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Volumn 33, Issue 3, 1996, Pages 223-240

Low molecular weight rat fibroblast tropomyosin 5 (TM-5): cDNA cloning, actin-binding, localization, and coiled-coil interactions

Author keywords

coiled coil; rat fibroblasts; TM 5; tropomyosin

Indexed keywords

ACTIN; COMPLEMENTARY DNA; TROPOMYOSIN;

EID: 0029932698     PISSN: 08861544     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-0169(1996)33:3<223::AID-CM6>3.0.CO;2-B     Document Type: Article
Times cited : (42)

References (52)
  • 1
    • 0028359143 scopus 로고
    • Identification of novel alternatively spliced isoforms of the tropomyosin-encodmg gene, TMnm, in the rat cochlea
    • Beisel, K.W., and Kennedy, J.E. (1994): Identification of novel alternatively spliced isoforms of the tropomyosin-encodmg gene, TMnm, in the rat cochlea. Gene 143:251-256.
    • (1994) Gene , vol.143 , pp. 251-256
    • Beisel, K.W.1    Kennedy, J.E.2
  • 2
    • 0022930024 scopus 로고
    • Low Mr tropomyosin isoforms from chicken brain and intestinal epithelium have distinct actin-binding properties
    • Broschat, K O., and Burgess, D R. (1986): Low Mr tropomyosin isoforms from chicken brain and intestinal epithelium have distinct actin-binding properties. J. Biol. Chem. 261:13350-13359.
    • (1986) J. Biol. Chem. , vol.261 , pp. 13350-13359
    • Broschat, K.O.1    Burgess, D.R.2
  • 3
    • 0021888890 scopus 로고
    • Renaturation of skeletal muscle tropomyosin: Implications for in vivo assembly
    • Brown, H.R., and Schachat, F.H. (1985): Renaturation of skeletal muscle tropomyosin: Implications for in vivo assembly. Proc. Natl. Acad. Sci. U.S.A. 82:2359-2363.
    • (1985) Proc. Natl. Acad. Sci. U.S.A. , vol.82 , pp. 2359-2363
    • Brown, H.R.1    Schachat, F.H.2
  • 4
    • 0018639079 scopus 로고
    • Isolation of biologically active ribonucleic acid from sources enriched in ribonuclease
    • Chirgwin, J.M., Przybyla, A.E., MacDonald, R.J., and Rutter, W.J. (1979): Isolation of biologically active ribonucleic acid from sources enriched in ribonuclease. Biochemistry 18:5294-5299.
    • (1979) Biochemistry , vol.18 , pp. 5294-5299
    • Chirgwin, J.M.1    Przybyla, A.E.2    MacDonald, R.J.3    Rutter, W.J.4
  • 5
    • 13344291324 scopus 로고
    • Organization of the hTMnm gene: Implications for the evolution of muscle and nonmuscle tropomyosins
    • Clayton, L., Reinach, F.C., Chumbley, G.M., and MacLeod, A.R. (1988): Organization of the hTMnm gene: Implications for the evolution of muscle and nonmuscle tropomyosins. J. Biol. Chem, 264:2935-2944.
    • (1988) J. Biol. Chem , vol.264 , pp. 2935-2944
    • Clayton, L.1    Reinach, F.C.2    Chumbley, G.M.3    MacLeod, A.R.4
  • 6
    • 0025057161 scopus 로고
    • Generation of skeletal, smooth and low molecular weight non-muscle tropomyosin isoforms from the chicken tropomyosin I gene
    • Forry-Schaudies, S., Maihle, N.J., and Hughes, S.H. (1990): Generation of skeletal, smooth and low molecular weight non-muscle tropomyosin isoforms from the chicken tropomyosin I gene. J. Mol. Biol. 211:321-330.
    • (1990) J. Mol. Biol. , vol.211 , pp. 321-330
    • Forry-Schaudies, S.1    Maihle, N.J.2    Hughes, S.H.3
  • 7
    • 0028822231 scopus 로고
    • Specificity of dimer formation in tropomyosins: Influence of alternatively spliced exons on homodimer and heterodimer assembly
    • Gimona, M . Watakabe, A., and Helfman, D.M. (1995): Specificity of dimer formation in tropomyosins: Influence of alternatively spliced exons on homodimer and heterodimer assembly. Proc. Natl. Acad. Sci. U.S.A. 92:9776-9780.
