메뉴 건너뛰기




Volumn 164, Issue 4, 1998, Pages 341-348

The cytoskeleton of the vertebrate smooth muscle cell

Author keywords

Actin; Calponin; Cytoskeleton; Desmin; Intermediate filaments

Indexed keywords

ACTIN; CALPONIN; DESMIN;

EID: 0032446186     PISSN: 00016772     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1365-201X.1998.00441.x     Document Type: Conference Paper
Times cited : (162)

References (64)
  • 1
    • 0026540611 scopus 로고
    • Cultured aortic smooth muscle cells from newborn and adult rats show distinct cytoskeletal features
    • Bochaton-Piallat, M.L., Gabbiani, F., Ropraz, P. & Gabbiani, G. 1992. Cultured aortic smooth muscle cells from newborn and adult rats show distinct cytoskeletal features. Differentiation 49, 175-185.
    • (1992) Differentiation , vol.49 , pp. 175-185
    • Bochaton-Piallat, M.L.1    Gabbiani, F.2    Ropraz, P.3    Gabbiani, G.4
  • 2
    • 0028927536 scopus 로고
    • Computer-assistant prediction of phospholipid binding sites of caldesmon and calponin
    • Bogatcheva, N.V. & Gusev, N.B. 1995a. Computer-assistant prediction of phospholipid binding sites of caldesmon and calponin. FEBS Lett 363, 269-272.
    • (1995) FEBS Lett , vol.363 , pp. 269-272
    • Bogatcheva, N.V.1    Gusev, N.B.2
  • 3
    • 0029080918 scopus 로고
    • Interaction of smooth muscle calponin with phospholipids
    • Bogatcheva, N.V. & Gusev, N.B. 1995b. Interaction of smooth muscle calponin with phospholipids. FEBS Lett 371, 123-126.
    • (1995) FEBS Lett , vol.371 , pp. 123-126
    • Bogatcheva, N.V.1    Gusev, N.B.2
  • 4
    • 0020399066 scopus 로고
    • Dense bodies and actin polarity in vertebrate smooth muscle
    • Bond, M. & Somlyo, A.V. 1982. Dense bodies and actin polarity in vertebrate smooth muscle, J Cell Biol 95, 403-413.
    • (1982) J Cell Biol , vol.95 , pp. 403-413
    • Bond, M.1    Somlyo, A.V.2
  • 5
    • 0028785252 scopus 로고
    • Does Vav bind to F-actin through a CH domain?
    • Castresana, J. & Saraste, M. 1995. Does Vav bind to F-actin through a CH domain? FEBS Lett 374, 149-151.
    • (1995) FEBS Lett , vol.374 , pp. 149-151
    • Castresana, J.1    Saraste, M.2
  • 7
    • 0029995797 scopus 로고    scopus 로고
    • Rhostimulated contractility drives the formation of stress fibers and focal adhesions
    • Chrzanowska-Wodnicka, M. & Burridge, K. 1996. Rhostimulated contractility drives the formation of stress fibers and focal adhesions. J Cell Biol 133, 1403-1415.
    • (1996) J Cell Biol , vol.133 , pp. 1403-1415
    • Chrzanowska-Wodnicka, M.1    Burridge, K.2
  • 9
    • 0024829338 scopus 로고
    • Unique geometry of actin-membrane anchorage sites in avian gizzard smooth muscle cells
    • Draeger, A., Stelzer, E.H.K., Herzog, M. & Small, J.V. 1989. Unique geometry of actin-membrane anchorage sites in avian gizzard smooth muscle cells. J Cell Sci 94, 703-711.
    • (1989) J Cell Sci , vol.94 , pp. 703-711
    • Draeger, A.1    Stelzer, E.H.K.2    Herzog, M.3    Small, J.V.4
  • 10
    • 0031912140 scopus 로고    scopus 로고
    • Vimentin: The conundrum of the intermediate filament gene family
    • Evans, R.M. 1998. Vimentin: the conundrum of the intermediate filament gene family. BioEssays 20, 79-86.
