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Volumn 2004, Issue 78, 2004, Pages 3-24

Isolation, characterization, and in vitro assembly of intermediate filaments

Author keywords

[No Author keywords available]

Indexed keywords

INTERMEDIATE FILAMENT PROTEIN; LAMIN; RECOMBINANT PROTEIN;

EID: 14244253598     PISSN: 0091679X     EISSN: None     Source Type: Book Series    
DOI: 10.1016/s0091-679x(04)78001-2     Document Type: Review
Times cited : (124)

References (62)
  • 1
    • 0022961251 scopus 로고
    • Separation of cytokeratin polypeptides by gel electrophoretic and chromatographic tecniques and their identification by immunoblotting
    • Achtstaetter, T., Hatzfeld, M., Quinlan, R. A., Parmelee, D. C., and Franke, W. W. (1986). Separation of cytokeratin polypeptides by gel electrophoretic and chromatographic tecniques and their identification by immunoblotting. Methods Enzymol. 134, 355-371.
    • (1986) Methods Enzymol , vol.134 , pp. 355-371
    • Achtstaetter, T.1    Hatzfeld, M.2    Quinlan, R.A.3    Parmelee, D.C.4    Franke, W.W.5
  • 2
    • 0023419545 scopus 로고
    • A glow discharge unit to render electron microscope grids and other surfaces hydrophilic
    • Aebi, U., and Pollard, T. D. (1987). A glow discharge unit to render electron microscope grids and other surfaces hydrophilic. J. Electron Microsc. Tech. 7, 29-33.
    • (1987) J. Electron Microsc. Tech. , vol.7 , pp. 29-33
    • Aebi, U.1    Pollard, T.D.2
  • 3
    • 0022519369 scopus 로고
    • The nuclear lamina is a meshwork of intermediate-type filaments
    • Aebi, U., Cohn, J., Buhle, L., and Gerace, L. (1986). The nuclear lamina is a meshwork of intermediate-type filaments. Nature 323, 560-564.
    • (1986) Nature , vol.323 , pp. 560-564
    • Aebi, U.1    Cohn, J.2    Buhle, L.3    Gerace, L.4
  • 4
    • 0020591925 scopus 로고
    • The fibrillar substructure of keratin filaments unraveled
    • Aebi, U., Fowler, W. E., Rew, P., and Sun, T. T. (1983). The fibrillar substructure of keratin filaments unraveled. J. Cell Biol. 97, 1131-1143.
    • (1983) J. Cell Biol. , vol.97 , pp. 1131-1143
    • Aebi, U.1    Fowler, W.E.2    Rew, P.3    Sun, T.T.4
  • 7
    • 0031043895 scopus 로고    scopus 로고
    • Identification of protein p270/Tpr as a constitutive component of the nuclear pore complex-attached intranuclear filaments
    • Cordes, V. C., Reidenbach, S., Rackwitz, H.-R., and Franke, W. W. (1997). Identification of protein p270/Tpr as a constitutive component of the nuclear pore complex-attached intranuclear filaments. J. Cell Biol. 136, 515-529.
    • (1997) J. Cell Biol. , vol.136 , pp. 515-529
    • Cordes, V.C.1    Reidenbach, S.2    Rackwitz, H.-R.3    Franke, W.W.4
  • 8
    • 0024245405 scopus 로고
    • Identification of attachment proteins for DNA in Chinese hamster ovary cells
    • Cress, A. E., and Kurath, K. M. (1988). Identification of attachment proteins for DNA in Chinese hamster ovary cells. J. Biol. Chem. 263, 19678-19683.
    • (1988) J. Biol. Chem. , vol.263 , pp. 19678-19683
    • Cress, A.E.1    Kurath, K.M.2
  • 9
    • 0025341392 scopus 로고
    • Elucidating the early stages of keratin filament assembly
    • Coulombe, P. A., and Fuchs, E. (1990). Elucidating the early stages of keratin filament assembly. J. Cell Biol. 111, 153-169.
    • (1990) J. Cell Biol. , vol.111 , pp. 153-169
    • Coulombe, P.A.1    Fuchs, E.2
  • 10
    • 0025633303 scopus 로고
    • Deletions in epidermal keratins leading to alterations in filament organization in vivo and in intermediate filament assembly in vitro
    • Coulombe, P. A., Chan, Y.-M., Albers, K., and Fuchs, E. (1990). Deletions in epidermal keratins leading to alterations in filament organization in vivo and in intermediate filament assembly in vitro. J. Cell Biol. 111, 3049-3064.
