메뉴 건너뛰기




Volumn 19, Issue 3, 2000, Pages 191-201

Cell-cell adhesion via the ECM: Integrin genetics in fly and worm

Author keywords

C. elegans; Cell adhesion; Drosophila; Extracellular matrix; Integrin

Indexed keywords

INTEGRIN; LAMININ;

EID: 0034233543     PISSN: 0945053X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0945-053X(00)00064-0     Document Type: Short Survey
Times cited : (105)

References (66)
  • 2
    • 0025824367 scopus 로고
    • Vinculin is essential for muscle function in the nematode
    • Barstead R.J., Waterston R.H. Vinculin is essential for muscle function in the nematode. J. Cell Biol. 114:1991;715-724.
    • (1991) J. Cell Biol. , vol.114 , pp. 715-724
    • Barstead, R.J.1    Waterston, R.H.2
  • 3
    • 0030762006 scopus 로고    scopus 로고
    • Neuronal migrations and axon fasciculation are disrupted in ina-1 integrin mutants
    • Baum P.D., Garriga G. Neuronal migrations and axon fasciculation are disrupted in ina-1 integrin mutants. Neuron. 19:1997;51-62.
    • (1997) Neuron , vol.19 , pp. 51-62
    • Baum, P.D.1    Garriga, G.2
  • 4
    • 0033398831 scopus 로고    scopus 로고
    • A role for PS integrins in morphological growth and synaptic function at the postembryonic neuromuscular junction of Drosophila
    • Beumer K., Rohrbough J., Prokop A., Broadie K. A role for PS integrins in morphological growth and synaptic function at the postembryonic neuromuscular junction of Drosophila. Development. 126:1999;5833-5846.
    • (1999) Development , vol.126 , pp. 5833-5846
    • Beumer, K.1    Rohrbough, J.2    Prokop, A.3    Broadie, K.4
  • 5
    • 0031961418 scopus 로고    scopus 로고
    • pS2 integrin subunit reveals discrete adhesive, morphogenetic and sarcomeric functions
    • PS2 integrin subunit reveals discrete adhesive, morphogenetic and sarcomeric functions. Genetics. 148:1998;1127-1142.
    • (1998) Genetics , vol.148 , pp. 1127-1142
    • Bloor, J.W.1    Brown, N.H.2
  • 6
    • 0023663872 scopus 로고
    • The Drosophila PS2 antigen is an invertebrate integrin that, like the fibronectin receptor, becomes localized to muscle attachments
    • Bogaert T., Brown N., Wilcox M. The Drosophila PS2 antigen is an invertebrate integrin that, like the fibronectin receptor, becomes localized to muscle attachments. Cell. 51:1987;929-940.
    • (1987) Cell , vol.51 , pp. 929-940
    • Bogaert, T.1    Brown, N.2    Wilcox, M.3
  • 7
    • 0030219918 scopus 로고    scopus 로고
    • The function of type IV collagen during Drosophila muscle development
    • Borchiellini C., Coulon L., Le Parco Y. The function of type IV collagen during Drosophila muscle development. Mech. Dev. 58:1996;179-191.
    • (1996) Mech. Dev. , vol.58 , pp. 179-191
    • Borchiellini, C.1    Coulon, L.2    Le Parco, Y.3
  • 8
    • 0027262541 scopus 로고
    • PS2 integrin requirements in Drosophila embryo and wing morphogenesis
    • Brabant M.C., Brower D.L. PS2 integrin requirements in Drosophila embryo and wing morphogenesis. Dev. Biol. 157:1993;49-59.
    • (1993) Dev. Biol. , vol.157 , pp. 49-59
    • Brabant, M.C.1    Brower, D.L.2
  • 9
    • 0029850115 scopus 로고    scopus 로고
    • Distinct spatial and temporal functions for PS integrins during Drosophila wing morphogenesis
    • Brabant M.C., Fristrom D., Bunch T.A., Brower D.L. Distinct spatial and temporal functions for PS integrins during Drosophila wing morphogenesis. Development. 122:1996;3307-3317.