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 9776-9780
    • Gimona, M.1    Watakabe, A.2    Helfman, D.M.3
  • 8
    • 0025247677 scopus 로고
    • Four fibroblast tropomyosin isoforms are expressed from the rat átropomyosin gene through the use of alternative promoters and alternative RNA processing
    • Goodwin, L.O., Lees-Miller, J.P., Leonard, M.A., Cheley, S.B., and Helfman, D.M. (1991): Four fibroblast tropomyosin isoforms are expressed from the rat átropomyosin gene through the use of alternative promoters and alternative RNA processing. Mol. Cell. Biol. 10:1729-1742.
    • (1991) Mol. Cell. Biol. , vol.10 , pp. 1729-1742
    • Goodwin, L.O.1    Lees-Miller, J.P.2    Leonard, M.A.3    Cheley, S.B.4    Helfman, D.M.5
  • 9
    • 0022820961 scopus 로고
    • Nonmuscle and muscle tropomyosin isoforms are expressed from a single gene by alternative RNA splicing and polyadenylation
    • Heifman, D.M., Cheley, S., Kuismanen, E., Finn, L.A., and Yamawaki-Kataoka, Y. (1986): Nonmuscle and muscle tropomyosin isoforms are expressed from a single gene by alternative RNA splicing and polyadenylation. Mol. Cell. Biol. 6:3582-3595.
    • (1986) Mol. Cell. Biol. , vol.6 , pp. 3582-3595
    • Heifman, D.M.1    Cheley, S.2    Kuismanen, E.3    Finn, L.A.4    Yamawaki-Kataoka, Y.5
  • 10
    • 0024432710 scopus 로고
    • Annealing of gelsolin-severed actin filaments by tropomyosin in the presence of calcium. Potentiation of the annealing process by caldesmon
    • Ishikawa, R., Yamashiro, S., and Matsumura, F. (1989b): Annealing of gelsolin-severed actin filaments by tropomyosin in the presence of calcium. Potentiation of the annealing process by caldesmon. J. Biol. Chem. 264:16746-16770.
    • (1989) J. Biol. Chem. , vol.264 , pp. 16746-16770
    • Ishikawa, R.1    Yamashiro, S.2    Matsumura, F.3
  • 11
    • 0024565757 scopus 로고
    • Differential modulation of actin-severing activity of gelsolin by multiple isoforms of cultured rat cell tropomyosin
    • Ishikawa, R., Yamashiro, S., and Matsumura, F. (1989a): Differential modulation of actin-severing activity of gelsolin by multiple isoforms of cultured rat cell tropomyosin J. Biol. Chem. 264: 7490-7497
    • (1989) J. Biol. Chem. , vol.264 , pp. 7490-7497
    • Ishikawa, R.1    Yamashiro, S.2    Matsumura, F.3
  • 12
    • 0026001768 scopus 로고
    • Smooth muscle tropomyosin coiled-coil dimers: Subunit composition, assembly, and end-to-end interaction
    • Jancso, A., and Graceffa, P. (1991): Smooth muscle tropomyosin coiled-coil dimers: Subunit composition, assembly, and end-to-end interaction. J. Biol Chem. 265:5891-5897.
    • (1991) J. Biol Chem. , vol.265 , pp. 5891-5897
    • Jancso, A.1    Graceffa, P.2
  • 13
    • 0021747202 scopus 로고
    • Recognition of cap structure in splicing in vitro mRNA precursors
    • Kornarska, M.M., Padgett, R.A., and Sharp. P.A. (1984): Recognition of cap structure in splicing in vitro mRNA precursors. Cell 38:731-736.
    • (1984) Cell , vol.38 , pp. 731-736
    • Kornarska, M.M.1    Padgett, R.A.2    Sharp, P.A.3
  • 14
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage Tj
    • Laemmli, U.K. (1970): Cleavage of structural proteins during the assembly of the head of bacteriophage Tj. Nature 227.680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 15
    • 0026218642 scopus 로고
    • The molecular basis for tropomyosin isoform diversity
    • Lees-Miller, J.P., and Helfman, D M. (1991): The molecular basis for tropomyosin isoform diversity. Bioessays 13:429-437.
