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Volumn 86, Issue 5, 2004, Pages 2993-3008

Structural and Functional Roles of Desmin in Mouse Skeletal Muscle during Passive Deformation

Author keywords

[No Author keywords available]

Indexed keywords

DESMIN; TALIN;

EID: 2142816651     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(04)74349-0     Document Type: Article
Times cited : (114)

References (64)
  • 1
    • 0034947560 scopus 로고    scopus 로고
    • Passive stiffness is increased in soleus muscle of desmin knockout mouse
    • Anderson, J., Z. Li, and F. Goubel. 2001. Passive stiffness is increased in soleus muscle of desmin knockout mouse. Muscle Nerve. 24:1090-1092.
    • (2001) Muscle Nerve , vol.24 , pp. 1090-1092
    • Anderson, J.1    Li, Z.2    Goubel, F.3
  • 2
    • 0014468808 scopus 로고
    • Conformational changes in myocardial nuclei of rats
    • Bloom, S., and P. A. Cancillia. 1969. Conformational changes in myocardial nuclei of rats. Circ. Res. 24:189-196.
    • (1969) Circ. Res. , vol.24 , pp. 189-196
    • Bloom, S.1    Cancillia, P.A.2
  • 4
    • 0001024259 scopus 로고
    • Relationship between muscle fiber types and sizes and muscle architectural properties in the mouse hindlimb
    • Burkholder, T. J., B. Fingado, S. Baron, and R. L. Lieber. 1994. Relationship between muscle fiber types and sizes and muscle architectural properties in the mouse hindlimb. J. Morphol. 220:1-14.
    • (1994) J. Morphol. , vol.220 , pp. 1-14
    • Burkholder, T.J.1    Fingado, B.2    Baron, S.3    Lieber, R.L.4
  • 5
    • 0035744938 scopus 로고    scopus 로고
    • Sarcomere length operating range of muscles during movement
    • Burkholder, T. J., and R. L. Lieber. 2001. Sarcomere length operating range of muscles during movement. J. Exp. Biol. 204:1529-1536.
    • (2001) J. Exp. Biol. , vol.204 , pp. 1529-1536
    • Burkholder, T.J.1    Lieber, R.L.2
  • 6
    • 0020162216 scopus 로고
    • The nuclear matrix: Three-dimensional architecture and protein composition
    • Capco, D. G., K. M. Wan, and S. Penman. 1982. The nuclear matrix: three-dimensional architecture and protein composition. Cell. 29:847-858.
    • (1982) Cell , vol.29 , pp. 847-858
    • Capco, D.G.1    Wan, K.M.2    Penman, S.3
  • 7
    • 0030966537 scopus 로고    scopus 로고
    • Desmin in muscle formation an maintenance: Knockouts and consequences
    • Capetanaki, Y., D. J. Milner, and G. Weitzer. 1997. Desmin in muscle formation an maintenance: knockouts and consequences. Cell Struct. Funct. 22:103-116.
    • (1997) Cell Struct. Funct. , vol.22 , pp. 103-116
    • Capetanaki, Y.1    Milner, D.J.2    Weitzer, G.3
  • 8
    • 0023953897 scopus 로고
    • Filamentous cross-bridges link intermediate filaments to the nuclear pore complexes
    • Carmo-Fonseca, M, A. J. Cidadao, and J. F. David-Ferreira. 1988. Filamentous cross-bridges link intermediate filaments to the nuclear pore complexes. Eur. J. Cell. Biol. 45:282-290.
    • (1988) Eur. J. Cell. Biol. , vol.45 , pp. 282-290
    • Carmo-Fonseca, M.1    Cidadao, A.J.2    David-Ferreira, J.F.3
  • 9
    • 0025669849 scopus 로고
    • Interactions of intermediate filaments with cell structures
    • Carmo-Fonseca, M., and J. F. David-Ferreira. 1990. Interactions of intermediate filaments with cell structures. Electron Microsc. Rev. 3:115-141.
