메뉴 건너뛰기




Volumn 315, Issue 7, 2009, Pages 1260-1272

Properties of astrocytes cultured from GFAP over-expressing and GFAP mutant mice

Author keywords

Alexander disease; Astrocytes; Glial fibrillary acidic protein (GFAP); Rosenthal fiber (RF)

Indexed keywords

GLIAL FIBRILLARY ACIDIC PROTEIN; PROTEASOME;

EID: 63049138899     PISSN: 00144827     EISSN: 10902422     Source Type: Journal    
DOI: 10.1016/j.yexcr.2008.12.012     Document Type: Article
Times cited : (43)

References (64)
  • 3
    • 0000879584 scopus 로고
    • Progressive fibrinoid degeneration of fibrillary astrocytes associated with mental retardation in a hydrocephalic infant
    • Alexander W.S. Progressive fibrinoid degeneration of fibrillary astrocytes associated with mental retardation in a hydrocephalic infant. Brain 72 (1949) 373-381
    • (1949) Brain , vol.72 , pp. 373-381
    • Alexander, W.S.1
  • 4
    • 0024521440 scopus 로고
    • B-Crystallin is expressed in non-lenticular tissues and accumulates in Alexander's disease brain
    • Iwaki T., Kume-Iwaki A., Liem R.K.H., and Goldman J.E. B-Crystallin is expressed in non-lenticular tissues and accumulates in Alexander's disease brain. Cell 57 (1989) 71-78
    • (1989) Cell , vol.57 , pp. 71-78
    • Iwaki, T.1    Kume-Iwaki, A.2    Liem, R.K.H.3    Goldman, J.E.4
  • 5
    • 0024446498 scopus 로고
    • On-grid immunogold labeling of glial intermediate filaments in epoxy-embedded tissue
    • Johnson A.B., and Bettica A. On-grid immunogold labeling of glial intermediate filaments in epoxy-embedded tissue. Am. J. Anat. 185 (1989) 335-341
    • (1989) Am. J. Anat. , vol.185 , pp. 335-341
    • Johnson, A.B.1    Bettica, A.2
  • 6
    • 0027724243 scopus 로고
    • Overexpression and abnormal modification of the stress proteins alpha B-crystallin and HSP27 in Alexander disease
    • Head M.W., Corbin E., and Goldman J.E. Overexpression and abnormal modification of the stress proteins alpha B-crystallin and HSP27 in Alexander disease. Am. J. Pathol. 143 (1993) 1743-1753
    • (1993) Am. J. Pathol. , vol.143 , pp. 1743-1753
    • Head, M.W.1    Corbin, E.2    Goldman, J.E.3
  • 8
    • 33644642950 scopus 로고    scopus 로고
    • Plectin regulates the organization of glial fibrillary acidic protein in Alexander disease
    • Tian R.J., Gregor M., Wiche G., and Goldman J.E. Plectin regulates the organization of glial fibrillary acidic protein in Alexander disease. Am. J. Pathol. 168 (2006) 888-897
    • (2006) Am. J. Pathol. , vol.168 , pp. 888-897
    • Tian, R.J.1    Gregor, M.2    Wiche, G.3    Goldman, J.E.4
  • 9
    • 0000704819 scopus 로고
    • Über eine eigenthümliche, mit syringomyelie complicirte geschwulst des rückenmarks
    • Rosenthal W. Über eine eigenthümliche, mit syringomyelie complicirte geschwulst des rückenmarks. Bietr. Pathol. Anat. 23 (1898) 111-143
    • (1898) Bietr. Pathol. Anat. , vol.23 , pp. 111-143
    • Rosenthal, W.1
  • 10
    • 0014864757 scopus 로고
    • Light and electron microscopic observations on Rosenthal fibers in Alexander's disease and in multiple sclerosis
    • Herndon R.M., Rubinstein L.J., Freeman J.M., and Mathieson G. Light and electron microscopic observations on Rosenthal fibers in Alexander's disease and in multiple sclerosis. J. Neuropathol. Exp. Neurol. 29 (1970) 524-551
    • (1970) J. Neuropathol. Exp. Neurol. , vol.29 , pp. 524-551
