메뉴 건너뛰기




Volumn 223, Issue , 2002, Pages 83-175

Functional complexity of intermediate filament cytoskeletons: From structure to assembly to gene ablation

Author keywords

Diseases; IF assembly; Intermediate filaments; Multigene family

Indexed keywords

DESMIN; GLIAL FIBRILLARY ACIDIC PROTEIN; INTERMEDIATE FILAMENT PROTEIN; KERATIN; LAMIN B; NUCLEAR PROTEIN; TETRAMER; VIMENTIN;

EID: 0037282536     PISSN: 00747696     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S0074-7696(05)23003-6     Document Type: Article
Times cited : (171)

References (441)
  • 1
    • 0025076790 scopus 로고
    • A single human keratin 18 gene is expressed in diverse epithelial cells of transgenic mice
    • Abe, M., and Oshima, R. G. (1990). A single human keratin 18 gene is expressed in diverse epithelial cells of transgenic mice. J. Cell Biol. 111, 1197-1206.
    • (1990) J. Cell Biol. , vol.111 , pp. 1197-1206
    • Abe, M.1    Oshima, R.G.2
  • 2
    • 0032215129 scopus 로고    scopus 로고
    • The pathway of assembly of intermediate filaments from recombinant α-internexin
    • Abumuhor, I. A., Spencer, P. H., and Cohlberg, J. A. (1998). The pathway of assembly of intermediate filaments from recombinant α-internexin. J. Struct. Biol. 123, 187-198.
    • (1998) J. Struct. Biol. , vol.123 , pp. 187-198
    • Abumuhor, I.A.1    Spencer, P.H.2    Cohlberg, J.A.3
  • 3
    • 0022519369 scopus 로고
    • The nuclear lamina is a meshwork of intermediate-type filaments
    • Aebi, U., Cohn, J., Buhle, L., and Gerace, L. (1986). The nuclear lamina is a meshwork of intermediate-type filaments. Nature 323, 560-564.
    • (1986) Nature , vol.323 , pp. 560-564
    • Aebi, U.1    Cohn, J.2    Buhle, L.3    Gerace, L.4
  • 5
    • 0028836521 scopus 로고
    • Expression of an epidermal keratin protein in liver of transgenic mice causes structural and functional abnormalities
    • Albers, K. M., Davis, F. E., Perrone, T. N., Lee, E. Y., Liu, Y., and Vore, M. (1995). Expression of an epidermal keratin protein in liver of transgenic mice causes structural and functional abnormalities. J. Cell Biol. 128, 157-169.
    • (1995) J. Cell Biol. , vol.128 , pp. 157-169
    • Albers, K.M.1    Davis, F.E.2    Perrone, T.N.3    Lee, E.Y.4    Liu, Y.5    Vore, M.6
  • 7
    • 0035110609 scopus 로고    scopus 로고
    • Anomalous apical plasma membrane phenotype in CK8-deficient mice indicates a novel role for intermediate filaments in the polarization of simple epithelia
    • Ameen, N. A., Figueroa, Y., and Salas, P. J. (2001). Anomalous apical plasma membrane phenotype in CK8-deficient mice indicates a novel role for intermediate filaments in the polarization of simple epithelia. J. Cell. Sci. 114, 563-575.
    • (2001) J. Cell. Sci. , vol.114 , pp. 563-575
    • Ameen, N.A.1    Figueroa, Y.2    Salas, P.J.3
  • 8
    • 0030721040 scopus 로고    scopus 로고
    • Targeted inactivation of plectin reveals essential function in maintaining the integrity of skin, muscle and heart cytoarchitecture
    • Andrä, K., Lassmann, H., Bittner, R., Shorny, S., Fässler, R., Propst, R., and Wiche, G. (1997). Targeted inactivation of plectin reveals essential function in maintaining the integrity of skin, muscle and heart cytoarchitecture. Genes Dev. 11, 3143-3156.
    • (1997) Genes Dev. , vol.11 , pp. 3143-3156
    • Andrä, K.1    Lassmann, H.2    Bittner, R.3    Shorny, S.4    Fässler, R.5    Propst, R.6    Wiche, G.7
  • 9
    • 0035809167 scopus 로고    scopus 로고
    • Focal activation of a mutant allele defines the role of stem cells in mosaic skin disorders
    • Arin, M., Longley, M., Wang, X., and Roop, D. (2001). Focal activation of a mutant allele defines the role of stem cells in mosaic skin disorders. J. Cell Biol. 152, 645-650.
    • (2001) J. Cell Biol. , vol.152 , pp. 645-650
    • Arin, M.1    Longley, M.2    Wang, X.3    Roop, D.4
  • 10
    • 0035901594 scopus 로고    scopus 로고
    • c-Myc activation in transgenic mouse epidermis results in mobilization of stem cells and differentiation of their progeny
    • Arnold, I., and Watt, F. M. (2001). c-Myc activation in transgenic mouse epidermis results in mobilization of stem cells and differentiation of their progeny. Curr. Biol. 11, 558-568.
    • (2001) Curr. Biol. , vol.11 , pp. 558-568
    • Arnold, I.1    Watt, F.M.2
  • 11
    • 0025337552 scopus 로고
    • Immunocytochemical localization of desmin at human neuromuscular junctions
    • Askanas, V., Bornemann, A., and Engel, W. K. (1990). Immunocytochemical localization of desmin at human neuromuscular junctions. Neurology 40, 949-953.
    • (1990) Neurology , vol.40 , pp. 949-953
    • Askanas, V.1    Bornemann, A.2    Engel, W.K.3
  • 12
    • 0025674247 scopus 로고
    • Cell type-specific and efficient synthesis of human cytokeratin 19 in transgenic mice
    • Bader, B. L., and Franke, W. W. (1990). Cell type-specific and efficient synthesis of human cytokeratin 19 in transgenic mice. Differentiation. 45, 109-118.
    • (1990) Differentiation , vol.45 , pp. 109-118
    • Bader, B.L.1    Franke, W.W.2
  • 13
    • 0025718837 scopus 로고
    • Intermediate filaments formed de novo from tailless cytokerytin in the cytoplasm and in the nucleus
    • Bader, B., Magin, T. M., Freudenmann, M., Stumpp, S., and Franke, W. W. (1991). Intermediate filaments formed de novo from tailless cytokerytin in the cytoplasm and in the nucleus. J. Cell Biol. 115, 1293-1307.
    • (1991) J. Cell Biol. , vol.115 , pp. 1293-1307
    • Bader, B.1    Magin, T.M.2    Freudenmann, M.3    Stumpp, S.4    Franke, W.W.5
  • 14
    • 0027227464 scopus 로고
    • Mid-gestational lethality in mice lacking keratin 8
    • Baribault, H., Price, J., Miyai, K., and Oshima, R. G. (1993). Mid-gestational lethality in mice lacking keratin 8. Genes Dev. 7, 1191-1202.
    • (1993) Genes Dev. , vol.7 , pp. 1191-1202
    • Baribault, H.1    Price, J.2    Miyai, K.3    Oshima, R.G.4
  • 15
    • 0028607055 scopus 로고
    • Colorectal hyperplasia and inflammation in keratin 8-deficient FVB/N mice
    • Baribault, H., Penner, J., Iozzo, R. V., and Wilson, H. M. (1994). Colorectal hyperplasia and inflammation in keratin 8-deficient FVB/N mice. Genes Dev. 8, 2964-2973.
    • (1994) Genes Dev. , vol.8 , pp. 2964-2973
    • Baribault, H.1    Penner, J.2    Iozzo, R.V.3    Wilson, H.M.4
  • 16
    • 0002501274 scopus 로고
    • Widespread occurrence of intermediate filaments in invertebrates; common principles and aspects of diversion
    • Bartnik, E., and Weber, K. (1989). Widespread occurrence of intermediate filaments in invertebrates; common principles and aspects of diversion. Eur. J. Cell Biol. 50, 17-33.
    • (1989) Eur. J. Cell Biol. , vol.50 , pp. 17-33
    • Bartnik, E.1    Weber, K.2
  • 18
    • 0035132933 scopus 로고    scopus 로고
    • A unique type I keratin intermediate filament gene family is abundantly expressed in the inner root sheaths of sheep and human hair follicles
    • Bawden, C. S., McLaughlan, C., Nesci, A., and Rogers, G. (2001). A unique type I keratin intermediate filament gene family is abundantly expressed in the inner root sheaths of sheep and human hair follicles. J. Invest. Dermatol. 116, 157-166.
    • (2001) J. Invest. Dermatol. , vol.116 , pp. 157-166
    • Bawden, C.S.1    McLaughlan, C.2    Nesci, A.3    Rogers, G.4
  • 19
    • 0032809052 scopus 로고    scopus 로고
    • Interactions between peripherin and neurofilaments in cultured cells: Disruption of peripherin assembly by the NF-M and NF-H subunits
    • Beaulieu, J. M., Robertson, J., and Julien, J. P. (1999). Interactions between peripherin and neurofilaments in cultured cells: Disruption of peripherin assembly by the NF-M and NF-H subunits. Biochem. Cell Biol. 77, 41-45.
    • (1999) Biochem. Cell Biol. , vol.77 , pp. 41-45
    • Beaulieu, J.M.1    Robertson, J.2    Julien, J.P.3
  • 20
    • 0034662120 scopus 로고    scopus 로고
    • Formation of intermediate filament protein aggregates with disparate effects in two transgenic mouse models lacking the neurofilament light subunit
    • Beaulieu, J. M., Jacomy, H., and Julien, J. P. (2000). Formation of intermediate filament protein aggregates with disparate effects in two transgenic mouse models lacking the neurofilament light subunit. J. Neurosci. 20, 5321-5328.
    • (2000) J. Neurosci. , vol.20 , pp. 5321-5328
    • Beaulieu, J.M.1    Jacomy, H.2    Julien, J.P.3
  • 22
    • 0032878518 scopus 로고    scopus 로고
    • Molecular characteristics and interactions of the intermediate filament protein synemin. Interactions with alpha-actinin may anchor synemin-containing heterofilaments
    • Bellin, R. M., Sernett, S. W., Becker, B., Ip, W., Huiatt, T. W., and Robson, R. M. (1999). Molecular characteristics and interactions of the intermediate filament protein synemin. Interactions with alpha-actinin may anchor synemin-containing heterofilaments. J. Biol. Chem. 274, 29493-29499.
    • (1999) J. Biol. Chem. , vol.274 , pp. 29493-29499
    • Bellin, R.M.1    Sernett, S.W.2    Becker, B.3    Ip, W.4    Huiatt, T.W.5    Robson, R.M.6
  • 23
    • 0034063280 scopus 로고    scopus 로고
    • Characterization of an inducible, epidermal-specific knockout system: Differential expression of lacZ in different Cre reporter mouse strains
    • Berton, T. R., Wang, X. J., Zhou, Z., Kellendonk, C., Schutz, G., Tsai, S., and Roop, D. R. (2000). Characterization of an inducible, epidermal-specific knockout system: Differential expression of lacZ in different Cre reporter mouse strains. Genesis 26, 160-161.
    • (2000) Genesis , vol.26 , pp. 160-161
    • Berton, T.R.1    Wang, X.J.2    Zhou, Z.3    Kellendonk, C.4    Schutz, G.5    Tsai, S.6    Roop, D.R.7
  • 24
    • 0030589631 scopus 로고    scopus 로고
    • Embryonic heart and skin defects in mice lacking plakoglobin
    • Bierkamp, C., Mclaughlin, K. J., Schwarz, H., Huber, O., and Kemler, R. (1996). Embryonic heart and skin defects in mice lacking plakoglobin. Dev. Biol. 180, 780-785.
    • (1996) Dev. Biol. , vol.180 , pp. 780-785
    • Bierkamp, C.1    Mclaughlin, K.J.2    Schwarz, H.3    Huber, O.4    Kemler, R.5
  • 25
    • 0027454775 scopus 로고
    • Ectopic synthesis of epidermal cytokeratins in pancreatic islet cells of transgenic mice interferes with cytoskeletal order and insulin production
    • Blessing, M., Rüther, U., and Franke, W. W. (1993). Ectopic synthesis of epidermal cytokeratins in pancreatic islet cells of transgenic mice interferes with cytoskeletal order and insulin production. J. Cell Biol 120, 743-755.
    • (1993) J. Cell Biol. , vol.120 , pp. 743-755
    • Blessing, M.1    Rüther, U.2    Franke, W.W.3
  • 26
    • 0023297921 scopus 로고
    • Differentially expressed bovine cytokeratin genes. Analysis of gene linkage and evolutionary conservation of 5′-upstream sequences
    • Blessing, M., Zentgraf, H., and Jorcano, J. L. (1987). Differentially expressed bovine cytokeratin genes. Analysis of gene linkage and evolutionary conservation of 5′-upstream sequences. EMBO J. 6, 567-575.
    • (1987) EMBO J. , vol.6 , pp. 567-575
    • Blessing, M.1    Zentgraf, H.2    Jorcano, J.L.3
  • 28
    • 0020512134 scopus 로고
    • Vimentin filaments are assembled from a soluble precursor in avian erythroid cells
    • Blikstad, I., and Lazarides, E. (1983). Vimentin filaments are assembled from a soluble precursor in avian erythroid cells. J. Cell Biol. 96, 1803-1808.
    • (1983) J. Cell Biol. , vol.96 , pp. 1803-1808
    • Blikstad, I.1    Lazarides, E.2
  • 31
    • 0013410311 scopus 로고    scopus 로고
    • Genome speak
    • Bork, P., and Copley, R. (2001). Genome speak. Nature 409(6822), 815.
    • (2001) Nature , vol.409 , Issue.6822 , pp. 815
    • Bork, P.1    Copley, R.2
  • 35
    • 0035163913 scopus 로고    scopus 로고
    • Mutations in GFAP, encoding glial fibrillary acidic protein, are associated with Alexander disease
    • Brenner, M., Johnson, A. B., Boespflug-Tanguy, O., Rodriguez, D., Goldman, J. E., and Messing, A. (2001). Mutations in GFAP, encoding glial fibrillary acidic protein, are associated with Alexander disease. Nat. Genet. 27, 117-120.
    • (2001) Nat. Genet. , vol.27 , pp. 117-120
    • Brenner, M.1    Johnson, A.B.2    Boespflug-Tanguy, O.3    Rodriguez, D.4    Goldman, J.E.5    Messing, A.6
  • 36
    • 0031802612 scopus 로고    scopus 로고
    • Identification of an interchromosomal compartment by polymerization of nuclear-targeted vimentin
    • Bridger, J. M., Herrmann, H., Münkel, C., and Lichter, P. (1998). Identification of an interchromosomal compartment by polymerization of nuclear-targeted vimentin. J. Cell Sci. 111, 1241-1253.
    • (1998) J. Cell Sci. , vol.111 , pp. 1241-1253
    • Bridger, J.M.1    Herrmann, H.2    Münkel, C.3    Lichter, P.4
  • 38
    • 0035335987 scopus 로고    scopus 로고
    • Rigidity of circulating lymphocytes is primarily conferred by vimentin intermediate filaments
    • Brown, M. J., Hallam, J. A., Colucci-Guyon, E., and Shaw, S. (2001a). Rigidity of circulating lymphocytes is primarily conferred by vimentin intermediate filaments. J. Immunol. 166, 6640-6646.
    • (2001) J. Immunol. , vol.166 , pp. 6640-6646
    • Brown, M.J.1    Hallam, J.A.2    Colucci-Guyon, E.3    Shaw, S.4
  • 39
    • 0035879352 scopus 로고    scopus 로고
    • Cutting edge: Integration of human T lymphocyte cytoskeleton by the cytolinker plectin
    • Brown, M. J., Hallam, J. A., Liu, Y., Yamada, K. M., and Shaw, S. (2001b). Cutting edge: Integration of human T lymphocyte cytoskeleton by the cytolinker plectin. J. Immunol. 167, 641-645.
    • (2001) J. Immunol. , vol.167 , pp. 641-645
    • Brown, M.J.1    Hallam, J.A.2    Liu, Y.3    Yamada, K.M.4    Shaw, S.5
  • 40
    • 0019312840 scopus 로고
    • Monoclonal antibodies against trophectoderm-specific markers during mouse blastocyst formation
    • Brulet, P., Babinet, C., Kemler, R., and Jacob, F. (1980). Monoclonal antibodies against trophectoderm-specific markers during mouse blastocyst formation. Proc. Natl. Acad. Sci. USA 77, 4113-4117.
    • (1980) Proc. Natl. Acad. Sci. USA , vol.77 , pp. 4113-4117
    • Brulet, P.1    Babinet, C.2    Kemler, R.3    Jacob, F.4
  • 41
    • 0034492490 scopus 로고    scopus 로고
    • Design of a minimal protein oligomerization domain by a structural approach
    • Burkhard, P., Meier, M., and Lustig, A. (2000). Design of a minimal protein oligomerization domain by a structural approach. Protein Sci. 9, 2294-2301.
    • (2000) Protein Sci. , vol.9 , pp. 2294-2301
    • Burkhard, P.1    Meier, M.2    Lustig, A.3
  • 42
    • 0035252931 scopus 로고    scopus 로고
    • Coiled coils: A highly versatile protein folding motif
    • Burkhard, P., Stetefeld, J., and Strelkov, S. V. (2001). Coiled coils: A highly versatile protein folding motif. Trends Cell Biol. 11, 82-88.
    • (2001) Trends Cell Biol. , vol.11 , pp. 82-88
    • Burkhard, P.1    Stetefeld, J.2    Strelkov, S.V.3
  • 43
    • 0032478181 scopus 로고    scopus 로고
    • A highly conserved lysine residue on the head domain of type II keratins is essential for the attachment of keratin intermediate filaments to the cornified cell envelope through isopeptide crosslinking by transglutaminases
    • Candi, E., Tarcsa, E., Digiovanna, J. J., Compton, J. G., Elias, P. M., Marekov, L. N., and Steinert, P. M. (1998). A highly conserved lysine residue on the head domain of type II keratins is essential for the attachment of keratin intermediate filaments to the cornified cell envelope through isopeptide crosslinking by transglutaminases. Proc. Natl. Acad. Sci. USA 95, 2067-2072.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 2067-2072
    • Candi, E.1    Tarcsa, E.2    Digiovanna, J.J.3    Compton, J.G.4    Elias, P.M.5    Marekov, L.N.6    Steinert, P.M.7
  • 44
    • 0035809198 scopus 로고    scopus 로고
    • An inducible mouse model for epidermolysis bullosa simplex. Implications for gene therapy
    • Cao, T., Longley, M., Wang, X., and Roop, D. (2001). An inducible mouse model for epidermolysis bullosa simplex. Implications for gene therapy. J. Cell Biol. 152, 651-656.
    • (2001) J. Cell Biol. , vol.152 , pp. 651-656
    • Cao, T.1    Longley, M.2    Wang, X.3    Roop, D.4
  • 45
    • 0032233810 scopus 로고    scopus 로고
    • Desmin cytoskeleton in muscle integrity and function
    • Capetanaki, Y., and Milner, D. J. (1998). Desmin cytoskeleton in muscle integrity and function. Subcell. Biochem. 31, 463-495.
    • (1998) Subcell. Biochem. , vol.31 , pp. 463-495
    • Capetanaki, Y.1    Milner, D.J.2
  • 46
    • 0033853845 scopus 로고    scopus 로고
    • Differences in the distribution of synemin, paranemin, and plectin in skeletal muscles of wildtype and desmin knock-out mice
    • Carlsson, L., Li, Z. L., Paulin, D., Price, M. G., Breckler, J., Robson, R. M., Wiche, G., and Thornell, L. E. (2000). Differences in the distribution of synemin, paranemin, and plectin in skeletal muscles of wildtype and desmin knock-out mice. Histochem. Cell Biol. 114, 39-47.
    • (2000) Histochem. Cell Biol. , vol.114 , pp. 39-47
    • Carlsson, L.1    Li, Z.L.2    Paulin, D.3    Price, M.G.4    Breckler, J.5    Robson, R.M.6    Wiche, G.7    Thornell, L.E.8
  • 47
    • 0024436494 scopus 로고
    • Presence of a protein immunologically related to lamin B in the postsynaptic membrane of Torpedo marmorata electrocyte
    • Cartaud, A., Courvalin, J. C., Ludosky, M. A., and Cartaud, J. (1989). Presence of a protein immunologically related to lamin B in the postsynaptic membrane of Torpedo marmorata electrocyte. J. Cell Biol. 109, 1745-1752.
    • (1989) J. Cell Biol. , vol.109 , pp. 1745-1752
    • Cartaud, A.1    Courvalin, J.C.2    Ludosky, M.A.3    Cartaud, J.4
  • 48
    • 0032570802 scopus 로고    scopus 로고
    • Neurofilament (NF) assembly; divergent characteristics of human and rodent NF-L subunits
    • Carter, J., Gragerov, A., Konvicka, K., Elder, G., Weinstein, H., and Lazzarini, R. A. (1998). Neurofilament (NF) assembly; divergent characteristics of human and rodent NF-L subunits. J. Biol. Chem. 273, 5101-5108.
    • (1998) J. Biol. Chem. , vol.273 , pp. 5101-5108
    • Carter, J.1    Gragerov, A.2    Konvicka, K.3    Elder, G.4    Weinstein, H.5    Lazzarini, R.A.6
  • 49
    • 0035313837 scopus 로고    scopus 로고
    • Gene silencing by double-stranded RNA
    • Carthew, R. W. (2001). Gene silencing by double-stranded RNA. Curr. Opin. Cell Biol. 13, 244-248.
    • (2001) Curr. Opin. Cell Biol. , vol.13 , pp. 244-248
    • Carthew, R.W.1
  • 50
    • 0028225888 scopus 로고
    • Differential organization of desmin and vimentin in muscle is due to differences in their head domains
    • Cary, R. B., and Klymkowsky, M. W. (1994a). Differential organization of desmin and vimentin in muscle is due to differences in their head domains. J. Cell Biol. 126, 445-456.
    • (1994) J. Cell Biol. , vol.126 , pp. 445-456
    • Cary, R.B.1    Klymkowsky, M.W.2
  • 51
    • 0028274143 scopus 로고
    • Desmin organization during the differentiation of the dorsal myotome in Xenopus laevis
    • Cary, R. B., and Klymkowsky, M. W. (1994b). Desmin organization during the differentiation of the dorsal myotome in Xenopus laevis. Differentiation 56, 31-38.
    • (1994) Differentiation , vol.56 , pp. 31-38
    • Cary, R.B.1    Klymkowsky, M.W.2
  • 52
    • 0028957558 scopus 로고
    • Tissue-specific and efficient expression of the human simple epithelial keratin 8 gene in transgenic mice
    • Casanova, L., Bravo, A., Were, F., Ramirez, A., Jorcano, J. J., and Vidal, M. (1995). Tissue-specific and efficient expression of the human simple epithelial keratin 8 gene in transgenic mice. J. Cell Sci. 108, 811-820.
    • (1995) J. Cell Sci. , vol.108 , pp. 811-820
    • Casanova, L.1    Bravo, A.2    Were, F.3    Ramirez, A.4    Jorcano, J.J.5    Vidal, M.6
  • 55
    • 0034599872 scopus 로고    scopus 로고
    • Keratin-dependent, epithelial resistance to tumor necrosis factor-induced apoptosis
    • Caulin, C., Ware, C. F., Magin, T. M., and Oshima, R. G. (2000). Keratin-dependent, epithelial resistance to tumor necrosis factor-induced apoptosis. J. Cell Biol. 149, 17-22.
    • (2000) J. Cell Biol. , vol.149 , pp. 17-22
    • Caulin, C.1    Ware, C.F.2    Magin, T.M.3    Oshima, R.G.4
  • 56
    • 0033228745 scopus 로고    scopus 로고
    • Mutation report: Identification of a germline mutation in keratin 17 in a family with pachyonychia congenita type 2
    • Celebi, J. T., Tanz, E. L., Yao, Y. J., Michael, E. J., and Peacocke, M. (1999). Mutation report: Identification of a germline mutation in keratin 17 in a family with pachyonychia congenita type 2. J. Invest. Dermatol. 113, 848-850.
    • (1999) J. Invest. Dermatol. , vol.113 , pp. 848-850
    • Celebi, J.T.1    Tanz, E.L.2    Yao, Y.J.3    Michael, E.J.4    Peacocke, M.5
  • 57
    • 0027943989 scopus 로고
    • A human keratin 14 "knockout": The absence of K14 leads to severe epidermolysis bullosa simplex and a function for an intermediate filament protein
    • Chan, Y., Anton, L. I., Yu, Q. C., Jackel, A., Zabel, B., Ernst, J. P., and Fuchs, E. (1994). A human keratin 14 "knockout": the absence of K14 leads to severe epidermolysis bullosa simplex and a function for an intermediate filament protein. Genes Dev. 8, 2574-2587.