    • (1990) Electron Microsc. Rev. , vol.3 , pp. 115-141
    • Carmo-Fonseca, M.1    David-Ferreira, J.F.2
  • 11
    • 0033553877 scopus 로고    scopus 로고
    • Differences in the localization and morphology of chromosomes in the human nucleus
    • Croft, J. A., J. M. Bridger, S. Boyle, P. Perry, P. Teague, and W. A. Bickmore. 1999. Differences in the localization and morphology of chromosomes in the human nucleus. J. Cell Biol. 145:1119-1131.
    • (1999) J. Cell Biol. , vol.145 , pp. 1119-1131
    • Croft, J.A.1    Bridger, J.M.2    Boyle, S.3    Perry, P.4    Teague, P.5    Bickmore, W.A.6
  • 12
    • 0026739841 scopus 로고
    • Costameres are sites of force transmission to the substratum in adult rat cardiomyocytes
    • Danowski, B. A., K. Imanaka-Yoshida, J. M. Sanger, and J. W. Sanger. 1992. Costameres are sites of force transmission to the substratum in adult rat cardiomyocytes. J. Cell Biol. 118:1411-1420.
    • (1992) J. Cell Biol. , vol.118 , pp. 1411-1420
    • Danowski, B.A.1    Imanaka-Yoshida, K.2    Sanger, J.M.3    Sanger, J.W.4
  • 13
    • 0026021706 scopus 로고
    • Network antibodies identify nuclear lamin B as a physiological attachment site for peripherin intermediate filaments
    • Djabali, K., M. M. Porfier, F. Gros, G. Blobel, and S. D. Georgatos. 1991. Network antibodies identify nuclear lamin B as a physiological attachment site for peripherin intermediate filaments. Cell. 64:109-121.
    • (1991) Cell , vol.64 , pp. 109-121
    • Djabali, K.1    Porfier, M.M.2    Gros, F.3    Blobel, G.4    Georgatos, S.D.5
  • 14
    • 0021244964 scopus 로고
    • Epithelial cytoskeletal framework and nuclear matrix-intermediate filament scaffold: Three-dimensional organization and protein composition
    • Fey, E. G., K. M. Wan, and S. Penman. 1984. Epithelial cytoskeletal framework and nuclear matrix-intermediate filament scaffold: three-dimensional organization and protein composition. J. Cell Biol. 98:1973-1984.
    • (1984) J. Cell Biol. , vol.98 , pp. 1973-1984
    • Fey, E.G.1    Wan, K.M.2    Penman, S.3
  • 15
    • 0015167123 scopus 로고
    • Relationship of nuclear membranes with filaments and microtubules
    • Franke, W. W. 1971. Relationship of nuclear membranes with filaments and microtubules. Protoplasma. 73:263-292.
    • (1971) Protoplasma , vol.73 , pp. 263-292
    • Franke, W.W.1
  • 17
    • 0031850337 scopus 로고    scopus 로고
    • Segmental muscle fiber lesions after repetitive eccentric contractions
    • Fridén, J., and R. L. Lieber. 1998. Segmental muscle fiber lesions after repetitive eccentric contractions. Cell Tissue Res. 293:165-171.
    • (1998) Cell Tissue Res. , vol.293 , pp. 165-171
    • Fridén, J.1    Lieber, R.L.2
  • 18
    • 0024487821 scopus 로고
    • Quick-freeze, deep-etch visualization of the nuclear pore complex
    • Fujitani, Y., S. Higaki, H. Sawada, and K. Hirosawa. 1989. Quick-freeze, deep-etch visualization of the nuclear pore complex. Electron Microsc. Rev. 38:34-40.
    • (1989) Electron Microsc. Rev. , vol.38 , pp. 34-40
    • Fujitani, Y.1    Higaki, S.2    Sawada, H.3    Hirosawa, K.4
  • 19
    • 0023371437 scopus 로고
    • Lamin B constitutes an intermediate filament attachment site at the nuclear envelope
    • Georgatos, S. D., and G. Blobel. 1987. Lamin B constitutes an intermediate filament attachment site at the nuclear envelope. J. Cell Biol. 2:117-125.
