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Volumn 164, Issue , 1996, Pages 91-138

Integration of intermediate filaments into cellular organelles

Author keywords

Centrosome; Cytoskeleton; Intermediate filaments; Lamins; Membrane skeleton; Nuclear envelope; Plasma membrane

Indexed keywords

KERATIN; LAMIN;

EID: 0030023118     PISSN: 00747696     EISSN: None     Source Type: Book Series    
DOI: 10.1016/s0074-7696(08)62385-2     Document Type: Review
Times cited : (44)

References (293)
  • 1
    • 0023545331 scopus 로고
    • The expression of mutant epidermal keratin cDNA transfected in simple epithelial and squamous cell carcinoma lines
    • K. Albers E. Fuchs The expression of mutant epidermal keratin cDNA transfected in simple epithelial and squamous cell carcinoma lines J. Cell Biol. 105 1987 791 806
    • (1987) J. Cell Biol. , vol.105 , pp. 791-806
    • Albers, K.1    Fuchs, E.2
  • 2
    • 0024504168 scopus 로고
    • Expression of mutant keratin cDNAs in epithelial cells reveals possible mechanisms for initiation and assembly of intermediate filaments
    • K. Albers E. Fuchs Expression of mutant keratin cDNAs in epithelial cells reveals possible mechanisms for initiation and assembly of intermediate filaments J. Cell Biol. 108 1989 1477 1493
    • (1989) J. Cell Biol. , vol.108 , pp. 1477-1493
    • Albers, K.1    Fuchs, E.2
  • 3
    • 0023668669 scopus 로고
    • Band 3 and ankyrin homologues are present in the eye lens: Evidence for all major erythrocyte membrane components in the same non-erythroid cell
    • D.P. Allen P.S. Low A. Dola H. Maisel Band 3 and ankyrin homologues are present in the eye lens: Evidence for all major erythrocyte membrane components in the same non-erythroid cell Biochem. Biophys. Res. Commun. 149 1987 266 275
    • (1987) Biochem. Biophys. Res. Commun. , vol.149 , pp. 266-275
    • Allen, D.P.1    Low, P.S.2    Dola, A.3    Maisel, H.4
  • 4
    • 0025674206 scopus 로고
    • The role of intermediate filaments in adrenal steroidogenesis
    • G. Almahbobi P.F. Hall The role of intermediate filaments in adrenal steroidogenesis J. Cell Sci. 97 1990 679 687
    • (1990) J. Cell Sci. , vol.97 , pp. 679-687
    • Almahbobi, G.1    Hall, P.F.2
  • 5
    • 0026753684 scopus 로고
    • Attachment of mitochondria to intermediate filaments in adrenal cells: Relevance to the regulation of steroid synthesis
    • G. Almahbobi L.J. Williams P.F. Hall Attachment of mitochondria to intermediate filaments in adrenal cells: Relevance to the regulation of steroid synthesis Exp. Cell Res. 200 1992 361 369
    • (1992) Exp. Cell Res. , vol.200 , pp. 361-369
    • Almahbobi, G.1    Williams, L.J.2    Hall, P.F.3
  • 6
    • 0026597697 scopus 로고
    • Attachment of steroidogenic lipid droplets to intermediate filaments in adrenal cells
    • G. Almahbobi L.J. Williams P.F. Hall Attachment of steroidogenic lipid droplets to intermediate filaments in adrenal cells J. Cell Sci. 101 1992 383 393
    • (1992) J. Cell Sci. , vol.101 , pp. 383-393
    • Almahbobi, G.1    Williams, L.J.2    Hall, P.F.3
  • 7
    • 0024600639 scopus 로고
    • Assembly and exchange of intermediate filament proteins of neurons: Neurofilaments are dynamic structures
    • K.J. Angelides K.E. Smith M. Takeda Assembly and exchange of intermediate filament proteins of neurons: Neurofilaments are dynamic structures J. Cell Biol. 198 1989 1495 1506
    • (1989) J. Cell Biol. , vol.198 , pp. 1495-1506
    • Angelides, K.J.1    Smith, K.E.2    Takeda, M.3
  • 8
    • 0025165922 scopus 로고
    • Desmoplakin II expression is not restricted to stratified epithelia
    • B.D. Angst L.A. Nilles K.J. Green Desmoplakin II expression is not restricted to stratified epithelia J. Cell Sci. 97 1990 247 257
    • (1990) J. Cell Sci. , vol.97 , pp. 247-257
    • Angst, B.D.1    Nilles, L.A.2    Green, K.J.3
  • 9
    • 0025339073 scopus 로고
    • Lipids noncovalently associated with keratins and other cytoskeletal proteins of mouse mammary epithelial cells in primary culture
    • H.L. Asch E. Mayhew R.O. Lazo B.B. Asch Lipids noncovalently associated with keratins and other cytoskeletal proteins of mouse mammary epithelial cells in primary culture Biochim. Biophys. Acta 1034 1990 303 308
    • (1990) Biochim. Biophys. Acta , vol.1034 , pp. 303-308
    • Asch, H.L.1    Mayhew, E.2    Lazo, R.O.3    Asch, B.B.4
  • 12
    • 0022486518 scopus 로고
    • The 4.1-like proteins of the bovine lens: Spectrin-binding proteins closely related in structure to the RBC protein 4.1
    • J.C. Aster G.J. Brewer H. Maisel The 4.1-like proteins of the bovine lens: Spectrin-binding proteins closely related in structure to the RBC protein 4.1 J. Cell Biol. 103 1986 115 122
    • (1986) J. Cell Biol. , vol.103 , pp. 115-122
    • Aster, J.C.1    Brewer, G.J.2    Maisel, H.3
  • 13
    • 0025718837 scopus 로고
    • Intermediate filaments formed de novo from tail-less cytokeratins in the cytoplasm and in the nucleus
    • B.L. Bader T.M. Magnin M. Freudenmann S. Stumpp W.W. Franke Intermediate filaments formed de novo from tail-less cytokeratins in the cytoplasm and in the nucleus J. Cell Biol. 115 1991 1293 1307
    • (1991) J. Cell Biol. , vol.115 , pp. 1293-1307
    • Bader, B.L.1    Magnin, T.M.2    Freudenmann, M.3    Stumpp, S.4    Franke, W.W.5
  • 14
    • 0025861822 scopus 로고
    • Characterization a 54-kD protein of the inner nuclear membrane: Evidence for cell cycle-dependent interaction with the nuclear lamina
    • S.M. Bailer H.M. Eppenberger G. Griffiths E.A. Nigg Characterization a 54-kD protein of the inner nuclear membrane: Evidence for cell cycle-dependent interaction with the nuclear lamina J. Cell Biol. 114 1991 389 400
    • (1991) J. Cell Biol. , vol.114 , pp. 389-400
    • Bailer, S.M.1    Eppenberger, H.M.2    Griffiths, G.3    Nigg, E.A.4
  • 15
    • 0027227464 scopus 로고
    • Mid-gestational lethality in mice lacking keratin 8
    • H. Baribault J. Price K. Miyai R.G. Oshima Mid-gestational lethality in mice lacking keratin 8 Genes Dev. 7 1993 1191 1201
    • (1993) Genes Dev. , vol.7 , pp. 1191-1201
    • Baribault, H.1    Price, J.2    Miyai, K.3    Oshima, R.G.4
  • 16
    • 0017650408 scopus 로고
    • Effects of anabolic steroids on rat heart muscle cells. I. Intermediate filaments
    • H. Behrendt Effects of anabolic steroids on rat heart muscle cells. I. Intermediate filaments Cell Tissue Res. 180 1977 303 315
    • (1977) Cell Tissue Res. , vol.180 , pp. 303-315
    • Behrendt, H.1
  • 17
    • 0003529799 scopus 로고
    • Lenticular plasma membranes and cytoskeleton
    • E.L. Benedetti L. Dunia F.C.S. Ramaekers M.A. Kibbelaar Lenticular plasma membranes and cytoskeleton H. Bloemendal “Molecular and Cellular Biology of the Eye Lens” 1981 Wiley New York 137 188
    • (1981) , pp. 137-188
    • Benedetti, E.L.1    Dunia, L.2    Ramaekers, F.C.S.3    Kibbelaar, M.A.4
  • 18
    • 0018234447 scopus 로고
    • Immunofluorescent visualization of 100 A filaments in different cultured chick embryo cell types
    • G.S. Bennett J.A. Fellini H. Holtzer Immunofluorescent visualization of 100 A filaments in different cultured chick embryo cell types Differentiation (Berlin) 12 1978 71 81
    • (1978) Differentiation (Berlin) , vol.12 , pp. 71-81
    • Bennett, G.S.1    Fellini, J.A.2    Holtzer, H.3
  • 19
    • 0018584180 scopus 로고
    • Redistribution of intermediate filament subunits during skeletal myogenesis and maturation in vitro
    • G.S. Bennett S.A. Fellini Y. Toyama H. Holtzer Redistribution of intermediate filament subunits during skeletal myogenesis and maturation in vitro J. Cell Biol. 82 1979 577 584
    • (1979) J. Cell Biol. , vol.82 , pp. 577-584
    • Bennett, G.S.1    Fellini, S.A.2    Toyama, Y.3    Holtzer, H.4
  • 20
    • 0024242826 scopus 로고
    • Isolation of an immunoreactive analogue of brain fodrin that is associated with the cell cortex of Dictyostelium amoebae
    • H. Bennett J. Condeelis Isolation of an immunoreactive analogue of brain fodrin that is associated with the cell cortex of Dictyostelium amoebae Cell Motil. Cytoskel. 11 1988 303 317
    • (1988) Cell Motil. Cytoskel. , vol.11 , pp. 303-317
    • Bennett, H.1    Condeelis, J.2
  • 21
    • 0016716878 scopus 로고
    • Association of mitochondria with desmosomes in the rate thyroid gland
    • L.H. Bernstein S.H. Wollman Association of mitochondria with desmosomes in the rate thyroid gland J. Ultrastruct. Res. 53 1975 87 92
    • (1975) J. Ultrastruct. Res. , vol.53 , pp. 87-92
    • Bernstein, L.H.1    Wollman, S.H.2
  • 22
    • 0014468808 scopus 로고
    • Conformational changes in myocardial nuclei of rats
    • S. Bloom P.A. Cincilla Conformational changes in myocardial nuclei of rats Circ. Res. 24 1969 189 196
    • (1969) Circ. Res. , vol.24 , pp. 189-196
    • Bloom, S.1    Cincilla, P.A.2
  • 23
    • 0021352916 scopus 로고
    • 10-nm filaments are induced to collapse in living cells microinjected with monoclonal and polyclonal antibodies against tubulin
    • S.H. Blose D.I. Meltzer J.R. Feramisco 10-nm filaments are induced to collapse in living cells microinjected with monoclonal and polyclonal antibodies against tubulin J. Cell Biol. 98 1984 847 858
    • (1984) J. Cell Biol. , vol.98 , pp. 847-858
    • Blose, S.H.1    Meltzer, D.I.2    Feramisco, J.R.3
  • 24
    • 0020399066 scopus 로고
    • Dense bodies and actin polarity in vertebrate smooth muscle
    • M. Bond A.V. Somlyo Dense bodies and actin polarity in vertebrate smooth muscle J. Cell Biol. 95 1982 403 413
    • (1982) J. Cell Biol. , vol.95 , pp. 403-413
    • Bond, M.1    Somlyo, A.V.2
  • 26
    • 0027095747 scopus 로고
    • Membrane-binding properties of filensin, cytoskeletal protein of the lens fiber cells
    • M. Brunkener S.D. Georgatos Membrane-binding properties of filensin, cytoskeletal protein of the lens fiber cells J. Cell Sci. 103 1992 709 718
    • (1992) J. Cell Sci. , vol.103 , pp. 709-718
    • Brunkener, M.1    Georgatos, S.D.2
  • 27
    • 0014183052 scopus 로고
    • Cytoplasmic fibrils in living cultured cells. A light and electron microscope study
    • I.K. Buckley K.R. Porter Cytoplasmic fibrils in living cultured cells. A light and electron microscope study Protoplasma 64 1967 349 380
    • (1967) Protoplasma , vol.64 , pp. 349-380
    • Buckley, I.K.1    Porter, K.R.2
  • 28
    • 0025056506 scopus 로고
    • On the cell-free association of lamins A and C with metaphase chromosomes
    • B. Burke On the cell-free association of lamins A and C with metaphase chromosomes Exp. Cell Res. 186 1990 169 176
    • (1990) Exp. Cell Res. , vol.186 , pp. 169-176
    • Burke, B.1
  • 29
    • 0026756891 scopus 로고
    • Plakoglobin and β-catenin: Distinct but closely related
    • S. Butz J. Stappert H. Weissig R. Kemler Plakoglobin and β-catenin: Distinct but closely related Science 257 1992 1442 1444
    • (1992) Science , vol.257 , pp. 1442-1444
    • Butz, S.1    Stappert, J.2    Weissig, H.3    Kemler, R.4
  • 30
    • 0026754234 scopus 로고
    • The complete sequence of Drosophila beta spectrin reveals supramotifs comprising eight 106-residue repeats
    • T.J. Byers E. Brandin R. Lue E. Winograd D. Branton The complete sequence of Drosophila beta spectrin reveals supramotifs comprising eight 106-residue repeats Proc. Natl. Acad. Sci. U.S.A. 89 1992 6187 6191
    • (1992) Proc. Natl. Acad. Sci. U.S.A. , vol.89 , pp. 6187-6191
    • Byers, T.J.1    Brandin, E.2    Lue, R.3    Winograd, E.4    Branton, D.5
  • 31
    • 0028091980 scopus 로고
    • Trp, a larger coiled coil protein whose amino terminus involved in activation oncogenic kinases, is localized to the cytoplasmic surface of the nuclear pore complex
    • D.A. Byrd D.J. Sweet N. Pante K.N. Konstantinov T. Guan A.C. Saphire P.J. Mitchell C.S. Cooper U. Aebi L. Gerace Trp, a larger coiled coil protein whose amino terminus involved in activation oncogenic kinases, is localized to the cytoplasmic surface of the nuclear pore complex J. Cell Biol. 127 1994 1515 1526
    • (1994) J. Cell Biol. , vol.127 , pp. 1515-1526
    • Byrd, D.A.1    Sweet, D.J.2    Pante, N.3    Konstantinov, K.N.4    Guan, T.5    Saphire, A.C.6    Mitchell, P.J.7    Cooper, C.S.8    Aebi, U.9    Gerace, L.10
  • 32
    • 0018657369 scopus 로고
    • Antibody staining of 10 nm (100 A) filaments in cultured smooth cardiac and skeletal muscle cells
    • G.R. Campbell J.C. Campbell U.G. Stewart J.V. Small P. Andersen Antibody staining of 10 nm (100 A) filaments in cultured smooth cardiac and skeletal muscle cells J. Cell Sci. 37 1979 303 322
    • (1979) J. Cell Sci. , vol.37 , pp. 303-322
    • Campbell, G.R.1    Campbell, J.C.2    Stewart, U.G.3    Small, J.V.4    Andersen, P.5
  • 33
    • 0020162216 scopus 로고
    • The nuclear matrix: Three-dimensional architecture and protein composition
    • D.G. Capco K.M. Wan S. Penman The nuclear matrix: Three-dimensional architecture and protein composition Cell (Cambridge, Mass.) 29 1982 847 858
    • (1982) Cell (Cambridge, Mass.) , vol.29 , pp. 847-858
    • Capco, D.G.1    Wan, K.M.2    Penman, S.3
  • 34
    • 0024470306 scopus 로고
    • Overexpression of the vimentin gene in transgenic mice inhibits normal lens cell differentiation
    • Y. Capetanaki S. Smith J.P. Health Overexpression of the vimentin gene in transgenic mice inhibits normal lens cell differentiation J. Cell Biol. 109 1989 1653 1664
    • (1989) J. Cell Biol. , vol.109 , pp. 1653-1664
    • Capetanaki, Y.1    Smith, S.2    Health, J.P.3
  • 36
    • 0023953897 scopus 로고
    • Filamentous cross-bridges link intermediate filaments to the nuclear pore complexes
    • M. Carmo-Fonseca A.J. Cidadao D.F. David-Ferreira Filamentous cross-bridges link intermediate filaments to the nuclear pore complexes Eur. J. Cell Biol. 45 1987 282 290
    • (1987) Eur. J. Cell Biol. , vol.45 , pp. 282-290
    • Carmo-Fonseca, M.1    Cidadao, A.J.2    David-Ferreira, D.F.3
  • 37
    • 0024436494 scopus 로고
    • Presence of a protein immunologically related to lamin B in the postsynaptic membrane of Torpedo marmorata electrocyte
    • A. Cartaud J.C. Courvalin M.A. Ludosky J. Cartaud Presence of a protein immunologically related to lamin B in the postsynaptic membrane of Torpedo marmorata electrocyte J. Cell Biol. 109 1989 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
  • 38
    • 0025316130 scopus 로고
    • A protein antigenically related to nuclear lamin B mediates the association of intermediate filaments with desmosomes
    • A. Cartaud M.A. Ludosky J.C. Courvalin J. Cartaud A protein antigenically related to nuclear lamin B mediates the association of intermediate filaments with desmosomes J. Cell Biol. 111 1990 581 588
    • (1990) J. Cell Biol. , vol.111 , pp. 581-588
    • Cartaud, A.1    Ludosky, M.A.2    Courvalin, J.C.3    Cartaud, J.4
  • 39
    • 0028896722 scopus 로고
    • Direct involvement of a lamin-B related (54KDa) protein in the association of intermediate filaments with the postsynaptic membrane of the Torpedo marmorata electrocyte
    • A. Cartaud B.J. Jasmin J.-P. Changeux J. Cartaud Direct involvement of a lamin-B related (54KDa) protein in the association of intermediate filaments with the postsynaptic membrane of the Torpedo marmorata electrocyte J. Cell Sci. 108 1995 153 160
    • (1995) J. Cell Sci. , vol.108 , pp. 153-160
    • Cartaud, A.1    Jasmin, B.J.2    Changeux, J.-P.3    Cartaud, J.4
  • 40
    • 0028225888 scopus 로고
    • Differential organization of desmin and vimentin in muscle is due to differences in their head domains
    • R.B. Cary M.W. Klymkowsky Differential organization of desmin and vimentin in muscle is due to differences in their head domains J. Cell Biol. 126 1994 445 456
    • (1994) J. Cell Biol. , vol.126 , pp. 445-456
    • Cary, R.B.1    Klymkowsky, M.W.2
  • 41
    • 0028274143 scopus 로고
    • Desmin organization during the differentiation of the dorsal myotome in Xenopus laevis.
