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Ando, S., Tanabe, K., Gonda, Y., Sato, C. and Inagaki, M (1989). Domain-and sequence-specific phosphorylation of vimentin induces disassembly of the filament structure. Biochemistry 28, 2974-2979.[Medline]

Ando, S., Tokui, T., Yamauchi, T., Sugiura, H., Tanabe, K. and Inagaki, M (1991). Evidence that Ser-82 is a unique phosphorylation site on vimentin for Ca2+-calmodulin-dependent protein kinase II. Biochem. Biophys. Res. Commun 175, 955-962.[Medline]

Balcarek, J. M. and Cowan, N. J (1985). Structure of the mouse glial fibrillary acidic protein gene: Implications for the evolution of the intermediate filament multigene family. Nucl. Acids Res 13, 5527-5543.[Abstract/Free Full Text]

Bujard, H., Gentz, R., Lanzer, M., Stueber, D., Mueller, M., Ibrahimi, I., Haeuptle, M.-T. and Dobberstein, B (1987). A T5 promoter-based transcription-translation system for the analysis of proteins in vitroand in vivo. Meth. Enzymol 155, 416-433.[Medline]

Cabral, F. and Gottesman, M. M (1979). Phosphorylation of the 10-nm filament protein from chinese hamster ovary cells. J. Biol. Chem 254, 6203-6206.[Free Full Text]

Carter, P., Bedouelle, H. and Winter, G (1985). Improved oligonucleotide site-directed mutagenesis using the M13 vectors. Nucl. Acids Res 13, 4431-4443.[Abstract/Free Full Text]

Carter, P (1987). Improved olignucleotide-directed mutagenesis using M13 vectors. Meth. Enzymol 154, 382-403.[Medline]

Chin, S. S. M., Macioce, P. and Liem, R. K. H (1991). Effects of truncated neurofilament proteins on the endogenous intermediate filaments in transfected fibroblasts. J. Cell Sci 99, 335-350.[Abstract/Free Full Text]

Chou, Y.-H., Rosevaar, E. and Goldman, R. D (1989). Phosphorylation and dissassembly of intermediate filaments in mitotic cells. Proc. Nat. Acad. Sci. USA 86, 1885-1889.[Abstract/Free Full Text]

Chou, Y.-H., Biscoff, J. R., Beach, D. and Goldman, R (1990). Intermediate filament reorganisation during mitosis is mediated by p34cdc2phosphorylation of vimentin. Cell 62, 1063-1071.[Medline]

Chou, Y.-H., Ngai, K. L. and Goldman, R (1991). The regulation of intermediate filament reorganization in mitosis. p34cdc2 phosphorylates vimentin at a unique N-terminal site. J. Biol. Chem 266, 7325-7328.[Abstract/Free Full Text]

Coulombe, P. A (1993). The cellular and molecular biology of keratins: beginning a new era. Curr. Opin. Cell Biol 5, 17-29.[Medline]

Debus, E., Weber, K. and Osborn, M (1983). Monoclonal antibodies specific for glial fibrillary acidic (GFa) protein and for each of the neurofilament triplet polypeptides. Differentiation 25, 193-203.[Medline]

Eriksson, J. E., Opal, P. and Goldman, R. D (1992). Intermediate filament dynamics. Curr. Opin. Cell Biol 4, 99-104.[Medline]

Evans, R. M (1988). Cyclic AMP-dependent protein kinase-induced vimentin filament disassembly involves modification of the N-terminal domain of intermediate filament subunits. FEBS Lett 234, 73-78.[Medline]

Evans, R. M (1989). Phosphorylation of vimentin in mitotically selected cells. In vitro cyclic AMP-independent kinase and calcium-stimulated phosphatase activities. J. Cell Biol 108, 67-78.[Abstract/Free Full Text]

Feinstein, D. L., Weinmaster, G. A. and Milner, R. J (1992). Isolation of cDNA clones encoding rat glial fibrillary acidic protein: expression in astrocytes and in Schwaan cells. J. Neurosci. Res 32, 1-14.[Medline]

Ferrari, S., Battini, R., Kaczmarek, L., Rittling, S., Calabretta, B., de Riel, K., Philiponis, V., Wei, J. F. and Baserga, R (1986). Coding sequence and growth regulation of the human vimentin gene. Mol. Cell Biol 6, 3614-3620.[Abstract/Free Full Text]