    • (1990) J. Cell Biol. , vol.111 , pp. 3049-3064
    • Coulombe, P.A.1    Chan, Y.-M.2    Albers, K.3    Fuchs, E.4
  • 13
    • 0018675951 scopus 로고
    • Two-dimensional gel electrophoresis and computer analysis of proteins synthesized by clonal cell lines
    • Garrels, J. I. (1979). Two-dimensional gel electrophoresis and computer analysis of proteins synthesized by clonal cell lines. J. Biol. Chem. 254, 7961-7977.
    • (1979) J. Biol. Chem. , vol.254 , pp. 7961-7977
    • Garrels, J.I.1
  • 14
    • 0020171992 scopus 로고
    • Proteinchemical characterization of three structurally distinct domains along the protofilament unit of desmin 10nm filaments
    • Geisler, N., Kaufmann, E., and Weber, K. (1982). Proteinchemical characterization of three structurally distinct domains along the protofilament unit of desmin 10nm filaments. Cell 30, 277-286.
    • (1982) Cell , vol.30 , pp. 277-286
    • Geisler, N.1    Kaufmann, E.2    Weber, K.3
  • 15
    • 0018840796 scopus 로고
    • The nuclear envelope lamina is reversibly depolymerized during mitosis
    • Gerace, L., and Blobel, G. (1980). The nuclear envelope lamina is reversibly depolymerized during mitosis. Cell 19, 277-287.
    • (1980) Cell , vol.19 , pp. 277-287
    • Gerace, L.1    Blobel, G.2
  • 16
    • 0025745453 scopus 로고
    • In vitro reconstitution of recombinant lamin a and a lamin a mutant lacking the carboxy-terminal tail
    • Gieffers, C., and Krohne, G. (1991). In vitro reconstitution of recombinant lamin A and a lamin A mutant lacking the carboxy-terminal tail. Eur. J. Cell Biol. 55, 191-199.
    • (1991) Eur. J. Cell Biol. , vol.55 , pp. 191-199
    • Gieffers, C.1    Krohne, G.2
  • 17
    • 0026478894 scopus 로고
    • Pathway of incorporation of microinjected lamin a into the nuclear envelope
    • Goldman, A. E., Moir, R. D., Montag-Lowy, M., Stewart, M., and Goldman, R. D. (1992). Pathway of incorporation of microinjected lamin A into the nuclear envelope. J. Cell Biol. 119, 725-735.
    • (1992) J. Cell Biol. , vol.119 , pp. 725-735
    • Goldman, A.E.1    Moir, R.D.2    Montag-Lowy, M.3    Stewart, M.4    Goldman, R.D.5
  • 18
    • 0012426291 scopus 로고    scopus 로고
    • Glycerol spraying/low-angle rotary metal shadowing
    • Academic Press, San Diego
    • Häner, M., Bremer, A., and Aebi, U. (1998). Glycerol spraying/low-angle rotary metal shadowing. In "Cell Biology. A Laboratory Handbook," 2nd ed., Vol. III, pp. 292-298. Academic Press, San Diego.
    • (1998) Cell Biology. A Laboratory Handbook, 2nd Ed. , vol.3 , pp. 292-298
    • Häner, M.1    Bremer, A.2    Aebi, U.3
  • 21
    • 3943078618 scopus 로고    scopus 로고
    • Intermediate filaments: Molecular structure, assembly mechanism, and integration into functionally distinct intracellular scaffolds
    • Herrmann, H., and Aebi, U. (2004). Intermediate filaments: Molecular structure, assembly mechanism, and integration into functionally distinct intracellular scaffolds. Annu. Rev. Biochem. 73, 749-789.
    • (2004) Annu. Rev. Biochem. , vol.73 , pp. 749-789
    • Herrmann, H.1    Aebi, U.2
  • 22
    • 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
  • 23
    • 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
  • 24
    • 0022271595 scopus 로고
    • r surface protein of a human leukaemia cell line (THP-1) crossreacts with the fibroblast intermediate filament protein vimentin
    • r surface protein of a human leukaemia cell line (THP-1) crossreacts with the fibroblast intermediate filament protein vimentin. J. Cell Sci. 73, 87-103.