    • (1991) Bioessays , vol.13 , pp. 429-437
    • Lees-Miller, J.P.1    Helfman, D.M.2
  • 16
    • 0025247677 scopus 로고
    • Three novel brain tropomyosin isoforms arc expressed from the rat α-tropomyosin gene through the use of alternative promoters and alternative RNA processing
    • Lees-Miller, J.P., Goodwin, L.O., and Helfman, D.M. (1990a): Three novel brain tropomyosin isoforms arc expressed from the rat α-tropomyosin gene through the use of alternative promoters and alternative RNA processing. Mol. Cell. Biol. 10:1729-1742.
    • (1990) Mol. Cell. Biol. , vol.10 , pp. 1729-1742
    • Lees-Miller, J.P.1    Goodwin, L.O.2    Helfman, D.M.3
  • 17
    • 0025286527 scopus 로고
    • Structure and complete nucleotide sequence of the gene encoding rat fibroblast tropomyosin 4
    • Lees-Miller, J.P , Yan. A., and Helfman, D.M (1990b): Structure and complete nucleotide sequence of the gene encoding rat fibroblast tropomyosin 4. J. Mol. Biol. 213:399-405.
    • (1990) J. Mol. Biol. , vol.213 , pp. 399-405
    • Lees-Miller, J.P.1    Yan, A.2    Helfman, D.M.3
  • 18
    • 0025058736 scopus 로고
    • Unfolding/refolding studies of smooth muscle muscle tropomyosin. Evidence for a chain exchange mechanism in the preferential assembly of the native heterodimer
    • Lehrer, S.S., and Qian, Y. (1990). Unfolding/refolding studies of smooth muscle muscle tropomyosin. Evidence for a chain exchange mechanism in the preferential assembly of the native heterodimer. J. Biol. Chem. 265:1134-1138.
    • (1990) J. Biol. Chem. , vol.265 , pp. 1134-1138
    • Lehrer, S.S.1    Qian, Y.2
  • 19
    • 0024310236 scopus 로고
    • Assembly of the native heterodimer of Rana esculenta tropomyosin by chain exchange
    • Lehrer, S.S., Qian, Y., and Hvidt, S. (1989): Assembly of the native heterodimer of Rana esculenta tropomyosin by chain exchange. Science 246:926-928.
    • (1989) Science , vol.246 , pp. 926-928
    • Lehrer, S.S.1    Qian, Y.2    Hvidt, S.3
  • 20
    • 0021928967 scopus 로고
    • Tropomyosin isoforms in chicken embryo fibroblasts: Purification, characterization, and changes in Rous sarcoma virus transformed cells
    • Lin, J.J.-C., Helfman, D.M., Hughes, S.H., and Chou, C.-S (1985): Tropomyosin isoforms in chicken embryo fibroblasts: Purification, characterization, and changes in Rous sarcoma virus transformed cells. J. Cell Biol. 100:692-703.
    • (1985) J. Cell Biol. , vol.100 , pp. 692-703
    • Lin, J.J.-C.1    Helfman, D.M.2    Hughes, S.H.3    Chou, C.-S.4
  • 21
    • 0023808937 scopus 로고
    • Differential localization of tropomyosin isoforms in cultured nonmuscle cells
    • Lin, J.J.-C., Hegmann, T.E., and Lin, J.L.-C. (1988): Differential localization of tropomyosin isoforms in cultured nonmuscle cells. J. Cell Biol. 107:563-572.
    • (1988) J. Cell Biol. , vol.107 , pp. 563-572
    • Lin, J.J.-C.1    Hegmann, T.E.2    Lin, J.L.-C.3
  • 24
    • 0022379564 scopus 로고
    • Purification and characterization of multiple isoforms of tropomyosin from rat cultured cells
    • Matsumura, F., and Yamashiro-Matsumura, S. (1985): Purification and characterization of multiple isoforms of tropomyosin from rat cultured cells. J. Biol. Chem. 260:13851-13859.
    • (1985) J. Biol. Chem. , vol.260 , pp. 13851-13859
    • Matsumura, F.1    Yamashiro-Matsumura, S.2
  • 25
    • 0021059305 scopus 로고
    • Differential expression of tropomyosin forms in the microfilaments isolated from normal and transformed rat cultured cells
    • Matsumura, F., Lin, J.J.-C., Yamashiro-Matsumura, S., Thomas, G.P., and Topp, W.C. (1983): Differential expression of tropomyosin forms in the microfilaments isolated from normal and transformed rat cultured cells. J, Biol. Chem. 258:13954-13964.