    • R.B. Cary M.W. Klymkowsky Desmin organization during the differentiation of the dorsal myotome in Xenopus laevis. Differentiation (Berlin) 56 1994 31 38
    • (1994) Differentiation (Berlin) , vol.56 , pp. 31-38
    • Cary, R.B.1    Klymkowsky, M.W.2
  • 42
    • 0028967854 scopus 로고
    • Disruption of intermediate filament organization leads to structural defects at the intersomite junction in Xenopus myotomal muscle
    • R.B. Cary M.W. Klymkowsky Disruption of intermediate filament organization leads to structural defects at the intersomite junction in Xenopus myotomal muscle Development 121 1995 1041 1052
    • (1995) Development , vol.121 , pp. 1041-1052
    • Cary, R.B.1    Klymkowsky, M.W.2
  • 43
    • 0021336448 scopus 로고
    • Intermediate filaments in monkey kidney TC7 cells: Focal centers and interrelationship with other cytoskeletal systems
    • J.E. Celis J.V. Small P.M. Larsen S.J. Fey J. De Mey A. Celis Intermediate filaments in monkey kidney TC7 cells: Focal centers and interrelationship with other cytoskeletal systems Proc. Natl. Acad. Sci. U.S.A. 81 1984 1117 1121
    • (1984) Proc. Natl. Acad. Sci. U.S.A. , vol.81 , pp. 1117-1121
    • Celis, J.E.1    Small, J.V.2    Larsen, P.M.3    Fey, S.J.4    De Mey, J.5    Celis, A.6
  • 44
    • 0022487317 scopus 로고
    • Structure and composition of the cytoskeleton of nucleated erythrocytes: III. Organization of the cytoskeleton of Bufo maranis erythrocytes as revealed by freeze-dried platinum carbon replicas and immunofluorescence microscopy
    • V.E. Centonze G.C. Ruben R.D. Sloboda Structure and composition of the cytoskeleton of nucleated erythrocytes: III. Organization of the cytoskeleton of Bufo maranis erythrocytes as revealed by freeze-dried platinum carbon replicas and immunofluorescence microscopy Cell Motil. Cytoskel. 6 1986 376 388
    • (1986) Cell Motil. Cytoskel. , vol.6 , pp. 376-388
    • Centonze, V.E.1    Ruben, G.C.2    Sloboda, R.D.3
  • 45
    • 0027275334 scopus 로고
    • Stepwise reassembly of the nuclear envelope at the end of mitosis
    • N. Chaudhary J.-N. Courvalin Stepwise reassembly of the nuclear envelope at the end of mitosis J. Cell Biol. 122 1993 295 306
    • (1993) J. Cell Biol. , vol.122 , pp. 295-306
    • Chaudhary, N.1    Courvalin, J.-N.2
  • 46
    • 0024148694 scopus 로고
    • Mitochondrial membrane potential in living cells
    • L.B. Chen Mitochondrial membrane potential in living cells Annu. Rev. Cell Biol. 4 1988 155 181
    • (1988) Annu. Rev. Cell Biol. , vol.4 , pp. 155-181
    • Chen, L.B.1
  • 48
    • 0024787034 scopus 로고
    • Expression of rat neurofilament proteins NF-L and NF-M in transfected non-neuronal cells
    • S.S.M. Chin R.K.H. Liem Expression of rat neurofilament proteins NF-L and NF-M in transfected non-neuronal cells Eur. J. Cell Biol. 50 1989 475 490
    • (1989) Eur. J. Cell Biol. , vol.50 , pp. 475-490
    • Chin, S.S.M.1    Liem, R.K.H.2
  • 50
    • 0026528959 scopus 로고
    • Assembly of contractile and cytoskeletal elements in developing smooth muscle cells
    • R.R. Chou M.H. Stromer Robson R.M. T.W. Huiatt Assembly of contractile and cytoskeletal elements in developing smooth muscle cells Dev. Biol. 149 1992 339 348
    • (1992) Dev. Biol. , vol.149 , pp. 339-348
    • Chou, R.R.1    Stromer, M.H.2    Robson, R.M.3    Huiatt, T.W.4
  • 51
    • 0026582529 scopus 로고
    • Redistribution of nuclear lamin A is an early event associated with differentiation of human promyelocytic leukemia HL-60 cells
    • J.-F. Collard J.L. Senecal Y. Raymond Redistribution of nuclear lamin A is an early event associated with differentiation of human promyelocytic leukemia HL-60 cells J. Cell Sci. 101 1992 657 670
    • (1992) J. Cell Sci. , vol.101 , pp. 657-670
    • Collard, J.-F.1    Senecal, J.L.2    Raymond, Y.3
  • 52
    • 0027226155 scopus 로고
    • Concomitant changes in mitochondria and intermediate filaments during heat shock and recovery of chicken embryo fibroblasts
    • N.C. Collier M.P. Sheetz M.J. Schlesinger Concomitant changes in mitochondria and intermediate filaments during heat shock and recovery of chicken embryo fibroblasts J. Cell. Biochem. 52 1993 297 307
    • (1993) J. Cell. Biochem. , vol.52 , pp. 297-307
    • Collier, N.C.1    Sheetz, M.P.2    Schlesinger, M.J.3
  • 54
    • 33749357063 scopus 로고
    • Intermediate filament structure: 3. Analysis of sequence homologies
    • J.F. Conway D.A.D. Parry Intermediate filament structure: 3. Analysis of sequence homologies Int. J. Biol. Macromol. 10 1988 79 98
    • (1988) Int. J. Biol. Macromol. , vol.10 , pp. 79-98
    • Conway, J.F.1    Parry, D.A.D.2
  • 55
    • 0025130161 scopus 로고
    • Structural features in the heptad substructure and longer range repeats of two-stranded α-fibrous proteins
    • J.F. Conway D.A.D. Parry Structural features in the heptad substructure and longer range repeats of two-stranded α-fibrous proteins Int. J. Biol. Macromol. 12 1990 328 334
    • (1990) Int. J. Biol. Macromol. , vol.12 , pp. 328-334
    • Conway, J.F.1    Parry, D.A.D.2
  • 56
    • 0017257712 scopus 로고
    • A filamentous cytoskeleton in vertebrate smooth muscle fibers
    • P. Cooke A filamentous cytoskeleton in vertebrate smooth muscle fibers J. Cell Biol. 68 1976 539 556
    • (1976) J. Cell Biol. , vol.68 , pp. 539-556
    • Cooke, P.1
  • 57
    • 0015073480 scopus 로고
    • Potassium chloride-insoluble myofilaments in vertebrate smooth muscle cells
    • P.H. Cooke R.H. Chase Potassium chloride-insoluble myofilaments in vertebrate smooth muscle cells Exp. Cell Res. 66 1971 417 425
    • (1971) Exp. Cell Res. , vol.66 , pp. 417-425
    • Cooke, P.H.1    Chase, R.H.2
  • 58
    • 0027465098 scopus 로고
    • Progressive neuronopathy in transgenic mice expressing the human neurofilament heavy gene: A mouse model of amyotrophic lateral sclerosis
    • F. Cote J.-F. Collard J.-P. Julien Progressive neuronopathy in transgenic mice expressing the human neurofilament heavy gene: A mouse model of amyotrophic lateral sclerosis Cell (Cambridge, Mass.) 73 1993 35 46
    • (1993) Cell (Cambridge, Mass.) , vol.73 , pp. 35-46
    • Cote, F.1    Collard, J.-F.2    Julien, J.-P.3
  • 59
    • 0026783801 scopus 로고
    • The lamin B receptor of the inner nuclear membrane undergoes mitosis-specific phosphorylation and is a substrate for p34cdc2-type protein kinase
    • J.-C. Courvalin N. Segil G. Blobel H.J. Worman The lamin B receptor of the inner nuclear membrane undergoes mitosis-specific phosphorylation and is a substrate for p34cdc2-type protein kinase J. Biol. Chem. 267 1992 19035 19038
    • (1992) J. Biol. Chem. , vol.267 , pp. 19035-19038
    • Courvalin, J.-C.1    Segil, N.2    Blobel, G.3    Worman, H.J.4
  • 60
    • 0020676510 scopus 로고
    • Antibodies to epithelial desmosomes show wide tissue and species cross-reactivity
    • P. Cowin D. Garrod Antibodies to epithelial desmosomes show wide tissue and species cross-reactivity Nature (London) 302 1983 148 150
    • (1983) Nature (London) , vol.302 , pp. 148-150
    • Cowin, P.1    Garrod, D.2
  • 61
    • 0022345716 scopus 로고
    • The complement of desmosomal plaque proteins in different cell types
    • P. Cowin H.-P. Kapprell W.W. Franke The complement of desmosomal plaque proteins in different cell types J. Cell Biol. 101 1985 1442 1454
    • (1985) J. Cell Biol. , vol.101 , pp. 1442-1454
    • Cowin, P.1    Kapprell, H.-P.2    Franke, W.W.3
  • 63
    • 0024245405 scopus 로고
    • Identification of attachment proteins for DNA in Chinese hamster ovary cells
    • A.E. Cress K.M. Kurath Identification of attachment proteins for DNA in Chinese hamster ovary cells J. Biol. Chem. 263 1988 19678 19683
    • (1988) J. Biol. Chem. , vol.263 , pp. 19678-19683
    • Cress, A.E.1    Kurath, K.M.2
  • 64
    • 0019309384 scopus 로고
    • Association between intermediate-sized filaments and mitochondria in rat Leydig cells
    • K.L. David-Ferreira J.F. David-Ferreira Association between intermediate-sized filaments and mitochondria in rat Leydig cells Cell Biol. Int. Rep. 4 1980 655 662
    • (1980) Cell Biol. Int. Rep. , vol.4 , pp. 655-662
    • David-Ferreira, K.L.1    David-Ferreira, J.F.2
  • 65
    • 0021689392 scopus 로고
    • Brain ankyrin—a membrane-associated protein with binding sites for spectrin, tubulin and the cytoplasmic domain of the erythrocyte anion channel
    • J.Q. Davis V. Bennett Brain ankyrin—a membrane-associated protein with binding sites for spectrin, tubulin and the cytoplasmic domain of the erythrocyte anion channel J. Biol. Chem. 259 1984 13550 133559
    • (1984) J. Biol. Chem. , vol.259 , pp. 13550-133559
    • Davis, J.Q.1    Bennett, V.2
  • 67
    • 0026021706 scopus 로고
    • Network antibodies identify nuclear lamin B as physiological attachment size for peripherin intermediate filaments
    • K. Djabali M.M. Portier F. Gros G. Blobel S.D. Georgatos Network antibodies identify nuclear lamin B as physiological attachment size for peripherin intermediate filaments Cell (Cambridge, Mass.) 64 1991 109 121
    • (1991) Cell (Cambridge, Mass.) , vol.64 , pp. 109-121
    • Djabali, K.1    Portier, M.M.2    Gros, F.3    Blobel, G.4    Georgatos, S.D.5
  • 69
    • 0025013610 scopus 로고
    • Structure of an invertebrate gene encoding cytoplasmic intermediate filament (IF) proteins: Implications for the origin and the diversification of IF proteins
    • H. Dodemont D. Riemer K. Weber Structure of an invertebrate gene encoding cytoplasmic intermediate filament (IF) proteins: Implications for the origin and the diversification of IF proteins EMBO J. 9 1990 4083 4094
    • (1990) EMBO J. , vol.9 , pp. 4083-4094
    • Dodemont, H.1    Riemer, D.2    Weber, K.3
  • 70
    • 0027761324 scopus 로고
    • A microtubule-interacting protein involved in coalignment of vimentin intermediate filaments with microtubules
    • E. Draberova P. Draber A microtubule-interacting protein involved in coalignment of vimentin intermediate filaments with microtubules J. Cell Sci. 106 1993 1263 1273
    • (1993) J. Cell Sci. , vol.106 , pp. 1263-1273
    • Draberova, E.1    Draber, P.2
  • 72
    • 0024449311 scopus 로고
    • The complete sequence of Drosophila alpha-spectrin: Conservation of structural domains between alpha-spectrins and alpha-actinin
    • R.R. Dubreuil T.J. Byers A.L. Sillman D. Bar-Zvi L.S.B. Goldstein D. Branton The complete sequence of Drosophila alpha-spectrin: Conservation of structural domains between alpha-spectrins and alpha-actinin J. Cell Biol. 109 1989 2197 2205
    • (1989) J. Cell Biol. , vol.109 , pp. 2197-2205
    • Dubreuil, R.R.1    Byers, T.J.2    Sillman, A.L.3    Bar-Zvi, D.4    Goldstein, L.S.B.5    Branton, D.6
  • 73
    • 0026706734 scopus 로고
    • Assembly of a tail-less mutant of the intermediate filament protein, vimentin, in vitro and in vivo
    • A. Eckelt H. Herrmann W.W. Franke Assembly of a tail-less mutant of the intermediate filament protein, vimentin, in vitro and in vivo Eur. J. Cell Biol. 58 1992 319 330
    • (1992) Eur. J. Cell Biol. , vol.58 , pp. 319-330
    • Eckelt, A.1    Herrmann, H.2    Franke, W.W.3
  • 74
    • 0022603842 scopus 로고
    • Alteration of the distribution of intermediate filaments in PtK1 cells by acrylamide. II: Effect on the organization of cytoplasmic organelles
    • B.S. Eckert Alteration of the distribution of intermediate filaments in PtK1 cells by acrylamide. II: Effect on the organization of cytoplasmic organelles Cell Motil. Cytoskel. 6 1986 15 24
    • (1986) Cell Motil. Cytoskel. , vol.6 , pp. 15-24
    • Eckert, B.S.1
  • 75
    • 0021118375 scopus 로고
    • Co-localization of the centriole and keratin intermediate filaments in PtK1 cells
    • B.S. Eckert S.E. Caputi B.R. Brinkley Co-localization of the centriole and keratin intermediate filaments in PtK1 cells Cell Motil. 4 1984 241 248
    • (1984) Cell Motil. , vol.4 , pp. 241-248
    • Eckert, B.S.1    Caputi, S.E.2    Brinkley, B.R.3
  • 76
  • 77
    • 0000752197 scopus 로고
    • Junctional complexes in various epithelia
    • M.G. Farquhar G.E. Palade Junctional complexes in various epithelia J. Cell Biol. 17 1963 375 412
    • (1963) J. Cell Biol. , vol.17 , pp. 375-412
    • Farquhar, M.G.1    Palade, G.E.2
  • 78
    • 0020532418 scopus 로고
    • Distribution of alpha-actinin in single isolated smooth muscle cells
    • F.S. Fay K. Fujiwara D.D. Rees K.E. Fogarty Distribution of alpha-actinin in single isolated smooth muscle cells J. Cell Biol. 96 1983 783 795
    • (1983) J. Cell Biol. , vol.96 , pp. 783-795
    • Fay, F.S.1    Fujiwara, K.2    Rees, D.D.3    Fogarty, K.E.4
  • 79
    • 0017309730 scopus 로고
    • Different distribution pattern of 100 A filaments in resting and locomotive leukaemia cells
    • H. Felix P. Strauli Different distribution pattern of 100 A filaments in resting and locomotive leukaemia cells Nature (London) 261 1976 604 606
    • (1976) Nature (London) , vol.261 , pp. 604-606
    • Felix, H.1    Strauli, P.2
  • 80
    • 0015828904 scopus 로고
    • Intermyofibrillar and nuclear-myofibrillar connections in human and canine myocardium. An ultrastructural study
    • V.J. Ferrans W.C. Roberts Intermyofibrillar and nuclear-myofibrillar connections in human and canine myocardium. An ultrastructural study J. Mol. Cell Cardiol. 5 1973 247 257
    • (1973) J. Mol. Cell Cardiol. , vol.5 , pp. 247-257
    • Ferrans, V.J.1    Roberts, W.C.2
  • 81
    • 0021244964 scopus 로고
