메뉴 건너뛰기




Volumn 24, Issue 4, 1996, Pages 467-484

Phylogenetic occurrence of coiled coil proteins: Implications for tissue structure in metazoa via a coiled coil tissue matrix

Author keywords

alpha helix; heptad repeat; intermediate filament; nuclear matrix

Indexed keywords

ARTICLE; CELL STRUCTURE; EXTRACELLULAR MATRIX; HUMAN; HUMAN CELL; HYDROPHOBICITY; INTERMEDIATE FILAMENT; METAZOON; PHYLOGENY; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE; TANDEM REPEAT;

EID: 0029879607     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-0134(199604)24:4<467::AID-PROT6>3.0.CO;2-B     Document Type: Article
Times cited : (32)

References (60)
  • 1
    • 0025272940 scopus 로고
    • α-Helical coiled coils and bundles: How to design an α-helical protein
    • Cohen, C., Parry, D.A.D. α-Helical coiled coils and bundles: How to design an α-helical protein. Proteins 7:1-15, 1990.
    • (1990) Proteins , vol.7 , pp. 1-15
    • Cohen, C.1    Parry, D.A.D.2
  • 2
    • 0004053615 scopus 로고
    • New York: Worth Publishers
    • Lehninger, A.L. "Biochemistry." New York: Worth Publishers, 1976:127-128.
    • (1976) Biochemistry , pp. 127-128
    • Lehninger, A.L.1
  • 3
    • 9244240852 scopus 로고
    • Foreword
    • Squire, J.M., Vibert, P.J. (eds.). Boston: Academic Press
    • Perutz, M.F. Foreword. In: "Fibrous Protein Structure." Squire, J.M., Vibert, P.J. (eds.). Boston: Academic Press, 1987:vii-viii.
    • (1987) Fibrous Protein Structure
    • Perutz, M.F.1
  • 4
    • 76549252207 scopus 로고
    • The structure of proteins: Two hydrogen-bonded helical configurations of the polypeptide chain
    • Pauling, L., Corey, R.B., Branson, H.R. The structure of proteins: Two hydrogen-bonded helical configurations of the polypeptide chain. Proc. Natl. Acad. Sci. USA 37:205-211, 1951.
    • (1951) Proc. Natl. Acad. Sci. USA , vol.37 , pp. 205-211
    • Pauling, L.1    Corey, R.B.2    Branson, H.R.3
  • 5
    • 0016774265 scopus 로고
    • Tropomyosin coiled-coil interactions: Evidence for an unstaggered structure
    • McLachlan, A.D., Stewart, M. Tropomyosin coiled-coil interactions: Evidence for an unstaggered structure. J. Mol. Biol. 98:293-304, 1975.
    • (1975) J. Mol. Biol. , vol.98 , pp. 293-304
    • McLachlan, A.D.1    Stewart, M.2
  • 6
    • 0025130161 scopus 로고
    • Structural features in the heptad substructure and longer range repeats of two-stranded α-fibrous proteins
    • Conway, J.F., Parry, D.A.D. Structural features in the heptad substructure and longer range repeats of two-stranded α-fibrous proteins. Int. J. Biol. Macromol. 12: 328-334, 1990.
    • (1990) Int. J. Biol. Macromol. , vol.12 , pp. 328-334
    • Conway, J.F.1    Parry, D.A.D.2
  • 7
    • 0024534241 scopus 로고
    • Evidence that the leucine zipper is a coiled coil
    • O'Shea, E.K., Rutkowski, R., Kim, P.S. Evidence that the leucine zipper is a coiled coil. Science 243:538-542, 1989.
    • (1989) Science , vol.243 , pp. 538-542
    • O'Shea, E.K.1    Rutkowski, R.2    Kim, P.S.3
  • 8
    • 0025272236 scopus 로고
    • Secondary structure of a leucine zipper determined by nuclear magnetic resonance spectroscopy
    • Oas, T.G., McIntosh, L.P., O'Shea, E.K., Dahlquist, F.W., Kim, P.S. Secondary structure of a leucine zipper determined by nuclear magnetic resonance spectroscopy. Biochemistry 29:2891-2894, 1990.
