메뉴 건너뛰기




Volumn 135, Issue 4, 1996, Pages 991-1007

Plectin sidearms mediate interaction of intermediate filaments with microtubules and other components of the cytoskeleton

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; GELSOLIN; MYOSIN; VIMENTIN;

EID: 0029805514     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.135.4.991     Document Type: Article
Times cited : (347)

References (60)
  • 1
    • 0026693017 scopus 로고
    • The molecular biology of intermediate filament proteins
    • Albers, K., and E. Fuchs. 1992. The molecular biology of intermediate filament proteins. Int. Rev. Cytol. 134:243-279.
    • (1992) Int. Rev. Cytol. , vol.134 , pp. 243-279
    • Albers, K.1    Fuchs, E.2
  • 2
    • 0023506775 scopus 로고
    • Association of intermediate filaments with vinculin-containing adhesion plaques of fibroblasts
    • Bershadsky, A.D., I.S. Tint, and T.M. Svitkina. 1987. Association of intermediate filaments with vinculin-containing adhesion plaques of fibroblasts. Cell Motil. Cytoskeleton. 8:274-283.
    • (1987) Cell Motil. Cytoskeleton , vol.8 , pp. 274-283
    • Bershadsky, A.D.1    Tint, I.S.2    Svitkina, T.M.3
  • 4
    • 0027378319 scopus 로고
    • Cytoskeleton architecture of C6 glioma cell subclones differing in intermediate filament protein expression
    • Bohn, W., K. Röser, H. Hohenberg, K. Mannweiler, and P. Traub. 1993. Cytoskeleton architecture of C6 glioma cell subclones differing in intermediate filament protein expression. J. Struct. Biol. 111:48-58.
    • (1993) J. Struct. Biol. , vol.111 , pp. 48-58
    • Bohn, W.1    Röser, K.2    Hohenberg, H.3    Mannweiler, K.4    Traub, P.5
  • 5
    • 0021734135 scopus 로고
    • The structure of cytoplasm in directly frozen cultured cells. I. Filamentous meshworks and the cytoplasmic ground substance
    • Bridgman, P.C., and T.S. Reese. 1984. The structure of cytoplasm in directly frozen cultured cells. I. Filamentous meshworks and the cytoplasmic ground substance. J. Cell Biol. 99:1655-1668.
    • (1984) J. Cell Biol. , vol.99 , pp. 1655-1668
    • Bridgman, P.C.1    Reese, T.S.2
  • 6
    • 0001579544 scopus 로고
    • MAP 4
    • J. Hyams and C.W. Lloyd, editors. Wiley & Sons., New York
    • Bulinski, J.C. 1994. MAP 4. In Microtubules. J. Hyams and C.W. Lloyd, editors. Wiley & Sons., New York. 167-182.
    • (1994) Microtubules , pp. 167-182
    • Bulinski, J.C.1
  • 7
    • 0019171148 scopus 로고
    • Microtubule-associated proteins from cultured HeLa cells: Analysis of molecular properties and effects on microtubule polymerization
    • Bulinski, J.C., and G.G. Borisy. 1980. Microtubule-associated proteins from cultured HeLa cells: analysis of molecular properties and effects on microtubule polymerization. J. Biol. Chem. 255:11570-11576.
    • (1980) J. Biol. Chem. , vol.255 , pp. 11570-11576
    • Bulinski, J.C.1    Borisy, G.G.2
  • 8
    • 0024150623 scopus 로고
    • Focal adhesions: Transmembrane junctions between the extracellular matrix and the cytoskeleton
    • Burridge, K., K. Fath., T. Kelly, G. Nuckolls, and C. Turner. 1988. Focal adhesions: transmembrane junctions between the extracellular matrix and the cytoskeleton. Annu. Rev. Cell Biol. 4:487-525.
    • (1988) Annu. Rev. Cell Biol. , vol.4 , pp. 487-525
    • Burridge, K.1    Fath, K.2    Kelly, T.3    Nuckolls, G.4    Turner, C.5
  • 9
  • 10
    • 0027761324 scopus 로고
    • A microtubule-interacting protein in volved in coalignment of vimentin intermediate filaments with microtubules
    • Draberova, E., and P. Draber. 1993. A microtubule-interacting protein in volved in coalignment of vimentin intermediate filaments with microtubules. J. Cell Sci. 106:1263-1273.