    • (1994) Genes Dev. , vol.8 , pp. 2574-2587
    • Chan, Y.1    Anton, L.I.2    Yu, Q.C.3    Jackel, A.4    Zabel, B.5    Ernst, J.P.6    Fuchs, E.7
  • 58
    • 0026699760 scopus 로고
    • The genetic basis of epidermolytic hyperkeratosis: A disorder of differentiation-specific epidermal keratin genes
    • Cheng, J., Syder, A. J., Yu, Q. C., Letai, A., Paller, A. S., and Fuchs, E. (1992). The genetic basis of epidermolytic hyperkeratosis: a disorder of differentiation-specific epidermal keratin genes. Cell 70, 811-819.
    • (1992) Cell , vol.70 , pp. 811-819
    • Cheng, J.1    Syder, A.J.2    Yu, Q.C.3    Letai, A.4    Paller, A.S.5    Fuchs, E.6
  • 59
    • 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. (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.2
  • 60
    • 0026612429 scopus 로고
    • A leucine → proline mutation in the H1 subdomain of keratin 1 causes epidermolytic hyperkeratosis
    • Chipev, C. C., Korge, B. P., Markova, N., Bale, S. J., Digiovanna, J. J., Compton, J. G., and Steinert, P. M. (1992). A leucine → proline mutation in the H1 subdomain of keratin 1 causes epidermolytic hyperkeratosis. Cell 70, 821-828.
    • (1992) Cell , vol.70 , pp. 821-828
    • Chipev, C.C.1    Korge, B.P.2    Markova, N.3    Bale, S.J.4    Digiovanna, J.J.5    Compton, J.G.6    Steinert, P.M.7
  • 61
    • 0027211896 scopus 로고
    • Expression of complete keratin filaments in mouse L cells augments cell migration and invasion
    • Chu, Y. W., Runyan, R. B., Oshima, R. G., and Hendrix, M. J. (1993). Expression of complete keratin filaments in mouse L cells augments cell migration and invasion. Proc. Natl. Acad. Sci. USA 90, 4261-4265.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 4261-4265
    • Chu, Y.W.1    Runyan, R.B.2    Oshima, R.G.3    Hendrix, M.J.4
  • 62
    • 0030052431 scopus 로고    scopus 로고
    • Experimental coexpression of vimentin and keratin intermediate filaments in human melanoma cells augments motility
    • Chu, Y. W., Seftor, E. A., Romer, L. H., and Hendrix, M. J. (1996). Experimental coexpression of vimentin and keratin intermediate filaments in human melanoma cells augments motility. Am. J. Pathol, 148, 63-69.
    • (1996) Am. J. Pathol. , vol.148 , pp. 63-69
    • Chu, Y.W.1    Seftor, E.A.2    Romer, L.H.3    Hendrix, M.J.4
  • 63
    • 0033231494 scopus 로고    scopus 로고
    • From Charcot to SOD1: Mechanisms of selective motor neuron death in ALS
    • Cleveland, D. W. (1999). From Charcot to SOD1: Mechanisms of selective motor neuron death in ALS. Neuron 24, 515-520.
    • (1999) Neuron , vol.24 , pp. 515-520
    • Cleveland, D.W.1
  • 66
    • 0035146907 scopus 로고    scopus 로고
    • Transcriptional repression, apoptosis, human disease and the functional evolution of the nuclear lamina
    • Cohen, M., Lee, K. K., Wilson, K. L., and Gruenbaum, Y. (2001). Transcriptional repression, apoptosis, human disease and the functional evolution of the nuclear lamina. Trends Biochem. Sci. 26, 41-47.
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 41-47
    • Cohen, M.1    Lee, K.K.2    Wilson, K.L.3    Gruenbaum, Y.4
  • 68
    • 0026802985 scopus 로고
    • Suprabasal marker proteins distinguishing keratinizing squamous epithelia: Cytokeratin 2 polypeptides of oral masticatory epithelium and epidermis are different
    • Collin, C., Ouhayoun, J. P., Grund, C., and Franke, W. W. (1992a). Suprabasal marker proteins distinguishing keratinizing squamous epithelia: Cytokeratin 2 polypeptides of oral masticatory epithelium and epidermis are different. Differentiation 51, 137-148.
    • (1992) Differentiation , vol.51 , pp. 137-148
    • Collin, C.1    Ouhayoun, J.P.2    Grund, C.3    Franke, W.W.4
  • 69
    • 0026666391 scopus 로고
    • Characterization of human cytokeratin 2, an epidermal cytoskeletal protein synthesized late during differentiation
    • Collin, C., Moll, R., Kubicka, S., Ouhayoun, J. P., and Franke, W. W. (1992b). Characterization of human cytokeratin 2, an epidermal cytoskeletal protein synthesized late during differentiation. Exp. Cell Res. 202, 132-141.
    • (1992) Exp. Cell Res. , vol.202 , pp. 132-141
    • Collin, C.1    Moll, R.2    Kubicka, S.3    Ouhayoun, J.P.4    Franke, W.W.5
  • 70
    • 0028004289 scopus 로고
    • Mice lacking vimentin develop and reproduce without an obvious phenotype
    • Colucci-Guyon, E., Portier, M. M., Dunia, I., Paulin, D., Pournin, S., and Babinet, C. (1994). Mice lacking vimentin develop and reproduce without an obvious phenotype. Cell 79, 679-694.
    • (1994) Cell , vol.79 , pp. 679-694
    • Colucci-Guyon, E.1    Portier, M.M.2    Dunia, I.3    Paulin, D.4    Pournin, S.5    Babinet, C.6
  • 71
    • 0032889664 scopus 로고    scopus 로고
    • Cerebellar defect and impaired motor coordination in mice lacking vimentin
    • Colucci-Guyon, E., Gimenez, Y. R., Maurice, T., Babinet, C., and Privat, A. (1998). Cerebellar defect and impaired motor coordination in mice lacking vimentin. Glia 25, 33-43.
    • (1998) Glia , vol.25 , pp. 33-43
    • Colucci-Guyon, E.1    Gimenez, Y.R.2    Maurice, T.3    Babinet, C.4    Privat, A.5
  • 72
    • 33749357063 scopus 로고
    • Intermediate filament structure: 3. Analysis of sequence homologies
    • Conway, J. F., and Parry, D. A. D. (1988). Intermediate filament structure: 3. Analysis of sequence homologies. Int. J. Biol. Macromol. 10, 79-88.
    • (1988) Int. J. Biol. Macromol. , vol.10 , pp. 79-88
    • Conway, J.F.1    Parry, D.A.D.2
  • 73
    • 0030455978 scopus 로고    scopus 로고
    • Human keratin diseases: Hereditary fragility of specific epithelial tissues
    • Corden, L. D., and McLean, W. H. (1996). Human keratin diseases: hereditary fragility of specific epithelial tissues. Exp. Dermatol. 5, 297-307.
    • (1996) Exp. Dermatol. , vol.5 , pp. 297-307
    • Corden, L.D.1    McLean, W.H.2
  • 75
    • 0027465098 scopus 로고
    • Progressive neuronopathy in transgenic mice expressing the human neurofilament heavy gene: A mouse model of amyotrophic lateral sclerosis
    • Cote, F., Collard, J. F., and Julien, J. P. (1993). Progressive 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
    • Cote, F.1    Collard, J.F.2    Julien, J.P.3
  • 76
    • 0032483016 scopus 로고    scopus 로고
    • Protective effect of neurofilament heavy gene overexpression in motor neuron disease induced by mutant superoxide dismutase
    • Couillard-Despres, S., Zhu, Q., Wong, P. C., Price, D. L., Cleveland, D. W., and Julien, J. P. (1998). Protective effect of neurofilament heavy gene overexpression in motor neuron disease induced by mutant superoxide dismutase. Proc. Natl. Acad. Sci. USA 95, 9626-9630.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 9626-9630
    • Couillard-Despres, S.1    Zhu, Q.2    Wong, P.C.3    Price, D.L.4    Cleveland, D.W.5    Julien, J.P.6
  • 77
    • 0025341392 scopus 로고
    • Elucidating the early stages of keratin filament assembly
    • Coulombe, P. A., and Fuchs, E. (1990). Elucidating the early stages of keratin filament assembly. J. Cell Biol. 111, 153-169.
    • (1990) J. Cell Biol. , vol.111 , pp. 153-169
    • Coulombe, P.A.1    Fuchs, E.2
  • 78
    • 0036468732 scopus 로고    scopus 로고
    • 'Hard' and 'soft' principles defining the structure, function and regulation of keratin intermediate filaments
    • Coulombe, P. A., and Omary, M. B. (2002). 'Hard' and 'soft' principles defining the structure, function and regulation of keratin intermediate filaments. Curr. Opin. Cell Biol. 14, 110-122.
    • (2002) Curr. Opin. Cell Biol. , vol.14 , pp. 110-122
    • Coulombe, P.A.1    Omary, M.B.2
  • 80
    • 0000920828 scopus 로고
    • The packing of a helices: Simple coiled-coils
    • Crick, F. H. C. (1953). The packing of a helices: Simple coiled-coils. Acta Crystallogr. 6, 689-697.
    • (1953) Acta Crystallogr. , vol.6 , pp. 689-697
    • Crick, F.H.C.1
  • 81
    • 0024289805 scopus 로고
    • Regeneration after cardiotoxin injury of innervated and denervated slow and fast muscles of mammals. Myosin isoform analysis
    • d'Albis, A., Couteaux, R., Janmot, C., Roulet, A., and Mira, J. C. (1988). Regeneration after cardiotoxin injury of innervated and denervated slow and fast muscles of mammals. Myosin isoform analysis. Eur. J. Biochem. 174, 103-110.
    • (1988) Eur. J. Biochem , vol.174 , pp. 103-110
    • D'Albis, A.1    Couteaux, R.2    Janmot, C.3    Roulet, A.4    Mira, J.C.5
  • 82
    • 0033564136 scopus 로고    scopus 로고
    • Dystonin-deficient mice exhibit an intrinsic muscle weakness and an instability of skeletal muscle cytoarchitecture
    • Dalpe, G., Mathieu, M., Comtois, A., Zhu, E., Wasiak, S., De Repentigny, Y., Leclerc, N., and Kothary, R. (1999). Dystonin-deficient mice exhibit an intrinsic muscle weakness and an instability of skeletal muscle cytoarchitecture. Dev. Biol. 210, 367-380.
    • (1999) Dev. Biol. , vol.210 , pp. 367-380
    • Dalpe, G.1    Mathieu, M.2    Comtois, A.3    Zhu, E.4    Wasiak, S.5    De Repentigny, Y.6    Leclerc, N.7    Kothary, R.8
  • 84
    • 0018647939 scopus 로고
    • Formation and involution of Mallory bodies ("alcoholic hyalin") in murine and human liver revealed by immunofluorescence microscopy with antibodies to prekeratin
    • Denk, H., Franke, W. W., Eckerstorfer, R, Schmid, E., and Kerjaschki, D. (1979). Formation and involution of Mallory bodies ("alcoholic hyalin") in murine and human liver revealed by immunofluorescence microscopy with antibodies to prekeratin. Proc. Natl. Acad. Sci. USA 76, 4112-4116.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 4112-4116
    • Denk, H.1    Franke, W.W.2    Eckerstorfer, R.3    Schmid, E.4    Kerjaschki, D.5
  • 86
    • 0025053673 scopus 로고
    • Gene structure of nuclear lamin LIII of Xenopus laevis; a model for the evolution of IF proteins from a lamin-like ancestor
    • Doring, V., and Stick, R. (1990). Gene structure of nuclear lamin LIII of Xenopus laevis; a model for the evolution of IF proteins from a lamin-like ancestor. EMBO J. 9, 4073-4081.
    • (1990) EMBO J. , vol.9 , pp. 4073-4081
    • Doring, V.1    Stick, R.2
  • 87
    • 0035911163 scopus 로고    scopus 로고
    • Hsp70 and antifibrillogenic peptides promote degradation and inhibit intracellular aggregation of amyloidogenic light chains
    • Dul, J. L., Davis, D. P., Williamson, E. K., Stevens, F. J., and Argon, Y. (2001). Hsp70 and antifibrillogenic peptides promote degradation and inhibit intracellular aggregation of amyloidogenic light chains. J. Cell Biol. 152, 705-716.
    • (2001) J. Cell Biol. , vol.152 , pp. 705-716
    • Dul, J.L.1    Davis, D.P.2    Williamson, E.K.3    Stevens, F.J.4    Argon, Y.5
  • 88
    • 0024094917 scopus 로고
    • The effects of variations in the number and sequence of targeting signals on nuclear uptake
    • Dworetzky, S. I., Lanford, R. E., and Feldherr, C. M. (1988). The effects of variations in the number and sequence of targeting signals on nuclear uptake. J. Cell Biol. 107, 1279-1287.
    • (1988) J. Cell Biol. , vol.107 , pp. 1279-1287
    • Dworetzky, S.I.1    Lanford, R.E.2    Feldherr, C.M.3
  • 89
    • 0026706734 scopus 로고
    • Assembly of a tail-less mutant of the intermediate filament protein, vimentin, in vitro and in vivo
    • Eckelt, A, Herrmann, H., and Franke, W. W. (1992). Assembly of a tail-less mutant of the intermediate filament 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.W.3
  • 92
    • 0030906239 scopus 로고    scopus 로고
    • Polarisation-dependent association of plectin with desmoplakin and the lateral submembrane skeleton in MDCK cells
    • Eger, A., Stockinger, A., Wiche, G., and Foisner, R. (1997). Polarisation-dependent association of plectin with desmoplakin and the lateral submembrane skeleton in MDCK cells. J. Cell Sci. 110, 1307-1316.
    • (1997) J. Cell Sci. , vol.110 , pp. 1307-1316
    • Eger, A.1    Stockinger, A.2    Wiche, G.3    Foisner, R.4
  • 93
    • 0035942736 scopus 로고    scopus 로고
    • Duplexes of 21-nucleotide RNAs mediate RNA interference in cultured cells
    • Elbashir, S. M., Harborth, J., Lendeckel, W., Yalcin, A., Weber, K., and Tuschl, T. (2001). Duplexes of 21-nucleotide RNAs mediate RNA interference in cultured cells. Nature 411, 494-498.
    • (2001) Nature , vol.411 , pp. 494-498
    • Elbashir, S.M.1    Harborth, J.2    Lendeckel, W.3    Yalcin, A.4    Weber, K.5    Tuschl, T.6
  • 95
    • 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., Friedrich, V. L. Jr., Bosco, P., Kang, C., Gourov, A., Tu, P. H., Lee, V. M., and Lazzarini, R. A. (1998b). 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., Jr.2    Bosco, P.3    Kang, C.4    Gourov, A.5    Tu, P.H.6    Lee, V.M.7    Lazzarini, R.A.8
  • 96
    • 0031570308 scopus 로고    scopus 로고
    • Plectin transcript diversity: Identification and tissue distribution of variants with distinct first coding exons and rodless isoforms
    • Elliot, C. E., Becker, B., Oehler, S., Castanon, M. J., Hauptmann, R., and Wiche, G. (1997). Plectin transcript diversity: Identification and tissue distribution of variants with distinct first coding exons and rodless isoforms. Genomics 42, 115-125.
    • (1997) Genomics , vol.42 , pp. 115-125
    • Elliot, C.E.1    Becker, B.2    Oehler, S.3    Castanon, M.J.4    Hauptmann, R.5    Wiche, G.6
  • 98
    • 0028261670 scopus 로고
    • Neurofilament-deficient axons and perikaryal aggregates in viable transgenic mice expressing a neurofilament-beta-galactosidase fusion protein
    • Eyer, J., and Peterson, A. (1994). Neurofilament-deficient axons and perikaryal aggregates in viable transgenic mice expressing a neurofilament-beta-galactosidase fusion protein. Neuron 12, 389-405.
    • (1994) Neuron , vol.12 , pp. 389-405
    • Eyer, J.1    Peterson, A.2
  • 99
    • 0033027625 scopus 로고    scopus 로고
    • Aptamers as tools in molecular biology and immunology
    • Famulok, M., and Mayer, G. (1999). Aptamers as tools in molecular biology and immunology. Curr. Top. Microbiol. Immunol. 243, 123-136.
    • (1999) Curr. Top. Microbiol. Immunol. , vol.243 , pp. 123-136
    • Famulok, M.1    Mayer, G.2
  • 100
    • 0034007745 scopus 로고    scopus 로고
    • Liver regeneration
    • Fausto, N. (2000). Liver regeneration. J. Hepatol. 32, 19-31.
    • (2000) J. Hepatol. , vol.32 , pp. 19-31
    • Fausto, N.1
  • 102
    • 0028001606 scopus 로고
    • Variants of the heavy neurofilament subunit are associated with the development of amyotrophic lateral sclerosis
    • Figlewicz, D. A., Krizus, A., Martinoli, M. G., Meininger, V., Dib, M., Rouleau, G. A., and Julien, J. P. (1994). Variants of the heavy neurofilament subunit are associated with the development of amyotrophic lateral sclerosis. Hum. Mol. Genet. 3, 1757-1761.
    • (1994) Hum. Mol. Genet. , vol.3 , pp. 1757-1761
    • Figlewicz, D.A.1    Krizus, A.2    Martinoli, M.G.3    Meininger, V.4    Dib, M.5    Rouleau, G.A.6    Julien, J.P.7
  • 103
    • 0030833816 scopus 로고    scopus 로고
    • Mutational analysis of Mdm1p function in nuclear and mitochondrial inheritance
    • Fisk, H. A., and Yaffe, M. P. (1997). Mutational analysis of Mdm1p function in nuclear and mitochondrial inheritance. J. Cell Biol. 138, 485-494.
    • (1997) J. Cell Biol. , vol.138 , pp. 485-494
    • Fisk, H.A.1    Yaffe, M.P.2
  • 104
    • 0035189722 scopus 로고    scopus 로고
    • Inner nuclear membrane proteins and the nuclear lamina
    • Foisner, R. (2001). Inner nuclear membrane proteins and the nuclear lamina. J. Cell Sci. 114, 3791-3792.
    • (2001) J. Cell Sci. , vol.114 , pp. 3791-3792
    • Foisner, R.1
  • 105
    • 0023840076 scopus 로고
    • Cytoskeleton-associated plectin: In situ localization, in vitro reconstitution, and binding to immobilized intermediate filament proteins
    • Foisner, R., Leichtfried, F. E., Herrmann, H., Small, J. V., Lawson, D., and Wiche, G. (1988). Cytoskeleton-associated plectin: in situ localization, in vitro reconstitution, and binding to immobilized intermediate filament proteins. J. Cell Biol. 106, 723-733.
    • (1988) J. Cell Biol. , vol.106 , pp. 723-733
    • Foisner, R.1    Leichtfried, F.E.2    Herrmann, H.3    Small, J.V.4    Lawson, D.5    Wiche, G.6
  • 106
    • 0030020359 scopus 로고    scopus 로고
    • M-phase-specific phosphorylation and structural rearrangement of the cytoplasmic cross-linking protein plectin involve p34cdc2 kinase
    • Foisner, R., Malecz, N., Dressel, N., Stadler, C., and Wiche, G. (1996). M-phase-specific phosphorylation and structural rearrangement of the cytoplasmic cross-linking protein plectin involve p34cdc2 kinase. Mol. Biol. Cell 7, 273-288.
    • (1996) Mol. Biol. Cell , vol.7 , pp. 273-288
    • Foisner, R.1    Malecz, N.2    Dressel, N.3    Stadler, C.4    Wiche, G.5
  • 107
    • 0023657388 scopus 로고
    • Nulcear lamins and cytoplasmic intermediate filament proteins: A growing multigene family
    • Franke, W. W. (1987). Nulcear lamins and cytoplasmic intermediate filament proteins: A growing multigene family. Cell 48, 3-4.
    • (1987) Cell , vol.48 , pp. 3-4
    • Franke, W.W.1
  • 108
    • 0019868888 scopus 로고
    • Electron microscopy of vimentin filaments and associated whisker structures in thin sections and freeze-fractures
    • Franke, W. W., Zerban, H., Grund, C., and Schmid, E. (1981). Electron microscopy of vimentin filaments and associated whisker structures in thin sections and freeze-fractures. Biol. Cell 41, 173-178.
    • (1981) Biol. Cell , vol.41 , pp. 173-178
    • Franke, W.W.1    Zerban, H.2    Grund, C.3    Schmid, E.4
  • 109
    • 84985759585 scopus 로고
    • Formation of cytoskeletal elements during mouse embryogenesis. III. Primary mesenchymal cells and the first appearance of vimentin filaments
    • Franke, W. W., Grund, C., Kuhn, C., Jackson, B. W., and Illmensee, K. (1982a). Formation of cytoskeletal elements during mouse embryogenesis. III. Primary mesenchymal cells and the first appearance of vimentin filaments. Differentiation 23, 43-59.
    • (1982) Differentiation , vol.23 , pp. 43-59
    • Franke, W.W.1    Grund, C.2    Kuhn, C.3    Jackson, B.W.4    Illmensee, K.5
  • 110
    • 0020399890 scopus 로고
    • Desmoplakins of epithelial and mycardial desmosomes are immunologically and biochemically related
    • Franke, W. W., Moll, R., Schiller, D. L., Schmid, E., Kartenbeck, J., and Müller, H. (1982b). Desmoplakins of epithelial and mycardial desmosomes are immunologically and biochemically related. Differentiation 23, 115-127.
    • (1982) Differentiation , vol.23 , pp. 115-127
    • Franke, W.W.1    Moll, R.2    Schiller, D.L.3    Schmid, E.4    Kartenbeck, J.5    Müller, H.6
  • 111
    • 0001657058 scopus 로고
    • Protofilamentous and annular structures as intermediates during reconstitution of cytokeratin filaments in vitro
    • Franke, W. W., Schiller, D. L., and Grund, C. (1982c). Protofilamentous and annular structures as intermediates during reconstitution of cytokeratin filaments in vitro. Biol. Cell 46, 257-268.
    • (1982) Biol. Cell , vol.46 , pp. 257-268
    • Franke, W.W.1    Schiller, D.L.2    Grund, C.3
  • 112
    • 0022969393 scopus 로고
    • Cloning of cDNA and amino acid sequence of a cytokeratin expressed in oocytes of Xenopus laevis
    • Franz, J. K., and Franke, W. W. (1986). Cloning of cDNA and amino acid sequence of a cytokeratin expressed in oocytes of Xenopus laevis. Proc. Natl. Acad. Sci. USA 83, 6475-6479.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 6475-6479
    • Franz, J.K.1    Franke, W.W.2
  • 113
    • 0023657022 scopus 로고
    • Binding of brain spectrin to the 70-kDa neurofilament subunit protein
    • Frappier, T., Regnouf, F., and Pradel, L. A. (1987). Binding of brain spectrin to the 70-kDa neurofilament subunit protein. Eur. J. Biochem. 169, 651-657.
    • (1987) Eur. J. Biochem , vol.169 , pp. 651-657
    • Frappier, T.1    Regnouf, F.2    Pradel, L.A.3
  • 114
    • 0034676457 scopus 로고    scopus 로고
    • Functional genomic analysis of C. elegans chromosome I by systematic RNA interference
    • Fraser, A. G., Kamath, R. S., Zipperlen, P., Martinez-Campos, M., Sohrmann, M., and Ahringer, J. (2000). Functional genomic analysis of C. elegans chromosome I by systematic RNA interference. Nature 408, 325-330.
    • (2000) Nature , vol.408 , pp. 325-330
    • Fraser, A.G.1    Kamath, R.S.2    Zipperlen, P.3    Martinez-Campos, M.4    Sohrmann, M.5    Ahringer, J.6
  • 116
  • 117
    • 0030474645 scopus 로고    scopus 로고
    • The cytoskeleton and disease: Genetic disorders of intermediate filaments
    • Fuchs, E. (1996). The cytoskeleton and disease: Genetic disorders of intermediate filaments. Annu. Rev. Genet. 30, 197-231.
    • (1996) Annu. Rev. Genet. , vol.30 , pp. 197-231
    • Fuchs, E.1
  • 118
    • 0032559341 scopus 로고    scopus 로고
    • A structural scaffolding of intermediate filaments in health and disease
    • Fuchs, E., and Cleveland, D. W. (1998). A structural scaffolding of intermediate filaments in health and disease. Science 279, 514-519.
    • (1998) Science , vol.279 , pp. 514-519
    • Fuchs, E.1    Cleveland, D.W.2
  • 119
    • 0018866880 scopus 로고
    • Changes in keratin gene expression during terminal differentiation of the keratinocyte
    • Fuchs, E., and Green, H. (1980). Changes in keratin gene expression during terminal differentiation of the keratinocyte. Cell 19, 1033-1042.
    • (1980) Cell , vol.19 , pp. 1033-1042
    • Fuchs, E.1    Green, H.2
  • 120
    • 0035181987 scopus 로고    scopus 로고
    • Bridging cytoskeletal intersections
    • Fuchs, E., and Karakesisoglou, I. (2001). Bridging cytoskeletal intersections. Genes Dev. 15, 1-14.