Ferrari, S., Cannizzaro, L. A., Battini, R., Huebner, K. and Baserga, R (1987). The gene encoding human vimentin is located on the short arm of chromosome 10. Amer. J. Hum. Genet 41, 616-626.[Medline]

Fleigner, K. H., Ching, G. Y. and Liem, R. K. H (1990). The predicted amino acid sequence of-internexin is that of a novel neuronal intermediate filament protein. EMBO J 9, 749-755.[Medline]

Geisler, N., Kaufmann, E. and Weber, K (1982). Protein-chemical characterization of three structurally distinct domains along the protofilament unit of desmin 10 nm filaments. Cell 30, 277-286.[Medline]

Geisler, N. and Weber, K (1982). The amino acid sequence of chicken muscle desmin provides a common structural model for intermediate filament proteins. EMBO J 1, 1649-1656.[Medline]

Geisler, N., Plessmann, U. and Weber, K (1983). Amino acid sequence characterization of mammalian vimentin, the mesenchymal intermediate filament protein. FEBS Lett 163, 22-24.[Medline]

Geisler, N. and Weber, K (1983). Amino acid sequence data on glial fibrillary acidic protein (GFa); implications for the subdivision of intermediate filaments into epithelial and non-epithelial members. EMBO J 2, 2059-2063.[Medline]

Geisler, N. and Weber, K (1988). Phosphorylation of desmin in vitro inhibits formation of intermediate filaments; identification of three kinase A sites in the aminoterminal head domain. EMBO J 7, 15-20.[Medline]

Geisler, N., Hatzfeld, M. and Weber, K (1989). Phosphorylation in vitro of vimentin by protein kinase A and C is restricted to the head domain.Identification of phosphoserine sites and their influence on filament formation. Eur. J. Cell Biol 183, 441-447.

Gill, S. R., Wong, P. C., Monteiro, M. J. and Cleveland, D. W (1990). Assembly properties of dominant and recessive mutations in the small mouse neurofilament (NF-L) subunit. J. Cell Biol 111, 2005-2019.[Abstract/Free Full Text]

Hatzfeld, M. and Weber, K (1990). The coiled coil of in vitro assembled keratin filaments is a heterodimer of type I and type II keratins; use of site directed mutagenesis and recombinant protein expression. J. Cell Biol 110, 1199-1210.[Abstract/Free Full Text]

Hatzfeld, M. and Weber, K (1990). Tailless keratins assemble into regular intermediate filaments in vitro. J. Cell Sci 97, 317-324.[Abstract/Free Full Text]

Hatzfeld, M., Dodemont, H., Plessmann, U. and Weber, K (1992). Truncation of recombinant vimentin by ompT. Identification of a short motif in the head domain necessary for assembly of type III intermediate filament proteins. FEBS Lett 302, 239-242.[Medline]

Herrmann, H., Fouquet, B. and Franke, W. W (1989). Expression of intermediate filament proteins during development of Xenopus laevis. I. cDNA clones encoding different forms of vimentin. Development 105, 279-298.[Abstract]

Herrmann, H., Fouquet, B. and Franke, W. W (1989). Expression of intermediate filament proteins during development of Xenopus laevis . II. Identification and molecular characterization of desmin. Development 105, 299-307.[Abstract]

Herrmann, H., Hofmann, I. and Franke, W. W (1992). Identification of a nonpeptide motif in the vimetin head domain involved in intermediate filament assembly. J. Mol. Biol 223, 637-650.[Medline]

Hofmann, I. and Herrmann, H (1992). Interference in vimentin assembly in vitro by synthetic peptides derived from the vimentin head domain. J. Cell Sci 101, 687-700.[Abstract/Free Full Text]

Honer, B., Shoeman, R. L. and Traub, P (1991). Human immunodeficiency virus type 1 protease microinjected into cultured human skin fibroblasts cleaves vimentin and affects cytoskeletal and nuclear architecture. J. Cell Sci 100, 799-807.[Abstract/Free Full Text]