    • (1984) J. Cell Sci. , vol.73 , pp. 87-103
    • Herrmann, H.1    Aberer, W.2    Majdic, O.3    Schuler, G.4    Wiche, G.5
  • 25
    • 0026559105 scopus 로고
    • Identification of a nonapeptide motif in the vimentin head domain involved in intermediate filament assembly
    • Herrmann, H., Hofmann, I., and Franke, W. W. (1992). Identification of a nonapeptide motif in the vimentin head domain involved in intermediate filament assembly. J. Mol. Biol. 223, 637-650.
    • (1992) J. Mol. Biol. , vol.223 , pp. 637-650
    • Herrmann, H.1    Hofmann, I.2    Franke, W.W.3
  • 26
    • 0030596170 scopus 로고    scopus 로고
    • Structure and assembly properties of the intermediate filament protein vimentin: The role of its head, rod and tail domains
    • Herrmann, H., Häner, M., Brettel, M., Müller, S. A., Goldie, K. N., Fedtke, B., Lustig, A., Franke, W. W., and Aebi, U. (1996). Structure and assembly properties of the intermediate filament protein vimentin: The role of its head, rod and tail domains. J. Mol. Biol. 264, 933-953.
    • (1996) J. Mol. Biol. , vol.264 , pp. 933-953
    • Herrmann, H.1    Häner, M.2    Brettel, M.3    Müller, S.A.4    Goldie, K.N.5    Fedtke, B.6    Lustig, A.7    Franke, W.W.8    Aebi, U.9
  • 27
    • 0344096498 scopus 로고    scopus 로고
    • Characterization of distinct early assembly units of different intermediate filament proteins
    • Herrmann, H., Häner, M., Brettel, M., Ku, N. O., and Aebi, U. (1999). Characterization of distinct early assembly units of different intermediate filament proteins. J. Mol. Biol. 286, 1403-1420.
    • (1999) J. Mol. Biol. , vol.286 , pp. 1403-1420
    • Herrmann, H.1    Häner, M.2    Brettel, M.3    Ku, N.O.4    Aebi, U.5
  • 28
    • 0036443637 scopus 로고    scopus 로고
    • Characterization of early assembly intermediates of recombinant human keratins
    • Herrmann, H., Wedig, T., Porter, R. M., Lane, E. B., and Aebi, U. (2002). Characterization of early assembly intermediates of recombinant human keratins. J. Struct. Biol. 137, 82-96.
    • (2002) J. Struct. Biol. , vol.137 , pp. 82-96
    • Herrmann, H.1    Wedig, T.2    Porter, R.M.3    Lane, E.B.4    Aebi, U.5
  • 29
    • 0037282536 scopus 로고    scopus 로고
    • Functional complexity of intermediate filament cytoskeletons: From structure to assembly to gene ablation
    • Herrmann, H., Hesse, M., Reichenzeller, M., Aebi, U., and Magin, T. M. (2003). Functional complexity of intermediate filament cytoskeletons: From structure to assembly to gene ablation. Int. Rev. Cytol. 223, 83-175.
    • (2003) Int. Rev. Cytol. , vol.223 , pp. 83-175
    • Herrmann, H.1    Hesse, M.2    Reichenzeller, M.3    Aebi, U.4    Magin, T.M.5
  • 30
    • 0034907507 scopus 로고    scopus 로고
    • Genes for intermediate filament proteins and the draft sequence of the human genome: Novel keratin genes and a surprisingly high number of pseudogenes related to keratin genes 8 and 18
    • Hesse, M., Magin, T. M., and Weber, K. (2001). Genes for intermediate filament proteins and the draft sequence of the human genome: Novel keratin genes and a surprisingly high number of pseudogenes related to keratin genes 8 and 18. J. Cell Sci. 114, 2569-2575.
    • (2001) J. Cell Sci. , vol.114 , pp. 2569-2575
    • Hesse, M.1    Magin, T.M.2    Weber, K.3
  • 31
    • 0032248098 scopus 로고    scopus 로고
    • Measuring the assembly kinetics and binding properties of intermediate filament proteins
    • Hofmann, I. (1998). Measuring the assembly kinetics and binding properties of intermediate filament proteins. Subcell. Biochem. 31, 363-380.
