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Volumn 135, Issue 4, 1996, Pages 1027-1042

Characterization of pinin, a novel protein associated with the desmosome-intermediate filament complex

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID SEQUENCE; ANIMAL CELL; ARTICLE; CELL ADHESION; CHICKEN; DESMOSOME; DNA DETERMINATION; DNA LIBRARY; DNA TRANSFECTION; IMMUNOBLOTTING; IMMUNOCOMPETENT CELL; IMMUNOFLUORESCENCE; INTERMEDIATE FILAMENT; MOLECULAR CLONING; NONHUMAN; OLIGONUCLEOTIDE PROBE; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN STRUCTURE; RNA SPLICING; SEQUENCE HOMOLOGY; SWINE;

EID: 0029836931     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.135.4.1027     Document Type: Article
Times cited : (88)

References (58)
  • 1
    • 0025165922 scopus 로고
    • Desmoplakin II expression is not restricted to stratified epithelia
    • Angst, B.D., L.A. Nilles, and K.J. Green. 1990. Desmoplakin II expression is not restricted to stratified epithelia. J. Cell Sci. 97:247-257.
    • (1990) J. Cell Sci. , vol.97 , pp. 247-257
    • Angst, B.D.1    Nilles, L.A.2    Green, K.J.3
  • 2
    • 0027151802 scopus 로고
    • Stratification-related expression of isoforms of the desmosomal cadherins in human epidermis
    • Arnemann, J., K.H. Sullivan, A.L. 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.L.3    King, I.A.4    Buxton, R.S.5
  • 3
    • 0019864228 scopus 로고
    • The structure and function of spot desmosomes
    • Arnn, J., and L.A. Staehelin. 1981. The structure and function of spot desmosomes. Int. J. Dermatol. 20(5):330-339.
    • (1981) Int. J. Dermatol. , vol.20 , Issue.5 , pp. 330-339
    • Arnn, J.1    Staehelin, L.A.2
  • 6
    • 0026878253 scopus 로고
    • Structure and interactions of desmosomal and other cadherins
    • Buxton, R.S., and A.I. Magee. 1992. Structure and interactions of desmosomal and other cadherins. Semin. Cell. Biol. 3(3):157-167.
    • (1992) Semin. Cell. Biol. , vol.3 , Issue.3 , pp. 157-167
    • Buxton, R.S.1    Magee, A.I.2
  • 7
    • 0023277545 scopus 로고
    • Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction
    • Chomczynski, P., and N. Sacchi. 1987. Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction. Anal. Biochem. 162(1):156-159.
    • (1987) Anal. Biochem. , vol.162 , Issue.1 , pp. 156-159
    • Chomczynski, P.1    Sacchi, N.2
  • 8
    • 0026505270 scopus 로고
    • Protein kinase inhibitors prevent junction dissociation induced by low extracellular calcium in MDCK epithelial cells
    • Citi, S. 1992. Protein kinase inhibitors prevent junction dissociation induced by low extracellular calcium in MDCK epithelial cells. J. Cell Biol. 117(1):169-178.
    • (1992) J. Cell Biol. , vol.117 , Issue.1 , pp. 169-178
    • Citi, S.1
  • 9
    • 0028273266 scopus 로고
    • Cytoskeletal involvement in the modulation of cell-cell junctions by the protein kinase inhibitor H-7
    • Citi, S., T. Volberg, A.D. Bershadsky, N. Denisenko, and B. Geiger. 1994. Cytoskeletal involvement in the modulation of cell-cell junctions by the protein kinase inhibitor H-7. J. Cell Sci. 107:683-692.
    • (1994) J. Cell Sci. , vol.107 , pp. 683-692
    • Citi, S.1    Volberg, T.2    Bershadsky, A.D.3    Denisenko, N.4    Geiger, B.5
  • 10
    • 0025821552 scopus 로고
    • Cloning and sequence analysis of desmosomal glycoproteins 2 and 3 (desmocollins): Cadherin-like desmosomal adhesion molecules with heterogeneous cytoplasmic domains
    • Collins, J.E., P.K. Legan, T.P. Kenny, J. MacGarvie, J.L. Holton, and D.R. Garrod. 1991. Cloning and sequence analysis of desmosomal glycoproteins 2 and 3 (desmocollins): cadherin-like desmosomal adhesion molecules with heterogeneous cytoplasmic domains. J. Cell Biol. 113(2):381-391.