    • (1996) Development , vol.122 , pp. 3307-3317
    • Brabant, M.C.1    Fristrom, D.2    Bunch, T.A.3    Brower, D.L.4
  • 10
    • 0031787977 scopus 로고    scopus 로고
    • The PS integrins are required for a regulatory event during Drosophila wing morphogenesis
    • Brabant M.C., Fristrom D., Bunch T.A., Baker S.E., Brower D.L. The PS integrins are required for a regulatory event during Drosophila wing morphogenesis. Ann. N.Y. Acad. Sci. 857:1998;99-109.
    • (1998) Ann. N.Y. Acad. Sci. , vol.857 , pp. 99-109
    • Brabant, M.C.1    Fristrom, D.2    Bunch, T.A.3    Baker, S.E.4    Brower, D.L.5
  • 12
    • 0030740244 scopus 로고    scopus 로고
    • Molecular evolution of integrins: Genes encoding integrin β subunits form a coral and a sponge
    • Brower D.L., Brower S.M., Hayward D.C., Ball E.E. Molecular evolution of integrins: genes encoding integrin β subunits form a coral and a sponge. Proc. Natl. Acad. Sci. U.S.A. 94:1997;9182-9187.
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 9182-9187
    • Brower, D.L.1    Brower, S.M.2    Hayward, D.C.3    Ball, E.E.4
  • 13
    • 0027619559 scopus 로고
    • Integrins hold Drosophila together
    • Brown N.H. Integrins hold Drosophila together. BioEssays. 15:1993;383-390.
    • (1993) BioEssays , vol.15 , pp. 383-390
    • Brown, N.H.1
  • 14
    • 0028173625 scopus 로고
    • pS integrin subunit genes have distinct phenotypes
    • PS integrin subunit genes have distinct phenotypes. Development. 120:1994;1221-1231.
    • (1994) Development , vol.120 , pp. 1221-1231
    • Brown, N.H.1
  • 15
    • 0031803665 scopus 로고    scopus 로고
    • The PS2 integrin ligand tiggrin is required for proper muscle function in Drosophila
    • Bunch T.A., Graner M.W., Fessler L.I. et al. The PS2 integrin ligand tiggrin is required for proper muscle function in Drosophila. Development. 125:1998;1679-1689.
    • (1998) Development , vol.125 , pp. 1679-1689
    • Bunch, T.A.1    Graner, M.W.2    Fessler, L.I.3
  • 16
    • 0032509302 scopus 로고    scopus 로고
    • Genome sequence of the nematode C. elegans: A platform for investigating biology
    • Genome sequence of the nematode C. elegans: a platform for investigating biology. Science. 282:1998;2012-2018.
    • (1998) Science , vol.282 , pp. 2012-2018
  • 19
    • 0022345717 scopus 로고
    • Muscle organization in Caenorhabditis elegans: Localization of proteins implicated in thin filament attachment and I-band organization
    • Francis G.R., Waterston R.H. Muscle organization in Caenorhabditis elegans: localization of proteins implicated in thin filament attachment and I-band organization. J. Cell Biol. 101:1985;1532-1549.
    • (1985) J. Cell Biol. , vol.101 , pp. 1532-1549
    • Francis, G.R.1    Waterston, R.H.2
  • 20
    • 0025734406 scopus 로고
    • Muscle cell attachment in Caenorhabditis elegans
    • Francis G.R., Waterston R.H. Muscle cell attachment in Caenorhabditis elegans. J. Cell Biol. 114:1991;465-479.
    • (1991) J. Cell Biol. , vol.114 , pp. 465-479
    • Francis, G.R.1    Waterston, R.H.2
  • 21
    • 0028990430 scopus 로고
    • Characterization of βpat-3 heterodimers, a family of essential integrin receptors in C. elegans
    • Gettner S.N., Kenyon C., Reichardt L.F. Characterization of βpat-3 heterodimers, a family of essential integrin receptors in C. elegans. J. Cell Biol. 129:1995;1127-1141.
