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Volumn 1, Issue 4, 2011, Pages 135-164

Tropomyosin isoforms and reagents

Author keywords

Antibodies; Cytoskeleton; Isoforms; Multi gene family; Reagents; Tropomyosin

Indexed keywords

ISOPROTEIN; PROTEIN ANTIBODY; TROPOMYOSIN; TROPOMYOSIN ANTIBODY; UNCLASSIFIED DRUG;

EID: 84992240335     PISSN: 19490992     EISSN: 1949100X     Source Type: Journal    
DOI: 10.4161/bioa.1.4.17897     Document Type: Article
Times cited : (118)

References (119)
  • 1
    • 38349059960 scopus 로고    scopus 로고
    • Tropomyosinbased regulation of the actin cytoskeleton in time and space
    • Gunning P, O'Neill G, Hardeman E. Tropomyosinbased regulation of the actin cytoskeleton in time and space. Physiol Rev 2008; 88:1-35.
    • (2008) Physiol Rev , vol.88 , pp. 1-35
    • Gunning, P.1    O'Neill, G.2    Hardeman, E.3
  • 3
    • 37249073377 scopus 로고    scopus 로고
    • Class-specific interaction of profilin and ADF isovariants with actin in the regulation of plant development
    • Kandasamy MK, Burgos-Rivera B, McKinney EC, Ruzicka DR, Meagher RB. Class-specific interaction of profilin and ADF isovariants with actin in the regulation of plant development. Plant Cell 2007; 19:3111-26.
    • (2007) Plant Cell , vol.19 , pp. 3111-3126
    • Kandasamy, M.K.1    Burgos-Rivera, B.2    McKinney, E.C.3    Ruzicka, D.R.4    Meagher, R.B.5
  • 4
    • 79951834827 scopus 로고    scopus 로고
    • Tropomyosin position on F-actin revealed by EM reconstruction and computational chemistry
    • Li XE, Tobacman LS, Mun JY, Craig R, Fischer S, Lehman W. Tropomyosin position on F-actin revealed by EM reconstruction and computational chemistry. Biophys J 2011; 100:1005-13.
    • (2011) Biophys J , vol.100 , pp. 1005-1013
    • Li, X.E.1    Tobacman, L.S.2    Mun, J.Y.3    Craig, R.4    Fischer, S.5    Lehman, W.6
  • 6
    • 60849107340 scopus 로고    scopus 로고
    • Tropomyosin gene expression in vivo and in vitro
    • Schevzov G, O'Neill G. Tropomyosin gene expression in vivo and in vitro. Adv Exp Med Biol 2008; 644:43-59.
    • (2008) Adv Exp Med Biol , vol.644 , pp. 43-59
    • Schevzov, G.1    O'Neill, G.2
  • 7
    • 60849097303 scopus 로고    scopus 로고
    • Isoform sorting of tropomyosins
    • Martin C, Gunning P. Isoform sorting of tropomyosins. Adv Exp Med Biol 2008; 644:187-200.
    • (2008) Adv Exp Med Biol , vol.644 , pp. 187-200
    • Martin, C.1    Gunning, P.2
  • 8
    • 20444398071 scopus 로고    scopus 로고
    • Tropomyosin isoforms: divining rods for actin cytoskeleton function
    • Gunning PW, Schevzov G, Kee AJ, Hardeman EC. Tropomyosin isoforms: divining rods for actin cytoskeleton function. Trends Cell Biol 2005; 15:333-41.
    • (2005) Trends Cell Biol , vol.15 , pp. 333-341
    • Gunning, P.W.1    Schevzov, G.2    Kee, A.J.3    Hardeman, E.C.4
  • 9
    • 62449145371 scopus 로고    scopus 로고
    • Gestalt-binding of tropomyosin to actin filaments
    • Holmes KC, Lehman W. Gestalt-binding of tropomyosin to actin filaments. J Muscle Res Cell Motil 2008; 29:213-9.
    • (2008) J Muscle Res Cell Motil , vol.29 , pp. 213-219
    • Holmes, K.C.1    Lehman, W.2
  • 11
    • 0024565757 scopus 로고
    • Differential modulation of actin-severing activity of gelsolin by multiple isoforms of cultured rat cell tropomyosin Potentiation of protective ability of tropomyosins by 83-kDa nonmuscle caldesmon
    • Ishikawa R, Yamashiro S, Matsumura F. Differential modulation of actin-severing activity of gelsolin by multiple isoforms of cultured rat cell tropomyosin. Potentiation of protective ability of tropomyosins by 83-kDa nonmuscle caldesmon. J Biol Chem 1989; 264:7490-7.
    • (1989) J Biol Chem , vol.264 , pp. 7490-7497
    • Ishikawa, R.1    Yamashiro, S.2    Matsumura, F.3
  • 12
    • 0020025754 scopus 로고
    • Tropomyosin binding to F-actin protects the F-actin from disassembly by brain actin-depolymerizing factor (ADF)
    • Bernstein BW, Bamburg JR. Tropomyosin binding to F-actin protects the F-actin from disassembly by brain actin-depolymerizing factor (ADF). Cell Motil 1982; 2:1-8.
    • (1982) Cell Motil , vol.2 , pp. 1-8
    • Bernstein, B.W.1    Bamburg, J.R.2
  • 13
    • 0021749110 scopus 로고
    • a protein in porcine brain that binds to actin filaments and inhibits their interactions with myosin and tropomyosin
    • Nishida E, Maekawa S, Sakai H. Cofilin, a protein in porcine brain that binds to actin filaments and inhibits their interactions with myosin and tropomyosin. Biochemistry 1984; 23:5307-13.
    • (1984) Biochemistry , vol.23 , pp. 5307-5313
    • Nishida, E.1    Maekawa, S.2    Cofilin, S.H.3
  • 14
    • 0037128928 scopus 로고    scopus 로고
    • Tropomyosin inhibits ADF/cofilindependent actin filament dynamics
    • Ono S, Ono K. Tropomyosin inhibits ADF/cofilindependent actin filament dynamics. J Cell Biol 2002; 156:1065-76.
    • (2002) J Cell Biol , vol.156 , pp. 1065-1076
    • Ono, S.1    Ono, K.2
  • 15
    • 79952104296 scopus 로고    scopus 로고
    • Three's company: the fission yeast actin cytoskeleton
    • Kovar DR, Sirotkin V, Lord M. Three's company: the fission yeast actin cytoskeleton. Trends Cell Biol 2011; 21:177-87.
    • (2011) Trends Cell Biol , vol.21 , pp. 177-187
    • Kovar, D.R.1    Sirotkin, V.2    Lord, M.3
  • 16
    • 0037343138 scopus 로고    scopus 로고
    • Specification of actin filament function and molecular composition by tropomyosin isoforms
    • Bryce NS, Schevzov G, Ferguson V, Percival JM, Lin JJ, Matsumura F, et al. Specification of actin filament function and molecular composition by tropomyosin isoforms. Mol Biol Cell 2003; 14:1002-16.