    • (1991) J. Cell Biol. , vol.113 , Issue.2 , pp. 381-391
    • Collins, J.E.1    Legan, P.K.2    Kenny, T.P.3    MacGarvie, J.4    Holton, J.L.5    Garrod, D.R.6
  • 11
    • 0025130161 scopus 로고
    • Structural features in the heptad substructure and longer range repeats of two-stranded alpha-fibrous proteins
    • Conway, J.F., and D.A. Parry. 1990. Structural features in the heptad substructure and longer range repeats of two-stranded alpha-fibrous proteins. Int. J. Biol. Macromol. 12(5):328-334.
    • (1990) Int. J. Biol. Macromol. , vol.12 , Issue.5 , pp. 328-334
    • Conway, J.F.1    Parry, D.A.2
  • 12
    • 0022345716 scopus 로고
    • The complement of desmosomal plaque proteins in different cell types
    • Cowin, P., H.P. Kapprell, and W.W. Franke. 1985. The complement of desmosomal plaque proteins in different cell types. J. Cell Biol. 101(4):1442-1454.
    • (1985) J. Cell Biol. , vol.101 , Issue.4 , pp. 1442-1454
    • Cowin, P.1    Kapprell, H.P.2    Franke, W.W.3
  • 13
    • 0022993985 scopus 로고
    • Plakoglobin: A protein common to different kinds of intercellular adhering junctions
    • Cowin, P., H.P. Kapprell, W.W. Franke, J. Tamkun, and R.O. Hynes. 1986. Plakoglobin: a protein common to different kinds of intercellular adhering junctions. Cell. 46(7):1063-1073.
    • (1986) Cell , vol.46 , Issue.7 , pp. 1063-1073
    • Cowin, P.1    Kapprell, H.P.2    Franke, W.W.3    Tamkun, J.4    Hynes, R.O.5
  • 14
    • 0028285028 scopus 로고
    • Different effects of protein kinase inhibitors on the localization of junctional proteins at cell-cell contact sites
    • Denisenko, N., P. Burighel, and S. Citi. 1994. Different effects of protein kinase inhibitors on the localization of junctional proteins at cell-cell contact sites. J. Cell Sci. 107:969-981.
    • (1994) J. Cell Sci. , vol.107 , pp. 969-981
    • Denisenko, N.1    Burighel, P.2    Citi, S.3
  • 15
    • 0029154616 scopus 로고
    • Anillin, a contractile ring protein that cycles from the nucleus to the cell cortex
    • Field, C.M., and B.M. Alberts. 1995. Anillin, a contractile ring protein that cycles from the nucleus to the cell cortex. J. Cell Biol. 131(1):165-178.
    • (1995) J. Cell Biol. , vol.131 , Issue.1 , pp. 165-178
    • Field, C.M.1    Alberts, B.M.2
  • 16
    • 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. 1991. Protein kinase A- and protein kinase C-regulated interaction of plectin with lamin B and vimentin. Proc. Natl. Acad. Sci. USA. 88(9):3812-3816.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , Issue.9 , pp. 3812-3816
    • Foisner, R.1    Traub, P.2    Wiche, G.3
  • 17
    • 0027548587 scopus 로고
    • Desmosomes and hemidesmosomes
    • Garrod, D.R. 1993. Desmosomes and hemidesmosomes. Curr. Opin. Cell Biol. 5(1):30-40.
    • (1993) Curr. Opin. Cell Biol. , vol.5 , Issue.1 , pp. 30-40
    • Garrod, D.R.1
  • 18
    • 0015847039 scopus 로고
    • A new technique for the assay of infectivity of human adenovirus 5 DNA
    • Graham, F.L., and A.v.d. Eb. 1973. A new technique for the assay of infectivity of human adenovirus 5 DNA. Virology. 52(2):456-467.
    • (1973) Virology , vol.52 , Issue.2 , pp. 456-467
    • Graham, F.L.1    Eb, A.V.D.2
  • 20
    • 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(3):145-153.
    • (1992) Int. J. Biol. Macromol. , vol.14 , Issue.3 , pp. 145-153
    • Green, K.J.1    Virata, M.L.2    Elgart, G.W.3    Stanley, J.R.4    Parry, D.A.5
  • 21
    • 0028144738 scopus 로고
    • Band 6 protein, a major constituent of desmosomes from stratified epithelia, is a novel member of the armadillo multigene family
    • Hatzfeld, M., G.I. Kristjansson, U. Plessmann, and K. Weber. 1994. Band 6 protein, a major constituent of desmosomes from stratified epithelia, is a novel member of the armadillo multigene family. J. Cell Sci. 107:2259-2270.