    • Herndon, R.M.1    Rubinstein, L.J.2    Freeman, J.M.3    Mathieson, G.4
  • 11
    • 0345478038 scopus 로고
    • Rosenthal fibres in tumours of the central nervous system
    • Grcevic N., and Yates P.O. Rosenthal fibres in tumours of the central nervous system. J. Path. Bact. 73 (1957) 467-472
    • (1957) J. Path. Bact. , vol.73 , pp. 467-472
    • Grcevic, N.1    Yates, P.O.2
  • 12
    • 33750576890 scopus 로고    scopus 로고
    • Neuropathology for the neuroradiologist: Rosenthal fibers
    • Wippold F.J., Perry A., and Lennerz J. Neuropathology for the neuroradiologist: Rosenthal fibers. Am. J. Neuroradiol. 27 (2006) 958-961
    • (2006) Am. J. Neuroradiol. , vol.27 , pp. 958-961
    • Wippold, F.J.1    Perry, A.2    Lennerz, J.3
  • 15
    • 26444449807 scopus 로고    scopus 로고
    • Models of Alexander disease
    • Lazzarini R.A. (Ed), Elsevier, Amsterdam
    • Messing A., and Brenner M. Models of Alexander disease. In: Lazzarini R.A. (Ed). Myelin Biology and Disorders 2 (2004), Elsevier, Amsterdam 1115-1124
    • (2004) Myelin Biology and Disorders , vol.2 , pp. 1115-1124
    • Messing, A.1    Brenner, M.2
  • 18
    • 0032956263 scopus 로고    scopus 로고
    • Formation of GFAP cytoplasmic inclusions in astrocytes and their disaggregation by αB-crystallin
    • Koyama Y., and Goldman J.E. Formation of GFAP cytoplasmic inclusions in astrocytes and their disaggregation by αB-crystallin. Am. J. Pathol. 154 (1999) 1563-1572
    • (1999) Am. J. Pathol. , vol.154 , pp. 1563-1572
    • Koyama, Y.1    Goldman, J.E.2
  • 19
    • 19444366359 scopus 로고    scopus 로고
    • Alexander-disease mutation of GFAP causes filament disorganization and decreased solubility of GFAP
    • Hsiao V.C., Tian R., Long H., Der Perng M., Brenner M., Quinlan R.A., and Goldman J.E. Alexander-disease mutation of GFAP causes filament disorganization and decreased solubility of GFAP. J. Cell Sci. 118 (2005) 2057-2065
    • (2005) J. Cell Sci. , vol.118 , pp. 2057-2065
    • Hsiao, V.C.1    Tian, R.2    Long, H.3    Der Perng, M.4    Brenner, M.5    Quinlan, R.A.6    Goldman, J.E.7
  • 20
    • 33746485560 scopus 로고    scopus 로고
    • The Alexander disease-causing GFAP mutant, R416W, accumulates into Rosenthal fibers by a pathway involving filament aggregation and the association of αB-crystallin and HSP27
    • Perng M.D., Su M., Wen S.F., Li R., Gibbon T., Prescott A.R., Brenner M., and Quinlan R.A. The Alexander disease-causing GFAP mutant, R416W, accumulates into Rosenthal fibers by a pathway involving filament aggregation and the association of αB-crystallin and HSP27. Am. J. Hum. Genet. 79 (2006) 197-213
    • (2006) Am. J. Hum. Genet. , vol.79 , pp. 197-213
    • Perng, M.D.1    Su, M.2    Wen, S.F.3    Li, R.4    Gibbon, T.5    Prescott, A.R.6    Brenner, M.7    Quinlan, R.A.8
  • 21
    • 33846002775 scopus 로고    scopus 로고
    • Synergistic effects of the SAPK/JNK and the proteasome pathway on glial fibrillary acidic protein (GFAP) accumulation in Alexander disease
    • Tang G., Xu Z., and Goldman J.E. Synergistic effects of the SAPK/JNK and the proteasome pathway on glial fibrillary acidic protein (GFAP) accumulation in Alexander disease. J. Biol. Chem. 281 (2006) 38634-38643
    • (2006) J. Biol. Chem. , vol.281 , pp. 38634-38643
    • Tang, G.1    Xu, Z.2    Goldman, J.E.3