    • (2003) Mol Biol Cell , vol.14 , pp. 1002-1016
    • Bryce, N.S.1    Schevzov, G.2    Ferguson, V.3    Percival, J.M.4    Lin, J.J.5    Matsumura, F.6
  • 17
    • 77956901465 scopus 로고    scopus 로고
    • The recruitment of acetylated and unacetylated tropomyosin to distinct actin polymers permits the discrete regulation of specific myosins in fission yeast
    • Coulton AT, East DA, Galinska-Rakoczy A, Lehman W, Mulvihill DP. The recruitment of acetylated and unacetylated tropomyosin to distinct actin polymers permits the discrete regulation of specific myosins in fission yeast. J Cell Sci 2010; 123:3235-43.
    • (2010) J Cell Sci , vol.123 , pp. 3235-3243
    • Coulton, A.T.1    East, D.A.2    Galinska-Rakoczy, A.3    Lehman, W.4    Mulvihill, D.P.5
  • 18
    • 0035943018 scopus 로고    scopus 로고
    • Motor domain-dependent localization of myo1b (myr-1)
    • Tang N, Ostap EM. Motor domain-dependent localization of myo1b (myr-1). Curr Biol 2001; 11:1131-5.
    • (2001) Curr Biol , vol.11 , pp. 1131-1135
    • Tang, N.1    Ostap, E.M.2
  • 19
    • 0035860720 scopus 로고    scopus 로고
    • Modulation of myosin function by isoform-specific properties of Saccharomyces cerevisiae and muscle tropomyosins
    • Strand J, Nili M, Homsher E, Tobacman LS. Modulation of myosin function by isoform-specific properties of Saccharomyces cerevisiae and muscle tropomyosins. J Biol Chem 2001; 276:34832-9.
    • (2001) J Biol Chem , vol.276 , pp. 34832-34839
    • Strand, J.1    Nili, M.2    Homsher, E.3    Tobacman, L.S.4
  • 20
    • 0027933182 scopus 로고
    • Differential regulation of skeletal muscle myosin-II and brush border myosin-I enzymology and mechanochemistry by bacterially produced tropomyosin isoforms
    • Fanning AS, Wolenski JS, Mooseker MS, Izant JG. Differential regulation of skeletal muscle myosin-II and brush border myosin-I enzymology and mechanochemistry by bacterially produced tropomyosin isoforms. Cell Motil Cytoskel 1994; 29:29-45.
    • (1994) Cell Motil Cytoskel , vol.29 , pp. 29-45
    • Fanning, A.S.1    Wolenski, J.S.2    Mooseker, M.S.3    Izant, J.G.4
  • 22
    • 0022270530 scopus 로고
    • Caldesmon150 regulates the tropomyosin-enhanced actin-myosin interaction in gizzard smooth muscle
    • Sobue K, Takahashi K, Wakabayashi I. Caldesmon150 regulates the tropomyosin-enhanced actin-myosin interaction in gizzard smooth muscle. Biochem Biophys Res Comm 1985; 132:645-51.
    • (1985) Biochem Biophys Res Comm , vol.132 , pp. 645-651
    • Sobue, K.1    Takahashi, K.2    Wakabayashi, I.3
  • 23
    • 0029838840 scopus 로고    scopus 로고
    • N-tropomodulin: a novel isoform of tropomodulin identified as the major binding protein to brain tropomyosin
    • Watakabe A, Kobayashi R, Helfman DM. N-tropomodulin: a novel isoform of tropomodulin identified as the major binding protein to brain tropomyosin. J Cell Sci 1996; 109:2299-310.
    • (1996) J Cell Sci , vol.109 , pp. 2299-2310
    • Watakabe, A.1    Kobayashi, R.2    Helfman, D.M.3
  • 24
    • 80052341378 scopus 로고    scopus 로고
    • Systematic analysis of tropomodulin/tropomyosin interactions uncovers fine-tuned binding specificity of intrinsically disordered proteins
    • Uversky VN, Shah SP, Gritsyna Y, Hitchcock-DeGregori SE, Kostyukova AS. Systematic analysis of tropomodulin/tropomyosin interactions uncovers fine-tuned binding specificity of intrinsically disordered proteins. J Mol Recognit 2011; 24:647-55.
    • (2011) J Mol Recognit , vol.24 , pp. 647-655
    • Uversky, V.N.1    Shah, S.P.2    Gritsyna, Y.3    Hitchcock-DeGregori, S.E.4    Kostyukova, A.S.5
  • 25
    • 1242294519 scopus 로고    scopus 로고
    • Effect of the structure of the N terminus of tropomyosin on tropomodulin function
    • Kostyukova AS, Hitchcock-DeGregori SE. Effect of the structure of the N terminus of tropomyosin on tropomodulin function. J Biol Chem 2004; 279:5066-71.
    • (2004) J Biol Chem , vol.279 , pp. 5066-5071
    • Kostyukova, A.S.1    Hitchcock-DeGregori, S.E.2
  • 26
    • 60849087095 scopus 로고    scopus 로고
    • Tropomyosin function in yeast
    • Pruyne D. Tropomyosin function in yeast. Adv Exp Med Biol 2008; 644:168-86.
    • (2008) Adv Exp Med Biol , vol.644 , pp. 168-186
    • Pruyne, D.1
  • 27
    • 60849099070 scopus 로고    scopus 로고
    • Structure and evolution of tropomyosin genes
    • Vrhovski B, Theze N, Thiebaud P. Structure and evolution of tropomyosin genes. Adv Exp Med Biol 2008; 644:6-26.
    • (2008) Adv Exp Med Biol , vol.644 , pp. 6-26
    • Vrhovski, B.1    Theze, N.2    Thiebaud, P.3
  • 28
    • 58149119313 scopus 로고    scopus 로고
    • A periodic Table of coiled-coil protein structures
    • Moutevelis E, Woolfson DN. A periodic Table of coiled-coil protein structures. J Mol Biol 2009; 385:726-32.
    • (2009) J Mol Biol , vol.385 , pp. 726-732
    • Moutevelis, E.1    Woolfson, D.N.2
  • 29
    • 69349084190 scopus 로고    scopus 로고
    • Identification of a unique "stability control region" that controls protein stability of tropomyosin: A two-stranded alpha-helical coiled-coil
    • Hodges RS, Mills J, McReynolds S, Kirwan JP, Tripet B, Osguthorpe D. Identification of a unique "stability control region" that controls protein stability of tropomyosin: A two-stranded alpha-helical coiled-coil. J Mol Biol 2009; 392:747-62.