    • (1987) J. Cell Biol. , vol.2 , pp. 117-125
    • Georgatos, S.D.1    Blobel, G.2
  • 20
    • 0030023118 scopus 로고    scopus 로고
    • Integration of intermediate filaments into cellular organelles
    • Georgatos, S. D., and C. Maison. 1996. Integration of intermediate filaments into cellular organelles. Int. Rev. Cytol. 164:91-138.
    • (1996) Int. Rev. Cytol. , vol.164 , pp. 91-138
    • Georgatos, S.D.1    Maison, C.2
  • 21
    • 0023430563 scopus 로고
    • Binding of two desmin derivatives to the plasma membrane and the nuclear envelope of avian erythrocytes: Evidence for a conserved site-specificity in intermediate filament-membrane interactions
    • Georgatos, S. D., K. Weber, N. Geisler, and G. Blobel. 1987. Binding of two desmin derivatives to the plasma membrane and the nuclear envelope of avian erythrocytes: evidence for a conserved site-specificity in intermediate filament-membrane interactions. Proc. Natl. Acad. Sci. USA. 84:6780-6784.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 6780-6784
    • Georgatos, S.D.1    Weber, K.2    Geisler, N.3    Blobel, G.4
  • 22
    • 0022272935 scopus 로고
    • Intermediate filaments: Possible functions as cytoskeletal connecting links between the nucleus and the cell surface
    • Goldman, R., A. Goldman, K. Green, J. Jones, N. Lieska, and H. Y. Yang. 1985. Intermediate filaments: possible functions as cytoskeletal connecting links between the nucleus and the cell surface. Ann. N. Y. Acad Sci. 455:1-17.
    • (1985) Ann. N. Y. Acad Sci. , vol.455 , pp. 1-17
    • Goldman, R.1    Goldman, A.2    Green, K.3    Jones, J.4    Lieska, N.5    Yang, H.Y.6
  • 23
    • 0017412670 scopus 로고
    • Swelling of skinned muscle fibers of the frog. Experimental observations
    • Godt, R. E., and D. W. Maughan. 1977. Swelling of skinned muscle fibers of the frog. Experimental observations. Biophys. J. 19:103-116.
    • (1977) Biophys. J. , vol.19 , pp. 103-116
    • Godt, R.E.1    Maughan, D.W.2
  • 24
    • 0028332180 scopus 로고
    • Age-related changes in collagen gene expression in the muscles of mdx dystrophic and normal mice
    • Goldspink, G., K. Femandes, P. E. Williams, and D. J. Wells. 1994. Age-related changes in collagen gene expression in the muscles of mdx dystrophic and normal mice. Neuromuscul. Disord. 4:183-191.
    • (1994) Neuromuscul. Disord. , vol.4 , pp. 183-191
    • Goldspink, G.1    Femandes, K.2    Williams, P.E.3    Wells, D.J.4
  • 25
    • 0018571673 scopus 로고
    • Desmin and vimentin coexist at the periphery of the myofibril Z disc
    • Granger, B. L., and E. Lazarides. 1979. Desmin and vimentin coexist at the periphery of the myofibril Z disc. Cell. 18:1053-1063.
    • (1979) Cell , vol.18 , pp. 1053-1063
    • Granger, B.L.1    Lazarides, E.2
  • 26
    • 0028957373 scopus 로고
    • Passive tension in cardiac muscle: Contribution of collagen, titib, microtubules, and intermediate filaments
    • Granzier, H., and T. Irving. 1995. Passive tension in cardiac muscle: contribution of collagen, titib, microtubules, and intermediate filaments. Biophys. J. 68:1027-1044.