    • (1998) BioEssays , vol.20 , pp. 79-86
    • Evans, R.M.1
  • 11
    • 0030003162 scopus 로고    scopus 로고
    • Acidic calponin cloned from neural cells is differentially expressed during rat brain development
    • Ferhat, L., Charton, G., Represa, A., Ben-Ari, Y., der Terrossian, K. & Khrestchatisky, M. 1996. Acidic calponin cloned from neural cells is differentially expressed during rat brain development. Eur J Neursci 8, 1501-1509.
    • (1996) Eur J Neursci , vol.8 , pp. 1501-1509
    • Ferhat, L.1    Charton, G.2    Represa, A.3    Ben-Ari, Y.4    Der Terrossian, K.5    Khrestchatisky, M.6
  • 12
    • 0345505811 scopus 로고
    • The intermediate filaments and associated proteins
    • T. Kreis & R. Vale (eds) Oxford University Press, Oxford
    • Franke, W.W. 1993. The intermediate filaments and associated proteins. In: T. Kreis & R. Vale (eds) Guidebook to the Cytoskeletal and Motor Proteins, pp. 137-143. Oxford University Press, Oxford.
    • (1993) Guidebook to the Cytoskeletal and Motor Proteins , pp. 137-143
    • Franke, W.W.1
  • 13
    • 0028287112 scopus 로고
    • Intermediate filaments and disease: Mutations that cripple cell strength
    • Fuchs, E. 1994. Intermediate filaments and disease: mutations that cripple cell strength. J Cell Biol 125, 511-516.
    • (1994) J Cell Biol , vol.125 , pp. 511-516
    • Fuchs, E.1
  • 14
    • 0030474645 scopus 로고    scopus 로고
    • The cytoskeleton and disease: Genetic disorders of intermediate filaments
    • Fuchs, E. 1996. The cytoskeleton and disease: genetic disorders of intermediate filaments. Annu Rev Genet 30, 197-231.
    • (1996) Annu Rev Genet , vol.30 , pp. 197-231
    • Fuchs, E.1
  • 15
    • 0027991511 scopus 로고
    • Calcium-dependent regulation of smooth muscle calponin by S100
    • Fujii, T., Oomatsuzawa, A., Kuzumaki, N. & Kondo, Y. 1994. Calcium-dependent regulation of smooth muscle calponin by S100. J Biochem 116, 121-127.
    • (1994) J Biochem , vol.116 , pp. 121-127
    • Fujii, T.1    Oomatsuzawa, A.2    Kuzumaki, N.3    Kondo, Y.4
  • 16
    • 0029070922 scopus 로고
    • Interaction of calponin with phospholipids
    • Fujii, T., Yamana, K., Ogoma, Y. & Kondo, Y. 1995. Interaction of calponin with phospholipids. J Biochem 117, 999-1003.
    • (1995) J Biochem , vol.117 , pp. 999-1003
    • Fujii, T.1    Yamana, K.2    Ogoma, Y.3    Kondo, Y.4
  • 18
    • 0024348057 scopus 로고
    • Myogenesis in the mouse embryo: Differential onset of expression of myogenic proteins and the involvement of titin in myofibril assembly
    • Fürst, D.O., Osborn, M. & Weber, K. 1989. Myogenesis in the mouse embryo: differential onset of expression of myogenic proteins and the involvement of titin in myofibril assembly. J Cell Biol 109, 517-527.
    • (1989) J Cell Biol , vol.109 , pp. 517-527
    • Fürst, D.O.1    Osborn, M.2    Weber, K.3
  • 20
    • 0031822886 scopus 로고    scopus 로고
    • The single CH domain of calponin is neither sufficient nor necessary for F-actin binding
    • in press
    • Gimona, M. & Mital, R. 1998. The single CH domain of calponin is neither sufficient nor necessary for F-actin binding. J Cell Sci 111, in press.