    • Epithelial cytoskeletal framework and nuclear matrix-intermediate filament scaffold: Three-dimensional organization and protein composition
    • E.G. Fey K.M. Wan S. Penman Epithelial cytoskeletal framework and nuclear matrix-intermediate filament scaffold: Three-dimensional organization and protein composition J. Cell Biol. 98 1984 1973 1984
    • (1984) J. Cell Biol. , vol.98 , pp. 1973-1984
    • Fey, E.G.1    Wan, K.M.2    Penman, S.3
  • 82
    • 0027763283 scopus 로고
    • The role of CaaX-dependent modifications in membrane association of Xenopus lamin B3 during meiosis and fate of B3 in transfected mitotic cells
    • I. Firmbach-Kraft R. Stick The role of CaaX-dependent modifications in membrane association of Xenopus lamin B3 during meiosis and fate of B3 in transfected mitotic cells J. Cell Biol. 123 1993 1661 1670
    • (1993) J. Cell Biol. , vol.123 , pp. 1661-1670
    • Firmbach-Kraft, I.1    Stick, R.2
  • 83
    • 0027276759 scopus 로고
    • Integral membrane proteins of the nuclear envelope interact with lamins and chromosomes, and binding is modulated by mitotic phosphorylation
    • R. Foisner L. Gerace Integral membrane proteins of the nuclear envelope interact with lamins and chromosomes, and binding is modulated by mitotic phosphorylation Cell (Cambridge, Mass.) 73 1993 1267 1279
    • (1993) Cell (Cambridge, Mass.) , vol.73 , pp. 1267-1279
    • Foisner, R.1    Gerace, L.2
  • 84
    • 0015167123 scopus 로고
    • Relationship of nuclear membranes with filaments and microtubules
    • W.W. Franke Relationship of nuclear membranes with filaments and microtubules Protoplasma 73 1971 263 292
    • (1971) Protoplasma , vol.73 , pp. 263-292
    • Franke, W.W.1
  • 85
    • 0014549251 scopus 로고
    • Nuclear shape in muscle cells
    • W.W. Franke W. Schinko Nuclear shape in muscle cells J. Cell Biol. 42 1969 326 331
    • (1969) J. Cell Biol. , vol.42 , pp. 326-331
    • Franke, W.W.1    Schinko, W.2
  • 87
    • 0023649685 scopus 로고
    • Rearrangement of the vimentin cytoskeleton during adipose conversion: Formation of an intermediate filament cage around lipid globules
    • W.W. Franke M. Hergt C. Grund Rearrangement of the vimentin cytoskeleton during adipose conversion: Formation of an intermediate filament cage around lipid globules Cell (Cambridge, Mass.) 49 1987 131 141
    • (1987) Cell (Cambridge, Mass.) , vol.49 , pp. 131-141
    • Franke, W.W.1    Hergt, M.2    Grund, C.3
  • 88
    • 0023353373 scopus 로고
    • Plakoglobin is a component of the filamentous subplasmalemmal coat of lens cells
    • W.W. Franke H.-P. Kapprell P. Cowin Plakoglobin is a component of the filamentous subplasmalemmal coat of lens cells Eur. J. Cell Biol. 43 1987 301 315
    • (1987) Eur. J. Cell Biol. , vol.43 , pp. 301-315
    • Franke, W.W.1    Kapprell, H.-P.2    Cowin, P.3
  • 91
    • 0028287112 scopus 로고
    • Intermediate filaments and disease: Mutations that cripple cell strength
    • E. Fuchs Intermediate filaments and disease: Mutations that cripple cell strength J. Cell Biol. 125 1994 511 516
    • (1994) J. Cell Biol. , vol.125 , pp. 511-516
    • Fuchs, E.1
  • 92
    • 0028283501 scopus 로고
    • Intermediate filaments: Structure, dynamics, function, and disease
    • E. Fuchs K. Weber Intermediate filaments: Structure, dynamics, function, and disease Annu. Rev. Biochem. 63 1994 345 382
    • (1994) Annu. Rev. Biochem. , vol.63 , pp. 345-382
    • Fuchs, E.1    Weber, K.2
  • 93
    • 0026725118 scopus 로고
    • Transgenic mice expressing a mutant keratin 10 gene reveal the likely genetic basis for epidermolytic hyperkeratosis
    • E. Fuchs R.A. Esteves P.A. Coulombe Transgenic mice expressing a mutant keratin 10 gene reveal the likely genetic basis for epidermolytic hyperkeratosis Proc. Natl. Acad. Sci. U.S.A. 89 1992 6909 6910
    • (1992) Proc. Natl. Acad. Sci. U.S.A. , vol.89 , pp. 6909-6910
    • Fuchs, E.1    Esteves, R.A.2    Coulombe, P.A.3
  • 95
    • 0028989340 scopus 로고
    • Cloning of a cDNA for lamina-associated polypeptide 2 (LAP2) and identification of regions that specify targeting to the nuclear envelope
    • K. Furukawa N. Pante U. Aebi L. Gerace Cloning of a cDNA for lamina-associated polypeptide 2 (LAP2) and identification of regions that specify targeting to the nuclear envelope EMBO J. 14 1995 1626 1636
    • (1995) EMBO J. , vol.14 , pp. 1626-1636
    • Furukawa, K.1    Pante, N.2    Aebi, U.3    Gerace, L.4
  • 96
    • 0018840795 scopus 로고
    • The synthesis and distribution of desmin and vimentin during myogenesis in vitro
    • D.L. Gard E. Lazarides The synthesis and distribution of desmin and vimentin during myogenesis in vitro Cell (Cambridge, Mass.) 19 1980 263 275
    • (1980) Cell (Cambridge, Mass.) , vol.19 , pp. 263-275
    • Gard, D.L.1    Lazarides, E.2
  • 97
    • 0019051614 scopus 로고
    • Association of microtubules and intermediate filaments in chicken gizzard cells as detected by double immunofluorescence
    • B. Geiger S.J. Singer Association of microtubules and intermediate filaments in chicken gizzard cells as detected by double immunofluorescence Proc. Natl. Acad. Sci. U.S.A. 77 1980 4769 4773
    • (1980) Proc. Natl. Acad. Sci. U.S.A. , vol.77 , pp. 4769-4773
    • Geiger, B.1    Singer, S.J.2
  • 98
    • 0023371437 scopus 로고
    • Lamin B constitutes an intermediate filament attachment site at the nuclear envelope
    • S.D. Georgatos G. Blobel Lamin B constitutes an intermediate filament attachment site at the nuclear envelope J. Cell Biol. 105 1987 117 125
    • (1987) J. Cell Biol. , vol.105 , pp. 117-125
    • Georgatos, S.D.1    Blobel, G.2
  • 99
    • 85012338162 scopus 로고
    • The binding of vimentin to human erythrocyte membranes: A model system for the study of intermediate filament membrane interactions
    • S.D. Georgatos V.T. Marchesi The binding of vimentin to human erythrocyte membranes: A model system for the study of intermediate filament membrane interactions J. Cell Biol. 100 1985 1955 1961
    • (1985) J. Cell Biol. , vol.100 , pp. 1955-1961
    • Georgatos, S.D.1    Marchesi, V.T.2
  • 100
    • 0021811570 scopus 로고
    • Site-specificity in vimentin-membrane interactions: Intermediate filament subunits associate with the plasma membrane via their head domains
    • S.D. Georgatos D.C. Weaver V.T. Marchesi Site-specificity in vimentin-membrane interactions: Intermediate filament subunits associate with the plasma membrane via their head domains J. Cell Biol. 100 1985 1962 1967
    • (1985) J. Cell Biol. , vol.100 , pp. 1962-1967
    • Georgatos, S.D.1    Weaver, D.C.2    Marchesi, V.T.3
  • 101
    • 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
    • S.D. Georgatos K. Weber N. Geisler G. Blobel 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. U.S.A. 84 1987 6780 6784
    • (1987) Proc. Natl. Acad. Sci. U.S.A. , vol.84 , pp. 6780-6784
    • Georgatos, S.D.1    Weber, K.2    Geisler, N.3    Blobel, G.4
  • 102
    • 0028446532 scopus 로고
    • The beaded intermediate filaments and their potential functions in eye lens
    • S.D. Georgatos F. Gounari S. Remington The beaded intermediate filaments and their potential functions in eye lens BioEssays 16 1994 413 418
    • (1994) BioEssays , vol.16 , pp. 413-418
    • Georgatos, S.D.1    Gounari, F.2    Remington, S.3
  • 104
    • 0020659368 scopus 로고
    • The interaction between microtubules and intermediate filaments in cultured cells treated with taxol and nocodazole
    • G. Geuens M. DeBrabander R. Nuydens J. DeMey The interaction between microtubules and intermediate filaments in cultured cells treated with taxol and nocodazole Cell Biol. Int. Rep. 7 1983 35 47
    • (1983) Cell Biol. Int. Rep. , vol.7 , pp. 35-47
    • Geuens, G.1    DeBrabander, M.2    Nuydens, R.3    DeMey, J.4
  • 105
    • 0025107358 scopus 로고
    • Assembly properties of dominant and recessive mutations in the small mouse neurofilament (NF-L) subunit
    • S.R. Gill P.C. Wong M.J. Monteiro D.W. Cleveland Assembly properties of dominant and recessive mutations in the small mouse neurofilament (NF-L) subunit J. Cell Biol. 111 1990 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
  • 106
    • 0026033375 scopus 로고
    • Association of glycosphingolipids with intermediate filaments of human umbilical vein endothelial cells
    • B.K. Gillard J.P. Heath L.T. Thurmon D.M. Marcus Association of glycosphingolipids with intermediate filaments of human umbilical vein endothelial cells Exp. Cell Res. 192 1991 433 444
    • (1991) Exp. Cell Res. , vol.192 , pp. 433-444
    • Gillard, B.K.1    Heath, J.P.2    Thurmon, L.T.3    Marcus, D.M.4
  • 107
    • 0026689736 scopus 로고
    • Association of glycosphingolipids with intermediate filaments of mesenchymal, epithelial, glial, and muscle cells
    • B.K. Gillard L.T. Thurmon D.M. Marcus Association of glycosphingolipids with intermediate filaments of mesenchymal, epithelial, glial, and muscle cells Cell Motil. Cytoskel. 21 1992 255 271
    • (1992) Cell Motil. Cytoskel. , vol.21 , pp. 255-271
    • Gillard, B.K.1    Thurmon, L.T.2    Marcus, D.M.3
  • 108
    • 0025979365 scopus 로고
    • Identification of two collagen domains within bullous pemphigoid autoantigen, BP180
    • G.J. Giudice H.L. Squiquera P.M. Elias L. Diaz Identification of two collagen domains within bullous pemphigoid autoantigen, BP180 J. Clin. Invest. 87 1991 734 738
    • (1991) J. Clin. Invest. , vol.87 , pp. 734-738
    • Giudice, G.J.1    Squiquera, H.L.2    Elias, P.M.3    Diaz, L.4
  • 109
    • 0027442899 scopus 로고
    • The α-helical rod domain of human lamins A and C contains a chromatin binding site
    • C.A. Glass J.R. Glass H. Taniura K.W. Hasel J.M. Blevitt L. Gerace The α-helical rod domain of human lamins A and C contains a chromatin binding site EMBO J. 12 1993 4413 4424
    • (1993) EMBO J. , vol.12 , pp. 4413-4424
    • Glass, C.A.1    Glass, J.R.2    Taniura, H.3    Hasel, K.W.4    Blevitt, J.M.5    Gerace, L.6
  • 110
    • 0025005766 scopus 로고
    • Lamins A and C bind and assemble at the surface of mitotic chromsomes
    • J.R. Glass L. Gerace Lamins A and C bind and assemble at the surface of mitotic chromsomes J. Cell Biol. 111 1990 1047 1057
    • (1990) J. Cell Biol. , vol.111 , pp. 1047-1057
    • Glass, J.R.1    Gerace, L.2
  • 111
    • 0019996450 scopus 로고
    • The intracellular localization of the microvillus 110 K protein, a component considered to be involved in side-on membrane attachment of F-actin
    • J.R. Glenney M. Osborn K. Weber The intracellular localization of the microvillus 110 K protein, a component considered to be involved in side-on membrane attachment of F-actin Exp. Cell Res. 138 1982 199 205
    • (1982) Exp. Cell Res. , vol.138 , pp. 199-205
    • Glenney, J.R.1    Osborn, M.2    Weber, K.3
  • 112
    • 0015181351 scopus 로고
    • The role of three cytoplasmic fibers in BHK-21 cell motility
    • R.D. Goldman The role of three cytoplasmic fibers in BHK-21 cell motility J. Cell Biol. 51 1971 752 769
    • (1971) J. Cell Biol. , vol.51 , pp. 752-769
    • Goldman, R.D.1
  • 113
    • 0010819007 scopus 로고
    • Intermediate filament-microtubule interactions: Evidence in support of a common organization center
    • R.D. Goldman B.F. Hill P. Steinert M.A. Whitman R.V. Zackroff Intermediate filament-microtubule interactions: Evidence in support of a common organization center M. de Brabander J. De Mey “Microtubules and Microtubule Inhibitors” 1980 Elsevier/North-Holland Amsterdam 91 102
    • (1980) , pp. 91-102
    • Goldman, R.D.1    Hill, B.F.2    Steinert, P.3    Whitman, M.A.4    Zackroff, R.V.5
  • 114
    • 0022272935 scopus 로고
    • Intermediate filaments: Possible functions as cytoskeletal connecting links between the nucleus and the cell surface
    • R.D. Goldman A. Goldman K. Green J. Jones N. Lieska H.-Y. Yang Intermediate filaments: Possible functions as cytoskeletal connecting links between the nucleus and the cell surface Ann. N. Y. Acad. Sci. 455 1985 1 17
    • (1985) Ann. N. Y. Acad. Sci. , vol.455 , pp. 1-17
    • Goldman, R.D.1    Goldman, A.2    Green, K.3    Jones, J.4    Lieska, N.5    Yang, H.-Y.6
  • 116
    • 0018221368 scopus 로고
    • The existence of an insoluble Z disc scaffold in chicken skeletal muscle
    • B.L. Granger E. Lazarides The existence of an insoluble Z disc scaffold in chicken skeletal muscle Cell (Cambridge, Mass.) 15 1978 1253 1268
    • (1978) Cell (Cambridge, Mass.) , vol.15 , pp. 1253-1268
    • Granger, B.L.1    Lazarides, E.2
  • 117
    • 0018571673 scopus 로고
    • Desmin and vimentin coexist at the periphery of the myofibril Z disc
    • B.L. Granger E. Lazarides Desmin and vimentin coexist at the periphery of the myofibril Z disc Cell (Cambridge, Mass.) 18 1979 1053 1063
    • (1979) Cell (Cambridge, Mass.) , vol.18 , pp. 1053-1063
    • Granger, B.L.1    Lazarides, E.2
  • 118
    • 0020096836 scopus 로고
    • Synemin and vimentin are components of intermediate filaments in avian erythrocytes
    • B.L. Granger E.A. Repasky E. Lazarides Synemin and vimentin are components of intermediate filaments in avian erythrocytes J. Cell Biol. 92 1982 299 312
    • (1982) J. Cell Biol. , vol.92 , pp. 299-312
    • Granger, B.L.1    Repasky, E.A.2    Lazarides, E.3
  • 119
    • 0023990634 scopus 로고
    • Isolation of cDNAs encoding desmosomal plaque proteins: Evidence that bovine desmoplakins I and II are derived from two mRNAs and a single gene