    • (2001) Genes Dev. , vol.15 , pp. 1-14
    • Fuchs, E.1    Karakesisoglou, I.2
  • 121
    • 0028283501 scopus 로고
    • Intermediate filaments: Structure, dynamics, function, and disease
    • Fuchs, E., and Weber, K. (1994). Intermediate filaments: Structure, dynamics, function, and disease. Annu. Rev. Biochem. 63, 345-382.
    • (1994) Annu. Rev. Biochem. , vol.63 , pp. 345-382
    • Fuchs, E.1    Weber, K.2
  • 123
    • 0035918303 scopus 로고    scopus 로고
    • Epiplakin, a novel member of the plakin family originally identified as a 450-kDa human epidermal autoantigen. Structure and tissue localization
    • Fujiwara, S., Takeo, N., Otani, Y., Parry, D. A., Kunimatsu, M., Lu, R., Sasaki, M., Matsuo, N., Khaleduzzaman, M., and Yoshioka, H. (2001). Epiplakin, a novel member of the plakin family originally identified as a 450-kDa human epidermal autoantigen. Structure and tissue localization. J. Biol. Chem. 276, 13340-13347.
    • (2001) J. Biol. Chem. , vol.276 , pp. 13340-13347
    • Fujiwara, S.1    Takeo, N.2    Otani, Y.3    Parry, D.A.4    Kunimatsu, M.5    Lu, R.6    Sasaki, M.7    Matsuo, N.8    Khaleduzzaman, M.9    Yoshioka, H.10
  • 124
    • 20644437528 scopus 로고    scopus 로고
    • Desmoplakin is required early in development for assembly of desmosomes and cytoskeletal linkage
    • Gallicano, G. I., Kouklis, P., Bauer, C., Yin, M., Vasioukhin, V., Degenstein, L., and Fuchs, E. (1998). Desmoplakin is required early in development for assembly of desmosomes and cytoskeletal linkage. J. Cell Biol. 143, 2009-2022.
    • (1998) J. Cell Biol. , vol.143 , pp. 2009-2022
    • Gallicano, G.I.1    Kouklis, P.2    Bauer, C.3    Yin, M.4    Vasioukhin, V.5    Degenstein, L.6    Fuchs, E.7
  • 125
    • 0030659119 scopus 로고    scopus 로고
    • The importance of intermediate filaments in the adaptation of tissues to mechanical stress: Evidence from gene knockout studies
    • Galou, M., Gao, J., Humbert, J., Mericskay, M., Li, Z., Paulin, D., and Vicart, P. (1997). The importance of intermediate filaments in the adaptation of tissues to mechanical stress: Evidence from gene knockout studies. Biol. Cell 89, 85-97.
    • (1997) Biol. Cell , vol.89 , pp. 85-97
    • Galou, M.1    Gao, J.2    Humbert, J.3    Mericskay, M.4    Li, Z.5    Paulin, D.6    Vicart, P.7
  • 127
    • 0021869590 scopus 로고
    • Extra-neural glial fibrillary acidic protein (GFAP) immunoreactivity in perisinusoidal stellate cells of rat liver
    • Gard, A. L., White, F. P., and Dutton, G. R. (1985). Extra-neural glial fibrillary acidic protein (GFAP) immunoreactivity in perisinusoidal stellate cells of rat liver. J. Neuroimmunol. 8, 359-75.
    • (1985) J. Neuroimmunol. , vol.8 , pp. 359-375
    • Gard, A.L.1    White, F.P.2    Dutton, G.R.3
  • 128
    • 0025990476 scopus 로고
    • Tissue distribution, quantitation and proliferation kinetics of fat-storing cells in carbon tetrachloride-injured rat liver
    • Geerts, A., Lazou, J. M., Bleser, P. De, and Wisse, E. (1991). Tissue distribution, quantitation and proliferation kinetics of fat-storing cells in carbon tetrachloride-injured rat liver. Hepatology 13, 1193-1202.
    • (1991) Hepatology , vol.13 , pp. 1193-1202
    • Geerts, A.1    Lazou, J.M.2    De Bleser, P.3    Wisse, E.4
  • 129
    • 0032589487 scopus 로고    scopus 로고
    • Binding of integrin alpha6beta4 to plectin prevents plectin association with F-actin but does not interfere with intermediate filament binding
    • Geerts, D., Fontao, L., Nievers, M. G., Schaapveld, R. Q., Purkis, P. E., Wheeler, G. N., Lane, E. B., Leigh, I. M., and Sonnenberg, A. (1999). Binding of integrin alpha6beta4 to plectin prevents plectin association with F-actin but does not interfere with intermediate filament binding. J. Cell Biol. 147, 417-434.
    • (1999) J. Cell Biol. , vol.147 , pp. 417-434
    • Geerts, D.1    Fontao, L.2    Nievers, M.G.3    Schaapveld, R.Q.4    Purkis, P.E.5    Wheeler, G.N.6    Lane, E.B.7    Leigh, I.M.8    Sonnenberg, A.9
  • 130
    • 0035200752 scopus 로고    scopus 로고
    • Formation of normal desmin intermediate filaments in mouse hepatic stellate cells requires vimentin
    • Geerts, A., Eliasson, C., Niki, T., Wielant, A., Vaeyens, F., and Pekny, M. (2001). Formation of normal desmin intermediate filaments in mouse hepatic stellate cells requires vimentin. Hepatology 33, 177-188.
    • (2001) Hepatology , vol.33 , pp. 177-188
    • Geerts, A.1    Eliasson, C.2    Niki, T.3    Wielant, A.4    Vaeyens, F.5    Pekny, M.6
  • 131
    • 0019888431 scopus 로고
    • Self-assembly in vitro of the 68,000 molecular weight component of the mammalian neurofilament triplet proteins into intermediate-sized filaments
    • Geisler, N., and Weber, K. (1981). Self-assembly in vitro of the 68,000 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
  • 132
    • 0020338526 scopus 로고
    • The amino acid sequence of chicken muscle desmin provides a common structural model for intermediate filament proteins
    • Geisler, N., and Weber, K. (1982). The amino acid sequence of chicken muscle desmin provides a common structural model for intermediate filament proteins. EMBO J. 1, 1649-1656.
    • (1982) EMBO J. , vol.1 , pp. 1649-1656
    • Geisler, N.1    Weber, K.2
  • 133
    • 0027305537 scopus 로고
    • Peptides from the conserved ends of the rod domain of desmin disassemble intermediate filaments and reveal unexpected structural features: A circular dichroism Fourier transform infrared, and electron microscopic study
    • Geisler, N., Heimburg, T, Schünemann, J., and Weber, K. (1993). Peptides from the conserved ends of the rod domain of desmin disassemble intermediate filaments and reveal unexpected structural features: A circular dichroism Fourier transform infrared, and electron microscopic study. J. Struct. Biol. 110, 205-214.
    • (1993) J. Struct. Biol. , vol.110 , pp. 205-214
    • Geisler, N.1    Heimburg, T.2    Schünemann, J.3    Weber, K.4
  • 134
    • 0032566613 scopus 로고    scopus 로고
    • Assembly and architecture of invetebrate cytoplasmic intermediate filaments reconcile features of vertebrate cytoplasmic and nuclear lamin-type intermediate filaments
    • Geisler, N., Schünemann, J., Weber, K., Häner, M., and Aebi, U. (1998). Assembly and architecture of invetebrate cytoplasmic intermediate filaments reconcile features of vertebrate cytoplasmic and nuclear lamin-type intermediate filaments. J. Mol. Biol. 282, 601-617.
    • (1998) J. Mol. Biol. , vol.282 , pp. 601-617
    • Geisler, N.1    Schünemann, J.2    Weber, K.3    Häner, M.4    Aebi, U.5
  • 135
    • 0023371437 scopus 로고
    • Lamin B constitutes an intermediate filament attachment site at the nuclear envelope
    • Georgatos, S. D., and Blobel, G. (1987a). Lamin B constitutes an intermediate filament attachment site at the nuclear envelope. J. Cell Biol. 105, 117-125.
    • (1987) J. Cell Biol. , vol.105 , pp. 117-125
    • Georgatos, S.D.1    Blobel, G.2
  • 136
    • 0023372471 scopus 로고
    • Two distinct attachment sites for vimentin along the plasma membrane and the nuclear envelope in avian erythrocytes: A basis for a vectorial assembly of intermediate filaments
    • Georgatos, S. D., and Blobel, G. (1987b). Two distinct attachment sites for vimentin along the plasma membrane and the nuclear envelope in avian erythrocytes: A basis for a vectorial assembly of intermediate filaments, J. Cell Biol. 105, 105-115.
    • (1987) J. Cell Biol. , vol.105 , pp. 105-115
    • Georgatos, S.D.1    Blobel, G.2
  • 137
    • 0023430563 scopus 로고
    • Binding of two desmin derivatives to the plasma membrane and the nuclear envelope of avian erythrocytes: Evidence for a conserved site-specificity in intermediate filament-membrane interactions
    • Georgatos, S. D., Weber, K., Geisler, N., and Blobel, G. (1987). Binding of two desmin derivatives to the plasma membrane and the nuclear envelope of avian erythrocytes: Evidence for a conserved site-specificity in intermediate filament-membrane interactions. Proc. Natl. Acad. Sci. USA 84, 6780-6784.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 6780-6784
    • Georgatos, S.D.1    Weber, K.2    Geisler, N.3    Blobel, G.4
  • 139
    • 0035921430 scopus 로고    scopus 로고
    • Simple epithelium keratins 8 and 18 provide resistance to Fas-mediated apoptosis. The protection occurs through a receptor-targeting modulation
    • Gilbert, S., Loranger, A., Daigle, N., and Marceau, N. (2001). Simple epithelium keratins 8 and 18 provide resistance to Fas-mediated apoptosis. The protection occurs through a receptor-targeting modulation. J. Cell Biol. 154, 763-773.
    • (2001) J. Cell Biol. , vol.154 , pp. 763-773
    • Gilbert, S.1    Loranger, A.2    Daigle, N.3    Marceau, N.4
  • 140
    • 0025107358 scopus 로고
    • Assembly properties of dominant and recessive mutations in the small mouse neurofilament (NF-L) subunit
    • Gill, S. R., Wong, P. C., Monteiro, M. J., and Cleveland, D. W. (1990). Assembly properties of dominant and recessive mutations 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
  • 141
    • 0020517951 scopus 로고
    • Lewy bodies of Parkinson's disease contain neurofilament antigens
    • Goldman, J. E., Yen, S. H., Chiu, F. C., and Peress, N. S. (1983). Lewy bodies of Parkinson's disease contain neurofilament antigens. Science 221, 1082-1084.
    • (1983) Science , vol.221 , pp. 1082-1084
    • Goldman, J.E.1    Yen, S.H.2    Chiu, F.C.3    Peress, N.S.4
  • 142
    • 0029795964 scopus 로고    scopus 로고
    • The function of intermediate filaments in cell shape and cytoskeletal integrity
    • Goldman, R. D., Khoun, S., Chou, Y.-H., Opal, R., and Steinert, P. M. (1996). The function of intermediate filaments in cell shape and cytoskeletal integrity. J. Cell Biol. 134, 971-983.
    • (1996) J. Cell Biol. , vol.134 , pp. 971-983
    • Goldman, R.D.1    Khoun, S.2    Chou, Y.-H.3    Opal, R.4    Steinert, P.M.5
  • 144
    • 0028878797 scopus 로고
    • Mice devoid of the glial fibrillary acidic protein develop normally and are susceptible to scrapie prions
    • Gomi, H., Yokoyama, T., Fujimoto, K., Ikeda, T., Katoh, A., Itoh, T., and Itohara, S. (1995). Mice devoid of the glial fibrillary acidic protein develop normally and are susceptible to scrapie prions. Neuron 14, 29-41.
    • (1995) Neuron , vol.14 , pp. 29-41
    • Gomi, H.1    Yokoyama, T.2    Fujimoto, K.3    Ikeda, T.4    Katoh, A.5    Itoh, T.6    Itohara, S.7
  • 145
    • 0010697803 scopus 로고    scopus 로고
    • Proteomics of multiprotein complexes: Answering fundamental questions in neuroscience
    • Grant, S. G., and Husi, H. (2001). Proteomics of multiprotein complexes: Answering fundamental questions in neuroscience. Trends Biotechnol. 19, S49-S54.
    • (2001) Trends Biotechnol. , vol.19
    • Grant, S.G.1    Husi, H.2
  • 146
    • 0027096705 scopus 로고
    • Structure of desmoplakin and its association with intermediate filaments
    • Green, K. J., Stappenbeck, T. S., Parry, D. A., and Virata, M. L. (1992). Structure of desmoplakin and its association with intermediate filaments. J. Dermatol. 19, 765-769.
    • (1992) J. Dermatol. , vol.19 , pp. 765-769
    • Green, K.J.1    Stappenbeck, T.S.2    Parry, D.A.3    Virata, M.L.4
  • 147
    • 0032583124 scopus 로고    scopus 로고
    • Kakapo, a gene required for adhesion between and within cell layers in Drosophila, encodes a large cytoskeletal linker protein related to plectin and dystrophin
    • Gregory, S. L., and Brown, N. H. (1998). Kakapo, a gene required for adhesion between and within cell layers in Drosophila, encodes a large cytoskeletal linker protein related to plectin and dystrophin. J. Cell Biol. 143, 1271-1282.
    • (1998) J. Cell Biol. , vol.143 , pp. 1271-1282
    • Gregory, S.L.1    Brown, N.H.2
  • 148
    • 0029066406 scopus 로고
    • Gene targeting of BPAG1: Abnormalities in mechanical strength and cell migration in stratified epithelia and neurologic degeneration
    • Guo, L., Degenstein, L., Dowling, J., Yu, Q. C., Wollmann, R., Perman, B., and Fuchs, E. (1995). Gene targeting of BPAG1: Abnormalities in mechanical strength and cell migration in stratified epithelia and neurologic degeneration. Cell 81, 233-243.
    • (1995) Cell , vol.81 , pp. 233-243
    • Guo, L.1    Degenstein, L.2    Dowling, J.3    Yu, Q.C.4    Wollmann, R.5    Perman, B.6    Fuchs, E.7
  • 149
    • 0035694237 scopus 로고    scopus 로고
    • Identification of essential genes in cultured mammalian cells using small interfering RNAs
    • Harborth, J., Elbashir, S. M., Bechert, K., Tuschl, T., and Weber, K. (2001). Identification of essential genes in cultured mammalian cells using small interfering RNAs. J. Cell Sci. 114, 4557-4565.
    • (2001) J. Cell Sci. , vol.114 , pp. 4557-4565
    • Harborth, J.1    Elbashir, S.M.2    Bechert, K.3    Tuschl, T.4    Weber, K.5
  • 150
    • 0028290358 scopus 로고
    • Function of type I and type II keratin head domains: Their role in dimer, tetramer and filament formation
    • Hatzfeld, M., and Burba, M. (1994). Function of type I and type II keratin head domains: Their role in dimer, tetramer and filament formation. J. Cell Sci. 107, 1959-1972.
    • (1994) J. Cell Sci. , vol.107 , pp. 1959-1972
    • Hatzfeld, M.1    Burba, M.2
  • 151
    • 0022348539 scopus 로고
    • Pair formation and promiscuity of cytokeratins: Formation in vitro of heterotypic complexes and intermediate-sized filaments by homologous and heterologous recombinations of purified polypeptides
    • Hatzfeld, M., and Franke, W. W. (1985). Pair formation and promiscuity of cytokeratins: Formation in vitro of heterotypic complexes and intermediate-sized filaments by homologous and heterologous recombinations of purified polypeptides. J. Cell Biol. 101, 1826-1841.
    • (1985) J. Cell Biol. , vol.101 , pp. 1826-1841
    • Hatzfeld, M.1    Franke, W.W.2
  • 152
    • 0025107377 scopus 로고
    • Tailless keratins assemble into regular intermediate filaments in vitro
    • Hatzfeld, M., and Weber, K. (1990). Tailless keratins assemble into regular intermediate filaments in vitro. J. Cell Sci. 97, 317-324.
    • (1990) J. Cell Sci. , vol.97 , pp. 317-324
    • Hatzfeld, M.1    Weber, K.2
  • 153
    • 0026570065 scopus 로고
    • A synthetic peptide representing the consensus sequence motif at the carboxy-terminal end of the rod domain inhibits intermediate filament assembly and disassembles preformed filaments
    • Hatzfeld, M., and Weber, K. (1992). A synthetic peptide representing the consensus sequence motif at the carboxy-terminal end of the rod domain inhibits intermediate filament assembly and disassembles preformed filaments. J. Cell Biol. 116, 157-166.
    • (1992) J. Cell Biol. , vol.116 , pp. 157-166
    • Hatzfeld, M.1    Weber, K.2
  • 155
    • 0032247869 scopus 로고    scopus 로고
    • Structure, assembly and dynamics of intermediate filaments
    • H. Herrmann and J. R. Harris, Eds. Plenum New York
    • Herrmann, H., and Aebi, U. (1998a). Structure, assembly and dynamics of intermediate filaments. In "Intermediate Filaments: Subcellular Biochemistry" (H. Herrmann and J. R. Harris, Eds.), Vol. 13, pp. 319-362. Plenum New York.
    • (1998) Intermediate Filaments: Subcellular Biochemistry , vol.13 , pp. 319-362
    • Herrmann, H.1    Aebi, U.2
  • 156
    • 0032053588 scopus 로고    scopus 로고
    • Intermediate filament assembly: Fibrillogenesis is driven by decisive dimer-dimer interactions
    • Herrmann, H., and Aebi, U. (1998b). Intermediate filament assembly: Fibrillogenesis is driven by decisive dimer-dimer interactions. Curr. Opin. Struct. Biol. 8, 177-185.
    • (1998) Curr. Opin. Struct. Biol. , vol.8 , pp. 177-185
    • Herrmann, H.1    Aebi, U.2
  • 157
    • 0033618848 scopus 로고    scopus 로고
    • Intermediate filament assembly: Temperature sensitivity and polymorphism
    • Herrmann, H., and Aebi, U. (1999a). Intermediate filament assembly: Temperature sensitivity and polymorphism. Cell. Mol. Life Sci. 55, 1416-1431.
    • (1999) Cell. Mol. Life Sci. , vol.55 , pp. 1416-1431
    • Herrmann, H.1    Aebi, U.2
  • 158
    • 34047196203 scopus 로고    scopus 로고
    • Neurofilament triplet proteins
    • T. Kreis and R. Vale, Eds. Sambrook & Tooze Publishing Partnership, Oxford University Press, Oxford
    • Herrmann, H., and Aebi, U. (1999b). Neurofilament triplet proteins. In" Guidebook to the Cytoskeletal and Motor Proteins" (T. Kreis and R. Vale, Eds.), pp. 313-317. Sambrook & Tooze Publishing Partnership, Oxford University Press, Oxford.
    • (1999) Guidebook to the Cytoskeletal and Motor Proteins , pp. 313-317
    • Herrmann, H.1    Aebi, U.2
  • 159
    • 0033960790 scopus 로고    scopus 로고
    • Intermediate filaments and their associates: Multi-talented structural elements specifying cytoarchitecture and cytodynamics
    • Herrmann, H., and Aebi, U. (2000). Intermediate filaments and their associates: Multi-talented structural elements specifying cytoarchitecture and cytodynamics. Curr. Opin. Cell Biol. 12, 79-90.
    • (2000) Curr. Opin. Cell Biol. , vol.12 , pp. 79-90
    • Herrmann, H.1    Aebi, U.2
  • 161
    • 0033382559 scopus 로고    scopus 로고
    • New ways to look at the interchromosomal-domain compartment
    • Herrmann, H., and Lichter, P. (1999). New ways to look at the interchromosomal-domain compartment. Protoplasma 209, 157-165.
    • (1999) Protoplasma , vol.209 , pp. 157-165
    • Herrmann, H.1    Lichter, P.2
  • 162
    • 0021053192 scopus 로고
    • Specific in situ phosphorylation of plectin in detergent-resistant cytoskeletons from cultured chinese hamster ovary cells
    • Herrmann, H., and Wiche, G. (1983). Specific in situ phosphorylation of plectin in detergent-resistant cytoskeletons from cultured chinese hamster ovary cells. J. Biol. Chem. 258, 14610-14618.
    • (1983) J. Biol. Chem. , vol.258 , pp. 14610-14618
    • Herrmann, H.1    Wiche, G.2
  • 163
    • 0023126564 scopus 로고
    • Plectin and IFAP-300K are homologous proteins binding to microtubule-associated proteins 1 and 2 and to the 240-kilodalton subunit of spectrin
    • Herrmann, H., and Wiche, G. (1987). Plectin and IFAP-300K are homologous proteins binding to microtubule-associated proteins 1 and 2 and to the 240-kilodalton subunit of spectrin. J. Biol. Chem. 262, 1320-1325.
    • (1987) J. Biol. Chem. , vol.262 , pp. 1320-1325
    • Herrmann, H.1    Wiche, G.2
  • 164
    • 0024505368 scopus 로고
    • Expression of intermediate filament proteins during development of Xenopus laevis I. cDNA clones encoding different forms of vimentin
    • Herrmann, H., Fouquet, B., and Franke, W. W. (1989). Expression of intermediate filament proteins during development of Xenopus laevis I. cDNA clones encoding different forms of vimentin. Development 105, 279-298.
    • (1989) Development , vol.105 , pp. 279-298
    • Herrmann, H.1    Fouquet, B.2    Franke, W.W.3
  • 165
    • 0026559105 scopus 로고
    • Identification of a nonapeptide motif in the vimentin head domain involved in intermediate filament assembly
    • Herrmann, H., Hofmann, I., and Franke, W. W. (1992). Identification of a nonapeptide motif in the vimentin head domain involved in intermediate filament assembly. J. Mol. Biol. 223, 637-650.
    • (1992) J. Mol. Biol. , vol.223 , pp. 637-650
    • Herrmann, H.1    Hofmann, I.2    Franke, W.W.3
  • 166
    • 0027519337 scopus 로고
    • Temperature-sensitive intermediate filament assembly: Alternative structures of Xenopus laevis vimentin in vitro and in vivo
    • Herrmann, H., Eckelt, A., Brettel, M., Grund, C., and Franke, W. W. (1993). Temperature-sensitive intermediate filament assembly: Alternative structures of Xenopus laevis vimentin in vitro and in vivo. J. Mol. Biol. 234, 99-113.
    • (1993) J. Mol. Biol. , vol.234 , pp. 99-113
    • Herrmann, H.1    Eckelt, A.2    Brettel, M.3    Grund, C.4    Franke, W.W.5
  • 167
    • 0030596170 scopus 로고    scopus 로고
    • Structure and assembly properties of the intermediate filament protein vimentin: The role of its head, rod and tail domains
    • Herrmann, H., Häner, M., Bretel, M., Müller, S. A., Goldie, K. N., Fedtke, B., Franke, W. W., and Aebi, U. (1996). Structure and assembly properties of the intermediate filament protein vimentin: The role of its head, rod and tail domains. J. Mol. Biol. 264, 933-953.
    • (1996) J. Mol. Biol. , vol.264 , pp. 933-953
    • Herrmann, H.1    Häner, M.2    Bretel, M.3    Müller, S.A.4    Goldie, K.N.5    Fedtke, B.6    Franke, W.W.7    Aebi, U.8
  • 168
    • 0344096498 scopus 로고    scopus 로고
    • Characterization of distinct early assembly units of different intermediate filament proteins
    • Herrmann, H., Häner, M., Bretel, M., Ku, N.-U., and Aebi, U. (1999). Characterization of distinct early assembly units of different intermediate filament proteins. J. Mol. Biol. 286, 1403-1420.
    • (1999) J. Mol. Biol. , vol.286 , pp. 1403-1420
    • Herrmann, H.1    Häner, M.2    Bretel, M.3    Ku, N.-U.4    Aebi, U.5
  • 170
    • 0036443637 scopus 로고    scopus 로고
    • Characterization of early assembly intermediates of recombinant human keratins
    • Herrmann, H., Wedig, T., Porter, R. M., Lane, E. B., and Aebi, U. (2002). Characterization of early assembly intermediates of recombinant human keratins. J. Struct. Biol. 137, 82-96.
    • (2002) J. Struct. Biol. , vol.137 , pp. 82-96
    • Herrmann, H.1    Wedig, T.2    Porter, R.M.3    Lane, E.B.4    Aebi, U.5
  • 171
    • 0026042995 scopus 로고
    • Cytopathology of amyotrophic lateral sclerosis
    • Hirano, A. (1991). Cytopathology of amyotrophic lateral sclerosis. Adv. Neurol. 56, 91-101.