    • (2009) J Mol Biol , vol.392 , pp. 747-762
    • Hodges, R.S.1    Mills, J.2    McReynolds, S.3    Kirwan, J.P.4    Tripet, B.5    Osguthorpe, D.6
  • 30
    • 0034703378 scopus 로고    scopus 로고
    • Tropomyosin and actin isoforms modulate the localization of tropomyosin strands on actin filaments
    • Lehman W, Hatch V, Korman V, Rosol M, Thomas L, Maytum R, et al. Tropomyosin and actin isoforms modulate the localization of tropomyosin strands on actin filaments. J Mol Biol 2000; 302:593-606.
    • (2000) J Mol Biol , vol.302 , pp. 593-606
    • Lehman, W.1    Hatch, V.2    Korman, V.3    Rosol, M.4    Thomas, L.5    Maytum, R.6
  • 31
    • 79959932890 scopus 로고    scopus 로고
    • Evolutionarily conserved surface residues constitute actin binding sites of tropomyosin
    • Barua B, Pamula MC, Hitchcock-Degregori SE. Evolutionarily conserved surface residues constitute actin binding sites of tropomyosin. Proc Natl Acad Sci USA 2011; 108:10150-5.
    • (2011) Proc Natl Acad Sci USA , vol.108 , pp. 10150-10155
    • Barua, B.1    Pamula, M.C.2    Hitchcock-Degregori, S.E.3
  • 32
    • 0035371460 scopus 로고    scopus 로고
    • Multiple combinations of alternatively spliced exons in rat tropomyosin-alpha gene mRNA: evidence for 20 new isoforms in adult tissues and cultured cells
    • Cooley BC, Bergtrom G. Multiple combinations of alternatively spliced exons in rat tropomyosin-alpha gene mRNA: evidence for 20 new isoforms in adult tissues and cultured cells. Arch Biochem Biophys 2001; 390:71-7.
    • (2001) Arch Biochem Biophys , vol.390 , pp. 71-77
    • Cooley, B.C.1    Bergtrom, G.2
  • 33
    • 0032541174 scopus 로고    scopus 로고
    • Splicing of two internal and four carboxylterminal alternative exons in nonmuscle tropomyosin 5 pre-mRNA is independently regulated during development
    • Dufour C, Weinberger RP, Schevzov G, Jeffrey PL, Gunning P. Splicing of two internal and four carboxylterminal alternative exons in nonmuscle tropomyosin 5 pre-mRNA is independently regulated during development. J Biol Chem 1998; 273:18547-55.
    • (1998) J Biol Chem , vol.273 , pp. 18547-18555
    • Dufour, C.1    Weinberger, R.P.2    Schevzov, G.3    Jeffrey, P.L.4    Gunning, P.5
  • 34
    • 0023645255 scopus 로고
    • Isolation and characterization of cDNA clones encoding a low molecular weight nonmuscle tropomyosin isoform
    • Yamawaki-Kataoka Y, Helfman DM. Isolation and characterization of cDNA clones encoding a low molecular weight nonmuscle tropomyosin isoform. J Biol Chem 1987; 262:10791-800.
    • (1987) J Biol Chem , vol.262 , pp. 10791-10800
    • Yamawaki-Kataoka, Y.1    Helfman, D.M.2
  • 35
    • 3142772675 scopus 로고    scopus 로고
    • Expression of a novel cardiac-specific tropomyosin isoform in humans
    • Denz CR, Narshi A, Zajdel RW, Dube DK. Expression of a novel cardiac-specific tropomyosin isoform in humans. Biochem Biophys Res Comm 2004; 320:1291-7.
    • (2004) Biochem Biophys Res Comm , vol.320 , pp. 1291-1297
    • Denz, C.R.1    Narshi, A.2    Zajdel, R.W.3    Dube, D.K.4
  • 36
    • 0033580434 scopus 로고    scopus 로고
    • Suppression of src-induced transformed phenotype by expression of tropomyosin-1
    • Prasad GL, Masuelli L, Raj MH, Harindranath N. Suppression of src-induced transformed phenotype by expression of tropomyosin-1. Oncogene 1999; 18:2027-31.
    • (1999) Oncogene , vol.18 , pp. 2027-2031
    • Prasad, G.L.1    Masuelli, L.2    Raj, M.H.3    Harindranath, N.4
  • 37
    • 0032004877 scopus 로고    scopus 로고
    • Tropomyosin in preimplantation mouse development: identification, expression and organization during cell division and polarization
    • Clayton L, Johnson MH. Tropomyosin in preimplantation mouse development: identification, expression and organization during cell division and polarization. Exp Cell Res 1998; 238:450-64.
    • (1998) Exp Cell Res , vol.238 , pp. 450-464
    • Clayton, L.1    Johnson, M.H.2
  • 38
    • 0025303805 scopus 로고
    • Differential control of tropomyosin mRNA levels during myogenesis suggests the existence of an isoform competition-autoregulatory compensation control mechanism
    • Gunning P, Gordon M, Wade R, Gahlmann R, Lin CS, Hardeman E. Differential control of tropomyosin mRNA levels during myogenesis suggests the existence of an isoform competition-autoregulatory compensation control mechanism. Dev Biol 1990; 138:443-53.
    • (1990) Dev Biol , vol.138 , pp. 443-453
    • Gunning, P.1    Gordon, M.2    Wade, R.3    Gahlmann, R.4    Lin, C.S.5    Hardeman, E.6
  • 39
    • 0028359143 scopus 로고
    • Identification of novel alternatively spliced isoforms of the tropomyosin-encoding gene, TMnm, in the rat cochlea
    • Beisel KW, Kennedy JE. Identification of novel alternatively spliced isoforms of the tropomyosin-encoding gene, TMnm, in the rat cochlea. Gene 1994; 143:251-6.
    • (1994) Gene , vol.143 , pp. 251-256
    • Beisel, K.W.1    Kennedy, J.E.2
  • 40
    • 0025247677 scopus 로고
    • Three novel brain tropomyosin isoforms are expressed from the rat alpha-tropomyosin gene through the use of alternative promoters and alternative RNA processing
    • Lees-Miller JP, Goodwin LO, Helfman DM. Three novel brain tropomyosin isoforms are expressed from the rat alpha-tropomyosin gene through the use of alternative promoters and alternative RNA processing. Mol Cell Biol 1990; 10:1729-42.
    • (1990) Mol Cell Biol , vol.10 , pp. 1729-1742
    • Lees-Miller, J.P.1    Goodwin, L.O.2    Helfman, D.M.3
  • 41
    • 0025286527 scopus 로고
    • Structure and complete nucleotide sequence of the gene encoding rat fibroblast tropomyosin 4
    • Lees-Miller JP, Yan A, Helfman DM. Structure and complete nucleotide sequence of the gene encoding rat fibroblast tropomyosin 4. J Mol Biol 1990; 213:399-405.
    • (1990) J Mol Biol , vol.213 , pp. 399-405
    • Lees-Miller, J.P.1    Yan, A.2    Helfman, D.M.3
  • 42
    • 60849113733 scopus 로고    scopus 로고
    • Human tropomyosin isoforms in the regulation of cytoskeleton functions
    • Lin JJ, Eppinga RD, Warren KS, McCrae KR. Human tropomyosin isoforms in the regulation of cytoskeleton functions. Adv Exp Med Biol 2008; 644:201-22.