    • (1993) J. Cell Sci. , vol.106 , pp. 1263-1273
    • Draberova, E.1    Draber, P.2
  • 11
    • 0028261670 scopus 로고
    • Neurofilament-deficient axons and perikarial aggregates in viable transgenic mice expressing a neurofilament-β-galactosidase fusion protein
    • Eyer, J., and A. Peterson. 1994. Neurofilament-deficient axons and perikarial aggregates in viable transgenic mice expressing a neurofilament-β-galactosidase fusion protein. Neuron. 12:389-405.
    • (1994) Neuron. , vol.12 , pp. 389-405
    • Eyer, J.1    Peterson, A.2
  • 12
    • 0023645941 scopus 로고
    • Structure and hydrodynamic properties of plectin molecules
    • Foisner, R., and G. Wiche. 1987. Structure and hydrodynamic properties of plectin molecules. J. Mol. Biol. 198:515-531.
    • (1987) J. Mol. Biol. , vol.198 , pp. 515-531
    • Foisner, R.1    Wiche, G.2
  • 13
    • 0025903440 scopus 로고
    • Intermediate filament-associated proteins
    • Foisner, R., and G. Wiche. 1991. Intermediate filament-associated proteins. Curr. Opin. Cell Biol. 3:75-81.
    • (1991) Curr. Opin. Cell Biol. , vol.3 , pp. 75-81
    • Foisner, R.1    Wiche, G.2
  • 14
    • 0023840076 scopus 로고
    • Cytoskeleton-associated plectin: In situ localization, in vitro reconstitution, and binding to immobilized intermediate filament proteins
    • Foisner, R., F.E. Leichtfried, H. Herrmann, J.V. Small, D. Lawson, and G. Wiche. 1988. Cytoskeleton-associated plectin: in situ localization, in vitro reconstitution, and binding to immobilized intermediate filament proteins. J. Cell Biol. 106:723-733.
    • (1988) J. Cell Biol. , vol.106 , pp. 723-733
    • Foisner, R.1    Leichtfried, F.E.2    Herrmann, H.3    Small, J.V.4    Lawson, D.5    Wiche, G.6
  • 15
    • 0025797361 scopus 로고
    • Protein kinase A- and protein kinase C-regulated interaction of plectin with lamin B and vimentin
    • Foisner, R., P. Traub, and G. Wiche. 1991a. Protein kinase A- and protein kinase C-regulated interaction of plectin with lamin B and vimentin. Proc. Natl. Acad. Sci. USA. 88:3812-3816.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 3812-3816
    • Foisner, R.1    Traub, P.2    Wiche, G.3
  • 16
    • 0026032167 scopus 로고
    • Monoclonal antibody mapping of structural and functional plectin epitopes
    • Foisner, R., B. Feldman, L. Sander, and G. Wiche. 1991b. Monoclonal antibody mapping of structural and functional plectin epitopes. J. Cell Biol. 112:397-405.
    • (1991) J. Cell Biol. , vol.112 , pp. 397-405
    • Foisner, R.1    Feldman, B.2    Sander, L.3    Wiche, G.4
  • 18
    • 0028287112 scopus 로고
    • Intermediate filaments and disease: Mutations that cripple cell strength
    • Fuchs, E. 1994. Intermediate filaments and disease: mutations that cripple cell strength. J. Cell Biol. 125:511-516.
    • (1994) J. Cell Biol. , vol.125 , pp. 511-516
    • Fuchs, E.1
  • 19
    • 0028283501 scopus 로고
    • Intermediate filaments: Structure, dynamics, function, and disease
    • Fuchs, E., and K. Weber. 1994. Intermediate filaments: structure, dynamics, function, and disease. Annu. Rev. Biochem. 63:345-382.
    • (1994) Annu. Rev. Biochem. , vol.63 , pp. 345-382
    • Fuchs, E.1    Weber, K.2
  • 22
    • 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
  • 23
    • 0022845405 scopus 로고
    • Intermediate filament networks: Organization and possible functions of a diverse group of cytoskeletal elements
    • Goldman, R.D., A.E. Goldman, K.J. Green, J.C.R. Jones, S.M. Jones, and H.-Y. Yang. 1986. Intermediate filament networks: organization and possible functions of a diverse group of cytoskeletal elements. J. Cell Sci. (Suppl). 5:69-97.