    • (1995) Biophys. J. , vol.68 , pp. 1027-1044
    • Granzier, H.1    Irving, T.2
  • 27
    • 0015092352 scopus 로고
    • Fractionation of the avian erythrocyte: An ultrastructural study
    • Harris, J. R., and J. N. Brown. 1971. Fractionation of the avian erythrocyte: an ultrastructural study. J. Ultrastruct. Res. 36:8-23.
    • (1971) J. Ultrastruct. Res. , vol.36 , pp. 8-23
    • Harris, J.R.1    Brown, J.N.2
  • 28
    • 0016158719 scopus 로고
    • Rapid degeneration and regeneration of a whole skeletal muscle following treatment with bupivacaine
    • Hall-Craggs, E. C. 1974. Rapid degeneration and regeneration of a whole skeletal muscle following treatment with bupivacaine. Exp. Neurol. 43:349-358.
    • (1974) Exp. Neurol. , vol.43 , pp. 349-358
    • Hall-Craggs, E.C.1
  • 29
    • 0021043896 scopus 로고
    • Immunolocalization of fibronectin and other macromolecules of the intercellular matrix in the striated muscle fiber of the adult rat
    • Hantai, D., J. Gautron, and J. Labat-Robert. 1983. Immunolocalization of fibronectin and other macromolecules of the intercellular matrix in the striated muscle fiber of the adult rat. Coll. Relat. Res. 3:381-391.
    • (1983) Coll. Relat. Res. , vol.3 , pp. 381-391
    • Hantai, D.1    Gautron, J.2    Labat-Robert, J.3
  • 30
    • 0028966575 scopus 로고
    • Regenerative capacity of mdx mouse muscles after repeated applications of myo-necrotic bupivacaine
    • Itagaki, Y., K. Saida, and K. Iwamura. 1995. Regenerative capacity of mdx mouse muscles after repeated applications of myo-necrotic bupivacaine. Acta Neuropathol. 89:380-384.
    • (1995) Acta Neuropathol. , vol.89 , pp. 380-384
    • Itagaki, Y.1    Saida, K.2    Iwamura, K.3
  • 31
    • 0029240501 scopus 로고
    • The mechanical properties of fast and slow skeletal muscles of the mouse in relation to their locomotory function
    • James, R. S., J. D. Altringham, and D. F. Goldspink. 1995. The mechanical properties of fast and slow skeletal muscles of the mouse in relation to their locomotory function. J. Exp. Biol. 196:491-502.
    • (1995) J. Exp. Biol. , vol.196 , pp. 491-502
    • James, R.S.1    Altringham, J.D.2    Goldspink, D.F.3
  • 32
    • 0020451332 scopus 로고
    • Dynamic aspects of the supramolecular organization of intermediate filament networks in cultured epidermal cells
    • Jones, J. C., A. E. Goldman, P. M. Steinert, S. Yuspa, and R. D. Goldman. 1982. Dynamic aspects of the supramolecular organization of intermediate filament networks in cultured epidermal cells. Cell Motil. 2:197-213.
    • (1982) Cell Motil. , vol.2 , pp. 197-213
    • Jones, J.C.1    Goldman, A.E.2    Steinert, P.M.3    Yuspa, S.4    Goldman, R.D.5
  • 33
    • 0023075406 scopus 로고
    • Connections of intermediate filaments with the nuclear lamina and the cell periphery
    • Katsuma, Y., S. H. Swierenga, N. Marceau, and S. W. French. 1987. Connections of intermediate filaments with the nuclear lamina and the cell periphery. Biol. Cell. 59:193-203.
    • (1987) Biol. Cell , vol.59 , pp. 193-203
    • Katsuma, Y.1    Swierenga, S.H.2    Marceau, N.3    French, S.W.4
  • 34
    • 0017883543 scopus 로고
    • Intermediate filaments anchor the nuclei in nuclear monolayers of cultured human fibroblasts
    • Lehto, V. P., I. Virtanen, and P. Kurki. 1978. Intermediate filaments anchor the nuclei in nuclear monolayers of cultured human fibroblasts. Nature. 272:175-177.
