메뉴 건너뛰기




Volumn 10, Issue 2, 1996, Pages 317-324

Effects of calcium-binding proteins (S-100ao, S-100a, S-100b) on desmin assembly in vitro

Author keywords

Calcium; Desmin intermediate filaments; S 100 proteins

Indexed keywords

CALCIUM BINDING PROTEIN; DESMIN; GLIAL FIBRILLARY ACIDIC PROTEIN; PROTEIN S 100;

EID: 0029988676     PISSN: 08926638     EISSN: None     Source Type: Journal    
DOI: 10.1096/fasebj.10.2.8641565     Document Type: Article
Times cited : (43)

References (64)
  • 1
    • 0023951297 scopus 로고
    • Molecular and cellular biology of intermediate filaments
    • Steinert, P. M., and Roop, D. R. (1988) Molecular and cellular biology of intermediate filaments. Annu. Rev. Riochem. 57, 593-625
    • (1988) Annu. Rev. Riochem. , vol.57 , pp. 593-625
    • Steinert, P.M.1    Roop, D.R.2
  • 2
    • 0026248292 scopus 로고
    • Molecular interactions in intermediate filaments
    • Quinlan, R. A., and Stewait, M. (1991) Molecular interactions in intermediate filaments. Bioessays 13, 597-600
    • (1991) Bioessays , vol.13 , pp. 597-600
    • Quinlan, R.A.1    Stewait, M.2
  • 3
    • 0026693017 scopus 로고
    • The molecular biology of intermediate filaments
    • Albers, K., and Fuchs, E. (1992) The molecular biology of intermediate filaments. Int. Rev. Cytol. 134, 243-279
    • (1992) Int. Rev. Cytol. , vol.134 , pp. 243-279
    • Albers, K.1    Fuchs, E.2
  • 5
    • 0027449959 scopus 로고
    • Dynamics of intermediate filaments. Recent progress and unanswered questions
    • Georgatos, S. D. (1993) Dynamics of intermediate filaments. Recent progress and unanswered questions. FEBS Lett. 318, 101-107
    • (1993) FEBS Lett. , vol.318 , pp. 101-107
    • Georgatos, S.D.1
  • 6
    • 0027550657 scopus 로고
    • Intermediate filament structure and assembly
    • Stewart, M. (1993) Intermediate filament structure and assembly. Curr. Opin. Cell Biol. 5, 3-11
    • (1993) Curr. Opin. Cell Biol. , vol.5 , pp. 3-11
    • Stewart, M.1
  • 7
    • 0028283501 scopus 로고
    • Intermediate filaments: Structure, function, and disease
    • Fuchs, E., and Weber, K. (1994) Intermediate filaments: structure, function, and disease. Annu. Rev. Biochem. 63, 345-382
    • (1994) Annu. Rev. Biochem. , vol.63 , pp. 345-382
    • Fuchs, E.1    Weber, K.2
  • 8
    • 0019206841 scopus 로고
    • Intermediate filaments of the vimentin type are distributed differently during mitosis
    • Aubin, J. E., Osborn, M., Franke, W. W., and Weber, K. (1980) Intermediate filaments of the vimentin type are distributed differently during mitosis. Exp. Cell Res. 129, 149-165
    • (1980) Exp. Cell Res. , vol.129 , pp. 149-165
    • Aubin, J.E.1    Osborn, M.2    Franke, W.W.3    Weber, K.4
  • 9
    • 0018840796 scopus 로고
    • The nuclear envelope lamina is reversibly depolymerized during mitosis
    • Gerace, L., and Blobel, G. (1980) The nuclear envelope lamina is reversibly depolymerized during mitosis. Cell 19, 277-287
    • (1980) Cell , vol.19 , pp. 277-287
    • Gerace, L.1    Blobel, G.2
  • 10
    • 0021133349 scopus 로고
    • Transient change of organization of vimentin filaments during mitosis as demonstrated by a monoclonal antibody
    • Franke, W. W., Grund, C., Kuhn, C., Letho, V.-P., and Virtanen, I. (1984) Transient change of organization of vimentin filaments during mitosis as demonstrated by a monoclonal antibody. Exp. Cell Res. 154, 567-580
    • (1984) Exp. Cell Res. , vol.154 , pp. 567-580
    • Franke, W.W.1    Grund, C.2    Kuhn, C.3    Letho, V.-P.4    Virtanen, I.5
  • 11
    • 0024600639 scopus 로고
    • Assembly and exchange of intermediate filament proteins in neurons: Neurofilaments are dynamic structures
