메뉴 건너뛰기




Volumn 134, Issue 3, 1996, Pages 715-729

Envoplakin, a novel precursor of the cornified envelope that has homology to desmoplakin

Author keywords

[No Author keywords available]

Indexed keywords

DESMOPLAKIN;

EID: 0029741672     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.134.3.715     Document Type: Article
Times cited : (153)

References (58)
  • 1
    • 0022484922 scopus 로고
    • Prediction of protein structure
    • Argos, P., and J.K. Rao. 1986. Prediction of protein structure. Methods Enzymol 130:185-207.
    • (1986) Methods Enzymol , vol.130 , pp. 185-207
    • Argos, P.1    Rao, J.K.2
  • 2
    • 0027151802 scopus 로고
    • Stratification-related expression of isoforms of the desmosomal cadherins in human epidermis
    • Arnemann, J., K.H. Sullivan, A.I. Magee, I.A. King, and R.S. Buxton. 1993. Stratification-related expression of isoforms of the desmosomal cadherins in human epidermis. J. Cell Sci. 104:741-750.
    • (1993) J. Cell Sci. , vol.104 , pp. 741-750
    • Arnemann, J.1    Sullivan, K.H.2    Magee, A.I.3    King, I.A.4    Buxton, R.S.5
  • 3
    • 0019822502 scopus 로고
    • Involucrin synthesis and tissue assembly by keratinocytes in natural and cultured human epithelia
    • Banks-Schlegel, S., and H. Green. 1981. Involucrin synthesis and tissue assembly by keratinocytes in natural and cultured human epithelia. J. Cell Biol. 90: 732-737.
    • (1981) J. Cell Biol. , vol.90 , pp. 732-737
    • Banks-Schlegel, S.1    Green, H.2
  • 4
    • 0029035706 scopus 로고
    • The mouse dystonia musculorum gene is a neural isoform of bullous pemphigoid antigen 1
    • Brown, A., G. Bernier, M. Mathieu, J. Rossant, and R. Kothary. 1995. The mouse dystonia musculorum gene is a neural isoform of bullous pemphigoid antigen 1. Nature Genetics. 10:301-306.
    • (1995) Nature Genetics , vol.10 , pp. 301-306
    • Brown, A.1    Bernier, G.2    Mathieu, M.3    Rossant, J.4    Kothary, R.5
  • 5
    • 0024570089 scopus 로고
    • Acylation of keratinocyte transglutaminase by palmitic and myristic acids in the membrane anchorage region
    • Chakravarty, R., and R.H. Rice. 1989. Acylation of keratinocyte transglutaminase by palmitic and myristic acids in the membrane anchorage region. J. Biol. Chem. 264:625-629.
    • (1989) J. Biol. Chem. , vol.264 , pp. 625-629
    • Chakravarty, R.1    Rice, R.H.2
  • 6
    • 0018110116 scopus 로고
    • Prediction of the secondary structure of proteins from their amino acid sequence
    • Chou, P.Y., and G.D. Fasman. 1987. Prediction of the secondary structure of proteins from their amino acid sequence. Adv. Enzymol. Relat. Areas Mol. Biol. 47:45-148.
    • (1987) Adv. Enzymol. Relat. Areas Mol. Biol. , vol.47 , pp. 45-148
    • Chou, P.Y.1    Fasman, G.D.2
  • 7
    • 0028568176 scopus 로고
    • TopPred II: An improved software for membrane structure predictions
    • Claros, M.G., and G. von Heijne. 1994. TopPred II: an improved software for membrane structure predictions. CABIOS. 10:685-686.
    • (1994) CABIOS , vol.10 , pp. 685-686
    • Claros, M.G.1    Von Heijne, G.2
  • 8
    • 0023280139 scopus 로고
    • Measurement of the rate of epidermal terminal differentiation: Expression of involucrin by S-phase keratinocytes in culture and in psoriatic plaques
    • Dover, R., and F.M. Watt. 1987. Measurement of the rate of epidermal terminal differentiation: expression of involucrin by S-phase keratinocytes in culture and in psoriatic plaques. J. Invest. Dermatol. 89:349-352.
    • (1987) J. Invest. Dermatol. , vol.89 , pp. 349-352
    • Dover, R.1    Watt, F.M.2
  • 9
    • 0024076701 scopus 로고
    • Organization of desmosomal plaque proteins in cells growing at low calcium concentrations
    • Duden, R., and W.W. Franke. 1988. Organization of desmosomal plaque proteins in cells growing at low calcium concentrations. J Cell. Biol. 107:1049-1063.
