메뉴 건너뛰기




Volumn 2004, Issue 78, 2004, Pages 721-755

Plectin

Author keywords

[No Author keywords available]

Indexed keywords

ANTIBODY; INTERMEDIATE FILAMENT PROTEIN; ISOPROTEIN; PLEC1 PROTEIN, HUMAN; PLEC1 PROTEIN, MOUSE; PLEC1 PROTEIN, RAT; PLECTIN; RECOMBINANT PROTEIN; RIBONUCLEASE;

EID: 14244268623     PISSN: 0091679X     EISSN: None     Source Type: Book Series    
DOI: 10.1016/s0091-679x(04)78025-5     Document Type: Review
Times cited : (35)

References (98)
  • 1
    • 0030721040 scopus 로고    scopus 로고
    • Targeted inactivation of plectin reveals essential function in maintaining the integrity of skin, muscle, and heart cytoarchitecture
    • Andrä, K., Lassmann, H., Bittner, R., Shorny, S., Fässler, R., Propst, F., and Wiche, G. (1997). Targeted inactivation of plectin reveals essential function in maintaining the integrity of skin, muscle, and heart cytoarchitecture. Genes Dev. 11, 3143-3156.
    • (1997) Genes Dev. , vol.11 , pp. 3143-3156
    • Andrä, K.1    Lassmann, H.2    Bittner, R.3    Shorny, S.4    Fässler, R.5    Propst, F.6    Wiche, G.7
  • 2
    • 0032213892 scopus 로고    scopus 로고
    • Not just scaffolding: Plectin regulates actin dynamics in cultured cells
    • Andrä, K., Nikolic, B., Stöcher, M., Drenckhahn, D., and Wiche, G. (1998). Not just scaffolding: Plectin regulates actin dynamics in cultured cells. Genes Dev. 12, 3442-3451.
    • (1998) Genes Dev. , vol.12 , pp. 3442-3451
    • Andrä, K.1    Nikolic, B.2    Stöcher, M.3    Drenckhahn, D.4    Wiche, G.5
  • 4
    • 0035134083 scopus 로고    scopus 로고
    • A compound heterozygous one amino-acid insertion/nonsense mutation in the plectin gene causes epidermolysis bullosa simplex with plectin deficiency
    • Bauer, J. W., Rouan, F., Kofler, B., Rezniczek, G. A., Kornacker, I., Muss, W., Hametner, R., Klausegger, A., Huber, A., Pohla-Gubo, G., et al. (2001). A compound heterozygous one amino-acid insertion/nonsense mutation in the plectin gene causes epidermolysis bullosa simplex with plectin deficiency. Am. J. Pathol. 158, 617-625.
    • (2001) Am. J. Pathol. , vol.158 , pp. 617-625
    • Bauer, J.W.1    Rouan, F.2    Kofler, B.3    Rezniczek, G.A.4    Kornacker, I.5    Muss, W.6    Hametner, R.7    Klausegger, A.8    Huber, A.9    Pohla-Gubo, G.10
  • 6
    • 0030310645 scopus 로고    scopus 로고
    • Cytoskeleton architecture of C6 rat glioma cell subclones whole mount electron microscopy and immunogold labeling
    • Bohn, W., Etzrodt, D., Foisner, R., Wiche, G., and Traub, P. (1996). Cytoskeleton architecture of C6 rat glioma cell subclones whole mount electron microscopy and immunogold labeling. Scanning Microsc. Suppl. 10, 285-293.
    • (1996) Scanning Microsc. Suppl. , vol.10 , pp. 285-293
    • Bohn, W.1    Etzrodt, D.2    Foisner, R.3    Wiche, G.4    Traub, P.5
  • 7
    • 0035879352 scopus 로고    scopus 로고
    • Cutting edge: Integration of human T lymphocyte cytoskeleton by the cytolinker plectin
    • Brown, M. J., Hallam, J. A., Liu, Y., Yamada, K. M., and Shaw, S. (2001). Cutting edge: Integration of human T lymphocyte cytoskeleton by the cytolinker plectin. J. Immunol. 167, 641-645.
    • (2001) J. Immunol. , vol.167 , pp. 641-645
    • Brown, M.J.1    Hallam, J.A.2    Liu, Y.3    Yamada, K.M.4    Shaw, S.5
  • 8
    • 0346363880 scopus 로고    scopus 로고
    • Identification of a lethal form of epidermolysis bullosa simplex associated with a homozygous genetic mutation in plectin
    • Charlesworth, A., Gagnoux-Palacios, L., Bonduelle, M., Ortonne, J. P., De Raeve, L., and Meneguzzi, G. (2003). Identification of a lethal form of epidermolysis bullosa simplex associated with a homozygous genetic mutation in plectin. J. Invest. Dermatol. 121, 1344-1348.
    • (2003) J. Invest. Dermatol. , vol.121 , pp. 1344-1348
    • Charlesworth, A.1    Gagnoux-Palacios, L.2    Bonduelle, M.3    Ortonne, J.P.4    De Raeve, L.5    Meneguzzi, G.6
  • 9
    • 0029811246 scopus 로고    scopus 로고
    • A homozygous nonsense mutation in the PLEC1 gene in patients with epidermolysis bullosa simplex with muscular dystrophy
    • Chavanas, S., Pulkkinen, L., Gache, Y., Smith, F. J., McLean, W. H., Uitto, J., Ortonne, J. P., and Meneguzzi, G. (1996). A homozygous nonsense mutation in the PLEC1 gene in patients with epidermolysis bullosa simplex with muscular dystrophy. J. Clin. Invest. 98, 2196-2200.
    • (1996) J. Clin. Invest. , vol.98 , pp. 2196-2200
    • Chavanas, S.1    Pulkkinen, L.2    Gache, Y.3    Smith, F.J.4    McLean, W.H.5    Uitto, J.6    Ortonne, J.P.7    Meneguzzi, G.8
  • 10
    • 0036316492 scopus 로고    scopus 로고
    • Structures of two intermediate filament-binding fragments of desmoplakin reveal a unique repeat motif structure
    • Choi, H. J., Park-Snyder, S., Pascoe, L. T., Green, K. J., and Weis, W. I. (2002). Structures of two intermediate filament-binding fragments of desmoplakin reveal a unique repeat motif structure. Nat. Struct. Biol. 9, 612-620.
