메뉴 건너뛰기




Volumn 40, Issue 4, 1998, Pages 393-407

Distinct localizations of tropomyosin isoforms in LLC-PK1 epithelial cells suggests specialized function at cell-cell adhesions

Author keywords

Brush border; Differentiation; Epitope tagging; Kidney; Temporal expression

Indexed keywords

EPITOPE; F ACTIN; TROPOMYOSIN;

EID: 0031880461     PISSN: 08861544     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-0169(1998)40:4<393::AID-CM7>3.0.CO;2-C     Document Type: Article
Times cited : (54)

References (57)
  • 1
    • 0028273237 scopus 로고
    • Role of cell density/cell-cell contact and growth state in expression of differentiated properties by the LLC-PK1 cell line
    • Amsler, K. (1994): Role of cell density/cell-cell contact and growth state in expression of differentiated properties by the LLC-PK1 cell line. J. Cell Physiol. 159:331-339.
    • (1994) J. Cell Physiol. , vol.159 , pp. 331-339
    • Amsler, K.1
  • 2
    • 0020067597 scopus 로고
    • + -dependent hexose transport in a cultured line of porcine kidney cells
    • + -dependent hexose transport in a cultured line of porcine kidney cells. Am. J. Physiol. 242:C94-101.
    • (1982) Am. J. Physiol. , vol.242
    • Amsler, K.1    Cook, J.S.2
  • 3
    • 0025228501 scopus 로고
    • Tropomyosins of human mammary epithelial cells: Consistent defects of expression in mammary carcinoma cell lines
    • Bhattacharya, B., Prasad, G.L., Valverius, E.M., Salomon, D.S., and Cooper, H.L. (1990): Tropomyosins of human mammary epithelial cells: Consistent defects of expression in mammary carcinoma cell lines. Cancer Res. 50: 2105-2112.
    • (1990) Cancer Res. , vol.50 , pp. 2105-2112
    • Bhattacharya, B.1    Prasad, G.L.2    Valverius, E.M.3    Salomon, D.S.4    Cooper, H.L.5
  • 4
    • 0029964673 scopus 로고    scopus 로고
    • Zipper protein, a B-G protein with the ability to regulate actin/myosin 1 interactions in the intestinal brush border
    • Bikle, D.D., Munson, S., and Komuves, L. (1996): Zipper protein, a B-G protein with the ability to regulate actin/myosin 1 interactions in the intestinal brush border. J. Biol. Chem. 271:9075-9083.
    • (1996) J. Biol. Chem. , vol.271 , pp. 9075-9083
    • Bikle, D.D.1    Munson, S.2    Komuves, L.3
  • 5
    • 0022930024 scopus 로고
    • r tropomyosin isoforms from chicken brain and intestinal epithelium have distinct actin-binding properties
    • r 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
  • 7
    • 0021888890 scopus 로고
    • Renaturation of skeletal muscle tropomyosin: Implication for in vivo assembly
    • Brown H.R., and Schachat, F.H. (1985): Renaturation of skeletal muscle tropomyosin: Implication for in vivo assembly. Proc. Natl. Acad. Sci. U.S.A. 87:2359-2363.
    • (1985) Proc. Natl. Acad. Sci. U.S.A. , vol.87 , pp. 2359-2363
    • Brown, H.R.1    Schachat, F.H.2
  • 8
    • 0023139873 scopus 로고
    • Tropomyosin distinguishes between the two actin-binding sites of villin and affects actin-binding properties of the brush border proteins
    • Burgess, D.R, Broschat, K.O., and Hayden, J.M. (1987): Tropomyosin distinguishes between the two actin-binding sites of villin and affects actin-binding properties of the brush border proteins. J. Cell Biol. 104:29-40.
    • (1987) J. Cell Biol. , vol.104 , pp. 29-40
    • Burgess, D.R.1    Broschat, K.O.2    Hayden, J.M.3
  • 9
    • 0025289278 scopus 로고
    • Cytoskeletal and mRNA accumulation during brush border formation in adult chicken enterocytes
    • Fath, K.R., Obenauf, S.D., and Burgess, D.R. (1990): Cytoskeletal and mRNA accumulation during brush border formation in adult chicken enterocytes. Development 109:449-459.