Inagaki, M., Nishi, Y., Nishizawa, K., Matsuyama, M. and Sato, C (1987). Site-specific phosphorylation induces disassembly of vimentin filaments in vitro. Nature 328, 649-652.[Medline]

Inagaki, M., Gonda, Y., Matsuyama, M., Nishizawa, K., Nishi, Y. and Sato, C (1988). Intermediate filament reconstitution in vitro. The role of phosphorylation on the assembly-disassembly of desmin. J. Biol. Chem 263, 5970-5978.[Abstract/Free Full Text]

Inagaki, M., Takahara, H., Nishi, Y., Sugawara, K. and Sato, C (1989). Ca2+-dependant deimination-induced disassembly of intermediate filaments involves the specific modification of the amino-terminal head domain. J. Biol. Chem 264, 18119-18127.[Abstract/Free Full Text]

Inagaki, M., Gonda, Y., Nishizawa, K., Kitamura, S., Sato, C., Ando, S., Tanabe, K., Kikuchi, K., Tsuiki, S. and Nishi, Y (1990). Phosphorylation sites linked to glial filament disassembly in vitro locate in a non--helical head domain. J. Biol. Chem 265, 4722-4729.[Abstract/Free Full Text]

Karpov, V., Landon, F., Djabali, K., Gros, F. and Portier, M. M (1992). Structure of the mouse gene encoding peripherin: a neuronal intermediate filament protein. Biol. Cell 76, 43-8.[Medline]

Kaufmann, E., Weber, K. and Geisler, N (1985). Intermediate filament forming ability of desmin derivatives lacking either the amino-terminal 67 or the carboxy-terminal 27 residues. J. Mol. Biol 185, 733-742.[Medline]

Kitamura, S., Ando, S., Shibata, M., Tanabe, K., Sato, C. and Inagaki, M (1989). Protein kinase C phosphorylation of desmin at four serine residues within the non--helical head domain. J. Biol. Chem 264, 5674-5678.[Abstract/Free Full Text]

Laemmli, U (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 277, 680-685.

Leonard, D. G., Gorham, J. D., Cole, P., Greene, L. A. and Ziff, E. B (1988). A nerve growth factor-regulated messenger RNA encodes a new intermediate filament protein. J. Cell Biol 106, 181-193.[Abstract/Free Full Text]

Lewis, S. A., Balcarek, J. M., Krek, V., Shelanski, M. and Cowan, N. J (1984). Sequence of a cDNA encoding mouse glial fibrillary acidic protein: Structural conservation of intermediate filaments. Proc. Nat. Acad. Sci. USA 81, 2743-2746.[Abstract/Free Full Text]

Li, Z., Lilienbaum, A., Butler-Browne, G. S. and Paulin, D (1989). Human desmin-coding gene: Complete nucleotide sequence, characterization and regulation of expression during myogenesis and development. Gene 78, 243-254.[Medline]

Lu, X. and Lane, E. B (1990). Retrovirus mediated transgenic keratin expression in cultured fibroblasts: Specific domain functions in keratin stabilization and filament formation. Cell 62, 681-696.[Medline]

Lu, X., Quinlan, R. A., Steel, J. B. and Lane, E. B (1993). Networkincorporation of intermediate filament molecules differs between preexisting and newly assembling filaments. Exp. Cell Res 208, 218-225.[Medline]

Magin, T. M., Hatzfeld, M. and Franke, W. W (1987). Analysis of cytokeratin domains by cloning and expression of intact and deleted polypeptides in Escherichia coli. EMBO J 6, 2607-2615.[Medline]

Matsuoka, Y., Nishizawa, K., Yano, T., Shibata, M., Ando, S., Takahashi, T. and Inagaki, M (1992). Two different protein kinases act on a different time schedule as glial filament kinases during mitosis. EMBO J 11, 2895-2902.[Medline]

Mattice, W. L., Riser, J. M. and Clark, D. S (1976). Conformational properties of the complexes formed by proteins and sodium dodecyl sulphate. Biochemistry 15, 4264-4272.[Medline]

Moir, R. D., Quinlan, R. A. and Stewart, M (1990). Expression and characterization of human lamin C. FEBS Lett 268, 301-305.[Medline]