    • (2002) Nat. Struct. Biol. , vol.9 , pp. 612-620
    • Choi, H.J.1    Park-Snyder, S.2    Pascoe, L.T.3    Green, K.J.4    Weis, W.I.5
  • 12
    • 0030906239 scopus 로고    scopus 로고
    • Polarisation-dependent association of plectin with desmoplakin and the lateral submembrane skeleton in MDCK cells
    • Eger, A., Stockinger, A., Wiche, G., and Foisner, R. (1997). Polarisation-dependent association of plectin with desmoplakin and the lateral submembrane skeleton in MDCK cells. J. Cell Sci. 110, 1307-1316.
    • (1997) J. Cell Sci. , vol.110 , pp. 1307-1316
    • Eger, A.1    Stockinger, A.2    Wiche, G.3    Foisner, R.4
  • 13
    • 0031570308 scopus 로고    scopus 로고
    • Plectin transcript diversity: Identification and tissue distribution of variants with distinct first coding exons and rodless isoforms
    • Elliott, C. E., Becker, B., Oehler, S., Castanon, M. J., Hauptmann, R., and Wiche, G. (1997). Plectin transcript diversity: Identification and tissue distribution of variants with distinct first coding exons and rodless isoforms. Genomics 42, 115-125.
    • (1997) Genomics , vol.42 , pp. 115-125
    • Elliott, C.E.1    Becker, B.2    Oehler, S.3    Castanon, M.J.4    Hauptmann, R.5    Wiche, G.6
  • 14
    • 0028326917 scopus 로고
    • Distribution of plectin, an intermediate filament-associated protein, in the adult rat central nervous system
    • Errante, L. D., Wiche, G., and Shaw, G. (1994). Distribution of plectin, an intermediate filament-associated protein, in the adult rat central nervous system. J. Neurosci. Res. 37, 515-528.
    • (1994) J. Neurosci. Res. , vol.37 , pp. 515-528
    • Errante, L.D.1    Wiche, G.2    Shaw, G.3
  • 15
    • 0023645941 scopus 로고
    • Structure and hydrodynamic properties of plectin molecules
    • Foisner, R., and Wiche, G. (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
  • 16
    • 0023840076 scopus 로고
    • Cytoskeleton-associated plectin: In situ localization, in vitro reconstitution, and binding to immobilized intermediate filament proteins
    • Foisner, R., Leichtfried, F. E., Herrmann, H., Small, J. V., Lawson, D., and Wiche, G. (1988). Cytoskeleton-associated plectin: In situ localization, in vitro reconstitution, and binding to immobilized intermediate filament proteins. J. Cell Biol. 106, 723-733.
    • (1988) J. Cell Biol. , vol.106 , pp. 723-733
    • Foisner, R.1    Leichtfried, F.E.2    Herrmann, H.3    Small, J.V.4    Lawson, D.5    Wiche, G.6
  • 17
    • 0026032167 scopus 로고
    • Monoclonal antibody mapping of structural and functional plectin epitopes
    • Foisner, R., Feldman, B., Sander, L., and Wiche, G. (1991a). 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
    • 0025797361 scopus 로고
    • Protein kinase A- and protein kinase C-regulated interaction of plectin with lamin B and vimentin
    • Foisner, R., Traub, P., and Wiche, G. (1991b). 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
  • 19
    • 0028578649 scopus 로고
    • A panel of monoclonal antibodies to rat plectin: Distinction by epitope mapping and immunoreactivity with different tissues and cell lines
    • Foisner, R., Feldman, B., Sander, L., Seifert, G., Artlieb, U., and Wiche, G. (1994). A panel of monoclonal antibodies to rat plectin: Distinction by epitope mapping and immunoreactivity with different tissues and cell lines. Acta Histochem. 96, 421-438.
    • (1994) Acta Histochem. , vol.96 , pp. 421-438
    • Foisner, R.1    Feldman, B.2    Sander, L.3    Seifert, G.4    Artlieb, U.5    Wiche, G.6
  • 20
    • 0029620499 scopus 로고
    • Distribution and ultrastructure of plectin arrays in subclones of rat glioma C6 cells differing in intermediate filament protein (vimentin) expression
    • Foisner, R., Bohn, W., Mannweiler, K., and Wiche, G. (1995). Distribution and ultrastructure of plectin arrays in subclones of rat glioma C6 cells differing in intermediate filament protein (vimentin) expression. J. Struct. Biol. 115, 304-317.
    • (1995) J. Struct. Biol. , vol.115 , pp. 304-317
    • Foisner, R.1    Bohn, W.2    Mannweiler, K.3    Wiche, G.4
  • 21
    • 0030020359 scopus 로고    scopus 로고
    • M-phase-specific phosphorylation and structural rearrangement of the cytoplasmic cross-linking protein plectin involve p34cdc2 kinase
    • Foisner, R., Malecz, N., Dressel, N., Stadler, C., and Wiche, G. (1996). M-phase-specific phosphorylation and structural rearrangement of the cytoplasmic cross-linking protein plectin involve p34cdc2 kinase. Mol. Biol. Cell 7, 273-288.
    • (1996) Mol. Biol. Cell , vol.7 , pp. 273-288
    • Foisner, R.1    Malecz, N.2    Dressel, N.3    Stadler, C.4    Wiche, G.5
  • 22
    • 0034953789 scopus 로고    scopus 로고
    • The interaction of plectin with actin: Evidence for cross-linking of actin filaments by dimerization of the actin-binding domain of plectin
    • Fontao, L., Geerts, D., Kuikman, I., Koster, J., Kramer, D., and Sonnenberg, A. (2001). The interaction of plectin with actin: Evidence for cross-linking of actin filaments by dimerization of the actin-binding domain of plectin. J. Cell Sci. 114, 2065-2076.
    • (2001) J. Cell Sci. , vol.114 , pp. 2065-2076
    • Fontao, L.1    Geerts, D.2    Kuikman, I.3    Koster, J.4    Kramer, D.5    Sonnenberg, A.6
  • 23
    • 0035181987 scopus 로고    scopus 로고
    • Bridging cytoskeletal intersections
    • Fuchs, E., and Karakesisoglou, I. (2001). Bridging cytoskeletal intersections. Genes Dev. 15, 1-14.