    • (1978) Nature , vol.272 , pp. 175-177
    • Lehto, V.P.1    Virtanen, I.2    Kurki, P.3
  • 35
    • 0032429751 scopus 로고    scopus 로고
    • Communication between the cell membrane and the nucleus: Role of protein compartmentalization
    • Lelievre, S. A., and M. J. Bissell. 1998. Communication between the cell membrane and the nucleus: role of protein compartmentalization. J. Cell. Biochem. Suppl. 31:250-263.
    • (1998) J. Cell. Biochem. Suppl. , vol.31 , pp. 250-263
    • Lelievre, S.A.1    Bissell, M.J.2
  • 36
    • 0030879081 scopus 로고    scopus 로고
    • Desmin is essential for the tensile strength and integrity of myofibrils but not for myogenic commitment, differentiation, and fusion of skeletal muscle
    • Li, Z., M. Mericskay, O. Agbulut, G. Butler-Browne, L. Carlsson, L. E. Thornell, C. Babinet, and D. Paulin. 1997. Desmin is essential for the tensile strength and integrity of myofibrils but not for myogenic commitment, differentiation, and fusion of skeletal muscle. J. Cell Biol. 139:129-144.
    • (1997) J. Cell Biol. , vol.139 , pp. 129-144
    • Li, Z.1    Mericskay, M.2    Agbulut, O.3    Butler-Browne, G.4    Carlsson, L.5    Thornell, L.E.6    Babinet, C.7    Paulin, D.8
  • 37
    • 0021271648 scopus 로고
    • Sarcomere length determination using laser diffraction. Effect of beam and fiber diameter
    • Lieber, R. L., Y. Yeh, and R. J. Baskin. 1984. Sarcomere length determination using laser diffraction. Effect of beam and fiber diameter. Biophys. J. 45:1007-1016.
    • (1984) Biophys. J. , vol.45 , pp. 1007-1016
    • Lieber, R.L.1    Yeh, Y.2    Baskin, R.J.3
  • 38
    • 0021351251 scopus 로고
    • Characterization of muscle epimysium, perimysium and endomysium collagens
    • Light, N., and A. E. Champion. 1984. Characterization of muscle epimysium, perimysium and endomysium collagens. Biochem. J. 219:1017-1026.
    • (1984) Biochem. J. , vol.219 , pp. 1017-1026
    • Light, N.1    Champion, A.E.2
  • 39
    • 0027262527 scopus 로고
    • Trans-cellular desmin-lamin B intermediate filament network in cardiac myocytes
    • Lockard, V. G., and S. Bloom. 1993. Trans-cellular desmin-lamin B intermediate filament network in cardiac myocytes. J. Mol. Cell Cardiol. 25:303-209.
    • (1993) J. Mol. Cell Cardiol. , vol.25 , pp. 303-209
    • Lockard, V.G.1    Bloom, S.2
  • 40
    • 0031017220 scopus 로고    scopus 로고
    • Demonstration of mechanical connections between integrins, cytoskeletal filaments, and nucleoplasm that stabilize nuclear structure
    • Maniotis, A. J., C. S. Chen, and D. E. Ingber. 1997. Demonstration of mechanical connections between integrins, cytoskeletal filaments, and nucleoplasm that stabilize nuclear structure. Proc. Natl. Acad. Sci. USA. 94:849-854.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 849-854
    • Maniotis, A.J.1    Chen, C.S.2    Ingber, D.E.3
  • 41
    • 0034881439 scopus 로고    scopus 로고
    • The integration of tissue structure and nuclear function
    • Maxwell, C. A., and M. J. Hendzel. 2001. The integration of tissue structure and nuclear function. Biochem. Cell Biol. 79:267-274.
    • (2001) Biochem. Cell Biol. , vol.79 , pp. 267-274
    • Maxwell, C.A.1    Hendzel, M.J.2
  • 42
    • 0034352171 scopus 로고    scopus 로고
    • Integrative models for understanding the structural basis of regional mechanical dysfunction in ischemic myocardium
    • Mazhari, R., and A. D. McCulloch. 2000. Integrative models for understanding the structural basis of regional mechanical dysfunction in ischemic myocardium. Ann. Biomed. Eng. 28:979-990.