Moll, R., Franke, W. W., Schiller, D. L., Geiger, B. and Krepler, R (1982). The catalogue of human keratins: patterns of expression in normal epithelia, tumours and cultured cells. Cell 31, 11-24.[Medline]

Moon, R. T. and Lazarides, E (1983). Canavanine inhibits vimentin assembly but not its synthesis in chicken embryo erythroid cells. J. Cell Biol 97, 1309-1314.[Abstract/Free Full Text]

Nagai, K. and Th\277gersen, H.-C (1987). Synthesis and sequence-specific proteolysis of a hybrid protein produced in Escherichia coli. Meth. Enzymol 153, 461-481.[Medline]

Nelson, W. J. and Traub, P (1983). Proteolysis of vimentin and desmin by the Ca2+-activated proteinase specific for these intermediate filament proteins. Mol. Cell Biol 3, 1146-1156.[Abstract/Free Full Text]

Nicholl, I. and Quinlan, R. A (1994). Chaperone activity of-crystallins modulates intermediate filament assembly. EMBO J 13, 945-953.[Medline]

Ngai, J., Bond, V. C., Wold, B. J. and Lazarides, E (1987). Expression of transfected vimentin genes in differentiating murine erythroleukemia cells reveals divergent cis-acting regulation of avian and mammalian vimentin sequences. Mol. Cell Biol 7, 3955-3970.[Abstract/Free Full Text]

Ngai, J., Coleman, T. R. and Lazarides, E (1990). Localisation of newly synthesised vimentin subunits reveals a novel mechanism of intermediate filament assembly. Cell 60, 415-427.[Medline]

Perides, G., Kuhn, S., Scherbarth, A. and Traub, P (1987). Probing of the structural stability of vimentin and desmin-type intermediate filaments with Ca2+-activated proteinase, thrombin and lysine-specific endoproteinase Lys-C. Eur. J. Cell Biol 43, 450-458.[Medline]

Quax, W., van, d. B. L., Egberts, W. V., Ramaekers, F. and Bloemendal, H (1985). Characterization of the hamster desmin gene: expression and formation of desmin filaments in nonmuscle cells after gene transfer. Cell 43, 327-338.[Medline]

Quinlan, R. A. and Franke, W. W (1982). Heterpolymer filaments of vimentin and desmin in vascular smooth muscle tissue and cultured baby hamster kidney cells demonstrated by chemical crosslinking. Proc. Nat. Acad. Sci. USA 79, 3452-3456.[Abstract/Free Full Text]

Quinlan, R. A. and Franke, W. W (1983). Molecular interactions in intermediate sized-filaments revealed by chemical cross-linking: heteroploymers of vimentin and glial filament protein in cultured human glioma cells. Eur. J. Cell Biol 132, 477-484.

Quinlan, R. A., Moir, R. D. and Stewart, M (1989). Expression in Escherichia coli of fragments of glial fibrillary acidic protein: characterization, assembly properties and paracrystal formation. J. Cell Sci 93, 71-83.[Abstract/Free Full Text]

Quinlan, R. A. and Stewart, M (1991). Molecular interactions in intermediate filaments. BioEssays 13, 597-600.[Medline]

Quinlan, R. A., Carter, J. M., Hutcheson, A. M. and Cambell, D. G (1992). The 53 kDa polypeptide component of the bovin lens fibre cell cytoskeleton is derived from the 115 kDa beaded filament protein: evidence for a fibre cell specific intermediate filament protein. Curr. Eye Res 11, 909-921.[Medline]

Raats, J. M. H., Pieper, F. R., Vree Egberts, W. T. M., Verrijp, K. N., Ramaekers, F. C. S. and Bloemendal, H (1990). Assembly of amino-terminally deleted desmin in vimentin-free cells. J. Cell Biol 111, 1971-1985.[Abstract/Free Full Text]

Raats, J. M., Gerards, W. L., Schreuder, M. I., Grund, C., Henderik, J. B., Hendriks, I. L., Ramaekers, F. C. and Bloemendal, H (1992). Biochemical and structural aspects of transiently and stably expressed mutant desmin in vimentin-free and vimentin-containing cells. Eur. J. Cell Biol 58, 108-127.[Medline]