    • (1998) Subcell. Biochem. , vol.31 , pp. 363-380
    • Hofmann, I.1
  • 32
    • 0026343580 scopus 로고
    • Assembly and structure of calcium-induced thick vimentin filaments
    • Hofmann, I., Herrmann, H., and Franke, W. W. (1991). Assembly and structure of calcium-induced thick vimentin filaments. Eur. J. Cell Biol. 56, 328-341.
    • (1991) Eur. J. Cell Biol. , vol.56 , pp. 328-341
    • Hofmann, I.1    Herrmann, H.2    Franke, W.W.3
  • 33
    • 0019332718 scopus 로고
    • Desmin from avian smooth muscle. Purification and partial characterization
    • Huiatt, T. W., Robson, R. M., Arakawa, N., and Stromer, M. H. (1980). Desmin from avian smooth muscle. Purification and partial characterization. J. Biol. Chem. 255, 6981-6989.
    • (1980) J. Biol. Chem. , vol.255 , pp. 6981-6989
    • Huiatt, T.W.1    Robson, R.M.2    Arakawa, N.3    Stromer, M.H.4
  • 34
    • 0026017781 scopus 로고
    • A torsion pendulum for measurement of the viscoelasticity of biopolymers and its application to actin networks
    • Janmey, P. A. (1991). A torsion pendulum for measurement of the viscoelasticity of biopolymers and its application to actin networks. J. Biophys. Biochem. Methods 22, 41-53.
    • (1991) J. Biophys. Biochem. Methods , vol.22 , pp. 41-53
    • Janmey, P.A.1
  • 35
    • 0025765110 scopus 로고
    • Viscoeleastic properties of vimentin compared with other filamentous biopolymer networks
    • Janmey, P. A., Euteneuer, U., Traub, P., and Schliwa, M. (1991). Viscoeleastic properties of vimentin compared with other filamentous biopolymer networks. J. Cell Biol. 113, 155-160.
    • (1991) J. Cell Biol. , vol.113 , pp. 155-160
    • Janmey, P.A.1    Euteneuer, U.2    Traub, P.3    Schliwa, M.4
  • 37
    • 0037227428 scopus 로고    scopus 로고
    • The single nuclear lamin of Caenorhabditis elegans for in vitro stable intermediate filaments and paracrystals with a reduced axial periodicity
    • Karabinos, A., Schünemann, J., Meyer, M., Aebi, U., and Weber, K. (2003). The single nuclear lamin of Caenorhabditis elegans for in vitro stable intermediate filaments and paracrystals with a reduced axial periodicity. J. Mol. Biol. 325, 241-247.
    • (2003) J. Mol. Biol. , vol.325 , pp. 241-247
    • Karabinos, A.1    Schünemann, J.2    Meyer, M.3    Aebi, U.4    Weber, K.5
  • 38
    • 0027138210 scopus 로고
    • Covalent binding of biological samples to solid supports for scanning probe microscopy in buffer solution
    • Karrasch, S., Dolder, M., Schabert, F., Ramsden, J., and Engel, A. (1993). Covalent binding of biological samples to solid supports for scanning probe microscopy in buffer solution. Biophys. J. 65, 2437-2446.
    • (1993) Biophys. J. , vol.65 , pp. 2437-2446
    • Karrasch, S.1    Dolder, M.2    Schabert, F.3    Ramsden, J.4    Engel, A.5
  • 39
    • 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 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 40
    • 0027254919 scopus 로고
    • The mechanism of interaction of filaggrin with intermediate filaments. The ionic zipper hypothesis
    • Mack, J. W., Steven, A. C., and Steinert, P. M. (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
  • 43
    • 0031194365 scopus 로고    scopus 로고
    • Structural changes in native membrane proteins monitored at subnanometer resolution with the atomic force microscope: A review
    • Müller, D. J., Schoenenberger, C.-A., Schabert, F., and Engel, A. (1997). Structural changes in native membrane proteins monitored at subnanometer resolution with the atomic force microscope: A review. J. Struct. Biol. 119, 149-157.
