메뉴 건너뛰기




Volumn 64, Issue 3, 2007, Pages 157-173

Talin2 is induced during striated muscle differentiation and is targeted to stable adhesion complexes in mature muscle

Author keywords

Costamere; Focal adhesion; Intercalated disk; Muscle differentiation; Talin

Indexed keywords

ACTIN; ALPHA ACTININ; ANTIBODY; ARCHVILLIN; BETA ACTIN; BETA1 INTEGRIN; CYTOSKELETON PROTEIN; DESMIN; FOCAL ADHESION KINASE; GLYCERALDEHYDE 3 PHOSPHATE DEHYDROGENASE; GREEN FLUORESCENT PROTEIN; INTEGRIN; MESSENGER RNA; METAVINCULIN; MYOSIN; SUPERVILLIN; TALIN; TALIN 1; TALIN 2; UNCLASSIFIED DRUG; VINCULIN;

EID: 33847217997     PISSN: 08861544     EISSN: 10970169     Source Type: Journal    
DOI: 10.1002/cm.20173     Document Type: Article
Times cited : (57)

References (76)
  • 1
    • 0032191350 scopus 로고    scopus 로고
    • Muscle differentiation: More complexity to the network of myogenic regulators
    • Arnold H, Winter B. 1998. Muscle differentiation: More complexity to the network of myogenic regulators. Curr Opin Genet Dev 8:539-544.
    • (1998) Curr Opin Genet Dev , vol.8 , pp. 539-544
    • Arnold, H.1    Winter, B.2
  • 2
    • 0033565992 scopus 로고    scopus 로고
    • Talin contains three similar vinculin-binding sites predicted to form an amphipathic helix
    • Bass MD, Smith BJ, Prigent SA, Critchley DR. 1999. Talin contains three similar vinculin-binding sites predicted to form an amphipathic helix. Biochem J 341(Part 2):257-263.
    • (1999) Biochem J , vol.341 , Issue.PART 2 , pp. 257-263
    • Bass, M.D.1    Smith, B.J.2    Prigent, S.A.3    Critchley, D.R.4
  • 3
    • 0022458171 scopus 로고
    • Localization of talin in skeletal and cardiac muscles
    • Belkin AM, Zhidkova NI, Koteliansky VE. 1986. Localization of talin in skeletal and cardiac muscles. FEBS Lett 200(1):32-36.
    • (1986) FEBS Lett , vol.200 , Issue.1 , pp. 32-36
    • Belkin, A.M.1    Zhidkova, N.I.2    Koteliansky, V.E.3
  • 4
    • 0029671374 scopus 로고    scopus 로고
    • β 1D integrin displaces the β 1A isoform in striated muscles: Localization at junctional structures and signaling potential in nonmuscle cells
    • Belkin AM, Zhidkova NI, Balzac F, Altruda F, Tomatis D, Maier A, Tarone G, Koteliansky VE, Burridge K. 1996. β 1D integrin displaces the β 1A isoform in striated muscles: Localization at junctional structures and signaling potential in nonmuscle cells. J Cell Biol 132(1/2):211-226.
    • (1996) J Cell Biol , vol.132 , Issue.1-2 , pp. 211-226
    • Belkin, A.M.1    Zhidkova, N.I.2    Balzac, F.3    Altruda, F.4    Tomatis, D.5    Maier, A.6    Tarone, G.7    Koteliansky, V.E.8    Burridge, K.9
  • 5
    • 2442575665 scopus 로고    scopus 로고
    • Pbx marks genes for activation by MyoD indicating a role for a homeodomain protein in establishing myogenic potential
    • Berkes CA, Bergstrom DA, Penn BH, Seaver KJ, Knoepfler PS, Tapscott SJ. 2004. Pbx marks genes for activation by MyoD indicating a role for a homeodomain protein in establishing myogenic potential. Mol Cell 14:465-477.