    • (1998) J Cell Sci , vol.111
    • Gimona, M.1    Mital, R.2
  • 22
    • 0027968795 scopus 로고
    • The Caenorhabditis elegans muscle-affecting gene unc-87 encodes novel thin filament-associated proteins
    • Goetinck, S. & Waterston, R.H. 1994a. The Caenorhabditis elegans muscle-affecting gene unc-87 encodes novel thin filament-associated proteins. J Cell Biol 127, 71-78.
    • (1994) J Cell Biol , vol.127 , pp. 71-78
    • Goetinck, S.1    Waterston, R.H.2
  • 23
    • 0027968795 scopus 로고
    • The Caenorhabditis elegans UNC-87 protein is essential for maintenance, but not assembly, of bodywall muscle
    • Goetinck, S. & Waterston, R.H. 1994b. The Caenorhabditis elegans UNC-87 protein is essential for maintenance, but not assembly, of bodywall muscle. J Cell Biol 127, 79-93.
    • (1994) J Cell Biol , vol.127 , pp. 79-93
    • Goetinck, S.1    Waterston, R.H.2
  • 24
    • 0032006027 scopus 로고    scopus 로고
    • Intermediate filaments and their associated proteins: Multiple dynamic personalities
    • Houseweart, M.K. & Cleveland, D.W. 1998. Intermediate filaments and their associated proteins: multiple dynamic personalities. Curr Opinion Cell Biol 10, 93-101.
    • (1998) Curr Opinion Cell Biol , vol.10 , pp. 93-101
    • Houseweart, M.K.1    Cleveland, D.W.2
  • 25
    • 0028108258 scopus 로고
    • Identification and characterization of an Onchocerca volvulus cDNA clone encoding a highly immunogenic calponin-like protein
    • Irvine, M., Huima, T., Prince, A.M. & Lustigman, S. 1994. Identification and characterization of an Onchocerca volvulus cDNA clone encoding a highly immunogenic calponin-like protein. Mol. Biochem. Parasitol 65, 135-146.
    • (1994) Mol Biochem Parasitol , vol.65 , pp. 135-146
    • Irvine, M.1    Huima, T.2    Prince, A.M.3    Lustigman, S.4
  • 26
    • 0029008415 scopus 로고
    • Calponin reduces shortening velocity in skinned taenia coli smooth muscle fibres
    • Jaworowski, A., Anderson, K.I., Arner, A. et al. 1995. Calponin reduces shortening velocity in skinned taenia coli smooth muscle fibres. FEBS Lett 365, 167-171.
    • (1995) FEBS Lett , vol.365 , pp. 167-171
    • Jaworowski, A.1    Anderson, K.I.2    Arner, A.3
  • 27
    • 0030880857 scopus 로고    scopus 로고
    • Adenovirus-mediated transfer of the smooth muscle cell calponin gene inhibits proliferation of smooth muscle cells and fibrobalsts
    • Jiang, Z., Grange, R.W., Walsh, M.P. & Kamm, K. E. 1997. Adenovirus-mediated transfer of the smooth muscle cell calponin gene inhibits proliferation of smooth muscle cells and fibrobalsts. FEBS Lett 413, 441-445.
    • (1997) FEBS Lett , vol.413 , pp. 441-445
    • Jiang, Z.1    Grange, R.W.2    Walsh, M.P.3    Kamm, K.E.4
  • 28
    • 0028967465 scopus 로고
    • Intermediate filaments: New proteins, some answers, more questions
    • Klymkowsky, M.W. 1995. Intermediate filaments: new proteins, some answers, more questions. Curr Opinion Cell Biol 7, 46-54.
    • (1995) Curr Opinion Cell Biol , vol.7 , pp. 46-54
    • Klymkowsky, M.W.1
  • 29
    • 0021711645 scopus 로고
    • Utrastructural localization of α-actinin and filamin in cultured cells with the immunogold staining (IGS) method
    • Langanger, G., de Mey, J., Moeremans, M., Daneels, G., de Brabander, M. & Small, J.V. 1984. Utrastructural localization of α-actinin and filamin in cultured cells with the immunogold staining (IGS) method. J Cell Biol 99, 1324-1334.