    • (1991) Adv. Neurol. , vol.56 , pp. 91-101
    • Hirano, A.1
  • 172
    • 0034596918 scopus 로고    scopus 로고
    • Targeted deletion of keratins 18 and 19 leads to trophoblast fragility and early embryonic lethality
    • Hesse, M., Franz, T., Tamai, Y., Taketo, M. M., and Magin, T. M. (2000). Targeted deletion of keratins 18 and 19 leads to trophoblast fragility and early embryonic lethality. EMBO J. 19, 5060-5070.
    • (2000) EMBO J. , vol.19 , pp. 5060-5070
    • Hesse, M.1    Franz, T.2    Tamai, Y.3    Taketo, M.M.4    Magin, T.M.5
  • 173
    • 0034907507 scopus 로고    scopus 로고
    • Genes for intermediate filament proteins and the draft sequence of the human genome: Novel keratin genes and a surprisingly high number of pseudogenes related to keratin genes 8 and 18
    • Hesse, M., Magin, T. M., and Weber, K. (2001). Genes for intermediate filament proteins and the draft sequence of the human genome: Novel keratin genes and a surprisingly high number of pseudogenes related to keratin genes 8 and 18. J. Cell Sci. 114, 2569-2575.
    • (2001) J. Cell Sci. , vol.114 , pp. 2569-2575
    • Hesse, M.1    Magin, T.M.2    Weber, K.3
  • 174
    • 0032899830 scopus 로고    scopus 로고
    • Plectin is a linker of intermediate filaments to Z-discs in skeletal muscle fibers
    • Hijikata, T., Murakami, T., Imamura, M., Fujimaki, N., and Ishikawa, H. (1999). Plectin is a linker of intermediate filaments to Z-discs in skeletal muscle fibers. J. Cell Sci. 112, 867-876.
    • (1999) J. Cell Sci. , vol.112 , pp. 867-876
    • Hijikata, T.1    Murakami, T.2    Imamura, M.3    Fujimaki, N.4    Ishikawa, H.5
  • 175
    • 0026042995 scopus 로고
    • Cytopathology of amyotrophic lateral sclerosis
    • Hirano, A. (1991). Cytopathology of amyotrophic lateral sclerosis. Adv. Neurol. 56, 91-101.
    • (1991) Adv. Neurol. , vol.56 , pp. 91-101
    • Hirano, A.1
  • 176
    • 0032487437 scopus 로고    scopus 로고
    • Gene targeting studies begin to reveal the function of neurofilament proteins
    • Hirokawa, N., and Takeda, S. (1998). Gene targeting studies begin to reveal the function of neurofilament proteins. J. Cell Biol. 143, 1-4.
    • (1998) J. Cell Biol. , vol.143 , pp. 1-4
    • Hirokawa, N.1    Takeda, S.2
  • 177
    • 0034490814 scopus 로고    scopus 로고
    • Association of prenylated proteins with the plasma membrane and the inner nuclear membrane is mediated by the same membrane-targeting motifs
    • Hofemeister, H., Weber, K., and Stick, R. (2000). Association of prenylated proteins with the plasma membrane and the inner nuclear membrane is mediated by the same membrane-targeting motifs. Mol. Biol. Cell 11, 3233-3246.
    • (2000) Mol. Biol. Cell , vol.11 , pp. 3233-3246
    • Hofemeister, H.1    Weber, K.2    Stick, R.3
  • 178
    • 0026522850 scopus 로고
    • Interference of in vitro vimentin assembly by synthetic peptides derived from the vimentin head domain
    • Hofmann, I., and Herrmann, H. (1992). Interference of in vitro vimentin assembly by synthetic peptides derived from the vimentin head domain. J. Cell Sci. 101, 687-700.
    • (1992) J. Cell Sci. , vol.101 , pp. 687-700
    • Hofmann, I.1    Herrmann, H.2
  • 179
    • 0033868312 scopus 로고    scopus 로고
    • Interaction of plakophilins with desmoplakin and intermediate filament proteins: An in vitro analysis
    • Hofmann, I., Mertens, C., Brettel, M., Nimmrich, V., Schnölzer, M., and Herrmann, H. (2000). Interaction of plakophilins with desmoplakin and intermediate filament proteins: An in vitro analysis. J. Cell Sci. 113, 2471-2483.
    • (2000) J. Cell Sci. , vol.113 , pp. 2471-2483
    • Hofmann, I.1    Mertens, C.2    Brettel, M.3    Nimmrich, V.4    Schnölzer, M.5    Herrmann, H.6
  • 180
    • 0025922755 scopus 로고
    • Immunolocalization of lamins in the thick nuclear lamina of human synovial cells
    • Höger, T. H., Grund, C., Franke, W. W., and Krohne, G. (1991). Immunolocalization of lamins in the thick nuclear lamina of human synovial cells. Eur. J. Cell Biol. 54, 150-156.
    • (1991) Eur. J. Cell Biol. , vol.54 , pp. 150-156
    • Höger, T.H.1    Grund, C.2    Franke, W.W.3    Krohne, G.4
  • 181
    • 0027480639 scopus 로고
    • A missense mutation in the rod domain of keratin 14 associated with recessive epidermolysis bullosa simplex
    • Hovnanian, A., Pollack, E., Hilal, L., Rochat, A., Prost, C., Barrandon, Y., and Goossens, M. (1993). A missense mutation in the rod domain of keratin 14 associated with recessive epidermolysis bullosa simplex. Nat. Genet. 3, 327-332.
    • (1993) Nat. Genet. , vol.3 , pp. 327-332
    • Hovnanian, A.1    Pollack, E.2    Hilal, L.3    Rochat, A.4    Prost, C.5    Barrandon, Y.6    Goossens, M.7
  • 183
    • 0017192307 scopus 로고
    • The ordered columnar structure of mouse filiform papillae
    • Hume, W. J., and Potten, C. S. (1976). The ordered columnar structure of mouse filiform papillae. J. Cell Sci. 22, 149-160.
    • (1976) J. Cell Sci. , vol.22 , pp. 149-160
    • Hume, W.J.1    Potten, C.S.2
  • 184
    • 0034003401 scopus 로고    scopus 로고
    • Exempting homologous pseudogene sequences from polymerase chain reaction amplification allows genomic keratin 14 hotspot mutation analysis
    • Hut, P. H., Vlies, P. M., Jonkman, F., Verlind, E., Shimizu, H., Buys, C. H., and Scheffer, H. (2000). Exempting homologous pseudogene sequences from polymerase chain reaction amplification allows genomic keratin 14 hotspot mutation analysis. J. Invest. Dermatol. 114, 616-619.
    • (2000) J. Invest. Dermatol. , vol.114 , pp. 616-619
    • Hut, P.H.1    Vlies, P.M.2    Jonkman, F.3    Verlind, E.4    Shimizu, H.5    Buys, C.H.6    Scheffer, H.7
  • 185
    • 0035153087 scopus 로고    scopus 로고
    • Lamins in disease: Why do ubiquitously expressed nuclear envelope proteins give rise to tissue-specific disease phenotypes?
    • Hutchison, C. J., Alvarez-Reyes, M., and Vaughan, O. A. (2001). Lamins in disease: Why do ubiquitously expressed nuclear envelope proteins give rise to tissue-specific disease phenotypes? J. Cell Sci. 114, 9-19.
    • (2001) J. Cell Sci. , vol.114 , pp. 9-19
    • Hutchison, C.J.1    Alvarez-Reyes, M.2    Vaughan, O.A.3
  • 186
    • 0032547734 scopus 로고    scopus 로고
    • Functional differences between keratins of stratified and simple epithelia
    • Hutton, E., Paladini, R. D., Yu, Q. C., Yen, M., Coulombe, P. A., and Fuchs, E. (1998). Functional differences between keratins of stratified and simple epithelia. J. Cell Biol. 143, 487-499.
    • (1998) J. Cell Biol. , vol.143 , pp. 487-499
    • Hutton, E.1    Paladini, R.D.2    Yu, Q.C.3    Yen, M.4    Coulombe, P.A.5    Fuchs, E.6
  • 190
    • 2042437650 scopus 로고    scopus 로고
    • Initial sequencing and analysis of the human genome
    • International Human Genome Sequencing Consortium. (2001). Initial sequencing and analysis of the human genome. Nature 409, 860-921.
    • (2001) Nature , vol.409 , pp. 860-921
  • 191
    • 0021888097 scopus 로고
    • Assembly of vimentin in vitro and its implications concerning the structure of intermediate filaments
    • Ip, W., Hartzer, M. K., Pang, Y.-Y. S., and Robson, R. M. (1985). Assembly of vimentin in vitro and its implications concerning the structure of intermediate filaments. J. Mol. Biol. 183, 365-375.
    • (1985) J. Mol. Biol. , vol.183 , pp. 365-375
    • Ip, W.1    Hartzer, M.K.2    Pang, Y.-Y.S.3    Robson, R.M.4
  • 192
    • 0032965997 scopus 로고    scopus 로고
    • Human keratin diseases: The increasing spectrum of disease and subtlety of the phenotype-genotype correlation
    • Irvine, A. D., and McLean, W. H. (1999). Human keratin diseases: The increasing spectrum of disease and subtlety of the phenotype-genotype correlation. Br. J. Dermatol. 140, 815-828.
    • (1999) Br. J. Dermatol. , vol.140 , pp. 815-828
    • Irvine, A.D.1    McLean, W.H.2
  • 193
    • 0014335827 scopus 로고
    • Mitosis and intermediate-sized filaments in developing skeletal muscle
    • Ishikawa, H., Bischoff, R., and Holtzer, H. (1968). Mitosis and intermediate-sized filaments in developing skeletal muscle. J. Cell Biol. 38, 538-555.
    • (1968) J. Cell Biol. , vol.38 , pp. 538-555
    • Ishikawa, H.1    Bischoff, R.2    Holtzer, H.3
  • 194
    • 0019198430 scopus 로고
    • Formation of cytoskeletal elements during mouse embryogenesis. Intermediate filaments of the cytokeratin type and desmosomes in preimplantation embryos
    • Jackson, B. W., Grund, C., Schmid, E., Burki, K., Franke, W. W., and Illmensee, K. (1980). Formation of cytoskeletal elements during mouse embryogenesis. Intermediate filaments of the cytokeratin type and desmosomes in preimplantation embryos. Differentiation 17, 161-179.
    • (1980) Differentiation , vol.17 , pp. 161-179
    • Jackson, B.W.1    Grund, C.2    Schmid, E.3    Burki, K.4    Franke, W.W.5    Illmensee, K.6
  • 195
    • 0019773566 scopus 로고
    • Formation of cytoskeletal elements during mouse embryogenesis. II. Epithelial differentiation and intermediate-sized filaments in early postimplantation embryos
    • Jackson, B. W., Grund, C., Winter, S., Franke, W. W., and Illmensee, K. (1981). Formation of cytoskeletal elements during mouse embryogenesis. II. Epithelial differentiation and intermediate-sized filaments in early postimplantation embryos. Differentiation 20, 203-216.
    • (1981) Differentiation , vol.20 , pp. 203-216
    • Jackson, B.W.1    Grund, C.2    Winter, S.3    Franke, W.W.4    Illmensee, K.5
  • 196
    • 0032817551 scopus 로고    scopus 로고
    • Disruption of type IV intermediate filament network in mice lacking the neurofilament medium and heavy subunits
    • Jacomy, H., Zhu, Q., Couillard-Despres, S., Beaulieu, J. M., and Julien, J. P. (1999). Disruption of type IV intermediate filament network in mice lacking the neurofilament medium and heavy subunits. J. Neurochem. 73, 972-984.
    • (1999) J. Neurochem. , vol.73 , pp. 972-984
    • Jacomy, H.1    Zhu, Q.2    Couillard-Despres, S.3    Beaulieu, J.M.4    Julien, J.P.5
  • 198
    • 0032821709 scopus 로고    scopus 로고
    • Neurofilament functions in health and disease
    • Julien, J. P. (1999). Neurofilament functions in health and disease. Curr. Opin. Neurobiol. 9, 554-560.
    • (1999) Curr. Opin. Neurobiol. , vol.9 , pp. 554-560
    • Julien, J.P.1
  • 199
    • 0035936804 scopus 로고    scopus 로고
    • Amyotrophic lateral sclerosis. Unfolding the toxicity of the misfolded
    • Julien, J. P. (2001). Amyotrophic lateral sclerosis. Unfolding the toxicity of the misfolded. Cell 104, 581-591.
    • (2001) Cell , vol.104 , pp. 581-591
    • Julien, J.P.1
  • 200
    • 0022827445 scopus 로고
    • Cloning and developmental expression of the murine neurofilament gene family
    • Julien, J. P., Meyer, D., Flavell, D., Hurst, J., and Grosveld, F. (1986). Cloning and developmental expression of the murine neurofilament gene family. Brain Res. 387, 243-250.
    • (1986) Brain Res. , vol.387 , pp. 243-250
    • Julien, J.P.1    Meyer, D.2    Flavell, D.3    Hurst, J.4    Grosveld, F.5
  • 201
    • 0034794332 scopus 로고    scopus 로고
    • Assembly of the epidermal cornified cell envelope
    • Kalinin, A., Marekov, L. N., and Steinert, P. M. (2001). Assembly of the epidermal cornified cell envelope. J. Cell Sci. 114, 3069-3070.
    • (2001) J. Cell Sci. , vol.114 , pp. 3069-3070
    • Kalinin, A.1    Marekov, L.N.2    Steinert, P.M.3
  • 202
    • 0034947231 scopus 로고    scopus 로고
    • Essential roles for four cytoplasmic intermediate filament proteins in Caenorhabditis elegans development
    • Karabinos, A., Schmidt, H., Harborth, J., Schnabel, R., and Weber, K. (2001). Essential roles for four cytoplasmic intermediate filament proteins in Caenorhabditis elegans development. Proc. Natl. Acad. Sci. USA 98, 7863-7868.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 7863-7868
    • Karabinos, A.1    Schmidt, H.2    Harborth, J.3    Schnabel, R.4    Weber, K.5
  • 203
    • 0021004748 scopus 로고
    • Specific attachment of desmin filaments to desmosomal plaques in cardiac myocytes
    • Kartenbeck, J., Schwechheimer, K., Moll, R., and Franke, W. W. (1983). Specific attachment of desmin filaments to desmosomal plaques in cardiac myocytes. EMBO J. 2, 735-742.
    • (1983) EMBO J. , vol.2 , pp. 735-742
    • Kartenbeck, J.1    Schwechheimer, K.2    Moll, R.3    Franke, W.W.4
  • 204
    • 0021331372 scopus 로고
    • Attachment of vimentin filaments to desmosomal plaques in human meningiomal cells and arachnoidal tissue
    • Kartenbeck, J., Schwechheimer, K., Moll, R., and Franke, W. W. (1984). Attachment of vimentin filaments to desmosomal plaques in human meningiomal cells and arachnoidal tissue. J. Cell Biol. 98, 1072-1081.
    • (1984) J. Cell Biol. , vol.98 , pp. 1072-1081
    • Kartenbeck, J.1    Schwechheimer, K.2    Moll, R.3    Franke, W.W.4
  • 205
    • 0038773214 scopus 로고
    • Replicating myoblasts express a muscle-specific phenotype
    • Kaufman, S. J., and Foster, R. F. (1988). Replicating myoblasts express a muscle-specific phenotype. Proc. Natl. Acad. Sci. USA 85, 9606-9610.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 9606-9610
    • Kaufman, S.J.1    Foster, R.F.2
  • 207
    • 0036514095 scopus 로고    scopus 로고
    • Expression of desmin in the basal epidermis of transgenic mice: A therapy for keratin deficiency syndromes?
    • Kirfel, J., Grund, C., Reifenberg, K., and Magin, T. M. (2002). Expression of desmin in the basal epidermis of transgenic mice: A therapy for keratin deficiency syndromes? Differentiation 70, 56-68.
    • (2002) Differentiation , vol.70 , pp. 56-68
    • Kirfel, J.1    Grund, C.2    Reifenberg, K.3    Magin, T.M.4
  • 209
    • 0030966529 scopus 로고    scopus 로고
    • The roles of maternal alpha-catenin and plakoglobin in the early Xenopus embryo
    • Kofron, M., Spagnuolo, A., Klymkowsky, M., Wylie, C., and Heasman, J. (1997). The roles of maternal alpha-catenin and plakoglobin in the early Xenopus embryo. Development 124, 1553-1560.
    • (1997) Development , vol.124 , pp. 1553-1560
    • Kofron, M.1    Spagnuolo, A.2    Klymkowsky, M.3    Wylie, C.4    Heasman, J.5
  • 210
    • 0034278759 scopus 로고    scopus 로고
    • Aggresomes and Russell bodies. Symptoms of cellular indigestion?
    • Kopito, R. R., and Sitia, R. (2000). Aggresomes and Russell bodies. Symptoms of cellular indigestion? EMBO Rep. 11, 225-231.
    • (2000) EMBO Rep. , vol.11 , pp. 225-231
    • Kopito, R.R.1    Sitia, R.2
  • 211
    • 0022512042 scopus 로고
    • Evidence for a polarity in the distribution of proteins from the cytoskeleton in Torpedo marmorata electrocytes
    • Kordeli, E., Cartaud, J., Nghiem, H. O., Pradel, L. A., Dubreuil, C., Paulin, D., and Changeux, J. P. (1986). Evidence for a polarity in the distribution of proteins from the cytoskeleton in Torpedo marmorata electrocytes. J. Cell Biol. 102, 748-761.
    • (1986) J. Cell Biol. , vol.102 , pp. 748-761
    • Kordeli, E.1    Cartaud, J.2    Nghiem, H.O.3    Pradel, L.A.4    Dubreuil, C.5    Paulin, D.6    Changeux, J.P.7
  • 212
    • 0031711226 scopus 로고    scopus 로고
    • AnkyrinG is associated with the postsynaptic membrane and the sarcoplasmic reticulum in the skeletal muscle fiber
    • Kordeli, E., Ludosky, M. A., Deprette, C., Frappier, T., and Cartaud, J. (1998). AnkyrinG is associated with the postsynaptic membrane and the sarcoplasmic reticulum in the skeletal muscle fiber. J. Cell Sci. 111, 2197-2207.
    • (1998) J. Cell Sci. , vol.111 , pp. 2197-2207
    • Kordeli, E.1    Ludosky, M.A.2    Deprette, C.3    Frappier, T.4    Cartaud, J.5
  • 213
    • 0026601521 scopus 로고
    • Extensive size polymorphism of the human keratin 10 chain resides in the C-terminal V2 subdomain due to variable numbers and sizes of glycine loops
    • Korge, B. P., Gan, S. Q., McBride, O. W., Mischke, D., and Steinert, P. M. (1992). Extensive size polymorphism of the human keratin 10 chain resides in the C-terminal V2 subdomain due to variable numbers and sizes of glycine loops. Proc. Natl. Acad. Sci. USA 89, 910-914.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 910-914
    • Korge, B.P.1    Gan, S.Q.2    McBride, O.W.3    Mischke, D.4    Steinert, P.M.5
  • 215
    • 0027484510 scopus 로고
    • In vitro assembly properties of vimentin mutagenized at the beta-site tail motif
    • Kouklis, P. D., Hatzfeld, M., Brunkener, M., Weber, K., and Georgatos, S. D. (1993). In vitro assembly properties of vimentin mutagenized at the beta-site tail motif. J. Cell Sci. 106, 919-928.
    • (1993) J. Cell Sci. , vol.106 , pp. 919-928
    • Kouklis, P.D.1    Hatzfeld, M.2    Brunkener, M.3    Weber, K.4    Georgatos, S.D.5
  • 216
    • 0027987929 scopus 로고
    • Making a connection: Direct binding between keratin intermediate filaments and desmosomal proteins
    • Kouklis, P. D., Hutton, E., and Fuchs, E. (1994). Making a connection: direct binding between keratin intermediate filaments and desmosomal proteins. J. Cell Biol. 127, 1049-1060.
    • (1994) J. Cell Biol. , vol.127 , pp. 1049-1060
    • Kouklis, P.D.1    Hutton, E.2    Fuchs, E.3
  • 217
    • 0031656747 scopus 로고    scopus 로고
    • Desmosomes: Intercellular adhesive junctions specialized for attachment of intermediate filaments
    • Kowalczyk, A. P., Bornslaeger, E. A., Norvell, S. M., Palka, H. L., and Green, K. J. (1999). Desmosomes: Intercellular adhesive junctions specialized for attachment of intermediate filaments. Int. Rev. Cytol. 185, 237-302.
    • (1999) Int. Rev. Cytol. , vol.185 , pp. 237-302
    • Kowalczyk, A.P.1    Bornslaeger, E.A.2    Norvell, S.M.3    Palka, H.L.4    Green, K.J.5
  • 218
    • 0020964827 scopus 로고
    • De novo synthesis and specific assembly of keratin filaments in nonepithelial cells after microinjection of mRNA for epidermal keratin
    • Kreis, T., Geiger, B., Schmid, E., Jorcano, J. L., and Franke, W. W. (1983). De novo synthesis and specific assembly of keratin filaments in nonepithelial cells after microinjection of mRNA for epidermal keratin. Cell 32, 1125-1137.
    • (1983) Cell , vol.32 , pp. 1125-1137
    • Kreis, T.1    Geiger, B.2    Schmid, E.3    Jorcano, J.L.4    Franke, W.W.5
  • 219
    • 0028865145 scopus 로고
    • Chronic hepatitis, hepatocyte fragility, and increased soluble phosphoglycokeratins in transgenic mice expressing a keratin 18 conserved arginnie mutant
    • Ku, N. O., Michie, S., Oshima, R. G., and Omary, M. B. (1995). Chronic hepatitis, hepatocyte fragility, and increased soluble phosphoglycokeratins in transgenic mice expressing a keratin 18 conserved arginnie mutant. J. Cell Biol. 131, 1303-1314.
    • (1995) J. Cell Biol. , vol.131 , pp. 1303-1314
    • Ku, N.O.1    Michie, S.2    Oshima, R.G.3    Omary, M.B.4
  • 220
    • 0031029525 scopus 로고    scopus 로고
    • Mutation of human keratin 18 in association with cryptogenic cirrhosis
    • Ku, N. O., Wright, T. L., Terrault, N. A., Gish, R., and Omary, M. B. (1997). Mutation of human keratin 18 in association with cryptogenic cirrhosis. J. Clin. Invest. 99, 19-23.
    • (1997) J. Clin. Invest. , vol.99 , pp. 19-23
    • Ku, N.O.1    Wright, T.L.2    Terrault, N.A.3    Gish, R.4    Omary, M.B.5
  • 221
    • 0032055050 scopus 로고    scopus 로고
    • Phosphorylation of human keratin 18 serine 33 regulates binding to 14-3-3 proteins
    • Ku, N. O., Liao, J., and Omary, M. B. (1998a). Phosphorylation of human keratin 18 serine 33 regulates binding to 14-3-3 proteins. EMBO J. 17, 1892-1906.
    • (1998) EMBO J. , vol.17 , pp. 1892-1906
    • Ku, N.O.1    Liao, J.2    Omary, M.B.3
  • 222
    • 0032576580 scopus 로고    scopus 로고
    • Mutation of a major keratin phosphorylation site predisposes to hepatotoxic injury in transgenic mice
    • Ku, N. O., Michie, S. A., Soetikno, R. M., Resurreccion, E. Z., Broome, R. L., and Omary, M. B. (1998b). Mutation of a major keratin phosphorylation site predisposes to hepatotoxic injury in transgenic mice. J. Cell Biol. 143, 2023-2032.
    • (1998) J. Cell Biol. , vol.143 , pp. 2023-2032
    • Ku, N.O.1    Michie, S.A.2    Soetikno, R.M.3    Resurreccion, E.Z.4    Broome, R.L.5    Omary, M.B.6
  • 223
    • 0033401358 scopus 로고    scopus 로고
    • The cytoskeleton of digestive epithelia in health and disease
    • Ku, N. O., Zhou, X., Toivola, D. M., and Omary, M. B. (1999). The cytoskeleton of digestive epithelia in health and disease. Am. J Physiol. 277, G1108-G1137.
    • (1999) Am. J. Physiol. , vol.277
    • Ku, N.O.1    Zhou, X.2    Toivola, D.M.3    Omary, M.B.4
  • 224
    • 0035942786 scopus 로고    scopus 로고
    • Keratin 8 mutations in patients with cryptogenic liver disease
    • Ku, N. O., Gish, R., Wright, T. L., and Omary, M. B. (2001). Keratin 8 mutations in patients with cryptogenic liver disease. N. Engl. J. Med. 344, 1580-1587.
    • (2001) N. Engl. J. Med. , vol.344 , pp. 1580-1587
    • Ku, N.O.1    Gish, R.2    Wright, T.L.3    Omary, M.B.4
  • 225
    • 0023929591 scopus 로고
    • Cloning of the human keratin 18 gene and its expression in nonepithelial mouse cells
    • Kulesh, D. A., and Oshima, R. G. (1988). Cloning of the human keratin 18 gene and its expression in nonepithelial mouse cells. Mol. Cell. Biol. 8, 1540-1550.