    • (2008) Adv Exp Med Biol , vol.644 , pp. 201-222
    • Lin, J.J.1    Eppinga, R.D.2    Warren, K.S.3    McCrae, K.R.4
  • 43
    • 0023655442 scopus 로고
    • Altered actin and troponin binding of amino-terminal variants of chicken striated muscle alpha-tropomyosin expressed in Escherichia coli
    • Hitchcock-DeGregori SE, Heald RW. Altered actin and troponin binding of amino-terminal variants of chicken striated muscle alpha-tropomyosin expressed in Escherichia coli. J Biol Chem 1987; 262:9730-5.
    • (1987) J Biol Chem , vol.262 , pp. 9730-9735
    • Hitchcock-DeGregori, S.E.1    Heald, R.W.2
  • 44
    • 0027971166 scopus 로고
    • Requirement of amino-terminal modification for striated muscle alpha-tropomyosin function
    • Urbancikova M, Hitchcock-DeGregori SE. Requirement of amino-terminal modification for striated muscle alpha-tropomyosin function. J Biol Chem 1994; 269:24310-5.
    • (1994) J Biol Chem , vol.269 , pp. 24310-24315
    • Urbancikova, M.1    Hitchcock-DeGregori, S.E.2
  • 45
    • 33750290244 scopus 로고    scopus 로고
    • Functional homodimers and heterodimers of recombinant smooth muscle tropomyosin
    • Coulton A, Lehrer SS, Geeves MA. Functional homodimers and heterodimers of recombinant smooth muscle tropomyosin. Biochemistry 2006; 45:12853-8.
    • (2006) Biochemistry , vol.45 , pp. 12853-12858
    • Coulton, A.1    Lehrer, S.S.2    Geeves, M.A.3
  • 47
    • 34249751177 scopus 로고    scopus 로고
    • Acetylation regulates tropomyosin function in the fission yeast Schizosaccharomyces pombe
    • Skoumpla K, Coulton AT, Lehman W, Geeves MA, Mulvihill DP. Acetylation regulates tropomyosin function in the fission yeast Schizosaccharomyces pombe. J Cell Sci 2007; 120:1635-45.
    • (2007) J Cell Sci , vol.120 , pp. 1635-1645
    • Skoumpla, K.1    Coulton, A.T.2    Lehman, W.3    Geeves, M.A.4    Mulvihill, D.P.5
  • 48
    • 0019798102 scopus 로고
    • Characterization of the tropomyosin present in various chick embryo muscle types and in muscle cells differentiated in vitro
    • Montarras D, Fiszman MY, Gros F. Characterization of the tropomyosin present in various chick embryo muscle types and in muscle cells differentiated in vitro. J Biol Chem 1981; 256:4081-6.
    • (1981) J Biol Chem , vol.256 , pp. 4081-4086
    • Montarras, D.1    Fiszman, M.Y.2    Gros, F.3
  • 49
    • 0017618863 scopus 로고
    • Phosphorylation of tropomyosin in live frog muscle
    • Ribolow H, Barany M. Phosphorylation of tropomyosin in live frog muscle. Arch Biochem Biophys 1977; 179:718-20.
    • (1977) Arch Biochem Biophys , vol.179 , pp. 718-720
    • Ribolow, H.1    Barany, M.2
  • 50
    • 0017864059 scopus 로고
    • Specific phosphorylation at serine-283 of alpha tropomyosin from frog skeletal and rabbit skeletal and cardiac muscle
    • Mak A, Smillie LB, Barany M. Specific phosphorylation at serine-283 of alpha tropomyosin from frog skeletal and rabbit skeletal and cardiac muscle. Proc Natl Acad Sci USA 1978; 75:3588-92.
    • (1978) Proc Natl Acad Sci USA , vol.75 , pp. 3588-3592
    • Mak, A.1    Smillie, L.B.2    Barany, M.3
  • 51
    • 0018409743 scopus 로고
    • Phosphorylation of subunit proteins of intermediate filaments from chicken muscle and nonmuscle cells
    • O'Connor CM, Balzer DR Jr, Lazarides E. Phosphorylation of subunit proteins of intermediate filaments from chicken muscle and nonmuscle cells. Proc Natl Acad Sci USA 1979; 76:819-23.
    • (1979) Proc Natl Acad Sci USA , vol.76 , pp. 819-823
    • O'Connor, C.M.1    Balzer Jr., D.R.2    Lazarides, E.3
  • 52
    • 0020381632 scopus 로고
    • Phosphorylation of tropomyosin during development in mammalian striated muscle
    • Heeley DA, Moir AJ, Perry SV. Phosphorylation of tropomyosin during development in mammalian striated muscle. FEBS Lett 1982; 146:115-8.
    • (1982) FEBS Lett , vol.146 , pp. 115-118
    • Heeley, D.A.1    Moir, A.J.2    Perry, S.V.3
  • 53
    • 0021994508 scopus 로고
    • Factors determining the subunit composition of tropomyosin in mammalian skeletal muscle
    • Heeley DH, Dhoot GK, Perry SV. Factors determining the subunit composition of tropomyosin in mammalian skeletal muscle. Biochem J 1985; 226:461-8.
    • (1985) Biochem J , vol.226 , pp. 461-468
    • Heeley, D.H.1    Dhoot, G.K.2    Perry, S.V.3
  • 54
    • 0020529404 scopus 로고
    • Some functional properties of nonpolymerizable and polymerizable tropomyosin
    • Dabrowska R, Nowak E, Drabikowski W. Some functional properties of nonpolymerizable and polymerizable tropomyosin. J Muscle Res Cell Motil 1983; 4:143-61.
    • (1983) J Muscle Res Cell Motil , vol.4 , pp. 143-161
    • Dabrowska, R.1    Nowak, E.2    Drabikowski, W.3
  • 55
    • 0024513868 scopus 로고
    • Effects of deletion of tropomyosin overlap on regulated actomyosin subfragment 1 ATPase
    • Heeley DH, Smillie LB, Lohmeier-Vogel EM. Effects of deletion of tropomyosin overlap on regulated actomyosin subfragment 1 ATPase. Biochem J 1989; 258:831-6.
    • (1989) Biochem J , vol.258 , pp. 831-836
    • Heeley, D.H.1    Smillie, L.B.2    Lohmeier-Vogel, E.M.3
  • 56
    • 0028324847 scopus 로고
    • Investigation of the effects of phosphorylation of rabbit striated muscle alpha alpha-tropomyosin and rabbit skeletal muscle troponin-T
    • Heeley DH. Investigation of the effects of phosphorylation of rabbit striated muscle alpha alpha-tropomyosin and rabbit skeletal muscle troponin-T. Eur J Biochem 1994; 221:129-37.