    • (1990) Development , vol.109 , pp. 449-459
    • Fath, K.R.1    Obenauf, S.D.2    Burgess, D.R.3
  • 10
    • 0027730205 scopus 로고
    • The cytoskeleton in development of epithelial cell polarity
    • Path, K.R., Mamajiwalla, S.N., and Burgess, D.R. (1993): The cytoskeleton in development of epithelial cell polarity. J. Cell Sci. 17(suppl.):65-73.
    • (1993) J. Cell Sci. , vol.17 , Issue.SUPPL. , pp. 65-73
    • Path, K.R.1    Mamajiwalla, S.N.2    Burgess, D.R.3
  • 11
    • 3542996764 scopus 로고
    • The role of cell adhesion and intercellular junctions during vertebrate early development
    • In Citi, S. (ed.): Austin, TX: R.G. Landes
    • Fleming, T.P. (1994): The role of cell adhesion and intercellular junctions during vertebrate early development. In Citi, S. (ed.): "Molecular Mechanisms of Epithelial Cell Junctions: From Development to Disease." Austin, TX: R.G. Landes, pp. 67-82.
    • (1994) Molecular Mechanisms of Epithelial Cell Junctions: from Development to Disease , pp. 67-82
    • Fleming, T.P.1
  • 12
    • 0025057161 scopus 로고
    • Generation of skeletal, smooth and LMW non-muscle tropomyosin from the chicken sm-1 gene
    • Forry-Schaudies, S., Maihlen, J., and Hughes, S.H. (1990): Generation of skeletal, smooth and LMW non-muscle tropomyosin from the chicken sm-1 gene. J. Mol. Biol. 211:321-330.
    • (1990) J. Mol. Biol. , vol.211 , pp. 321-330
    • Forry-Schaudies, S.1    Maihlen, J.2    Hughes, S.H.3
  • 13
    • 0023272783 scopus 로고
    • r 43,000 tropomyosin-binding protein from human erythrocyte membranes
    • r 43,000 tropomyosin-binding protein from human erythrocyte membranes. J. Biol. Chem. 262:12792-12800.
    • (1987) J. Biol. Chem. , vol.262 , pp. 12792-12800
    • Fowler, V.1
  • 14
    • 0025314680 scopus 로고
    • Tropomodulin: A cytoskeletal protein that binds to the end of erythrocyte tropomyosin and inhibits tropomyosin binding to actin
    • Fowler, V. (1990): Tropomodulin: A cytoskeletal protein that binds to the end of erythrocyte tropomyosin and inhibits tropomyosin binding to actin. J. Cell Biol. 111:471-482.
    • (1990) J. Cell Biol. , vol.111 , pp. 471-482
    • Fowler, V.1
  • 15
    • 0024524329 scopus 로고
    • Transformation-sensitive and growth-related changes of protein synthesis in REF-52 cells
    • Carrels, J.I., and Franza, B.R., Jr. (1989): Transformation-sensitive and growth-related changes of protein synthesis in REF-52 cells. J. Biol. Chem. 264:5299-5312.
    • (1989) J. Biol. Chem. , vol.264 , pp. 5299-5312
    • Carrels, J.I.1    Franza Jr., B.R.2
  • 16
    • 0019820867 scopus 로고
    • Immunoelectron microscope studies of membrane filament interactions: Distribution of-actinin. tropomyosin. and vinculin in intestinal epithelial brush border and chicken gizzard smooth muscle cells
    • Geiger, B., Dutton, A.M., Tokuyasu, K.T., and Singer, S.J. (1981): Immunoelectron microscope studies of membrane filament interactions: Distribution of-actinin. tropomyosin. and vinculin in intestinal epithelial brush border and chicken gizzard smooth muscle cells. J. Cell Biol. 91:614-628.