    • (1995) J. Cell Biol. , vol.129 , pp. 1127-1141
    • Gettner, S.N.1    Kenyon, C.2    Reichardt, L.F.3
  • 22
    • 0033551899 scopus 로고    scopus 로고
    • Integrin signaling
    • Giancotti F., Ruoslahti E. Integrin signaling. Science. 285:1999;1028-1032.
    • (1999) Science , vol.285 , pp. 1028-1032
    • Giancotti, F.1    Ruoslahti, E.2
  • 23
    • 0027986667 scopus 로고
    • Drosophila PS1 integrin is a laminin receptor and differs in ligand specificity from PS2
    • Gotwals P.J., Fessler L.I., Wehril M., Hynes R.O. Drosophila PS1 integrin is a laminin receptor and differs in ligand specificity from PS2. Proc. Natl. Acad. Sci. 91:1994;11447-11451.
    • (1994) Proc. Natl. Acad. Sci. , vol.91 , pp. 11447-11451
    • Gotwals, P.J.1    Fessler, L.I.2    Wehril, M.3    Hynes, R.O.4
  • 25
    • 0030989696 scopus 로고    scopus 로고
    • Type IV collagen is detectable in most, but not all, basement membranes of Caenorhabditis elegans and assembles on tissues that do not express it
    • Graham P.L., Johnson J.J., Wang S.R., Sibley M.H., Gupta M.C., Kramer J.M. Type IV collagen is detectable in most, but not all, basement membranes of Caenorhabditis elegans and assembles on tissues that do not express it. J. Cell Biol. 137:1997;1171-1183.
    • (1997) J. Cell Biol. , vol.137 , pp. 1171-1183
    • Graham, P.L.1    Johnson, J.J.2    Wang, S.R.3    Sibley, M.H.4    Gupta, M.C.5    Kramer, J.M.6
  • 26
    • 0032541043 scopus 로고    scopus 로고
    • Splice variants of the Drosophila PS2 integrins differentially interact with RGD-containing fragments of the extracellular proteins tiggrin, ten-m, and D-laminin 2
    • Graner M.W., Bunch T.A., Baumgartner S., Kerschen A., Brower D.L. Splice variants of the Drosophila PS2 integrins differentially interact with RGD-containing fragments of the extracellular proteins tiggrin, ten-m, and D-laminin 2. J. Biol. Chem. 273:1998;18235-18241.
    • (1998) J. Biol. Chem. , vol.273 , pp. 18235-18241
    • Graner, M.W.1    Bunch, T.A.2    Baumgartner, S.3    Kerschen, A.4    Brower, D.L.5
  • 27
    • 0032583124 scopus 로고    scopus 로고
    • Kakapo, a gene required for adhesion between and within cell layers in Drosophila, encodes a large cytoskeletal linker protein related to plectin and dystrophin
    • Gregory S.L., Brown N.H. kakapo, a gene required for adhesion between and within cell layers in Drosophila, encodes a large cytoskeletal linker protein related to plectin and dystrophin. J. Cell Biol. 143:1998;1271-1282.
    • (1998) J. Cell Biol. , vol.143 , pp. 1271-1282
    • Gregory, S.L.1    Brown, N.H.2
  • 29
    • 0031696484 scopus 로고    scopus 로고
    • Mouse myoblasts can fuse and form a normal sarcomere in the absence of betal integrin expression
    • Hirsch E., Lohikangas L., Gullberg D., Johansson S., Fassler R. Mouse myoblasts can fuse and form a normal sarcomere in the absence of betal integrin expression. J. Cell Sci. 111:1998;2397-2409.
    • (1998) J. Cell Sci. , vol.111 , pp. 2397-2409
    • Hirsch, E.1    Lohikangas, L.2    Gullberg, D.3    Johansson, S.4    Fassler, R.5
  • 30
    • 0032189545 scopus 로고    scopus 로고
    • Genetic analysis on the role of integrin during axon guidance in Drosophila
    • Hoang B., Chiba A. Genetic analysis on the role of integrin during axon guidance in Drosophila. J. Neurosci. 18:1998;7847-7855.