  • 22
    • 33751073409 scopus 로고    scopus 로고
    • Alexander disease-associated glial fibrillary acidic protein mutations in mice induce Rosenthal fiber formation and a white matter stress response
    • Hagemann T.L., Connor J.X., and Messing A. Alexander disease-associated glial fibrillary acidic protein mutations in mice induce Rosenthal fiber formation and a white matter stress response. J. Neurosci. 26 (2006) 11162-11173
    • (2006) J. Neurosci. , vol.26 , pp. 11162-11173
    • Hagemann, T.L.1    Connor, J.X.2    Messing, A.3
  • 23
    • 33947542997 scopus 로고    scopus 로고
    • The murine model of Alexander disease: analysis of GFAP aggregate formation and its pathological significance
    • Tanaka K.F., Takebayashi H., Yamazaki Y., Ono K., Naruse M., Iwasato T., Itohara S., Kato H., and Ikenaka K. The murine model of Alexander disease: analysis of GFAP aggregate formation and its pathological significance. Glia 55 (2007) 617-631
    • (2007) Glia , vol.55 , pp. 617-631
    • Tanaka, K.F.1    Takebayashi, H.2    Yamazaki, Y.3    Ono, K.4    Naruse, M.5    Iwasato, T.6    Itohara, S.7    Kato, H.8    Ikenaka, K.9
  • 24
    • 26444621444 scopus 로고    scopus 로고
    • Gene expression analysis in mice with elevated glial fibrillary acidic protein and Rosenthal fibers reveals a stress response followed by glial activation and neuronal dysfunction
    • Hagemann T.L., Gaeta S.A., Smith M.A., Johnson D.A., Johnson J.A., and Messing A. Gene expression analysis in mice with elevated glial fibrillary acidic protein and Rosenthal fibers reveals a stress response followed by glial activation and neuronal dysfunction. Hum. Mol. Genet. 14 (2005) 2443-2458
    • (2005) Hum. Mol. Genet. , vol.14 , pp. 2443-2458
    • Hagemann, T.L.1    Gaeta, S.A.2    Smith, M.A.3    Johnson, D.A.4    Johnson, J.A.5    Messing, A.6
  • 25
    • 0032146766 scopus 로고    scopus 로고
    • Astrocytes cultured from transgenic mice carrying the added human glial fibrillary acidic protein gene contain Rosenthal fibers
    • Eng L.F., Lee Y.L., Kwan H., Brenner M., and Messing A. Astrocytes cultured from transgenic mice carrying the added human glial fibrillary acidic protein gene contain Rosenthal fibers. J. Neurosci. Res. 53 (1998) 353-360
    • (1998) J. Neurosci. Res. , vol.53 , pp. 353-360
    • Eng, L.F.1    Lee, Y.L.2    Kwan, H.3    Brenner, M.4    Messing, A.5
  • 26
    • 0025976155 scopus 로고
    • Mutant keratin expression in transgenic mice causes marked abnormalities resembling a human genetic skin disease
    • Vassar R., Coulombe P.A., Degenstein L., Albers K., and Fuchs E. Mutant keratin expression in transgenic mice causes marked abnormalities resembling a human genetic skin disease. Cell 64 (1991) 365-380
    • (1991) Cell , vol.64 , pp. 365-380
    • Vassar, R.1    Coulombe, P.A.2    Degenstein, L.3    Albers, K.4    Fuchs, E.5
  • 27
    • 19744363995 scopus 로고    scopus 로고
    • Pathogenic effects of a novel heterozygous R350P desmin mutation on the assembly of desmin intermediate filaments in vivo and in vitro
    • Bär H., Fischer D., Goudeau B., Kley R.A., Clemen C.S., Vicart P., Herrmann H., Borgerd M., and Schröder R. Pathogenic effects of a novel heterozygous R350P desmin mutation on the assembly of desmin intermediate filaments in vivo and in vitro. Hum. Mol. Genet. 14 (2005) 1251-1260