    • (1981) J. Cell Biol. , vol.91 , pp. 614-628
    • Geiger, B.1    Dutton, A.M.2    Tokuyasu, K.T.3    Singer, S.J.4
  • 17
    • 0028822231 scopus 로고
    • Specificity of dimer formation in tropomyosins: Influence of alternative spliced exons on homodimer and heterodimer assembly
    • Gimona, M., Watakabe, A., and Helfman, D.M. (1995): Specificity of dimer formation in tropomyosins: Influence of alternative 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
  • 19
    • 0025887613 scopus 로고
    • Four rat tropomyosin isoforms are expressed from a single gene via alternative RNA splicing and the use of two promoters
    • Goodwin, L.O., Lees-Miller, J.P., Cheley, S., Leonard, M., and Helfman, D.M. (1991): Four rat tropomyosin isoforms are expressed from a single gene via alternative RNA splicing and the use of two promoters. J. Biol. Chein. 266:8408-8415.
    • (1991) J. Biol. Chein. , vol.266 , pp. 8408-8415
    • Goodwin, L.O.1    Lees-Miller, J.P.2    Cheley, S.3    Leonard, M.4    Helfman, D.M.5
  • 20
    • 0028806707 scopus 로고
    • Intracellular localization of tropomyosin mRNA and protein is associated with development of neuronal polarity
    • Hannan, A.J., Schevzov, G., Gunning, P., Jeffrey, P.L., and Weinberger, R.P. (1995): Intracellular localization of tropomyosin mRNA and protein is associated with development of neuronal polarity. Mol. Cell. Neurosci. 6:397-412.
    • (1995) Mol. Cell. Neurosci. , vol.6 , pp. 397-412
    • Hannan, A.J.1    Schevzov, G.2    Gunning, P.3    Jeffrey, P.L.4    Weinberger, R.P.5
  • 21
    • 0027184250 scopus 로고
    • Beta and gamma act in mRNAs are differentially located within myoblasts
    • Hill, M.A., and Gunning, P. (1993): Beta and gamma act in mRNAs are differentially located within myoblasts. J. Cell Biol. 122:441-451.
    • (1993) J. Cell Biol. , vol.122 , pp. 441-451
    • Hill, M.A.1    Gunning, P.2
  • 23
    • 0026001768 scopus 로고
    • Smooth muscle tropomyosin coiled-coil dimer: Subunit composition, assembly, and end-to-end interaction
    • Jancsó, A., and Graceffa, P. (1991): Smooth muscle tropomyosin coiled-coil dimer: Subunit composition, assembly, and end-to-end interaction. J. Biol. Chem. 265:5891-5897.
    • (1991) J. Biol. Chem. , vol.265 , pp. 5891-5897
    • Jancsó, A.1    Graceffa, P.2
  • 24
    • 0021907521 scopus 로고
    • Role of myosin in terminal web contraction in isolated intestinal epithelial brush border
    • Keller, T.C.S. III, Conzelman, K.A., Chasin, R., and Mooseker, M. (1985): Role of myosin in terminal web contraction in isolated intestinal epithelial brush border. J. Cell Biol. 101:1647-1655.
    • (1985) J. Cell Biol. , vol.101 , pp. 1647-1655
    • Keller III, T.C.S.1    Conzelman, K.A.2    Chasin, R.3    Mooseker, M.4
  • 25
    • 0344207353 scopus 로고    scopus 로고
    • G alpha(i-2) mediates renal LLC-PK1 growth by a Raf-independent activation of p42/p44 MAP kinase
    • Kinane, T.B., Kang, I., Chu, A., Chin, S.H., and Ercolani, L. (1997): G alpha(i-2) mediates renal LLC-PK1 growth by a Raf-independent activation of p42/p44 MAP kinase. Am. J. Phys. 272(2 pt 2):F273-782.