    • (2001) Genes Dev. , vol.15 , pp. 1-14
    • Fuchs, E.1    Karakesisoglou, I.2
  • 24
    • 0344462732 scopus 로고    scopus 로고
    • Unusual 5′ transcript complexity of plectin isoforms: Novel tissue-specific exons modulate actin binding activity
    • Fuchs, P., Zörer, M., Rezniczek, G. A., Spazierer, D., Oehler, S., Castanon, M. J., Hauptmann, R., and Wiche, G. (1999). Unusual 5′ transcript complexity of plectin isoforms: Novel tissue-specific exons modulate actin binding activity. Hum. Mol. Genet. 8, 2461-2472.
    • (1999) Hum. Mol. Genet. , vol.8 , pp. 2461-2472
    • Fuchs, P.1    Zörer, M.2    Rezniczek, G.A.3    Spazierer, D.4    Oehler, S.5    Castanon, M.J.6    Hauptmann, R.7    Wiche, G.8
  • 25
    • 33747365079 scopus 로고    scopus 로고
    • Intermediate filament linker proteins: PIectin and BPAG1
    • (W. J. Lennartzand M. D. Lane, eds.). Elsevier, New York, In press
    • Fuchs, P., and Wiche, G. (2004). Intermediate filament linker proteins: PIectin and BPAG1. In "Encyclopedia of Biological Chemistry" (W. J. Lennartzand M. D. Lane, eds.). Elsevier, New York, In press.
    • (2004) Encyclopedia of Biological Chemistry
    • Fuchs, P.1    Wiche, G.2
  • 26
    • 0035918303 scopus 로고    scopus 로고
    • Epiplakin, a novel member of the Plakin family originally identified as a 450-kDa human epidermal autoantigen. Structure and tissue localization
    • Fujiwara, S., Takeo, N., Otani, Y., Parry, D. A., Kunimatsu, M., Lu, R., Sasaki, M., Matsuo, N., Khaleduzzaman, M., and Yoshioka, H. (2001). Epiplakin, a novel member of the Plakin family originally identified as a 450-kDa human epidermal autoantigen. Structure and tissue localization. J. Biol. Chem. 276, 13340-13347.
    • (2001) J. Biol. Chem. , vol.276 , pp. 13340-13347
    • Fujiwara, S.1    Takeo, N.2    Otani, Y.3    Parry, D.A.4    Kunimatsu, M.5    Lu, R.6    Sasaki, M.7    Matsuo, N.8    Khaleduzzaman, M.9    Yoshioka, H.10
  • 28
    • 0141631492 scopus 로고    scopus 로고
    • Structural and functional analysis of the actin binding domain of plectin suggests alternative mechanisms for binding to F-actin and integrin beta4
    • Garcia-Alvarez, B., Bobkov, A., Sonnenberg, A., and de Pereda, J. M. (2003). Structural and functional analysis of the actin binding domain of plectin suggests alternative mechanisms for binding to F-actin and integrin beta4. Structure 11, 615-625.
    • (2003) Structure , vol.11 , pp. 615-625
    • Garcia-Alvarez, B.1    Bobkov, A.2    Sonnenberg, A.3    De Pereda, J.M.4
  • 29
    • 0032589487 scopus 로고    scopus 로고
    • Binding of integrin alpha6beta4 to plectin prevents plectin association with F-actin but does not interfere with intermediate filament binding
    • Geerts, D., Fontao, L., Nievers, M. G., Schaapveld, R. Q., Purkis, P. E., Wheeler, G. N., Lane, E. B., Leigh, I. M., and Sonnenberg, A. (1999). Binding of integrin alpha6beta4 to plectin prevents plectin association with F-actin but does not interfere with intermediate filament binding. J. Cell Biol. 147, 417-434.
    • (1999) J. Cell Biol. , vol.147 , pp. 417-434
    • Geerts, D.1    Fontao, L.2    Nievers, M.G.3    Schaapveld, R.Q.4    Purkis, P.E.5    Wheeler, G.N.6    Lane, E.B.7    Leigh, I.M.8    Sonnenberg, A.9
  • 32
    • 0021053192 scopus 로고
    • Specific in situ phosphorylation of plectin in detergent-resistant cytoskeletons from cultured Chinese hamster ovary cells
    • Herrmann, H., and Wiche, G. (1983). Specific in situ phosphorylation of plectin in detergent-resistant cytoskeletons from cultured Chinese hamster ovary cells. J. Biol. Chem. 258, 14610-14618.
    • (1983) J. Biol. Chem. , vol.258 , pp. 14610-14618
    • Herrmann, H.1    Wiche, G.2
  • 33
    • 0023126564 scopus 로고
    • Plectin and IFAP-300K are homologous proteins binding to microtubule-associated proteins 1 and 2 and to the 240-kilodalton subunit of spectrin
    • Herrmann, H., and Wiche, G. (1987). Plectin and IFAP-300K are homologous proteins binding to microtubule-associated proteins 1 and 2 and to the 240-kilodalton subunit of spectrin. J. Biol. Chem. 262, 1320-1325.
    • (1987) J. Biol. Chem. , vol.262 , pp. 1320-1325
    • Herrmann, H.1    Wiche, G.2
  • 34
    • 0026577999 scopus 로고
    • Identification of a new hemidesmosomal protein, HD1: A major, high molecular mass component of isolated hemidesmosomes
    • Hieda, Y., Nishizawa, Y., Uematsu, J., and Owaribe, K. (1992). Identification of a new hemidesmosomal protein, HD1: A major, high molecular mass component of isolated hemidesmosomes. J. Cell Biol. 116, 1497-1506.
    • (1992) J. Cell Biol. , vol.116 , pp. 1497-1506
    • Hieda, Y.1    Nishizawa, Y.2    Uematsu, J.3    Owaribe, K.4
  • 35
    • 0032899830 scopus 로고    scopus 로고
    • Plectin is a linker of intermediate filaments to Z-discs in skeletal muscle fibers
    • Hijikata, T., Murakami, T., Imamura, M., Fujimaki, N., and Ishikawa, H. (1999). Plectin is a linker of intermediate filaments to Z-discs in skeletal muscle fibers. J. Cell Sci. 112, 867-876.