    • (1998) J. Neurosci. , vol.18 , pp. 7847-7855
    • Hoang, B.1    Chiba, A.2
  • 31
    • 0033545214 scopus 로고    scopus 로고
    • A conserved LIM protein that affects muscular adherens junction integrity and mechanosensory function in Caenorhabditis elegans
    • Hobert O., Moerman D.G., Clark K.A., Beckerle M.C., Ruvkin G. A conserved LIM protein that affects muscular adherens junction integrity and mechanosensory function in Caenorhabditis elegans. J. Cell Biol. 144:1999;45-57.
    • (1999) J. Cell Biol. , vol.144 , pp. 45-57
    • Hobert, O.1    Moerman, D.G.2    Clark, K.A.3    Beckerle, M.C.4    Ruvkin, G.5
  • 32
    • 0028055026 scopus 로고
    • Assembly of body wall muscle and muscle cell attachment structures in Caenorhabditis elegans
    • Hresko M.C., Williams B.D., Waterston R.H. Assembly of body wall muscle and muscle cell attachment structures in Caenorhabditis elegans. J. Cell Biol. 124:1994;491-506.
    • (1994) J. Cell Biol. , vol.124 , pp. 491-506
    • Hresko, M.C.1    Williams, B.D.2    Waterston, R.H.3
  • 33
    • 0033538845 scopus 로고    scopus 로고
    • Myotactin, a novel hpodermal protein involved in muscle-cell adhesion in Caenorhabditis elegans
    • Hresko M.C., Schriefer L.A., Shrimankar P., Waterston R.H. Myotactin, a novel hpodermal protein involved in muscle-cell adhesion in Caenorhabditis elegans. J. Cell Biol. 146:1999;659-672.
    • (1999) J. Cell Biol. , vol.146 , pp. 659-672
    • Hresko, M.C.1    Schriefer, L.A.2    Shrimankar, P.3    Waterston, R.H.4
  • 34
    • 0033552634 scopus 로고    scopus 로고
    • Microtubule actin cross-linking factor (MACF): A hybrid of dystonin and dystrophin that can interact with the actin and microtubule cytoskeletons
    • Leung C.L., Sun D., Zheng M., Knowles D.R., Liem R.K.H. Microtubule actin cross-linking factor (MACF): a hybrid of dystonin and dystrophin that can interact with the actin and microtubule cytoskeletons. J. Cell Biol. 147:1999;1275-1285.
    • (1999) J. Cell Biol. , vol.147 , pp. 1275-1285
    • Leung, C.L.1    Sun, D.2    Zheng, M.3    Knowles, D.R.4    Liem, R.K.H.5
  • 35
    • 0033526047 scopus 로고    scopus 로고
    • Wing blister, a new Drosophila laminin alpha chain required for cell adhesion and migration during embryonic and imaginal development
    • Martin D., Zusman S., Li X. et al. wing blister, a new Drosophila laminin alpha chain required for cell adhesion and migration during embryonic and imaginal development. J. Cell Biol. 145:1999;191-201.
    • (1999) J. Cell Biol. , vol.145 , pp. 191-201
    • Martin, D.1    Zusman, S.2    Li, X.3
  • 36
    • 0029959355 scopus 로고    scopus 로고
    • Intracellular signals direct integrin localization to sites of function in embryonic muscles
    • Martin-Bermudo M.D., Brown N.H. Intracellular signals direct integrin localization to sites of function in embryonic muscles. J. Cell. Biol. 134:1996;217-226.
    • (1996) J. Cell. Biol. , vol.134 , pp. 217-226
    • Martin-Bermudo, M.D.1    Brown, N.H.2
  • 37
    • 0033558941 scopus 로고    scopus 로고
    • pS cytoplasmic domain is sufficient to regulate gene expression in the Drosophila embryo
    • PS cytoplasmic domain is sufficient to regulate gene expression in the Drosophila embryo. Genes Dev. 13:1999;729-739.