    • (1988) J Cell. Biol. , vol.107 , pp. 1049-1063
    • Duden, R.1    Franke, W.W.2
  • 10
    • 0022446229 scopus 로고
    • Structure and evolution of the human involucrin gene
    • Eckert, R.L., and H. Green. 1986. Structure and evolution of the human involucrin gene. Cell. 46:583-589.
    • (1986) Cell , vol.46 , pp. 583-589
    • Eckert, R.L.1    Green, H.2
  • 12
    • 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
  • 13
    • 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
  • 14
    • 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
  • 15
    • 0017873321 scopus 로고
    • Analysis of the accuracy and implications of simple methods for predicting the secondary structure of globular proteins
    • Garnier, J., D.J. Osguthorpe, and B. Robson. 1978. Analysis of the accuracy and implications of simple methods for predicting the secondary structure of globular proteins. J. Mol. Biol. 120:97-120.
    • (1978) J. Mol. Biol. , vol.120 , pp. 97-120
    • Garnier, J.1    Osguthorpe, D.J.2    Robson, B.3
  • 16
    • 0017756282 scopus 로고
    • Terminal differentiation of cultured human epidermal cells
    • Green, H. 1977. Terminal differentiation of cultured human epidermal cells. Cell. 11:405-416.
    • (1977) Cell , vol.11 , pp. 405-416
    • Green, H.1
  • 18
    • 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. Virata, G.W. Elgart, J.R. Stanley, and D.A. Parry. 1992. Comparative structural analysis of desmoplakin, bullous pemphigoid antigen and plectin: members of a new gene family involved in organization of intermediate filaments. Int. J. Biol. Macromol. 14:145-153.
    • (1992) Int. J. Biol. Macromol. , vol.14 , pp. 145-153
    • Green, K.J.1    Virata, M.L.2    Elgart, G.W.3    Stanley, J.R.4    Parry, D.A.5
  • 19
    • 0029066406 scopus 로고
    • Gene targeting of BPAG1: Abnormalities in mechanical strength and cell migration in stratified epithelia and neurologic degeneration
    • Guo, L., L. Degenstein, J. Dowling, Q.C. Yu, R. Wollmann, B. Perman, and E. Fuchs. 1995. Gene targeting of BPAG1: abnormalities in mechanical strength and cell migration in stratified epithelia and neurologic degeneration. Cell. 81:233-243.
    • (1995) Cell , vol.81 , pp. 233-243
    • Guo, L.1    Degenstein, L.2    Dowling, J.3    Yu, Q.C.4    Wollmann, R.5    Perman, B.6    Fuchs, E.7
  • 20
    • 0025941524 scopus 로고
    • Immunocytochemical evidence for a possible role of cross-linked keratinocyte envelopes in stratum corneum cohesion
    • Haftek, M., G. Serre, V. Mils, and J. Thirolet. 1991. Immunocytochemical evidence for a possible role of cross-linked keratinocyte envelopes in stratum corneum cohesion. J. Histochem. Cytochem. 39:1531-1538.
    • (1991) J. Histochem. Cytochem. , vol.39 , pp. 1531-1538
    • Haftek, M.1    Serre, G.2    Mils, V.3    Thirolet, J.4
  • 21
    • 0028355658 scopus 로고
    • Identification of a second protein product of the gene encoding a human epidermal autoantigen
    • Hopkinson, S.B., and J.C. Jones. 1994. Identification of a second protein product of the gene encoding a human epidermal autoantigen. Biochem. J. 300:851-857.
    • (1994) Biochem. J. , vol.300 , pp. 851-857
    • Hopkinson, S.B.1    Jones, J.C.2
  • 23
    • 0026465089 scopus 로고
    • Characterisation of eight monoclonal antibodies to ivolucrin
    • Hudson, D.L., K.L. Weiland, T.P. Dooley, M. Simon, and F.M. Watt. 1992. Characterisation of eight monoclonal antibodies to ivolucrin. Hybridoma. 11:367-379.
    • (1992) Hybridoma , vol.11 , pp. 367-379
    • Hudson, D.L.1    Weiland, K.L.2    Dooley, T.P.3    Simon, M.4    Watt, F.M.5
  • 24
    • 0030045163 scopus 로고    scopus 로고
    • Immunoelectron microscopic analysis of cornified cell envelope formation in normal and psoriatic epidermis
    • Ishida-Yamamoto, A., R.A. Eady, F.M. Watt, D.R. Roop, D. Hohl, and H. Iizuka. 1996. Immunoelectron microscopic analysis of cornified cell envelope formation in normal and psoriatic epidermis. J. Histochem. Cytochem. 44: 167-175.