    • (1994) Eur J Biochem , vol.221 , pp. 129-137
    • Heeley, D.H.1
  • 57
    • 0038032832 scopus 로고    scopus 로고
    • Extracellular signal-regulated kinase mediates phosphorylation of tropomyosin-1 to promote cytoskeleton remodeling in response to oxidative stress: impact on membrane blebbing
    • Houle F, Rousseau S, Morrice N, Luc M, Mongrain S, Turner CE, et al. Extracellular signal-regulated kinase mediates phosphorylation of tropomyosin-1 to promote cytoskeleton remodeling in response to oxidative stress: impact on membrane blebbing. Mol Biol Cell 2003; 14:1418-32.
    • (2003) Mol Biol Cell , vol.14 , pp. 1418-1432
    • Houle, F.1    Rousseau, S.2    Morrice, N.3    Luc, M.4    Mongrain, S.5    Turner, C.E.6
  • 58
    • 23144450820 scopus 로고    scopus 로고
    • Protein kinase activity of phosphoinositide-3-kinase regulates beta-adrenergic receptor endocytosis
    • Naga Prasad SV, Jayatilleke A, Madamanchi A, Rockman HA. Protein kinase activity of phosphoinositide-3-kinase regulates beta-adrenergic receptor endocytosis. Nat Cell Biol 2005; 7:785-96.
    • (2005) Nat Cell Biol , vol.7 , pp. 785-796
    • Naga Prasad, S.V.1    Jayatilleke, A.2    Madamanchi, A.3    Rockman, H.A.4
  • 59
    • 67651102789 scopus 로고    scopus 로고
    • Shear flow increases S-nitrosylation of proteins in endothelial cells
    • Huang B, Chen SC, Wang DL. Shear flow increases S-nitrosylation of proteins in endothelial cells. Cardiovasc Res 2009; 83:536-46.
    • (2009) Cardiovasc Res , vol.83 , pp. 536-546
    • Huang, B.1    Chen, S.C.2    Wang, D.L.3
  • 61
    • 0022349490 scopus 로고
    • Monoclonal antibodies against chicken tropomyosin isoforms: production, characterization and application
    • Lin JJ, Chou CS, Lin JL. Monoclonal antibodies against chicken tropomyosin isoforms: production, characterization and application. Hybridoma 1985; 4:223-42.
    • (1985) Hybridoma , vol.4 , pp. 223-242
    • Lin, J.J.1    Chou, C.S.2    Lin, J.L.3
  • 62
    • 0028926206 scopus 로고
    • Forced expression of chimeric human fibroblast tropomyosin mutants affects cytokinesis
    • Warren KS, Lin JL, McDermott JP, Lin JJ. Forced expression of chimeric human fibroblast tropomyosin mutants affects cytokinesis. J Cell Biol 1995; 129:697-708.
    • (1995) J Cell Biol , vol.129 , pp. 697-708
    • Warren, K.S.1    Lin, J.L.2    McDermott, J.P.3    Lin, J.J.4
  • 63
    • 0342316450 scopus 로고    scopus 로고
    • Tropomyosin isoform 5b is expressed in human erythrocytes: implications of tropomodulin-TM5 or tropomodulin-TM5b complexes in the protofilament and hexagonal organization of membrane skeletons
    • Sung LA, Gao KM, Yee LJ, Temm-Grove CJ, Helfman DM, Lin JJ, et al. Tropomyosin isoform 5b is expressed in human erythrocytes: implications of tropomodulin-TM5 or tropomodulin-TM5b complexes in the protofilament and hexagonal organization of membrane skeletons. Blood 2000; 95:1473-80.
    • (2000) Blood , vol.95 , pp. 1473-1480
    • Sung, L.A.1    Gao, K.M.2    Yee, L.J.3    Temm-Grove, C.J.4    Helfman, D.M.5    Lin, J.J.6
  • 64
    • 0027367331 scopus 로고
    • In vitro functional characterization of bacterially expressed human fibroblast tropomyosin isoforms and their chimeric mutants
    • Novy RE, Sellers JR, Liu LF, Lin JJ. In vitro functional characterization of bacterially expressed human fibroblast tropomyosin isoforms and their chimeric mutants. Cell Motil Cytoskel 1993; 26:248-61.
    • (1993) Cell Motil Cytoskel , vol.26 , pp. 248-261
    • Novy, R.E.1    Sellers, J.R.2    Liu, L.F.3    Lin, J.J.4
  • 65
    • 4444219750 scopus 로고    scopus 로고
    • Sorting of a nonmuscle tropomyosin to a novel cytoskeletal compartment in skeletal muscle results in muscular dystrophy
    • Kee AJ, Schevzov G, Nair-Shalliker V, Robinson CS, Vrhovski B, Ghoddusi M, et al. Sorting of a nonmuscle tropomyosin to a novel cytoskeletal compartment in skeletal muscle results in muscular dystrophy. J Cell Biol 2004; 166:685-96.
    • (2004) J Cell Biol , vol.166 , pp. 685-696
    • Kee, A.J.1    Schevzov, G.2    Nair-Shalliker, V.3    Robinson, C.S.4    Vrhovski, B.5    Ghoddusi, M.6
  • 66
    • 0023808937 scopus 로고
    • Differential localization of tropomyosin isoforms in cultured nonmuscle cells
    • Lin JJ, Hegmann TE, Lin JL. Differential localization of tropomyosin isoforms in cultured nonmuscle cells. J Cell Biol 1988; 107:563-72.
    • (1988) J Cell Biol , vol.107 , pp. 563-572
    • Lin, J.J.1    Hegmann, T.E.2    Lin, J.L.3
  • 67
    • 0031759354 scopus 로고    scopus 로고
    • Tropomyosin isoform diversity and neuronal morphogenesis
    • Dufour C, Weinberger RP, Gunning P. Tropomyosin isoform diversity and neuronal morphogenesis. Imm Cell Biol 1998; 76:424-9.
    • (1998) Imm Cell Biol , vol.76 , pp. 424-429
    • Dufour, C.1    Weinberger, R.P.2    Gunning, P.3
  • 68
    • 0037404638 scopus 로고    scopus 로고
    • Tropomyosin isoforms from the gamma gene differing at the C-terminus are spatially and developmentally regulated in the brain
    • Vrhovski B, Schevzov G, Dingle S, Lessard JL, Gunning P, Weinberger RP. Tropomyosin isoforms from the gamma gene differing at the C-terminus are spatially and developmentally regulated in the brain. J Neurosci Res 2003; 72:373-83.