    • (1999) Genes Dev. , vol.13 , pp. 729-739
    • Martin-Bermudo, M.D.1    Brown, N.H.2
  • 38
    • 0030752303 scopus 로고    scopus 로고
    • Specificity of PS integrin function during embryogenesis resides in the α subunit extracellular domain
    • Martin-Bermudo M.D., Dunin-Borkowski O.M., Brown N.H. Specificity of PS integrin function during embryogenesis resides in the α subunit extracellular domain. EMBO. 16:1997;4184-4193.
    • (1997) EMBO , vol.16 , pp. 4184-4193
    • Martin-Bermudo, M.D.1    Dunin-Borkowski, O.M.2    Brown, N.H.3
  • 39
    • 0033430250 scopus 로고    scopus 로고
    • Migration of the Drosophila primordial midgut cells requires coordination of diverse PS integrin functions
    • Martin-Bermudo M.D., Alvarez-Garcia I., Brown N.H. Migration of the Drosophila primordial midgut cells requires coordination of diverse PS integrin functions. Development. 126:1999;5161-5169.
    • (1999) Development , vol.126 , pp. 5161-5169
    • Martin-Bermudo, M.D.1    Alvarez-Garcia, I.2    Brown, N.H.3
  • 40
    • 0030724952 scopus 로고    scopus 로고
    • Absence of integrin alpha 7 causes a novel form of muscular dystrophy
    • Mayer U., Saher G., Fassler R. et al. Absence of integrin alpha 7 causes a novel form of muscular dystrophy. Nat. Genet. 17:1997;318-323.
    • (1997) Nat. Genet. , vol.17 , pp. 318-323
    • Mayer, U.1    Saher, G.2    Fassler, R.3
  • 41
    • 0030063741 scopus 로고    scopus 로고
    • Cell autonomous expression of perlecan and plasticity of cell shape in embryonic muscle of Caenorhabditis elegans
    • Moerman D.G., Hutter H., Mullen G.P., Schnabel R. Cell autonomous expression of perlecan and plasticity of cell shape in embryonic muscle of Caenorhabditis elegans. Dev. Biol. 173:1996;228-242.
    • (1996) Dev. Biol. , vol.173 , pp. 228-242
    • Moerman, D.G.1    Hutter, H.2    Mullen, G.P.3    Schnabel, R.4
  • 42
    • 0029741101 scopus 로고    scopus 로고
    • Talin requires β-integrin, but not vinculin, for its assembly into focal adhesion-like structures in the nematode Caenorhabditis elegans
    • Moulder G.L., Huang M.M., Waterston R.H., Barstead R.J. Talin requires β-integrin, but not vinculin, for its assembly into focal adhesion-like structures in the nematode Caenorhabditis elegans. Mol. Biol. Cell. 7:1996;1181-1193.
    • (1996) Mol. Biol. Cell , vol.7 , pp. 1181-1193
    • Moulder, G.L.1    Huang, M.M.2    Waterston, R.H.3    Barstead, R.J.4
  • 44
    • 0033595691 scopus 로고    scopus 로고
    • Molecular cloning of macrophin, a human homologue of Drosophila kakapo with a close structural similarity to plectin and dystrophin
    • Okuda T., Matsuda S., Nakatsugawa S. et al. Molecular cloning of macrophin, a human homologue of Drosophila kakapo with a close structural similarity to plectin and dystrophin. Biochem Biophys Res Commun. 264:1999;568-574.
    • (1999) Biochem Biophys Res Commun , vol.264 , pp. 568-574
    • Okuda, T.1    Matsuda, S.2    Nakatsugawa, S.3
  • 45
    • 0345055334 scopus 로고    scopus 로고
    • In Drosophila embryos, the absence of the PS integrins or laminin A affects the extracellular adhesion of hemiadherens and neuromuscular junctions, but not their intracellular assembly
    • Prokop A., Martin-Bermudo M.D., Bate M., Brown N.H. In Drosophila embryos, the absence of the PS integrins or laminin A affects the extracellular adhesion of hemiadherens and neuromuscular junctions, but not their intracellular assembly. Dev. Biol. 196:1998;58-76.