    • (1996) J. Histochem. Cytochem. , vol.44 , pp. 167-175
    • Ishida-Yamamoto, A.1    Eady, R.A.2    Watt, F.M.3    Roop, D.R.4    Hohl, D.5    Iizuka, H.6
  • 25
    • 0027278759 scopus 로고
    • A myosin-like protein from a higher plant
    • Knight, A.E., and J. Kendrick-Jones. 1993. A myosin-like protein from a higher plant. J. Mol. Biol. 1991:148-154.
    • (1993) J. Mol. Biol. , vol.1991 , pp. 148-154
    • Knight, A.E.1    Kendrick-Jones, J.2
  • 26
    • 0027987929 scopus 로고
    • Making a connection: Direct binding between keratin intermediate filaments and desmosomal proteins
    • Kouklis, P.D., E. Hutton, and E. Fuchs. 1994. Making a connection: direct binding between keratin intermediate filaments and desmosomal proteins. J. Cell Biol. 127:1049-1060.
    • (1994) J. Cell Biol. , vol.127 , pp. 1049-1060
    • Kouklis, P.D.1    Hutton, E.2    Fuchs, E.3
  • 27
    • 0025792297 scopus 로고
    • Structural features in eukaryotic mRNAs that modulate the initiation of translation
    • Kozak, M. 1991. Structural features in eukaryotic mRNAs that modulate the initiation of translation. J. Biol. Chem. 266:19867-19870.
    • (1991) J. Biol. Chem. , vol.266 , pp. 19867-19870
    • Kozak, M.1
  • 28
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • Kyte, J., and R.F. Doolittle. 1982. A simple method for displaying the hydropathic character of a protein. J. Mol. Biol. 157:105-132.
    • (1982) J. Mol. Biol. , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 29
    • 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 (Lond.). 227:680-685.
    • (1970) Nature (Lond.) , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 30
    • 0026356891 scopus 로고
    • Predicting coiled coils from protein sequences
    • Lupas, A., M. Van Dyke, and J. Stock. 1991. Predicting coiled coils from protein sequences. Science (Wash. DC). 252:1162-1164.
    • (1991) Science (Wash. DC) , vol.252 , pp. 1162-1164
    • Lupas, A.1    Van Dyke, M.2    Stock, J.3
  • 31
    • 0028572509 scopus 로고
    • Binding of keratin intermediate filaments (K10) to the cornified envelope in mouse epidermis: Implications for barrier function
    • Ming, M.E., H.A. Daryanani, L.P. Roberts, H.P. Baden, and J.C. Kvedar. 1994. Binding of keratin intermediate filaments (K10) to the cornified envelope in mouse epidermis: implications for barrier function. J. Invest. Dermatol. 103: 780-784.
    • (1994) J. Invest. Dermatol. , vol.103 , pp. 780-784
    • Ming, M.E.1    Daryanani, H.A.2    Roberts, L.P.3    Baden, H.P.4    Kvedar, J.C.5
  • 32
    • 0026021123 scopus 로고
    • Decreased expression of fibronectin and the alpha 5 beta 1 integrin during terminal differentiation of human keratinocytes
    • Nicholson, L.J., and F.M. Watt. 1991. Decreased expression of fibronectin and the alpha 5 beta 1 integrin during terminal differentiation of human keratinocytes. J. Cell Sci. 98:225-232.
    • (1991) J. Cell Sci. , vol.98 , pp. 225-232
    • Nicholson, L.J.1    Watt, F.M.2
  • 33
    • 0024371499 scopus 로고
    • Desmoplakin I and desmoplakin II. Purification and characterization
    • O'Keefe, E.J., H.P. Erickson, and V. Bennett. 1989. Desmoplakin I and desmoplakin II. Purification and characterization. J. Biol. Chem. 264:8310-8318.
    • (1989) J. Biol. Chem. , vol.264 , pp. 8310-8318
    • O'Keefe, E.J.1    Erickson, H.P.2    Bennett, V.3
  • 34
    • 0023838729 scopus 로고
    • Kinetics of desmosome assembly in Madin-Darby canine kidney epithelial cells: Temporal and spatial regulation of desmoplakin organization and stabilization upon cell-cell contact. II. Morphological analysis
    • Pasdar, M., and W.J. Nelson. 1988a. Kinetics of desmosome assembly in Madin-Darby canine kidney epithelial cells: temporal and spatial regulation of desmoplakin organization and stabilization upon cell-cell contact. II. Morphological analysis. J. Cell Biol. 106:687-695.