    • K.J. Green R.D. Goldman R.L. Chisholm Isolation of cDNAs encoding desmosomal plaque proteins: Evidence that bovine desmoplakins I and II are derived from two mRNAs and a single gene Proc. Natl. Acad. Sci. U.S.A. 85 1988 2613 2617
    • (1988) Proc. Natl. Acad. Sci. U.S.A. , vol.85 , pp. 2613-2617
    • Green, K.J.1    Goldman, R.D.2    Chisholm, R.L.3
  • 121
    • 0028286596 scopus 로고
    • A serine kinase regulates intracellular localization of splicing factors in the cell cycle
    • J.F. Gui W.S. Lane X.D. Fu A serine kinase regulates intracellular localization of splicing factors in the cell cycle Nature (London) 23 1994 678 682
    • (1994) Nature (London) , vol.23 , pp. 678-682
    • Gui, J.F.1    Lane, W.S.2    Fu, X.D.3
  • 122
    • 0029066406 scopus 로고
    • Gene targeting of BPAG1: Abnormalities in mechanical strength and cell migration in stratified epithelia and neurologic degeneration
    • L. Guo L. Degenstein J. Dowling Q.C. Yu R. Wollmann B. Perman E. Fuchs Gene targeting of BPAG1: Abnormalities in mechanical strength and cell migration in stratified epithelia and neurologic degeneration Cell (Cambridge, Mass.) 81 1995 233 243
    • (1995) Cell (Cambridge, Mass.) , 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
  • 123
    • 0025743437 scopus 로고
    • Coalignment of vimentin intermediate filaments with microtubules depends on kinesin
    • F.K. Gyoeva V.I. Gelfand Coalignment of vimentin intermediate filaments with microtubules depends on kinesin Nature (London) 353 1991 445 448
    • (1991) Nature (London) , vol.353 , pp. 445-448
    • Gyoeva, F.K.1    Gelfand, V.I.2
  • 124
    • 0015092352 scopus 로고
    • Fractionation of the avian erythrocyte: An ultrastructural study
    • J.R. Harris J.N. Brown Fractionation of the avian erythrocyte: An ultrastructural study J. Ultrastruct. Res. 36 1971 8 23
    • (1971) J. Ultrastruct. Res. , vol.36 , pp. 8-23
    • Harris, J.R.1    Brown, J.N.2
  • 125
    • 0025882273 scopus 로고
    • Modulation of keratin intermediate filament assembly by single amino acid exchanges in the consensus sequence at the C-terminal end of the rod domain
    • M. Hatzfeld K. Weber Modulation of keratin intermediate filament assembly by single amino acid exchanges in the consensus sequence at the C-terminal end of the rod domain J. Cell Sci. 99 1991 351 362
    • (1991) J. Cell Sci. , vol.99 , pp. 351-362
    • Hatzfeld, M.1    Weber, K.2
  • 126
    • 0025959176 scopus 로고
    • Chromatin motion in neuronal interphase nuclei: Changes induced by disruption of intermediate filaments
    • M. Hay U. De Boni Chromatin motion in neuronal interphase nuclei: Changes induced by disruption of intermediate filaments Cell Motil. Cytoskel. 18 1991 63 75
    • (1991) Cell Motil. Cytoskel. , vol.18 , pp. 63-75
    • Hay, M.1    De Boni, U.2
  • 128
    • 0024437488 scopus 로고
    • A new high molecular mass protein showing unique localization in desmosomal plaque
    • Y. Heida S. Tsukita S. Tsukita A new high molecular mass protein showing unique localization in desmosomal plaque J. Cell Biol. 109 1989 1511 1518
    • (1989) J. Cell Biol. , vol.109 , pp. 1511-1518
    • Heida, Y.1    Tsukita, S.2    Tsukita, S.3
  • 129
    • 4644343677 scopus 로고
    • Specific binding of MAPs to the 68,000 dalton neurofilament protein
    • R. Heinmann M.L. Shelanski R.K.H. Liem Specific binding of MAPs to the 68,000 dalton neurofilament protein J. Cell Biol. 97 5, Pt.2 1983 286a
    • (1983) J. Cell Biol. , vol.97 , Issue.5, Pt.2 , pp. 286a
    • Heinmann, R.1    Shelanski, M.L.2    Liem, R.K.H.3
  • 130
    • 0027463042 scopus 로고
    • cDNA analysis of the 49 kDa lens fiber cell cytoskeletal protein: A new lens specific member of the intermediate filament family?
    • J.F. Hess J.T. Casselman P.G. FitzGerald cDNA analysis of the 49 kDa lens fiber cell cytoskeletal protein: A new lens specific member of the intermediate filament family? Curr. Eye Res. 12 1993 77 88
    • (1993) Curr. Eye Res. , vol.12 , pp. 77-88
    • Hess, J.F.1    Casselman, J.T.2    FitzGerald, P.G.3
  • 131
    • 0026577999 scopus 로고
    • Identification of a new major hemidesmosomal protein, HD1: A major, high molecular mass component of isolated hemidesmosomes
    • Y. Hieda Y. Nishizawa J. Uematsu K. Owaribe Identification of a new major hemidesmosomal protein, HD1: A major, high molecular mass component of isolated hemidesmosomes J. Cell Biol. 116 1992 1497 1506
    • (1992) J. Cell Biol. , vol.116 , pp. 1497-1506
    • Hieda, Y.1    Nishizawa, Y.2    Uematsu, J.3    Owaribe, K.4
  • 132
    • 0019975040 scopus 로고
    • The organization of actin, myosin, and intermediate filaments in the brush border of intestinal epithelial cells
    • N. Hirokawa L.B. Tilney K. Fujiwara J.E. Heuser The organization of actin, myosin, and intermediate filaments in the brush border of intestinal epithelial cells J. Cell Biol. 94 1982 425 443
    • (1982) J. Cell Biol. , vol.94 , pp. 425-443
    • Hirokawa, N.1    Tilney, L.B.2    Fujiwara, K.3    Heuser, J.E.4
  • 133
    • 0020728714 scopus 로고
    • Location of a protein of the fodrinspectrin-TW260/240 family in the mouse intestinal brush border
    • N. Hirokawa R.E. Cheney M. Willard Location of a protein of the fodrinspectrin-TW260/240 family in the mouse intestinal brush border Cell (Cambridge, Mass.) 32 1983 953 965
    • (1983) Cell (Cambridge, Mass.) , vol.32 , pp. 953-965
    • Hirokawa, N.1    Cheney, R.E.2    Willard, M.3
  • 134
    • 0024817731 scopus 로고
    • The CaaX motif of lamin A functions in conjunction with the nuclear localization signal to target assembly to the nuclear envelope
    • D. Holtz R.A. Tanaka J. Hartwig F. McKeon The CaaX motif of lamin A functions in conjunction with the nuclear localization signal to target assembly to the nuclear envelope Cell (Cambridge, Mass.). 59 1989 969 977
    • (1989) Cell (Cambridge, Mass.). , vol.59 , pp. 969-977
    • Holtz, D.1    Tanaka, R.A.2    Hartwig, J.3    McKeon, F.4
  • 136
    • 0026730506 scopus 로고
    • Cytoplasmic domain of the 180-kD bullous pemphigoid antigen, a hemidesmosomal component: Molecular and cell biologic characterization
    • S.B. Hopkinson K.S. Ridelle J.C.R. Jones Cytoplasmic domain of the 180-kD bullous pemphigoid antigen, a hemidesmosomal component: Molecular and cell biologic characterization J. Invest. Dermatol. 99 1992 264 270
    • (1992) J. Invest. Dermatol. , vol.99 , pp. 264-270
    • Hopkinson, S.B.1    Ridelle, K.S.2    Jones, J.C.R.3
  • 137
    • 0018411023 scopus 로고
    • The terminal web: A reevaluation of its structure and function
    • B.E. Hull L.A. Staehelin The terminal web: A reevaluation of its structure and function J. Cell Biol. 81 1979 67 82
    • (1979) J. Cell Biol. , vol.81 , pp. 67-82
    • Hull, B.E.1    Staehelin, L.A.2
  • 138
    • 0014335827 scopus 로고
    • Mitosis and intermediate-sized filaments in developing skeletal muscle
    • H. Ishikawa R. Bischoff H. Holtzer Mitosis and intermediate-sized filaments in developing skeletal muscle J. Cell Biol. 38 1968 538 555
    • (1968) J. Cell Biol. , vol.38 , pp. 538-555
    • Ishikawa, H.1    Bischoff, R.2    Holtzer, H.3
  • 139
    • 0025765110 scopus 로고
    • Viscoelastic properties of vimentin compared with other filamentous biopolymer networks
    • P.A. Janmey U. Euteneuer P. Traub M. Schliwa Viscoelastic properties of vimentin compared with other filamentous biopolymer networks J. Cell Biol. 113 1991 155 160
    • (1991) J. Cell Biol. , vol.113 , pp. 155-160
    • Janmey, P.A.1    Euteneuer, U.2    Traub, P.3    Schliwa, M.4
  • 140
    • 0026323478 scopus 로고
    • Toward a more complete 3-D structure of the nuclear pore complex
    • M. Jarnik U. Aebi Toward a more complete 3-D structure of the nuclear pore complex J. Struct. Biol. 107 1991 291 308
    • (1991) J. Struct. Biol. , vol.107 , pp. 291-308
    • Jarnik, M.1    Aebi, U.2
  • 141
    • 0023906026 scopus 로고
    • Characterization of a 125K glycoprotein associated with bovine epithelial desmosomes
    • J.C.R. Jones Characterization of a 125K glycoprotein associated with bovine epithelial desmosomes J. Cell Sci. 89 1988 207 216
    • (1988) J. Cell Sci. , vol.89 , pp. 207-216
    • Jones, J.C.R.1
  • 142
    • 0020451332 scopus 로고
    • The dynamic aspects of the supramolecular organization of the intermediate filament networks in cultured epidermal cells
    • J.C.R. Jones E. Goldman P.M. Steinert S. Yuspa R.D. Goldman The dynamic aspects of the supramolecular organization of the intermediate filament networks in cultured epidermal cells Cell Motil. Cytoskel. 2 1982 197 213
    • (1982) Cell Motil. Cytoskel. , vol.2 , pp. 197-213
    • Jones, J.C.R.1    Goldman, E.2    Steinert, P.M.3    Yuspa, S.4    Goldman, R.D.5
  • 143
    • 0022916479 scopus 로고
    • Is the hemidesmosome a half desmosome? An immunologocal comparison of mammalian desmosomes and hemidesmosomes
    • J.C.R. Jones K.M. Yokoo R.D. Goldman Is the hemidesmosome a half desmosome? An immunologocal comparison of mammalian desmosomes and hemidesmosomes Cell Motil. Cytoskel. 6 1986 560 569
    • (1986) Cell Motil. Cytoskel. , vol.6 , pp. 560-569
    • Jones, J.C.R.1    Yokoo, K.M.2    Goldman, R.D.3
  • 145
    • 0023917828 scopus 로고
    • Identification of a basic protein of Mr 75,000 as an accessory desmosomal plaque protein in stratified and complex epithelia
    • H.-P. Kapprell K. Owaribe W.W. Franke Identification of a basic protein of Mr 75,000 as an accessory desmosomal plaque protein in stratified and complex epithelia J. Cell Biol. 106 1988 1679 1691
    • (1988) J. Cell Biol. , vol.106 , pp. 1679-1691
    • Kapprell, H.-P.1    Owaribe, K.2    Franke, W.W.3
  • 146
    • 0002689748 scopus 로고
    • Subplasmalemmal plaques of intercellular junctions: Common and distinguishing proteins
    • H.-P. Kapprell R. Duden K. Owaribe M. Schmelz W.W. Franke Subplasmalemmal plaques of intercellular junctions: Common and distinguishing proteins G.M. Edelman B.A. Cuningham J.P. Thiery “Morphoregulatory Molecules” 1990 Wiley New York 285 314
    • (1990) , pp. 285-314
    • Kapprell, H.-P.1    Duden, R.2    Owaribe, K.3    Schmelz, M.4    Franke, W.W.5
  • 147
    • 0021004748 scopus 로고
    • Specific attachment of desmin filaments to desmosomal plaques in cardiac myocytes
    • J. Kartenbeck W.W. Franke J.G. Moser U. Stoffels Specific attachment of desmin filaments to desmosomal plaques in cardiac myocytes EMBO J. 2 1983 735 742
    • (1983) EMBO J. , vol.2 , pp. 735-742
    • Kartenbeck, J.1    Franke, W.W.2    Moser, J.G.3    Stoffels, U.4
  • 148
    • 0021331372 scopus 로고
    • Attachment of vimentin filaments to desmosomal plaques in human meningioma cells and arachnoidal tissue
    • J. Kartenbeck K. Schwechheimer R. Moll W.W. Franke Attachment of vimentin filaments to desmosomal plaques in human meningioma cells and arachnoidal tissue J. Cell Biol. 98 1984 1072 1081
    • (1984) J. Cell Biol. , vol.98 , pp. 1072-1081
    • Kartenbeck, J.1    Schwechheimer, K.2    Moll, R.3    Franke, W.W.4
  • 149
    • 0023075406 scopus 로고
    • Connections of intermediate filaments with the nuclear lamina and the cell periphery
    • Y. Katsuma S.H.H. Swierenga M. Marceau S.W. French Connections of intermediate filaments with the nuclear lamina and the cell periphery Biol. Cell. 59 1987 193 204
    • (1987) Biol. Cell. , vol.59 , pp. 193-204
    • Katsuma, Y.1    Swierenga, S.H.H.2    Marceau, M.3    French, S.W.4
  • 150
    • 0013865428 scopus 로고
    • Fine structure of desmosomes, hemidesmosomes, and an adepidermal globular layer in developing newt epidermis
    • D.E. Kelly Fine structure of desmosomes, hemidesmosomes, and an adepidermal globular layer in developing newt epidermis J. Cell Biol. 28 1966 51 72
    • (1966) J. Cell Biol. , vol.28 , pp. 51-72
    • Kelly, D.E.1
  • 151
    • 0025845750 scopus 로고
    • The CaaX motif is required for isoprenylation, carboxyl methylation and nuclear membrane association of lamin B2
    • G.T. Kitten E.A. Nigg The CaaX motif is required for isoprenylation, carboxyl methylation and nuclear membrane association of lamin B2 J. Cell Biol. 113 1991 13 23
    • (1991) J. Cell Biol. , vol.113 , pp. 13-23
    • Kitten, G.T.1    Nigg, E.A.2
  • 152
    • 0024814987 scopus 로고
    • Immunochemical characterization of three components of the hemidesmosome and their expression in cultured epithelial cells
    • D.H. Klatte M.A. Kurpakus K.A. Grelling J.C.R. Jones Immunochemical characterization of three components of the hemidesmosome and their expression in cultured epithelial cells J Cell Biol. 109 1989 3377 3390
    • (1989) J Cell Biol. , vol.109 , pp. 3377-3390
    • Klatte, D.H.1    Kurpakus, M.A.2    Grelling, K.A.3    Jones, J.C.R.4
  • 153
    • 0019885815 scopus 로고
    • Intermediate filaments in 3T3 cells collapses after intracellular injection of a monoclonal anti-intermediate filament antibody
    • M.W. Klymkowsky Intermediate filaments in 3T3 cells collapses after intracellular injection of a monoclonal anti-intermediate filament antibody Nature (London) 291 1981 249 251
    • (1981) Nature (London) , vol.291 , pp. 249-251
    • Klymkowsky, M.W.1
  • 154
    • 0028967465 scopus 로고
    • Intermediate filaments: New proteins, some answers, more questions
    • M.W. Klymkowsky Intermediate filaments: New proteins, some answers, more questions Curr. Opin. Cell Biol. 7 1995 46 54
    • (1995) Curr. Opin. Cell Biol. , vol.7 , pp. 46-54
    • Klymkowsky, M.W.1
  • 155
    • 0026687386 scopus 로고