    • (1998) Dev. Biol. , vol.196 , pp. 58-76
    • Prokop, A.1    Martin-Bermudo, M.D.2    Bate, M.3    Brown, N.H.4
  • 46
    • 0032583166 scopus 로고    scopus 로고
    • The kakapo mutation affects terminal arborization and central dendritic sprouting of Drosophila motorneurons
    • Prokop A., Uhler J., Roote L., Bate M. The kakapo mutation affects terminal arborization and central dendritic sprouting of Drosophila motorneurons. J. Cell Biol. 143:1998;1283-1294.
    • (1998) J. Cell Biol. , vol.143 , pp. 1283-1294
    • Prokop, A.1    Uhler, J.2    Roote, L.3    Bate, M.4
  • 47
    • 0030978261 scopus 로고    scopus 로고
    • Autosomal mutations affecting adhesion between wing surfaces in Drosophila melanogaster
    • Prout M., Damania Z., Soong J., Fristrom D., Fristrom J.W. Autosomal mutations affecting adhesion between wing surfaces in Drosophila melanogaster. Genetics. 146:1997;275-285.
    • (1997) Genetics , vol.146 , pp. 275-285
    • Prout, M.1    Damania, Z.2    Soong, J.3    Fristrom, D.4    Fristrom, J.W.5
  • 48
    • 0027965633 scopus 로고
    • Homology of the eyeless gene of Drosophila to the Small eye gene in mice and Aniridia in humans
    • Quiring R., Walldorf U., Kloter U., Gehring W.J. Homology of the eyeless gene of Drosophila to the Small eye gene in mice and Aniridia in humans. Science. 265:1994;785-789.
    • (1994) Science , vol.265 , pp. 785-789
    • Quiring, R.1    Walldorf, U.2    Kloter, U.3    Gehring, W.J.4
  • 49
    • 0027325671 scopus 로고
    • Products of the unc-52 gene in Caenorhabditis elegans are homologous to the core protein of the mammalian basement membrane heparin sulfate proteoglycan
    • Rogalski T.M., Williams B.D., Mullen G.P., Moerman D.G. Products of the unc-52 gene in Caenorhabditis elegans are homologous to the core protein of the mammalian basement membrane heparin sulfate proteoglycan. Genes Dev. 7:1993;1471-1484.
    • (1993) Genes Dev. , vol.7 , pp. 1471-1484
    • Rogalski, T.M.1    Williams, B.D.2    Mullen, G.P.3    Moerman, D.G.4
  • 50
    • 0029032944 scopus 로고
    • Functions for PS integrins in tissue adhesion, migration, and shape changes during early embryonic development in Drosophila
    • Roote C.E., Zusman S. Functions for PS integrins in tissue adhesion, migration, and shape changes during early embryonic development in Drosophila. Dev. Biol. 169:1995;322-336.
    • (1995) Dev. Biol. , vol.169 , pp. 322-336
    • Roote, C.E.1    Zusman, S.2
  • 51
    • 0029955198 scopus 로고    scopus 로고
    • Alternatively spliced forms of the Drosophila αpS2 subunit of integrin are sufficient for viability and can replace the function of the αpSI subunit of integrin in the retina
    • Roote C.E., Zusman S. Alternatively spliced forms of the Drosophila αPS2 subunit of integrin are sufficient for viability and can replace the function of the αPSI subunit of integrin in the retina. Development. 122:1996;1985-1994.
    • (1996) Development , vol.122 , pp. 1985-1994
    • Roote, C.E.1    Zusman, S.2
  • 53
    • 0031013031 scopus 로고    scopus 로고
    • Folding of the N-terminal, ligand-binding region of integrin alpha subunits into a beta-propeller domain
    • Springer T.A. Folding of the N-terminal, ligand-binding region of integrin alpha subunits into a beta-propeller domain. Proc. Natl. Acad. Sci. U.S.A. 94:1997;65-72.