    • (2003) J Neurosci Res , vol.72 , pp. 373-383
    • Vrhovski, B.1    Schevzov, G.2    Dingle, S.3    Lessard, J.L.4    Gunning, P.5    Weinberger, R.P.6
  • 70
    • 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 JP, Helfman DM. Brain-specific tropomyosins TMBr-1 and TMBr-3 have distinct patterns of expression during development and in adult brain. Proc Natl Acad Sci USA 1993; 90:9857-61.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 9857-9861
    • Stamm, S.1    Casper, D.2    Lees-Miller, J.P.3    Helfman, D.M.4
  • 71
    • 0028117925 scopus 로고
    • Tropomyosin isoforms in rat neurons: the different developmental profiles and distributions of TM-4 and TMBr-3 are consistent with different functions
    • Had L, Faivre-Sarrailh C, Legrand C, Mery J, Brugidou J, Rabie A. Tropomyosin isoforms in rat neurons: the different developmental profiles and distributions of TM-4 and TMBr-3 are consistent with different functions. J Cell Sci 1994; 107:2961-73.
    • (1994) J Cell Sci , vol.107 , pp. 2961-2973
    • Had, L.1    Faivre-Sarrailh, C.2    Legrand, C.3    Mery, J.4    Brugidou, J.5    Rabie, A.6
  • 72
    • 79957643206 scopus 로고    scopus 로고
    • Tropomyosin variants describe distinct functional subcellular domains in differentiated vascular smooth muscle cells
    • Gallant C, Appel S, Graceffa P, Leavis P, Lin JJ, Gunning PW, et al. Tropomyosin variants describe distinct functional subcellular domains in differentiated vascular smooth muscle cells. Am J Physiol Cell Physiol 2011; 300:1356-65.
    • (2011) Am J Physiol Cell Physiol , vol.300 , pp. 1356-1365
    • Gallant, C.1    Appel, S.2    Graceffa, P.3    Leavis, P.4    Lin, J.J.5    Gunning, P.W.6
  • 73
    • 36248956949 scopus 로고    scopus 로고
    • DAP kinase mediates the phosphorylation of tropomyosin-1 downstream of the ERK pathway, which regulates the formation of stress fibers in response to oxidative stress
    • Houle F, Poirier A, Dumaresq J, Huot J. DAP kinase mediates the phosphorylation of tropomyosin-1 downstream of the ERK pathway, which regulates the formation of stress fibers in response to oxidative stress. J Cell Sci 2007; 120:3666-77.
    • (2007) J Cell Sci , vol.120 , pp. 3666-3677
    • Houle, F.1    Poirier, A.2    Dumaresq, J.3    Huot, J.4
  • 74
    • 0344392913 scopus 로고    scopus 로고
    • Polarization of specific tropomyosin isoforms in gastrointestinal epithelial cells and their impact on CFTR at the apical surface
    • Dalby-Payne JR, O'Loughlin EV, Gunning P. Polarization of specific tropomyosin isoforms in gastrointestinal epithelial cells and their impact on CFTR at the apical surface. Mol Biol Cell 2003; 14:4365-75.
    • (2003) Mol Biol Cell , vol.14 , pp. 4365-4375
    • Dalby-Payne, J.R.1    O'Loughlin, E.V.2    Gunning, P.3
  • 75
    • 77951975127 scopus 로고    scopus 로고
    • Alternatively spliced N-terminal exons in tropomyosin isoforms do not act as autonomous targeting signals
    • Martin C, Schevzov G, Gunning P. Alternatively spliced N-terminal exons in tropomyosin isoforms do not act as autonomous targeting signals. J Struct Biol 2010; 170:286-93.
    • (2010) J Struct Biol , vol.170 , pp. 286-293
    • Martin, C.1    Schevzov, G.2    Gunning, P.3
  • 76
    • 62849099763 scopus 로고    scopus 로고
    • Tropomyosin Isoform Expression Regulates the Transition of Adhesions To Determine Cell Speed and Direction
    • Bach CTT, Creed S, Zhong J, Mahmassani M, Schevzov G, Stehn J, et al. Tropomyosin Isoform Expression Regulates the Transition of Adhesions To Determine Cell Speed and Direction. Mol Cell Biol 2009; 29:1506-14.
    • (2009) Mol Cell Biol , vol.29 , pp. 1506-1514
    • Bach, C.T.T.1    Creed, S.2    Zhong, J.3    Mahmassani, M.4    Schevzov, G.5    Stehn, J.6
  • 77
    • 38149026973 scopus 로고    scopus 로고
    • Tropomyosin 4 regulates adhesion structures and resorptive capacity in osteoclasts
    • McMichael BK, Lee BS. Tropomyosin 4 regulates adhesion structures and resorptive capacity in osteoclasts. Exp Cell Res 2008; 314:564-73.
    • (2008) Exp Cell Res , vol.314 , pp. 564-573
    • McMichael, B.K.1    Lee, B.S.2
  • 78
    • 53349179574 scopus 로고    scopus 로고
    • High molecular weight tropomyosins regulate osteoclast cytoskeletal morphology
    • Kotadiya P, McMichael BK, Lee BS. High molecular weight tropomyosins regulate osteoclast cytoskeletal morphology. Bone 2008; 43:951-60.
    • (2008) Bone , vol.43 , pp. 951-960
    • Kotadiya, P.1    McMichael, B.K.2    Lee, B.S.3
  • 79
    • 78650056157 scopus 로고    scopus 로고
    • Tropomyosin isoform 3 promotes the formation of filopodia by regulating the recruitment of actinbinding proteins to actin filaments
    • Creed SJ, Desouza M, Bamburg JR, Gunning P, Stehn J. Tropomyosin isoform 3 promotes the formation of filopodia by regulating the recruitment of actinbinding proteins to actin filaments. Exp Cell Res 2011; 317:249-61.
    • (2011) Exp Cell Res , vol.317 , pp. 249-261
    • Creed, S.J.1    Desouza, M.2    Bamburg, J.R.3    Gunning, P.4    Stehn, J.5
  • 81
  • 82
    • 60549114494 scopus 로고    scopus 로고
    • Mouse models for thin filament disease
    • Nguyen MA, Hardeman EC. Mouse models for thin filament disease. Adv Exp Med Biol 2008; 642:66-77.
    • (2008) Adv Exp Med Biol , vol.642 , pp. 66-77
    • Nguyen, M.A.1    Hardeman, E.C.2
  • 83
    • 60849113734 scopus 로고    scopus 로고
    • Tropomyosins in skeletal muscle diseases
    • Kee AJ, Hardeman EC. Tropomyosins in skeletal muscle diseases. Adv Exp Med Biol 2008; 644:143-57.
    • (2008) Adv Exp Med Biol , vol.644 , pp. 143-157
    • Kee, A.J.1    Hardeman, E.C.2
  • 84
    • 77951623501 scopus 로고    scopus 로고
    • Investigations into tropomyosin function using mouse models
    • Jagatheesan G, Rajan S, Wieczorek DF. Investigations into tropomyosin function using mouse models. J Mol Cell Cardiol 2010; 48:893-8.
    • (2010) J Mol Cell Cardiol , vol.48 , pp. 893-898
    • Jagatheesan, G.1    Rajan, S.2    Wieczorek, D.F.3
  • 85
    • 78649862670 scopus 로고    scopus 로고
    • Intracellular structural compartments, disease and tropomyosins
    • Schevzov G, Fath TPG. Intracellular structural compartments, disease and tropomyosins. Curr Top Pharmacol 2009; 13:1-15.