    • (1983) J, Biol. Chem. , vol.258 , pp. 13954-13964
    • Matsumura, F.1    Lin, J.J.-C.2    Yamashiro-Matsumura, S.3    Thomas, G.P.4    Topp, W.C.5
  • 26
    • 0022410877 scopus 로고
    • An actin-depolymerizing protein (destrin) from porcine kidney. Its action on F-actin containing or lacking tropomyosin
    • Nishida, E., Muneyuki, E., Maekawa, S., Ohta, Y., and Sakai H. (1985): An actin-depolymerizing protein (destrin) from porcine kidney. Its action on F-actin containing or lacking tropomyosin. Biochemistry 24:6624-6630.
    • (1985) Biochemistry , vol.24 , pp. 6624-6630
    • Nishida, E.1    Muneyuki, E.2    Maekawa, S.3    Ohta, Y.4    Sakai, H.5
  • 27
    • 0027408064 scopus 로고
    • Expression of smooth muscle and nonmuscie tropomyosins in E. coli and characterization of bactenally produced tropomyosins
    • Novy, R.E., Liu, L.-F., Lin, C.S., Helfman, D.M., and Lin, J.J.-C. (1993a): Expression of smooth muscle and nonmuscie tropomyosins in E. coli and characterization of bactenally produced tropomyosins. Biochim. Biophys. Acta, 1162:255-265.
    • (1993) Biochim. Biophys. Acta , vol.1162 , pp. 255-265
    • Novy, R.E.1    Liu, L.-F.2    Lin, C.S.3    Helfman, D.M.4    Lin, J.J.-C.5
  • 28
    • 0027367331 scopus 로고
    • In vitro functional characterization of bacterially expressed human fibroblast tropomyosin isoforms and their chimeric mutants
    • Novy, R.E., Sellers, J.R., Liu, L.-F., and Lin. J.J.-C. (1993b): In vitro functional characterization of bacterially expressed human fibroblast tropomyosin isoforms and their chimeric mutants. Cell Motil. Cytoskeleton 26:248-261.
    • (1993) Cell Motil. Cytoskeleton , vol.26 , pp. 248-261
    • Novy, R.E.1    Sellers, J.R.2    Liu, L.-F.3    Lin, J.J.-C.4
  • 29
    • 0016711037 scopus 로고
    • High resolution two-dimensional electrophoresis of proteins
    • O'Farrell, P.H. (1975); High resolution two-dimensional electrophoresis of proteins. J. Biol. Chem. 250:4007-4021.
    • (1975) J. Biol. Chem. , vol.250 , pp. 4007-4021
    • O'Farrell, P.H.1
  • 30
    • 0020021878 scopus 로고
    • Purification of muscle actin
    • Pardee, J.D., and Spudich, J.A. (1982): Purification of muscle actin. Methods Enzymol. 85:164-181.
    • (1982) Methods Enzymol. , vol.85 , pp. 164-181
    • Pardee, J.D.1    Spudich, J.A.2
  • 31
    • 0017191401 scopus 로고
    • An efficient mRNA-dependent translation system from reticulocyte lysates
    • Pelham, H.R., and Jackson, R.J. (1976): An efficient mRNA-dependent translation system from reticulocyte lysates. Eur. J. Biochem. 67:247-256.
    • (1976) Eur. J. Biochem. , vol.67 , pp. 247-256
    • Pelham, H.R.1    Jackson, R.J.2
  • 32
    • 0026713920 scopus 로고
    • In vitro and in vivo characterization of four fibroblast tropomyosins produced in bacteria: TM-2, TM-3, TM-5a and TM-5b are colocalized in interphase fibroblasts
    • Pittenger, M.F., and Helfman, D.M. (1992): In vitro and in vivo characterization of four fibroblast tropomyosins produced in bacteria: TM-2, TM-3, TM-5a and TM-5b are colocalized in interphase fibroblasts. J. Cell Biol. 118:841-858.
    • (1992) J. Cell Biol. , vol.118 , pp. 841-858
    • Pittenger, M.F.1    Helfman, D.M.2
  • 34
    • 0029091378 scopus 로고
    • Alternatively spliced exons of the β tropomyosin gene exhibit different affinities for F-actin and effects with nonmuscle caldesmon
    • Pittenger, M.F., Kistler, A., and Helfman, D.M. (1995): Alternatively spliced exons of the β tropomyosin gene exhibit different affinities for F-actin and effects with nonmuscle caldesmon. J. Cell Sci. 108:3253-3265.