    • (1997) J. Struct. Biol. , vol.119 , pp. 149-157
    • Müller, D.J.1    Schoenenberger, C.-A.2    Schabert, F.3    Engel, A.4
  • 44
    • 0023517015 scopus 로고
    • Synthesis and sequence-specific proteolysis of hybrid proteins produced in Escherichia coli
    • Nagai, K., and Thogersen, H.-C. (1987). Synthesis and sequence-specific proteolysis of hybrid proteins produced in Escherichia coli. Methods Enzymol. 153, 461-481.
    • (1987) Methods Enzymol , vol.153 , pp. 461-481
    • Nagai, K.1    Thogersen, H.-C.2
  • 45
    • 0020965175 scopus 로고
    • 2+-activated proteinase specific for these intermediate filament proteins
    • 2+-activated proteinase specific for these intermediate filament proteins. Mol. Cell. Biol. 3, 1146-1156.
    • (1983) Mol. Cell. Biol. , vol.3 , pp. 1146-1156
    • Nelson, W.J.1    Traub, P.2
  • 46
    • 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
  • 47
    • 0020769815 scopus 로고
    • Primary and secondary structure of hamster vimentin predicted from the nucleotide sequence
    • Quax-Jeuken, Y. E. F. M., Quax, W. J., and Bloemendal, H. (1983). Primary and secondary structure of hamster vimentin predicted from the nucleotide sequence. Proc. Natl. Acad. Sci. USA 80, 3548-3552.
    • (1983) Proc. Natl. Acad. Sci. USA , vol.80 , pp. 3548-3552
    • Quax-Jeuken, Y.E.F.M.1    Quax, W.J.2    Bloemendal, H.3
  • 48
    • 0021645934 scopus 로고
    • Heterotypic tetramer (A2D2) complexes of non-epidermal keratins isolated from cytoskeletons of rat hepatocytes and hepatoma cells
    • Quinlan, R. A., Cohlberg, J. A., Schiller, D. L., Hatzfeld, M., and Franke, W. W. (1984). Heterotypic tetramer (A2D2) complexes of non-epidermal keratins isolated from cytoskeletons of rat hepatocytes and hepatoma cells. J. Mol. Biol. 178, 365-388.
    • (1984) J. Mol. Biol. , vol.178 , pp. 365-388
    • Quinlan, R.A.1    Cohlberg, J.A.2    Schiller, D.L.3    Hatzfeld, M.4    Franke, W.W.5
  • 50
    • 0035050279 scopus 로고    scopus 로고
    • Defining the mycoplasma 'cytoskelton': The protein composition of the Triton X-100 insoluble fraction of the bacterium Mycoplasma pneumoniae determined by 2-D gel electrophoresis and mass spectrometry
    • Regula, J. T., Boguth, G., Gorg, A., Hegermann, J., Mayer, F., Frank, R., and Herrmann, R. (2001). Defining the mycoplasma 'cytoskelton': The protein composition of the Triton X-100 insoluble fraction of the bacterium Mycoplasma pneumoniae determined by 2-D gel electrophoresis and mass spectrometry. Microbiology 147, 1045-1057.
    • (2001) Microbiology , vol.147 , pp. 1045-1057
    • Regula, J.T.1    Boguth, G.2    Gorg, A.3    Hegermann, J.4    Mayer, F.5    Frank, R.6    Herrmann, R.7
  • 51
    • 0019888143 scopus 로고
    • Reconstitution of intermediate-sized filaments from denatured monomeric vimentin
    • Renner, W., Franke, W. W., Schmidt, E., Geisler, N., Weber, K., and Mandelkow, E. (1981). Reconstitution of intermediate-sized filaments from denatured monomeric vimentin. J. Mol. Biol. 149, 285-306.
    • (1981) J. Mol. Biol. , vol.149 , pp. 285-306
    • Renner, W.1    Franke, W.W.2    Schmidt, E.3    Geisler, N.4    Weber, K.5    Mandelkow, E.6
  • 52
    • 0028984981 scopus 로고
    • Truncation mutagenesis of the non-α-helical carboxyterminal tail domain of vimentin reveals contributions to cellular localization but not to filament assembly
    • Rogers, K. R., Eckelt, A., Nimmrich, V., Janssen, K. P., Schliwa, M., Herrmann, H., and Franke, W. W. (1995). Truncation mutagenesis of the non-α-helical carboxyterminal tail domain of vimentin reveals contributions to cellular localization but not to filament assembly. Eur. J. Cell Biol. 66, 136-150.