    • (1994) J. Cell Sci. , vol.107 , pp. 2259-2270
    • Hatzfeld, M.1    Kristjansson, G.I.2    Plessmann, U.3    Weber, K.4
  • 23
    • 0027467268 scopus 로고
    • Phosphorylation on protein kinase C sites inhibits nuclear import of lamin B2
    • Hennekes, H., M. Peter, K. Weber, and E.A. Nigg. 1993. Phosphorylation on protein kinase C sites inhibits nuclear import of lamin B2. J. Cell Biol. 120(6):1293-1304.
    • (1993) J. Cell Biol. , vol.120 , Issue.6 , pp. 1293-1304
    • Hennekes, H.1    Peter, M.2    Weber, K.3    Nigg, E.A.4
  • 24
    • 0024507707 scopus 로고
    • Tau consists of a set of proteins with repeated C-terminal microtubule-binding domains and variable N-terminal domains
    • Himmler, A., D. Drechsel, M.W. Kirschner, and D.W. Martin, Jr. 1989. Tau consists of a set of proteins with repeated C-terminal microtubule-binding domains and variable N-terminal domains. Mol. Cell. Biol. 9(4):1381-1388.
    • (1989) Mol. Cell. Biol. , vol.9 , Issue.4 , pp. 1381-1388
    • Himmler, A.1    Drechsel, D.2    Kirschner, M.W.3    Martin Jr., D.W.4
  • 25
    • 0025811645 scopus 로고
    • Characterization of human loricrin. Structure and function of a new class of epidermal cell envelope proteins
    • Hohl, D., T. Mehrel, U. Lichti, M.L. Turner, D.R. Roop, and P.M. Steinert. 1991. Characterization of human loricrin. Structure and function of a new class of epidermal cell envelope proteins. J. Biol. Chem. 266(10):6626-6636.
    • (1991) J. Biol. Chem. , vol.266 , Issue.10 , pp. 6626-6636
    • Hohl, D.1    Mehrel, T.2    Lichti, U.3    Turner, M.L.4    Roop, D.R.5    Steinert, P.M.6
  • 26
    • 10544246781 scopus 로고
    • Desmosomal glycoproteins 2 and 3 (desmocollins) show N-terminal similarity to calcium-dependent cell-cell adhesion molecules
    • Holton, J.L., T.P. Kenny, P.K. Legan, J.E. Collins, J.N. Keen, and D.R. Garrod. 1990. Desmosomal glycoproteins 2 and 3 (desmocollins) show N-terminal similarity to calcium-dependent cell-cell adhesion molecules. J. Cell Sci. 113: 381-391.
    • (1990) J. Cell Sci. , vol.113 , pp. 381-391
    • Holton, J.L.1    Kenny, T.P.2    Legan, P.K.3    Collins, J.E.4    Keen, J.N.5    Garrod, D.R.6
  • 27
    • 0025158107 scopus 로고
    • Protein kinase recognition sequence motifs
    • Kemp, B.E., and R.B. Pearson. 1990. Protein kinase recognition sequence motifs. Trends Biochem. Sci. 15(9):342-346.
    • (1990) Trends Biochem. Sci. , vol.15 , Issue.9 , pp. 342-346
    • Kemp, B.E.1    Pearson, R.B.2
  • 28
    • 0025736474 scopus 로고
    • Amino acid sequence of bovine muzzle epithelial desmocollin derived from cloned cDNA: A novel subtype of desmosomal cadherins
    • Koch, P.J., M.D. Goldschmidt, M.J. Walsh, and R. Zimbelmann. 1991. Amino acid sequence of bovine muzzle epithelial desmocollin derived from cloned cDNA: a novel subtype of desmosomal cadherins. Differentiation. 47(1):29-36.
    • (1991) Differentiation , vol.47 , Issue.1 , pp. 29-36
    • Koch, P.J.1    Goldschmidt, M.D.2    Walsh, M.J.3    Zimbelmann, R.4
  • 29
    • 0026342613 scopus 로고
    • An analysis of vertebrate mRNA sequences: Intimations of translational control
    • Kozak, M. 1991. An analysis of vertebrate mRNA sequences: intimations of translational control. J. Cell Biol. 115(4):887-903.
    • (1991) J. Cell Biol. , vol.115 , Issue.4 , pp. 887-903
    • Kozak, M.1
  • 30
    • 0026877993 scopus 로고
    • The molecular biology of desmosomes and hemidesmosomes: What's in a name?