    • (1984) J Cell Biol , vol.99 , pp. 1324-1334
    • Langanger, G.1    De Mey, J.2    Moeremans, M.3    Daneels, G.4    De Brabander, M.5    Small, J.V.6
  • 30
    • 0030879081 scopus 로고    scopus 로고
    • Desmin is essential for the tensile strength and integrity of myofibrils but not for myogenic commitment, differentiation, and fusion of skeletal muscle
    • Li, Z., Mericskay, M., Agbulut, O., Butler-Browne, G. et al. 1997. Desmin is essential for the tensile strength and integrity of myofibrils but not for myogenic commitment, differentiation, and fusion of skeletal muscle. J Cell Biol 139, 129-144.
    • (1997) J Cell Biol , vol.139 , pp. 129-144
    • Li, Z.1    Mericskay, M.2    Agbulut, O.3    Butler-Browne, G.4
  • 31
    • 0029893923 scopus 로고    scopus 로고
    • Cardiovascular lesions and skeletal myopathy in mice lacking desmin
    • Li, Z., Colucci-Guyon, E., Pincon-Raymond, M. et al. 1996. Cardiovascular lesions and skeletal myopathy in mice lacking desmin. Der Biol 175, 362-366.
    • (1996) Der Biol , vol.175 , pp. 362-366
    • Li, Z.1    Colucci-Guyon, E.2    Pincon-Raymond, M.3
  • 32
    • 0030832240 scopus 로고    scopus 로고
    • Slow cycling of unphosphorylated myosin is inhibited by calponin, thus keeping smooth muscle relaxed
    • Malmqvist, U., Trybus, K.M., Yagi, S., Carmichael, J. & Fay, F.S. 1997. Slow cycling of unphosphorylated myosin is inhibited by calponin, thus keeping smooth muscle relaxed. Proc Natl Acad Sci USA 94 7655-7660.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 7655-7660
    • Malmqvist, U.1    Trybus, K.M.2    Yagi, S.3    Carmichael, J.4    Fay, F.S.5
  • 33
    • 0031468943 scopus 로고    scopus 로고
    • Echinococcus granulosus Myophilin-ralationship with protein homologues containing 'calponin-motifs'
    • Martin, R.M., Chilton, N.B., Lightowlers, M.W. & Gasser, R.B. Echinococcus granulosus Myophilin-ralationship with protein homologues containing 'calponin-motifs'. Intern J Parasitol 27, 1561-1567.
    • Intern J Parasitol , vol.27 , pp. 1561-1567
    • Martin, R.M.1    Chilton, N.B.2    Lightowlers, M.W.3    Gasser, R.B.4
  • 34
    • 0030868556 scopus 로고    scopus 로고
    • Calponin and mitogen-activated protein kinase signaling in differentiated vascular smooth muscle
    • Menice, C.B., Hulvershorn, J., Adam, L.P., Wang, C.-L.A. & Moragn, K.G. 1997. Calponin and mitogen-activated protein kinase signaling in differentiated vascular smooth muscle. J Biol Chem 272, 25157-25161.
    • (1997) J Biol Chem , vol.272 , pp. 25157-25161
    • Menice, C.B.1    Hulvershorn, J.2    Adam, L.P.3    Wang, C.-L.A.4    Moragn, K.G.5
  • 35
    • 0026780387 scopus 로고
    • Mapping of the functional domains in the amino-terminal region of calponin
    • Mezgueldi, M., Fattoum, A., Derancourt, J. & Kassab, R. 1992. Mapping of the functional domains in the Amino-terminal region of calponin. J Biol Chem 267, 15943-15951.