    • (1995) J. Cell Sci. , vol.108 , pp. 3253-3265
    • Pittenger, M.F.1    Kistler, A.2    Helfman, D.M.3
  • 35
    • 0027240578 scopus 로고
    • Expression of transduced tropomyosin 1 cDNA suppresses neoplastic growth of cells transformed by the ras oncogene
    • Prasad, G.L., Fuldner, R. A., and Cooper, H.L. (1993): Expression of transduced tropomyosin 1 cDNA suppresses neoplastic growth of cells transformed by the ras oncogene. Proc. Natl. Acad. Sci. U.S.A. 90:7039-7043.
    • (1993) Proc. Natl. Acad. Sci. U.S.A. , vol.90 , pp. 7039-7043
    • Prasad, G.L.1    Fuldner, R.A.2    Cooper, H.L.3
  • 36
    • 0023180728 scopus 로고
    • α-Tropomyosin gene organization
    • Ruiz-Opazo, N., and Nadal-Ginard, B. (1987): α-Tropomyosin gene organization. J. Biol. Chem. 262:4755-4765.
    • (1987) J. Biol. Chem. , vol.262 , pp. 4755-4765
    • Ruiz-Opazo, N.1    Nadal-Ginard, B.2
  • 39
    • 0018762433 scopus 로고
    • Structure and functions of tropomyosins from muscle and nonmtiscle sources
    • Smillie, L. B. (1979): Structure and functions of tropomyosins from muscle and nonmtiscle sources. Trends Biochem. Sci. 4:151-54.
    • (1979) Trends Biochem. Sci. , vol.4 , pp. 151-154
    • Smillie, L.B.1
  • 40
    • 0025917462 scopus 로고
    • Intracompartmental sorting of essential myosin light chains: Molecular dissection and in vivo monitoring by epitope tagging
    • Soldati, T., and Perriard, J.-C. (1991): Intracompartmental sorting of essential myosin light chains: Molecular dissection and in vivo monitoring by epitope tagging. Cell 66:277-289.
    • (1991) Cell , vol.66 , pp. 277-289
    • Soldati, T.1    Perriard, J.-C.2
  • 41
    • 0027375844 scopus 로고
    • Brain-specific tropomyosins TMBr-1 and TMBr-3 have distinct patterns of expression during development and in adult brain
    • Stamm, S., Casper, D., Lees-Miller, J.P., and Helfman, D.M. (1993): Brain-specific tropomyosins TMBr-1 and TMBr-3 have distinct patterns of expression during development and in adult brain. Proc. Natl. Acad. Sci. U.S.A. 90:9857-9861.
    • (1993) Proc. Natl. Acad. Sci. U.S.A. , vol.90 , pp. 9857-9861
    • Stamm, S.1    Casper, D.2    Lees-Miller, J.P.3    Helfman, D.M.4
  • 43
    • 0026010429 scopus 로고
    • Requirement of microfilaments in sorting of actin mRNAs.b
    • Sundell, C.C., and Singer, R.H. (1991): Requirement of microfilaments in sorting of actin mRNAs.b Science 253:1275-1277.
    • (1991) Science , vol.253 , pp. 1275-1277
    • Sundell, C.C.1    Singer, R.H.2
  • 44
    • 0024998854 scopus 로고
    • Nucleotide sequence of cDNA for nonmuscle tropomyosin 5 of mouse fibroblast
    • Takenaga, K., Nakamura, Y., Kageyama, H., and Sakiyama, S. (1990): Nucleotide sequence of cDNA for nonmuscle tropomyosin 5 of mouse fibroblast. Biochim. Biophys. Acta 1087:101-103.
    • (1990) Biochim. Biophys. Acta , vol.1087 , pp. 101-103
    • Takenaga, K.1    Nakamura, Y.2    Kageyama, H.3    Sakiyama, S.4
  • 45
    • 0025186708 scopus 로고
    • Differential transcriptional activation by oct-1 and oct-2: Interdependent activation domains induce oct-2 phosphorylation
    • 63860
    • Tanaka, M., and Herr, W. (1990): Differential transcriptional activation by oct-1 and oct-2: Interdependent activation domains induce oct-2 phosphorylation. Cell 63860:375-386.