    • (1988) Mol. Cell. Biol. , vol.8 , pp. 1540-1550
    • Kulesh, D.A.1    Oshima, R.G.2
  • 226
    • 0032322895 scopus 로고    scopus 로고
    • Genetic control of extraembryonic cell lineages studied with tetraploid-diploid chimeric concepti
    • Kupriyanov, S., and Baribault, H. (1998). Genetic control of extraembryonic cell lineages studied with tetraploid-diploid chimeric concepti. Biochem. Cell Biol. 76, 1017-1027.
    • (1998) Biochem. Cell Biol. , vol.76 , pp. 1017-1027
    • Kupriyanov, S.1    Baribault, H.2
  • 227
    • 0026328816 scopus 로고
    • Anatomical mapping of Merkel cells in normal human adult epidermis
    • Lacour, J. P., Dubois, D., Pisani, A., and Ortonne, J. P. (1991). Anatomical mapping of Merkel cells in normal human adult epidermis. Br J. Dermatol. 125, 535-542.
    • (1991) Br J. Dermatol. , vol.125 , pp. 535-542
    • Lacour, J.P.1    Dubois, D.2    Pisani, A.3    Ortonne, J.P.4
  • 228
    • 0032517773 scopus 로고    scopus 로고
    • Cellular interaction of integrin alpha3beta1 with laminin 5 promotes gap junctional communication
    • Lampe, P. D., Nguyen, B. P., Gil, S., Usui, M., Olerud, J., Takada, Y., and Carter, W. G. (1998). Cellular interaction of integrin alpha3beta1 with laminin 5 promotes gap junctional communication. J. Cell Biol. 143, 1735-1747.
    • (1998) J. Cell Biol. , vol.143 , pp. 1735-1747
    • Lampe, P.D.1    Nguyen, B.P.2    Gil, S.3    Usui, M.4    Olerud, J.5    Takada, Y.6    Carter, W.G.7
  • 229
    • 0020633323 scopus 로고
    • Co-expression of vimentin and cytokeratins in parietal endoderm cells of early mouse embryo
    • Lane, E. B., Hogan, B. L., Kurkinen, M., and Garrels, J. I. (1983). Co-expression of vimentin and cytokeratins in parietal endoderm cells of early mouse embryo. Nature 303, 701-704.
    • (1983) Nature , vol.303 , pp. 701-704
    • Lane, E.B.1    Hogan, B.L.2    Kurkinen, M.3    Garrels, J.I.4
  • 230
    • 0026545645 scopus 로고
    • A mutation in the conserved helix termination peptide of keratin 5 in hereditary skin blistering
    • Lane, E. B., Rugg, E. L., Navsaria, H. I., Leigh, M., Heagerty, A. H., Ishida, Y. A., and Eady, R. A. (1992). A mutation in the conserved helix termination peptide of keratin 5 in hereditary skin blistering. Nature 356, 244-246.
    • (1992) Nature , vol.356 , pp. 244-246
    • Lane, E.B.1    Rugg, E.L.2    Navsaria, H.I.3    Leigh, M.4    Heagerty, A.H.5    Ishida, Y.A.6    Eady, R.A.7
  • 231
  • 232
    • 0035860762 scopus 로고    scopus 로고
    • The catalog of human hair keratins. II. Expression of the six type II members in the hair follicle and the combined catalog of human type I and II keratins
    • Langbein, L., Rogers, M. A., Winter, H., Praetzel, S., and Schweizer, J. (2001). The catalog of human hair keratins. II. Expression of the six type II members in the hair follicle and the combined catalog of human type I and II keratins. J. Biol. Chem. 276, 35123-35132.
    • (2001) J. Biol. Chem. , vol.276 , pp. 35123-35132
    • Langbein, L.1    Rogers, M.A.2    Winter, H.3    Praetzel, S.4    Schweizer, J.5
  • 233
    • 0022596012 scopus 로고
    • Association of spectrin with desmin intermediate filaments
    • Langley, R. C., Jr., and Cohen, C. M. (1986). Association of spectrin with desmin intermediate filaments. J. Cell. Biochem. 30, 101-109.
    • (1986) J. Cell. Biochem. , vol.30 , pp. 101-109
    • Langley R.C., Jr.1    Cohen, C.M.2
  • 234
    • 0023497802 scopus 로고
    • Cell type-specific association between two types of spectrin and two types of intermediate filaments
    • Langley, R. C., Jr., and Cohen, C. M. (1987). Cell type-specific association between two types of spectrin and two types of intermediate filaments. Cell Motil. Cytoskeleton 8, 165-173.
    • (1987) Cell Motil. Cytoskeleton , vol.8 , pp. 165-173
    • Langley R.C., Jr.1    Cohen, C.M.2
  • 235
    • 0018842868 scopus 로고
    • Intermediate filaments as mechanical integrators of cellular space
    • Lazarides, E. (1980). Intermediate filaments as mechanical integrators of cellular space. Nature 293, 249-256.
    • (1980) Nature , vol.293 , pp. 249-256
    • Lazarides, E.1
  • 236
    • 0020024240 scopus 로고
    • Intermediate filaments: A chemically heterogeneous, developmentally regulated class of proteins
    • Lazarides, E. (1982). Intermediate filaments: A chemically heterogeneous, developmentally regulated class of proteins. Annu. Rev. Biochem. 51, 219-250.
    • (1982) Annu. Rev. Biochem. , vol.51 , pp. 219-250
    • Lazarides, E.1
  • 237
    • 0011497688 scopus 로고
    • Immunological characterization of the subunit of the 100 A filaments from muscle cells
    • Lazarides, E., and Hubbard, B. D. (1976). Immunological characterization of the subunit of the 100 A filaments from muscle cells. Proc. Natl. Acad. Sci. USA 73, 4344-4348.
    • (1976) Proc. Natl. Acad. Sci. USA , vol.73 , pp. 4344-4348
    • Lazarides, E.1    Hubbard, B.D.2
  • 238
    • 0029972544 scopus 로고    scopus 로고
    • Neuronal intermediate filaments
    • Lee, M. K., and Cleveland, D. W. (1996). Neuronal intermediate filaments. Annu. Rev. Neurosci. 19, 187-217.
    • (1996) Annu. Rev. Neurosci. , vol.19 , pp. 187-217
    • Lee, M.K.1    Cleveland, D.W.2
  • 239
    • 0027293898 scopus 로고
    • Neurofilaments are obligate heteropolymers in vivo
    • Lee, M. K., Xu, Z., Wong, P. C., and Cleveland, D. W. (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
  • 240
    • 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., Marszalek, J. R., and Cleveland, D. W. (1994). A mutant neurofilament subunit causes massive, selective motor neuron death: Implications for the pathogenesis of human motor neuron disease. Neuron 13, 975-988.
    • (1994) Neuron , vol.13 , pp. 975-988
    • Lee, M.K.1    Marszalek, J.R.2    Cleveland, D.W.3
  • 241
    • 0348047709 scopus 로고
    • Alzheimer disease tangles share immunological similarities with multiphosphorylation repeats in the two large neurofilament proteins
    • Lee, V. M., Otvos, L., Jr., Schmidt, M. L., and Trojanowski, J. Q. (1988). Alzheimer disease tangles share immunological similarities with multiphosphorylation repeats in the two large neurofilament proteins. Proc. Natl. Acad. Sci. USA 85, 7384-7388.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 7384-7388
    • Lee, V.M.1    Otvos L., Jr.2    Schmidt, M.L.3    Trojanowski, J.Q.4
  • 242
    • 0031005809 scopus 로고    scopus 로고
    • Insertional mutation of the Drosophila nuclear lamin Dmo gene results in defective nuclear envelopes, clustering of nuclear pore cpmplexes, and accumulation of annulate lamellae
    • Lenz-Bohme, B., Wismar, J., Fuchs, S., Reifegerste, R., Buchner, E., Betz, H., and Schmitt, B. (1997). Insertional mutation of the Drosophila nuclear lamin Dmo gene results in defective nuclear envelopes, clustering of nuclear pore cpmplexes, and accumulation of annulate lamellae. J. Cell Biol. 137, 1001-1016.
    • (1997) J. Cell Biol. , vol.137 , pp. 1001-1016
    • Lenz-Bohme, B.1    Wismar, J.2    Fuchs, S.3    Reifegerste, R.4    Buchner, E.5    Betz, H.6    Schmitt, B.7
  • 243
    • 0023892995 scopus 로고
    • Molecular characterization and expression of the stratification-related cytokeratins 4 and 15
    • Leube, R. E., Bader, B. L., Bosch, F. X., Zimbelmann, R., Achtstaetter, T., and Franke, W. W. (1988). Molecular characterization and expression of the stratification-related cytokeratins 4 and 15. J. Cell Biol. 106, 1249-1261.
    • (1988) J. Cell Biol. , vol.106 , pp. 1249-1261
    • Leube, R.E.1    Bader, B.L.2    Bosch, F.X.3    Zimbelmann, R.4    Achtstaetter, T.5    Franke, W.W.6
  • 247
    • 0030273614 scopus 로고    scopus 로고
    • GFAP is necessary for the integrity of CNS white matter architecture and long-term maintenance of myelination
    • Liedtke, W., Edelmann, W., Bieri, P. L., Chiu, N. J., Cowan, F. C., Kucherlapati, R., and Raine, C. S. (1996). GFAP is necessary for the integrity of CNS white matter architecture and long-term maintenance of myelination. Neuron 17, 607-615.
    • (1996) Neuron , vol.17 , pp. 607-615
    • Liedtke, W.1    Edelmann, W.2    Bieri, P.L.3    Chiu, N.J.4    Cowan, F.C.5    Kucherlapati, R.6    Raine, C.S.7
  • 248
    • 0022245790 scopus 로고
    • Purification of the 300K intermediate filament-associated protein and its in vitro recombination with intermediate filaments
    • Lieska, N., Yang, H. Y., and Goldman, R. D. (1985). Purification of the 300K intermediate filament-associated protein and its in vitro recombination with intermediate filaments. J. Cell Biol. 101, 802-813.
    • (1985) J. Cell Biol. , vol.101 , pp. 802-813
    • Lieska, N.1    Yang, H.Y.2    Goldman, R.D.3
  • 249
    • 0033749567 scopus 로고    scopus 로고
    • Essential roles for Caenorhabditis elegans lamin gene in nuclear organization, cell cycle progression, and spatial organization of nuclear pore complexes
    • Liu, J., Ben Shahar, T. R., Riemer, D., Treinin, M., Spann, P., Weber, K., Fire, A., and Gruenbaum, Y. (2000). Essential roles for Caenorhabditis elegans lamin gene in nuclear organization, cell cycle progression, and spatial organization of nuclear pore complexes. Mol. Biol. Cell 11, 3937-3947.
    • (2000) Mol. Biol. Cell , vol.11 , pp. 3937-3947
    • Liu, J.1    Ben Shahar, T.R.2    Riemer, D.3    Treinin, M.4    Spann, P.5    Weber, K.6    Fire, A.7    Gruenbaum, Y.8
  • 250
    • 0034984620 scopus 로고    scopus 로고
    • Expression of a truncated keratin 5 may contribute to severe palmar-plantar hyperkeratosis in epidermolysis bullosa simplex patients
    • Livingston, R. J., Sybert, V. P., Smith, L. T., Dale, B. A., Presland, R. B., and Stephens, K. (2001). Expression of a truncated keratin 5 may contribute to severe palmar-plantar hyperkeratosis in epidermolysis bullosa simplex patients. J. Invest. Dermatol. 116, 970-974.
    • (2001) J. Invest. Dermatol. , vol.116 , pp. 970-974
    • Livingston, R.J.1    Sybert, V.P.2    Smith, L.T.3    Dale, B.A.4    Presland, R.B.5    Stephens, K.6
  • 251
    • 0029043889 scopus 로고
    • The basal keratin network of stratified squamous epithelia: Defining K15 function in the absence of K14
    • Lloyd, C., Yu, Q. C., Cheng, J., Turksen, K., Degenstein, L., Hutton, E., and Fuchs, E. (1995). The basal keratin network of stratified squamous epithelia: Defining K15 function in the absence of K14. J. Cell Biol. 129, 1329-1344.
    • (1995) J. Cell Biol. , vol.129 , pp. 1329-1344
    • Lloyd, C.1    Yu, Q.C.2    Cheng, J.3    Turksen, K.4    Degenstein, L.5    Hutton, E.6    Fuchs, E.7
  • 254
    • 0031947591 scopus 로고    scopus 로고
    • Activated keratinocytes in the epidermis of hypertrophic scars
    • Machesney, M., Tidman, N., Waseem, A., Kirby, L., and Leigh, I. (1998). Activated keratinocytes in the epidermis of hypertrophic scars. Am. J. Pathol. 152, 1133-1141.
    • (1998) Am. J. Pathol. , vol.152 , pp. 1133-1141
    • Machesney, M.1    Tidman, N.2    Waseem, A.3    Kirby, L.4    Leigh, I.5
  • 255
    • 0027254919 scopus 로고
    • The mechanism of interaction of filaggrin with intermediate filaments. The ionic zipper hypothesis
    • Mack, J. W., Steven, A. C., and Steinert, P. M. (1993). The mechanism of interaction of filaggrin with intermediate filaments. The ionic zipper hypothesis. J. Mol. Biol. 232, 50-66.
    • (1993) J. Mol. Biol. , vol.232 , pp. 50-66
    • Mack, J.W.1    Steven, A.C.2    Steinert, P.M.3
  • 256
    • 0025696851 scopus 로고
    • De novo formation of cytokeratin filaments in calf lens cells and cytoplasts after transfection with cDNAs or microinjection with mRNAs encoding human cytokeratins
    • Magin, T. M., Bader, B., Freudenmann, M., and Franke, W. W. (1990). De novo formation of cytokeratin filaments in calf lens cells and cytoplasts after transfection with cDNAs or microinjection with mRNAs encoding human cytokeratins. Eur. J. Cell Biol. 53, 333-348.
    • (1990) Eur. J. Cell Biol. , vol.53 , pp. 333-348
    • Magin, T.M.1    Bader, B.2    Freudenmann, M.3    Franke, W.W.4
  • 257
    • 2642684550 scopus 로고    scopus 로고
    • Lessons from keratin 18 knockout mice: Formation of novel keratin filaments, secondary loss of keratin 7 and accumulation of liver-specific keratin 8-positive aggregates
    • Magin, T. M., Schroder, R., Leitgeb, S., Wanninger, F., Zatloukal, K., Grund, C., and Melton, D. W. (1998). Lessons from keratin 18 knockout mice: Formation of novel keratin filaments, secondary loss of keratin 7 and accumulation of liver-specific keratin 8-positive aggregates. J. Cell Biol. 140, 1441-1451.
    • (1998) J. Cell Biol. , vol.140 , pp. 1441-1451
    • Magin, T.M.1    Schroder, R.2    Leitgeb, S.3    Wanninger, F.4    Zatloukal, K.5    Grund, C.6    Melton, D.W.7
  • 258
    • 0034534608 scopus 로고    scopus 로고
    • Supplementation of a mutant keratin by stable expression of desmin in cultured human EBS keratinocytes
    • Magin, T. M., Kaiser, H. W., Leitgeb, S., Grund, C., Leigh, I. M., Morely, S. M., and Lane, E. B. (2000a). Supplementation of a mutant keratin by stable expression of desmin in cultured human EBS keratinocytes. J. Cell Sci. 113, 4231-4239.
    • (2000) J. Cell Sci. , vol.113 , pp. 4231-4239
    • Magin, T.M.1    Kaiser, H.W.2    Leitgeb, S.3    Grund, C.4    Leigh, I.M.5    Morely, S.M.6    Lane, E.B.7
  • 259
    • 0034078564 scopus 로고    scopus 로고
    • Novel insights into intermediate filament function from studies of transgenic and knockout mice
    • Magin, T. M., Hesse, M., and Schroder, R. (2000b). Novel insights into intermediate filament function from studies of transgenic and knockout mice. Protoplasma 211, 140-150.
    • (2000) Protoplasma , vol.211 , pp. 140-150
    • Magin, T.M.1    Hesse, M.2    Schroder, R.3
  • 260
    • 0030755443 scopus 로고    scopus 로고
    • A novel nonepidermolytic palmoplantar keratoderma: A clinical and histopathologic study of six cases
    • Magro, C. M., Baden, L. A., Crowson, A. N., Bowden, P. E., and Baden, H. P. (1997). A novel nonepidermolytic palmoplantar keratoderma: A clinical and histopathologic study of six cases. J. Am. Acad. Dermatol. 37, 27-33.
    • (1997) J. Am. Acad. Dermatol. , vol.37 , pp. 27-33
    • Magro, C.M.1    Baden, L.A.2    Crowson, A.N.3    Bowden, P.E.4    Baden, H.P.5
  • 261
    • 0035861737 scopus 로고    scopus 로고
    • Homerin, a novel profilaggrin-like protein and differentiation-specific marker isolated from mouse skin
    • Makino, T., Takaishi, M., Morohashi, M., and Huh, N. H. (2001). Homerin, a novel profilaggrin-like protein and differentiation-specific marker isolated from mouse skin. J. Biol. Chem. 276, 47445-47452.
    • (2001) J. Biol. Chem. , vol.276 , pp. 47445-47452
    • Makino, T.1    Takaishi, M.2    Morohashi, M.3    Huh, N.H.4
  • 262
    • 0032949408 scopus 로고    scopus 로고
    • Intermediate filaments in motion: Observations of intermediate filaments in cells using green fluorescent protein-vimentin
    • Martys, J. L., Ho, C. L., Liem, R. K., and Gundersen, G. G. (1999). Intermediate filaments in motion: Observations of intermediate filaments in cells using green fluorescent protein-vimentin. Mol. Biol. Cell 10, 1289-1295.
    • (1999) Mol. Biol. Cell , vol.10 , pp. 1289-1295
    • Martys, J.L.1    Ho, C.L.2    Liem, R.K.3    Gundersen, G.G.4
  • 263
    • 0011358850 scopus 로고    scopus 로고
    • On the rigidity of the cytoskeleton: Are MAPs crosslinkers or spacers of microtubules?
    • Marx, A., Pless, J., Mandelkow, E.-M., and Mandelkow, E. (2000). On the rigidity of the cytoskeleton: Are MAPs crosslinkers or spacers of microtubules? Cell. Mol. Biol. 46, 949-965.
    • (2000) Cell. Mol. Biol. , vol.46 , pp. 949-965
    • Marx, A.1    Pless, J.2    Mandelkow, E.-M.3    Mandelkow, E.4
  • 265
    • 0032234101 scopus 로고    scopus 로고
    • The wound repair-associated keratins 6, 16, and 17. Insights into the role of intermediate filaments in specifying keratinocyte cytoarchitecture
    • McGowan, K., and Coulombe, P. A. (1998). The wound repair-associated keratins 6, 16, and 17. Insights into the role of intermediate filaments in specifying keratinocyte cytoarchitecture. Subcell. Biochem. 31, 173-204.
    • (1998) Subcell. Biochem. , vol.31 , pp. 173-204
    • McGowan, K.1    Coulombe, P.A.2
  • 266
    • 0034118521 scopus 로고    scopus 로고
    • Keratin 17 expression in the hard epithelial context of the hair and nail, and its relevance for the pachyonychia congenita phenotype
    • McGowan, K. M., and Coulombe, P. A. (2000). Keratin 17 expression in the hard epithelial context of the hair and nail, and its relevance for the pachyonychia congenita phenotype. J. Invest. Dermatol. 114, 1101-1107.
    • (2000) J. Invest. Dermatol. , vol.114 , pp. 1101-1107
    • McGowan, K.M.1    Coulombe, P.A.2
  • 268
    • 0028936437 scopus 로고
    • Intermediate filaments in disease
    • McLean, W. H., and Lane, E. B. (1995). Intermediate filaments in disease. Curr. Opin. Cell Biol. 7, 118-125.
    • (1995) Curr. Opin. Cell Biol. , vol.7 , pp. 118-125
    • McLean, W.H.1    Lane, E.B.2
  • 269
    • 0033824641 scopus 로고    scopus 로고
    • GFAP null astrocytes are a favorable substrate for neuronal survival and neurite growth
    • Menet, V., Gimenez, Y. R., Sandillon, F., and Privat, A. (2000). GFAP null astrocytes are a favorable substrate for neuronal survival and neurite growth. Glia 31, 267-272.
    • (2000) Glia , vol.31 , pp. 267-272
    • Menet, V.1    Gimenez, Y.R.2    Sandillon, F.3    Privat, A.4
  • 270
    • 0030856050 scopus 로고    scopus 로고
    • Two-hybrid analysis reveals fundamental differences in direct interactions between desmoplakin and cell type-specific intermediate filaments
    • Meng, J. J., Bornslaeger, E. A., Green, K. J., Steinert, P. M., and Ip, W. (1997). Two-hybrid analysis reveals fundamental differences in direct interactions between desmoplakin and cell type-specific intermediate filaments. J. Biol. Chem. 272, 21495-21503.
    • (1997) J. Biol. Chem. , vol.272 , pp. 21495-21503
    • Meng, J.J.1    Bornslaeger, E.A.2    Green, K.J.3    Steinert, P.M.4    Ip, W.5
  • 272
    • 0032970165 scopus 로고    scopus 로고
    • Desmosomal plakophilin 2 as a differentiation marker in normal and malignant tissues
    • Mertens, C., Kuhn, C., Moll, R., Schwetlick, I., and Franke, W. W. (1999). Desmosomal plakophilin 2 as a differentiation marker in normal and malignant tissues. Differentiation 64, 277-290.
    • (1999) Differentiation , vol.64 , pp. 277-290
    • Mertens, C.1    Kuhn, C.2    Moll, R.3    Schwetlick, I.4    Franke, W.W.5
  • 275
    • 0029970965 scopus 로고    scopus 로고
    • Keratin 19 as a biochemical marker of skin stem cells in vivo and in vitro: Keratin 19 expressing cells are differentially localized in function of anatomic sites, and their number varies with donor age and culture stage
    • Michel, M., Torok, N., Godbout, M. J., Lussier, M., Gaudreau, P., Royal, A., and Germain, L, (1996). Keratin 19 as a biochemical marker of skin stem cells in vivo and in vitro: Keratin 19 expressing cells are differentially localized in function of anatomic sites, and their number varies with donor age and culture stage. J. Cell Sci. 109, 1017-1028.
    • (1996) J. Cell Sci. , vol.109 , pp. 1017-1028
    • Michel, M.1    Torok, N.2    Godbout, M.J.3    Lussier, M.4    Gaudreau, P.5    Royal, A.6    Germain, L.7
  • 276
    • 0035802226 scopus 로고    scopus 로고
    • Future for ovarian cancer screening: Novel markers from emerging technologies of transcriptional profiling and proteomics
    • Mills, G. B., Bast, R. C., Jr., and Srivastava, S. (2001). Future for ovarian cancer screening: Novel markers from emerging technologies of transcriptional profiling and proteomics. J. Natl. Cancer Inst. 93, 1437-1439.
    • (2001) J. Natl. Cancer Inst. , vol.93 , pp. 1437-1439
    • Mills, G.B.1    Bast R.C., Jr.2    Srivastava, S.3
  • 277
    • 0035940437 scopus 로고    scopus 로고
    • The intestinal stem cell niche: There grows the neighborhood
    • Mills, J. C., and Gordon, J. I. (2001). The intestinal stem cell niche: There grows the neighborhood. Proc. Natl. Acad. Sci. USA 98, 12334-12336.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 12334-12336
    • Mills, J.C.1    Gordon, J.I.2
  • 278
    • 0034683573 scopus 로고    scopus 로고
    • Desmin cytoskeleton linked to muscle mitochondrial distribution and respiratory function
    • Milner, D. J., Mavroidis, M., Weisleder, N., and Capetanaki, Y. (2000). Desmin cytoskeleton linked to muscle mitochondrial distribution and respiratory function. J. Cell Biol. 150, 1283-1298.
    • (2000) J. Cell Biol. , vol.150 , pp. 1283-1298
    • Milner, D.J.1    Mavroidis, M.2    Weisleder, N.3    Capetanaki, Y.4
  • 279
    • 0029738727 scopus 로고    scopus 로고
    • Disruption of muscle architecture and myocardial degeneration in mice lacking desmin
    • Milner, D. J., Weitzer, G., Tran, D., Bradley, A., and Capetanaki, Y. (1996). Disruption of muscle architecture and myocardial degeneration in mice lacking desmin. J. Cell Biol. 134, 1255-1270.
    • (1996) J. Cell Biol. , vol.134 , pp. 1255-1270
    • Milner, D.J.1    Weitzer, G.2    Tran, D.3    Bradley, A.4    Capetanaki, Y.5
  • 280
    • 0028572509 scopus 로고
    • Binding of keratin intermediate filaments (K10) to the cornified envelope in mouse epidermis: Implications for barrier function
    • Ming, M. E., Daryanani, H. A., Roberts, L. P., Baden, H. P., and Kvedar, J. C. (1994). Binding of keratin intermediate filaments (K10) to the cornified envelope in mouse epidermis: implications for barrier function. J. Invest. Dermatol. 103, 780-784.