    • (1990) Biochemistry , vol.29 , pp. 2891-2894
    • Oas, T.G.1    McIntosh, L.P.2    O'Shea, E.K.3    Dahlquist, F.W.4    Kim, P.S.5
  • 9
    • 0028559469 scopus 로고
    • Effect of chain length on the formation and stability of synthetic peptide alpha-helical coiled coils
    • Su, J.Y., Hodges, R.S., Kay, C.M. Effect of chain length on the formation and stability of synthetic peptide alpha-helical coiled coils. Biochemistry 33:15501-15510, 1994.
    • (1994) Biochemistry , vol.33 , pp. 15501-15510
    • Su, J.Y.1    Hodges, R.S.2    Kay, C.M.3
  • 10
    • 0026693017 scopus 로고
    • The molecular biology of intermediate filament proteins
    • Albers, K., Fuchs, E. The molecular biology of intermediate filament proteins. Int. Rev. Cytol. 134:243-279, 1992.
    • (1992) Int. Rev. Cytol. , vol.134 , pp. 243-279
    • Albers, K.1    Fuchs, E.2
  • 11
    • 0021219218 scopus 로고
    • Epithelial structure revealed by chemical dissection and unembedded electron microscopy
    • Fey, E.G., Capco, D.G., Krochmalnic, G., Penman, S. Epithelial structure revealed by chemical dissection and unembedded electron microscopy. J. Cell Biol. 99:203s-208s, 1984.
    • (1984) J. Cell Biol. , vol.99
    • Fey, E.G.1    Capco, D.G.2    Krochmalnic, G.3    Penman, S.4
  • 12
    • 0343001074 scopus 로고
    • Tumor promoters induce a specific morphological signature in the nuclear matrix-intermediate filament scaffold of Madin-Darby canine kidney (MDCK) cell colonies
    • Fey, E.G., Penman, S. Tumor promoters induce a specific morphological signature in the nuclear matrix-intermediate filament scaffold of Madin-Darby canine kidney (MDCK) cell colonies. Proc. Natl. Acad. Sci. USA 81:4409-4413, 1984.
    • (1984) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 4409-4413
    • Fey, E.G.1    Penman, S.2
  • 13
    • 0021244964 scopus 로고
    • Epithelial cytoskeletal framework and nuclear matrix-intermediate filament scaffold: Three-dimensional organization and protein composition
    • Fey, E.G., Wan, K.M., Penman, S. Epithelial cytoskeletal framework and nuclear matrix-intermediate filament scaffold: Three-dimensional organization and protein composition. J. Cell Biol. 98:1973-1984, 1984.
    • (1984) J. Cell Biol. , vol.98 , pp. 1973-1984
    • Fey, E.G.1    Wan, K.M.2    Penman, S.3
  • 14
    • 0022521416 scopus 로고
    • The nonchromatin substructures of the nucleus: The ribonucleoprotein-containing and RNP-depleted matrices analyzed by sequential fractionation and resinless section electron microscopy
    • Fey, E.G., Krochmalnic, G., Penman, S. The nonchromatin substructures of the nucleus: The ribonucleoprotein-containing and RNP-depleted matrices analyzed by sequential fractionation and resinless section electron microscopy. J. Cell Biol. 102:1654-1665, 1986.
    • (1986) J. Cell Biol. , vol.102 , pp. 1654-1665
    • Fey, E.G.1    Krochmalnic, G.2    Penman, S.3
  • 15
    • 0022821750 scopus 로고
    • The morphological oncogenic signature. Reorganization of epithelial cytoarchitecture and metabolic regulation by tumor promoters and by transformation
    • Fey, E.G., Penman, S. The morphological oncogenic signature. Reorganization of epithelial cytoarchitecture and metabolic regulation by tumor promoters and by transformation. Dev. Biol. 3:81-100, 1986.