Rayment, I., Rypniewski, W. R., Scmidt-B\212se, K., Smith, R., Tomchick, D. R., Benning, M. M., Winkelman, D. A., Wesenberg, G. and Holden, H. M (1993). Three-dimensional structure of myosin subfragment-1: a molecular motor. Science 261, 50-58.[Abstract/Free Full Text]

Reeves, S. A., Helman, L. J., Allison, A. and Israel, M. A (1989). Molecular cloning and primary structure of human glial fibrillary acidic protein. Proc. Nat. Acad. Sci. USA 86, 5178-5182.[Abstract/Free Full Text]

Reynolds, J. A. and Tanford, C (1970). The gross conformation of protein-sodium dodecyl sulphate complexes. J. Biol. Chem 245, 5161-5165.[Abstract/Free Full Text]

Saeed, T. and Ip, W (1989). Assembly properties of 2 CNBr fragments of avian desmin that correspond to the headpiece domain and helix-1b. Biochem. Biophys. Res. Commun 165, 1059-1066.[Medline]

Sanger, F., Nicklen, S. and Coulson, A. R (1977). DNA sequencing with chain-terminating inhibitors. Proc. Nat. Acad. Sci. USA 75, 5463-5467.

Schauder, B., Bl\232cker, H., Frank, R. and McCarthy, J. E. G (1987). Inducible expression vectors incorporating the Escherichia coli atpE translational initiation region. Gene 52, 279-283.[Medline]

Schoeman, R. L. and Traub, P (1993). Assembly of intermediate filaments. BioEssays 15, 605-611.[Medline]

Shoeman, R. L., Mothes, E., Honer, B., Kesselmeier, C. and Traub, P (1991). Effect of human immunodeficiency virus type 1 protease on the intermediate filament subunit protein vimentin: cleavage, in vitro assembly and altered distribution of filaments in vivo following microinjection of protease. Acta Histochem. Suppl 41, 129-141.[Medline]

Steinert, P. M. and Roop, D. R (1988). Molecular and cellular biology of intermediate filaments. Annu. Rev. Biochem 57, 593-625.[Medline]

Stewart, M (1993). Intermediate filament structure and assembly. Curr. Opin. Cell Biol 5, 3-11.[Medline]

Stuber, D., Ibrahimi, I., Cutler, D., Dobberstein, B. and Bujard, H (1984). A novel in vitro transcription-translation system. Accurate and efficient synthesis of single proteins from cloned DNA sequences. EMBO J 3, 3143-3148.[Medline]

Tokutaki, S., Hutchison, S. B., Pachter, J. S. and Liem, R. K. H (1983). A batchwise purification procedure of neurofilament proteins. Anal. Biochem 135, 102-105.[Medline]

Traub, P. and Vorgias, C. E (1983). Involvement of the N-terminal polypeptide of vimentin in the formation of intermediate filaments. J. Cell Sci 63, 43-67.[Abstract]

Traub, P. and Vorgias, C. E (1984). Differential effect of arginine modification with 1,2-cyclohexanedione on the capacity of vimentin and desmin to assemble into intermediate filaments and to bind to nucleic acids. J. Cell Sci 63, 1-20.

Traub, P., Scherbarth, A., Wiegers, W. and Shoeman, R. L (1992). Salt-stable interaction of the amino-terminal head region of vimentin with the alpha-helical rod domain of cytoplasmic intermediate filament proteins and its relevance to protofilament structure and filament formation and stability. J. Cell Sci 101, 363-381.[Abstract/Free Full Text]

Wessel, D. and Flugge, U. I (1984). A method for the quantitative recovery of protein in dilute solution in the presence of detergents and lipids. Anal. Biochem 138, 141-143.[Medline]

Wilson, A. K., Coulombe, P. A. and Fuchs, E (1992). The roles of K5 and K14 head, tail, and R/K L L E G E domains in keratin filament assembly in vitro. J. Cell Biol 119, 401-414.[Abstract/Free Full Text]

Zehner, Z. E., Li, Y., Roe, B. A., Paterson, B. M. and Sax, C. M (1987). The chicken vimentin gene. Nucleotide sequence, regulatory elements, and comparison to the hamster gene. J. Biol. Chem 262, 8112-8120.[Abstract/Free Full Text]




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