    • (1986) J. Cell Sci. (Suppl) , vol.5 , pp. 69-97
    • Goldman, R.D.1    Goldman, A.E.2    Green, K.J.3    Jones, J.C.R.4    Jones, S.M.5    Yang, H.-Y.6
  • 24
    • 0026755162 scopus 로고
    • Comparative structural analysis of desmoplakin, bullous pemphigoid antigen and plectin: Members of a new gene family involved in organization of intermediate filaments
    • Green, K.J., M.L.A. Virata, G.W. Elgart, J.R. Stanley, and D.A.D. Parry. 1992. Comparative structural analysis of desmoplakin, bullous pemphigoid antigen and plectin: members of a new gene family involved in organization of intermediate filaments. Intern. J. Biol. Macromol. 14:145-153.
    • (1992) Intern. J. Biol. Macromol. , vol.14 , pp. 145-153
    • Green, K.J.1    Virata, M.L.A.2    Elgart, G.W.3    Stanley, J.R.4    Parry, D.A.D.5
  • 25
    • 0021752265 scopus 로고
    • Distinct populations of microtubules: Tyrosinated and non-tyrosinated α-tubulin are distributed differently in cells
    • Gundersen, G.G., M.H. Kalonoski, and J.C. Bulinski. 1984. Distinct populations of microtubules: tyrosinated and non-tyrosinated α-tubulin are distributed differently in cells. Cell. 38:779-789.
    • (1984) Cell , vol.38 , pp. 779-789
    • Gundersen, G.G.1    Kalonoski, M.H.2    Bulinski, J.C.3
  • 26
    • 0028883469 scopus 로고
    • Stable, detyrosinated microtubules function to localize vimentin intermediate filaments in fibroblasts
    • Gurland, G., and G.G. Gundersen. 1995. Stable, detyrosinated microtubules function to localize vimentin intermediate filaments in fibroblasts. J. Cell Biol. 131:1275-1290.
    • (1995) J. Cell Biol. , vol.131 , pp. 1275-1290
    • Gurland, G.1    Gundersen, G.G.2
  • 27
    • 0025743437 scopus 로고
    • Coalignment of vimentin intermediate filaments with microtubules depends on kinesin
    • Gyoeva, F.K., and V.I. Gelfand. 1991. Coalignment of vimentin intermediate filaments with microtubules depends on kinesin. Nature (Lond.). 353:445-448.
    • (1991) Nature (Lond.) , vol.353 , pp. 445-448
    • Gyoeva, F.K.1    Gelfand, V.I.2
  • 28
    • 0022406440 scopus 로고
    • Microtubule-associated proteins bind specifically to the 70-kDa neurofilament protein
    • Heiman, R., M. Shelanski, and R.K. Liem. 1985. Microtubule-associated proteins bind specifically to the 70-kDa neurofilament protein. J. Biol. Chem. 260:12160-12166.
    • (1985) J. Biol. Chem. , vol.260 , pp. 12160-12166
    • Heiman, R.1    Shelanski, M.2    Liem, R.K.3
  • 29
    • 0028091403 scopus 로고
    • Making heads and tails of intermediate filament assembly, dynamics and networks
    • Heins, S., and U. Aebi. 1994. Making heads and tails of intermediate filament assembly, dynamics and networks. Curr. Opin. Cell Biol. 6:25-33.
    • (1994) Curr. Opin. Cell Biol. , vol.6 , pp. 25-33
    • Heins, S.1    Aebi, U.2
  • 30
    • 0023126564 scopus 로고
    • Plectin and IFAP-300 are homologous proteins binding to microtubule-associated proteins 1 and 2 and to the 240 kilodalton subunit of spectrin
    • Herrmann, H., and G. Wiche. 1987. Plectin and IFAP-300 are homologous proteins binding to microtubule-associated proteins 1 and 2 and to the 240 kilodalton subunit of spectrin. J. Biol. Chem. 262:1320-1325.
    • (1987) J. Biol. Chem. , vol.262 , pp. 1320-1325
    • Herrmann, H.1    Wiche, G.2
  • 31
    • 0020326774 scopus 로고
    • Cross-linker system between neurofilaments, microtubules and membranous organelles in frog axons revealed by the quick-freeze, deep-etching method
    • Hirokawa, N. 1982. Cross-linker system between neurofilaments, microtubules and membranous organelles in frog axons revealed by the quick-freeze, deep-etching method. J. Cell Biol. 94:129-142.