    • (1999) J. Cell Sci. , vol.112 , pp. 867-876
    • Hijikata, T.1    Murakami, T.2    Imamura, M.3    Fujimaki, N.4    Ishikawa, H.5
  • 36
    • 0037295486 scopus 로고    scopus 로고
    • Plectin tethers desmin intermediate filaments onto subsarcolemmal dense plaques containing dystrophin and vinculin
    • Hijikata, T., Murakami, T., Ishikawa, H., and Yorifuji, H. (2003). Plectin tethers desmin intermediate filaments onto subsarcolemmal dense plaques containing dystrophin and vinculin. Histochem. Cell Biol. 119, 109-123.
    • (2003) Histochem. Cell Biol. , vol.119 , pp. 109-123
    • Hijikata, T.1    Murakami, T.2    Ishikawa, H.3    Yorifuji, H.4
  • 38
    • 0035197616 scopus 로고    scopus 로고
    • Plectin repeats and modules: Strategic cysteines and their presumed impact on cytolinker functions
    • Janda, L., Damborsky, J., Rezniczek, G. A., and Wiche, G. (2001). Plectin repeats and modules: Strategic cysteines and their presumed impact on cytolinker functions. Bioessays 23, 1064-1069.
    • (2001) Bioessays , vol.23 , pp. 1064-1069
    • Janda, L.1    Damborsky, J.2    Rezniczek, G.A.3    Wiche, G.4
  • 39
    • 0343484996 scopus 로고    scopus 로고
    • Plectin immunopositivity appears in the astrocytes in the white matter but not in the gray matter after stab wounds
    • Kalman, M., and Szabo, A. (2000). Plectin immunopositivity appears in the astrocytes in the white matter but not in the gray matter after stab wounds. Brain Res. 857, 291-294.
    • (2000) Brain Res. , vol.857 , pp. 291-294
    • Kalman, M.1    Szabo, A.2
  • 40
    • 0030934281 scopus 로고    scopus 로고
    • Plectin abnormality in epidermolysis bullosa simplex Ogna: Non-responsiveness of basal keratinocytes to some anti-rat plectin antibodies
    • Koss-Harnes, D., Jahnsen, F. L., Wiche, G., Soyland, E., Brandtzaeg, P., and Gedde-Dahl, T., Jr. (1997). Plectin abnormality in epidermolysis bullosa simplex Ogna: Non-responsiveness of basal keratinocytes to some anti-rat plectin antibodies. Exp. Dermatol. 6, 41-48.
    • (1997) Exp. Dermatol. , vol.6 , pp. 41-48
    • Koss-Harnes, D.1    Jahnsen, F.L.2    Wiche, G.3    Soyland, E.4    Brandtzaeg, P.5    Gedde-Dahl Jr., T.6
  • 42
    • 0035670672 scopus 로고    scopus 로고
    • Two different mutations in the cytoplasmic domain of the integrin beta 4 subunit in nonlethal forms of epidermolysis bullosa prevent interaction of beta 4 with plectin
    • Koster, J., Kuikman, I., Kreft, M., and Sonnenberg, A. (2001). Two different mutations in the cytoplasmic domain of the integrin beta 4 subunit in nonlethal forms of epidermolysis bullosa prevent interaction of beta 4 with plectin. J. Invest. Dermatol. 117, 1405-1411.
    • (2001) J. Invest. Dermatol. , vol.117 , pp. 1405-1411
    • Koster, J.1    Kuikman, I.2    Kreft, M.3    Sonnenberg, A.4
  • 43
    • 0037439896 scopus 로고    scopus 로고
    • Analysis of the interactions between BP180, BP230, plectin and the integrin alpha6beta4 important for hemidesmosome assembly
    • Koster, J., Geerts, D., Favre, B., Borradori, L., and Sonnenberg, A. (2003). Analysis of the interactions between BP180, BP230, plectin and the integrin alpha6beta4 important for hemidesmosome assembly. J. Cell Sci. 116, 387-399.
    • (2003) J. Cell Sci. , vol.116 , pp. 387-399
    • Koster, J.1    Geerts, D.2    Favre, B.3    Borradori, L.4    Sonnenberg, A.5
  • 44
    • 1542344031 scopus 로고    scopus 로고
    • Role of binding of plectin to the integrin {beta}4 subunit in the assembly of hemidesmosomes
    • Koster, J., Van Wilpe, S., Kuikman, I., Litjens, S. H., and Sonnenberg, A. (2004). Role of binding of plectin to the integrin {beta}4 subunit in the assembly of hemidesmosomes. Mol. Biol. Cell 15, 1211-1223.
    • (2004) Mol. Biol. Cell , vol.15 , pp. 1211-1223
    • Koster, J.1    Van Wilpe, S.2    Kuikman, I.3    Litjens, S.H.4    Sonnenberg, A.5
  • 45
    • 0021828069 scopus 로고
    • r 300 000-330 000) co-assembling with microtubules from a cultured cell line (rat glioma C6)
    • r 300 000-330 000) co-assembling with microtubules from a cultured cell line (rat glioma C6). Eur. J. Cell Biol. 38, 149-156.
    • (1985) Eur. J. Cell Biol. , vol.38 , pp. 149-156
    • Koszka, C.1    Leichtfried, F.E.2    Wiche, G.3
  • 46
    • 0037144405 scopus 로고    scopus 로고
    • Naringin-sensitive phosphorylation of plectin, a cytoskeletal cross-linking protein, in isolated rat hepatocytes
    • Larsen, A. K., Moller, M. T., Blankson, H., Samari, H. R., Holden, L., and Seglen, P. O. (2002). Naringin-sensitive phosphorylation of plectin, a cytoskeletal cross-linking protein, in isolated rat hepatocytes. J. Biol. Chem. 277, 34826-34835.
    • (2002) J. Biol. Chem. , vol.277 , pp. 34826-34835
    • Larsen, A.K.1    Moller, M.T.2    Blankson, H.3    Samari, H.R.4    Holden, L.5    Seglen, P.O.6
  • 47
    • 0036169110 scopus 로고    scopus 로고
    • Plakins: A family of versatile cytolinker proteins
    • Leung, C. L., Green, K. J., and Liera, R. K. (2002). Plakins: A family of versatile cytolinker proteins. Trends Cell Biol. 12, 37-45.