    • (2000) Ann. Biomed. Eng. , vol.28 , pp. 979-990
    • Mazhari, R.1    McCulloch, A.D.2
  • 43
    • 0032159228 scopus 로고    scopus 로고
    • Regional myocardial perfusion and mechanics: A model-based method of analysis
    • Mazhari, R., J. H. Omens, L. K. Waldman, and A. D. McCulloch. 1998. Regional myocardial perfusion and mechanics: a model-based method of analysis. Ann. Biomed. Eng. 26:743-755.
    • (1998) Ann. Biomed. Eng. , vol.26 , pp. 743-755
    • Mazhari, R.1    Omens, J.H.2    Waldman, L.K.3    McCulloch, A.D.4
  • 44
    • 0034683573 scopus 로고    scopus 로고
    • Desmin cytoskeleton linked to muscle mitochondrial distribution and respiratory function
    • Milner, D. J., M. Mavroidis, N. Weisleder, and Y. Capetanaki. 2000. Desmin cytoskeleton linked to muscle mitochondrial distribution and respiratory function. J. Cell Biol. 150:1283-1298.
    • (2000) J. Cell Biol. , vol.150 , pp. 1283-1298
    • Milner, D.J.1    Mavroidis, M.2    Weisleder, N.3    Capetanaki, Y.4
  • 45
    • 0029738727 scopus 로고    scopus 로고
    • Disruption of muscle architecture and myocardial degeneration in mice lacking desmin
    • Milner, D. J., G. Weitzer, D. Tran, A. Bradley, and Y. Capetanaki. 1996. Disruption of muscle architecture and myocardial degeneration in mice lacking desmin. J. Cell Biol. 134:1255-1270.
    • (1996) J. Cell Biol. , vol.134 , pp. 1255-1270
    • Milner, D.J.1    Weitzer, G.2    Tran, D.3    Bradley, A.4    Capetanaki, Y.5
  • 46
    • 0029990461 scopus 로고    scopus 로고
    • Immunolocalization of the costameres in human skeletal muscle fibers: Confocal scanning laser microscope investigations
    • Mondello, M. R., P. Bramanti, G. Cutroneo, G. Santoro, D. Di Mauro, and G. Anastasi. 1996. Immunolocalization of the costameres in human skeletal muscle fibers: confocal scanning laser microscope investigations. Anat. Rec. 245:481-487.
    • (1996) Anat. Rec. , vol.245 , pp. 481-487
    • Mondello, M.R.1    Bramanti, P.2    Cutroneo, G.3    Santoro, G.4    Di Mauro, D.5    Anastasi, G.6
  • 47
    • 0036320665 scopus 로고    scopus 로고
    • Sarcolemmal organization in skeletal muscle lacking desmin: Evidence for cytokeratins associated with the membrane skeleton at costameres
    • O'Neill, A., M. W. Williams, W. G. Resneck, D. J. Milner, Y. Capetanaki, and R. J. Bloch. 2002. Sarcolemmal organization in skeletal muscle lacking desmin: evidence for cytokeratins associated with the membrane skeleton at costameres. Mol. Biol. Cell. 13:2347-2359.
    • (2002) Mol. Biol. Cell , vol.13 , pp. 2347-2359
    • O'Neill, A.1    Williams, M.W.2    Resneck, W.G.3    Milner, D.J.4    Capetanaki, Y.5    Bloch, R.J.6
  • 48
    • 0025747945 scopus 로고
    • The "lamin B-fold". Anti-idiotypic antibodies reveal a structural complementarity between nuclear lamin B and cytoplasmic intermediate filament epitopes
    • Papamarcaki, T., P. D. Kouklis, T. E. Kreis, and S. D. Georgatos. 1991. The "lamin B-fold". Anti-idiotypic antibodies reveal a structural complementarity between nuclear lamin B and cytoplasmic intermediate filament epitopes. J. Biol. Chem. 266:21247-21251.