    • (1982) J. Cell Biol. , vol.94 , pp. 129-142
    • Hirokawa, N.1
  • 32
    • 0023766743 scopus 로고
    • MAP2 is a component of crossbridges between microtubules and neurofilaments in the neuronal cytoskeleton: Quick-freeze, deep-etch immunoelectron microscopy and reconstitution studies
    • Hirokawa, N., S. Hisanaga, and Y. Shiomura. 1988. MAP2 is a component of crossbridges between microtubules and neurofilaments in the neuronal cytoskeleton: quick-freeze, deep-etch immunoelectron microscopy and reconstitution studies. J. Neurosci. 8:2769-2779.
    • (1988) J. Neurosci. , vol.8 , pp. 2769-2779
    • Hirokawa, N.1    Hisanaga, S.2    Shiomura, Y.3
  • 33
    • 0028036369 scopus 로고
    • Membrane interactions with actin cytoskeleton
    • Hitt, A.L., and E.J. Luna. 1994. Membrane interactions with actin cytoskeleton. Curr. Opin. Cell Biol. 6:120-130.
    • (1994) Curr. Opin. Cell Biol. , vol.6 , pp. 120-130
    • Hitt, A.L.1    Luna, E.J.2
  • 34
    • 0014335827 scopus 로고
    • Mitosis and intermediate-sized filaments in developing skeletal muscle
    • Ishikawa, H., R. Bischoff, and H. Holtzer. 1968. Mitosis and intermediate-sized filaments in developing skeletal muscle. J. Cell Biol. 38:538-555.
    • (1968) J. Cell Biol. , vol.38 , pp. 538-555
    • Ishikawa, H.1    Bischoff, R.2    Holtzer, H.3
  • 35
    • 0028967465 scopus 로고
    • Intermediate filaments: New proteins, some answers, more questions
    • Klymkowsky, M.W. 1995. Intermediate filaments: new proteins, some answers, more questions. Curr. Opin. Cell Biol. 7:46-54.
    • (1995) Curr. Opin. Cell Biol. , vol.7 , pp. 46-54
    • Klymkowsky, M.W.1
  • 36
    • 0020365611 scopus 로고
    • Interactions between neurofilaments and microtubule-associated proteins: A possible mechanism for interorganellar bridging
    • Leterrier, J.F., R.K. Liem, and M. Shelanski. 1982. Interactions between neurofilaments and microtubule-associated proteins: a possible mechanism for interorganellar bridging. J. Cell Biol. 95:982-986.
    • (1982) J. Cell Biol. , vol.95 , pp. 982-986
    • Leterrier, J.F.1    Liem, R.K.2    Shelanski, M.3
  • 37
    • 0019436188 scopus 로고
    • Disruption of the in vivo distribution of the intermediate filaments through the microinjection of a specific monoclonal antibody
    • Lin, J. J.-J., and J.R. Feramisco. 1981. Disruption of the in vivo distribution of the intermediate filaments through the microinjection of a specific monoclonal antibody. Cell. 24:185-193.
    • (1981) Cell , vol.24 , pp. 185-193
    • Lin, J.J.-J.1    Feramisco, J.R.2
  • 38
  • 40
    • 0027530064 scopus 로고
    • Neurofilament deficiency in quail caused by nonsense mutation in neurofilament-L gene
    • Ohara, O., Y. Gahara, T. Miyake, H. Teraoka, and T. Kitamura. 1993. Neurofilament deficiency in quail caused by nonsense mutation in neurofilament-L gene. J. Cell Biol. 121:387-395.
    • (1993) J. Cell Biol. , vol.121 , pp. 387-395
    • Ohara, O.1    Gahara, Y.2    Miyake, T.3    Teraoka, H.4    Kitamura, T.5
  • 41
    • 0019051839 scopus 로고
    • High molecular weight polypeptides (270,000-340,000) from cultured cells are related to hog brain microtubule-associated proteins but copurify with intermediate filaments
    • Pytela, R., and G. Wiche. 1980. High molecular weight polypeptides (270,000-340,000) from cultured cells are related to hog brain microtubule-associated proteins but copurify with intermediate filaments. Proc. Natl. Acad. Sci. USA. 77:4808-4812.
    • (1980) Proc. Natl. Acad. Sci. USA , vol.77 , pp. 4808-4812
    • Pytela, R.1    Wiche, G.2
  • 42
    • 0019720977 scopus 로고
    • Structural interaction of cytoskeletal components
    • Schliwa, M., and J. van Blerkom. 1981. Structural interaction of cytoskeletal components. J. Cell Biol. 90:222-235.