    • (2005) Hum. Mol. Genet. , vol.14 , pp. 1251-1260
    • Bär, H.1    Fischer, D.2    Goudeau, B.3    Kley, R.A.4    Clemen, C.S.5    Vicart, P.6    Herrmann, H.7    Borgerd, M.8    Schröder, R.9
  • 29
    • 44349107112 scopus 로고    scopus 로고
    • Autophagy induced by Alexander disease-mutant GFAP accumulation is regulated by p38/MAPK and mTOR signaling pathways
    • Tang G., Yue Z., Talloczy Z., Hagemann T., Cho W., Messing A., Sulzer D.L., and Goldman J.E. Autophagy induced by Alexander disease-mutant GFAP accumulation is regulated by p38/MAPK and mTOR signaling pathways. Hum. Mol. Genet. 17 (2008) 1540-1555
    • (2008) Hum. Mol. Genet. , vol.17 , pp. 1540-1555
    • Tang, G.1    Yue, Z.2    Talloczy, Z.3    Hagemann, T.4    Cho, W.5    Messing, A.6    Sulzer, D.L.7    Goldman, J.E.8
  • 31
    • 0021353436 scopus 로고
    • Growth kinetics, cell shape, and the cytoskeleton of primary astrocyte cultures
    • Goldman J.E., and Chiu F.C. Growth kinetics, cell shape, and the cytoskeleton of primary astrocyte cultures. J. Neurochem. 42 (1984) 175-184
    • (1984) J. Neurochem. , vol.42 , pp. 175-184
    • Goldman, J.E.1    Chiu, F.C.2
  • 32
    • 0025024730 scopus 로고
    • Cyclic AMP-induced shape changes of astrocytes are accompanied by rapid depolymerization of actin
    • Goldman J.E., and Abramson B. Cyclic AMP-induced shape changes of astrocytes are accompanied by rapid depolymerization of actin. Brain Res. 528 (1990) 189-196
    • (1990) Brain Res. , vol.528 , pp. 189-196
    • Goldman, J.E.1    Abramson, B.2
  • 33
    • 0031929760 scopus 로고    scopus 로고
    • Vinculin knockout results in heart and brain defects during embryonic development
    • Xu W.M., Baribault H., and Adamson E.D. Vinculin knockout results in heart and brain defects during embryonic development. Development 125 (1998) 327-337
    • (1998) Development , vol.125 , pp. 327-337
    • Xu, W.M.1    Baribault, H.2    Adamson, E.D.3
  • 35
    • 33947687584 scopus 로고    scopus 로고
    • The functional alteration of mutant GFAP depends on the location of the domain: morphological and functional studies using astrocytoma-derived cells
    • Yoshida T., Tomozawa Y., Arisato T., Okamoto Y., Hirano H., and Nakagawa M. The functional alteration of mutant GFAP depends on the location of the domain: morphological and functional studies using astrocytoma-derived cells. J. Hum. Genet. 52 (2007) 362-369
    • (2007) J. Hum. Genet. , vol.52 , pp. 362-369
    • Yoshida, T.1    Tomozawa, Y.2    Arisato, T.3    Okamoto, Y.4    Hirano, H.5    Nakagawa, M.6
  • 38
    • 0026694490 scopus 로고
    • Alpha B-crystallin in cardiac tissue. Association with actin and desmin filaments
    • Bennardini F., Wrzosek A., and Chiesi M. Alpha B-crystallin in cardiac tissue. Association with actin and desmin filaments. Circ. Res. 71 (1992) 288-294
    • (1992) Circ. Res. , vol.71 , pp. 288-294
    • Bennardini, F.1    Wrzosek, A.2    Chiesi, M.3
  • 39
    • 0028176579 scopus 로고
    • Chaperone activity of α-crystallins modulates intermediate filament assembly
    • Nicholl I.D., and Quinlan R.A. Chaperone activity of α-crystallins modulates intermediate filament assembly. EMBO J. 13 (1994) 945-953
    • (1994) EMBO J. , vol.13 , pp. 945-953
    • Nicholl, I.D.1    Quinlan, R.A.2
  • 40
    • 33749322941 scopus 로고    scopus 로고