    • (2004) Mol Cell , vol.14 , pp. 465-477
    • Berkes, C.A.1    Bergstrom, D.A.2    Penn, B.H.3    Seaver, K.J.4    Knoepfler, P.S.5    Tapscott, S.J.6
  • 7
    • 0032547737 scopus 로고    scopus 로고
    • Layilin, a novel talin-binding transmembrane protein homologous with C-type lectins, is localized in membrane ruffles
    • Borowsky ML, Hynes RO. 1998. Layilin, a novel talin-binding transmembrane protein homologous with C-type lectins, is localized in membrane ruffles. J Cell Biol 143(2):429-442.
    • (1998) J Cell Biol , vol.143 , Issue.2 , pp. 429-442
    • Borowsky, M.L.1    Hynes, R.O.2
  • 8
    • 11244316522 scopus 로고    scopus 로고
    • Talin distribution during the differentiation of satellite cells isolated from rat skeletal muscle
    • Brzoska E, Wrobel E, Grabowska I, Moraczewski J. 2004. Talin distribution during the differentiation of satellite cells isolated from rat skeletal muscle. Cell Mol Biol Lett 9:723-737.
    • (2004) Cell Mol Biol Lett , vol.9 , pp. 723-737
    • Brzoska, E.1    Wrobel, E.2    Grabowska, I.3    Moraczewski, J.4
  • 9
    • 0020805412 scopus 로고
    • A new protein of adhesion plaques and ruffling membranes
    • Burridge K, Connell L. 1983a. A new protein of adhesion plaques and ruffling membranes. J Cell Biol 97(2):359-367.
    • (1983) J Cell Biol , vol.97 , Issue.2 , pp. 359-367
    • Burridge, K.1    Connell, L.2
  • 10
    • 0020999298 scopus 로고
    • Talin: A cytoskeletal component concentrated in adhesion plaques and other sites of actin-membrane interaction
    • Burridge K, Connell L. 1983b. Talin: A cytoskeletal component concentrated in adhesion plaques and other sites of actin-membrane interaction. Cell Motil 3(5/6):405-417.
    • (1983) Cell Motil , vol.3 , Issue.5-6 , pp. 405-417
    • Burridge, K.1    Connell, L.2
  • 11
    • 0021214312 scopus 로고
    • An interaction between vinculin and talin
    • Burridge K, Mangeat P. 1984. An interaction between vinculin and talin. Nature 308(5961):744-746.
    • (1984) Nature , vol.308 , Issue.5961 , pp. 744-746
    • Burridge, K.1    Mangeat, P.2
  • 12
    • 1442331993 scopus 로고    scopus 로고
    • Integrin activation
    • Calderwood DA. 2004. Integrin activation. J Cell Sci 117:657-666.
    • (2004) J Cell Sci , vol.117 , pp. 657-666
    • Calderwood, D.A.1
  • 13
    • 0042195824 scopus 로고    scopus 로고
    • Talin forges the links between integrins and actin
    • Calderwood DA, Ginsberg MH. 2003. Talin forges the links between integrins and actin. Nat Cell Biol 5(8):694-697.
    • (2003) Nat Cell Biol , vol.5 , Issue.8 , pp. 694-697
    • Calderwood, D.A.1    Ginsberg, M.H.2
  • 14
    • 0033213922 scopus 로고    scopus 로고
    • The talin head domain binds to integrin β subunit cytoplasmic tails and regulates integrin activation
    • Calderwood DA, Zent R, Grant R, Rees DJ, Hynes RO, Ginsberg MH. 1999. The talin head domain binds to integrin β subunit cytoplasmic tails and regulates integrin activation. J Biol Chem 274(40):28071-28074.
    • (1999) J Biol Chem , vol.274 , Issue.40 , pp. 28071-28074
    • Calderwood, D.A.1    Zent, R.2    Grant, R.3    Rees, D.J.4    Hynes, R.O.5    Ginsberg, M.H.6
  • 19
    • 20444492339 scopus 로고    scopus 로고
    • Two distinct head-tail interfaces cooperate to suppress activation of vinculin by talin
    • Cohen DM, Chen H, Johnson RP, Choudhury B, Craig SW. 2005. Two distinct head-tail interfaces cooperate to suppress activation of vinculin by talin. J Biol Chem 280:17109-17117.