    • (2002) Trends Cell Biol. , vol.12 , pp. 37-45
    • Leung, C.L.1    Green, K.J.2    Liera, R.K.3
  • 48
    • 0031686709 scopus 로고    scopus 로고
    • Plectin in the human central nervous system: Predominant expression at pia/glia and endothelia/glia interfaces
    • Lie, A. A., Schröder, R., Blümcke, I., Magin, T. M., Wiestler, O. D., and Elger, C. E. (1998). Plectin in the human central nervous system: Predominant expression at pia/glia and endothelia/glia interfaces. Acta Neuropathol. 96, 215-221.
    • (1998) Acta Neuropathol. , vol.96 , pp. 215-221
    • Lie, A.A.1    Schröder, R.2    Blümcke, I.3    Magin, T.M.4    Wiestler, O.D.5    Elger, C.E.6
  • 50
    • 0029961661 scopus 로고    scopus 로고
    • Human plectin: Organization of the gene, sequence analysis, and chromosome localization (8q24)
    • Liu, C. G., Maercker, C., Castanon, M. J., Hauptmann, R., and Wiche, G. (1996). Human plectin: Organization of the gene, sequence analysis, and chromosome localization (8q24). Proc. Natl. Acad. Sci. USA. 93, 4278-4283.
    • (1996) Proc. Natl. Acad. Sci. USA. , vol.93 , pp. 4278-4283
    • Liu, C.G.1    Maercker, C.2    Castanon, M.J.3    Hauptmann, R.4    Wiche, G.5
  • 51
    • 0036385851 scopus 로고    scopus 로고
    • Direct binding of plectin to Fer kinase and negative regulation of its catalytic activity
    • Lunter, P. C., and Wiche, G. (2002). Direct binding of plectin to Fer kinase and negative regulation of its catalytic activity. Biochem. Biophys. Res. Commun. 296, 904-910.
    • (2002) Biochem. Biophys. Res. Commun. , vol.296 , pp. 904-910
    • Lunter, P.C.1    Wiche, G.2
  • 52
    • 0029873478 scopus 로고    scopus 로고
    • Identification of plectin as a substrate of p34cdc2 kinase and mapping of a single phosphorylation site
    • Malecz, N., Foisner, R., Stadler, C., and Wiche, G. (1996). Identification of plectin as a substrate of p34cdc2 kinase and mapping of a single phosphorylation site. J. Biol. Chem. 271, 8203-8208.
    • (1996) J. Biol. Chem. , vol.271 , pp. 8203-8208
    • Malecz, N.1    Foisner, R.2    Stadler, C.3    Wiche, G.4
  • 53
    • 0016774265 scopus 로고
    • Tropomyosin coiled-coil interactions: Evidence for an unstaggered structure
    • McLachlan, A. D., and Stewart, M. (1975). Tropomyosin coiled-coil interactions: Evidence for an unstaggered structure. J. Mol. Biol. 98, 293-304.
    • (1975) J. Mol. Biol. , vol.98 , pp. 293-304
    • McLachlan, A.D.1    Stewart, M.2
  • 55
    • 0029013310 scopus 로고
    • Absence of p53 allows direct immortalization of hematopoietic cells by the myc and raf oncogenes
    • Metz, T., Harris, A. W., and Adams, J. M. (1995). Absence of p53 allows direct immortalization of hematopoietic cells by the myc and raf oncogenes. Cell 82, 29-36.
    • (1995) Cell , vol.82 , pp. 29-36
    • Metz, T.1    Harris, A.W.2    Adams, J.M.3
  • 57
    • 0030820604 scopus 로고    scopus 로고
    • A minimal region on the integrin beta4 subunit that is critical to its localization in hemidesmosomes regulates the distribution of HD1/plectin in COS-7 cells
    • Niessen, C. M., Hulsman, E. H., Oomen, L. C., Kuikman, I., and Sonnenberg, A. (1997). A minimal region on the integrin beta4 subunit that is critical to its localization in hemidesmosomes regulates the distribution of HD1/plectin in COS-7 cells. J. Cell Sci. 110, 1705-1716.
    • (1997) J. Cell Sci. , vol.110 , pp. 1705-1716
    • Niessen, C.M.1    Hulsman, E.H.2    Oomen, L.C.3    Kuikman, I.4    Sonnenberg, A.5
  • 58
    • 0034110936 scopus 로고    scopus 로고
    • Formation of hemidesmosome-like structures in the absence of ligand binding by the (alpha)6(beta)4 integrin requires binding of HD1/plectin to the cytoplasmic domain of the (beta)4 integrin subunit
    • Nievers, M. G., Kuikman, I., Geerts, D., Leigh, I. M., and Sonnenberg, A. (2000). Formation of hemidesmosome-like structures in the absence of ligand binding by the (alpha)6(beta)4 integrin requires binding of HD1/plectin to the cytoplasmic domain of the (beta)4 integrin subunit. J. Cell Sci. 113, 963-973.
    • (2000) J. Cell Sci. , vol.113 , pp. 963-973
    • Nievers, M.G.1    Kuikman, I.2    Geerts, D.3    Leigh, I.M.4    Sonnenberg, A.5
  • 59
    • 10144233447 scopus 로고    scopus 로고
    • Basic amino acid residue cluster within nuclear targeting sequence motif is essential for cytoplasmic plectin-vimentin network junctions
    • Nikolic, B., Mac Nulty, E., Mir, B., and Wiche, G. (1996). Basic amino acid residue cluster within nuclear targeting sequence motif is essential for cytoplasmic plectin-vimentin network junctions. J. Cell Biol. 134, 1455-1467.
    • (1996) J. Cell Biol. , vol.134 , pp. 1455-1467
    • Nikolic, B.1    Mac Nulty, E.2    Mir, B.3    Wiche, G.4
  • 61
    • 2442605590 scopus 로고    scopus 로고
    • Plectin-RACK1 (Receptor for Activated C Kinase 1) scaffolding: A novel mechanism to regulate protein kinase C activity
    • Osmanagic-Myers, S., and Wiche, G. (2004). Plectin-RACK1 (Receptor for Activated C Kinase 1) Scaffolding: A Novel Mechanism to Regulate Protein Kinase C Activity. J. Biol. Chem. 279, 18701-18710.