    • Angelidcs, K. J., Smith, K. E., and Tokeda, M. (1989) Assembly and exchange of intermediate filament proteins in neurons: neurofilaments are dynamic structures. J. Cell Biol. 108, 1495-1506
    • (1989) J. Cell Biol. , vol.108 , pp. 1495-1506
    • Angelidcs, K.J.1    Smith, K.E.2    Tokeda, M.3
  • 12
    • 0024590924 scopus 로고
    • Dynamic aspects of intermediate filaments networks in BHK-21 cells
    • Vikstrom, K. L., Borisy, G. G., and Goldman, R. D. (1989) Dynamic aspects of intermediate filaments networks in BHK-21 cells. Proc. Natl. Acad. Sci. USA 86, 549-553
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 549-553
    • Vikstrom, K.L.1    Borisy, G.G.2    Goldman, R.D.3
  • 13
    • 0025915554 scopus 로고
    • Keratin incorporation into intermediate filament networks is a rapid process
    • Miller, R. A., Vikstrom, K., and Goldman, R. D. (1991) Keratin incorporation into intermediate filament networks is a rapid process. J. Cell Biol. 113, 843-855
    • (1991) J. Cell Biol. , vol.113 , pp. 843-855
    • Miller, R.A.1    Vikstrom, K.2    Goldman, R.D.3
  • 14
    • 0026085062 scopus 로고
    • Assembly, disassembly, and subunit exchange of glial fibrillary acidic protein
    • Nakamura, Y., Takeda, M., Angelides, K. J., Tada, K., Hariguchi, S., and Nishimura, T. (1991) Assembly, disassembly, and subunit exchange of glial fibrillary acidic protein. Glia 4, 101-110
    • (1991) Glia , vol.4 , pp. 101-110
    • Nakamura, Y.1    Takeda, M.2    Angelides, K.J.3    Tada, K.4    Hariguchi, S.5    Nishimura, T.6
  • 15
    • 0026570065 scopus 로고
    • A synthetic peptide representing the consensus sequence motif at the carboxy-terminal end of the rod domain inhibits intermediate filament assembly and disassembles preformed filaments
    • Hatzfeld, M., and Weber, K. (1992) A synthetic peptide representing the consensus sequence motif at the carboxy-terminal end of the rod domain inhibits intermediate filament assembly and disassembles preformed filaments. J. Cell Biol. 116, 157-166
    • (1992) J. Cell Biol. , vol.116 , pp. 157-166
    • Hatzfeld, M.1    Weber, K.2
  • 16
    • 0026723964 scopus 로고
    • Involvement of the consensus sequence motif at coil 2b in the assembly and stability of vimentin filaments
    • Kouklis, P. D., Traub, P., and Georgatos, S. D. (1992) Involvement of the consensus sequence motif at coil 2b in the assembly and stability of vimentin filaments. J. Cell Sci. 102, 31-41
    • (1992) J. Cell Sci. , vol.102 , pp. 31-41
    • Kouklis, P.D.1    Traub, P.2    Georgatos, S.D.3
  • 17
    • 0026735638 scopus 로고
    • Steady state dynamics of intermediate filaments networks
    • Vikstrom, K. L., Lim, S.-S., Goldman, R. D., and Borisy, G. G. (1992) Steady state dynamics of intermediate filaments networks. J. Cell Biol. 118, 121-129
    • (1992) J. Cell Biol. , vol.118 , pp. 121-129
    • Vikstrom, K.L.1    Lim, S.-S.2    Goldman, R.D.3    Borisy, G.G.4
  • 18
    • 0020328231 scopus 로고
    • An alteration in the phosphorylation of vimentin-type intermediate filaments is associated with mitosis in cultured mammalian cells
    • Evans, R. M., and Fink, L. M. (1982) An alteration in the phosphorylation of vimentin-type intermediate filaments is associated with mitosis in cultured mammalian cells. Cell 29, 43-52
    • (1982) Cell , vol.29 , pp. 43-52
    • Evans, R.M.1    Fink, L.M.2
  • 19
    • 0021044471 scopus 로고
    • Phosphorylation of keratin and vimentin polypeptides in normal and transformed mitotic human epithelial amnion cells: Behavior of keratin and vimentin filaments during mitosis