    • Plakoglobin, or an 83-kD homologue distinct from b-catenin, interacts with E-cadherin and N-cadherin
    • K.A. Knudsen M.J. Wheelock Plakoglobin, or an 83-kD homologue distinct from b-catenin, interacts with E-cadherin and N-cadherin J. Cell Biol. 118 1992 671 679
    • (1992) J. Cell Biol. , vol.118 , pp. 671-679
    • Knudsen, K.A.1    Wheelock, M.J.2
  • 156
    • 0025081307 scopus 로고
    • Identification of desmoglein, a constitutive desmosomal glycoprotein, as a member of the cadherin family of cell adhesion molecules
    • P.J. Koch M.J. Walsh M. Schmelz M.D. Goldschmidt R. Zimbelmann W.W. Franke Identification of desmoglein, a constitutive desmosomal glycoprotein, as a member of the cadherin family of cell adhesion molecules Eur. J. Cell Biol. 53 1990 1 12
    • (1990) Eur. J. Cell Biol. , vol.53 , pp. 1-12
    • Koch, P.J.1    Walsh, M.J.2    Schmelz, M.3    Goldschmidt, M.D.4    Zimbelmann, R.5    Franke, W.W.6
  • 158
    • 0026723964 scopus 로고
    • Involvement of the consensus sequence motif at coil 2b in the assembly and stability of vimentin filaments
    • P.D. Kouklis P. Traub S.D. Georgatos Involvement of the consensus sequence motif at coil 2b in the assembly and stability of vimentin filaments J. Cell Sci. 102 1992 31 41
    • (1992) J. Cell Sci. , vol.102 , pp. 31-41
    • Kouklis, P.D.1    Traub, P.2    Georgatos, S.D.3
  • 159
    • 0027715992 scopus 로고
    • Transient arrest of 3T3 cells in mitosis and inhibition of nuclear lamin reassembly around chromatin induced by anti-vimentin antibodies
    • P.D. Kouklis A. Merdes T. Papamarcaki S.D. Georgatos Transient arrest of 3T3 cells in mitosis and inhibition of nuclear lamin reassembly around chromatin induced by anti-vimentin antibodies Eur. J. Cell Biol. 62 1993 224 236
    • (1993) Eur. J. Cell Biol. , vol.62 , pp. 224-236
    • Kouklis, P.D.1    Merdes, A.2    Papamarcaki, T.3    Georgatos, S.D.4
  • 160
    • 0027987929 scopus 로고
    • Making a connection: Direct binding between keratin intermediate filaments and desmosomal proteins
    • P.D. Kouklis E. Hutton E. Fuchs Making a connection: Direct binding between keratin intermediate filaments and desmosomal proteins J. Cell Biol. 127 1994 1049 1060
    • (1994) J. Cell Biol. , vol.127 , pp. 1049-1060
    • Kouklis, P.D.1    Hutton, E.2    Fuchs, E.3
  • 161
    • 0025743575 scopus 로고
    • Functional expression of cloned human splicing factor SF2: Homology to RNA-binding proteins, U1 70K, and Drosophila splicing regulators
    • A.R. Krainer A. Mayeda D. Kozak G. Binns Functional expression of cloned human splicing factor SF2: Homology to RNA-binding proteins, U1 70K, and Drosophila splicing regulators Cell (Cambridge, Mass.) 66 1991 383 394
    • (1991) Cell (Cambridge, Mass.) , vol.66 , pp. 383-394
    • Krainer, A.R.1    Mayeda, A.2    Kozak, D.3    Binns, G.4
  • 162
    • 0020964827 scopus 로고
    • De novo synthesis and specific assembly of keratin filaments, in nonepithelial cells after microinjection of mRNA for epidermal keratin
    • T.E. Kreis B. Geiger E. Schmid J.L. Jorcano W.W. Franke De novo synthesis and specific assembly of keratin filaments, in nonepithelial cells after microinjection of mRNA for epidermal keratin Cell (Cambridge, Mass.) 32 1983 1125 1137
    • (1983) Cell (Cambridge, Mass.) , vol.32 , pp. 1125-1137
    • Kreis, T.E.1    Geiger, B.2    Schmid, E.3    Jorcano, J.L.4    Franke, W.W.5
  • 163
    • 0024444733 scopus 로고
    • The conserved carboxy-terminal cysteine of nuclear lamins is essential for lamin association with the nuclear envelope
    • G. Krohne I. Waizenegger T.H. Höger The conserved carboxy-terminal cysteine of nuclear lamins is essential for lamin association with the nuclear envelope J. Cell Biol. 109 1989 2003 2013
    • (1989) J. Cell Biol. , vol.109 , pp. 2003-2013
    • Krohne, G.1    Waizenegger, I.2    Höger, T.H.3
  • 164
    • 0023251448 scopus 로고
    • Interaction in vitro of non-epithelial intermediate filament proteins with supercoiled plasmid DNA
    • S. Kühn C.E. Vorgias P. Traub Interaction in vitro of non-epithelial intermediate filament proteins with supercoiled plasmid DNA J. Cell Sci. 87 1987 543 554
    • (1987) J. Cell Sci. , vol.87 , pp. 543-554
    • Kühn, S.1    Vorgias, C.E.2    Traub, P.3
  • 165
    • 0026166472 scopus 로고
    • A novel hemidesmosomal plaque component: Tissue distribution and incorporation into assembling hemidesmosomes in an in vitro model
    • M.A. Kurpakus J.C.R. Jones A novel hemidesmosomal plaque component: Tissue distribution and incorporation into assembling hemidesmosomes in an in vitro model Exp. Cell Res. 194 1991 139 146
    • (1991) Exp. Cell Res. , vol.194 , pp. 139-146
    • Kurpakus, M.A.1    Jones, J.C.R.2
  • 166
    • 0022596012 scopus 로고
    • Associations of spectrin with desmin intermediate filaments
    • R.C. Langley Jr. C.M. Cohen Associations of spectrin with desmin intermediate filaments J. Cell. Biochem. 30 1986 101 109
    • (1986) J. Cell. Biochem. , vol.30 , pp. 101-109
    • Langley, R.C.1    Cohen, C.M.2
  • 167
    • 0023497802 scopus 로고
    • Cell type-specific association between two types of spectrin and two types of intermediate filaments
    • R.C. Langley Jr. C.M. Cohen Cell type-specific association between two types of spectrin and two types of intermediate filaments Cell Motil. Cytoskel. 8 1987 165 173
    • (1987) Cell Motil. Cytoskel. , vol.8 , pp. 165-173
    • Langley, R.C.1    Cohen, C.M.2
  • 168
    • 0018842868 scopus 로고
    • Intermediate filaments as mechanical integrators of cellular space
    • E. Lazarides Intermediate filaments as mechanical integrators of cellular space Nature (London) 283 1980 249 256
    • (1980) Nature (London) , vol.283 , pp. 249-256
    • Lazarides, E.1
  • 169
    • 0011511766 scopus 로고
    • Fluorescent localization of membrane sites in glycerinated chicken skeletal muscle fibers and the relationship of these sites to the protein composition of the Z-discs
    • E. Lazarides B.L. Granger Fluorescent localization of membrane sites in glycerinated chicken skeletal muscle fibers and the relationship of these sites to the protein composition of the Z-discs Proc. Natl. Acad. Sci. U.S.A. 75 1978 3683 3687
    • (1978) Proc. Natl. Acad. Sci. U.S.A. , vol.75 , pp. 3683-3687
    • Lazarides, E.1    Granger, B.L.2
  • 170
    • 0002084716 scopus 로고
    • Transcytoplasmic integration in avian erythrocytes and striated muscle; the role of intermediate filaments
    • E. Lazarides B.L. Granger Transcytoplasmic integration in avian erythrocytes and striated muscle; the role of intermediate filaments Mod. Cell Biol. 2 1983 143 162
    • (1983) Mod. Cell Biol. , vol.2 , pp. 143-162
    • Lazarides, E.1    Granger, B.L.2
  • 171
    • 0011497688 scopus 로고
    • Immunological characterization of the subunit of the 100 A filaments from muscle cells
    • E. Lazarides B.D. Hubbard Immunological characterization of the subunit of the 100 A filaments from muscle cells Proc. Natl. Acad. Sci. U.S.A. 73 1976 4344 4348
    • (1976) Proc. Natl. Acad. Sci. U.S.A. , vol.73 , pp. 4344-4348
    • Lazarides, E.1    Hubbard, B.D.2
  • 172
    • 0018651446 scopus 로고
    • Mitochondria and mitochondria-tonofilament-desmosomal association in the mammary gland secretory epithelium of lactating cows
    • C.S. Lee G. Morgan F.B.P. Wooding Mitochondria and mitochondria-tonofilament-desmosomal association in the mammary gland secretory epithelium of lactating cows J. Cell Sci. 38 1979 125 135
    • (1979) J. Cell Sci. , vol.38 , pp. 125-135
    • Lee, C.S.1    Morgan, G.2    Wooding, F.B.P.3
  • 173
    • 0017883543 scopus 로고
    • Intermediate filaments anchor the nuclei in nuclear monolayers of cultured human fibroblasts
    • V.P. Lehto I. Virtanen P. Kurki Intermediate filaments anchor the nuclei in nuclear monolayers of cultured human fibroblasts Nature (London) 272 1978 175 177
    • (1978) Nature (London) , vol.272 , pp. 175-177
    • Lehto, V.P.1    Virtanen, I.2    Kurki, P.3
  • 174
    • 0028963211 scopus 로고
    • The importance of intramolecular ion pairing in intermediate filaments
    • A. Letai E. Fuchs The importance of intramolecular ion pairing in intermediate filaments Proc. Natl. Acad. Sci. U.S.A. 92 1995 92 96
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 92-96
    • Letai, A.1    Fuchs, E.2
  • 175
    • 0019815675 scopus 로고
    • Fodrin: Axonally transported polypeptides associated with the internal periphery of many cells
    • J. Levine M. Willard Fodrin: Axonally transported polypeptides associated with the internal periphery of many cells J. Cell Biol. 90 1981 631 643
    • (1981) J. Cell Biol. , vol.90 , pp. 631-643
    • Levine, J.1    Willard, M.2
  • 176
    • 0028197466 scopus 로고
    • Inhibition of desmin expression blocks myoblast fusion and interferes with myogenic regulators myoD and myogenin
    • H. Li S.K. Choudhary D.J. Milner M.I. Munir I.R. Kuisk Y. Capetanaki Inhibition of desmin expression blocks myoblast fusion and interferes with myogenic regulators myoD and myogenin J. Cell Biol. 124 1994 827 841
    • (1994) J. Cell Biol. , vol.124 , pp. 827-841
    • Li, H.1    Choudhary, S.K.2    Milner, D.J.3    Munir, M.I.4    Kuisk, I.R.5    Capetanaki, Y.6
  • 177
    • 85113065978 scopus 로고
    • C. elegans spectrin/fodrin-like clone free to a good home
    • C. Loer C. elegans spectrin/fodrin-like clone free to a good home Worm Breeder's Gaz. 12 1992 54
    • (1992) Worm Breeder's Gaz. , vol.12 , pp. 54
    • Loer, C.1
  • 178
    • 0013954216 scopus 로고
    • The association of lipid droplets with cytoplasmic filaments in avian subsynovial adipose cells
    • L.M. Luckenbill A.S. Cohen The association of lipid droplets with cytoplasmic filaments in avian subsynovial adipose cells J. Cell Biol. 31 1966 195 199
    • (1966) J. Cell Biol. , vol.31 , pp. 195-199
    • Luckenbill, L.M.1    Cohen, A.S.2
  • 180
    • 0002063301 scopus 로고
    • The morphology of the lens
    • H. Maisel C.V. Harding J.R. Alcala J. Kuszak R. Bradley The morphology of the lens H. Bloemendal “Molecular and Cellular Biology of the Eye Lens” 1981 Wiley New-York 49 84
    • (1981) , pp. 49-84
    • Maisel, H.1    Harding, C.V.2    Alcala, J.R.3    Kuszak, J.4    Bradley, R.5
  • 181
    • 0027715286 scopus 로고
    • Regulated docking of nuclear membrane vesicles to vimentin filaments during mitosis
    • C. Maison H. Horstmann S.D. Georgatos Regulated docking of nuclear membrane vesicles to vimentin filaments during mitosis J. Cell Biol. 123 1993 1491 1505
    • (1993) J. Cell Biol. , vol.123 , pp. 1491-1505
    • Maison, C.1    Horstmann, H.2    Georgatos, S.D.3
  • 182
    • 0029031611 scopus 로고
    • Vimentin-associated mitotic vesicles interact with chromosomes in a lamin B and phosphorylation-dependent manner
    • C. Maison A. Pyrpasopoulou S.D. Georgatos Vimentin-associated mitotic vesicles interact with chromosomes in a lamin B and phosphorylation-dependent manner EMBO J. 14 1995 3311 3324
    • (1995) EMBO J. , vol.14 , pp. 3311-3324
    • Maison, C.1    Pyrpasopoulou, A.2    Georgatos, S.D.3
  • 183
    • 0021187624 scopus 로고
    • Immunoprecipitation of nonerythrocyte spectrin within live cells following microinjection of specific antibodies: Relation to cytoskeletal structures
    • P.H. Mangeat K. Burridge Immunoprecipitation of nonerythrocyte spectrin within live cells following microinjection of specific antibodies: Relation to cytoskeletal structures J. Cell Biol. 98 1984 1363 1377
    • (1984) J. Cell Biol. , vol.98 , pp. 1363-1377
    • Mangeat, P.H.1    Burridge, K.2
  • 184
    • 0020058373 scopus 로고
    • Reorganization of HeLa cell cytoskeleton induced by an uncoupler of oxidative phosphorylation
    • B. Maro M. Bornens Reorganization of HeLa cell cytoskeleton induced by an uncoupler of oxidative phosphorylation Nature (London) 295 1982 334 336
    • (1982) Nature (London) , vol.295 , pp. 334-336
    • Maro, B.1    Bornens, M.2
  • 185
    • 0020408608 scopus 로고
    • Taxol induced redistribution of vimentin filaments in HeLa cells
    • B. Maro M.-E. Sauron D. Paulin M. Bornens Taxol induced redistribution of vimentin filaments in HeLa cells Biol. Cell. 45 1982 204
    • (1982) Biol. Cell. , vol.45 , pp. 204
    • Maro, B.1    Sauron, M.-E.2    Paulin, D.3    Bornens, M.4
  • 187
    • 0028949732 scopus 로고
    • cDNA cloning and characterization of lamina-associated polypeptide 1C (LAP1C), and integral protein of the inner nuclear-membrane
    • L. Martin C. Crimaudo L. Gerace cDNA cloning and characterization of lamina-associated polypeptide 1C (LAP1C), and integral protein of the inner nuclear-membrane J. Biol. Chem. 270 1995 8822 8828
    • (1995) J. Biol. Chem. , vol.270 , pp. 8822-8828
    • Martin, L.1    Crimaudo, C.2    Gerace, L.3
  • 188
    • 0026546662 scopus 로고
    • Transient storage of a nuclear matrix protein along intermediate-type filaments during mitosis: A novel function of cytoplasmic intermediate filaments
    • R.A. Marugg Transient storage of a nuclear matrix protein along intermediate-type filaments during mitosis: A novel function of cytoplasmic intermediate filaments J. Struct. Biol. 108 1992 129 139
    • (1992) J. Struct. Biol. , vol.108 , pp. 129-139
    • Marugg, R.A.1
  • 189
    • 0026706184 scopus 로고
    • cDNA sequence analysis of CP94: Rat lens fiber cell beaded-filament structural protein shows homology to cytokeratins