    • (1986) Dev. Biol. , vol.3 , pp. 81-100
    • Fey, E.G.1    Penman, S.2
  • 16
    • 0023088072 scopus 로고
    • The protein composition and morphology of the nuclear matrix-intermediate filament scaffold reflect cell type
    • Fey, E.G., Penman, S. The protein composition and morphology of the nuclear matrix-intermediate filament scaffold reflect cell type. Prog. Clin. Biol. Res. 249:263-272, 1987.
    • (1987) Prog. Clin. Biol. Res. , vol.249 , pp. 263-272
    • Fey, E.G.1    Penman, S.2
  • 17
    • 0026356891 scopus 로고
    • Predicting coiled coils from protein sequences
    • Lupas, A., Van Dyke, M., Stock, J. Predicting coiled coils from protein sequences. Science 252:1162-1164, 1991.
    • (1991) Science , vol.252 , pp. 1162-1164
    • Lupas, A.1    Van Dyke, M.2    Stock, J.3
  • 18
    • 0023704381 scopus 로고
    • Nuclear matrix proteins reflect cell type of origin in cultured human cells
    • Fey, E.G., Penman, S. Nuclear matrix proteins reflect cell type of origin in cultured human cells. Proc. Natl. Acad. Sci. USA 85:121-125, 1988.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 121-125
    • Fey, E.G.1    Penman, S.2
  • 19
    • 0024561176 scopus 로고
    • The protein composition of the nuclear matrix of murine P19 embryonic carcinoma cells is differentiation-stage dependent
    • Stuurman, N., van Driel, R., de Jong, L., Meijne, A.M., van Renswoude, J. The protein composition of the nuclear matrix of murine P19 embryonic carcinoma cells is differentiation-stage dependent. Exp. Cell Res. 180:460-466, 1989.
    • (1989) Exp. Cell Res. , vol.180 , pp. 460-466
    • Stuurman, N.1    Van Driel, R.2    De Jong, L.3    Meijne, A.M.4    Van Renswoude, J.5
  • 20
    • 0025107396 scopus 로고
    • Tissue specificity of the hormonal response in sex accessory tissues is associated with the nuclear matrix protein patterns
    • Getzenberg, R.H., Coffey, D.S. Tissue specificity of the hormonal response in sex accessory tissues is associated with the nuclear matrix protein patterns. Mol. Endocrinol. 4:1336-1342, 1990.
    • (1990) Mol. Endocrinol. , vol.4 , pp. 1336-1342
    • Getzenberg, R.H.1    Coffey, D.S.2
  • 21
    • 0028283501 scopus 로고
    • Intermediate filaments: Structure, dynamics, function, and disease
    • Fuchs, E., Weber, K. Intermediate filaments: Structure, dynamics, function, and disease. Annu. Rev. Biochem. 63: 345-382, 1994.
    • (1994) Annu. Rev. Biochem. , vol.63 , pp. 345-382
    • Fuchs, E.1    Weber, K.2
  • 22
    • 0028889852 scopus 로고
    • Drosophila development requires spectrin network formation
    • Deng, H., Lee, J.K., Goldstein, L.S.B., Branton, D. Drosophila development requires spectrin network formation. J. Cell Biol. 128:71-79, 1995.
    • (1995) J. Cell Biol. , vol.128 , pp. 71-79
    • Deng, H.1    Lee, J.K.2    Goldstein, L.S.B.3    Branton, D.4
  • 23
    • 0000557448 scopus 로고
    • Replication of poxviruses
    • Fields, B.N., Knipe, D.M. (eds.). New York: Raven Press
    • Moss, B. Replication of poxviruses. In: "Fundamental Virology." Fields, B.N., Knipe, D.M. (eds.). New York: Raven Press, 1986:649.