    • (1992) J Biol Chem , vol.267 , pp. 15943-15951
    • Mezgueldi, M.1    Fattoum, A.2    Derancourt, J.3    Kassab, R.4
  • 36
    • 0029878648 scopus 로고    scopus 로고
    • Expressing functional domains of mouse calponin: Involvement of the region around alanine 145 in the actomyosin ATPase inhibitory activity of calponin
    • Mezgueldi, M., Strasser, P., Fattoum, A. & Gimona, M. 1996. Expressing functional domains of mouse calponin: involvement of the region around alanine 145 in the actomyosin ATPase inhibitory activity of calponin. Biochem 35, 3654-3661.
    • (1996) Biochem , vol.35 , pp. 3654-3661
    • Mezgueldi, M.1    Strasser, P.2    Fattoum, A.3    Gimona, M.4
  • 37
    • 0029738727 scopus 로고    scopus 로고
    • Disruption of muscle architeclure and myocardial degeneration in mice lacking desmin
    • Milner, D.J., Weitzer, G., Tran, D., Bradley, A. & Capetanaki, Y. 1996. Disruption of muscle architeclure and myocardial degeneration in mice lacking desmin. J Cell Biol 134, 1255-1270.
    • (1996) J Cell Biol , vol.134 , pp. 1255-1270
    • Milner, D.J.1    Weitzer, G.2    Tran, D.3    Bradley, A.4    Capetanaki, Y.5
  • 38
    • 0032518319 scopus 로고    scopus 로고
    • Two distinct actin-binding sites of smooth muscle calponin
    • Mino, T., Yuasa, U., Nakamura, F., Naka, M. & Tanaka, T. 1998. Two distinct actin-binding sites of smooth muscle calponin. Eur J Biochem 251, 262-268.
    • (1998) Eur J Biochem , vol.251 , pp. 262-268
    • Mino, T.1    Yuasa, U.2    Nakamura, F.3    Naka, M.4    Tanaka, T.5
  • 39
    • 0027476106 scopus 로고
    • Complementary distributions of vinculin and dystrophin define two distinct sarcolemma domains in smooth muscle
    • North, A., Galazkiewicz, B., Byers, T.J., Glenney, J.R. & Small, J.V. 1993. Complementary distributions of vinculin and dystrophin define two distinct sarcolemma domains in smooth muscle. J Cell Biol 120, 1159-1167.
    • (1993) J Cell Biol , vol.120 , pp. 1159-1167
    • North, A.1    Galazkiewicz, B.2    Byers, T.J.3    Glenney, J.R.4    Small, J.V.5
  • 40
    • 0028196621 scopus 로고
    • Actin isoform compartments in chicken gizzard smooth muscle cells
    • North, A.J., Gimona, M., Lando, Z. & Small, J.V. 1994. Actin isoform compartments in chicken gizzard smooth muscle cells. J Cell Sci 107, 445-455.
    • (1994) J Cell Sci , vol.107 , pp. 445-455
    • North, A.J.1    Gimona, M.2    Lando, Z.3    Small, J.V.4
  • 41
    • 0019835206 scopus 로고
    • Heterogeneity of intermediate filament expression in vascular smooth muscle: A gradient in desmin positive cells from the rat aortic arch to the level of the arteria iliaca communis
    • Osborn, M., Caselitz, J. & Weber, K. 1981. Heterogeneity of intermediate filament expression in vascular smooth muscle: a gradient in desmin positive cells from the rat aortic arch to the level of the arteria iliaca communis. Differentiation 20, 196-202.
    • (1981) Differentiation , vol.20 , pp. 196-202
    • Osborn, M.1    Caselitz, J.2    Weber, K.3
  • 42
    • 0028057169 scopus 로고
    • Agonist-induced redistribution of calponin in contractile vascular smooth muscle cells
    • Parker, C.A., Takahashi, K., Tao, T. & Morgan, K. G. 1994. Agonist-induced redistribution of calponin in contractile vascular smooth muscle cells. Am J Physiol 267, C1262-C1270.