    • S. Masaki T. Watanabe cDNA sequence analysis of CP94: Rat lens fiber cell beaded-filament structural protein shows homology to cytokeratins Biochem. Biophys. Res. Commun. 186 1992 190 198
    • (1992) Biochem. Biophys. Res. Commun. , vol.186 , pp. 190-198
    • Masaki, S.1    Watanabe, T.2
  • 190
    • 0028318203 scopus 로고
    • Interactions of the cytoplasmic domain of the desmosomal cadherin Dsg1 with plakoglobin
    • M. Mathur L. Goodwin P. Cowin Interactions of the cytoplasmic domain of the desmosomal cadherin Dsg1 with plakoglobin J. Biol. Chem. 269 1994 14075 14080
    • (1994) J. Biol. Chem. , vol.269 , pp. 14075-14080
    • Mathur, M.1    Goodwin, L.2    Cowin, P.3
  • 191
    • 0019731978 scopus 로고
    • Lavender, chick melanocyte mutant with defective melanosome translocation: A possible role for 10 nm filaments and microfilaments but not microtubules
    • P.L. Mayerson J.A. Brumbaugh Lavender, chick melanocyte mutant with defective melanosome translocation: A possible role for 10 nm filaments and microfilaments but not microtubules J. Cell Sci. 51 1981 25 51
    • (1981) J. Cell Sci. , vol.51 , pp. 25-51
    • Mayerson, P.L.1    Brumbaugh, J.A.2
  • 192
    • 0020508521 scopus 로고
    • Morphological characterization of the cholesteryl ester cycle in cultured mouse macrophage foam cells
    • D.J. McGookey R.G.W. Anderson Morphological characterization of the cholesteryl ester cycle in cultured mouse macrophage foam cells J. Cell Biol. 97 1983 1156 1168
    • (1983) J. Cell Biol. , vol.97 , pp. 1156-1168
    • McGookey, D.J.1    Anderson, R.G.W.2
  • 193
    • 0025910747 scopus 로고
    • Desmocollins form a distinct subset of the cadherin family of cell adhesion molecules
    • S. Mechanic K. Raynor J.E. Hill P. Cowin Desmocollins form a distinct subset of the cadherin family of cell adhesion molecules Proc. Natl. Acad. Sci. U.S.A. 88 1991 4476 4480
    • (1991) Proc. Natl. Acad. Sci. U.S.A. , vol.88 , pp. 4476-4480
    • Mechanic, S.1    Raynor, K.2    Hill, J.E.3    Cowin, P.4
  • 194
    • 0028204109 scopus 로고
    • Type B lamins remain associated with the integral nuclear envelope protein p58 during mitosis: Implications for nuclear reassembly
    • J. Meier S.D. Georgatos Type B lamins remain associated with the integral nuclear envelope protein p58 during mitosis: Implications for nuclear reassembly EMBO J. 13 1994 1888 1898
    • (1994) EMBO J. , vol.13 , pp. 1888-1898
    • Meier, J.1    Georgatos, S.D.2
  • 195
    • 0026046947 scopus 로고
    • Filensin: A new vimentin-binding, polymerization-competent, and membrane-associated protein of the lens fiber cell
    • A. Merdes M. Brunkener H. Horstmann S.D. Georgatos Filensin: A new vimentin-binding, polymerization-competent, and membrane-associated protein of the lens fiber cell J. Cell Biol. 115 1991 397 410
    • (1991) J. Cell Biol. , vol.115 , pp. 397-410
    • Merdes, A.1    Brunkener, M.2    Horstmann, H.3    Georgatos, S.D.4
  • 196
    • 0027722988 scopus 로고
    • The 47-kD lens-specific protein phakinin is a tailless intermediate filament protein and an assembly partner of filensin
    • A. Merdes F. Gounari S.D. Georgatos The 47-kD lens-specific protein phakinin is a tailless intermediate filament protein and an assembly partner of filensin J. Cell Biol. 23 1993 1507 1516
    • (1993) J. Cell Biol. , vol.23 , pp. 1507-1516
    • Merdes, A.1    Gounari, F.2    Georgatos, S.D.3
  • 197
    • 0020469904 scopus 로고
    • Putative association of mitochondria with a subpopulation of intermediate-sized filaments in cultured human skin fibroblasts
    • P. Mose-Larsen R. Bravo S.J. Fey J.V. Small J.E. Celis Putative association of mitochondria with a subpopulation of intermediate-sized filaments in cultured human skin fibroblasts Cell (Cambridge, Mass.) 31 1982 681 692
    • (1982) Cell (Cambridge, Mass.) , vol.31 , pp. 681-692
    • Mose-Larsen, P.1    Bravo, R.2    Fey, S.J.3    Small, J.V.4    Celis, J.E.5
  • 198
    • 0020538869 scopus 로고
    • Biochemical and immunological characterization of desmoplakins I and II, the major polypeptides of the desmosomal plaque
    • H. Muller W.W. Franke Biochemical and immunological characterization of desmoplakins I and II, the major polypeptides of the desmosomal plaque J. Mol. Biol. 163 1983 647 671
    • (1983) J. Mol. Biol. , vol.163 , pp. 647-671
    • Muller, H.1    Franke, W.W.2
  • 199
    • 0025190741 scopus 로고
    • Localization of newly synthesized vimentin subunits reveals a novel mechanism of intermediate filament assembly
    • J. Ngai T.R. Coleman E. Lazarides Localization of newly synthesized vimentin subunits reveals a novel mechanism of intermediate filament assembly Cell (Cambridge, Mass.) 60 1990 415 427
    • (1990) Cell (Cambridge, Mass.) , vol.60 , pp. 415-427
    • Ngai, J.1    Coleman, T.R.2    Lazarides, E.3
  • 200
    • 0014863173 scopus 로고
    • Observation of filaments in the adrenal of androgen-treated rats
    • P.A. Nickerson F.R. Skelton A. Molteni Observation of filaments in the adrenal of androgen-treated rats J. Cell Biol. 47 1970 277 280
    • (1970) J. Cell Biol. , vol.47 , pp. 277-280
    • Nickerson, P.A.1    Skelton, F.R.2    Molteni, A.3
  • 201
    • 0026813618 scopus 로고
    • Assembly and disassembly of the nuclear lamina
    • E.A. Nigg Assembly and disassembly of the nuclear lamina Curr. Opin. Cell Biol. 4 1992 105 109
    • (1992) Curr. Opin. Cell Biol. , vol.4 , pp. 105-109
    • Nigg, E.A.1
  • 202
    • 0025779541 scopus 로고
    • Structural analysis and expression of human desmoglein: A cadherin-like component of the desmosome
    • L.A. Nilles D.A.D. Parry E.E. Powers B.D. Angst R.M. Wagner K.J. Green Structural analysis and expression of human desmoglein: A cadherin-like component of the desmosome J. Cell Sci. 99 1991 809 821
    • (1991) J. Cell Sci. , vol.99 , pp. 809-821
    • Nilles, L.A.1    Parry, D.A.D.2    Powers, E.E.3    Angst, B.D.4    Wagner, R.M.5    Green, K.J.6
  • 204
    • 0024371499 scopus 로고
    • Desmoplakin I and desmoplakin II: Purification and characterization
    • E.J. O'Keefe H.P. Erickson V. Bennett Desmoplakin I and desmoplakin II: Purification and characterization J. Biol. Chem. 264 1989 8310 8318
    • (1989) J. Biol. Chem. , vol.264 , pp. 8310-8318
    • O'Keefe, E.J.1    Erickson, H.P.2    Bennett, V.3
  • 205
    • 0026709315 scopus 로고
    • Identification of an epithelial protein related to the desmosome and intermediate filament network
    • P. Ouyang S.P. Sugrue Identification of an epithelial protein related to the desmosome and intermediate filament network J. Cell Biol. 118 1992 1477 1488
    • (1992) J. Cell Biol. , vol.118 , pp. 1477-1488
    • Ouyang, P.1    Sugrue, S.P.2
  • 207
    • 0017379297 scopus 로고
    • Structure of α-keratin: Structural implication of the amino acid sequences of the type I and II chain segments
    • D.A.D. Parry W.G. Crewther R.D.B. Fraser T.P. MacRae Structure of α-keratin: Structural implication of the amino acid sequences of the type I and II chain segments J. Mol. Biol. 113 1977 449 454
    • (1977) J. Mol. Biol. , vol.113 , pp. 449-454
    • Parry, D.A.D.1    Crewther, W.G.2    Fraser, R.D.B.3    MacRae, T.P.4
  • 208
    • 0026661360 scopus 로고
    • The vertebrate adhesive junction proteins b-catenin and plakoglobin and the Drosophila segment polarity gene armadillo form a multigene family with similar properties
    • M. Peifer P. McCrea K.J. Green E. Wieschaus B. Gumbiner The vertebrate adhesive junction proteins b-catenin and plakoglobin and the Drosophila segment polarity gene armadillo form a multigene family with similar properties J. Cell Biol. 118 1992 681 691
    • (1992) J. Cell Biol. , vol.118 , pp. 681-691
    • Peifer, M.1    McCrea, P.2    Green, K.J.3    Wieschaus, E.4    Gumbiner, B.5
  • 212
    • 85018008101 scopus 로고
    • Lens morphology
    • N.S. Rafferty Lens morphology H. Maisel “The Ocular Lens, Structure, Function, and Pathology” 1985 Dekker New York 1 160
    • (1985) , pp. 1-160
    • Rafferty, N.S.1
  • 213
    • 0005728981 scopus 로고
    • Cytoskeletal and contractile structures in lens cell differentiation
    • F.C.S. Ramaekers H. Bloemendal Cytoskeletal and contractile structures in lens cell differentiation H. Bloemendal “Molecular and Cellular Biology of the Eye Lens” 1981 Wiley New York 85 136
    • (1981) , pp. 85-136
    • Ramaekers, F.C.S.1    Bloemendal, H.2
  • 215
    • 0014544626 scopus 로고
    • Ultrastructure of desmosomes in mammalian intercalated discs: Appearances after lanthanum treatment
    • D.G. Rayns L.O. Simpson J.M. Ledingham Ultrastructure of desmosomes in mammalian intercalated discs: Appearances after lanthanum treatment J. Cell Biol. 42 1969 322 326
    • (1969) J. Cell Biol. , vol.42 , pp. 322-326
    • Rayns, D.G.1    Simpson, L.O.2    Ledingham, J.M.3
  • 216
    • 0027182464 scopus 로고
    • Chicken filensin: A lens fiber cell protein that exhibits sequence similarity to intermediate filament proteins
    • S.G. Remington Chicken filensin: A lens fiber cell protein that exhibits sequence similarity to intermediate filament proteins J. Cell Sci. 105 1993 1057 1068
    • (1993) J. Cell Sci. , vol.105 , pp. 1057-1068
    • Remington, S.G.1
  • 217
    • 0019841086 scopus 로고
    • Immunoelectron and immunofluorescence localization of desmin in mature avian muscles
    • F.L. Richardson M.H. Stromer T.W. Huiatt R.M. Robson Immunoelectron and immunofluorescence localization of desmin in mature avian muscles Eur. J. Cell Biol. 26 1981 91 101
    • (1981) Eur. J. Cell Biol. , vol.26 , pp. 91-101
    • Richardson, F.L.1    Stromer, M.H.2    Huiatt, T.W.3    Robson, R.M.4
  • 218
    • 0026778228 scopus 로고
    • Analysis of the cDNA and gene encoding a cytoplasmic intermediate filament (IF) protein from the cephalochordate Branchiostoma lanceolatum; implications for the evolution of the IF protein family
    • D. Riemer H. Dodemont K. Weber Analysis of the cDNA and gene encoding a cytoplasmic intermediate filament (IF) protein from the cephalochordate Branchiostoma lanceolatum; implications for the evolution of the IF protein family Eur. J. Cell Biol. 58 1992 128 135
    • (1992) Eur. J. Cell Biol. , vol.58 , pp. 128-135
    • Riemer, D.1    Dodemont, H.2    Weber, K.3
  • 219
    • 0002272634 scopus 로고
    • The three dimensional structure of the nuclear pore complex as seen by high voltage electron microscopy and high resolution low voltage scanning electron microscopy
    • H. Ris The three dimensional structure of the nuclear pore complex as seen by high voltage electron microscopy and high resolution low voltage scanning electron microscopy EMSA Bull. 21 1991 54 56
    • (1991) EMSA Bull. , vol.21 , pp. 54-56
    • Ris, H.1
  • 220
    • 0024312984 scopus 로고
    • An epithelium-type cytoskeleton in a glial cell: Astrocytes of amphibian optic nerves contain cytokeratin filaments and are connected by desmosomes
    • E. Rungger-Brandle T. Achtstatter W.W. Franke An epithelium-type cytoskeleton in a glial cell: Astrocytes of amphibian optic nerves contain cytokeratin filaments and are connected by desmosomes J. Cell Biol. 109 1989 705 716
    • (1989) J. Cell Biol. , vol.109 , pp. 705-716
    • Rungger-Brandle, E.1    Achtstatter, T.2    Franke, W.W.3
  • 221
    • 0025339874 scopus 로고
    • Regulated expression of vimentin cDNA in cells in the presence and abscence of a preexisting vimentin filaments network
    • A.J. Sarria S.K. Nordeen R.M. Evans Regulated expression of vimentin cDNA in cells in the presence and abscence of a preexisting vimentin filaments network J. Cell Biol. 111 1990 553 565
    • (1990) J. Cell Biol. , vol.111 , pp. 553-565
    • Sarria, A.J.1    Nordeen, S.K.2    Evans, R.M.3
  • 222
    • 0026744762 scopus 로고
    • A functional role for vimentin-intermediate filaments in the metabolism of lipoprotein derived cholesterol in human SW-13 cells
    • A.J. Sarria S.R. Panini R.M. Evans A functional role for vimentin-intermediate filaments in the metabolism of lipoprotein derived cholesterol in human SW-13 cells J. Biol. Chem. 267 1992 19455 19463
    • (1992) J. Biol. Chem. , vol.267 , pp. 19455-19463
    • Sarria, A.J.1    Panini, S.R.2    Evans, R.M.3
  • 223
    • 0028361169 scopus 로고
    • The presence or absence of a vimentin-type intermediate filament network affects the shape of the nucleus in human SW13 cells
    • A.J. Sarria J.G. Leiber S.K. Nordeen R.M. Evans The presence or absence of a vimentin-type intermediate filament network affects the shape of the nucleus in human SW13 cells J. Cell Sci. 107 1994 1593 1607
    • (1994) J. Cell Sci. , vol.107 , pp. 1593-1607
    • Sarria, A.J.1    Leiber, J.G.2    Nordeen, S.K.3    Evans, R.M.4
  • 224
    • 0028360311 scopus 로고
    • Identification of the ubiquitous human desmoglein, Dsg2, and the expression catalogue of the desmoglein subfamily of desmosomal cadherins
    • S. Schafer P.J. Koch W.W. Franke Identification of the ubiquitous human desmoglein, Dsg2, and the expression catalogue of the desmoglein subfamily of desmosomal cadherins Exp. Cell Res. 211 1994 391 399
    • (1994) Exp. Cell Res. , vol.211 , pp. 391-399
    • Schafer, S.1    Koch, P.J.2    Franke, W.W.3
  • 225
    • 0027491462 scopus 로고
    • Complexus adhaerentes, a new group of desmoplakin-containing junctions in endothelial cells. The syndesmos connecting retothelial cells of lymph nodes
    • M. Schmelz W.W. Franke Complexus adhaerentes, a new group of desmoplakin-containing junctions in endothelial cells. The syndesmos connecting retothelial cells of lymph nodes Eur. J. Cell Biol. 61 1993 274 289