    • (2005) J Biol Chem , vol.280 , pp. 17109-17117
    • Cohen, D.M.1    Chen, H.2    Johnson, R.P.3    Choudhury, B.4    Craig, S.W.5
  • 20
    • 0027247797 scopus 로고
    • A new isoform of the laminin receptor integrin α7β1 is developmentally regulated in skeletal muscle
    • Collo G, Starr L, Quaranta V. 1993. A new isoform of the laminin receptor integrin α7β1 is developmentally regulated in skeletal muscle. J Biol Chem 268:19019-19024.
    • (1993) J Biol Chem , vol.268 , pp. 19019-19024
    • Collo, G.1    Starr, L.2    Quaranta, V.3
  • 21
    • 0037350396 scopus 로고    scopus 로고
    • TES is a novel focal adhesion protein with a role in cell spreading
    • Coutts A, MacKenzie E, Griffith E, Black D. 2003. TES is a novel focal adhesion protein with a role in cell spreading. J Cell Sci 116:897-906.
    • (2003) J Cell Sci , vol.116 , pp. 897-906
    • Coutts, A.1    MacKenzie, E.2    Griffith, E.3    Black, D.4
  • 22
    • 0021009545 scopus 로고
    • γ actin, spectrin, and intermediate filament proteins colocalize with vinculin at costameres, myofibril-to- sarcolemma attachment sites
    • Craig SW, Pardo JV. 1983. γ actin, spectrin, and intermediate filament proteins colocalize with vinculin at costameres, myofibril-to- sarcolemma attachment sites. Cell Motil 3(5/6):449-462.
    • (1983) Cell Motil , vol.3 , Issue.5-6 , pp. 449-462
    • Craig, S.W.1    Pardo, J.V.2
  • 23
    • 0026739841 scopus 로고
    • Costameres are sites of force transmission to the substratum in adult rat cardiomyocytes
    • Danowski BA, Imanaka-Yoshida K, Sanger JM, Sanger JW. 1992. Costameres are sites of force transmission to the substratum in adult rat cardiomyocytes. J Cell Biol 118(6):1411-1420.
    • (1992) J Cell Biol , vol.118 , Issue.6 , pp. 1411-1420
    • Danowski, B.A.1    Imanaka-Yoshida, K.2    Sanger, J.M.3    Sanger, J.W.4
  • 25
    • 0038190993 scopus 로고    scopus 로고
    • Costameres: The Achilles' heel of Herculean muscle
    • Ervasti E. 2003. Costameres: The Achilles' heel of Herculean muscle. J Biol Chem 278:13591-13594.
    • (2003) J Biol Chem , vol.278 , pp. 13591-13594
    • Ervasti, E.1
  • 26
    • 0034920526 scopus 로고    scopus 로고
    • Cytoskeletal proteins and platelet signaling
    • Fox JEB. 2001. Cytoskeletal proteins and platelet signaling. Thromb Haemost 86:198-213.
    • (2001) Thromb Haemost , vol.86 , pp. 198-213
    • Fox, J.E.B.1
  • 29
    • 0026687925 scopus 로고
    • Cyclic amplification and selection of targets for multicomponent complexes: Myogenin interacts with factors recognizing biding sites for basic-helix-loop-helix, nuclear factor1, myocyte-specific enhancer-binding factor 2, and COMP1 factor
    • Funk WD, Wright WE. 1992. Cyclic amplification and selection of targets for multicomponent complexes: Myogenin interacts with factors recognizing biding sites for basic-helix-loop-helix, nuclear factor1, myocyte-specific enhancer-binding factor 2, and COMP1 factor. Proc Natl Acad Sci USA 89:9484-9488.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 9484-9488
    • Funk, W.D.1    Wright, W.E.2
  • 31
    • 0032513116 scopus 로고    scopus 로고
    • A novel site, Mt, in the human desmin enhancer is necessary for maximal expression in skeletal muscle
    • Gao J, Li Z, Paulin D. 1998. A novel site, Mt, in the human desmin enhancer is necessary for maximal expression in skeletal muscle. J Biol Chem 273:6402-6409.