    • Legan, P.K., J.E. Collins, and D.R. Garrod. 1992. The molecular biology of desmosomes and hemidesmosomes: what's in a name? Bioessays. 14(6):385-393.
    • (1992) Bioessays , vol.14 , Issue.6 , pp. 385-393
    • Legan, P.K.1    Collins, J.E.2    Garrod, D.R.3
  • 31
    • 0024693747 scopus 로고
    • Definition of an efficient synthetic poly(A) site
    • Levitt, N., D. Briggs, A. Gil, and N.J. Proudfoot. 1989. Definition of an efficient synthetic poly(A) site. Genes Dev. 3(7):1019-1025.
    • (1989) Genes Dev. , vol.3 , Issue.7 , pp. 1019-1025
    • Levitt, N.1    Briggs, D.2    Gil, A.3    Proudfoot, N.J.4
  • 32
    • 0027254919 scopus 로고
    • The mechanism of interaction of filaggrin with intermediate filaments. The ionic zipper hypothesis
    • Mack, J.W., A.C. Steven, and P.M. Steinert. 1993. The mechanism of interaction of filaggrin with intermediate filaments. The ionic zipper hypothesis. J. Mol. Biol. 232:50-66.
    • (1993) J. Mol. Biol. , vol.232 , pp. 50-66
    • Mack, J.W.1    Steven, A.C.2    Steinert, P.M.3
  • 33
    • 0020538869 scopus 로고
    • Biochemical and immunological characterization of desmoplakins I and II, the major polypeptides of the desmosomal plaque
    • Mueller, H., and W.W. Franke. 1983. Biochemical and immunological characterization of desmoplakins I and II, the major polypeptides of the desmosomal plaque. J. Mol. Biol. 163(4):647-671.
    • (1983) J. Mol. Biol. , vol.163 , Issue.4 , pp. 647-671
    • Mueller, H.1    Franke, W.W.2
  • 34
    • 0022595998 scopus 로고
    • Cytoskeletal organization, vinculin-phosphorylation, and fibronectin expression in transformed fibroblasts with different cell morphologies
    • Nigg, E.A., B.M. Sefton, S.J. Singer, and P.K. Vogt. 1986. Cytoskeletal organization, vinculin-phosphorylation, and fibronectin expression in transformed fibroblasts with different cell morphologies. Virology. 151(1):50-65.
    • (1986) Virology , vol.151 , Issue.1 , pp. 50-65
    • Nigg, E.A.1    Sefton, B.M.2    Singer, S.J.3    Vogt, P.K.4
  • 35
    • 0025943790 scopus 로고
    • Neurofilament phosphorylation: A new look at regulation and function
    • Nixon, R.A., and R.K. Sihag. 1991. Neurofilament phosphorylation: a new look at regulation and function. Trends Neurosci. 14(11):501-506.
    • (1991) Trends Neurosci. , vol.14 , Issue.11 , pp. 501-506
    • Nixon, R.A.1    Sihag, R.K.2
  • 36
    • 0024534241 scopus 로고
    • Evidence that the leucine zipper is a coiled coil
    • O'Shea, E.K., R. Rutkowski, and P.S. Kim. 1989. Evidence that the leucine zipper is a coiled coil. Science (Wash. DC). 243(4890):538-542.
    • (1989) Science (Wash. DC) , vol.243 , Issue.4890 , pp. 538-542
    • O'Shea, E.K.1    Rutkowski, R.2    Kim, P.S.3
  • 37
    • 0025272236 scopus 로고
    • Secondary structure of a leucine zipper determined by nuclear magnetic resonance spectroscopy
    • Oas, T.G., L.P. McIntosh, E.K. O'Shea, F.W. Dahlquist, and P.S. Kim. 1990. Secondary structure of a leucine zipper determined by nuclear magnetic resonance spectroscopy. Biochemistry. 29(12):2891-2894.
    • (1990) Biochemistry , vol.29 , Issue.12 , pp. 2891-2894
    • Oas, T.G.1    McIntosh, L.P.2    O'Shea, E.K.3    Dahlquist, F.W.4    Kim, P.S.5
  • 38
    • 0026709315 scopus 로고
    • Identification of an epithelial protein related to the desmosome and intermediate filament network
    • Ouyang, P., and S.P. Sugrue. 1992. Identification of an epithelial protein related to the desmosome and intermediate filament network. J. Cell Biol. 118(6): 1477-1488.