    • Celis, J. E., Larsen, P. M., Fey, S. J., and Celis, A. (1983) Phosphorylation of keratin and vimentin polypeptides in normal and transformed mitotic human epithelial amnion cells: behavior of keratin and vimentin filaments during mitosis. J. Cell Biol. 97, 1429-1434
    • (1983) J. Cell Biol. , vol.97 , pp. 1429-1434
    • Celis, J.E.1    Larsen, P.M.2    Fey, S.J.3    Celis, A.4
  • 20
    • 0021955147 scopus 로고
    • Phosphorylation of the nuclear lamins during interphase and mitosis
    • Ottaviano, Y., and Gerace, L. (1985) Phosphorylation of the nuclear lamins during interphase and mitosis. J. Biol. Chem. 260, 624-632
    • (1985) J. Biol. Chem. , vol.260 , pp. 624-632
    • Ottaviano, Y.1    Gerace, L.2
  • 21
    • 0005175316 scopus 로고
    • Phosphorylation and disassembly of intermediate filaments in mitotic cells
    • Chou, Y.-H., Rosevear, E., and Goldman, R. (1989) Phosphorylation and disassembly of intermediate filaments in mitotic cells. Proc. Natl. Acad. Sci. USA 86, 1885-1889
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 1885-1889
    • Chou, Y.-H.1    Rosevear, E.2    Goldman, R.3
  • 24
    • 0025939163 scopus 로고
    • Perspectives in S-100 protein biology
    • Donato, R. (1991) Perspectives in S-100 protein biology. Cell Calcium 12, 713-726
    • (1991) Cell Calcium , vol.12 , pp. 713-726
    • Donato, R.1
  • 26
    • 0028111973 scopus 로고
    • Mechanism of S-100 protein-dependent inhibition of glial fibrillary acidic protein (GFAP) polymerization
    • Bianchi, R., Verzini, M., Garbuglia, M., Giambanco, I., and Donato, R. (1994) Mechanism of S-100 protein-dependent inhibition of glial fibrillary acidic protein (GFAP) polymerization. Biochim. Biophys. Acta 1223, 354-360
    • (1994) Biochim. Biophys. Acta , vol.1223 , pp. 354-360
    • Bianchi, R.1    Verzini, M.2    Garbuglia, M.3    Giambanco, I.4    Donato, R.5
  • 28
    • 0024324934 scopus 로고
    • Regulation of the S-100 protein and GFAP genes is mediated by two common mechanisms in RT4 neuro-glial cell lines
    • Freeman, M. R., Beckmann, S. L., and Sueoka, N. (1989) Regulation of the S-100 protein and GFAP genes is mediated by two common mechanisms in RT4 neuro-glial cell lines. Exp. Cell Res. 182, 370-383
    • (1989) Exp. Cell Res. , vol.182 , pp. 370-383
    • Freeman, M.R.1    Beckmann, S.L.2    Sueoka, N.3
  • 29
    • 0028176579 scopus 로고
    • Chaperone activity of α-crystallins modulates intermediate filament assembly
    • Nicholl, I. D., and Quinlan, R. A. (1994) Chaperone activity of α-crystallins modulates intermediate filament assembly. EMBO J. 13, 945-953
    • (1994) EMBO J. , vol.13 , pp. 945-953
    • Nicholl, I.D.1    Quinlan, R.A.2
  • 30
    • 0021299594 scopus 로고
    • Identity of p36K phosphorylated upon Rous sarcoma virus transformation with a protein purified from brush borders: Calcium-dependent binding to non-erythroid spectrin and F-actin
    • Gerke, V., and Weber, K. (1984) Identity of p36K phosphorylated upon Rous sarcoma virus transformation with a protein purified from brush borders: calcium-dependent binding to non-erythroid spectrin and F-actin. EMBO J. 3, 227-233
    • (1984) EMBO J. , vol.3 , pp. 227-233
    • Gerke, V.1    Weber, K.2
  • 31
    • 0022157945 scopus 로고
    • The regulatory chain in the p36-kd substrate complex of viral tyrosine-specifie protein kinases is related in sequence to the S-100 protein of glial cells
    • Gerke, V., and Weber, K. (1985) The regulatory chain in the p36-kd substrate complex of viral tyrosine-specifie protein kinases is related in sequence to the S-100 protein of glial cells. EMBO J. 4, 2917-2920
    • (1985) EMBO J. , vol.4 , pp. 2917-2920
    • Gerke, V.1    Weber, K.2
  • 32
    • 0001171815 scopus 로고