    • (1998) J Biol Chem , vol.273 , pp. 6402-6409
    • Gao, J.1    Li, Z.2    Paulin, D.3
  • 33
    • 0038495876 scopus 로고    scopus 로고
    • A locus on chromosome 15q for a dominantly inherited nemaline myopathy with core-like lesions
    • Gommans IMP, Davis M, Saar K, Kremer H. 2003. A locus on chromosome 15q for a dominantly inherited nemaline myopathy with core-like lesions. Brain 126:1545-1551.
    • (2003) Brain , vol.126 , pp. 1545-1551
    • Gommans, I.M.P.1    Davis, M.2    Saar, K.3    Kremer, H.4
  • 35
    • 0022534722 scopus 로고
    • Interaction of plasma membrane fibronectin receptor with talin-A transmembrane linkage
    • Horwitz A, Duggan K, Buck C, Beckerle MC, Burridge K. 1986. Interaction of plasma membrane fibronectin receptor with talin-A transmembrane linkage. Nature 320(6062):531-533.
    • (1986) Nature , vol.320 , Issue.6062 , pp. 531-533
    • Horwitz, A.1    Duggan, K.2    Buck, C.3    Beckerle, M.C.4    Burridge, K.5
  • 36
    • 0026775471 scopus 로고
    • Different effects of A23187 and PMA on palmitoylated platelet proteins
    • Huang EM. 1992. Different effects of A23187 and PMA on palmitoylated platelet proteins. Thromb Res 68(1):75-86.
    • (1992) Thromb Res , vol.68 , Issue.1 , pp. 75-86
    • Huang, E.M.1
  • 37
    • 3042600016 scopus 로고    scopus 로고
    • Structural basis for amplifying vinculin activation by talin
    • Izard T, Vonrhein C. 2004. Structural basis for amplifying vinculin activation by talin. J Biol Chem 279:27667-27678.
    • (2004) J Biol Chem , vol.279 , pp. 27667-27678
    • Izard, T.1    Vonrhein, C.2
  • 39
    • 0041461882 scopus 로고    scopus 로고
    • Two-piconewton slip bond between fibronectin and the cytoskeleton depends on talin
    • Jiang G, Giannone G, Critchley DR, Fukumoto E, Sheetz MP. 2003. Two-piconewton slip bond between fibronectin and the cytoskeleton depends on talin. Nature 424:334-337.
    • (2003) Nature , vol.424 , pp. 334-337
    • Jiang, G.1    Giannone, G.2    Critchley, D.R.3    Fukumoto, E.4    Sheetz, M.P.5
  • 40
    • 0028318397 scopus 로고
    • An intramolecular association between the head and tail domains of vinculin modulates talin binding
    • Johnson RP, Craig SW. 1994. An intramolecular association between the head and tail domains of vinculin modulates talin binding. J Biol Chem 269(17):12611-12619.
    • (1994) J Biol Chem , vol.269 , Issue.17 , pp. 12611-12619
    • Johnson, R.P.1    Craig, S.W.2
  • 41
    • 0019201264 scopus 로고
    • Isolation of mouse myocardial gap junctions
    • Kensler RW, Goodenough DA. 1980. Isolation of mouse myocardial gap junctions. J Cell Biol 86(3):755-764.
    • (1980) J Cell Biol , vol.86 , Issue.3 , pp. 755-764
    • Kensler, R.W.1    Goodenough, D.A.2
  • 44
    • 0037038412 scopus 로고    scopus 로고
    • Type I γ phosphatidylinositol phosphate kinase targets and regulates focal adhesions
    • Ling K, Doughman RL, Firestone AJ, Bunce MW, Anderson RA. 2002. Type I γ phosphatidylinositol phosphate kinase targets and regulates focal adhesions. Nature 420(6911):89-93.
    • (2002) Nature , vol.420 , Issue.6911 , pp. 89-93
    • Ling, K.1    Doughman, R.L.2    Firestone, A.J.3    Bunce, M.W.4    Anderson, R.A.5
  • 45
    • 0033731119 scopus 로고    scopus 로고
    • Integrin cytoplasmic domain-binding proteins
    • Liu S, Calderwood DA, Ginsberg MH. 2000. Integrin cytoplasmic domain-binding proteins. J Cell Sci 113:3563-3571.