    • (1993) Eur. J. Cell Biol. , vol.61 , pp. 274-289
    • Schmelz, M.1    Franke, W.W.2
  • 226
    • 0022913182 scopus 로고
    • A constitutive transmembrane glycoprotein of Mr 165 000 (desmoglein) in epidermal and nonepidermal desmosomes: I. Biochemical identification of the polypeptide
    • Schmelz M. R. Duden P. Cowin W.W. Franke A constitutive transmembrane glycoprotein of Mr 165 000 (desmoglein) in epidermal and nonepidermal desmosomes: I. Biochemical identification of the polypeptide Eur. J. Cell Biol. 42 1986 177 183
    • (1986) Eur. J. Cell Biol. , vol.42 , pp. 177-183
    • Schmelz, M.1    Duden, R.2    Cowin, P.3    Franke, W.W.4
  • 227
    • 0028577357 scopus 로고
    • Desmosomes and cytoskeletal architecture in epithelial differentiation: Cell type-specific plaque components and intermediate filament anchorage
    • A. Schmidt H.W. Heid S. Schafer U.A. Nuber R. Zimbelmann W.W. Franke Desmosomes and cytoskeletal architecture in epithelial differentiation: Cell type-specific plaque components and intermediate filament anchorage Eur. J. Cell Biol. 65 1994 229 245
    • (1994) Eur. J. Cell Biol. , vol.65 , pp. 229-245
    • Schmidt, A.1    Heid, H.W.2    Schafer, S.3    Nuber, U.A.4    Zimbelmann, R.5    Franke, W.W.6
  • 230
    • 0024263203 scopus 로고
    • Integral membrane proteins specific to the inner nuclear membrane and associated with the nuclear lamina
    • A. Senior L. Gerace Integral membrane proteins specific to the inner nuclear membrane and associated with the nuclear lamina J. Cell Biol. 107 1988 2029 2036
    • (1988) J. Cell Biol. , vol.107 , pp. 2029-2036
    • Senior, A.1    Gerace, L.2
  • 231
    • 0019215750 scopus 로고
    • Specific disruption of vimentin filament organization in monkey kidney CV-1 cells by diphteria toxin, endotoxin A and cycloheximide
    • A.H. Sharpe L.B. Chen J.R. Murphy B.N. Fields Specific disruption of vimentin filament organization in monkey kidney CV-1 cells by diphteria toxin, endotoxin A and cycloheximide Proc. Natl. Acad. Sci. U.S.A. 77 1980 7267 7271
    • (1980) Proc. Natl. Acad. Sci. U.S.A. , vol.77 , pp. 7267-7271
    • Sharpe, A.H.1    Chen, L.B.2    Murphy, J.R.3    Fields, B.N.4
  • 232
    • 0025302814 scopus 로고
    • The in vitro DNA-properties of purified nuclear lamins proteins and vimentin
    • R.L. Shoeman P. Traub The in vitro DNA-properties of purified nuclear lamins proteins and vimentin J. Biol. Chem. 265 1990 9055 9061
    • (1990) J. Biol. Chem. , vol.265 , pp. 9055-9061
    • Shoeman, R.L.1    Traub, P.2
  • 233
    • 0024577383 scopus 로고
    • Concurrent collapse of keratin filaments, aggregation of organelles and inhibition of protein synthesis during the heat shock response in mammary epithelial cells
    • T.T. Shyy B.A. Asch H.L. Asch Concurrent collapse of keratin filaments, aggregation of organelles and inhibition of protein synthesis during the heat shock response in mammary epithelial cells J. Cell Biol. 108 1989 997 1008
    • (1989) J. Cell Biol. , vol.108 , pp. 997-1008
    • Shyy, T.T.1    Asch, B.A.2    Asch, H.L.3
  • 234
    • 0026671560 scopus 로고
    • The inner nuclear membrane protein p58 associates in vitro with a p58 kinase and the nuclear lamins
    • 58 kinase and the nuclear lamins EMBO J. 11 1992 4027 4036
    • (1992) EMBO J. , vol.11 , pp. 4027-4036
    • Simos, G.1    Georgatos, S.D.2
  • 235
    • 0028263453 scopus 로고
    • The lamin B receptor-associated protein p34 shares sequence homology and antigenic determinants with the splicing factor 2-associated protein
    • 34 shares sequence homology and antigenic determinants with the splicing factor 2-associated protein FEBS Lett. 346 1994 225 228
    • (1994) FEBS Lett. , vol.346 , pp. 225-228
    • Simos, G.1    Georgatos, S.D.2
  • 236
    • 0025803568 scopus 로고
    • Recent insights into the assembly, dynamics, and function of intermediate filament networks
    • O. Skalli R.D. Goldman Recent insights into the assembly, dynamics, and function of intermediate filament networks Cell Motil. Cytoskel. 19 1991 67 79
    • (1991) Cell Motil. Cytoskel. , vol.19 , pp. 67-79
    • Skalli, O.1    Goldman, R.D.2
  • 237
    • 0028178390 scopus 로고
    • IFAP 300 is common to desmosomes and hemidesmosomes and is a possible linker of intermediate filaments to these junctions
    • O. Skalli J.C.R. Jones R. Gagescu R.D. Goldman IFAP 300 is common to desmosomes and hemidesmosomes and is a possible linker of intermediate filaments to these junctions J. Cell Biol. 125 1994 159 170
    • (1994) J. Cell Biol. , vol.125 , pp. 159-170
    • Skalli, O.1    Jones, J.C.R.2    Gagescu, R.3    Goldman, R.D.4
  • 238
    • 0016291430 scopus 로고
    • Isolation of epidermal desmosomes
    • C.J. Skerrow A.G. Matolsy Isolation of epidermal desmosomes J. Cell Biol. 63 1974 515 523
    • (1974) J. Cell Biol. , vol.63 , pp. 515-523
    • Skerrow, C.J.1    Matolsy, A.G.2
  • 239
    • 0017366003 scopus 로고
    • Studies on the function and composition of the 10-nm (100-A) filaments of vertebrate smooth muscle
    • J.V. Small A. Sobieszek Studies on the function and composition of the 10-nm (100-A) filaments of vertebrate smooth muscle J. Cell Sci. 23 1977 243 268
    • (1977) J. Cell Sci. , vol.23 , pp. 243-268
    • Small, J.V.1    Sobieszek, A.2
  • 240
    • 0000651603 scopus 로고
    • The contractile apparatus of smooth muscle
    • J.V. Small A. Sobieszek The contractile apparatus of smooth muscle Int. Rev. Cytol. 64 1980 241 306
    • (1980) Int. Rev. Cytol. , vol.64 , pp. 241-306
    • Small, J.V.1    Sobieszek, A.2
  • 241
    • 0027386803 scopus 로고
    • The first membrane spanning region of the lamin B receptor is sufficient for sorting to the inner nuclear membrane
    • S. Smith G. Blobel The first membrane spanning region of the lamin B receptor is sufficient for sorting to the inner nuclear membrane J. Cell Biol. 120 1993 631 637
    • (1993) J. Cell Biol. , vol.120 , pp. 631-637
    • Smith, S.1    Blobel, G.2
  • 242
    • 0021831946 scopus 로고
    • New views of smooth muscle structure using freezing, deep-etching and rotary shadowing
    • A.V. Somlyo C. Franzini-Armstrong New views of smooth muscle structure using freezing, deep-etching and rotary shadowing Experientia 41 1985 841 856
    • (1985) Experientia , vol.41 , pp. 841-856
    • Somlyo, A.V.1    Franzini-Armstrong, C.2
  • 244
    • 0027369205 scopus 로고
    • The beta 4 subunit cytoplasmic domain mediates the interaction of alpha 6 beta 4 integrin with the cytoskeleton of hemidesmosomes
    • L. Spinardi Y.L. Ren R. Sanders F.G. Giancotti The beta 4 subunit cytoplasmic domain mediates the interaction of alpha 6 beta 4 integrin with the cytoskeleton of hemidesmosomes Mol. Cell. Biol. 4 1993 871 884
    • (1993) Mol. Cell. Biol. , vol.4 , pp. 871-884
    • Spinardi, L.1    Ren, Y.L.2    Sanders, R.3    Giancotti, F.G.4
  • 245
    • 0016140812 scopus 로고
    • Structure and function of intercellular junctions
    • L.A. Staehelin Structure and function of intercellular junctions Int. Rev. Cytol. 39 1974 191 283
    • (1974) Int. Rev. Cytol. , vol.39 , pp. 191-283
    • Staehelin, L.A.1
  • 246
    • 0026511055 scopus 로고
    • The desmoplakin carboxyl terminus coaligns with and specifically disrupts intermediate filament networks when expressed in cultured cells
    • T.S. Stappenbeck K.J. Green The desmoplakin carboxyl terminus coaligns with and specifically disrupts intermediate filament networks when expressed in cultured cells J. Cell Biol. 116 1992 1197 1209
    • (1992) J. Cell Biol. , vol.116 , pp. 1197-1209
    • Stappenbeck, T.S.1    Green, K.J.2
  • 247
    • 0027428693 scopus 로고
    • Functional analysis of desmoplakin domains: Specification of the interaction with keratin versus vimentin intermediate filament networks
    • T.S. Stappenbeck E.A. Bornslaeger C.M. Corcoran H.H. Luu M.L.A. Viarata K.J. Green Functional analysis of desmoplakin domains: Specification of the interaction with keratin versus vimentin intermediate filament networks J. Cell Biol. 123 1993 691 705
    • (1993) J. Cell Biol. , vol.123 , pp. 691-705
    • Stappenbeck, T.S.1    Bornslaeger, E.A.2    Corcoran, C.M.3    Luu, H.H.4    Viarata, M.L.A.5    Green, K.J.6
  • 248
    • 0023951297 scopus 로고
    • Molecular and cellular biology of intermediate filaments
    • P.M. Steinert D.R. Roop Molecular and cellular biology of intermediate filaments Annu. Rev. Biochem. 57 1988 593 625
    • (1988) Annu. Rev. Biochem. , vol.57 , pp. 593-625
    • Steinert, P.M.1    Roop, D.R.2
  • 250
    • 0023690364 scopus 로고
    • The fates of chicken nuclear lamin proteins during mitosis: Evidence for a reversible redistribution of lamin B2 between inner nuclear membrane and elements of the endoplasmic reticulum
    • R. Stick B. Angres Lehner G. E.A. Nigg The fates of chicken nuclear lamin proteins during mitosis: Evidence for a reversible redistribution of lamin B2 between inner nuclear membrane and elements of the endoplasmic reticulum J. Cell Biol. 107 1988 397 406
    • (1988) J. Cell Biol. , vol.107 , pp. 397-406
    • Stick, R.1    Angres, B.2    Lehner, G.3    Nigg, E.A.4
  • 251
    • 0023716339 scopus 로고
    • Arrangement of desmin intermediate filaments in smooth muscle cells as shown by high-resolution immunocytochemistry
    • M.H. Stromer M. Bendayan Arrangement of desmin intermediate filaments in smooth muscle cells as shown by high-resolution immunocytochemistry Cell Motil. Cytoskel. 11 1988 117 125
    • (1988) Cell Motil. Cytoskel. , vol.11 , pp. 117-125
    • Stromer, M.H.1    Bendayan, M.2
  • 252
    • 0025082774 scopus 로고
    • Immunocytochemical identification of cytoskeletal linkages to smooth muscle cell nuclei and mitochondria
    • M.H. Stromer M. Bendayan Immunocytochemical identification of cytoskeletal linkages to smooth muscle cell nuclei and mitochondria Cell Motil. Cytoskel. 17 1990 11 18
    • (1990) Cell Motil. Cytoskel. , vol.17 , pp. 11-18
    • Stromer, M.H.1    Bendayan, M.2
  • 253
    • 0020760101 scopus 로고
    • Effect of microtubules and intermediate filaments on mitochondrial distribution
    • I.C. Summerhayes D. Wong L.B. Chen Effect of microtubules and intermediate filaments on mitochondrial distribution J. Cell Sci. 61 1983 87 105
    • (1983) J. Cell Sci. , vol.61 , pp. 87-105
    • Summerhayes, I.C.1    Wong, D.2    Chen, L.B.3
  • 254
    • 0025020280 scopus 로고
    • Amino acid sequence of a novel integrin B4 subunit and primary expression of the mRNA in epithelial cells
    • S. Suzuki Y. Naitoh Amino acid sequence of a novel integrin B4 subunit and primary expression of the mRNA in epithelial cells EMBO J. 9 1990 757 763
    • (1990) EMBO J. , vol.9 , pp. 757-763
    • Suzuki, S.1    Naitoh, Y.2
  • 255
    • 0027397194 scopus 로고
    • Reorganization of brain spectrin (fodrin) during differentiation of PC12 cells
    • R. Takemura S. Okabe N. Kobayashi N. Hirokawa Reorganization of brain spectrin (fodrin) during differentiation of PC12 cells Neuroscience 52 1993 381 391
    • (1993) Neuroscience , vol.52 , pp. 381-391
    • Takemura, R.1    Okabe, S.2    Kobayashi, N.3    Hirokawa, N.4
  • 257
    • 0025743954 scopus 로고
    • Comparison of molecularly cloned bullous pemphigoid antigen to desmoplakin I confirms that they define a new family of cell adhesion junction plaque proteins
    • T. Tanaka D.A.D. Parry V. Klaus-Kovtun P.M. Steinert J.R. Stanley Comparison of molecularly cloned bullous pemphigoid antigen to desmoplakin I confirms that they define a new family of cell adhesion junction plaque proteins J. Biol. Chem. 266 1991 12555 12559
    • (1991) J. Biol. Chem. , vol.266 , pp. 12555-12559
    • Tanaka, T.1    Parry, D.A.D.2    Klaus-Kovtun, V.3    Steinert, P.M.4    Stanley, J.R.5
  • 258
    • 0019226175 scopus 로고
    • Association of mitochondria with intermediate filaments and of polyribosomes with cytoplasmic actin
    • B.H. Toh S.J. Lolait J.P. Mathy R. Baum Association of mitochondria with intermediate filaments and of polyribosomes with cytoplasmic actin Cell Tissue Res. 211 1980 163 169
    • (1980) Cell Tissue Res. , vol.211 , pp. 163-169
    • Toh, B.H.1    Lolait, S.J.2    Mathy, J.P.3    Baum, R.4
  • 259
    • 0020803501 scopus 로고
    • Visualization of longitudinally-oriented intermediate filaments in frozen sections of chicken cardiac muscle by a new staining method
    • K.T. Tokuyasu Visualization of longitudinally-oriented intermediate filaments in frozen sections of chicken cardiac muscle by a new staining method J. Cell Biol. 97 1983 562 565
    • (1983) J. Cell Biol. , vol.97 , pp. 562-565
    • Tokuyasu, K.T.1
  • 260
    • 0020955372 scopus 로고
    • Immunoelectron microscopic studies of desmin (skeletin) localization and intermediate filament organization in chicken skeletal muscle
    • K.T. Tokuyasu A.H. Dutton S.J. Singer Immunoelectron microscopic studies of desmin (skeletin) localization and intermediate filament organization in chicken skeletal muscle J. Cell Biol. 96 1983 1727 1735
    • (1983) J. Cell Biol. , vol.96 , pp. 1727-1735
    • Tokuyasu, K.T.1    Dutton, A.H.2    Singer, S.J.3
  • 261
    • 0021264715 scopus 로고
    • Distributions of vimentin and desmin in developing chick myotubes in vivo. I. Immunofluorescence study
    • K.T. Tokuyasu P.A. Maher S.J. Singer Distributions of vimentin and desmin in developing chick myotubes in vivo. I. Immunofluorescence study J. Cell Biol. 98 1984 1961 1972