    • Amino-terminal sequence of p36 and associated p10: Identification of the site of tyrosine phosphorylation and homology with S-100
    • Glenney, J. R., and Tack, B. F. (1985) Amino-terminal sequence of p36 and associated p10: identification of the site of tyrosine phosphorylation and homology with S-100. Proc. Natl. Acad. Sci. USA 82, 7884-7888
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 7884-7888
    • Glenney, J.R.1    Tack, B.F.2
  • 33
    • 0022996716 scopus 로고
    • Association of the S-100-related calpactin I light chain with the amino-terminal tail of the 36kDa heavy chain
    • Glenney, J. R., Jr., Boudreau, M., Galyean, R., Hunter, T., and Tack, B. (1986) Association of the S-100-related calpactin I light chain with the amino-terminal tail of the 36kDa heavy chain. J. Biol. Chem. 261, 10485-10488
    • (1986) J. Biol. Chem. , vol.261 , pp. 10485-10488
    • Glenney Jr., J.R.1    Boudreau, M.2    Galyean, R.3    Hunter, T.4    Tack, B.5
  • 34
    • 0022651502 scopus 로고
    • Homology between the subunits of S100 and a 10kDa polypeptide associated with p36 of pig lymphocytes
    • Hexham, J. M., Totty, N. F., Waterfield, M. D., and Crumpton, M. J. (1986) Homology between the subunits of S100 and a 10kDa polypeptide associated with p36 of pig lymphocytes. Biochem. Biophys. Res. Commun. 134, 248-254
    • (1986) Biochem. Biophys. Res. Commun. , vol.134 , pp. 248-254
    • Hexham, J.M.1    Totty, N.F.2    Waterfield, M.D.3    Crumpton, M.J.4
  • 35
    • 0028102423 scopus 로고
    • 2+-dependent manner. Implications for concerted regulatory effects of calpactin I and S-100 protein on glial filaments
    • 2+-dependent manner. Implications for concerted regulatory effects of calpactin I and S-100 protein on glial filaments. Biochim. Biophys. Acta 1223, 361-367
    • (1994) Biochim. Biophys. Acta , vol.1223 , pp. 361-367
    • Bianchi, R.1    Garbuglia, M.2    Verzini, M.3    Giambanco, I.4    Donato, R.5
  • 39
    • 0021715923 scopus 로고
    • Mechanism of action of S-100 protein(s) on brain microtubule protein assembly
    • Donato, R. (1984) Mechanism of action of S-100 protein(s) on brain microtubule protein assembly. Biochem. Biophys. Res. Commun. 124, 850-856
    • (1984) Biochem. Biophys. Res. Commun. , vol.124 , pp. 850-856
    • Donato, R.1
  • 40
    • 0023878297 scopus 로고
    • Calcium-independent, pH-regulated effects of S-100 proteins on assembly-disassembly of brain microtubule proteins in vitro
    • Donato, R. (1988) Calcium-independent, pH-regulated effects of S-100 proteins on assembly-disassembly of brain microtubule proteins in vitro. J. Biol. Chem. 263, 106-110
    • (1988) J. Biol. Chem. , vol.263 , pp. 106-110
    • Donato, R.1
  • 41
    • 0021943945 scopus 로고
    • Calcium-dependent conformational changes in the 36-kDa subunit of intestinal protein I related to the cellular 36-kDa target of Rous sarcoma virus tyrosine kinase
    • Gerke, V., and Weber, K. (1985) Calcium-dependent conformational changes in the 36-kDa subunit of intestinal protein I related to the cellular 36-kDa target of Rous sarcoma virus tyrosine kinase. J. Biol. Chem. 260, 1688-1695
    • (1985) J. Biol. Chem. , vol.260 , pp. 1688-1695
    • Gerke, V.1    Weber, K.2
  • 42
    • 0025215463 scopus 로고
    • Calcium-dependent regulation of actin filament bundling by lipocortin-85
    • Ikebuchi, N. W., and Waisman, D. M. (1990) Calcium-dependent regulation of actin filament bundling by lipocortin-85. J. Biol. Chem. 265, 3393-3400
    • (1990) J. Biol. Chem. , vol.265 , pp. 3393-3400
    • Ikebuchi, N.W.1    Waisman, D.M.2
  • 43
    • 0019133440 scopus 로고
    • Purification of smooth-muscle desmin and a protein-chemical comparison of desmins from chicken gizzard and hog stomach