    • (1997) Am. J. Phys. , vol.272 , Issue.2 PT 2
    • Kinane, T.B.1    Kang, I.2    Chu, A.3    Chin, S.H.4    Ercolani, L.5
  • 26
    • 0028027909 scopus 로고
    • Sequences responsible for intracellular localization of b-actin messenger RNA also affect cell phenotype
    • Kislauskis, E.H., Xiaochun, Z., and Singer, R.H. (1994): Sequences responsible for intracellular localization of b-actin messenger RNA also affect cell phenotype J. Cell Biol. 127:441-451.
    • (1994) J. Cell Biol. , vol.127 , pp. 441-451
    • Kislauskis, E.H.1    Xiaochun, Z.2    Singer, R.H.3
  • 27
    • 0028839834 scopus 로고
    • The body language of cells: The intimate connection between cell adhesion and behavior
    • Klymkowsky, M.W., and Parr, B. (1995): The body language of cells: The intimate connection between cell adhesion and behavior. Cell 83:5-8.
    • (1995) Cell , vol.83 , pp. 5-8
    • Klymkowsky, M.W.1    Parr, B.2
  • 28
    • 0026031446 scopus 로고
    • Epitope tagging and protein surveillance
    • Kolodziej, P.A., and Young, R.A. (1991): Epitope tagging and protein surveillance. Methods Enzymol. 194:508-519.
    • (1991) Methods Enzymol , vol.194 , pp. 508-519
    • Kolodziej, P.A.1    Young, R.A.2
  • 29
    • 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 (Lond.) 227:680-685.
    • (1970) Nature (Lond.) , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 30
    • 0026218642 scopus 로고
    • The molecular basis for tropomyosin isoform diversity
    • Lees-Miller, J., 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.1    Helfman, D.M.2
  • 31
    • 0025058736 scopus 로고
    • Unfolding/refolding studies of smooth 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 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
  • 32
    • 0024535550 scopus 로고
    • Chemical inducers of differentiation in a long-term renal cell line
    • Lever, J. (1989): Chemical inducers of differentiation in a long-term renal cell line. Environ. Health Persp. 80:173-180.
    • (1989) Environ. Health Persp. , vol.80 , pp. 173-180
    • Lever, J.1
  • 33
    • 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
  • 34
    • 3543003382 scopus 로고
    • Characterization of a cDNA defining a gene family encoding TM30pl, a human fibroblast TM
    • MacLeod, A.R., Talbot, K., Smilie, L.B., and Houlker, C. (1987): Characterization of a cDNA defining a gene family encoding TM30pl, a human fibroblast TM. J. Biol. Chem. 27:14440-14445.
    • (1987) J. Biol. Chem. , vol.27 , pp. 14440-14445
    • MacLeod, A.R.1    Talbot, K.2    Smilie, L.B.3    Houlker, C.4
  • 35
    • 0021059305 scopus 로고
    • Differential expression of tropomyosin forms in the microfilaments isolated from normal und 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 und 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
  • 36
    • 0242718534 scopus 로고
    • Effect of SV40 transformation on the growth-factor requirements of the rat embryo cell line REF-52 in serum-free medium
    • McClure, D.B., Hightower, M.J., and Topp, W.C. (1982): Effect of SV40 transformation on the growth-factor requirements of the rat embryo cell line REF-52 in serum-free medium. Cold Spring Harbor Conf. Cell Prolif. 9:345-364.
    • (1982) Cold Spring Harbor Conf. Cell Prolif. , vol.9 , pp. 345-364
    • McClure, D.B.1    Hightower, M.J.2    Topp, W.C.3
  • 37
    • 0025125799 scopus 로고
    • Identification of a membrane-cytoskeletal complex containing the cell adhesion molecule uvomorulin (E-cadherin), ankyrin, and fodrin in Madin-Darby canine kidney epithelial cells
    • Nelson, W.J., Shore, E., Wang, A.Z., and Hammerton, R.W. (1990): Identification of a membrane-cytoskeletal complex containing the cell adhesion molecule uvomorulin (E-cadherin), ankyrin, and fodrin in Madin-Darby canine kidney epithelial cells. J. Cell. Biol. 110:349-357.