    • (2009) Curr Top Pharmacol , vol.13 , pp. 1-15
    • Schevzov, G.1    Fath, T.P.G.2
  • 87
    • 1542374026 scopus 로고    scopus 로고
    • Gamma tropomyosin gene products are required for embryonic development
    • Hook J, Lemckert F, Qin H, Schevzov G, Gunning P. Gamma tropomyosin gene products are required for embryonic development. Mol Cell Biol 2004; 24:2318-23.
    • (2004) Mol Cell Biol , vol.24 , pp. 2318-2323
    • Hook, J.1    Lemckert, F.2    Qin, H.3    Schevzov, G.4    Gunning, P.5
  • 88
    • 84992231763 scopus 로고    scopus 로고
    • Functional identity of the gamma tropomyosin gene Implications for embryonic development, reproduction and cell viability
    • Hook J, Lemckert F, Schevzov G, Fath T, Gunning P. Functional identity of the gamma tropomyosin gene Implications for embryonic development, reproduction and cell viability. BioArch 2011; 1:49-59.
    • (2011) BioArch , vol.1 , pp. 49-59
    • Hook, J.1    Lemckert, F.2    Schevzov, G.3    Fath, T.4    Gunning, P.5
  • 91
    • 68549107626 scopus 로고    scopus 로고
    • A cytoskeletal tropomyosin can compromise the structural integrity of skeletal muscle
    • Kee AJ, Gunning PW, Hardeman EC. A cytoskeletal tropomyosin can compromise the structural integrity of skeletal muscle. Cell Motil Cytoskeleton 2009; 66:710-20.
    • (2009) Cell Motil Cytoskeleton , vol.66 , pp. 710-720
    • Kee, A.J.1    Gunning, P.W.2    Hardeman, E.C.3
  • 92
    • 63049113333 scopus 로고    scopus 로고
    • Cytoskeletal tropomyosin Tm5NM1 is required for normal excitation-contraction coupling in skeletal muscle
    • Vlahovich N, Kee AJ, Van der Poel C, Kettle E, Hernandez-Deviez D, Lucas C, et al. Cytoskeletal tropomyosin Tm5NM1 is required for normal excitation-contraction coupling in skeletal muscle. Mol Biol Cell 2009; 20:400-9.
    • (2009) Mol Biol Cell , vol.20 , pp. 400-409
    • Vlahovich, N.1    Kee, A.J.2    Van der Poel, C.3    Kettle, E.4    Hernandez-Deviez, D.5    Lucas, C.6
  • 93
    • 77952009376 scopus 로고    scopus 로고
    • New aspects of tropomyosin-regulated neuritogenesis revealed by the deletion of Tm5NM1 and 2
    • Fath T, Agnes Chan YK, Vrhovski B, Clarke H, Curthoys N, Hook J, et al. New aspects of tropomyosin-regulated neuritogenesis revealed by the deletion of Tm5NM1 and 2. Eur J Cell Biol 2010; 89:489-98.
    • (2010) Eur J Cell Biol , vol.89 , pp. 489-498
    • Fath, T.1    Agnes Chan, Y.K.2    Vrhovski, B.3    Clarke, H.4    Curthoys, N.5    Hook, J.6
  • 94
    • 60849099954 scopus 로고    scopus 로고
    • Dimerization of tropomyosins
    • Gimona M. Dimerization of tropomyosins. Adv Exp Med Biol 2008; 644:73-84.
    • (2008) Adv Exp Med Biol , vol.644 , pp. 73-84
    • Gimona, M.1
  • 95
    • 67650762824 scopus 로고    scopus 로고
    • Super-resolution fluorescence microscopy
    • Huang B, Bates M, Zhuang X. Super-resolution fluorescence microscopy. Annu Rev Biochem 2009; 78:993-1016.
    • (2009) Annu Rev Biochem , vol.78 , pp. 993-1016
    • Huang, B.1    Bates, M.2    Zhuang, X.3
  • 97
    • 0021355340 scopus 로고
    • A method for the quantitative recovery of protein in dilute solution in the presence of detergents and lipids
    • Wessel D, Flugge UI. A method for the quantitative recovery of protein in dilute solution in the presence of detergents and lipids. Anal Biochem 1984; 138:141-3.
    • (1984) Anal Biochem , vol.138 , pp. 141-143
    • Wessel, D.1    Flugge, U.I.2
  • 98
    • 0029958680 scopus 로고    scopus 로고
    • Restricted expression of the actin-regulatory protein, tropomyosin, defines distinct boundaries, evaginating neuroepithelium and choroid plexus forerunners during early CNS development
    • Nicholson-Flynn K, Hitchcock-DeGregori SE, Levitt P. Restricted expression of the actin-regulatory protein, tropomyosin, defines distinct boundaries, evaginating neuroepithelium and choroid plexus forerunners during early CNS development. J Neurosci 1996; 16:6853-63.
    • (1996) J Neurosci , vol.16 , pp. 6853-6863
    • Nicholson-Flynn, K.1    Hitchcock-DeGregori, S.E.2    Levitt, P.3
  • 99
    • 17844364567 scopus 로고    scopus 로고
    • Smooth muscle-specific alpha tropomyosin is a marker of fully differentiated smooth muscle in lung
    • Vrhovski B, McKay K, Schevzov G, Gunning PW, Weinberger RP. Smooth muscle-specific alpha tropomyosin is a marker of fully differentiated smooth muscle in lung. J Histochem Cytochem 2005; 53:875-83.
    • (2005) J Histochem Cytochem , vol.53 , pp. 875-883
    • Vrhovski, B.1    McKay, K.2    Schevzov, G.3    Gunning, P.W.4    Weinberger, R.P.5
  • 100
    • 0030032902 scopus 로고    scopus 로고
    • The molecular composition of neuronal microfilaments is spatially and temporally regulated
    • Weinberger R, Schevzov G, Jeffrey P, Gordon K, Hill M, Gunning P. The molecular composition of neuronal microfilaments is spatially and temporally regulated. J Neurosci 1996; 16:238-52.
    • (1996) J Neurosci , vol.16 , pp. 238-252
    • Weinberger, R.1    Schevzov, G.2    Jeffrey, P.3    Gordon, K.4    Hill, M.5    Gunning, P.6
  • 103
    • 0031841942 scopus 로고    scopus 로고
    • Structural compartments within neurons: developmentally regulated organization of microfilament isoform mRNA and protein
    • Hannan AJ, Gunning P, Jeffrey PL, Weinberger RP. Structural compartments within neurons: developmentally regulated organization of microfilament isoform mRNA and protein. Mol Cell Neurosci 1998; 11:289-304.