    • (1981) J. Cell Biol. , vol.90 , pp. 222-235
    • Schliwa, M.1    Van Blerkom, J.2
  • 43
    • 0028577357 scopus 로고
    • Desmosomes and cytoskeletal architecture in epithelial differentiation: Cell type-specific plaque components and intermediate filament anchorage
    • Schmidt, A., H.W. Heid, S. Schafer, U.A. Nuber, R. Zimbelmann, and W.W. Franke. 1994. Desmosomes and cytoskeletal architecture in epithelial differentiation: cell type-specific plaque components and intermediate filament anchorage. Eur. J. Cell Biol. 65:229-245.
    • (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
  • 44
    • 0026442554 scopus 로고
    • Immunolocalization of the intermediate filament-associated protein plectin at focal contacts and actin stress fibers
    • Seifert, G.J., D. Lawson, and G. Wiche. 1992. Immunolocalization of the intermediate filament-associated protein plectin at focal contacts and actin stress fibers. Eur. J. Cell. Biol. 59:138-147.
    • (1992) Eur. J. Cell. Biol. , vol.59 , pp. 138-147
    • Seifert, G.J.1    Lawson, D.2    Wiche, G.3
  • 46
    • 0021601213 scopus 로고
    • Cytoskeleton of mouse embryo fibroblasts. Electron microscopy of platinum replicas
    • Svitkina, T.M., A.A. Shevelev, A.D. Bershadsky, and V.I. Gelfand. 1984. Cytoskeleton of mouse embryo fibroblasts. Electron microscopy of platinum replicas. Eur. J. Cell Biol. 34:64-74.
    • (1984) Eur. J. Cell Biol. , vol.34 , pp. 64-74
    • Svitkina, T.M.1    Shevelev, A.A.2    Bershadsky, A.D.3    Gelfand, V.I.4
  • 48
    • 0029621142 scopus 로고
    • Improved procedures for electron microscopic visualization of the cytoskeleton of cultured cells
    • Svitkina, T.M., A.B. Verkhovsky, and G.G. Borisy. 1995. Improved procedures for electron microscopic visualization of the cytoskeleton of cultured cells. J. Struct. Biol. 115:290-303.
    • (1995) J. Struct. Biol. , vol.115 , pp. 290-303
    • Svitkina, T.M.1    Verkhovsky, A.B.2    Borisy, G.G.3
  • 50
    • 0026245786 scopus 로고
    • Transmembrane molecular assemblies in cell-extracellular matrix interactions
    • Turner, C.E., and K. Burridge. 1991. Transmembrane molecular assemblies in cell-extracellular matrix interactions. Curr. Opin. Cell Biol. 3:849-853.
    • (1991) Curr. Opin. Cell Biol. , vol.3 , pp. 849-853
    • Turner, C.E.1    Burridge, K.2
  • 51
    • 0023492049 scopus 로고
    • Organization of stress fibers in cultured fibroblasts after extraction of actin with bovine brain gelsolin-like protein
    • Verkhovsky, A.B., I.G. Surgucheva, T.M. Svitkina, I.S. Tint, and V.I. Gelfand. 1987. Organization of stress fibers in cultured fibroblasts after extraction of actin with bovine brain gelsolin-like protein. Exp. Cell Res. 173:244-255.
    • (1987) Exp. Cell Res. , vol.173 , pp. 244-255
    • Verkhovsky, A.B.1    Surgucheva, I.G.2    Svitkina, T.M.3    Tint, I.S.4    Gelfand, V.I.5
  • 52
    • 0027524780 scopus 로고
    • Non-sarcomeric mode of myosin II organization in the fibroblast lamellum
    • Verkhovsky, A.B., and G.G. Borisy. 1993. Non-sarcomeric mode of myosin II organization in the fibroblast lamellum. J. Cell Biol. 123:637-652.
    • (1993) J. Cell Biol. , vol.123 , pp. 637-652
    • Verkhovsky, A.B.1    Borisy, G.G.2
  • 53
    • 0028818253 scopus 로고
    • Myosin II filament assemblies in the active lamella of fibroblasts: Their morphogenesis and role in the formation of actin filament bundles
    • Verkhovsky, A.B., T.M. Svitkina, and G.G. Borisy. 1995.Myosin II filament assemblies in the active lamella of fibroblasts: their morphogenesis and role in the formation of actin filament bundles. J. Cell Biol. 131:989-1002.