    • (1986) Fundamental Virology , pp. 649
    • Moss, B.1
  • 24
    • 0343443742 scopus 로고
    • Effect of mucosal antibodies to M protein on colonization by group A streptococci
    • Switalski, L., Hook, M., Beachey, E. (eds.). New York: Springer-Verlag
    • Fischetti, V.A., Bessen, D. Effect of mucosal antibodies to M protein on colonization by group A streptococci. In: "Molecular Mechanisms of Microbial Adhesion." Switalski, L., Hook, M., Beachey, E. (eds.). New York: Springer-Verlag, 1988:128-142.
    • (1988) Molecular Mechanisms of Microbial Adhesion , pp. 128-142
    • Fischetti, V.A.1    Bessen, D.2
  • 26
    • 0026439779 scopus 로고
    • Isolation and cloning of Omp alpha, a coiled coil protein spanning the periplasmic space of the ancestral eubacteriuni Thermotoga maritima
    • Engel, A.M., Cejka, Z., Lupas, A., Lottspeich, F., Baumeister, W. Isolation and cloning of Omp alpha, a coiled coil protein spanning the periplasmic space of the ancestral eubacteriuni Thermotoga maritima. EMBO J. 11:4369-4378, 1992.
    • (1992) EMBO J. , vol.11 , pp. 4369-4378
    • Engel, A.M.1    Cejka, Z.2    Lupas, A.3    Lottspeich, F.4    Baumeister, W.5
  • 27
    • 0023754370 scopus 로고
    • The role of kinesin and other soluble factors in organelle movement along microtubules
    • Schroer, T.A., Schnapp, B.J., Reese, T.S., Sheetz, M.P. The role of kinesin and other soluble factors in organelle movement along microtubules. J. Cell Biol. 107:1785-1792, 1989.
    • (1989) J. Cell Biol. , vol.107 , pp. 1785-1792
    • Schroer, T.A.1    Schnapp, B.J.2    Reese, T.S.3    Sheetz, M.P.4
  • 28
    • 0026345013 scopus 로고
    • Dynactin, a conserved, ubiquitously expressed component of an activator of vesicle motility mediated by cytoplasmic dynein
    • Gill, S.R., Schroer, T.A., Szilak, I., Steuer, E.R., Sheetz, M.P., Cleveland, D.W. Dynactin, a conserved, ubiquitously expressed component of an activator of vesicle motility mediated by cytoplasmic dynein. J. Cell Biol. 115:1639-1650, 1991.
    • (1991) J. Cell Biol. , vol.115 , pp. 1639-1650
    • Gill, S.R.1    Schroer, T.A.2    Szilak, I.3    Steuer, E.R.4    Sheetz, M.P.5    Cleveland, D.W.6
  • 29
    • 0026069582 scopus 로고
    • The new gene mukB codes for a 177 kd protein with coiled-coil domains involved in chromosome partitioning of E. coli
    • Niki, H., Jaffe, A., Imamura, R., Ogura, T., Hiraga, S. The new gene mukB codes for a 177 kd protein with coiled-coil domains involved in chromosome partitioning of E. coli. EMBO J. 10:183-193, 1991.
    • (1991) EMBO J. , vol.10 , pp. 183-193
    • Niki, H.1    Jaffe, A.2    Imamura, R.3    Ogura, T.4    Hiraga, S.5
  • 30
    • 0027515251 scopus 로고
    • Chromosome partitioning in E. coli
    • Hiraga, S. Chromosome partitioning in E. coli. Curr. Opin. Genet. Dev. 3:789-801, 1993.
    • (1993) Curr. Opin. Genet. Dev. , vol.3 , pp. 789-801
    • Hiraga, S.1
  • 31
    • 0023503414 scopus 로고
    • Laminin and other basement membrane components
    • Martin, G.R., Timpl, R. Laminin and other basement membrane components. Annu. Rev. Cell Biol. 3:57-85, 1987.
    • (1987) Annu. Rev. Cell Biol. , vol.3 , pp. 57-85
    • Martin, G.R.1    Timpl, R.2
  • 32
    • 0018788274 scopus 로고
    • Dissecting the red cell membrane skeleton
    • Lux, S.E. Dissecting the red cell membrane skeleton. Nature 281:426-429, 1979.