    • (1994) Am J Physiol , vol.267
    • Parker, C.A.1    Takahashi, K.2    Tao, T.3    Morgan, K.G.4
  • 44
    • 0021994415 scopus 로고
    • Geometry of actin-membrane attachments in the smooth muscle cell: The localisations of vinculin and x-actinin
    • Small, J.V. 1985. Geometry of actin-membrane attachments in the smooth muscle cell: the localisations of vinculin and x-actinin. EMBO J 4, 45-49.
    • (1985) EMBO J , vol.4 , pp. 45-49
    • Small, J.V.1
  • 45
    • 0029360691 scopus 로고
    • Structure-function relationships in smooth muscle: The missing links
    • Small, J.V. 1995. Structure-function relationships in smooth muscle: the missing links. Biol Essays 17, 785-792.
    • (1995) Biol Essays , vol.17 , pp. 785-792
    • Small, J.V.1
  • 46
  • 47
    • 0025640819 scopus 로고
    • Supercontracted state of vertebrate smooth muscle cell fragements reveals myofilament lengths
    • Small, J.V., Fürst, M., Barth, M. & Draeger, A. 1990. Supercontracted state of vertebrate smooth muscle cell fragements reveals myofilament lengths. J Cell Biol 111, 2451-2461.
    • (1990) J Cell Biol , vol.111 , pp. 2451-2461
    • Small, J.V.1    Fürst, M.2    Barth, M.3    Draeger, A.4
  • 48
    • 0011829864 scopus 로고
    • Architecture of the smooth muscle cell
    • S.M. Schwartz & R-P. Machem (eds) Academic Press, San Diego
    • Small, J.V. & North, A.J. 1995. Architecture of the smooth muscle cell. In: S.M. Schwartz & R-P. Machem (eds) Vascular Smooth Muscle Cell, pp. 169-185. Academic Press, San Diego.
    • (1995) Vascular Smooth Muscle Cell , pp. 169-185
    • Small, J.V.1    North, A.J.2
  • 49
    • 0017366003 scopus 로고
    • Studies on the function and composition of the 10-nm (100 A) filaments of vertebrate smooth muscle
    • Small, J.V. & Sobieszek, A. 1977. Studies on the function and composition of the 10-nm (100 A) filaments of vertebrate smooth muscle. J Cell Sci 25, 243-268.
    • (1977) J Cell Sci , vol.25 , pp. 243-268
    • Small, J.V.1    Sobieszek, A.2
  • 52
    • 0000067990 scopus 로고    scopus 로고
    • Targeted disruption of calponin results in rapid cross-bridge cycling and reduced force in phasic smooth muscle
    • Takahashi, K., Mitsui-Saito, M., Fuchibe, K. et al. 1998. Targeted disruption of calponin results in rapid cross-bridge cycling and reduced force in phasic smooth muscle. Biophys J 74, A38.
    • (1998) Biophys J , vol.74
    • Takahashi, K.1    Mitsui-Saito, M.2    Fuchibe, K.3
  • 53
    • 0025879757 scopus 로고
    • Molecular cloning and sequence analysis of smooth muscle calponin
    • Takahashi, K. & Nadal-Ginard, B. 1991. Molecular cloning and sequence analysis of smooth muscle calponin. J Biol Chem 266, 13284-13288.
    • (1991) J Biol Chem , vol.266 , pp. 13284-13288
    • Takahashi, K.1    Nadal-Ginard, B.2
  • 56
    • 0020569947 scopus 로고
    • Association of actin and 10 nm filaments with the dense body in smooth muscle cells of the chicken gizzard
    • Tsukita, S., Tsukita, S. & Ishikawa, H. 1983. Association of actin and 10 nm filaments with the dense body in smooth muscle cells of the chicken gizzard. Cell Tissue Res 229, 223-242.