    • (1995) J. Cell Biol. , vol.131 , pp. 989-1002
    • Verkhovsky, A.B.1    Svitkina, T.M.2    Borisy, G.G.3
  • 54
    • 0025860352 scopus 로고
    • Analyzing dynamic properties of intermediate filaments
    • Vikstrom, K.L., R.K. Miller, and R.D. Goldman. 1991. Analyzing dynamic properties of intermediate filaments. Methods Enzymol. 196:506-525.
    • (1991) Methods Enzymol. , vol.196 , pp. 506-525
    • Vikstrom, K.L.1    Miller, R.K.2    Goldman, R.D.3
  • 55
    • 0011214518 scopus 로고    scopus 로고
    • Removal of MAP4 from microtubules in vivo produces no observable phenotype at the cellular level
    • Wang, X.-M., J.G. Peloquin, Y. Zhai, J.C. Bulinski, and G.G. Borisy. 1996. Removal of MAP4 from microtubules in vivo produces no observable phenotype at the cellular level. J. Cell Biol. 132:345-357.
    • (1996) J. Cell Biol. , vol.132 , pp. 345-357
    • Wang, X.-M.1    Peloquin, J.G.2    Zhai, Y.3    Bulinski, J.C.4    Borisy, G.G.5
  • 56
    • 0018217063 scopus 로고
    • Three-dimensional electron microscopical visualization of the cytoskeleton of animal cells: Immunoferritin identification of actin- and tubulin-containing structures
    • Webster, R.E., D. Henderson, M. Osborn, and K. Weber. 1978. Three-dimensional electron microscopical visualization of the cytoskeleton of animal cells: immunoferritin identification of actin- and tubulin-containing structures. Proc. Natl. Acad. Sci. USA. 75:5511-5515.
    • (1978) Proc. Natl. Acad. Sci. USA , vol.75 , pp. 5511-5515
    • Webster, R.E.1    Henderson, D.2    Osborn, M.3    Weber, K.4
  • 57
    • 0024329341 scopus 로고
    • Plectin: General overview and appraisals of its potential role as a subunit protein of the cytomatrix
    • Wiche, G. 1989. Plectin: general overview and appraisals of its potential role as a subunit protein of the cytomatrix. Crit. Rev. Biochem. Mol. Biol. 24:41-67.
    • (1989) Crit. Rev. Biochem. Mol. Biol. , vol.24 , pp. 41-67
    • Wiche, G.1
  • 58
    • 0026014584 scopus 로고
    • Cloning and sequencing of rat plectin indicates a 466-kD polypeptide chain with a three-domain structure based on a central α-helical coiled coil
    • Wiche, G., B. Becker, K. Luber, G. Weizer, M.J. Castanon, R. Hauptmann, C. Stratowa, and M. Stewart. 1991. Cloning and sequencing of rat plectin indicates a 466-kD polypeptide chain with a three-domain structure based on a central α-helical coiled coil. J. Cell Biol. 114:83-99.
    • (1991) J. Cell Biol. , vol.114 , pp. 83-99
    • Wiche, G.1    Becker, B.2    Luber, K.3    Weizer, G.4    Castanon, M.J.5    Hauptmann, R.6    Stratowa, C.7    Stewart, M.8
  • 59
    • 0027159977 scopus 로고
    • Expression of plectin mutant cDNA in cultured cells indicates a role of COOH-terminal domain in intermediate filament association
    • Wiche, G., D. Gromov, A. Donovan, M.J. Castanon, and E. Fuchs. 1993. Expression of plectin mutant cDNA in cultured cells indicates a role of COOH-terminal domain in intermediate filament association. J. Cell Biol. 121:607-619.
    • (1993) J. Cell Biol. , vol.121 , pp. 607-619
    • Wiche, G.1    Gromov, D.2    Donovan, A.3    Castanon, M.J.4    Fuchs, E.5
  • 60
    • 0002421880 scopus 로고
    • Intermediate filament-associated proteins
    • R. D. Goldman and P. M. Steinert, editors. Plenum Press, New York
    • Yang, H.-Y., N. Lieska, and R.D. Goldman. 1990. Intermediate filament-associated proteins. In Cellular and Molecular Biology of Intermediate Filaments. R. D. Goldman and P. M. Steinert, editors. Plenum Press, New York. 371-391.
    • (1990) Cellular and Molecular Biology of Intermediate Filaments , pp. 371-391
    • Yang, H.-Y.1    Lieska, N.2    Goldman, R.D.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.