    • (1979) Nature , vol.281 , pp. 426-429
    • Lux, S.E.1
  • 33
    • 0026497661 scopus 로고
    • Cytoskeleton-plasma membrane interactions
    • Luna, E.J., Hitt, A.L. Cytoskeleton-plasma membrane interactions. Science 258:955-964, 1992.
    • (1992) Science , vol.258 , pp. 955-964
    • Luna, E.J.1    Hitt, A.L.2
  • 35
    • 0027159977 scopus 로고
    • Expression of plectin mutants indicates a role of COOH-terminal domain in intermediate filament association
    • Wiche, G., Gromov, D., Donovan, A., Castanon, M.J., Fuchs, E. Expression of plectin mutants indicates a role of COOH-terminal domain in intermediate filament association. J. Cell Biol. 121:607-619, 1993.
    • (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
  • 36
    • 0028218025 scopus 로고
    • Pericentrin, a highly conserved centrosome protein involved in microtubule organization
    • Doxsey, S.J., Stein, P., Evans, L., Calarco, P.D., Kirschner, M. Pericentrin, a highly conserved centrosome protein involved in microtubule organization. Cell 76:639-650, 1994.
    • (1994) Cell , vol.76 , pp. 639-650
    • Doxsey, S.J.1    Stein, P.2    Evans, L.3    Calarco, P.D.4    Kirschner, M.5
  • 37
    • 0027172919 scopus 로고
    • Mechanotransduction across the cell surface and through the cytoskeleton
    • Wang, N., Butler, J.P., Ingber, D.E. Mechanotransduction across the cell surface and through the cytoskeleton. Science 260:1124-1127, 1993.
    • (1993) Science , vol.260 , pp. 1124-1127
    • Wang, N.1    Butler, J.P.2    Ingber, D.E.3
  • 38
    • 0027221483 scopus 로고
    • Cellular tensegrity: Defining new rules of biological design that govern the cytoskeleton
    • Ingber, D.E. Cellular tensegrity: Defining new rules of biological design that govern the cytoskeleton. J. Cell Sci. 104:613-627, 1993.
    • (1993) J. Cell Sci. , vol.104 , pp. 613-627
    • Ingber, D.E.1
  • 40
    • 0026730766 scopus 로고
    • Nuclear-cytoskeletal interactions: Evidence for physical connections between the nucleus and cell periphery and their alteration by transformation
    • Pienta, K., Coffey, D.S. Nuclear-cytoskeletal interactions: Evidence for physical connections between the nucleus and cell periphery and their alteration by transformation. J. Cell. Biochem. 49:357-365, 1992.
    • (1992) J. Cell. Biochem. , vol.49 , pp. 357-365
    • Pienta, K.1    Coffey, D.S.2
  • 41
    • 0023425135 scopus 로고
    • Intermediate filaments. Looking for a function
    • Geiger, B. Intermediate filaments. Looking for a function. Nature 329:392-393, 1987.
    • (1987) Nature , vol.329 , pp. 392-393
    • Geiger, B.1
  • 42
    • 0026935532 scopus 로고
    • Intermediate filament proteins: Many unanswered questions, few unquestioned answers
    • Paulin-Levasseur, M. Intermediate filament proteins: Many unanswered questions, few unquestioned answers. Biochem. Cell Biol. 70:842-848, 1992.
    • (1992) Biochem. Cell Biol. , vol.70 , pp. 842-848
    • Paulin-Levasseur, M.1
  • 43
    • 0027943989 scopus 로고
    • A human keratin 14 "knockout": The absence of K14 leads to severe epidermolysis bullosa simplex and a function for an intermediate filament protein
    • Chan, Y., Anton-Lamprecht, I., Yu, Q.C., Jackel, A., Zabel, B., Ernst, J.P., Fuchs, E. A human keratin 14 "knockout": The absence of K14 leads to severe epidermolysis bullosa simplex and a function for an intermediate filament protein. Genes Dev. 8:2574-2587, 1994.