    • (1994) J. Invest. Dermatol. , vol.103 , pp. 780-784
    • Ming, M.E.1    Daryanani, H.A.2    Roberts, L.P.3    Baden, H.P.4    Kvedar, J.C.5
  • 281
    • 0023153775 scopus 로고
    • Polymorphic keratins in human epidermis
    • Mischke, D., and Wild, G. (1987). Polymorphic keratins in human epidermis. J. Invest. Dermatol. 88, 191-197.
    • (1987) J. Invest. Dermatol. , vol.88 , pp. 191-197
    • Mischke, D.1    Wild, G.2
  • 282
    • 0042611650 scopus 로고    scopus 로고
    • Genomic organization and single-nucleotide polymorphism map of desmuslin, a novel intermediate filament protein on chromosome 15q26.3
    • Mizuno, Y., Puca, A. A., O'Brien, K. F., Beggs, A. H., and Kunkel, L. M. (2001a). Genomic organization and single-nucleotide polymorphism map of desmuslin, a novel intermediate filament protein on chromosome 15q26.3. BMC Genet. 2, 8.
    • (2001) BMC Genet. , vol.2 , pp. 8
    • Mizuno, Y.1    Puca, A.A.2    O'Brien, K.F.3    Beggs, A.H.4    Kunkel, L.M.5
  • 284
    • 0032233043 scopus 로고    scopus 로고
    • Cytokeratins as markers of differentiation in the diagnosis of epithelial tumors
    • H. Herrmann and J. R. Harris, Eds. Plenum, New York
    • Moll, R. (1998). Cytokeratins as markers of differentiation in the diagnosis of epithelial tumors. In "Intermediate Filaments: Subcellular Biochemistry" (H. Herrmann and J. R. Harris, Eds.), Vol. 31, pp. 205-262. Plenum, New York.
    • (1998) Intermediate Filaments: Subcellular Biochemistry , vol.31 , pp. 205-262
    • Moll, R.1
  • 285
    • 0020467073 scopus 로고
    • The catalog of human cytokeratins: Patterns of expression in normal epithelia, tumors and cultured cells
    • Moll, R., Franke, W. W., Schiller, D. L., Geiger, B., and Krepler, R. (1982). The catalog of human cytokeratins: Patterns of expression in normal epithelia, tumors and cultured cells. Cell 31, 11-24.
    • (1982) Cell , vol.31 , pp. 11-24
    • Moll, R.1    Franke, W.W.2    Schiller, D.L.3    Geiger, B.4    Krepler, R.5
  • 286
    • 0028012217 scopus 로고
    • Effects of ultraviolet B radiation on cytoskeletal and adhesion molecules in human epidermis
    • Moll, I., Bohnert, E., Treib, U., and Jung, E. G. (1994). Effects of ultraviolet B radiation on cytoskeletal and adhesion molecules in human epidermis. Photodermatol. Photoimmunol. Photomed. 10, 26-32.
    • (1994) Photodermatol. Photoimmunol. Photomed. , vol.10 , pp. 26-32
    • Moll, I.1    Bohnert, E.2    Treib, U.3    Jung, E.G.4
  • 287
    • 0020538869 scopus 로고
    • Biochemical and immunological characterization of desmoplakins I and II, the major polypeptides of the desmosomal plaque
    • Müller, H., and Franke, W. W. (1983). Biochemical and immunological characterization of desmoplakins I and II, the major polypeptides of the desmosomal plaque. J. Mol. Biol. 163, 647-671.
    • (1983) J. Mol. Biol. , vol.163 , pp. 647-671
    • Müller, H.1    Franke, W.W.2
  • 288
    • 0029116226 scopus 로고
    • Elements controlling the expression and induction of the skin hyperproliferation-associated keratin K6
    • Navarro, J. M., Casatorres, J., and Jorcano, J. L. (1995). Elements controlling the expression and induction of the skin hyperproliferation-associated keratin K6. J. Biol. Chem. 270, 21362-21367.
    • (1995) J. Biol. Chem. , vol.270 , pp. 21362-21367
    • Navarro, J.M.1    Casatorres, J.2    Jorcano, J.L.3
  • 289
    • 0035794230 scopus 로고    scopus 로고
    • Syncoilin, a novel member of the intermediate filament superfamily that interacts with alpha-dystrobrevin in skeletal muscle
    • Newey, S. E., Howman, E. V., Ponting, C. P., Benson, M. A., Nawrotzki, R., Loh, N. Y., Davies, K. E., and Blake, D. J. (2001). Syncoilin, a novel member of the intermediate filament superfamily that interacts with alpha-dystrobrevin in skeletal muscle. J. Biol. Chem. 276, 6645-6655.
    • (2001) J. Biol. Chem. , vol.276 , pp. 6645-6655
    • Newey, S.E.1    Howman, E.V.2    Ponting, C.P.3    Benson, M.A.4    Nawrotzki, R.5    Loh, N.Y.6    Davies, K.E.7    Blake, D.J.8
  • 290
    • 0025190741 scopus 로고
    • Localization of newly synthesized vimentin subunits reveals a novel mechanism of intermediate filament assembly
    • Ngai, J., Coleman, T. R., and Lazarides, E. (1990). Localization of newly synthesized vimentin subunits reveals a novel mechanism of intermediate filament assembly. Cell 60, 415-427.
    • (1990) Cell , vol.60 , pp. 415-427
    • Ngai, J.1    Coleman, T.R.2    Lazarides, E.3
  • 291
    • 17744368458 scopus 로고    scopus 로고
    • Deregulation of Cdk5 in a mouse model of ALS: Toxicity alleviated by perikaryal neurofilament inclusions
    • Nguyen, M. D., Lariviere, R. C., and Julien, J. P. (2001). Deregulation of Cdk5 in a mouse model of ALS: Toxicity alleviated by perikaryal neurofilament inclusions. Neuron 30, 135-147.
    • (2001) Neuron , vol.30 , pp. 135-147
    • Nguyen, M.D.1    Lariviere, R.C.2    Julien, J.P.3
  • 293
    • 0024801564 scopus 로고
    • Keratin, transglutaminase, and mallory bodies - The really insoluble stuff
    • Osborn, M., and Weber, K. (1989). Keratin, transglutaminase, and mallory bodies - The really insoluble stuff. Lab. Invest. 61, 585-587.
    • (1989) Lab. Invest. , vol.61 , pp. 585-587
    • Osborn, M.1    Weber, K.2
  • 294
    • 0018789453 scopus 로고
    • Purified desmin from adult mammalian skeletal muscle: A peptide mapping comparison with desmins from adult mammalian and avian smooth muscle
    • O'Shea, J. M., Robson, R. M., Huiatt, T. W., Hartzer, M. K., and Stomer, M. H. (1979). Purified desmin from adult mammalian skeletal muscle: A peptide mapping comparison with desmins from adult mammalian and avian smooth muscle. Biochem. Biophys. Res. Commun. 89, 972-980.
    • (1979) Biochem. Biophys. Res. Commun. , vol.89 , pp. 972-980
    • O'Shea, J.M.1    Robson, R.M.2    Huiatt, T.W.3    Hartzer, M.K.4    Stomer, M.H.5
  • 295
    • 0035951372 scopus 로고    scopus 로고
    • Morphogenesis and renewal of hair follicles from adult multipotent stem cells
    • Oshima, H., Rochat, A., Kedzia, C., Kobayashi, K., and Barrandon, Y. (2001). Morphogenesis and renewal of hair follicles from adult multipotent stem cells. Cell 104, 233-245.
    • (2001) Cell , vol.104 , pp. 233-245
    • Oshima, H.1    Rochat, A.2    Kedzia, C.3    Kobayashi, K.4    Barrandon, Y.5
  • 296
    • 0021064832 scopus 로고
    • Intermediate filament protein synthesis in preimplantation murine embryos
    • Oshima, R. G., Howe, W. E., Klier, F. G., Adamson, E. D., and Shevinsky, L. H. (1983). Intermediate filament protein synthesis in preimplantation murine embryos. Dev. Biol. 99, 447-455.
    • (1983) Dev. Biol. , vol.99 , pp. 447-455
    • Oshima, R.G.1    Howe, W.E.2    Klier, F.G.3    Adamson, E.D.4    Shevinsky, L.H.5
  • 297
    • 0030035021 scopus 로고    scopus 로고
    • Onset of reepithelialization after skin injury correlates with a reorganization of keratin filaments in wound edge keratinocytes: Defining a potential role for keratin 16
    • Paladini, R. D., Takahashi, K., Bravo, N. S., and Coulombe, P. A. (1996). Onset of reepithelialization after skin injury correlates with a reorganization of keratin filaments in wound edge keratinocytes: defining a potential role for keratin 16. J. Cell Biol. 132, 381-397.
    • (1996) J. Cell Biol. , vol.132 , pp. 381-397
    • Paladini, R.D.1    Takahashi, K.2    Bravo, N.S.3    Coulombe, P.A.4
  • 298
    • 0032563572 scopus 로고    scopus 로고
    • Directed expression of keratin 16 to the progenitor basal cells of transgenic mouse skin delays skin maturation
    • Paladini, R. D., and Coulombe, P. A. (1999). Directed expression of keratin 16 to the progenitor basal cells of transgenic mouse skin delays skin maturation. J. Cell Biol. 142, 1035-1051.
    • (1999) J. Cell Biol. , vol.142 , pp. 1035-1051
    • Paladini, R.D.1    Coulombe, P.A.2
  • 299
    • 0032824490 scopus 로고    scopus 로고
    • The functional diversity of epidermal keratins revealed by the partial rescue of the keratin 14 null phenotype by keratin 16
    • Paladini, R. D., and Coulombe, P. A. (1999). The functional diversity of epidermal keratins revealed by the partial rescue of the keratin 14 null phenotype by keratin 16. J. Cell Biol. 146, 1185-1201.
    • (1999) J. Cell Biol. , vol.146 , pp. 1185-1201
    • Paladini, R.D.1    Coulombe, P.A.2
  • 301
    • 0034791125 scopus 로고    scopus 로고
    • Inhibition of protein kinase B (PKB) and PKCζ mediates keratin K10-induced cell cycle arrest
    • Paramio, J. M., Segrelles, C., Ruiz, S., and Jorcano, J. L. (2001). Inhibition of protein kinase B (PKB) and PKCζ mediates keratin K10-induced cell cycle arrest. Mol. Cell. Biol. 21, 7449-7459.
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 7449-7459
    • Paramio, J.M.1    Segrelles, C.2    Ruiz, S.3    Jorcano, J.L.4
  • 302
    • 0002255793 scopus 로고    scopus 로고
    • Structural features of IF proteins
    • T. Kreis and R. Vale, Eds. Oxford University Press, Oxford
    • Parry, D. A. D. (1999). Structural features of IF proteins. In "Guidebook to the Cytoskeletal and Motor Proteins" (T. Kreis and R. Vale, Eds.), pp. 285-291. Oxford University Press, Oxford.
    • (1999) Guidebook to the Cytoskeletal and Motor Proteins , pp. 285-291
    • Parry, D.A.D.1
  • 304
    • 0033540060 scopus 로고    scopus 로고
    • Conversion of p35 to p25 deregulates Cdk5 activity and promotes neurodegeneration
    • Patrick, G. N., Zukerberg, L., Nikolic, M., de la Monte, S., Dikkes, P., and Tsai, L. H. (1999). Conversion of p35 to p25 deregulates Cdk5 activity and promotes neurodegeneration. Nature 402, 615-622.
    • (1999) Nature , vol.402 , pp. 615-622
    • Patrick, G.N.1    Zukerberg, L.2    Nikolic, M.3    De la Monte, S.4    Dikkes, P.5    Tsai, L.H.6
  • 305
    • 0019121814 scopus 로고
    • Antibodies as probes of cellular differentiation and cytoskeletal organization in the mouse blastocyst
    • Paulin, D., Babinet, C., Weber, K., and Osborn, M. (1980). Antibodies as probes of cellular differentiation and cytoskeletal organization in the mouse blastocyst. Exp. Cell Res. 130, 297-304.
    • (1980) Exp. Cell Res. , vol.130 , pp. 297-304
    • Paulin, D.1    Babinet, C.2    Weber, K.3    Osborn, M.4
  • 306
    • 0021923259 scopus 로고
    • Scanning electron microscope study of tongue development in the CD-1 mouse fetus
    • Paulson, R. B., Hayes, T. G., and Sucheston, M. E. (1985). Scanning electron microscope study of tongue development in the CD-1 mouse fetus. J. Craniofac. Genet. Dev. Biol. 5, 59-73.
    • (1985) J. Craniofac. Genet. Dev. Biol. , vol.5 , pp. 59-73
    • Paulson, R.B.1    Hayes, T.G.2    Sucheston, M.E.3
  • 307
    • 0035783778 scopus 로고    scopus 로고
    • Astrocytic intermediate filaments: Lessons from GFAP and vimentin knock-out mice
    • Pekny, M. (2001). Astrocytic intermediate filaments: Lessons from GFAP and vimentin knock-out mice. Prog. Brain Res. 132, 23-30.
    • (2001) Prog. Brain Res. , vol.132 , pp. 23-30
    • Pekny, M.1
  • 308
    • 0029012164 scopus 로고
    • Mice lacking glial fibrillary acidic protein display astrocytes devoid of intermediate filaments but develop and reproduce normally
    • Pekny, M., Leveen, P., Pekna, M., Eliasson, C., Berthold, C. H., Westermark, B., and Betsholtz, C. (1995). Mice lacking glial fibrillary acidic protein display astrocytes devoid of intermediate filaments but develop and reproduce normally. EMBO J. 14, 1590-1598.
    • (1995) EMBO J. , vol.14 , pp. 1590-1598
    • Pekny, M.1    Leveen, P.2    Pekna, M.3    Eliasson, C.4    Berthold, C.H.5    Westermark, B.6    Betsholtz, C.7
  • 309
    • 0035158066 scopus 로고    scopus 로고
    • Complete cytolysis and neonatal lethality in keratin 5 knockout mice reveal its fundamental role in skin integrity and in epidermolysis bullosa simplex
    • Peters, B., Kirfel, J., Bussow, H., Vidal, M., and Magin, T. M. (2001). Complete cytolysis and neonatal lethality in keratin 5 knockout mice reveal its fundamental role in skin integrity and in epidermolysis bullosa simplex. Mol. Biol. Cell 12, 1775-1789.
    • (2001) Mol. Biol. Cell , vol.12 , pp. 1775-1789
    • Peters, B.1    Kirfel, J.2    Bussow, H.3    Vidal, M.4    Magin, T.M.5
  • 310
    • 0028352092 scopus 로고
    • Characterization of a shared epitope in cortical Lewy body fibrils and Alzheimer paired helical filaments
    • Pollanen, M. S., Bergeron, C., and Weyer, L. (1994). Characterization of a shared epitope in cortical Lewy body fibrils and Alzheimer paired helical filaments. Acta Neuropathol., (Berl.) 88, 1-6.
    • (1994) Acta Neuropathol., (Berl.) , vol.88 , pp. 1-6
    • Pollanen, M.S.1    Bergeron, C.2    Weyer, L.3
  • 311
    • 0033610836 scopus 로고    scopus 로고
    • cDNA cloning, expression, and assembly characteristics of mouse keratin 16
    • Porter, R. M., Hutcheson, A. M., Rugg, E. L., Quinlan, R. A., and Lane, E. B. (1998a). cDNA cloning, expression, and assembly characteristics of mouse keratin 16. J. Biol. Chem. 273, 32265-32272.
    • (1998) J. Biol. Chem. , vol.273 , pp. 32265-32272
    • Porter, R.M.1    Hutcheson, A.M.2    Rugg, E.L.3    Quinlan, R.A.4    Lane, E.B.5
  • 312
    • 0029670060 scopus 로고    scopus 로고
    • Gene targeting at the mouse cytokeratin 10 locus: Severe skin fragility and changes of cytokeratin expression in the epidermis
    • Porter, R. M., Leitgeb, S., Melton, D. W., Swensson, O., Eady, R. A., and Magin, T. M. (1996). Gene targeting at the mouse cytokeratin 10 locus: severe skin fragility and changes of cytokeratin expression in the epidermis. J. Cell Biol. 132, 925-936.
    • (1996) J. Cell Biol. , vol.132 , pp. 925-936
    • Porter, R.M.1    Leitgeb, S.2    Melton, D.W.3    Swensson, O.4    Eady, R.A.5    Magin, T.M.6
  • 313
    • 0031808587 scopus 로고    scopus 로고
    • The relationship between hyperproliferation and epidermal thickening in a mouse model for BCIE
    • Porter, R. M., Reichelt, J., Lunny, D. P., Magin, T. M., and Lane, E. B. (1998b). The relationship between hyperproliferation and epidermal thickening in a mouse model for BCIE. J. Invest. Dermatol. 110, 951-957.
    • (1998) J. Invest. Dermatol. , vol.110 , pp. 951-957
    • Porter, R.M.1    Reichelt, J.2    Lunny, D.P.3    Magin, T.M.4    Lane, E.B.5
  • 315
    • 0023084052 scopus 로고
    • Epidermal cell proliferation. I. Changes with time in the proportion of isolated, paired and clustered labelled cells in sheets of murine epidermis
    • Potten, C. S., and Loeffler, M. (1987). Epidermal cell proliferation. I. Changes with time in the proportion of isolated, paired and clustered labelled cells in sheets of murine epidermis. Virchows Arch. B Cell Pathol. Incl. Mol. Pathol. 53, 279-285.
    • (1987) Virchows Arch. B Cell Pathol. Incl. Mol. Pathol. , vol.53 , pp. 279-285
    • Potten, C.S.1    Loeffler, M.2
  • 316
    • 0032487522 scopus 로고    scopus 로고
    • Rapid movements of vimentin on microtubule tracks: Kinesin-dependent assembly of intermediate filament networks
    • Prahlad, V., Yoon, M., Moir, R. D., Vale, R. D., and Goldman, R. D. (1998). Rapid movements of vimentin on microtubule tracks: kinesin-dependent assembly of intermediate filament networks. J. Cell Biol. 143, 159-170.
    • (1998) J. Cell Biol. , vol.143 , pp. 159-170
    • Prahlad, V.1    Yoon, M.2    Moir, R.D.3    Vale, R.D.4    Goldman, R.D.5
  • 317
    • 0023227133 scopus 로고
    • Skelemins: Cytoskeletal proteins located at the periphery of M-discs in mammalian striated muscle
    • Price, M. G. (1987). Skelemins: cytoskeletal proteins located at the periphery of M-discs in mammalian striated muscle. J. Cell Biol. 104, 1325-1336.
    • (1987) J. Cell Biol. , vol.104 , pp. 1325-1336
    • Price, M.G.1
  • 318
    • 0022000778 scopus 로고
    • Identification and isolation of a 140 kd cell surface glycoprotein with properties expected of a fibronectin receptor
    • Pytela, R., Pierschbacher, M. D., and Ruoslahti, E. (1985). Identification and isolation of a 140 kd cell surface glycoprotein with properties expected of a fibronectin receptor. Cell 40, 191-198.
    • (1985) Cell , vol.40 , pp. 191-198
    • Pytela, R.1    Pierschbacher, M.D.2    Ruoslahti, E.3
  • 319
    • 0019051839 scopus 로고
    • High molecular weight polypeptides (270,000-340,000) from cultured cells are related to hog brain microtubule-associated proteins but copurify with intermediate filaments
    • Pytela, R., and Wiche, G. (1980). High molecular weight polypeptides (270,000-340,000) from cultured cells are related to hog brain microtubule-associated proteins but copurify with intermediate filaments. Proc. Natl. Acad. Sci. USA 77, 4808-4812.
    • (1980) Proc. Natl. Acad. Sci. USA , vol.77 , pp. 4808-4812
    • Pytela, R.1    Wiche, G.2
  • 320
    • 0035159695 scopus 로고    scopus 로고
    • Cytoskeletal catastrophe causes brain degeneration
    • Quinlan, R. A. (2001). Cytoskeletal catastrophe causes brain degeneration. Nat. Genet. 27, 10-11.
    • (2001) Nat. Genet. , vol.27 , pp. 10-11
    • Quinlan, R.A.1
  • 321
    • 0033016166 scopus 로고    scopus 로고
    • Fatal attraction: When chaperone turns harlot
    • Quinlan, R. A., and van den Ijsell, P. (1999). Fatal attraction: When chaperone turns harlot. Nat. Med. 5, 25-26.
    • (1999) Nat. Med. , vol.5 , pp. 25-26
    • Quinlan, R.A.1    Van den Ijsell, P.2
  • 322
    • 0022972141 scopus 로고
    • Characterization of dimer subunits of intermediate filament proteins
    • Quinlan, R. A., Hatzfeld, M., and Franke, W. W. (1986). Characterization of dimer subunits of intermediate filament proteins. J. Mol. Biol. 192, 337-349.
    • (1986) J. Mol. Biol. , vol.192 , pp. 337-349
    • Quinlan, R.A.1    Hatzfeld, M.2    Franke, W.W.3
  • 323
    • 0000374963 scopus 로고
    • Protein profile
    • P. Sheterline, ed. Academic Press
    • Quinlan, R., Hutchison, C., and Lane, B. (1995). Protein profile. In "Intermediate Filament Proteins," P. Sheterline, ed. Vol. 2(8), pp. 801-832. Academic Press.
    • (1995) Intermediate Filament Proteins , vol.2 , Issue.8 , pp. 801-832
    • Quinlan, R.1    Hutchison, C.2    Lane, B.3
  • 324
    • 0035163065 scopus 로고    scopus 로고
    • Formation of a normal epidermis supported by increased stability of keratins 5 and 14 in keratin 10 null mice
    • Reichelt, J., Büssow, H., Grund, C., and Magin, T. M. (2001). Formation of a normal epidermis supported by increased stability of keratins 5 and 14 in keratin 10 null mice. Mol. Biol. Cell 12, 1557-1568.
    • (2001) Mol. Biol. Cell , vol.12 , pp. 1557-1568
    • Reichelt, J.1    Büssow, H.2    Grund, C.3    Magin, T.M.4
  • 325
    • 0036629336 scopus 로고    scopus 로고
    • Hyperproliferation, induction of c-Myc and 14-3-3sigma, but no cell fragility in keratin-10-null mice
    • Reichelt, J., and Magin, T. M. (2002). Hyperproliferation, induction of c-Myc and 14-3-3sigma, but no cell fragility in keratin-10-null mice. J. Cell Sci. 115, 2639-2350.
    • (2002) J. Cell Sci. , vol.115 , pp. 2639-2350
    • Reichelt, J.1    Magin, T.M.2
  • 326
    • 0033909368 scopus 로고    scopus 로고
    • In Vivo observation of a nuclear channel-like system: Evidence for a distinct interchromosomal domain compartment in interphase cells
    • Reichenzeller, M., Burzlaff, A., Lichter, P., and Herrmann, H. (2000). In Vivo observation of a nuclear channel-like system: Evidence for a distinct interchromosomal domain compartment in interphase cells. J. Struct. Biol. 129, 175-185.
    • (2000) J. Struct. Biol. , vol.129 , pp. 175-185
    • Reichenzeller, M.1    Burzlaff, A.2    Lichter, P.3    Herrmann, H.4
  • 327
    • 0344462724 scopus 로고    scopus 로고
    • Association of mitochondria with plectin and desmin intermediate filaments in striated muscle
    • Reipert, S., Steinbock, F., Fischer, I., Bittner, R. E., Zeold, A., and Wiche, G. (1999). Association of mitochondria with plectin and desmin intermediate filaments in striated muscle. Exp. Cell Res. 252, 479-491.
    • (1999) Exp. Cell Res. , vol.252 , pp. 479-491
    • Reipert, S.1    Steinbock, F.2    Fischer, I.3    Bittner, R.E.4    Zeold, A.5    Wiche, G.6
  • 328
    • 0019888143 scopus 로고
    • Reconstitution of intermediate-sized filaments from denatured monomeric vimentin
    • Renner, W., Franke, W. W., Schmid, E., Geisler, N., Weber, K., and Mandelkow, E. (1981). Reconstitution of intermediate-sized filaments from denatured monomeric vimentin. J. Mol. Biol. 149, 285-306.
    • (1981) J. Mol. Biol. , vol.149 , pp. 285-306
    • Renner, W.1    Franke, W.W.2    Schmid, E.3    Geisler, N.4    Weber, K.5    Mandelkow, E.6
  • 330
    • 0031761461 scopus 로고    scopus 로고
    • Common and varaint properties of intermediate filament proteins from lower chordates and vertebrates; Two proteins from the tunicate Styela and the identification of a type III homologue
    • Riemer, D., and Weber, K. (1998). Common and varaint properties of intermediate filament proteins from lower chordates and vertebrates; two proteins from the tunicate Styela and the identification of a type III homologue. J. Cell Sci. 111, 2967-2975.