    • (2004) J. Biol. Chem. , vol.279 , pp. 18701-18710
    • Osmanagic-Myers, S.1    Wiche, G.2
  • 62
    • 0032916947 scopus 로고    scopus 로고
    • Human autoantibodies against HD1/plectin in paraneoplastic pemphigus
    • Proby, C., Fujii, Y., Owaribe, K., Nishikawa, T., and Amagai, M. (1999). Human autoantibodies against HD1/plectin in paraneoplastic pemphigus. J. Invest. Dermatol. 112, 153-156.
    • (1999) J. Invest. Dermatol. , vol.112 , pp. 153-156
    • Proby, C.1    Fujii, Y.2    Owaribe, K.3    Nishikawa, T.4    Amagai, M.5
  • 63
    • 0029798270 scopus 로고    scopus 로고
    • Homozygous deletion mutations in the plectin gene (PLEC1) in patients with epidermolysis bullosa simplex associated with late-onset muscular dystrophy
    • Pulkkinen, L., Smith, F. J., Shimizu, H., Murata, S., Yaoita, H., Hachisuka, H., Nishikawa, T., McLean, W. H., and Uitto, J. (1996). Homozygous deletion mutations in the plectin gene (PLEC1) in patients with epidermolysis bullosa simplex associated with late-onset muscular dystrophy. Hum. Mol. Genet. 5, 1539-1546.
    • (1996) Hum. Mol. Genet. , vol.5 , pp. 1539-1546
    • Pulkkinen, L.1    Smith, F.J.2    Shimizu, H.3    Murata, S.4    Yaoita, H.5    Hachisuka, H.6    Nishikawa, T.7    McLean, W.H.8    Uitto, J.9
  • 64
    • 0019051839 scopus 로고
    • High molecular weight polypeptides (270,000-340,000) from cultured cells are related to hog brain microtubule-associated proteins but copurify with intermediate filaments
    • Pytela, R., and Wiche, G. (1980). High molecular weight polypeptides (270,000-340,000) from cultured cells are related to hog brain microtubule-associated proteins but copurify with intermediate filaments. Proc. Natl. Acad. Sci. USA 77, 4808-4812.
    • (1980) Proc. Natl. Acad. Sci. USA , vol.77 , pp. 4808-4812
    • Pytela, R.1    Wiche, G.2
  • 65
    • 0344462724 scopus 로고    scopus 로고
    • Association of mitochondria with plectin and desmin intermediate filaments in striated muscle
    • Reipert, S., Steinböck, F., Fischer, I., Bittner, R. E., Zeöld, A., and Wiche, G. (1999). Association of mitochondria with plectin and desmin intermediate filaments in striated muscle. Exp. Cell Res. 252, 479-491.
    • (1999) Exp. Cell Res. , vol.252 , pp. 479-491
    • Reipert, S.1    Steinböck, F.2    Fischer, I.3    Bittner, R.E.4    Zeöld, A.5    Wiche, G.6
  • 66
    • 0742286842 scopus 로고    scopus 로고
    • High-pressure freezing of epithelial cells on sapphire coverslips
    • Reipert, S., Fischer, I., and Wiche, G. (2004). High-pressure freezing of epithelial cells on sapphire coverslips. J. Microsc. 213, 81-85.
    • (2004) J. Microsc. , vol.213 , pp. 81-85
    • Reipert, S.1    Fischer, I.2    Wiche, G.3
  • 67
    • 0032489678 scopus 로고    scopus 로고
    • Linking integrin alpha6beta4-based cell adhesion to the intermediate filament cytoskeleton: Direct interaction between the beta4 subunit and plectin at multiple molecular sites
    • Rezniczek, G. A., de Pereda, J. M., Reipert, S., and Wiche, G. (1998). Linking integrin alpha6beta4-based cell adhesion to the intermediate filament cytoskeleton: Direct interaction between the beta4 subunit and plectin at multiple molecular sites. J. Cell Biol. 141, 209-225.
    • (1998) J. Cell Biol. , vol.141 , pp. 209-225
    • Rezniczek, G.A.1    De Pereda, J.M.2    Reipert, S.3    Wiche, G.4
  • 68
    • 0344668724 scopus 로고    scopus 로고
    • Plectin 5′-transcript diversity: Short alternative sequences determine stability of gene products, initiation of translation and subcellular localization of isoforms
    • Rezniczek, G. A., Abrahamsberg, C., Fuchs, P., Spazierer, D., and Wiche, G. (2003). Plectin 5′-transcript diversity: Short alternative sequences determine stability of gene products, initiation of translation and subcellular localization of isoforms. Hum. Mol. Genet. 12, 3181-3194.
    • (2003) Hum. Mol. Genet. , vol.12 , pp. 3181-3194
    • Rezniczek, G.A.1    Abrahamsberg, C.2    Fuchs, P.3    Spazierer, D.4    Wiche, G.5
  • 69
    • 0037112997 scopus 로고    scopus 로고
    • The 'spectraplakins': Cytoskeletal giants with characteristics of both spectrin and plakin families
    • Röper, K., Gregory, S. L., and Brown, N. H. (2002). The 'spectraplakins': Cytoskeletal giants with characteristics of both spectrin and plakin families. J. Cell Sci. 115, 4215-4225.
    • (2002) J. Cell Sci. , vol.115 , pp. 4215-4225
    • Röper, K.1    Gregory, S.L.2    Brown, N.H.3
  • 70
    • 0029741672 scopus 로고    scopus 로고
    • Envoplakin, a novel precursor of the cornified envelope that has homology to desmoplakin
    • Ruhrberg, C., Hajibagheri, M. A., Simon, M., Dooley, T. P., and Watt, F. M. (1996). Envoplakin, a novel precursor of the cornified envelope that has homology to desmoplakin. J. Cell Biol. 134, 715-729.
    • (1996) J. Cell Biol. , vol.134 , pp. 715-729
    • Ruhrberg, C.1    Hajibagheri, M.A.2    Simon, M.3    Dooley, T.P.4    Watt, F.M.5
  • 71
    • 0026052915 scopus 로고
    • Human bullous pemphigoid antigen (BPAG1). Amino acid sequences deduced from cloned cDNAs predict biologically important peptide segments and protein domains
    • Sawamura, D., Li, K., Chu, M. L., and Uitto, J. (1991). Human bullous pemphigoid antigen (BPAG1). Amino acid sequences deduced from cloned cDNAs predict biologically important peptide segments and protein domains. J. Biol. Chem. 266, 17784-17790.