    • (1988) J. Cell Biol. , vol.106 , pp. 687-695
    • Pasdar, M.1    Nelson, W.J.2
  • 35
    • 0023864445 scopus 로고
    • Kinetics of desmosome assembly in Madin-Darby canine kidney epithelial cells: Temporal and spatial regulation of desmoplakin organization and stabilization upon cell-cell contact. I. Biochemical analysis
    • Pasdar, M., and W.J. Nelson. 1988b. Kinetics of desmosome assembly in Madin-Darby canine kidney epithelial cells: temporal and spatial regulation of desmoplakin organization and stabilization upon cell-cell contact. I. Biochemical analysis. J. Cell Biol. 106:677-685.
    • (1988) J. Cell Biol. , vol.106 , pp. 677-685
    • Pasdar, M.1    Nelson, W.J.2
  • 36
    • 0001490507 scopus 로고
    • The cornified envelope: A key structure of terminally differentiating keratinocytes
    • M. Darmon and M. Blumenberg, editors. Academic Press, Inc., San Diego
    • Reichert, U., S. Michel, and R. Schmidt. 1993. The cornified envelope: a key structure of terminally differentiating keratinocytes. In Molecular Biology of the Skin. M. Darmon and M. Blumenberg, editors. Academic Press, Inc., San Diego. 107-150.
    • (1993) Molecular Biology of the Skin , pp. 107-150
    • Reichert, U.1    Michel, S.2    Schmidt, R.3
  • 37
    • 0016729431 scopus 로고
    • Serial cultivation of strains of human epidermal keratinocytes: The formation of keratinizing colonies from single cells
    • Rheinwald, J.G., and H. Green. 1975. Serial cultivation of strains of human epidermal keratinocytes: the formation of keratinizing colonies from single cells. Cell. 6:331-343.
    • (1975) Cell , vol.6 , pp. 331-343
    • Rheinwald, J.G.1    Green, H.2
  • 38
    • 0018721266 scopus 로고
    • Presence in human epidermal cells of a soluble protein precursor of the cross-linked envelope: Activation of the cross-linking by calcium ions
    • Rice, R.H., and H. Green. 1979. Presence in human epidermal cells of a soluble protein precursor of the cross-linked envelope: activation of the cross-linking by calcium ions. Cell. 18:681-694.
    • (1979) Cell , vol.18 , pp. 681-694
    • Rice, R.H.1    Green, H.2
  • 40
    • 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., K. Li, M.L. Chu, and J. Uitto. 1991a. 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
  • 41
    • 0025843554 scopus 로고
    • Bullous pemphigoid antigen: CDNA cloning, cellular expression, and evidence for polymorphism of the human gene
    • Sawamura, D., K.H. Li, K. Nomura, Y. Sugita, A.M. Christiano, and J. Uitto. 1991b. Bullous pemphigoid antigen: cDNA cloning, cellular expression, and evidence for polymorphism of the human gene. J. Invest. Dermatol. 96:908-915.
    • (1991) J. Invest. Dermatol. , vol.96 , pp. 908-915
    • Sawamura, D.1    Li, K.H.2    Nomura, K.3    Sugita, Y.4    Christiano, A.M.5    Uitto, J.6
  • 44
    • 0021132365 scopus 로고
    • Participation of membrane-associated proteins in the formation of the cross-linked envelope of the keratinocyte
    • Simon, M., and H. Green. 1984. Participation of membrane-associated proteins in the formation of the cross-linked envelope of the keratinocyte. Cell. 36: 827-834.
    • (1984) Cell , vol.36 , pp. 827-834
    • Simon, M.1    Green, H.2
  • 45
    • 0002911990 scopus 로고
    • The epidermal cornified envelope and its precursors
    • I.M. Leigh, E.B. Lane, and F.M. Watt, editors. Cambridge University Press, Cambridge
    • Simon, M. 1994. The epidermal cornified envelope and its precursors. In The Keratinocyte Handbook. I.M. Leigh, E.B. Lane, and F.M. Watt, editors. Cambridge University Press, Cambridge. 275-292.
    • (1994) The Keratinocyte Handbook , pp. 275-292
    • Simon, M.1
  • 46
    • 0026511055 scopus 로고
    • The desmoplakin carboxyl terminus coaligns with and specifically disrupts intermediate filament networks when expressed in cultured cells
    • Stappenbeck, T.S., and K.J. Green. 1992. The desmoplakin carboxyl terminus coaligns with and specifically disrupts intermediate filament networks when expressed in cultured cells. J. Cell Biol. 116:1197-1209.