    • (2000) J Cell Sci , vol.113 , pp. 3563-3571
    • Liu, S.1    Calderwood, D.A.2    Ginsberg, M.H.3
  • 46
    • 0033545894 scopus 로고    scopus 로고
    • Molecular interactions of N-RAP, a nebulin-related protein of striated muscle myotendon junctions and intercalated disks
    • Luo G, Herrera AH, Horowits R. 1999. Molecular interactions of N-RAP, a nebulin-related protein of striated muscle myotendon junctions and intercalated disks. Biochemistry 38(19):6135-6143.
    • (1999) Biochemistry , vol.38 , Issue.19 , pp. 6135-6143
    • Luo, G.1    Herrera, A.H.2    Horowits, R.3
  • 47
    • 0033040628 scopus 로고    scopus 로고
    • The Arp2/3 complex: A multifunctional actin organizer
    • Machesky LM, Gould KL. 1999. The Arp2/3 complex: A multifunctional actin organizer. Curr Opin Cell Biol 11(1):117-121.
    • (1999) Curr Opin Cell Biol , vol.11 , Issue.1 , pp. 117-121
    • Machesky, L.M.1    Gould, K.L.2
  • 48
    • 0242470705 scopus 로고    scopus 로고
    • Identification of a novel isoform of the focal adhesion protein talin
    • McCann RO, Craig SW. 1998. Identification of a novel isoform of the focal adhesion protein talin. Mol Biol Cell 9(Suppl):138A.
    • (1998) Mol Biol Cell , vol.9 , Issue.SUPPL.
    • McCann, R.O.1    Craig, S.W.2
  • 49
    • 0028784365 scopus 로고
    • Nebulette: A 107 kD nebulin-like protein in cardiac muscle
    • Moncman CL, Wang K. 1995. Nebulette: A 107 kD nebulin-like protein in cardiac muscle. Cell Motil Cytoskeleton 32(3):205-225.
    • (1995) Cell Motil Cytoskeleton , vol.32 , Issue.3 , pp. 205-225
    • Moncman, C.L.1    Wang, K.2
  • 52
    • 0031589004 scopus 로고    scopus 로고
    • Prediction of the coding sequences of unidentified human genes. VII. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro
    • Nagase T, Ishikawa K, Nakajima D, Ohira M, Seki N, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O. 1997. Prediction of the coding sequences of unidentified human genes. VII. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro. DNA Res 4(2):141-150.
    • (1997) DNA Res , vol.4 , Issue.2 , pp. 141-150
    • Nagase, T.1    Ishikawa, K.2    Nakajima, D.3    Ohira, M.4    Seki, N.5    Miyajima, N.6    Tanaka, A.7    Kotani, H.8    Nomura, N.9    Ohara, O.10
  • 53
    • 1642341451 scopus 로고    scopus 로고
    • Talin: An emerging focal point of adhesion dynamics
    • Nayal A, Webb DJ, Horwitz AF. 2004. Talin: An emerging focal point of adhesion dynamics. Curr Opin Cell Biol 16:94-98.
    • (2004) Curr Opin Cell Biol , vol.16 , pp. 94-98
    • Nayal, A.1    Webb, D.J.2    Horwitz, A.F.3
  • 54
    • 0037044851 scopus 로고    scopus 로고
    • Proteomic analysis of a detergent-resistant membrane skeleton from neutrophil plasma membranes
    • Nebl T, Pestonjamasp KN, Leszyk JD, Crowley JL, Oh SW, Luna EJ. 2002. Proteomic analysis of a detergent-resistant membrane skeleton from neutrophil plasma membranes. J Biol Chem 277:43399-43409.
    • (2002) J Biol Chem , vol.277 , pp. 43399-43409
    • Nebl, T.1    Pestonjamasp, K.N.2    Leszyk, J.D.3    Crowley, J.L.4    Oh, S.W.5    Luna, E.J.6
  • 55
    • 0038348502 scopus 로고    scopus 로고
    • Archvillin, a muscle-specific isoform of supervillin, is an early expressed component of the costameric membrane skeleton
    • Oh SW, Pope RK, Smith KP, Crowley JL, Nebl T, Lawrence JB, Luna EJ. 2003. Archvillin, a muscle-specific isoform of supervillin, is an early expressed component of the costameric membrane skeleton. J Cell Sci 116:2261-2275.