    • Geisler, R., and Weber, K. (1980) Purification of smooth-muscle desmin and a protein-chemical comparison of desmins from chicken gizzard and hog stomach. Eur. J. Biochem. 111, 425-433
    • (1980) Eur. J. Biochem. , vol.111 , pp. 425-433
    • Geisler, R.1    Weber, K.2
  • 44
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature (London) 227, 680-685
    • (1970) Nature (London) , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 45
    • 0020022510 scopus 로고
    • Methods to measure actin polymerization
    • Cooper, J. A., and Pollard, T. D. (1982) Methods to measure actin polymerization. Methods Enzymol. 85, 182-210
    • (1982) Methods Enzymol. , vol.85 , pp. 182-210
    • Cooper, J.A.1    Pollard, T.D.2
  • 46
    • 0026450902 scopus 로고
    • S-100 protein binds to annexin II and p11, the heavy and light chains of calpactin I
    • Bianchi, R., Pula, G., Ceccarelli, P., Giambanco, I., and Donato, R. (1992) S-100 protein binds to annexin II and p11, the heavy and light chains of calpactin I. Biochim. Biophys. Acta 1160, 67-75
    • (1992) Biochim. Biophys. Acta , vol.1160 , pp. 67-75
    • Bianchi, R.1    Pula, G.2    Ceccarelli, P.3    Giambanco, I.4    Donato, R.5
  • 47
    • 0021112116 scopus 로고
    • Synthesis, spectral properties, and use of 6-acryloyl-2-dimethylaminonaph-talene (Acrylodan), a thiol-selective, polarity-sensitive fluorescent probe
    • Pendergast, F. G., Meyer, M., Carlson, G. L., Iida, S., and Potter, J. D. (1983) Synthesis, spectral properties, and use of 6-acryloyl-2-dimethylaminonaph-talene (Acrylodan), a thiol-selective, polarity-sensitive fluorescent probe. J. Blol. Chem. 258, 7541-7544
    • (1983) J. Blol. Chem. , vol.258 , pp. 7541-7544
    • Pendergast, F.G.1    Meyer, M.2    Carlson, G.L.3    Iida, S.4    Potter, J.D.5
  • 48
    • 0019011113 scopus 로고
    • Re-examination of the apparent binding constant of ethylene glycol bis(βaminoethyl ether)-N,N,N′,N′-tetraacetic acid with calcium around neutral pH
    • Harafuji, H., and Ogawa, Y. (1980) Re-examination of the apparent binding constant of ethylene glycol bis(βaminoethyl ether)-N,N,N′,N′-tetraacetic acid with calcium around neutral pH. J. Biochem. 87, 1305-1312
    • (1980) J. Biochem. , vol.87 , pp. 1305-1312
    • Harafuji, H.1    Ogawa, Y.2
  • 50
    • 0023818922 scopus 로고
    • o (αα) protein in cardiac tissue. Isolation from human cardiac muscle and ultrastructural localization
    • o (αα) protein in cardiac tissue. Isolation from human cardiac muscle and ultrastructural localization. Eur. J. Biochem. 171, 409-415
    • (1988) Eur. J. Biochem. , vol.171 , pp. 409-415
    • Haimoto, H.1    Kato, K.2
  • 52
    • 0029043797 scopus 로고
    • Characterization of S-100b binding epitopes: Identification of a novel target, the actin capping protein, Cap Z
    • Ivanenkov, V. V., Jamieson, Jr., G. A., Gruenstein, E., and Dimlich, R. V. W. (1995) Characterization of S-100b binding epitopes: identification of a novel target, the actin capping protein, Cap Z. J. Biol. Chem. 270, 14651-14658
    • (1995) J. Biol. Chem. , vol.270 , pp. 14651-14658
    • Ivanenkov, V.V.1    Jamieson Jr., G.A.2    Gruenstein, E.3    Dimlich, R.V.W.4
  • 53
    • 0028329819 scopus 로고
    • Binding of pEL98 protein, an S100-related calcium-binding prolein, to nonmuscle tropomyosin
    • Takenaga, K., Nakamura, Y., Sakiyama, S., Hasegawa, Y., Sato, K., and Endo, H. (1994) Binding of pEL98 protein, an S100-related calcium-binding prolein, to nonmuscle tropomyosin. J. Cell Biol. 124, 757-768
    • (1994) J. Cell Biol. , vol.124 , pp. 757-768
    • Takenaga, K.1    Nakamura, Y.2    Sakiyama, S.3    Hasegawa, Y.4    Sato, K.5    Endo, H.6