    • (1983) Cell Tissue Res , vol.229 , pp. 223-242
    • Tsukita, S.1    Tsukita, S.2    Ishikawa, H.3
  • 57
    • 1842301116 scopus 로고    scopus 로고
    • Smoothelin expression characteristics: Development of smooth muscle cell in vitro system and identification of a vascular variant
    • Van Eys, G.J.J.M., Völler, M.C.W., Timmer, E.D. J. et al. 1997. Smoothelin expression characteristics: development of smooth muscle cell in vitro system and identification of a vascular variant. Cell Structure Function 22, 65-72.
    • (1997) Cell Structure Function , vol.22 , pp. 65-72
    • Van Eys, G.J.J.M.1    Völler, M.C.W.2    Timmer, E.D.J.3
  • 58
    • 0028818253 scopus 로고
    • Myosin II filament assemblies in the active lamella of fibroblasts: Their morphogenesis and role in the formation of actin filament bundles
    • Verkhovsky, A.B., Svitkina, T.M. & Bonrisy, G.G. 1995. Myosin II filament assemblies in the active lamella of fibroblasts: their morphogenesis and role in the formation of actin filament bundles. J Cell Biol 131, 989-1002.
    • (1995) J Cell Biol , vol.131 , pp. 989-1002
    • Verkhovsky, A.B.1    Svitkina, T.M.2    Bonrisy, G.G.3
  • 59
    • 0027134999 scopus 로고
    • Characterization and confocal imaging of calponin in gastrointestinal smooth muscle
    • Walsh, M.P., Carmichael, J.D. & Kargacin, G.G. 1993. Characterization and confocal imaging of calponin in gastrointestinal smooth muscle. Am J Physiol 265, C1371-C1378.
    • (1993) Am J Physiol , vol.265
    • Walsh, M.P.1    Carmichael, J.D.2    Kargacin, G.G.3
  • 60
    • 0039154943 scopus 로고
    • Filamin, a new high-molecular-weight protein found in smooth muscle and non-muscle cells
    • Wang, K., Ash, J.F. & Singer, S.J. 1975. Filamin, a new high-molecular-weight protein found in smooth muscle and non-muscle cells. Proc Natl Acad Sci USA 72, 4483-4486.
    • (1975) Proc Natl Acad Sci USA , vol.72 , pp. 4483-4486
    • Wang, K.1    Ash, J.F.2    Singer, S.J.3
  • 61
    • 0028584314 scopus 로고
    • Two domains of interaction with calcium binding proteins can be mapped using fragments of calponin
    • Wills, F.L., McCubbin, W.D., Gimona, M., Strasser, P. & Kay, C.M. 1994. Two domains of interaction with calcium binding proteins can be mapped using fragments of calponin. Protein Sci 3, 2311-2321.
    • (1994) Protein Sci , vol.3 , pp. 2311-2321
    • Wills, F.L.1    McCubbin, W.D.2    Gimona, M.3    Strasser, P.4    Kay, C.M.5
  • 62
    • 0027536846 scopus 로고
    • Characterization of the smooth muscle calponin and calmodulin complex
    • Wills, F.L., McCubbin, W.D. & Kay, C.M. 1993. Characterization of the smooth muscle calponin and calmodulin complex. Biochem 32, 2321-2328.
    • (1993) Biochem , vol.32 , pp. 2321-2328
    • Wills, F.L.1    McCubbin, W.D.2    Kay, C.M.3
  • 64
    • 0032550177 scopus 로고    scopus 로고
    • Rho-mediated contractility exposes a cryptic site in fibronectin and induces fibronectin matrix assembly
    • Zhong, C., Chrzanowska-Wodnicka, M., Brown, J., Shaub, A., Belkin, A.M. & Burridge, K. 1998. Rho-mediated contractility exposes a cryptic site in fibronectin and induces fibronectin matrix assembly. J Cell Biol 141, 539-551.
    • (1998) J Cell Biol , vol.141 , pp. 539-551
    • Zhong, C.1    Chrzanowska-Wodnicka, M.2    Brown, J.3    Shaub, A.4    Belkin, A.M.5    Burridge, K.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.