    • (1998) Mol Cell Neurosci , vol.11 , pp. 289-304
    • Hannan, A.J.1    Gunning, P.2    Jeffrey, P.L.3    Weinberger, R.P.4
  • 105
    • 0033058418 scopus 로고    scopus 로고
    • Nonmuscle tropomyosin-4 requires coexpression with other low molecular weight isoforms for binding to thin filaments in cardiomyocytes
    • Helfman DM, Berthier C, Grossman J, Leu M, Ehler E, Perriard E, et al. Nonmuscle tropomyosin-4 requires coexpression with other low molecular weight isoforms for binding to thin filaments in cardiomyocytes. J Cell Sci 1999; 112:371-80.
    • (1999) J Cell Sci , vol.112 , pp. 371-380
    • Helfman, D.M.1    Berthier, C.2    Grossman, J.3    Leu, M.4    Ehler, E.5    Perriard, E.6
  • 106
    • 49249092510 scopus 로고    scopus 로고
    • Tropomyosin isoforms define distinct microfilament populations with different drug susceptibility
    • Creed SJ, Bryce N, Naumanen P, Weinberger R, Lappalainen P, Stehn J, et al. Tropomyosin isoforms define distinct microfilament populations with different drug susceptibility. Eur J Cell Biol 2008; 87:709-20.
    • (2008) Eur J Cell Biol , vol.87 , pp. 709-720
    • Creed, S.J.1    Bryce, N.2    Naumanen, P.3    Weinberger, R.4    Lappalainen, P.5    Stehn, J.6
  • 107
    • 79952534369 scopus 로고    scopus 로고
    • The actin-associating protein Tm5NM1 blocks mesenchymal motility without transition to amoeboid motility
    • Lees JG, Bach CT, Bradbury P, Paul A, Gunning PW, O'Neill GM. The actin-associating protein Tm5NM1 blocks mesenchymal motility without transition to amoeboid motility. Oncogene 2011; 30:1241-51.
    • (2011) Oncogene , vol.30 , pp. 1241-1251
    • Lees, J.G.1    Bach, C.T.2    Bradbury, P.3    Paul, A.4    Gunning, P.W.5    O'Neill, G.M.6
  • 108
    • 0035864823 scopus 로고    scopus 로고
    • A mutation in alphatropomyosin(slow) affects muscle strength, maturation and hypertrophy in a mouse model for nemaline myopathy
    • Corbett MA, Robinson CS, Dunglison GF, Yang N, Joya JE, Stewart AW, et al. A mutation in alphatropomyosin(slow) affects muscle strength, maturation and hypertrophy in a mouse model for nemaline myopathy. Hum Mol Gen 2001; 10:317-28.
    • (2001) Hum Mol Gen , vol.10 , pp. 317-328
    • Corbett, M.A.1    Robinson, C.S.2    Dunglison, G.F.3    Yang, N.4    Joya, J.E.5    Stewart, A.W.6
  • 109
    • 0033538612 scopus 로고    scopus 로고
    • Mouse model of a familial hypertrophic cardiomyopathy mutation in alphatropomyosin manifests cardiac dysfunction
    • Muthuchamy M, Pieples K, Rethinasamy P, Hoit B, Grupp IL, Boivin GP, et al. Mouse model of a familial hypertrophic cardiomyopathy mutation in alphatropomyosin manifests cardiac dysfunction. Circ Res 1999; 85:47-56.
    • (1999) Circ Res , vol.85 , pp. 47-56
    • Muthuchamy, M.1    Pieples, K.2    Rethinasamy, P.3    Hoit, B.4    Grupp, I.L.5    Boivin, G.P.6
  • 110
    • 0034781383 scopus 로고    scopus 로고
    • A familial hypertrophic cardiomyopathy alpha-tropomyosin mutation causes severe cardiac hypertrophy and death in mice
    • Prabhakar R, Boivin GP, Grupp IL, Hoit B, Arteaga G, Solaro JR, et al. A familial hypertrophic cardiomyopathy alpha-tropomyosin mutation causes severe cardiac hypertrophy and death in mice. J Mol Cell Cardiol 2001; 33:1815-28.
    • (2001) J Mol Cell Cardiol , vol.33 , pp. 1815-1828
    • Prabhakar, R.1    Boivin, G.P.2    Grupp, I.L.3    Hoit, B.4    Arteaga, G.5    Solaro, J.R.6
  • 111
    • 34547605959 scopus 로고    scopus 로고
    • Dilated cardiomyopathy mutant tropomyosin mice develop cardiac dysfunction with significantly decreased fractional shortening and myofilament calcium sensitivity
    • Rajan S, Ahmed RP, Jagatheesan G, Petrashevskaya N, Boivin GP, Urboniene D, et al. Dilated cardiomyopathy mutant tropomyosin mice develop cardiac dysfunction with significantly decreased fractional shortening and myofilament calcium sensitivity. Circ Res 2007; 101:205-14.
    • (2007) Circ Res , vol.101 , pp. 205-214
    • Rajan, S.1    Ahmed, R.P.2    Jagatheesan, G.3    Petrashevskaya, N.4    Boivin, G.P.5    Urboniene, D.6
  • 112
    • 0036784002 scopus 로고    scopus 로고
    • Tropomyosin 3 expression leads to hypercontractility and attenuates myofilament lengthdependent Ca(2+) activation
    • Pieples K, Arteaga G, Solaro RJ, Grupp I, Lorenz JN, Boivin GP, et al. Tropomyosin 3 expression leads to hypercontractility and attenuates myofilament lengthdependent Ca(2+) activation. Am J Physiol Heart Circ Physiol 2002; 283:1344-53.
    • (2002) Am J Physiol Heart Circ Physiol , vol.283 , pp. 1344-1353
    • Pieples, K.1    Arteaga, G.2    Solaro, R.J.3    Grupp, I.4    Lorenz, J.N.5    Boivin, G.P.6
  • 114
    • 0029559447 scopus 로고
    • Molecular and physiological effects of overexpressing striated muscle beta-tropomyosin in the adult murine heart
    • Muthuchamy M, Grupp IL, Grupp G, O'Toole BA, Kier AB, Boivin GP, et al. Molecular and physiological effects of overexpressing striated muscle beta-tropomyosin in the adult murine heart. J Biol Chem 1995; 270:30593-603.
    • (1995) J Biol Chem , vol.270 , pp. 30593-30603
    • Muthuchamy, M.1    Grupp, I.L.2    Grupp, G.3    O'Toole, B.A.4    Kier, A.B.5    Boivin, G.P.6
  • 119
    • 5344222725 scopus 로고    scopus 로고
    • Modification of the tropomyosin isoform composition of actin filaments in the brain by deletion of an alternatively spliced exon
    • Vrhovski B, Lemckert F, Gunning P. Modification of the tropomyosin isoform composition of actin filaments in the brain by deletion of an alternatively spliced exon. Neuropharmacology 2004; 47:684-93.
    • (2004) Neuropharmacology , vol.47 , pp. 684-693
    • Vrhovski, B.1    Lemckert, F.2    Gunning, P.3


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