    • (2003) J Cell Sci , vol.116 , pp. 2261-2275
    • Oh, S.W.1    Pope, R.K.2    Smith, K.P.3    Crowley, J.L.4    Nebl, T.5    Lawrence, J.B.6    Luna, E.J.7
  • 56
    • 0010935732 scopus 로고
    • A vinculin-containing cortical lattice in skeletal muscle: Transverse lattice elements ("costameres") mark sites of attachment between myofibrils and sarcolemma
    • Pardo JV, Siliciano JD, Craig SW. 1983. A vinculin-containing cortical lattice in skeletal muscle: Transverse lattice elements ("costameres") mark sites of attachment between myofibrils and sarcolemma. Proc Natl Acad Sci USA 80(4):1008-1012.
    • (1983) Proc Natl Acad Sci USA , vol.80 , Issue.4 , pp. 1008-1012
    • Pardo, J.V.1    Siliciano, J.D.2    Craig, S.W.3
  • 59
    • 33646043789 scopus 로고    scopus 로고
    • Focal adhesion kinase is essential for costamerogenesis in cultured skeletal muscle cells
    • Quach NL, Rando TA. 2006. Focal adhesion kinase is essential for costamerogenesis in cultured skeletal muscle cells. Dev Biol 293(1):38-52.
    • (2006) Dev Biol , vol.293 , Issue.1 , pp. 38-52
    • Quach, N.L.1    Rando, T.A.2
  • 60
    • 28244491001 scopus 로고    scopus 로고
    • Gene duplication and functional divergence during evolution of the cytoskeletal linker protein talin
    • Senetar MA, McCann RO. 2005. Gene duplication and functional divergence during evolution of the cytoskeletal linker protein talin. Gene 362:141-152.
    • (2005) Gene , vol.362 , pp. 141-152
    • Senetar, M.A.1    McCann, R.O.2
  • 61
    • 10644221869 scopus 로고    scopus 로고
    • Intrasteric inhibition mediates the interaction of the 1/LWEQ module proteins Talin1, Talin2, Hip1, and Hip12 with actin
    • Senetar MA, Foster SJ, McCann RO. 2004. Intrasteric inhibition mediates the interaction of the 1/LWEQ module proteins Talin1, Talin2, Hip1, and Hip12 with actin. Biochemistry 43:15418-15428.
    • (2004) Biochemistry , vol.43 , pp. 15418-15428
    • Senetar, M.A.1    Foster, S.J.2    McCann, R.O.3
  • 63
    • 10644287785 scopus 로고    scopus 로고
    • Engrailed genes control developmental fate of serotonergic and noradrenergic neurons in mid- and hindbrain in a gene dose-dependent manner
    • Simon HH, Scholz C, O'Leary DD. 2005. Engrailed genes control developmental fate of serotonergic and noradrenergic neurons in mid- and hindbrain in a gene dose-dependent manner. Mol Cell Neurosci 28:96-105.
    • (2005) Mol Cell Neurosci , vol.28 , pp. 96-105
    • Simon, H.H.1    Scholz, C.2    O'Leary, D.D.3
  • 64
    • 0025917462 scopus 로고
    • Intracompartmental sorting of essential myosin light chains: Molecular dissection and in vivo monitoring by epitope tagging
    • Soldati T, Perriard JC. 1991. Intracompartmental sorting of essential myosin light chains: Molecular dissection and in vivo monitoring by epitope tagging. Cell 66(2):277-289.
    • (1991) Cell , vol.66 , Issue.2 , pp. 277-289
    • Soldati, T.1    Perriard, J.C.2
  • 65
    • 0033984014 scopus 로고    scopus 로고
    • Inositol 1, 4,5-trisphosphate receptor associated with focal contact cytoskeletal proteins
    • Sugiyama T, Matsuda Y, Mikoshiba K. 2000. Inositol 1, 4,5-trisphosphate receptor associated with focal contact cytoskeletal proteins. FEBS Lett 466(1):29-34.