    • (1984) J. Cell Biol. , vol.98 , pp. 1961-1972
    • Tokuyasu, K.T.1    Maher, P.A.2    Singer, S.J.3
  • 262
    • 85012367314 scopus 로고
    • Distributions of vimentin and desmin in developing chick myotubes in vivo. II. Immunoelectron microscopic study
    • K.T. Tokuyasu P.A. Maher S.J. Singer Distributions of vimentin and desmin in developing chick myotubes in vivo. II. Immunoelectron microscopic study J. Cell Biol. 100 1985 1157 1166
    • (1985) J. Cell Biol. , vol.100 , pp. 1157-1166
    • Tokuyasu, K.T.1    Maher, P.A.2    Singer, S.J.3
  • 263
    • 0022272936 scopus 로고
    • Intermediate filaments in skeletal and cardiac muscle tissue in embryonic and adult chicken
    • K.T. Tokuyasu P.A. Maher A.H. Dutton S.J. Singer Intermediate filaments in skeletal and cardiac muscle tissue in embryonic and adult chicken Ann. N. Y. Acad. Sci. 455 1985 200 212
    • (1985) Ann. N. Y. Acad. Sci. , vol.455 , pp. 200-212
    • Tokuyasu, K.T.1    Maher, P.A.2    Dutton, A.H.3    Singer, S.J.4
  • 264
    • 0020760248 scopus 로고
    • The interaction in vitro of the intermediate filament protein vimentin with synthetic polyribo- and polydeoxyribonucleotides
    • P. Traub W.J. Nelson The interaction in vitro of the intermediate filament protein vimentin with synthetic polyribo- and polydeoxyribonucleotides Hoppe-Seyler's Z. Physiol. Chem. 364 1983 575 592
    • (1983) Hoppe-Seyler's Z. Physiol. Chem. , vol.364 , pp. 575-592
    • Traub, P.1    Nelson, W.J.2
  • 265
    • 0020533605 scopus 로고
    • The interaction in vitro of the intermediate filament protein vimentin with naturally occuring RNAs and DNAs
    • P. Traub W.J. Nelson S. Kühn C.E. Vorgias The interaction in vitro of the intermediate filament protein vimentin with naturally occuring RNAs and DNAs J. Biol. Chem. 258 1983 1456 1466
    • (1983) J. Biol. Chem. , vol.258 , pp. 1456-1466
    • Traub, P.1    Nelson, W.J.2    Kühn, S.3    Vorgias, C.E.4
  • 266
    • 0022041763 scopus 로고
    • Interaction in vitro of the neurofilament triplet proteins from porcine spinal cord with natural RNA and DNA
    • P. Traub C.E. Vorgias W.J. Nelson Interaction in vitro of the neurofilament triplet proteins from porcine spinal cord with natural RNA and DNA Mol. Biol. Rep. 10 1985 129 136
    • (1985) Mol. Biol. Rep. , vol.10 , pp. 129-136
    • Traub, P.1    Vorgias, C.E.2    Nelson, W.J.3
  • 267
    • 0022397820 scopus 로고
    • Tenacious binding of lipids to vimentin during its isolation and purification from Ehrlich ascites tumor cells
    • P. Traub G. Perides A. Scherbarth U. Traub Tenacious binding of lipids to vimentin during its isolation and purification from Ehrlich ascites tumor cells FEBS Lett. 193 1985 217 221
    • (1985) FEBS Lett. , vol.193 , pp. 217-221
    • Traub, P.1    Perides, G.2    Scherbarth, A.3    Traub, U.4
  • 268
    • 0023075726 scopus 로고
    • Interaction in vitro of nonepithelial intermediate filament proteins with histones
    • P. Traub G. Perides S. Kühn A. Scherbarth Interaction in vitro of nonepithelial intermediate filament proteins with histones Z. Naturforsch. C: Biosci. 42C 1986 47 63
    • (1986) Z. Naturforsch. C: Biosci. , vol.42C , pp. 47-63
    • Traub, P.1    Perides, G.2    Kühn, S.3    Scherbarth, A.4
  • 269
    • 0022981412 scopus 로고
    • Interaction in vitro of nonepithelial intermediate filament proteins with total cellular lipids, individual phospholipids, and a phospholipid mixture
    • P. Traub G. Perides H. Schimmel A. Scherbarth Interaction in vitro of nonepithelial intermediate filament proteins with total cellular lipids, individual phospholipids, and a phospholipid mixture J. Biol. Chem. 261 1986 10558 10568
    • (1986) J. Biol. Chem. , vol.261 , pp. 10558-10568
    • Traub, P.1    Perides, G.2    Schimmel, H.3    Scherbarth, A.4
  • 270
    • 0023284867 scopus 로고
    • Efficient interaction of nonpolar lipids with intermediate filaments of the vimentin type
    • P. Traub G. Perides S. Kuhn A. Scherbarth Efficient interaction of nonpolar lipids with intermediate filaments of the vimentin type Eur. J. Cell Biol. 43 1987 55 64
    • (1987) Eur. J. Cell Biol. , vol.43 , pp. 55-64
    • Traub, P.1    Perides, G.2    Kuhn, S.3    Scherbarth, A.4
  • 271
    • 0027050860 scopus 로고
    • Binding of nuclei acids to intermediate filaments of the vimentin type and their effects on filament formation and stability
    • P. Traub E. Mothes R.L. Shoeman R. Schroder A. Scherbarth Binding of nuclei acids to intermediate filaments of the vimentin type and their effects on filament formation and stability J. Biomol. Struct. Dyn. 10 1992 505 531
    • (1992) J. Biomol. Struct. Dyn. , vol.10 , pp. 505-531
    • Traub, P.1    Mothes, E.2    Shoeman, R.L.3    Schroder, R.4    Scherbarth, A.5
  • 272
    • 0028821094 scopus 로고
    • Association of vimentin intermediate filaments with the centrosome
    • K.T. Trevor J.G. McGuire E.V. Leonova Association of vimentin intermediate filaments with the centrosome J. Cell Sci. 108 1995 343 356
    • (1995) J. Cell Sci. , vol.108 , pp. 343-356
    • Trevor, K.T.1    McGuire, J.G.2    Leonova, E.V.3
  • 273
    • 0027468175 scopus 로고
    • Contributions of cytoplasmic domains of desmosomal cadherins to desmosome assembly and intermediate filament anchorage
    • S.M. Troyanovsky L.G. Eshkind R.B. Troyanovsky R.E. Leube W.W. Franke Contributions of cytoplasmic domains of desmosomal cadherins to desmosome assembly and intermediate filament anchorage Cell (Cambridge, Mass.) 72 1993 561 574
    • (1993) Cell (Cambridge, Mass.) , vol.72 , pp. 561-574
    • Troyanovsky, S.M.1    Eshkind, L.G.2    Troyanovsky, R.B.3    Leube, R.E.4    Franke, W.W.5
  • 274
    • 0022371564 scopus 로고
    • Desmocalmin: A calmodulin-binding high molecular weight protein isolated from desmosomes
    • S. Tsukita S. Tsukita Desmocalmin: A calmodulin-binding high molecular weight protein isolated from desmosomes J. Cell Biol. 101 1985 2070 2080
    • (1985) J. Cell Biol. , vol.101 , pp. 2070-2080
    • Tsukita, S.1    Tsukita, S.2
  • 275
    • 0015112167 scopus 로고
    • Cytoplasmic filaments in developing and adult vertebrate smooth muscle
    • Y. Uehara G.R. Campbell G. Burnstock Cytoplasmic filaments in developing and adult vertebrate smooth muscle J. Cell Biol. 50 1971 484 497
    • (1971) J. Cell Biol. , vol.50 , pp. 484-497
    • Uehara, Y.1    Campbell, G.R.2    Burnstock, G.3
  • 276
    • 0020472010 scopus 로고
    • A large particle associated with the perimeter of the nuclear pore complex
    • P.N.T. Unwin R.A. Milligan A large particle associated with the perimeter of the nuclear pore complex J. Cell Biol. 93 1982 63 75
    • (1982) J. Cell Biol. , vol.93 , pp. 63-75
    • Unwin, P.N.T.1    Milligan, R.A.2
  • 277
    • 0022785881 scopus 로고
    • Nucleic acid-binding activities of the intermediate filament subunit proteins desmin and glial fibrillary acidic protein
    • C.E. Vorgias P. Traub Nucleic acid-binding activities of the intermediate filament subunit proteins desmin and glial fibrillary acidic protein Z. Naturforsch., C: Biosci. 41C 1986 897 909
    • (1986) Z. Naturforsch., C: Biosci. , vol.41C , pp. 897-909
    • Vorgias, C.E.1    Traub, P.2
  • 278
    • 0020639339 scopus 로고
    • A network of transverse and longitudinal intermediate filaments is associated with sarcomeres of adult vertebrate skeletal muscle
    • K. Wang R. Ramirez-Mitchell A network of transverse and longitudinal intermediate filaments is associated with sarcomeres of adult vertebrate skeletal muscle J. Cell Biol. 96 1983 562 570
    • (1983) J. Cell Biol. , vol.96 , pp. 562-570
    • Wang, K.1    Ramirez-Mitchell, R.2
  • 279
    • 0026034276 scopus 로고
    • Resinless section immunogold electron microscopy of karyocytoskeletal frameworks of eukaryotic cells cultured in vitro. Absence of a salt-stable nuclear matrix from mouse plasmacytoma MPC-11 cells
    • X. Wang P. Traub Resinless section immunogold electron microscopy of karyocytoskeletal frameworks of eukaryotic cells cultured in vitro. Absence of a salt-stable nuclear matrix from mouse plasmacytoma MPC-11 cells J. Cell Sci. 98 1991 107 122
    • (1991) J. Cell Sci. , vol.98 , pp. 107-122
    • Wang, X.1    Traub, P.2
  • 280
    • 0024790391 scopus 로고
    • Ultrastructural analysis of cytoplasmic intermediate filaments and the nuclear lamina in the mouse plasmacytoma cell line MPC-11 after the induction of vimentin synthesis
    • X. Wang J. Willingale-Theune R.L. Shoeman G. Giese P. Traub Ultrastructural analysis of cytoplasmic intermediate filaments and the nuclear lamina in the mouse plasmacytoma cell line MPC-11 after the induction of vimentin synthesis Eur. J. Cell Biol. 50 1989 462 474
    • (1989) Eur. J. Cell Biol. , vol.50 , pp. 462-474
    • Wang, X.1    Willingale-Theune, J.2    Shoeman, R.L.3    Giese, G.4    Traub, P.5
  • 281
    • 0022973972 scopus 로고
    • The in vitro cross-linking of proteins and DNA by heavy metals
    • A. Wedrychowski W.N. Schmidt L.S. Hnilica The in vitro cross-linking of proteins and DNA by heavy metals J. Biol. Chem. 261 1986 3370 3376
    • (1986) J. Biol. Chem. , vol.261 , pp. 3370-3376
    • Wedrychowski, A.1    Schmidt, W.N.2    Hnilica, L.S.3
  • 282
    • 0022493192 scopus 로고
    • Cross-linking of cytokeratins to DNA in vivo by chromium salt and cis-diamminechloroplatinum (II)
    • A. Wedrychowski W.N. Schmidt W.S. Ward L.S. Hnilica Cross-linking of cytokeratins to DNA in vivo by chromium salt and cis-diamminechloroplatinum (II) Biochemistry 25 1986 1 9
    • (1986) Biochemistry , vol.25 , pp. 1-9
    • Wedrychowski, A.1    Schmidt, W.N.2    Ward, W.S.3    Hnilica, L.S.4
  • 283
    • 0026082642 scopus 로고
    • Suppression by anti-sense mRNA demonstrates a requirement for the glial fibrillary acidic protein in the formation of stable astrocytic processes in response to neurons
    • Weinstein D.E. Shelanski M.L. Liem R.M. Suppression by anti-sense mRNA demonstrates a requirement for the glial fibrillary acidic protein in the formation of stable astrocytic processes in response to neurons J. Cell Biol. 112 1991 1205 1213
    • (1991) J. Cell Biol. , vol.112 , pp. 1205-1213
    • Weinstein, D.E.1    Shelanski, M.L.2    Liem, R.M.3
  • 284
    • 0027416935 scopus 로고
    • Transient localized accumulation of alpha spectrin during sea urchin morphogenesis
    • G.M. Wessels S.W. Chen Transient localized accumulation of alpha spectrin during sea urchin morphogenesis Dev. Biol. 155 1993 161 171
    • (1993) Dev. Biol. , vol.155 , pp. 161-171
    • Wessels, G.M.1    Chen, S.W.2
  • 285
    • 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
    • G. Wiche B. Becker K. Luber G. Weitzer M.J. Castanon R. Hauptmann C. Stratowa M. Stewart 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 1991 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
  • 286
    • 0019312094 scopus 로고
    • Nucleus-associated intermediate filaments from chicken erythrocytes
    • C.L.F. Woodcock Nucleus-associated intermediate filaments from chicken erythrocytes J. Cell Biol. 85 1980 881 889
    • (1980) J. Cell Biol. , vol.85 , pp. 881-889
    • Woodcock, C.L.F.1
  • 288
    • 0025149541 scopus 로고
    • The lamin B receptor of the nuclear envelope inner membrane: A polytopic protein with eight potential transmembrane domains
    • H.J. Worman C.D. Evans G. Blobel The lamin B receptor of the nuclear envelope inner membrane: A polytopic protein with eight potential transmembrane domains J. Cell Biol. 110 1990 1535 1542
    • (1990) J. Cell Biol. , vol.110 , pp. 1535-1542
    • Worman, H.J.1    Evans, C.D.2    Blobel, G.3
  • 289
    • 0027410516 scopus 로고
    • Increased expression of neurofilament subunit NF-L produces morphological alterations that resemble the pathology of human motor neuron disease
    • Z. Xu L.C. Cork J.W. Griffin D.M. Cleveland Increased expression of neurofilament subunit NF-L produces morphological alterations that resemble the pathology of human motor neuron disease Cell (Cambridge, Mass.) 73 1993 23 33
    • (1993) Cell (Cambridge, Mass.) , vol.73 , pp. 23-33
    • Xu, Z.1    Cork, L.C.2    Griffin, J.W.3    Cleveland, D.M.4
  • 290
    • 0028363978 scopus 로고
    • Primary structure analysis and lamin B and Dna binding of human LBR, an integral protein on the nuclear envelope inner membrane
    • Q. Ye H.J. Worman Primary structure analysis and lamin B and Dna binding of human LBR, an integral protein on the nuclear envelope inner membrane J. Biol. Chem. 269 1994 11306 11311
    • (1994) J. Biol. Chem. , vol.269 , pp. 11306-11311
    • Ye, Q.1    Worman, H.J.2
  • 292
    • 0344048011 scopus 로고
    • In vitro assembly of intermediate filaments from baby hamster kidney (BHK-21) cells
    • R.V. Zackroff R.D. Goldman In vitro assembly of intermediate filaments from baby hamster kidney (BHK-21) cells Proc. Natl. Acad. Sci. U.S.A. 76 1979 6226 6230
    • (1979) Proc. Natl. Acad. Sci. U.S.A. , vol.76 , pp. 6226-6230
    • Zackroff, R.V.1    Goldman, R.D.2
  • 293
    • 0017356619 scopus 로고
    • Structures indicative of keratinization in lactating cells of bovine mammary gland
    • H. Zerban W.W. Franke Structures indicative of keratinization in lactating cells of bovine mammary gland Differentiation (Berlin) 7 1977 127 131
    • (1977) Differentiation (Berlin) , vol.7 , pp. 127-131
    • Zerban, H.1    Franke, W.W.2


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