    • (1992) J. Cell Biol. , vol.118 , Issue.6 , pp. 1477-1488
    • Ouyang, P.1    Sugrue, S.P.2
  • 39
    • 0022551912 scopus 로고
    • Mouse antisera specific for desmosomal adhesion molecules of suprabasal skin cells, meninges, and meningioma
    • Parrish, E.P., D.R. Garrod, D.E. Mattey, L. Hand, P.V. Steart, and R.O. Weiler. 1986. Mouse antisera specific for desmosomal adhesion molecules of suprabasal skin cells, meninges, and meningioma. Proc. Natl. Acad. Sci. USA. 83(8):2657-2661.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , Issue.8 , pp. 2657-2661
    • Parrish, E.P.1    Garrod, D.R.2    Mattey, D.E.3    Hand, L.4    Steart, P.V.5    Weiler, R.O.6
  • 41
    • 0025078367 scopus 로고
    • The structure of the gene for mouse filaggrin and a comparison of the repeating units
    • Rothnagel, J.A., and P.M. Steinert. 1990. The structure of the gene for mouse filaggrin and a comparison of the repeating units. J. Biol. Chem. 265(4): 1862-1865.
    • (1990) J. Biol. Chem. , vol.265 , Issue.4 , pp. 1862-1865
    • Rothnagel, J.A.1    Steinert, P.M.2
  • 42
    • 0023656867 scopus 로고
    • The gene for mouse epidermal filaggrin precursor. Its partial characterization, expression, and sequence of a repeating filaggrin unit
    • Rothnagel, J.A., T. Mehrel, W.W. Idler, D.R. Roop, and P.M. Steinert. 1987. The gene for mouse epidermal filaggrin precursor. Its partial characterization, expression, and sequence of a repeating filaggrin unit. J. Biol. Chem. 262(32):15643-15648.
    • (1987) J. Biol. Chem. , vol.262 , Issue.32 , pp. 15643-15648
    • Rothnagel, J.A.1    Mehrel, T.2    Idler, W.W.3    Roop, D.R.4    Steinert, P.M.5
  • 43
    • 0025186246 scopus 로고
    • Dynamics of phosphorylation and assembly of the high molecular weight neurofilament subunit in NB2a/ d1 neuroblastoma
    • Shea, T.B., R.K. Sihag, and R.A. Nixon. 1990. Dynamics of phosphorylation and assembly of the high molecular weight neurofilament subunit in NB2a/ d1 neuroblastoma. J. Neurochem. 55(5):1784-1792.
    • (1990) J. Neurochem. , vol.55 , Issue.5 , pp. 1784-1792
    • Shea, T.B.1    Sihag, R.K.2    Nixon, R.A.3
  • 44
    • 0023916538 scopus 로고
    • Phosphorylation of neurofilament proteins by protein kinase C
    • Sihag, R.K., A.Y. Jeng, and R.A. Nixon. 1988. Phosphorylation of neurofilament proteins by protein kinase C. FEBS Lett. 233(1):181-185.
    • (1988) FEBS Lett. , vol.233 , Issue.1 , pp. 181-185
    • Sihag, R.K.1    Jeng, A.Y.2    Nixon, R.A.3
  • 45
    • 0028178390 scopus 로고
    • IFAP 300 is common to desmosomes and hemidesmosomes and is a possible linker of intermediate filaments to these junctions
    • Skalli, O., J.C. Jones, R. Gagescu, and R.D. Goldman. 1994. IFAP 300 is common to desmosomes and hemidesmosomes and is a possible linker of intermediate filaments to these junctions. J. Cell Biol. 125(1):159-170.
    • (1994) J. Cell Biol. , vol.125 , Issue.1 , pp. 159-170
    • Skalli, O.1    Jones, J.C.2    Gagescu, R.3    Goldman, R.D.4
  • 46
    • 0016140812 scopus 로고
    • Structure and function of intercellular junctions
    • Staehelin, L.A. 1974. Structure and function of intercellular junctions. Int. Rev. Cytol. 39(191):191-283.
    • (1974) Int. Rev. Cytol. , vol.39 , Issue.191 , pp. 191-283
    • Staehelin, L.A.1
  • 47
    • 0028028177 scopus 로고
    • Phosphorylation of the desmoplakin COOH terminus negatively regulates its interaction with keratin intermediate filament networks
    • Stappenbeck, T.S., J.A. Lamb, C.M. Corcoran, and K.J. Green. 1994. Phosphorylation of the desmoplakin COOH terminus negatively regulates its interaction with keratin intermediate filament networks. J. Biol. Chem. 269(47): 29351-29354.