    • Redistribution of GFAP and αB-crystallin after thermal stress in C6 glioma cell line
    • Tseng W.C., Lu K.S., Lee W.C., and Chien C.L. Redistribution of GFAP and αB-crystallin after thermal stress in C6 glioma cell line. J. Biomed. Sci. 13 (2006) 681-694
    • (2006) J. Biomed. Sci. , vol.13 , pp. 681-694
    • Tseng, W.C.1    Lu, K.S.2    Lee, W.C.3    Chien, C.L.4
  • 42
    • 0027183871 scopus 로고
    • Transfection of human astrocytoma cells with glial fibrillary acidic protein complementary DNA: analysis of expression, proliferation, and tumorigenicity
    • Rutka J.T., and Smith S.L. Transfection of human astrocytoma cells with glial fibrillary acidic protein complementary DNA: analysis of expression, proliferation, and tumorigenicity. Cancer Res. 53 (1993) 3624-3631
    • (1993) Cancer Res. , vol.53 , pp. 3624-3631
    • Rutka, J.T.1    Smith, S.L.2
  • 43
    • 0028264312 scopus 로고
    • Effects of antisense glial fibrillary acidic protein complementary DNA on the growth, invasion, and adhesion of human astrocytoma cells
    • Rutka J.T., Hubbard S.L., Fukuyama K., Matsuzawa K., Dirks P.B., and Becker L.E. Effects of antisense glial fibrillary acidic protein complementary DNA on the growth, invasion, and adhesion of human astrocytoma cells. Cancer Res. 54 (1994) 3267-3272
    • (1994) Cancer Res. , vol.54 , pp. 3267-3272
    • Rutka, J.T.1    Hubbard, S.L.2    Fukuyama, K.3    Matsuzawa, K.4    Dirks, P.B.5    Becker, L.E.6
  • 44
    • 0032927737 scopus 로고    scopus 로고
    • Suppression of glial tumor growth by expression of glial fibrillary acidic protein
    • Toda M., Miura M., Asou H., Sugiyama I., Kawase T., and Uyemura K. Suppression of glial tumor growth by expression of glial fibrillary acidic protein. Neurochem. Res. 24 (1999) 339-343
    • (1999) Neurochem. Res. , vol.24 , pp. 339-343
    • Toda, M.1    Miura, M.2    Asou, H.3    Sugiyama, I.4    Kawase, T.5    Uyemura, K.6
  • 45
    • 0031814670 scopus 로고    scopus 로고
    • GFAP-deficient astrocytes are capable of stellation in vitro when cocultured with neurons and exhibit a reduced amount of intermediate filaments and an increased saturation density
    • Pekny M., Eliasson C., Chien C.L., Kindblom L.G., Liem R., Hamberger A., and Betsholtz C. GFAP-deficient astrocytes are capable of stellation in vitro when cocultured with neurons and exhibit a reduced amount of intermediate filaments and an increased saturation density. Exp. Cell Res. 239 (1998) 332-343
    • (1998) Exp. Cell Res. , vol.239 , pp. 332-343
    • Pekny, M.1    Eliasson, C.2    Chien, C.L.3    Kindblom, L.G.4    Liem, R.5    Hamberger, A.6    Betsholtz, C.7
  • 46
    • 44449140379 scopus 로고    scopus 로고
    • Providing cellular signposts-post-translational modifications of intermediate filaments
    • Hyder C.L., Pallari H.M., Kochin V., and Eriksson J.E. Providing cellular signposts-post-translational modifications of intermediate filaments. FEBS Lett. 582 (2008) 2140-2148
    • (2008) FEBS Lett. , vol.582 , pp. 2140-2148
    • Hyder, C.L.1    Pallari, H.M.2    Kochin, V.3    Eriksson, J.E.4
  • 47
    • 0025801842 scopus 로고
    • Specific localization of phosphointermediate filament protein in the constricted area of dividing cells
    • Nishizawa K., Yano T., Shibata M., Ando S., Takahashi T., and Inagaki M. Specific localization of phosphointermediate filament protein in the constricted area of dividing cells. J. Biol. Chem. 266 (1991) 3074-3079