    • (1991) J. Biol. Chem. , vol.266 , pp. 21247-21251
    • Papamarcaki, T.1    Kouklis, P.D.2    Kreis, T.E.3    Georgatos, S.D.4
  • 49
    • 0020506125 scopus 로고
    • Vinculin is a component of an extensive network of myofibril-sarcolemma attachment regions in cardiac muscle fibers
    • Pardo, J. V., J. D. Siliciano, and S. W. Craig. 1983a. Vinculin is a component of an extensive network of myofibril-sarcolemma attachment regions in cardiac muscle fibers. J. Cell Biol. 97:1081-1088.
    • (1983) J. Cell Biol. , vol.97 , pp. 1081-1088
    • Pardo, J.V.1    Siliciano, J.D.2    Craig, S.W.3
  • 50
    • 0010935732 scopus 로고
    • A vinculin-containing cortical lattice in skeletal muscle: Transverse lattice elements ("costameres") mark sites of Attachment between myofibrils and sarcolemma
    • Pardo, J. V., J. D. Siliciano, and S. W. Craig. 1983b. A vinculin-containing cortical lattice in skeletal muscle: transverse lattice elements ("costameres") mark sites of attachment between myofibrils and sarcolemma. Proc. Natl. Acad. Sci. USA. 80:1008-1012.
    • (1983) Proc. Natl. Acad. Sci. USA , vol.80 , pp. 1008-1012
    • Pardo, J.V.1    Siliciano, J.D.2    Craig, S.W.3
  • 51
    • 0019841086 scopus 로고
    • Immunoelectron and immunofluorescence localization of desmin in mature avian muscles
    • Richardson, F. L., M. H. Stromer, T. W. Huiatt, and R. M. Robson. 1981. Immunoelectron and immunofluorescence localization of desmin in mature avian muscles. Eur. J. Cell Biol. 26:91-101.
    • (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
  • 52
    • 0033679588 scopus 로고    scopus 로고
    • Desmin knockout muscles generate lower stress and are less vulnerable to injury compared to wildtype muscles
    • Sam, M., S. Shah, S. Fridén, D. J. Milner, Y. Capetanaki, and R. L. Lieber. 2000. Desmin knockout muscles generate lower stress and are less vulnerable to injury compared to wildtype muscles. Am. J. Physiol. 279: C1116-C1122.
    • (2000) Am. J. Physiol. , vol.279
    • Sam, M.1    Shah, S.2    Fridén, S.3    Milner, D.J.4    Capetanaki, Y.5    Lieber, R.L.6
  • 53
    • 0036324480 scopus 로고    scopus 로고
    • Evidence for increased mobility of myofibrils in desmin null skeletal muscles
    • Shah, S., J. Fridén, F.-C. Su, D. J. Milner, Y. Capetanaki, and R. L. Lieber. 2002. Evidence for increased mobility of myofibrils in desmin null skeletal muscles. J. Exp. Biol. 205:321-325.
    • (2002) J. Exp. Biol. , vol.205 , pp. 321-325
    • Shah, S.1    Fridén, J.2    Su, F.-C.3    Milner, D.J.4    Capetanaki, Y.5    Lieber, R.L.6
  • 54
    • 0037252444 scopus 로고    scopus 로고
    • Real-time imaging and mechanical measurement of muscle cytoskeletal proteins
    • Shah, S., and R. L. Lieber. 2003. Real-time imaging and mechanical measurement of muscle cytoskeletal proteins. J. Histochem. Cytochem. 51:19-29.
    • (2003) J. Histochem. Cytochem. , vol.51 , pp. 19-29
    • Shah, S.1    Lieber, R.L.2
  • 55
    • 0003482279 scopus 로고
    • London, England. Longman Group Limited
    • Spencer, A. J. M. Continuum Mechanics, London, England. Longman Group Limited, 1980.