    • (2000) FEBS Lett , vol.466 , Issue.1 , pp. 29-34
    • Sugiyama, T.1    Matsuda, Y.2    Mikoshiba, K.3
  • 66
    • 0029737526 scopus 로고    scopus 로고
    • Talin and vinculin play distinct roles in filopodial motility in the neuronal growth cone
    • Sydor AM, Su AL, Wang FS, Xu A, Jay DG. 1996. Talin and vinculin play distinct roles in filopodial motility in the neuronal growth cone. J Cell Biol 134(5):1197-1207.
    • (1996) J Cell Biol , vol.134 , Issue.5 , pp. 1197-1207
    • Sydor, A.M.1    Su, A.L.2    Wang, F.S.3    Xu, A.4    Jay, D.G.5
  • 71
    • 0028984183 scopus 로고
    • A novel b1 integrin isoform produced by alternative splicing: Unique expression in cardiac and skeletal muscle
    • van der Flier A, Kuikman I, Baudoin C, van der Neut R, Sonnenberg A. 1995. A novel b1 integrin isoform produced by alternative splicing: Unique expression in cardiac and skeletal muscle. FEBS Lett 369:340-344.
    • (1995) FEBS Lett , vol.369 , pp. 340-344
    • van der Flier, A.1    Kuikman, I.2    Baudoin, C.3    van der Neut, R.4    Sonnenberg, A.5
  • 72
    • 3843052495 scopus 로고    scopus 로고
    • Comparitive biochemical analysis suggests that vinculin and metavinculin cooperate in muscular adhesion sites
    • Witte S, Zieseniss A, Fock U, Jockusch BM, Illenberger S. 2004. Comparitive biochemical analysis suggests that vinculin and metavinculin cooperate in muscular adhesion sites. J Biol Chem 279:31533-31543.
    • (2004) J Biol Chem , vol.279 , pp. 31533-31543
    • Witte, S.1    Zieseniss, A.2    Fock, U.3    Jockusch, B.M.4    Illenberger, S.5
  • 73
    • 0032820201 scopus 로고    scopus 로고
    • Domain analysis of supervillin, an F-actin bundling plasma membrane protein with functional nuclear localization signals
    • Wulfkuhle JD, Donina IE, Stark NH, Pope RK, Pestonjamasp KN, Niswonger ML, Luna EJ. 1999. Domain analysis of supervillin, an F-actin bundling plasma membrane protein with functional nuclear localization signals. J Cell Sci 112:2125-2136.
    • (1999) J Cell Sci , vol.112 , pp. 2125-2136
    • Wulfkuhle, J.D.1    Donina, I.E.2    Stark, N.H.3    Pope, R.K.4    Pestonjamasp, K.N.5    Niswonger, M.L.6    Luna, E.J.7
  • 74
    • 0017759258 scopus 로고
    • Serial passaging and differentiation of myogenic cells isolated from dystrophic mouse muscle
    • Yaffe D, Saxel O. 1977. Serial passaging and differentiation of myogenic cells isolated from dystrophic mouse muscle. Nature 270(5639):725-727.
    • (1977) Nature , vol.270 , Issue.5639 , pp. 725-727
    • Yaffe, D.1    Saxel, O.2
  • 75
    • 0035846582 scopus 로고    scopus 로고
    • Ultrastructural and biochemical localization of N-RAP at the interface between myofibrils and intercalated disks in the mouse heart
    • Zhang JQ, Elzey B, Williams G, Lu S, Law DJ, Horowits R. 2001. Ultrastructural and biochemical localization of N-RAP at the interface between myofibrils and intercalated disks in the mouse heart. Biochemistry 40(49):14898-14906.
    • (2001) Biochemistry , vol.40 , Issue.49 , pp. 14898-14906
    • Zhang, J.Q.1    Elzey, B.2    Williams, G.3    Lu, S.4    Law, D.J.5    Horowits, R.6
  • 76
    • 0942287279 scopus 로고    scopus 로고
    • Embryonic myogenesis pathways in muscle regeneration
    • Zhao P, Hoffman EP. 2004. Embryonic myogenesis pathways in muscle regeneration. Dev Dyn 229:380-392.
    • (2004) Dev Dyn , vol.229 , pp. 380-392
    • Zhao, P.1    Hoffman, E.P.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.