    • (1990) Cell , pp. 375-386
    • Tanaka, M.1    Herr, W.2
  • 46
    • 0028178083 scopus 로고
    • α-Tropomyosin and cardiac troponin T mutations cause familial hypertrophie cardiomyopathy: A disease of the sarcomere
    • Thierfelder, L.H. Watkins, MacRae, C., Lamas, R., McKenna, W., Vosberg, H.-P., Seidman, J.G., and Seidman, C.E. (1994): α-Tropomyosin and cardiac troponin T mutations cause familial hypertrophie cardiomyopathy: A disease of the sarcomere. Cell 77.701-712.
    • (1994) Cell , vol.77 , pp. 701-712
    • Thierfelder, L.H.1    Watkins2    MacRae, C.3    Lamas, R.4    McKenna, W.5    Vosberg, H.-P.6    Seidman, J.G.7    Seidman, C.E.8
  • 47
    • 0026769376 scopus 로고
    • Splicing of two alternative exon pairs in β-tropomyosin pre-mRNA is independently controlled during myogenesis
    • Wang, Y.-C., and Rubenstein, P.A. (1992): Splicing of two alternative exon pairs in β-tropomyosin pre-mRNA is independently controlled during myogenesis. J Biol. Chem. 267:12004-12010.
    • (1992) J Biol. Chem. , vol.267 , pp. 12004-12010
    • Wang, Y.-C.1    Rubenstein, P.A.2
  • 48
    • 0027444227 scopus 로고
    • Induction of neuron-specific tropomyosin mRNAs by nerve growth factor is dependent on morphological differentiation
    • Weinberger, R.P., Henke, R.C., Tolhurst, O., Jeffrey, P.L., and Gunning, P. (1993): Induction of neuron-specific tropomyosin mRNAs by nerve growth factor is dependent on morphological differentiation. J. Cell Biol. 120:205-215.
    • (1993) J. Cell Biol. , vol.120 , pp. 205-215
    • Weinberger, R.P.1    Henke, R.C.2    Tolhurst, O.3    Jeffrey, P.L.4    Gunning, P.5
  • 49
    • 0023848561 scopus 로고
    • The rat α-tropomyosin gene generates a minimum of six different mRNAs coding for striated, smooth, and nonmuscle isoforms by alternative splicing
    • Wieczorek, D.F., Smith, C.W.J., and Nadal-Ginard. B. (1988): The rat α-tropomyosin gene generates a minimum of six different mRNAs coding for striated, smooth, and nonmuscle isoforms by alternative splicing. Mol. Cell. Biol. 8:679-694.
    • (1988) Mol. Cell. Biol. , vol.8 , pp. 679-694
    • Wieczorek, D.F.1    Smith, C.W.J.2    Nadal-Ginard, B.3
  • 50
    • 0022400162 scopus 로고
    • Rat embryo fibroblast tropomyosin 1
    • Yamawaki-Kataoka, Y., and Helfman, D.M. (1985): Rat embryo fibroblast tropomyosin 1. J. Biol. Chem. 260:14440-14445.
    • (1985) J. Biol. Chem. , vol.260 , pp. 14440-14445
    • Yamawaki-Kataoka, Y.1    Helfman, D.M.2
  • 51
    • 0023645255 scopus 로고
    • Isolation and characterization of cDNA clones encoding a low molecular weight nonmuscle tropomyosin isoform
    • Yamawaki-Kataoka, Y., and Helfman, D.M. (1987): Isolation and characterization of cDNA clones encoding a low molecular weight nonmuscle tropomyosin isoform. J. Biol. Chem. 262: 10791-10800.
    • (1987) J. Biol. Chem. , vol.262 , pp. 10791-10800
    • Yamawaki-Kataoka, Y.1    Helfman, D.M.2
  • 52
    • 0020523431 scopus 로고
    • Identification of two distinct regulatory regions adjacent to the human beta-interferon gene
    • Zinn, K., DiMaio, D., and Maniatis, T. (1983): Identification of two distinct regulatory regions adjacent to the human beta-interferon gene. Cell 34:865-879.
    • (1983) Cell , vol.34 , pp. 865-879
    • Zinn, K.1    DiMaio, D.2    Maniatis, T.3


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