    • (1992) J. Cell Biol. , vol.116 , pp. 1197-1209
    • Stappenbeck, T.S.1    Green, K.J.2
  • 47
    • 0027428693 scopus 로고
    • Functional analysis of desmoplakin domains: Specification of the interaction with keratin versus vimentin intermediate filament networks
    • Stappenbeck, T.S., E.A. Bornslaeger, C.M. Corcoran, H.H. Luu, M.L. Virata, and K.J. Green. 1993. Functional analysis of desmoplakin domains: specification of the interaction with keratin versus vimentin intermediate filament networks. J. Cell Biol. 123:691-705.
    • (1993) J. Cell Biol. , vol.123 , pp. 691-705
    • Stappenbeck, T.S.1    Bornslaeger, E.A.2    Corcoran, C.M.3    Luu, H.H.4    Virata, M.L.5    Green, K.J.6
  • 48
    • 0029050246 scopus 로고
    • The proteins elafin, filaggrin, keratin intermediate filaments, loricrin, and small proline-rich proteins 1 and 2 are isodipeptide cross-linked components of the human epidermal cornified cell envelope
    • Steinert, P.M., and L.N. Marekov. 1995. The proteins elafin, filaggrin, keratin intermediate filaments, loricrin, and small proline-rich proteins 1 and 2 are isodipeptide cross-linked components of the human epidermal cornified cell envelope. J. Biol. Chem. 270:17702-17711.
    • (1995) J. Biol. Chem. , vol.270 , pp. 17702-17711
    • Steinert, P.M.1    Marekov, L.N.2
  • 50
    • 0017047237 scopus 로고
    • Differentiation of the epidermal keratinocyte in cell culture: Formation of the cornified envelope
    • Sun, T.T., and H. Green. 1976. Differentiation of the epidermal keratinocyte in cell culture: formation of the cornified envelope. Cell. 9:511-521.
    • (1976) Cell , vol.9 , pp. 511-521
    • Sun, T.T.1    Green, H.2
  • 51
    • 0027308212 scopus 로고
    • The human 230-kD bullous pemphigoid antigen gene (BPAG1). Exon-intron organization and identification of regulatory tissue specific elements in the promoter region
    • Tamai, K., D. Sawamura, H.C. Do, Y. Tamai, K. Li, and J. Uitto. 1993. The human 230-kD bullous pemphigoid antigen gene (BPAG1). Exon-intron organization and identification of regulatory tissue specific elements in the promoter region. J. Clin. Invest. 92:814-822.
    • (1993) J. Clin. Invest. , vol.92 , pp. 814-822
    • Tamai, K.1    Sawamura, D.2    Do, H.C.3    Tamai, Y.4    Li, K.5    Uitto, J.6
  • 52
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin, H., T. Staehelin, and J. Gordon. 1979. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl. Acad. Sci. USA. 76:4350-4354.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 54
    • 0021717130 scopus 로고
    • Calcium-induced reorganization of desmosomal components in cultured human keratinocytes
    • Watt, F.M., D.L. Mattey, and D.R. Garrod. 1984. Calcium-induced reorganization of desmosomal components in cultured human keratinocytes. J. Cell Biol. 99:2211-2215.
    • (1984) J. Cell Biol. , vol.99 , pp. 2211-2215
    • Watt, F.M.1    Mattey, D.L.2    Garrod, D.R.3
  • 55
    • 0013686883 scopus 로고
    • Cultivation of human epidermal keratinocytes with a 3T3 feeder layer
    • J.E. Celis, editor. Academic Press, Inc., San Diego
    • Watt, F.M. 1994a. Cultivation of human epidermal keratinocytes with a 3T3 feeder layer. In Cell Biology: A Laboratory Handbook. J.E. Celis, editor. Academic Press, Inc., San Diego. 83-89.
    • (1994) Cell Biology: A Laboratory Handbook , pp. 83-89
    • Watt, F.M.1
  • 56
    • 0012109366 scopus 로고
    • Suspension-induced terminal differentiation of keratinocytes
    • I. L. Leigh, and F. M. Watt, editors. Cambridge University Press, Cambridge
    • Watt, F.M. 1994b. Suspension-induced terminal differentiation of keratinocytes. In Keratinocyte Methods. I. L. Leigh, and F. M. Watt, editors. Cambridge University Press, Cambridge. 113.
    • (1994) Keratinocyte Methods , pp. 113
    • Watt, F.M.1
  • 57
    • 0026014584 scopus 로고
    • Cloning and sequencing of rat plectin indicates a 466-kD polypeptide chain with a three-domain structure based or a central alpha-helical coiled coil
    • Wiche, G., B. Becker, K. Luber, G. Weitzer, 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 or 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
  • 58
    • 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.