  • 55
    • 0027182472 scopus 로고
    • MRP8 and MRP14, S-100-like proteins associated with myeloid differentiation, are translocated to plasma membranes and intermediate filaments in a calcium-dependent manner
    • Roth, J., Burwinkel, F., van den Bos, C., Goebeler, M., Vollmer, E., and Sorg, C. (1993) MRP8 and MRP14, S-100-like proteins associated with myeloid differentiation, are translocated to plasma membranes and intermediate filaments in a calcium-dependent manner. Blood 82, 1875-1883
    • (1993) Blood , vol.82 , pp. 1875-1883
    • Roth, J.1    Burwinkel, F.2    Van Den Bos, C.3    Goebeler, M.4    Vollmer, E.5    Sorg, C.6
  • 57
    • 0023890716 scopus 로고
    • Modulation of tyrosine phosphorylation of p36 and other substrates by the S-100 protein
    • Hagiwara, M., Ochiai, M., Owada, K., Tanaka, T., and Hidaka, H. (1988) Modulation of tyrosine phosphorylation of p36 and other substrates by the S-100 protein. J. Biol. Chem. 263, 6438-6441
    • (1988) J. Biol. Chem. , vol.263 , pp. 6438-6441
    • Hagiwara, M.1    Ochiai, M.2    Owada, K.3    Tanaka, T.4    Hidaka, H.5
  • 58
    • 0024593613 scopus 로고
    • Isolation of a new member of the S100 protein family: Amino acid sequence, tissue, and subcellular distribution
    • Glenney, J. R., Jr., Kindy, M. S., and Zokas, L. (1989) Isolation of a new member of the S100 protein family: amino acid sequence, tissue, and subcellular distribution. J. Cell Biol. 108, 569-578
    • (1989) J. Cell Biol. , vol.108 , pp. 569-578
    • Glenney Jr., J.R.1    Kindy, M.S.2    Zokas, L.3
  • 60
    • 0018584180 scopus 로고
    • Redistribution of intermediate filament subunits during skeletal myogenesis and maturation in vitro
    • Bennet, G. S., Fellini, S. A., Toyama, Y., and Holtzer, H. (1979) Redistribution of intermediate filament subunits during skeletal myogenesis and maturation in vitro. J. Cell Biol. 82, 577-584
    • (1979) J. Cell Biol. , vol.82 , pp. 577-584
    • Bennet, G.S.1    Fellini, S.A.2    Toyama, Y.3    Holtzer, H.4
  • 61
    • 0018840795 scopus 로고
    • The sinthesys and distribution of desmin and vimentin during myogenesis in vitro
    • Card, D. L., and Lazarides, E. (1980) The sinthesys and distribution of desmin and vimentin during myogenesis in vitro. Cell 19, 263-275
    • (1980) Cell , vol.19 , pp. 263-275
    • Card, D.L.1    Lazarides, E.2
  • 62
    • 0021264715 scopus 로고
    • Distributions of vimentin and desmin in developing chiuk myotubes in vivo
    • Tokuyasu, K., Maher, P. A., and Singer, S. J. (1984) Distributions of vimentin and desmin in developing chiuk myotubes in vivo. J. Cell Biol. 98, 1961-1972
    • (1984) J. Cell Biol. , vol.98 , pp. 1961-1972
    • Tokuyasu, K.1    Maher, P.A.2    Singer, S.J.3
  • 63
    • 0018842868 scopus 로고
    • Intermediate filaments as mechanical integrators of intercellular spaces
    • Lazandes, E. (1980) Intermediate filaments as mechanical integrators of intercellular spaces. Nature (London) 238, 249-256
    • (1980) Nature (London) , vol.238 , pp. 249-256
    • Lazandes, E.1
  • 64
    • 0028197466 scopus 로고
    • Inhibition of desrmin expression blocks myoblast fusion and interferes with the myogenic regulators myoD and myogenin
    • Li, S. H., Choudhary, S. K., Milner, D. J., Munir, M. I., Kuisk, I. R., and Capetanaki, Y. (1994) Inhibition of desrmin expression blocks myoblast fusion and interferes with the myogenic regulators myoD and myogenin. J. Cell Biol. 124, 827-841
    • (1994) J. Cell Biol. , vol.124 , pp. 827-841
    • Li, S.H.1    Choudhary, S.K.2    Milner, D.J.3    Munir, M.I.4    Kuisk, I.R.5    Capetanaki, Y.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.