    • (1998) J. Cell Sci. , vol.111 , pp. 2967-2975
    • Riemer, D.1    Weber, K.2
  • 331
    • 0023449347 scopus 로고
    • Functional analysis and growth factor regulation of the human vimentin
    • Rittling, S. R., and Baserga, R. (1987). Functional analysis and growth factor regulation of the human vimentin promoter. Mol. Cell. Biol. 7, 3908-3915.
    • (1987) Mol. Cell. Biol. , vol.7 , pp. 3908-3915
    • Rittling, S.R.1    Baserga, R.2
  • 332
    • 0028984981 scopus 로고
    • Truncation mutagenesis of the non-α-helical carboxyterminal tail domain of vimentin reveals contributions to cellular localization but not to filament assembly
    • Rogers, K., Eckelt, A., Nimmrich, V., Janssen, K.-P., Schliwa, M., Herrmann, H., and Franke, W. W. (1995). Truncation mutagenesis of the non-α-helical carboxyterminal tail domain of vimentin reveals contributions to cellular localization but not to filament assembly. Eur. J. Cell Biol. 66, 136-150.
    • (1995) Eur. J. Cell Biol. , vol.66 , pp. 136-150
    • Rogers, K.1    Eckelt, A.2    Nimmrich, V.3    Janssen, K.-P.4    Schliwa, M.5    Herrmann, H.6    Franke, W.W.7
  • 333
    • 0030198631 scopus 로고    scopus 로고
    • Characterization of disulfide crosslink formation of human vimentin at the dimer, tetramer, and intermediate filament levels
    • Rogers, K. R., Herrmann, H., and Franke, W. W. (1996). Characterization of disulfide crosslink formation of human vimentin at the dimer, tetramer, and intermediate filament levels. J. Struct. Biol. 117, 55-69.
    • (1996) J. Struct. Biol. , vol.117 , pp. 55-69
    • Rogers, K.R.1    Herrmann, H.2    Franke, W.W.3
  • 334
    • 0000406655 scopus 로고    scopus 로고
    • Characterization of a 300 kbp region of human DNA containing the type II hair keratin gene domain
    • Rogers, M. A., Winter, H., Langbein, L., Wolf, C., and Schweizer, J. (2000). Characterization of a 300 kbp region of human DNA containing the type II hair keratin gene domain. J. Invest. Dermatol. 114, 464-472.
    • (2000) J. Invest. Dermatol. , vol.114 , pp. 464-472
    • Rogers, M.A.1    Winter, H.2    Langbein, L.3    Wolf, C.4    Schweizer, J.5
  • 336
    • 0023867610 scopus 로고
    • A group of type I keratin genes on human chromosome 17: Characterization and expression
    • Rosenberg, M., RayChaudhury, A., Shows, T. B., Le, B. M., and Fuchs, E. (1988). A group of type I keratin genes on human chromosome 17: Characterization and expression. Mol. Cell. Biol. 8, 722-736.
    • (1988) Mol. Cell. Biol. , vol.8 , pp. 722-736
    • Rosenberg, M.1    RayChaudhury, A.2    Shows, T.B.3    Le, B.M.4    Fuchs, E.5
  • 337
    • 0035406530 scopus 로고    scopus 로고
    • Placental development: Lessons from mouse mutants
    • Rossant, J., and Cross, J. C. (2001). Placental development: Lessons from mouse mutants. Nat. Rev. Genet. 2, 538-548.
    • (2001) Nat. Rev. Genet. , vol.2 , pp. 538-548
    • Rossant, J.1    Cross, J.C.2
  • 339
    • 0032735482 scopus 로고    scopus 로고
    • The mouse keratin 6 isoforms are differentially expressed in the hair follicle, footpad, tongue and activated epidermis
    • Rothnagel, J. A., Seki, T., Ogo, M., Longley, M. A., Wojcik, S. M., Bundman, D. S., Bickenbach, J. R., and Roop, D. R. (1999). The mouse keratin 6 isoforms are differentially expressed in the hair follicle, footpad, tongue and activated epidermis. Differentiation 65, 119-130.
    • (1999) Differentiation , vol.65 , pp. 119-130
    • Rothnagel, J.A.1    Seki, T.2    Ogo, M.3    Longley, M.A.4    Wojcik, S.M.5    Bundman, D.S.6    Bickenbach, J.R.7    Roop, D.R.8
  • 340
    • 0019888471 scopus 로고
    • Purified glial fibrillary acidic protein and desmin are distinct intermediate filament proteins exhibiting similar properties
    • Rueger, D. C., Gardner, E. E., der Simonian, H., Dahl, D., and Bignami, A. (1981). Purified glial fibrillary acidic protein and desmin are distinct intermediate filament proteins exhibiting similar properties. J. Biol. Chem. 256, 10606-10612.
    • (1981) J. Biol. Chem. , vol.256 , pp. 10606-10612
    • Rueger, D.C.1    Gardner, E.E.2    Der Simonian, H.3    Dahl, D.4    Bignami, A.5
  • 342
    • 0030795164 scopus 로고    scopus 로고
    • The plakin family: Versatile organizers of cytoskeletal architecture
    • Ruhrberg, C., and Watt, E M. (1997). The plakin family: Versatile organizers of cytoskeletal architecture. Curr. Opiin. Genet. Dev. 7, 392-397.
    • (1997) Curr. Opiin. Genet. Dev. , vol.7 , pp. 392-397
    • Ruhrberg, C.1    Watt, E.M.2
  • 344
    • 0033524377 scopus 로고    scopus 로고
    • Identification of a novel cytokeratin 19 pseudogene that may interfere with reverse transcriptase-polymerase chain reaction assays used to detect micrometastatic tumor cells
    • Ruud, P., Fodstad, O., and Hovig, E. (1999). Identification of a novel cytokeratin 19 pseudogene that may interfere with reverse transcriptase-polymerase chain reaction assays used to detect micrometastatic tumor cells. Int. J. Cancer 80, 119-125.
    • (1999) Int. J. Cancer , vol.80 , pp. 119-125
    • Ruud, P.1    Fodstad, O.2    Hovig, E.3
  • 345
    • 0034722377 scopus 로고    scopus 로고
    • Local control of neurofilament accumulation during radial growth of myelinating axons in vivo. Selective role of site-specific phosphorylation
    • Sanchez, I., Hassinger, L., Sihag, R. K., Cleveland, D. W., Mohan, P., and Nixon, R. A. (2000). Local control of neurofilament accumulation during radial growth of myelinating axons in vivo. Selective role of site-specific phosphorylation. J. Cell Biol. 151, 1013-1024.
    • (2000) J. Cell Biol. , vol.151 , pp. 1013-1024
    • Sanchez, I.1    Hassinger, L.2    Sihag, R.K.3    Cleveland, D.W.4    Mohan, P.5    Nixon, R.A.6
  • 346
    • 0025125457 scopus 로고
    • Three parallel linkage groups of human acidic keratin genes
    • Savtchenko, E. S., Tomic, M., Ivker, R., and Blumenberg, M. (1990). Three parallel linkage groups of human acidic keratin genes. Genomics 7, 394-407.
    • (1990) Genomics , vol.7 , pp. 394-407
    • Savtchenko, E.S.1    Tomic, M.2    Ivker, R.3    Blumenberg, M.4
  • 347
    • 0035696945 scopus 로고    scopus 로고
    • Vimentin and desmin of a cartilaginous fish, the shark Scyliorhinus stellaris: Sequence, expression patterns and in vitro assembly
    • Schaffeld, M., Herrmann, H., Schultess, J., and Markl, J. (2001). Vimentin and desmin of a cartilaginous fish, the shark Scyliorhinus stellaris: Sequence, expression patterns and in vitro assembly. Eur. J. Cell Biol. 80, 692-702.
    • (2001) Eur. J. Cell Biol. , vol.80 , pp. 692-702
    • Schaffeld, M.1    Herrmann, H.2    Schultess, J.3    Markl, J.4
  • 349
    • 0025833558 scopus 로고
    • Epitope map of neurofilament protein domains in cortical and peripheral nervous system Lewy bodies
    • Schmidt, M. L., Murray, J., Lee, V. M., Hill, W. D., Wertkin, A., and Trojanowski, J. Q. (1991). Epitope map of neurofilament protein domains in cortical and peripheral nervous system Lewy bodies. Am. J. Pathol. 139, 53-65.
    • (1991) Am. J. Pathol. , vol.139 , pp. 53-65
    • Schmidt, M.L.1    Murray, J.2    Lee, V.M.3    Hill, W.D.4    Wertkin, A.5    Trojanowski, J.Q.6
  • 355
    • 0024368974 scopus 로고
    • Immunochemical identification of desmin in Torpedo postsynaptic membranes and at the rat neuromuscular junction
    • Sealock, R., Mumane, A. A., Paulin, D., and Froehner, S. C. (1989). Immunochemical identification of desmin in Torpedo postsynaptic membranes and at the rat neuromuscular junction. Synapse 3, 315-324.
    • (1989) Synapse , vol.3 , pp. 315-324
    • Sealock, R.1    Mumane, A.A.2    Paulin, D.3    Froehner, S.C.4
  • 356
    • 0027764507 scopus 로고
    • Transient expression of the intermediate filament nestin during skeletal muscle development
    • Sejersen, T., and Lendahl, U. (1993). Transient expression of the intermediate filament nestin during skeletal muscle development. J. Cell Sci. 106(Pt. 4), 1291-1300.
    • (1993) J. Cell Sci. , vol.106 , Issue.PART 4 , pp. 1291-1300
    • Sejersen, T.1    Lendahl, U.2
  • 358
    • 0019968002 scopus 로고
    • Differential expression of neurofilament triplet proteins in brain development
    • Shaw, G., and Weber, K. (1982). Differential expression of neurofilament triplet proteins in brain development. Nature 298, 277-279.
    • (1982) Nature , vol.298 , pp. 277-279
    • Shaw, G.1    Weber, K.2
  • 359
    • 0027383641 scopus 로고
    • A molecular snapshot of the metazoan "Eve"
    • Shenk, M. A., and Steele, R. E. (1993). A molecular snapshot of the metazoan "Eve." Trends Biochem. Sci. 18, 459-463.
    • (1993) Trends Biochem. Sci. , vol.18 , pp. 459-463
    • Shenk, M.A.1    Steele, R.E.2
  • 360
    • 0032100705 scopus 로고    scopus 로고
    • Defining the interactions between intermediate filaments and desmosomes
    • Smith, E. A., and Fuchs, E. (1998). Defining the interactions between intermediate filaments and desmosomes. J. Cell Biol. 141, 1229-1241.
    • (1998) J. Cell Biol. , vol.141 , pp. 1229-1241
    • Smith, E.A.1    Fuchs, E.2
  • 361
    • 0031802077 scopus 로고    scopus 로고
    • A mutation in human keratin K6b produces a phenocopy of the K17 disorder pachyonychia congenita type 2
    • Smith, F. J., Jonkman, M. F., van Goor, H., Coleman, C. M., Covello, S. P., Uitto, J., and McLean, W. H. (1998). A mutation in human keratin K6b produces a phenocopy of the K17 disorder pachyonychia congenita type 2. Hum. Mol. Genet. 7, 1143-1148.
    • (1998) Hum. Mol. Genet. , vol.7 , pp. 1143-1148
    • Smith, F.J.1    Jonkman, M.F.2    Van Goor, H.3    Coleman, C.M.4    Covello, S.P.5    Uitto, J.6    McLean, W.H.7
  • 363
    • 0344286480 scopus 로고    scopus 로고
    • A mutation detection strategy for the human keratin 6A gene and novel missense mutations in two cases of pachyonychia congenita type 1
    • Smith, F. J., McKenna, K. E., Irvine, A. D., Bingham, E. A., Coleman, C. M., Uitto, J., and McLean, W. H. (1999b). A mutation detection strategy for the human keratin 6A gene and novel missense mutations in two cases of pachyonychia congenita type 1. Exp. Dermatol. 8, 109-114.
    • (1999) Exp. Dermatol. , vol.8 , pp. 109-114
    • Smith, F.J.1    McKenna, K.E.2    Irvine, A.D.3    Bingham, E.A.4    Coleman, C.M.5    Uitto, J.6    McLean, W.H.7
  • 364
    • 0032848822 scopus 로고    scopus 로고
    • Cloning of multiple keratin 16 genes facilitates prenatal diagnosis of pachyonychia congenita type 1
    • Smith, F. J., McKusick, V. A., Nielsen, K., Pfendner, E., Uitto, J., and McLean, W. H. (1999c). Cloning of multiple keratin 16 genes facilitates prenatal diagnosis of pachyonychia congenita type 1. Prenat. Diagn. 19, 941-946.
    • (1999) Prenat. Diagn. , vol.19 , pp. 941-946
    • Smith, F.J.1    McKusick, V.A.2    Nielsen, K.3    Pfendner, E.4    Uitto, J.5    McLean, W.H.6
  • 365
    • 0022342580 scopus 로고
    • Identification of a distinct soluble subunit of an intermediate filament protein: Tetrameric vimentin from living cells
    • Soellner, P., Quinlan, R. A., and Franke, W. W. (1985). Identification of a distinct soluble subunit of an intermediate filament protein: Tetrameric vimentin from living cells. Proc. Natl. Acad. Sci. USA 82, 7929-7933.
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 7929-7933
    • Soellner, P.1    Quinlan, R.A.2    Franke, W.W.3
  • 367
    • 0026511055 scopus 로고
    • The desmoplakin carboxyl terminus coaligns with and specifically disrupts intermediate filament networks when expressed in cultured cells
    • Stappenbeck, T. S., and Green, K. J. (1992). The desmoplakin carboxyl terminus coaligns with and specifically disrupts intermediate filament networks when expressed in cultured cells. J. Cell Biol. 116, 1197-1209.
    • (1992) J. Cell Biol. , vol.116 , pp. 1197-1209
    • Stappenbeck, T.S.1    Green, K.J.2
  • 368
    • 0017864456 scopus 로고
    • Biochemical and immunological analysis of rapidly purified 10nm filaments from baby hamster kidney (BHK-21) cells
    • Starger, J., Brown, W. E., Goldmann, A. E., and Goldman, R. D. (1978). Biochemical and immunological analysis of rapidly purified 10nm filaments from baby hamster kidney (BHK-21) cells. J. Cell Biol. 78, 93-109.
    • (1978) J. Cell Biol. , vol.78 , pp. 93-109
    • Starger, J.1    Brown, W.E.2    Goldmann, A.E.3    Goldman, R.D.4
  • 369
    • 0033927556 scopus 로고    scopus 로고
    • Identification of the cytolinker plectin as a major early in vivo substrate for caspase 8 during CD95- and tumor necrosis factor receptor-mediated apoptosis
    • Stegh, A. H., Herrmann, H., Lampel, S., Weisenberger, D., Andra, K., Seper, M., Wiche, G., Krammer, P. H., and Peter, M. E. (2000). Identification of the cytolinker plectin as a major early in vivo substrate for caspase 8 during CD95- and tumor necrosis factor receptor-mediated apoptosis. Mol. Cell. Biol. 20, 5665-5679.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 5665-5679
    • Stegh, A.H.1    Herrmann, H.2    Lampel, S.3    Weisenberger, D.4    Andra, K.5    Seper, M.6    Wiche, G.7    Krammer, P.H.8    Peter, M.E.9
  • 370
    • 12244261689 scopus 로고
    • Intermediate filaments
    • J. R. Harris, Ed. Academic Press, New York
    • Steinert, P. M. (1981). Intermediate filaments. In "Electron Microscopy of Proteins" (J. R. Harris, Ed.), Vol. 1, pp. 126-166. Academic Press, New York.
    • (1981) Electron Microscopy of Proteins , vol.1 , pp. 126-166
    • Steinert, P.M.1
  • 371
    • 0029050246 scopus 로고
    • The proteins elafin, filaggrin, keratin intermediate filaments, loricrin, and small proline-rich proteins 1 and 2 are isodipeptide cross-linked components of the human epidermal cornified cell envelope
    • Steinert, P. M., and Marekov, L. N. (1995). The proteins elafin, filaggrin, keratin intermediate filaments, loricrin, and small proline-rich proteins 1 and 2 are isodipeptide cross-linked components of the human epidermal cornified cell envelope. J. Biol. Chem. 270, 17702-17711.
    • (1995) J. Biol. Chem. , vol.270 , pp. 17702-17711
    • Steinert, P.M.1    Marekov, L.N.2
  • 372
    • 0031037715 scopus 로고    scopus 로고
    • Direct evidence that involucrin is a major early isopeptide cross-linked component of the keratinocyte cornified cell envelope
    • Steinert, P. M., and Marekov, L. N. (1997). Direct evidence that involucrin is a major early isopeptide cross-linked component of the keratinocyte cornified cell envelope. J. Biol. Chem. 272, 2021-2030.
    • (1997) J. Biol. Chem. , vol.272 , pp. 2021-2030
    • Steinert, P.M.1    Marekov, L.N.2
  • 373
    • 0027476386 scopus 로고
    • The conserved HI domain of the type II keratin I chain plays an essential role in the alignment of nearest neighbor molecules in mouse and human keratin 1/keratin 10 intermediate filaments at the two-to-four-molecule level of structure
    • Steinert, P. M., and Parry, D. A. (1993). The conserved HI domain of the type II keratin I chain plays an essential role in the alignment of nearest neighbor molecules in mouse and human keratin 1/keratin 10 intermediate filaments at the two-to-four-molecule level of structure. J. Biol. Chem. 268, 2878-2887.
    • (1993) J. Biol. Chem. , vol.268 , pp. 2878-2887
    • Steinert, P.M.1    Parry, D.A.2
  • 374
    • 0017054951 scopus 로고
    • Self-assembly of bovine epidermal keratin filaments in vitro
    • Steinert, P. M., Idler, W. W., and Zimmerman, S. B. (1976). Self-assembly of bovine epidermal keratin filaments in vitro. J. Mol. Biol. 108, 547-567.
    • (1976) J. Mol. Biol. , vol.108 , pp. 547-567
    • Steinert, P.M.1    Idler, W.W.2    Zimmerman, S.B.3
  • 375
    • 0010556492 scopus 로고
    • Structure of fibroblastic intermediate filaments: Analysis by scanning transmission electron microscopy
    • Steven, A. C., Wall, J., Hainfeld, J., and Steinert, P. M. (1982). Structure of fibroblastic intermediate filaments: Analysis by scanning transmission electron microscopy. Proc. Natl. Acad. Sci. USA 79, 3101-3105.
    • (1982) Proc. Natl. Acad. Sci. USA , vol.79 , pp. 3101-3105
    • Steven, A.C.1    Wall, J.2    Hainfeld, J.3    Steinert, P.M.4
  • 376
    • 0035313072 scopus 로고    scopus 로고
    • Neurofilaments are nonessential to the pathogenesis of toxicant-induced axonal degeneration
    • Stone, J. D., Peterson, A. P., Eyer, J., Oblak, T. G., and Sickles, D. W. (2001). Neurofilaments are nonessential to the pathogenesis of toxicant-induced axonal degeneration. J. Neurosci. 21, 2278-2287.
    • (2001) J. Neurosci. , vol.21 , pp. 2278-2287
    • Stone, J.D.1    Peterson, A.P.2    Eyer, J.3    Oblak, T.G.4    Sickles, D.W.5
  • 378
    • 0037086445 scopus 로고    scopus 로고
    • Evolutionarily conserved a-helical segments 1A and 2B of the intermediate filament dimer: Their atomic structures and role in filament assembly
    • Strelkov, S. V., Herrmann, H., Geisler, N., Wedig, T., Zimbelmann, R., Aebi, U., and Burkhard, P. (2002). Evolutionarily conserved a-helical segments 1A and 2B of the intermediate filament dimer: Their atomic structures and role in filament assembly. EMBO J. 21, 1255-1266.
    • (2002) EMBO J. , vol.21 , pp. 1255-1266
    • Strelkov, S.V.1    Herrmann, H.2    Geisler, N.3    Wedig, T.4    Zimbelmann, R.5    Aebi, U.6    Burkhard, P.7
  • 379
    • 0034998784 scopus 로고    scopus 로고
    • Sequence of events in the assembly of Mallory body components in mouse liver: Clues to the pathogenesis and significance of Mallory body formation
    • Stumptner, C., Fuchsbichler, A., Lehner, M., Zatloukal, K., and Denk, H. (2001). Sequence of events in the assembly of Mallory body components in mouse liver: Clues to the pathogenesis and significance of Mallory body formation. J. Hepatol. 34, 665-675.
    • (2001) J. Hepatol. , vol.34 , pp. 665-675
    • Stumptner, C.1    Fuchsbichler, A.2    Lehner, M.3    Zatloukal, K.4    Denk, H.5
  • 380
    • 0031686054 scopus 로고    scopus 로고
    • Nuclear lamins: Their structure, assembly, and interactions
    • Stuurman, N., Heins, S., and Aebi, U. (1998). Nuclear lamins: Their structure, assembly, and interactions. J. Struct. Biol. 122, 42-66.
    • (1998) J. Struct. Biol. , vol.122 , pp. 42-66
    • Stuurman, N.1    Heins, S.2    Aebi, U.3
  • 382
    • 0032574706 scopus 로고    scopus 로고
    • A cytoplasmic protein, bystin, interacts with trophinin, tastin, and cytokeratin and may be involved in trophinin-mediated cell adhesion between trophoblast and endometrial epithelial cells
    • Suzuki, N., Zara, J., Sato, T., Ong, E., Bakhiet, N., Oshima, R. G., Watson, K. L., and Fukuda, M. N. (1998). A cytoplasmic protein, bystin, interacts with trophinin, tastin, and cytokeratin and may be involved in trophinin-mediated cell adhesion between trophoblast and endometrial epithelial cells. Proc. Natl. Acad. Sci. USA 95, 5027-5032.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 5027-5032
    • Suzuki, N.1    Zara, J.2    Sato, T.3    Ong, E.4    Bakhiet, N.5    Oshima, R.G.6    Watson, K.L.7    Fukuda, M.N.8
  • 383
    • 0029805514 scopus 로고    scopus 로고
    • Plectin sidearms mediate interaction of intermediate filaments with microtubules and other components of the cytoskeleton
    • Svitkina, T. M., Verkhovsky, A. B., and Borisy, G. G. (1996). Plectin sidearms mediate interaction of intermediate filaments with microtubules and other components of the cytoskeleton. J. Cell Biol. 135, 991-1007.
    • (1996) J. Cell Biol. , vol.135 , pp. 991-1007
    • Svitkina, T.M.1    Verkhovsky, A.B.2    Borisy, G.G.3
  • 384
    • 0028109866 scopus 로고
    • Increased expression of keratin 16 causes anomalies in cytoarchitecture and keratinization in transgenic mouse skin
    • Takahashi, K., Folmer, J., and Coulombe, P. A. (1994). Increased expression of keratin 16 causes anomalies in cytoarchitecture and keratinization in transgenic mouse skin. J. Cell Biol. 127, 505-520.
    • (1994) J. Cell Biol. , vol.127 , pp. 505-520
    • Takahashi, K.1    Folmer, J.2    Coulombe, P.A.3
  • 385
    • 0029127184 scopus 로고
    • Cloning and characterization of multiple human genes and cDNAs encoding highly related type II keratin 6 isoforms
    • Takahashi, K., Paladini, R. D., and Coulombe, P. A. (1995). Cloning and characterization of multiple human genes and cDNAs encoding highly related type II keratin 6 isoforms. J. Biol. Chem. 270, 18581-18592.
    • (1995) J. Biol. Chem. , vol.270 , pp. 18581-18592
    • Takahashi, K.1    Paladini, R.D.2    Coulombe, P.A.3
  • 386
    • 0032532129 scopus 로고    scopus 로고
    • The two functional keratin 6 genes of mouse are differentially regulated and evolved independently from their human orthologs
    • Takahashi, K., Yan, B., Yamanishi, K., Imamura, S., and Coulombe, P. A. (1998). The two functional keratin 6 genes of mouse are differentially regulated and evolved independently from their human orthologs. Genomics 53, 170-183.
    • (1998) Genomics , vol.53 , pp. 170-183
    • Takahashi, K.1    Yan, B.2    Yamanishi, K.3    Imamura, S.4    Coulombe, P.A.5
  • 388
    • 0034682742 scopus 로고    scopus 로고
    • Involvement of follicular stem cells in forming not only the follicle but also the epidermis
    • Taylor, G., Lehrer, M. S., Jensen, P. J., Sun, T. T., and Lavker, R. M. (2000). Involvement of follicular stem cells in forming not only the follicle but also the epidermis. Cell 102, 451-461.
    • (2000) Cell , vol.102 , pp. 451-461
    • Taylor, G.1    Lehrer, M.S.2    Jensen, P.J.3    Sun, T.T.4    Lavker, R.M.5
  • 392
    • 0026654245 scopus 로고
    • Desmin at myotendinous junctions
    • Tidball, J. G. (1992). Desmin at myotendinous junctions. Exp. Cell Res. 199, 206-212.