    • (1990) J. Cell. Biol. , vol.110 , pp. 349-357
    • Nelson, W.J.1    Shore, E.2    Wang, A.Z.3    Hammerton, R.W.4
  • 38
    • 0025164958 scopus 로고
    • Morphology of the differentiation and maturation of LLC-PK1 epithelia
    • Pfaller, W., Gstraunthaler, G., and Loidl, P. (1990): Morphology of the differentiation and maturation of LLC-PK1 epithelia. J. Cell Physiol. 142:247-254.
    • (1990) J. Cell Physiol. , vol.142 , pp. 247-254
    • Pfaller, W.1    Gstraunthaler, G.2    Loidl, P.3
  • 39
    • 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 co-localized in interphase fibroblasts
    • Pittenger, M., 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 co-localized in interphase fibroblasts. J. Cell Biol. 118:841-858.
    • (1992) J. Cell Biol. , vol.118 , pp. 841-858
    • Pittenger, M.1    Helfman, D.M.2
  • 40
    • 0028091405 scopus 로고
    • Functional properties of non-muscle tropomyosin isoforms
    • Pittenger, M., Kazzaz, J.A., and Helfman, D.M. (1994): Functional properties of non-muscle tropomyosin isoforms. Curr. Opin. Cell Biol. 6:96-104.
    • (1994) Curr. Opin. Cell Biol. , vol.6 , pp. 96-104
    • Pittenger, M.1    Kazzaz, J.A.2    Helfman, D.M.3
  • 41
    • 0029091378 scopus 로고
    • Alternatively spliced exons of the b tropomyosin gene exhibit different affinities for F-actin and effects with nonmuscle caldesmon
    • Pittenger, M., Kistler, A., and Helfman, D.M. (1995): Alternatively spliced exons of the b 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.1    Kistler, A.2    Helfman, D.M.3
  • 42
    • 0024209184 scopus 로고
    • Unique isoactins in the brush border of rat intestinal epithelial cells
    • Sawtell, N.M., Hartman, A.L., and Lessard, J.L. (1988): Unique isoactins in the brush border of rat intestinal epithelial cells. Cell Motil.Cytoskeleton 11:318-325.
    • (1988) Cell Motil.Cytoskeleton , vol.11 , pp. 318-325
    • Sawtell, N.M.1    Hartman, A.L.2    Lessard, J.L.3
  • 43
    • 0027262207 scopus 로고
    • Differential regulation of tropomyosin isoform organization and gene expression in response to altered actin gene expression
    • Schevzov, G., Lloyd, C., Hailstones, D., and Gunning, P. (1993): Differential regulation of tropomyosin isoform organization and gene expression in response to altered actin gene expression. J. Cell Biol. 121:811-821.
    • (1993) J. Cell Biol. , vol.121 , pp. 811-821
    • Schevzov, G.1    Lloyd, C.2    Hailstones, D.3    Gunning, P.4
  • 45
    • 0028343964 scopus 로고
    • Chicken antibodies to rabbit muscle actin with a restricted repertoire of F-actin recognition
    • Schrader, M., Temm-Grove, C.J., Lessard, J.L., and Jockusch, B.M. (1994): Chicken antibodies to rabbit muscle actin with a restricted repertoire of F-actin recognition. Eur. J. Cell Biol. 63:326-335.
    • (1994) Eur. J. Cell Biol. , vol.63 , pp. 326-335
    • Schrader, M.1    Temm-Grove, C.J.2    Lessard, J.L.3    Jockusch, B.M.4
  • 46
    • 0022165946 scopus 로고
    • Cell surface polarity in epithelia
    • Simons, K., and Fuller, S.D. (1985): Cell surface polarity in epithelia. Annu. Rev. Cell Biol. 1:243-288.