    • (1994) J. Biol. Chem. , vol.269 , Issue.47 , pp. 29351-29354
    • Stappenbeck, T.S.1    Lamb, J.A.2    Corcoran, C.M.3    Green, K.J.4
  • 48
    • 0025857630 scopus 로고
    • Glycine loops in proteins: Their occurrence in certain intermediate filament chains, loricrins and single-stranded RNA binding proteins
    • Steinert, P.M., J.W. Mack, B.P. Korge, S.O. Gan, S.R. Haynes, and A.C. Steven. 1991. Glycine loops in proteins: their occurrence in certain intermediate filament chains, loricrins and single-stranded RNA binding proteins. Int. J. Biol. Macromol. 13(3):130-139.
    • (1991) Int. J. Biol. Macromol. , vol.13 , Issue.3 , pp. 130-139
    • Steinert, P.M.1    Mack, J.W.2    Korge, B.P.3    Gan, S.O.4    Haynes, S.R.5    Steven, A.C.6
  • 50
    • 0027251723 scopus 로고
    • Differential synthesis of type 1 and type 2 desmocollin mRNAs in human stratified epithelia
    • Theis, D.G., P.J. Koch, and W.W. Franke. 1993. Differential synthesis of type 1 and type 2 desmocollin mRNAs in human stratified epithelia. Int. J. Dev. Biol. 37(1):101-110.
    • (1993) Int. J. Dev. Biol. , vol.37 , Issue.1 , pp. 101-110
    • Theis, D.G.1    Koch, P.J.2    Franke, W.W.3
  • 51
    • 0025913788 scopus 로고
    • Specific proto-oncogenic tyrosine kinases of src family are enriched in cell-to-cell adherens junctions where the level of tyrosine phosphorylation is elevated
    • Tsukita, S., K. Oishi, T. Akiyama, Y. Yamanashi, T. Yamamoto, and S. Tsukita. 1991. Specific proto-oncogenic tyrosine kinases of src family are enriched in cell-to-cell adherens junctions where the level of tyrosine phosphorylation is elevated. J. Cell Biol. 113(4):867-879.
    • (1991) J. Cell Biol. , vol.113 , Issue.4 , pp. 867-879
    • Tsukita, S.1    Oishi, K.2    Akiyama, T.3    Yamanashi, Y.4    Yamamoto, T.5    Tsukita, S.6
  • 52
    • 0022371564 scopus 로고
    • Desmocalmin: A calmodulin-binding high molecular weight protein isolated from desmosomes
    • Tsukita, S., and S. Tsukita. 1985. Desmocalmin: a calmodulin-binding high molecular weight protein isolated from desmosomes. J. Cell Biol. 101(6):2070-2080.
    • (1985) J. Cell Biol. , vol.101 , Issue.6 , pp. 2070-2080
    • Tsukita, S.1    Tsukita, S.2
  • 53
    • 0027971015 scopus 로고
    • Effect of protein kinase inhibitor H-7 on the contractility, integrity, and membrane anchorage of the microfilament system
    • Volberg, T., B. Geiger, S. Citi, and A.D. Bershadsky. 1994. Effect of protein kinase inhibitor H-7 on the contractility, integrity, and membrane anchorage of the microfilament system. Cell Motil. Cytoskeleton. 29(4):321-338.
    • (1994) Cell Motil. Cytoskeleton , vol.29 , Issue.4 , pp. 321-338
    • Volberg, T.1    Geiger, B.2    Citi, S.3    Bershadsky, A.D.4
  • 54
    • 0026114963 scopus 로고
    • Modulation of intercellular adherens-type junctions and tyrosine phosphorylation of their components in RSV-transformed cultured chick lens cells
    • Volberg, T., B. Geiger, R. Dror, and Y. Zick. 1991. Modulation of intercellular adherens-type junctions and tyrosine phosphorylation of their components in RSV-transformed cultured chick lens cells. Cell Regulation. 2(2):105-120.
    • (1991) Cell Regulation , vol.2 , Issue.2 , pp. 105-120
    • Volberg, T.1    Geiger, B.2    Dror, R.3    Zick, Y.4
  • 57
    • 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. 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 on a central α-helical coiled coil. J. Cell Biol. 114(1):83-99.
    • (1991) J. Cell Biol. , vol.114 , Issue.1 , 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(3): 607-619.
    • (1993) J. Cell Biol. , vol.121 , Issue.3 , 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.