nat. Rev. Mol. Cell Biol. 8 (2007) 562-573
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 562-573
    • Herrmann, H.1
  • 97
    • 0037044764 scopus 로고    scopus 로고
    • Binding of p190RhoGEF to a destabilizing element on the light neurofilament mRNA is competed by BC1 mRNA
    • Ge W., et al. Binding of p190RhoGEF to a destabilizing element on the light neurofilament mRNA is competed by BC1 mRNA. J. Biol. Chem. 277 (2002) 42701-42705
    • (2002) J. Biol. Chem. , vol.277 , pp. 42701-42705
    • Ge, W.1
  • 98
    • 70349482318 scopus 로고    scopus 로고
    • Neuronal intermediate filaments and neurodegenerative disorders
    • Perrot R., and Eyer J. Neuronal intermediate filaments and neurodegenerative disorders. Brain Res. Bull. 80 (2009) 282-295
    • (2009) Brain Res. Bull. , vol.80 , pp. 282-295
    • Perrot, R.1    Eyer, J.2
  • 99
    • 0033911099 scopus 로고    scopus 로고
    • A new variant of Charcot-Marie-Tooth disease type 2 is probably the result of a mutation in the neurofilament-light gene
    • Mersiyanova I.V., et al. A new variant of Charcot-Marie-Tooth disease type 2 is probably the result of a mutation in the neurofilament-light gene. Am. J. Hum. Genet. 67 (2000) 37-46
    • (2000) Am. J. Hum. Genet. , vol.67 , pp. 37-46
    • Mersiyanova, I.V.1
  • 100
    • 0035136847 scopus 로고    scopus 로고
    • Further evidence that neurofilament light chain mutations can cause Charcot-Marie-Tooth disease type 2E
    • De Jonghe P., et al. Further evidence that neurofilament light chain mutations can cause Charcot-Marie-Tooth disease type 2E. Ann. Neurol. 49 (2001) 245-249
    • (2001) Ann. Neurol. , vol.49 , pp. 245-249
    • De Jonghe, P.1
  • 101
    • 0036849511 scopus 로고    scopus 로고
    • Charcot-Marie-Tooth disease neurofilament mutations disrupt neurofilament assembly and axonal transport
    • Brownlees J., et al. Charcot-Marie-Tooth disease neurofilament mutations disrupt neurofilament assembly and axonal transport. Hum. Mol. Gen. 11 (2002) 2837-2844
    • (2002) Hum. Mol. Gen. , vol.11 , pp. 2837-2844
    • Brownlees, J.1
  • 102
    • 18844446126 scopus 로고    scopus 로고
    • Mutations in the neurofilament light gene linked to Charcot-Marie-Tooth disease cause defects in transport
    • Perez-Olle R., et al. Mutations in the neurofilament light gene linked to Charcot-Marie-Tooth disease cause defects in transport. J. Neurochem. 93 (2005) 861-874
    • (2005) J. Neurochem. , vol.93 , pp. 861-874
    • Perez-Olle, R.1
  • 103
    • 0025345913 scopus 로고
    • Relative abundance of tau and neurofilament epitopes in hippocampal neurofibrillary tangles
    • Schmidt M.L., et al. Relative abundance of tau and neurofilament epitopes in hippocampal neurofibrillary tangles. Am. J. Pathol. 136 (1990) 1069-1075
    • (1990) Am. J. Pathol. , vol.136 , pp. 1069-1075
    • Schmidt, M.L.1
  • 104
    • 0038509194 scopus 로고    scopus 로고
    • Frontotemporal and motor neurone degeneration with neurofilament inclusion bodies: additional evidence for overlap between FTD and ALS
    • Bigio E.H., et al. Frontotemporal and motor neurone degeneration with neurofilament inclusion bodies: additional evidence for overlap between FTD and ALS. Neuropathol. Appl. Neurobiol. 29 (2003) 239-253
    • (2003) Neuropathol. Appl. Neurobiol. , vol.29 , pp. 239-253
    • Bigio, E.H.1
  • 105
    • 4444255628 scopus 로고    scopus 로고
    • a-Internexin aggregates are abundant in neuronal intermediate filament inclusion disease (NIFID) but rare in other neurodegenerative disease
    • Cairns N.J., et al. a-Internexin aggregates are abundant in neuronal intermediate filament inclusion disease (NIFID) but rare in other neurodegenerative disease. Acta Neuropathol. 108 (2004) 213-223
    • (2004) Acta Neuropathol. , vol.108 , pp. 213-223
    • Cairns, N.J.1
  • 106
    • 0033763056 scopus 로고    scopus 로고
    • The gene encoding gigaxonin, a new member of the cytoskeletal BTB/kelch repeat family, is mutated in giant axonal neuropathy
    • Bomont P., et al. The gene encoding gigaxonin, a new member of the cytoskeletal BTB/kelch repeat family, is mutated in giant axonal neuropathy. Nat. Genet. 26 (2000) 370-374
    • (2000) Nat. Genet. , vol.26 , pp. 370-374
    • Bomont, P.1
  • 107
    • 0030041802 scopus 로고    scopus 로고
    • Aggregation of a subpopulation of vimentin filaments in cultured human skin fibroblasts derived from patients with giant axonal neuropathy
    • Bousquet O., et al. Aggregation of a subpopulation of vimentin filaments in cultured human skin fibroblasts derived from patients with giant axonal neuropathy. Cell Motil. Cytoskeleton 33 (1996) 115-129
    • (1996) Cell Motil. Cytoskeleton , vol.33 , pp. 115-129
    • Bousquet, O.1
  • 108
    • 0024316666 scopus 로고
    • Giant axonal neuropathy: intermediate filament disease with involvement of the peripheral and central nervous system
    • Buissonniere R.F., et al. Giant axonal neuropathy: intermediate filament disease with involvement of the peripheral and central nervous system. Rev. Neurol. 145 (1989) 355-361
    • (1989) Rev. Neurol. , vol.145 , pp. 355-361
    • Buissonniere, R.F.1
  • 109
    • 0025365347 scopus 로고
    • Reduced myelinated fiber size correlates with loss of axonal neurofilaments in peripheral nerve of chronically streptozotocin diabetic rats
    • Yagihashi S., et al. Reduced myelinated fiber size correlates with loss of axonal neurofilaments in peripheral nerve of chronically streptozotocin diabetic rats. Am. J. Pathol. 136 (1990) 1365-1373
    • (1990) Am. J. Pathol. , vol.136 , pp. 1365-1373
    • Yagihashi, S.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.