    • (1991) J. Biol. Chem. , vol.266 , pp. 3074-3079
    • Nishizawa, K.1    Yano, T.2    Shibata, M.3    Ando, S.4    Takahashi, T.5    Inagaki, M.6
  • 48
    • 33745628320 scopus 로고    scopus 로고
    • A disease- and phosphorylation-related nonmechanical function for keratin 8
    • Ku N.O., and Omary M.B. A disease- and phosphorylation-related nonmechanical function for keratin 8. J. Cell Biol. 174 (2006) 115-125
    • (2006) J. Cell Biol. , vol.174 , pp. 115-125
    • Ku, N.O.1    Omary, M.B.2
  • 49
    • 0030929849 scopus 로고    scopus 로고
    • Phosphorylation of glial fibrillary acidic protein at the same sites by cleavage furrow kinase and Rho-associated kinase
    • Kosako H., Amano M., Yanagida M., Tanabe K., Nishi Y., Kaibuchi K., and Inagaki M. Phosphorylation of glial fibrillary acidic protein at the same sites by cleavage furrow kinase and Rho-associated kinase. J. Biol. Chem. 272 (1997) 10333-10336
    • (1997) J. Biol. Chem. , vol.272 , pp. 10333-10336
    • Kosako, H.1    Amano, M.2    Yanagida, M.3    Tanabe, K.4    Nishi, Y.5    Kaibuchi, K.6    Inagaki, M.7
  • 51
    • 33751509047 scopus 로고    scopus 로고
    • 14-3-3 gamma affects dynamics and integrity of glial filaments by binding to phosphorylated GFAP
    • Li H.H. 14-3-3 gamma affects dynamics and integrity of glial filaments by binding to phosphorylated GFAP. J. Cell Sci. 119 (2006) 4452-4461
    • (2006) J. Cell Sci. , vol.119 , pp. 4452-4461
    • Li, H.H.1
  • 52
    • 33745003902 scopus 로고    scopus 로고
    • A keratin cytoskeletal protein regulates protein synthesis and epithelial cell growth
    • Kim S., Wong P., and Coulombe P.A. A keratin cytoskeletal protein regulates protein synthesis and epithelial cell growth. Nature 441 (2006) 362-365
    • (2006) Nature , vol.441 , pp. 362-365
    • Kim, S.1    Wong, P.2    Coulombe, P.A.3
  • 53
    • 0035844174 scopus 로고    scopus 로고
    • The small heat shock protein αB-crystallin negatively regulates cytochrome c- and caspase-8-dependent activation of caspase-3 by inhibiting its autoproteolytic maturation
    • Kamradt M.C., Chen F., and Cryns V.L. The small heat shock protein αB-crystallin negatively regulates cytochrome c- and caspase-8-dependent activation of caspase-3 by inhibiting its autoproteolytic maturation. J. Biol. Chem. 276 (2001) 16059-16063
    • (2001) J. Biol. Chem. , vol.276 , pp. 16059-16063
    • Kamradt, M.C.1    Chen, F.2    Cryns, V.L.3
  • 54
    • 2442681777 scopus 로고    scopus 로고
    • Human αA- and αB-crystallins bind to Bax and Bcl-Xs to sequester their translocation during staurosporine-induced apoptosis
    • Mao Y.W., Liu J.P., Xiang H., and Li D.W. Human αA- and αB-crystallins bind to Bax and Bcl-Xs to sequester their translocation during staurosporine-induced apoptosis. Cell Death Differ. 11 (2004) 512-526
    • (2004) Cell Death Differ. , vol.11 , pp. 512-526
    • Mao, Y.W.1    Liu, J.P.2    Xiang, H.3    Li, D.W.4
  • 55
    • 24344508124 scopus 로고    scopus 로고
    • Calcium-activated RAF/MEK/ERK signaling pathway mediates p53-dependent apoptosis and is abrogated by αB-crystallin through inhibition of RAS activation