    • (1992) Exp. Cell Res. , vol.199 , pp. 206-212
    • Tidball, J.G.1
  • 393
    • 0035660405 scopus 로고    scopus 로고
    • Human synemin gene generates splice variants encoding two distinct intermediate filament proteins
    • Titeux, M., Brocheriou, V., Xue, Z., Gao, J., Guicheney, P., Paulin, D., and Li, Z. (2001). Human synemin gene generates splice variants encoding two distinct intermediate filament proteins. Eur. J. Biochem. 268, 6435-6449.
    • (2001) Eur. J. Biochem. , vol.268 , pp. 6435-6449
    • Titeux, M.1    Brocheriou, V.2    Xue, Z.3    Gao, J.4    Guicheney, P.5    Paulin, D.6    Li, Z.7
  • 394
    • 0031836071 scopus 로고    scopus 로고
    • Protein phosphatase inhibition in normal and keratin 8/18 assembly-incompetent mouse strains supports a functional role of keratin intermediate filaments in preserving hepatocyte integrity
    • Toivola, D. M., Omary, M. B., Ku, N. O., Peltola, O., Baribault, H., and Eriksson, J. E. (1998). Protein phosphatase inhibition in normal and keratin 8/18 assembly-incompetent mouse strains supports a functional role of keratin intermediate filaments in preserving hepatocyte integrity. Hepatology 28, 116-128.
    • (1998) Hepatology , vol.28 , pp. 116-128
    • Toivola, D.M.1    Omary, M.B.2    Ku, N.O.3    Peltola, O.4    Baribault, H.5    Eriksson, J.E.6
  • 396
    • 0034654035 scopus 로고    scopus 로고
    • Effects of keratin filament disruption on exocrine pancreas-stimulated secretion and susceptibility to injury
    • Toivola, D. M., Ku, N. O., Ghori, N., Lowe, A. W., Michie, S. A., and Omary, M. B. (2000b). Effects of keratin filament disruption on exocrine pancreas-stimulated secretion and susceptibility to injury. Exp. Cell Res. 255, 156-170.
    • (2000) Exp. Cell Res. , vol.255 , pp. 156-170
    • Toivola, D.M.1    Ku, N.O.2    Ghori, N.3    Lowe, A.W.4    Michie, S.A.5    Omary, M.B.6
  • 398
    • 0020803501 scopus 로고
    • Visualization of longitudinally-oriented intermediate filaments in frozen sections of chicken cardiac muscle by a new staining method
    • Tokuyasu, K. T. (1983). Visualization of longitudinally-oriented intermediate filaments in frozen sections of chicken cardiac muscle by a new staining method. J. Cell Biol. 97, 562-565.
    • (1983) J. Cell Biol. , vol.97 , pp. 562-565
    • Tokuyasu, K.T.1
  • 399
    • 0020960791 scopus 로고
    • Immunoelectron microscopic studies of desmin (skeletin) localization and intermediate filament organization in chicken cardiac muscle
    • Tokuyasu, K. T., Dutton, A. H., and Singer, S. J. (1983). Immunoelectron microscopic studies of desmin (skeletin) localization and intermediate filament organization in chicken cardiac muscle. J. Cell Biol. 96, 1736-1742.
    • (1983) J. Cell Biol. , vol.96 , pp. 1736-1742
    • Tokuyasu, K.T.1    Dutton, A.H.2    Singer, S.J.3
  • 400
    • 0021264715 scopus 로고
    • Distributions of vimentin and desmin in developing chick myotubes in vivo. I. Immunofluorescence study
    • Tokuyasu, K. T., Maher, P. A., and Singer, S. J. (1984). Distributions of vimentin and desmin in developing chick myotubes in vivo. I. Immunofluorescence study. J. Cell Biol. 98, 1961-1972.
    • (1984) J. Cell Biol. , vol.98 , pp. 1961-1972
    • Tokuyasu, K.T.1    Maher, P.A.2    Singer, S.J.3
  • 401
    • 85012367314 scopus 로고
    • Distributions of vimentin and desmin in developing chick myotubes in vivo. II. Immunoelectron microscopic study
    • Tokuyasu, K. T., Maher, P. A., and Singer, S. J. (1985). Distributions of vimentin and desmin in developing chick myotubes in vivo. II. Immunoelectron microscopic study. J. Cell Biol. 100, 1157-1166.
    • (1985) J. Cell Biol. , vol.100 , pp. 1157-1166
    • Tokuyasu, K.T.1    Maher, P.A.2    Singer, S.J.3
  • 402
    • 0032427646 scopus 로고    scopus 로고
    • Novel insertion in the KSP region of the neurofilament heavy gene in amyotrophic lateral sclerosis (ALS)
    • Tomkins, J., Usher, P., Slade, J. Y., Ince, P. G., Curtis, A., Bushby, K., and Shaw, P. J. (1998). Novel insertion in the KSP region of the neurofilament heavy gene in amyotrophic lateral sclerosis (ALS). Neuroreport 9, 3967-3970.
    • (1998) Neuroreport , vol.9 , pp. 3967-3970
    • Tomkins, J.1    Usher, P.2    Slade, J.Y.3    Ince, P.G.4    Curtis, A.5    Bushby, K.6    Shaw, P.J.7
  • 404
    • 0003517815 scopus 로고
    • Springer-Verlag, Berlin, Heidelberg, New York, Tokyo
    • Traub, P. (1985). "Intermediate Filaments." Springer-Verlag, Berlin, Heidelberg, New York, Tokyo.
    • (1985) Intermediate Filaments
    • Traub, P.1
  • 405
    • 0032781147 scopus 로고    scopus 로고
    • In vitro characteristics of early epidermal progenitors isolated from keratin 14 (K14)-deficient mice: Insights into the role of keratin 17 in mouse keratinocytes
    • Troy, T. C., and Turksen, K. (1999). In vitro characteristics of early epidermal progenitors isolated from keratin 14 (K14)-deficient mice: insights into the role of keratin 17 in mouse keratinocytes. J. Cell Physiol. 180, 409-421.
    • (1999) J. Cell Physiol. , vol.180 , pp. 409-421
    • Troy, T.C.1    Turksen, K.2
  • 406
    • 0026442553 scopus 로고
    • Characterization of the human gene encoding cytokeratin 17 and its expression pattern
    • Troyanovsky, S. M., Leube, R. E., and Franke, W. W. (1992). Characterization of the human gene encoding cytokeratin 17 and its expression pattern. Eur. J. Cell Biol. 59, 127-137.
    • (1992) Eur. J. Cell Biol. , vol.59 , pp. 127-137
    • Troyanovsky, S.M.1    Leube, R.E.2    Franke, W.W.3
  • 407
    • 0034788964 scopus 로고    scopus 로고
    • 14-3-3 Proteins: Key regulators of cell division, signalling and apoptosis
    • van Hemert, M. J., Steensma, H. Y., and van Heusden, G. P. (2001). 14-3-3 proteins: Key regulators of cell division, signalling and apoptosis. Bioessays 23, 936-946.
    • (2001) Bioessays , vol.23 , pp. 936-946
    • Van Hemert, M.J.1    Steensma, H.Y.2    Van Heusden, G.P.3
  • 408
    • 0036143190 scopus 로고    scopus 로고
    • Imaging into the future: Visualizing gene expression and protein interactions with fluorescent proteins
    • van Roessel, P., and Brand, A. H. (2002). Imaging into the future: Visualizing gene expression and protein interactions with fluorescent proteins. Nat. Cell Biol. 4, E15-E20.
    • (2002) Nat. Cell Biol. , vol.4
    • Van Roessel, P.1    Brand, A.H.2
  • 409
    • 0035193241 scopus 로고    scopus 로고
    • Nuclear envelope and nuclear matrix interactions and dynamics
    • Vlcek, S., Dechat, T., and Foisner, R. (2001). Nuclear envelope and nuclear matrix interactions and dynamics. Cell. Mol. Life Sci. 58, 1758-1765.
    • (2001) Cell. Mol. Life Sci. , vol.58 , pp. 1758-1765
    • Vlcek, S.1    Dechat, T.2    Foisner, R.3
  • 410
    • 0034978920 scopus 로고    scopus 로고
    • Deregulated expression of c-Myc depletes epidermal stem cells
    • Waikel, R. L., Kawachi, Y., Waikel, P. A., Wang, X. J., and Roop, D. R. (2001). Deregulated expression of c-Myc depletes epidermal stem cells. Nat. Genet. 28, 165-168.
    • (2001) Nat. Genet. , vol.28 , pp. 165-168
    • Waikel, R.L.1    Kawachi, Y.2    Waikel, P.A.3    Wang, X.J.4    Roop, D.R.5
  • 411
    • 0025282832 scopus 로고
    • Embryonic simple epithelial keratins 8 and 18: Chromosomal location emphasizes difference from other keratin pairs
    • Waseem, A., Alexander, C. M., Steel, J. B., and Lane, E. B. (1990). Embryonic simple epithelial keratins 8 and 18: Chromosomal location emphasizes difference from other keratin pairs. New Biol. 2, 464-478.
    • (1990) New Biol. , vol.2 , pp. 464-478
    • Waseem, A.1    Alexander, C.M.2    Steel, J.B.3    Lane, E.B.4
  • 412
    • 0034712109 scopus 로고    scopus 로고
    • Out of Eden: Stem cells and their niches
    • Watt, F. M., and Hogan, B. L. (2000). Out of Eden: stem cells and their niches. Science 287, 1427-1430.
    • (2000) Science , vol.287 , pp. 1427-1430
    • Watt, F.M.1    Hogan, B.L.2
  • 413
    • 0033790353 scopus 로고    scopus 로고
    • Forced expression of keratin 16 alters the adhesion, differentiation, and migration of mouse skin keratinocytes
    • Wawersik, M., and Coulombe, P. A. (2000). Forced expression of keratin 16 alters the adhesion, differentiation, and migration of mouse skin keratinocytes. Mol. Biol. Cell 11, 3315-3327.
    • (2000) Mol. Biol. Cell , vol.11 , pp. 3315-3327
    • Wawersik, M.1    Coulombe, P.A.2
  • 414
    • 0035196621 scopus 로고    scopus 로고
    • Increased levels of keratin 16 alter epithelialization potential of mouse skin keratinocytes in vivo and ex vivo
    • Wawersik, M. J., Mazzalupo, S., Nguyen, D., and Coulombe, P. A. (2001). Increased levels of keratin 16 alter epithelialization potential of mouse skin keratinocytes in vivo and ex vivo. Mol. Biol. Cell 12, 3439-3450.
    • (2001) Mol. Biol. Cell , vol.12 , pp. 3439-3450
    • Wawersik, M.J.1    Mazzalupo, S.2    Nguyen, D.3    Coulombe, P.A.4
  • 415
    • 0000568164 scopus 로고    scopus 로고
    • Evolutionary aspects of IF proteins
    • T. Kreis and R. Vale, Eds. Oxford University Press, Oxford
    • Weber, K. (1999). Evolutionary aspects of IF proteins. In "Guidebook to the Cystoskeletal and Motor Proteins" (T. Kreis and R. Vale, Eds.), pp. 291-293. Oxford University Press, Oxford.
    • (1999) Guidebook to the Cystoskeletal and Motor Proteins , pp. 291-293
    • Weber, K.1
  • 416
    • 0002796676 scopus 로고
    • Intermediate filaments from wool a-keratin to neurofilaments: A structural overview
    • A. J. Levine, G. F. Van de Woude, W. C. Topp, and J. D. Watson, Eds. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Weber, K., and Geisler, N. (1984). Intermediate filaments from wool a-keratin to neurofilaments: A structural overview. In "Cancer Cells 1, The Transformed Phenotype" (A. J. Levine, G. F. Van de Woude, W. C. Topp, and J. D. Watson, Eds.), pp. 153-159. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
    • (1984) Cancer Cells 1, The Transformed Phenotype , pp. 153-159
    • Weber, K.1    Geisler, N.2
  • 417
    • 0031663054 scopus 로고    scopus 로고
    • Role of plectin in cytoskeleton organization and dynamics
    • Wiche, G. (1998). Role of plectin in cytoskeleton organization and dynamics. J. Cell Sci. 111, 2477-2486.
    • (1998) J. Cell Sci. , vol.111 , pp. 2477-2486
    • Wiche, G.1
  • 418
    • 0026014584 scopus 로고
    • Cloning and sequencing of rat plectin indicates a 466-kD polypeptide chain with a three-domain structure based on a central alpha-helical coiled coil
    • Wiche, G., Becker, B., Luber, K., Weitzer, G., Castanon, M. J., Hauptmann, R., Stratowa, C., and Stewart, M. (1991). Cloning and sequencing of rat plectin indicates a 466-kD polypeptide chain with a three-domain structure based on a central alpha-helical coiled coil. J. Cell Biol. 114, 83-99.
    • (1991) J. Cell Biol. , vol.114 , pp. 83-99
    • Wiche, G.1    Becker, B.2    Luber, K.3    Weitzer, G.4    Castanon, M.J.5    Hauptmann, R.6    Stratowa, C.7    Stewart, M.8
  • 419
    • 0020329482 scopus 로고
    • Plectin: A high-molecular-weight cytoskeletal polypeptide component that copurifies with intermediate filaments of the vimentin type
    • Wiche, G., Herrmann, H., Leichtfried, F., and Pytela, R. (1982). Plectin: A high-molecular-weight cytoskeletal polypeptide component that copurifies with intermediate filaments of the vimentin type. Cold Spring Harbor Symp. Quant. Biol. 46, 475-482.
    • (1982) Cold Spring Harbor Symp. Quant. Biol. , vol.46 , pp. 475-482
    • Wiche, G.1    Herrmann, H.2    Leichtfried, F.3    Pytela, R.4
  • 420
    • 0020612365 scopus 로고
    • Occurrence and immunolocalization of plectin in tissues
    • Wiche, G., Krepler, R., Artlieb, U., Pytela, R., and Denk, H. (1983). Occurrence and immunolocalization of plectin in tissues. J. Cell Biol. 97, 887-901.
    • (1983) J. Cell Biol. , vol.97 , pp. 887-901
    • Wiche, G.1    Krepler, R.2    Artlieb, U.3    Pytela, R.4    Denk, H.5
  • 421
    • 0032482976 scopus 로고    scopus 로고
    • Absence of neurofilaments reduces the selective vulnerability of motor neurons and slows disease caused by a familial amyotrophic lateral sclerosis-linked superoxide dismutase I mutant
    • Williamson, T. L., Bruijn, L. I., Zhu, Q., Anderson, K. L., Anderson, S. D., Julien, J. P., and Cleveland, D. W. (1998). Absence of neurofilaments reduces the selective vulnerability of motor neurons and slows disease caused by a familial amyotrophic lateral sclerosis-linked superoxide dismutase I mutant. Proc. Natl. Acad. Sci. USA 95, 9631-9636.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 9631-9636
    • Williamson, T.L.1    Bruijn, L.I.2    Zhu, Q.3    Anderson, K.L.4    Anderson, S.D.5    Julien, J.P.6    Cleveland, D.W.7
  • 422
    • 0034176682 scopus 로고    scopus 로고
    • The nuclear envelope, muscular dystrophy and gene expression
    • Wilson, K. L. (2000). The nuclear envelope, muscular dystrophy and gene expression. Trends Cell Biol. 10, 125-129.
    • (2000) Trends Cell Biol. , vol.10 , pp. 125-129
    • Wilson, K.L.1
  • 423
    • 0035831041 scopus 로고    scopus 로고
    • Lamins and disease: Insights into nuclear infrastructure
    • Wilson, K. L., Zastrow, M. S., and Lee, K. K. (2001). Lamins and disease: Insights into nuclear infrastructure. Cell 104, 647-650.
    • (2001) Cell , vol.104 , pp. 647-650
    • Wilson, K.L.1    Zastrow, M.S.2    Lee, K.K.3
  • 424
    • 0033375650 scopus 로고    scopus 로고
    • Detection of cytokeratin dynamics by time-lapse fluorescence microscopy in living cells
    • Windhoffer, R., and Leube, R. L. (1999). Detection of cytokeratin dynamics by time-lapse fluorescence microscopy in living cells. J. Cell Sci. 112, 4521-4534.
    • (1999) J. Cell Sci. , vol.112 , pp. 4521-4534
    • Windhoffer, R.1    Leube, R.L.2
  • 425
    • 0034794313 scopus 로고    scopus 로고
    • De Novo formation of cytokeratin filament networks originates from the cell cortex in A-431 cells
    • Windhoffer, R., and Leube, R. L. (2001). De Novo formation of cytokeratin filament networks originates from the cell cortex in A-431 cells. Cell Motil. Cytoskeleton 50, 33-44.
    • (2001) Cell Motil. Cytoskeleton , vol.50 , pp. 33-44
    • Windhoffer, R.1    Leube, R.L.2
  • 427
    • 0035122674 scopus 로고    scopus 로고
    • Human type I hair keratin pseudogene phihHaA has functional orthologs in the chimpanzee and gorilla: Evidence for recent inactivation of the human gene after the Pan-Homo divergence
    • Winter, H., Langbein, L., Krawczak, M., Cooper, D. N., Jave-Suarez, L. F., Rogers, M. A., Praetzel, S., Heidt, P. J., and Schweizer, J. (2001). Human type I hair keratin pseudogene phihHaA has functional orthologs in the chimpanzee and gorilla: Evidence for recent inactivation of the human gene after the Pan-Homo divergence. Hum. Genet. 108, 37-42.
    • (2001) Hum. Genet. , vol.108 , pp. 37-42
    • Winter, H.1    Langbein, L.2    Krawczak, M.3    Cooper, D.N.4    Jave-Suarez, L.F.5    Rogers, M.A.6    Praetzel, S.7    Heidt, P.J.8    Schweizer, J.9
  • 428
    • 0033934479 scopus 로고    scopus 로고
    • Delayed wound healing in keratin 6a knockout mice
    • Wojcik, S. M., Bundman, D. S., and Roop, D. R. (2000). Delayed wound healing in keratin 6a knockout mice. Mol. Cell. Biol. 20, 5248-5255.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 5248-5255
    • Wojcik, S.M.1    Bundman, D.S.2    Roop, D.R.3
  • 429
    • 0032750099 scopus 로고    scopus 로고
    • Expression of MK6a dominant-negative and C-terminal mutant transgenes in mice has distinct phenotypic consequences in the epidermis and hair follicle
    • Wojcik, S. M., Imakado, S., Seki, T., Longley, M. A., Petherbridge, L., Bundman, D. S., Bickenbach, J. R., Rothnagel, J. A., and Roop, D. R. (1999). Expression of MK6a dominant-negative and C-terminal mutant transgenes in mice has distinct phenotypic consequences in the epidermis and hair follicle. Differentiation 65, 97-112.
    • (1999) Differentiation , vol.65 , pp. 97-112
    • Wojcik, S.M.1    Imakado, S.2    Seki, T.3    Longley, M.A.4    Petherbridge, L.5    Bundman, D.S.6    Bickenbach, J.R.7    Rothnagel, J.A.8    Roop, D.R.9
  • 430
    • 0035817630 scopus 로고    scopus 로고
    • Discovery of a novel murine keratin 6 (K6) isoform explains the absence of hair and nail defects in mice deficient for K6a and K6b
    • Wojcik, S. M., Longley, M. A., and Roop, D. R. (2001). Discovery of a novel murine keratin 6 (K6) isoform explains the absence of hair and nail defects in mice deficient for K6a and K6b. J. Cell Biol. 154, 619-630.
    • (2001) J. Cell Biol. , vol.154 , pp. 619-630
    • Wojcik, S.M.1    Longley, M.A.2    Roop, D.R.3
  • 431
    • 0034698869 scopus 로고    scopus 로고
    • Introducing a null mutation in the mouse k6alpha and k6beta genes reveals their essential structural role in the oral mucosa
    • Wong, P., Colucci-Guyon, E., Takahashi, K., Gu, C., Babinet, C., and Coulombe, P. A. (2000). Introducing a null mutation in the mouse k6alpha and k6beta genes reveals their essential structural role in the oral mucosa. J. Cell Biol. 150, 921-8.
    • (2000) J. Cell Biol. , vol.150 , pp. 921-928
    • Wong, P.1    Colucci-Guyon, E.2    Takahashi, K.3    Gu, C.4    Babinet, C.5    Coulombe, P.A.6
  • 432
    • 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., Marszalek, J., Crawford, T. O., Xu, Z., Hsieh, S. T., Griffin, J. W., and Cleveland, D. W. (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    Crawford, T.O.3    Xu, Z.4    Hsieh, S.T.5    Griffin, J.W.6    Cleveland, D.W.7
  • 434
  • 435
    • 0032694199 scopus 로고    scopus 로고
    • Kinesin-mediated transport of neurofilament protein oligomers in growing axons
    • Yabe, J. T., Pimenta, A., and Shea, T. B. (1999). Kinesin-mediated transport of neurofilament protein oligomers in growing axons. J. Cell Sci. 112, 3799-3814.
    • (1999) J. Cell Sci. , vol.112 , pp. 3799-3814
    • Yabe, J.T.1    Pimenta, A.2    Shea, T.B.3
  • 436
    • 0034030749 scopus 로고    scopus 로고
    • Phospho-dependent association of neurofilament proteins with kinesin in situ
    • Yabe, J. T., Jung Chan, W. K., and Shea, T. B. (2000). Phospho-dependent association of neurofilament proteins with kinesin in situ. Cell. Motil. Cytoskeleton 45, 249-262.
    • (2000) Cell. Motil. Cytoskeleton , vol.45 , pp. 249-262
    • Yabe, J.T.1    Jung Chan, W.K.2    Shea, T.B.3
  • 437
    • 0035972146 scopus 로고    scopus 로고
    • Insights into the dynamic properties of keratin intermediate filaments in living epithelial cells
    • Yoon, K. H., Yoon, M., Moir, R. D., Khuon, S., Flitney, F. W., and Goldman, R. D. (2001). Insights into the dynamic properties of keratin intermediate filaments in living epithelial cells. J. Cell Biol. 153, 503-516.
    • (2001) J. Cell Biol. , vol.153 , pp. 503-516
    • Yoon, K.H.1    Yoon, M.2    Moir, R.D.3    Khuon, S.4    Flitney, F.W.5    Goldman, R.D.6
  • 438
    • 0032487443 scopus 로고    scopus 로고
    • Motile properties of vimentin intermediate filament networks in living cells
    • Yoon, M., Moir, R. D., Prahlad, V., and Goldman, R. D. (1998). Motile properties of vimentin intermediate filament networks in living cells. J. Cell Biol. 143, 147-157.
    • (1998) J. Cell Biol. , vol.143 , pp. 147-157
    • Yoon, M.1    Moir, R.D.2    Prahlad, V.3    Goldman, R.D.4
  • 439
    • 0344048011 scopus 로고
    • In vitro assembly of intermediate filaments from baby hamster kidney (BHK-21) cells
    • Zackroff, R. V., and Goldman, R. D. (1979). In vitro assembly of intermediate filaments from baby hamster kidney (BHK-21) cells. Proc. Natl. Acad. Sci. USA 76, 6226-6230.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 6226-6230
    • Zackroff, R.V.1    Goldman, R.D.2
  • 440
    • 0033843879 scopus 로고    scopus 로고
    • Cytokeratin 8 protects from hepatotoxicity, and its ratio to cytokeratin 18 determines the ability of hepatocytes to form Mallory bodies
    • Zatloukal, K., Stumptner, C., Zatloukal, K., Stumptner, C., Lehner, M., Denk, H., Baribault, H., Eshkind, L. G., and Franke, W. W. (2000). Cytokeratin 8 protects from hepatotoxicity, and its ratio to cytokeratin 18 determines the ability of hepatocytes to form Mallory bodies. Am. J. Pathol. 156, 1263-1274.
    • (2000) Am. J. Pathol. , vol.156 , pp. 1263-1274
    • Zatloukal, K.1    Stumptner, C.2    Zatloukal, K.3    Stumptner, C.4    Lehner, M.5    Denk, H.6    Baribault, H.7    Eshkind, L.G.8    Franke, W.W.9
  • 441
    • 0035158886 scopus 로고    scopus 로고
    • Keratin 23 (K23), a novel acidic keratin, is highly induced by histone deacetylase inhibitors during differentiation of pancreatic cancer cells
    • Zhang, J. S., Wang, L., Huang, H., Nelson, M., and Smith, D. I. (2001). Keratin 23 (K23), a novel acidic keratin, is highly induced by histone deacetylase inhibitors during differentiation of pancreatic cancer cells. Genes Chromosomes Cancer 30, 123-135.
    • (2001) Genes Chromosomes Cancer , vol.30 , pp. 123-135
    • Zhang, J.S.1    Wang, L.2    Huang, H.3    Nelson, M.4    Smith, D.I.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.