    • (1991) J. Biol. Chem. , vol.266 , pp. 17784-17790
    • Sawamura, D.1    Li, K.2    Chu, M.L.3    Uitto, J.4
  • 74
    • 0342424740 scopus 로고    scopus 로고
    • Association of plectin with Z-discs is a prerequisite for the formation of the intermyofibrillar desmin cytoskeleton
    • Schröder, R., Fürst, D. O., Klasen, C., Reimann, J., Herrmann, H., and van der Ven, P. F. (2000). Association of plectin with Z-discs is a prerequisite for the formation of the intermyofibrillar desmin cytoskeleton. Lab. Invest. 80, 455-464.
    • (2000) Lab. Invest. , vol.80 , pp. 455-464
    • Schröder, R.1    Fürst, D.O.2    Klasen, C.3    Reimann, J.4    Herrmann, H.5    Van Der Ven, P.F.6
  • 76
    • 0026442554 scopus 로고
    • Immunolocalization of the intermediate filament-associated protein plectin at focal contacts and actin stress fibers
    • Seifert, G. J., Lawson, D., and Wiche, G. (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
  • 77
    • 2442675099 scopus 로고    scopus 로고
    • Actin-binding domain of mouse plectin: Crystal structure and binding to vimentin
    • Sevcik, J., Urbanikova, L., Kostan, J., Janda, L., and Wiche, G. (2004). Actin-binding domain of mouse plectin: Crystal structure and binding to vimentin. Eur. J. Biochem. 271, 1873-1884.
    • (2004) Eur. J. Biochem. , vol.271 , pp. 1873-1884
    • Sevcik, J.1    Urbanikova, L.2    Kostan, J.3    Janda, L.4    Wiche, G.5
  • 79
    • 0041355342 scopus 로고    scopus 로고
    • Epiplakin gene analysis in mouse reveals a single exon encoding a 725 kDa protein with expression restricted to epithelial tissues
    • Spazierer, D., Fuchs, P., Pröll, V., Janda, L., Oehler, S., Fischer, I., Hauptmann, R., and Wiche, G. (2003). Epiplakin gene analysis in mouse reveals a single exon encoding a 725 kDa protein with expression restricted to epithelial tissues. J. Biol. Chem. 278, 31657-31666.
    • (2003) J. Biol. Chem. , vol.278 , pp. 31657-31666
    • Spazierer, D.1    Fuchs, P.2    Pröll, V.3    Janda, L.4    Oehler, S.5    Fischer, I.6    Hauptmann, R.7    Wiche, G.8
  • 80
    • 0033927556 scopus 로고    scopus 로고
    • Identification of the cytolinker plectin as a major early in vivo substrate for caspase 8 during CD95- and tumor necrosis factor receptor-mediated apoptosis
    • Stegh, A. H., Herrmann, H., Lampel, S., Weisenberger, D., Andrä, K., Seper, M., Wiche, G., Krammer, P. H., and Peter, M. E. (2000). Identification of the cytolinker plectin as a major early in vivo substrate for caspase 8 during CD95- and tumor necrosis factor receptor-mediated apoptosis. Mol. Cell. Biol. 20, 5665-5679.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 5665-5679
    • Stegh, A.H.1    Herrmann, H.2    Lampel, S.3    Weisenberger, D.4    Andrä, K.5    Seper, M.6    Wiche, G.7    Krammer, P.H.8    Peter, M.E.9
  • 81
    • 0034003558 scopus 로고    scopus 로고
    • Dose-dependent linkage, assembly inhibition and disassembly of vimentin and cytokeratin 5/14 filaments through plectin's intermediate filament-binding domain
    • Steinböck, F. A., Nikolic, B., Coulombe, P. A., Fuchs, E., Traub, P., and Wiche, G. (2000). Dose-dependent linkage, assembly inhibition and disassembly of vimentin and cytokeratin 5/14 filaments through plectin's intermediate filament-binding domain. J. Cell Sci. 113, 483-491.
    • (2000) J. Cell Sci. , vol.113 , pp. 483-491
    • Steinböck, F.A.1    Nikolic, B.2    Coulombe, P.A.3    Fuchs, E.4    Traub, P.5    Wiche, G.6
  • 82
    • 0034303493 scopus 로고    scopus 로고
    • The use of yeast two-hybrid screens in studies of protein:Protein interactions involved in trafficking
    • Stephens, D. J., and Banting, G. (2000). The use of yeast two-hybrid screens in studies of protein:Protein interactions involved in trafficking. Traffic 1, 763-768.
    • (2000) Traffic , vol.1 , pp. 763-768
    • Stephens, D.J.1    Banting, G.2
  • 84
    • 0029805514 scopus 로고    scopus 로고
    • Plectin sidearms mediate interaction of intermediate filaments with microtubules and other components of the cytoskeleton
    • Svitkina, T. M., Verkhovsky, A. B., and Borisy, G. G. (1996). Plectin sidearms mediate interaction of intermediate filaments with microtubules and other components of the cytoskeleton. J. Cell Biol. 135, 991-1007.
    • (1996) J. Cell Biol. , vol.135 , pp. 991-1007
    • Svitkina, T.M.1    Verkhovsky, A.B.2    Borisy, G.G.3
  • 85
    • 0036024528 scopus 로고    scopus 로고
    • Purification, crystallization and preliminary X-ray analysis of the plectin actin-binding domain
    • Urbanikova, L., Janda, L., Popov, A., Wiche, G., and Sevcik, J. (2002). Purification, crystallization and preliminary X-ray analysis of the plectin actin-binding domain. Acta Crystallogr. D Biol. Crystallogr. 58, 1368-1370.
    • (2002) Acta Crystallogr. D Biol. Crystallogr. , vol.58 , pp. 1368-1370
    • Urbanikova, L.1    Janda, L.2    Popov, A.3    Wiche, G.4    Sevcik, J.5
  • 86
    • 0042164507 scopus 로고    scopus 로고
    • Expression of plectin in muscle fibers with cytoarchitectural abnormalities
    • Vita, G., Monici, M. C., Owaribe, K., and Messina, C. (2003). Expression of plectin in muscle fibers with cytoarchitectural abnormalities. Neuromuscul. Disord. 13, 485-492.