    • (1994) Genes Dev. , vol.8 , pp. 2574-2587
    • Chan, Y.1    Anton-Lamprecht, I.2    Yu, Q.C.3    Jackel, A.4    Zabel, B.5    Ernst, J.P.6    Fuchs, E.7
  • 44
    • 0028836521 scopus 로고
    • Expression of an epidermal keratin protein in liver of transgenic mice causes structural and functional abnormalities
    • Albers, K.M., Davis, F.E., Perrone, T.N., Lee, E.Y., Liu, Y., Vore, M. Expression of an epidermal keratin protein in liver of transgenic mice causes structural and functional abnormalities. J. Cell Biol. 128:157-169, 1995.
    • (1995) J. Cell Biol. , vol.128 , pp. 157-169
    • Albers, K.M.1    Davis, F.E.2    Perrone, T.N.3    Lee, E.Y.4    Liu, Y.5    Vore, M.6
  • 45
    • 0023371437 scopus 로고
    • Lamin B constitutes an intermediate filament attachment site at the nuclear envelope
    • Georgatos, S.D., Blobel, G. Lamin B constitutes an intermediate filament attachment site at the nuclear envelope. J. Cell Biol. 105:117-125, 1987.
    • (1987) J. Cell Biol. , vol.105 , pp. 117-125
    • Georgatos, S.D.1    Blobel, G.2
  • 46
    • 0023372471 scopus 로고
    • Two distinct attachment sites for vimentin along the plasma membrane and the nuclear envelope in avian erythrocytes: A basis for a vectorial assembly of intermediate filaments
    • Georgatos, S.D., Blobel, G. Two distinct attachment sites for vimentin along the plasma membrane and the nuclear envelope in avian erythrocytes: A basis for a vectorial assembly of intermediate filaments. J. Cell Biol. 105:105-115, 1987.
    • (1987) J. Cell Biol. , vol.105 , pp. 105-115
    • Georgatos, S.D.1    Blobel, G.2
  • 47
    • 0027987929 scopus 로고
    • Making a connection: Direct binding between keratin intermediate filaments and desmosomal proteins
    • Kouklis, P.D., Hutton, E., Fuchs, E. Making a connection: Direct binding between keratin intermediate filaments and desmosomal proteins. J. Cell Biol. 127:1049-1060, 1994.
    • (1994) J. Cell Biol. , vol.127 , pp. 1049-1060
    • Kouklis, P.D.1    Hutton, E.2    Fuchs, E.3
  • 48
    • 0027195421 scopus 로고
    • The structure of tricohyalin. Potential multiple roles as a functional EF-hand-like calcium-binding protein, a cornified cell envelope precursor, and an intermediate filament-associated (cross-linking) protein
    • Lee, S.C., Kim, I.G., Marekov, L.N., O'Keefe, E.J., Parry, D.A.D., Steinert, P.M. The structure of tricohyalin. Potential multiple roles as a functional EF-hand-like calcium-binding protein, a cornified cell envelope precursor, and an intermediate filament-associated (cross-linking) protein. J. Biol. Chem. 268:12164-12176, 1993.
    • (1993) J. Biol. Chem. , vol.268 , pp. 12164-12176
    • Lee, S.C.1    Kim, I.G.2    Marekov, L.N.3    O'Keefe, E.J.4    Parry, D.A.D.5    Steinert, P.M.6
  • 49
    • 0028022979 scopus 로고
    • NuMA/centrophilin: Sequence analysis of the coiled-coil rod domain
    • Parry, D.A. NuMA/centrophilin: Sequence analysis of the coiled-coil rod domain. Biophys. J. 67:1203-1206, 1994.