    • (1980) Continuum Mechanics
    • Spencer, A.J.M.1
  • 57
    • 0031830805 scopus 로고    scopus 로고
    • Interrelationships of nuclear structure and transcriptional control: Functional consequences of being in the right place at the right time
    • Stein, G. S., A. J. van Wijnen, J. L. Stein, J. B. Lian, S. Pockwinse, and S. McNeil. 1998. Interrelationships of nuclear structure and transcriptional control: functional consequences of being in the right place at the right time. J. Cell. Biochem. 70:200-212.
    • (1998) J. Cell. Biochem. , vol.70 , pp. 200-212
    • Stein, G.S.1    Van Wijnen, A.J.2    Stein, J.L.3    Lian, J.B.4    Pockwinse, S.5    McNeil, S.6
  • 58
    • 0028845066 scopus 로고
    • Dystrophin-glycoprotein complex: Molecular organization and critical roles in skeletal muscle
    • Sunada, Y., and K. P. Campbell. 1995. Dystrophin-glycoprotein complex: molecular organization and critical roles in skeletal muscle. Curr. Opin. Neurol. 8:379-384.
    • (1995) Curr. Opin. Neurol. , vol.8 , pp. 379-384
    • Sunada, Y.1    Campbell, K.P.2
  • 60
    • 0020955372 scopus 로고
    • Immunoelectron microscopic studies of desmin (skeletin) localization and intermediate filament organization in chicken skeletal muscle
    • Tokuyasu, K. T., A. H. Dutton, and S. J. Singer. 1983. Immunoelectron microscopic studies of desmin (skeletin) localization and intermediate filament organization in chicken skeletal muscle. J. Cell Biol. 96:1727-1735.
    • (1983) J. Cell Biol. , vol.96 , pp. 1727-1735
    • Tokuyasu, K.T.1    Dutton, A.H.2    Singer, S.J.3
  • 61
    • 0027189534 scopus 로고
    • Viscoelasticity of the sarcomere matrix of skeletal muscles. The titin-myosin composite filament is a dual-stage molecular spring
    • Wang, K., R. McCarter, J. Wright, J. Beverly, and R. Ramirez-Mitchell. 1993. Viscoelasticity of the sarcomere matrix of skeletal muscles. The titin-myosin composite filament is a dual-stage molecular spring. Biophys. J. 64:1161-1177.
    • (1993) Biophys. J. , vol.64 , pp. 1161-1177
    • Wang, K.1    McCarter, R.2    Wright, J.3    Beverly, J.4    Ramirez-Mitchell, R.5
  • 62
    • 0020639339 scopus 로고
    • A network of transverse and longitudinal intermediate filaments is associated with sarcomeres of adult vertebrate skeletal muscle
    • Wang, K., and R. Ramirez-Mitchell. 1983. A network of transverse and longitudinal intermediate filaments is associated with sarcomeres of adult vertebrate skeletal muscle. J. Cell Biol. 96:562-570.
    • (1983) J. Cell Biol. , vol.96 , pp. 562-570
    • Wang, K.1    Ramirez-Mitchell, R.2
  • 63
    • 0024790391 scopus 로고
    • UntrastructuraI analysis of cytoplasmic intermediate filaments and the nuclear lamina in the mouse plasmacytoma cell line MPC-11 after the induction of vimentin synthesis
    • Wang, X., J. Willingale-Theune, R. L. Shoeman, G. Giese, and P. Traub. 1989. UntrastructuraI 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. 50:462-474.
    • (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
  • 64
    • 0019312094 scopus 로고
    • Nucleus-associated intermediate filaments from chicken erythrocytes
    • Woodcock, C. L. 1980. Nucleus-associated intermediate filaments from chicken erythrocytes. J. Cell Biol. 85:881-889.
    • (1980) J. Cell Biol. , vol.85 , pp. 881-889
    • Woodcock, C.L.1


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