    • (2003) Neuromuscul. Disord. , vol.13 , pp. 485-492
    • Vita, G.1    Monici, M.C.2    Owaribe, K.3    Messina, C.4
  • 87
    • 0023657934 scopus 로고
    • Plectin from bovine lenses. Chemical properties, structural analysis and initial identification of interaction partners
    • Weitzer, G., and Wiche, G. (1987). Plectin from bovine lenses. Chemical properties, structural analysis and initial identification of interaction partners. Eur. J. Biochem. 169, 41-52.
    • (1987) Eur. J. Biochem. , vol.169 , pp. 41-52
    • Weitzer, G.1    Wiche, G.2
  • 88
    • 0020326907 scopus 로고
    • Cytoplasmic network arrays demonstrated by immunolocalization using antibodies to a high molecular weight protein present in cytoskeletal preparations from cultured cells
    • Wiche, G., and Baker, M. A. (1982). Cytoplasmic network arrays demonstrated by immunolocalization using antibodies to a high molecular weight protein present in cytoskeletal preparations from cultured cells. Exp. Cell Res. 138, 15-29.
    • (1982) Exp. Cell Res. , vol.138 , pp. 15-29
    • Wiche, G.1    Baker, M.A.2
  • 89
    • 0020329482 scopus 로고
    • Plectin: A high-molecular-weight cytoskeletal polypeptide component that copurifies with intermediate filaments of the vimentin type
    • Wiche, G., Herrmann, H., Leichtfried, F., and Pytela, R. (1982). Plectin: A high-molecular-weight cytoskeletal polypeptide component that copurifies with intermediate filaments of the vimentin type. Cold Spring Harb. Symp. Quant. Biol. 46, 475-482.
    • (1982) Cold Spring Harb. Symp. Quant. Biol. , vol.46 , pp. 475-482
    • Wiche, G.1    Herrmann, H.2    Leichtfried, F.3    Pytela, R.4
  • 90
    • 0020612365 scopus 로고
    • Occurrence and immunolocalization of plectin in tissues
    • Wiche, G., Krepler, R., Artlieb, U., Pytela, R., and Denk, H. (1983). Occurrence and immunolocalization of plectin in tissues. J. Cell Biol. 97, 887-901.
    • (1983) J. Cell Biol. , vol.97 , pp. 887-901
    • Wiche, G.1    Krepler, R.2    Artlieb, U.3    Pytela, R.4    Denk, H.5
  • 91
    • 0021749865 scopus 로고
    • Identification of plectin in different human cell types and immunolocalization at epithelial basal cell surface membranes
    • Wiche, G., Krepler, R., Artlieb, U., Pytela, R., and Aberer, W. (1984). Identification of plectin in different human cell types and immunolocalization at epithelial basal cell surface membranes. Exp. Cell Res. 155, 43-49.
    • (1984) Exp. Cell Res. , vol.155 , pp. 43-49
    • Wiche, G.1    Krepler, R.2    Artlieb, U.3    Pytela, R.4    Aberer, W.5
  • 92
    • 0024329341 scopus 로고
    • Plectin: General overview and appraisal of its potential role as a subunit protein of the cytomatrix
    • Wiche, G. (1989). Plectin: General overview and appraisal 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
  • 93
    • 0026014584 scopus 로고
    • Cloning and sequencing of rat plectin indicates a 466-kD polypeptide chain with a three-domain structure based on a central alpha-helical coiled coil
    • Wiche, G., Becker, B., Luber, K., Weitzer, G., Castanon, M. J., Hauptmann, R., Stratowa, C., and Stewart, M. (1991). Cloning and sequencing of rat plectin indicates a 466-kD polypeptide chain with a three-domain structure based on a central alpha-helical coiled coil. J. Cell Biol. 114, 83-99.
    • (1991) J. Cell Biol. , vol.114 , pp. 83-99
    • Wiche, G.1    Becker, B.2    Luber, K.3    Weitzer, G.4    Castanon, M.J.5    Hauptmann, R.6    Stratowa, C.7    Stewart, M.8
  • 94
    • 0027159977 scopus 로고
    • Expression of plectin mutant cDNA in cultured cells indicates a role of COOH-terminal domain in intermediate filament association
    • Wiche, G., Gromov, D., Donovan, A., Castanon, M. J., and Fuchs, E. (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
  • 95
    • 0031663054 scopus 로고    scopus 로고
    • Role of plectin in cytoskeleton organization and dynamics
    • Wiche, G. (1998). Role of plectin in cytoskeleton organization and dynamics. J. Cell Sci. 111, 2477-2486.
    • (1998) J. Cell Sci. , vol.111 , pp. 2477-2486
    • Wiche, G.1
  • 96
    • 0029982832 scopus 로고    scopus 로고
    • Perinuclear distribution of plectin characterizes visceral epithelial cells of rat glomeruli
    • Yaoita, E., Wiche, G., Yamamoto, T., Kawasaki, K., and Kihara, I. (1996). Perinuclear distribution of plectin characterizes visceral epithelial cells of rat glomeruli. Am. J. Pathol. 149, 319-327.
    • (1996) Am. J. Pathol. , vol.149 , pp. 319-327
    • Yaoita, E.1    Wiche, G.2    Yamamoto, T.3    Kawasaki, K.4    Kihara, I.5
  • 97
    • 0021828068 scopus 로고
    • Morphological integrity of single adult cardiac myocytes isolated by collagenase treatment: Immunolocalization of tubulin, microtubule-associated proteins 1 and 2, plectin, vimentin, and vinculin
    • Zernig, G., and Wiche, G. (1985). Morphological integrity of single adult cardiac myocytes isolated by collagenase treatment: Immunolocalization of tubulin, microtubule-associated proteins 1 and 2, plectin, vimentin, and vinculin. Eur. J. Cell Biol. 38, 113-122.
    • (1985) Eur. J. Cell Biol. , vol.38 , pp. 113-122
    • Zernig, G.1    Wiche, G.2
  • 98
    • 0345874728 scopus 로고    scopus 로고
    • Multiple variable first exons: A mechanism for cell- and tissue-specific gene regulation
    • Zhang, T., Haws, P., and Wu, Q. (2004). Multiple variable first exons: a mechanism for cell- and tissue-specific gene regulation. Genome Res. 14, 79-89.
    • (2004) Genome Res. , vol.14 , pp. 79-89
    • Zhang, T.1    Haws, P.2    Wu, Q.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.