    • Li D.W., Liu J.P., Mao Y.W., Xiang H., Wang J., Ma W.Y., Dong Z., Pike H.M., Brown R.E., and Reed J.C. Calcium-activated RAF/MEK/ERK signaling pathway mediates p53-dependent apoptosis and is abrogated by αB-crystallin through inhibition of RAS activation. Mol. Biol. Cell 16 (2005) 4437-4453
    • (2005) Mol. Biol. Cell , vol.16 , pp. 4437-4453
    • Li, D.W.1    Liu, J.P.2    Mao, Y.W.3    Xiang, H.4    Wang, J.5    Ma, W.Y.6    Dong, Z.7    Pike, H.M.8    Brown, R.E.9    Reed, J.C.10
  • 56
    • 33644638355 scopus 로고    scopus 로고
    • Caspase-mediated cleavage of glial fibrillary acidic protein within degenerating astrocytes of the Alzheimer's disease brain
    • Mouser P.E., Head E., Ha K.H., and Rohn T.T. Caspase-mediated cleavage of glial fibrillary acidic protein within degenerating astrocytes of the Alzheimer's disease brain. Am. J. Pathol. 168 (2006) 936-946
    • (2006) Am. J. Pathol. , vol.168 , pp. 936-946
    • Mouser, P.E.1    Head, E.2    Ha, K.H.3    Rohn, T.T.4
  • 57
    • 34250157784 scopus 로고    scopus 로고
    • Caspase-3 activation in astrocytes following postnatal excitotoxic damage correlates with cytoskeletal remodeling but not with cell death or proliferation
    • Acarin L., Villapol S., Faiz M., Rohn T.T., Castellano B., and Gonzalez B. Caspase-3 activation in astrocytes following postnatal excitotoxic damage correlates with cytoskeletal remodeling but not with cell death or proliferation. Glia 55 (2007) 954-965
    • (2007) Glia , vol.55 , pp. 954-965
    • Acarin, L.1    Villapol, S.2    Faiz, M.3    Rohn, T.T.4    Castellano, B.5    Gonzalez, B.6
  • 58
    • 0036097410 scopus 로고    scopus 로고
    • Apoptosis and keratin intermediate filaments
    • Oshima R.G. Apoptosis and keratin intermediate filaments. Cell Death Differ. 9 (2002) 486-492
    • (2002) Cell Death Differ. , vol.9 , pp. 486-492
    • Oshima, R.G.1
  • 59
    • 34347374872 scopus 로고    scopus 로고
    • Intermediate filament scaffolds fulfill mechanical, organizational, and signaling functions in the cytoplasm
    • Kim S., and Coulombe P.A. Intermediate filament scaffolds fulfill mechanical, organizational, and signaling functions in the cytoplasm. Genes Dev. 21 (2007) 1581-1597
    • (2007) Genes Dev. , vol.21 , pp. 1581-1597
    • Kim, S.1    Coulombe, P.A.2
  • 60
    • 14844282022 scopus 로고    scopus 로고
    • Alexander disease
    • Lazzarini R.A. (Ed), Elsevier, Amsterdam
    • Messing A., and Goldman J.E. Alexander disease. In: Lazzarini R.A. (Ed). Myelin Biology and Disorders 2 (2004), Elsevier, Amsterdam 851-866
    • (2004) Myelin Biology and Disorders , vol.2 , pp. 851-866
    • Messing, A.1    Goldman, J.E.2
  • 62
    • 0242266623 scopus 로고    scopus 로고
    • A keaper and a striker maintain epidermal homeostasis
    • Magin T.M. A keaper and a striker maintain epidermal homeostasis. Nat. Genet. 35 (2003) 202-204
    • (2003) Nat. Genet. , vol.35 , pp. 202-204
    • Magin, T.M.1
  • 64
    • 0032005805 scopus 로고    scopus 로고
    • 4-hydroxynonenal, a lipid peroxidation product, impairs glutamate transport in cortical astrocytes
    • Blanc E.M., Keller J.N., Fernandez S., and Mattson M.P. 4-hydroxynonenal, a lipid peroxidation product, impairs glutamate transport in cortical astrocytes. Glia 22 (1998) 149-160
    • (1998) Glia , vol.22 , pp. 149-160
    • Blanc, E.M.1    Keller, J.N.2    Fernandez, S.3    Mattson, M.P.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.