    • (1994) Biophys. J. , vol.67 , pp. 1203-1206
    • Parry, D.A.1
  • 50
    • 0024498788 scopus 로고
    • Highly localized tracks of specific transcripts within interphase nuclei visualized by in situ hybridization
    • Lawrence, J.B., Singer, R.H., Marselle, L.M. Highly localized tracks of specific transcripts within interphase nuclei visualized by in situ hybridization. Cell 57:493-502, 1989.
    • (1989) Cell , vol.57 , pp. 493-502
    • Lawrence, J.B.1    Singer, R.H.2    Marselle, L.M.3
  • 51
    • 0026065461 scopus 로고
    • Preservation of in vivo RNA distribution within the nuclear matrix demonstrated by in situ hybridization coupled with biochemical fractionation
    • Xing, Y., Lawrence, J.B. Preservation of in vivo RNA distribution within the nuclear matrix demonstrated by in situ hybridization coupled with biochemical fractionation. J. Cell Biol. 112:1055-1063, 1991.
    • (1991) J. Cell Biol. , vol.112 , pp. 1055-1063
    • Xing, Y.1    Lawrence, J.B.2
  • 53
    • 0027435594 scopus 로고
    • Immunological characterization of lamins in the nuclear matrix of onion cells
    • Minguez, A., Moreno Diaz de la Espina, S. Immunological characterization of lamins in the nuclear matrix of onion cells. J. Cell Sci. 106:431-439, 1993.
    • (1993) J. Cell Sci. , vol.106 , pp. 431-439
    • Minguez, A.1    Moreno Diaz De La Espina, S.2
  • 54
    • 0026629410 scopus 로고
    • Intermediate filament antigens of 60 and 65 kDa in the nuclear matrix of plants: Their detection and localization
    • Frederick, S.E., Mangan, M.E., Carey, J.B., Gruber, P.J. Intermediate filament antigens of 60 and 65 kDa in the nuclear matrix of plants: Their detection and localization. Exp. Cell Res. 199:213-222, 1992.
    • (1992) Exp. Cell Res. , vol.199 , pp. 213-222
    • Frederick, S.E.1    Mangan, M.E.2    Carey, J.B.3    Gruber, P.J.4
  • 55
    • 0028596270 scopus 로고
    • Why should stationary plant cells have such dynamic microtubules?
    • Lloyd, C. Why should stationary plant cells have such dynamic microtubules? Mol. Biol. Cell 5:1277-1280, 1994.
    • (1994) Mol. Biol. Cell , vol.5 , pp. 1277-1280
    • Lloyd, C.1
  • 57
    • 0026802042 scopus 로고
    • Dimeric transcription factor families: It takes two to tango but who decides on partners and the venue?
    • Lee, K.A. Dimeric transcription factor families: It takes two to tango but who decides on partners and the venue? J. Cell Sci. 103:9-14, 1992.
    • (1992) J. Cell Sci. , vol.103 , pp. 9-14
    • Lee, K.A.1
  • 58
    • 0026052405 scopus 로고
    • Diversity and specificity in transcriptional regulation: The benefits of heterotypic dimerization
    • Lamb, P., McKnight, S.L. Diversity and specificity in transcriptional regulation: The benefits of heterotypic dimerization. Trends Biochem. Sci. 16:417-422, 1991.
    • (1991) Trends Biochem. Sci. , vol.16 , pp. 417-422
    • Lamb, P.1    McKnight, S.L.2
  • 59
    • 0018140371 scopus 로고
    • Role of cell shape in growth control
    • Folkman, J., Moscona, A. Role of cell shape in growth control. Nature 273:345-349, 1979.
    • (1979) Nature , vol.273 , pp. 345-349
    • Folkman, J.1    Moscona, A.2
  • 60
    • 0028025616 scopus 로고
    • Programming gene expression in developing epidermis
    • Byrne, C., Tainsky, M., Fuchs, E. Programming gene expression in developing epidermis. Development 120:2369-2383, 1994.
    • (1994) Development , vol.120 , pp. 2369-2383
    • Byrne, C.1    Tainsky, M.2    Fuchs, E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.