    • (1985) Annu. Rev. Cell Biol. , vol.1 , pp. 243-288
    • Simons, K.1    Fuller, S.D.2
  • 47
    • 0028242534 scopus 로고
    • Erythrocyte tropomodulin binds to the N-terminus of hTM5, a tropomyosin isoform encoded by the -tropomyosin gene
    • Sung, L.A., and Lin, J.J.-C. (1994): Erythrocyte tropomodulin binds to the N-terminus of hTM5, a tropomyosin isoform encoded by the -tropomyosin gene. Biochem Biophys. Res. Commun. 201:627-634.
    • (1994) Biochem Biophys. Res. Commun. , vol.201 , pp. 627-634
    • Sung, L.A.1    Lin, J.J.-C.2
  • 48
    • 0023812337 scopus 로고
    • Isolation and characterization of a cDNA that encodes mouse fibroblast tropomyosin isoform 2
    • Takenaga, K., Nakamura, Y., Tokunaga, K., Kageyama, H., and Sakiyama, S. (1988): Isolation and characterization of a cDNA that encodes mouse fibroblast tropomyosin isoform 2. Mol. Cell. Biol. 8:5561-5565.
    • (1988) Mol. Cell. Biol. , vol.8 , pp. 5561-5565
    • Takenaga, K.1    Nakamura, Y.2    Tokunaga, K.3    Kageyama, H.4    Sakiyama, S.5
  • 49
    • 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
  • 50
    • 0026509182 scopus 로고
    • The upright position of brush border-type microvilli depends on myosin filaments
    • Temm-Grove, C.J., Helbing, D., Wiegand, C., Höner, B., and Jockusch, B.M. (1992): The upright position of brush border-type microvilli depends on myosin filaments. J. Cell Sci. 101:599-610.
    • (1992) J. Cell Sci. , vol.101 , pp. 599-610
    • Temm-Grove, C.J.1    Helbing, D.2    Wiegand, C.3    Höner, B.4    Jockusch, B.M.5
  • 51
    • 0029932698 scopus 로고    scopus 로고
    • Low molecular weight rat fibroblast tropomyosin 5 (TM-5): CDNA Cloning, actin-binding, localization, and coiled-coil interactions
    • Temm-Grove, C.J., Guo, W., and Helfman, D.M. (1996): Low molecular weight rat fibroblast tropomyosin 5 (TM-5): cDNA Cloning, actin-binding, localization, and coiled-coil interactions. Cell Motil. Cytoskeleton 33:223-240.
    • (1996) Cell Motil. Cytoskeleton , vol.33 , pp. 223-240
    • Temm-Grove, C.J.1    Guo, W.2    Helfman, D.M.3
  • 53
    • 0028099996 scopus 로고
    • Tropomodulin caps the pointed ends of actin filaments
    • Weber, A., Pennise, C.R., Babcock, G.G., and Fowler, V.M. (1994): Tropomodulin caps the pointed ends of actin filaments. J. Cell Biol. 127:1627-1635.
    • (1994) J. Cell Biol. , vol.127 , pp. 1627-1635
    • Weber, A.1    Pennise, C.R.2    Babcock, G.G.3    Fowler, V.M.4
  • 54
    • 0019305048 scopus 로고
    • Distribution of fluorescently labeled actin and tropomyosin after microinjection in living tissue culture cells as observed with TV image intensification
    • Wehland, J., and Weber, K. (1980): Distribution of fluorescently labeled actin and tropomyosin after microinjection in living tissue culture cells as observed with TV image intensification. Exp. Cell Res. 127:397-408.
    • (1980) Exp. Cell Res. , vol.127 , pp. 397-408
    • Wehland, J.1    Weber, K.2
  • 55
    • 0030032902 scopus 로고    scopus 로고
    • The molecular composition of neuronal microfilaments is spatially and temporally regulated
    • Weinberger, R.P., Schevzov, G., Jeffrey, P., Gordon, K., Hill, M., and Gunning, P. (1996): The molecular composition of neuronal microfilaments is spatially and temporally regulated. J. Neurosci. 16:238-252.
    • (1996) J. Neurosci. , vol.16 , pp. 238-252
    • Weinberger, R.P.1    Schevzov, G.2    Jeffrey, P.3    Gordon, K.4    Hill, M.5    Gunning, P.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.