    • (1995) Eur. J. Cell Biol. , vol.66 , pp. 136-150
    • Rogers, K.R.1    Eckelt, A.2    Nimmrich, V.3    Janssen, K.P.4    Schliwa, M.5    Herrmann, H.6    Franke, W.W.7
  • 53
    • 0017864456 scopus 로고
    • Biochemical and immunological analysis of rapidly purified 10-nm filaments from baby hamster kidney (BHK-21) cells
    • Starger, J. M., Brown, W. E., Goldman, A. E., and Goldman, R. D. (1978). Biochemical and immunological analysis of rapidly purified 10-nm filaments from baby hamster kidney (BHK-21) cells. J. Cell Biol. 78, 93-109.
    • (1978) J. Cell Biol. , vol.78 , pp. 93-109
    • Starger, J.M.1    Brown, W.E.2    Goldman, A.E.3    Goldman, R.D.4
  • 54
    • 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
  • 55
    • 0017054951 scopus 로고
    • Self-assembly of bovine epidermal keratin filaments in vitro
    • Steinert, P. M., Idler, W. W., and Zimmermann, S. B. (1976). Self-assembly of bovine epidermal keratin filaments in vitro. J. Mol. Biol. 108, 547-567.
    • (1976) J. Mol. Biol. , vol.108 , pp. 547-567
    • Steinert, P.M.1    Idler, W.W.2    Zimmermann, S.B.3
  • 57
    • 0027435278 scopus 로고
    • Diversity of intermediate filament structure. Evidence that the alignment of coiled-coil molecules in vimentin is different from that in keratin intermediate filaments
    • Steinert, P. M., Marekov, L. N., and Parry, D. A. (1993). Diversity of intermediate filament structure. Evidence that the alignment of coiled-coil molecules in vimentin is different from that in keratin intermediate filaments. J. Biol. Chem. 268, 24916-24925.
    • (1993) J. Biol. Chem. , vol.268 , pp. 24916-24925
    • Steinert, P.M.1    Marekov, L.N.2    Parry, D.A.3
  • 58
    • 0019406415 scopus 로고
    • Disassembly of synthetic 10-nm desmin filaments from smooth muscle into protofilaments
    • Stromer, M. H., Huiatt, T. W., Richardson, R. L., and Robson, R. M. (1981). Disassembly of synthetic 10-nm desmin filaments from smooth muscle into protofilaments. Eur. J. Cell Biol. 25, 136-143.
    • (1981) Eur. J. Cell Biol. , vol.25 , pp. 136-143
    • Stromer, M.H.1    Huiatt, T.W.2    Richardson, R.L.3    Robson, R.M.4
  • 59
    • 0032249645 scopus 로고    scopus 로고
    • Transient electric birefringence in the study of intermediate filament assembly
    • van Amerongen, H., Kooijman, M., and Bloemendal, M. (1998). Transient electric birefringence in the study of intermediate filament assembly. Subcell. Biochem. 31, 399-421.
    • (1998) Subcell. Biochem. , vol.31 , pp. 399-421
    • Amerongen, H.1    Kooijman, M.2    Bloemendal, M.3
  • 60
    • 0021075446 scopus 로고
    • Isolation, purification and characterization of the intermediate filament protein desmin from porcine smooth muscle
    • Vorgias, C. E., and Traub, P. (1983). Isolation, purification and characterization of the intermediate filament protein desmin from porcine smooth muscle. Prep. Biochem. 13, 227-243.
    • (1983) Prep. Biochem. , vol.13 , pp. 227-243
    • Vorgias, C.E.1    Traub, P.2
  • 61
    • 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
  • 62
    • 0036151692 scopus 로고    scopus 로고
    • Pairwise assembly determines the intrinsic potential for self-organization and mechanical properties of keratin filaments
    • Yamada, S., Wirtz, D., and Coulombe, P. A. (2002). Pairwise assembly determines the intrinsic potential for self-organization and mechanical properties of keratin filaments. Mol. Biol. Cell. 13, 382-392.
    • (2002) Mol. Biol. Cell. , vol.13 , pp. 382-392
    • Yamada, S.1    Wirtz, D.2    Coulombe, P.A.3


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