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 65-72
    • Springer, T.A.1
  • 54
    • 0030687614 scopus 로고    scopus 로고
    • A novel α integrin subunit associates with βpS and functions in tissue morphogenesis and movement during Drosophila development
    • Stark K.A., Yee G.H., Roote C.E., Williams E.L., Zusman S., Hynes R.O. A novel α integrin subunit associates with βPS and functions in tissue morphogenesis and movement during Drosophila development. Development. 124:1997;4583-4594.
    • (1997) Development , vol.124 , pp. 4583-4594
    • Stark, K.A.1    Yee, G.H.2    Roote, C.E.3    Williams, E.L.4    Zusman, S.5    Hynes, R.O.6
  • 55
    • 0032583165 scopus 로고    scopus 로고
    • Kakapo, a novel cytoskeletal-associated protein is essential for the restricted localization of the neuregulin-like factor, vein, at the muscle-tendon junction site
    • Strumpf D., Volk T. Kakapo, a novel cytoskeletal-associated protein is essential for the restricted localization of the neuregulin-like factor, vein, at the muscle-tendon junction site. J. Cell Biol. 143:1998;1259-1270.
    • (1998) J. Cell Biol. , vol.143 , pp. 1259-1270
    • Strumpf, D.1    Volk, T.2
  • 56
    • 0024727606 scopus 로고
    • Location of integrin complex and extracellular matrix molecules at the chicken myotendinous junction
    • Swadison S., Mayne R. Location of integrin complex and extracellular matrix molecules at the chicken myotendinous junction. Cell Tissue Res. 257:1989;537-543.
    • (1989) Cell Tissue Res. , vol.257 , pp. 537-543
    • Swadison, S.1    Mayne, R.2
  • 57
    • 0026318162 scopus 로고
    • Force transmission across muscle cell membranes
    • Tidball J. Force transmission across muscle cell membranes. J. Biomech. 24(Suppl. 1):1991;43-52.
    • (1991) J. Biomech. , vol.24 , Issue.SUPPL. 1 , pp. 43-52
    • Tidball, J.1
  • 58
    • 0033520330 scopus 로고    scopus 로고
    • CDNA cloning and chromosomal localization of human alpha(11) integrin: A collagen-binding, I domain-containing, beta(1)-associated integrin alpha-chain present in muscle tissues
    • Velling T., Kusche-Gullberg M., Sejersen T., Gullberg D. cDNA cloning and chromosomal localization of human alpha(11) integrin: a collagen-binding, I domain-containing, beta(1)-associated integrin alpha-chain present in muscle tissues. J. Biol. Chem. 274:1999;25735-25742.
    • (1999) J. Biol. Chem. , vol.274 , pp. 25735-25742
    • Velling, T.1    Kusche-Gullberg, M.2    Sejersen, T.3    Gullberg, D.4
  • 59
    • 0033230721 scopus 로고    scopus 로고
    • Singling out Drosophila tendon cells: A dialogue between two distinct cell types
    • Volk T. Singling out Drosophila tendon cells: a dialogue between two distinct cell types. Trends Genet. 15:1999;448-453.
    • (1999) Trends Genet. , vol.15 , pp. 448-453
    • Volk, T.1
  • 60
    • 0025153883 scopus 로고
    • A role for integrin in the formation of sarcometic cytoarchitecture
    • Volk T., Fessler L.I., Fessler J.H. A role for integrin in the formation of sarcometic cytoarchitecture. Cell. 63:1990;525-536.
    • (1990) Cell , vol.63 , pp. 525-536
    • Volk, T.1    Fessler, L.I.2    Fessler, J.H.3
  • 61
    • 0031692762 scopus 로고    scopus 로고
    • A screen to identify Drosophila genes required for integrin mediated adhesion
    • Walsh E.R., Brown N.H. A screen to identify Drosophila genes required for integrin mediated adhesion. Genetics. 150:1998;791-805.
    • (1998) Genetics , vol.150 , pp. 791-805
    • Walsh, E.R.1    Brown, N.H.2
  • 63
    • 0028089203 scopus 로고
    • Genes critical for muscle development and function in Caenorhabditis elegans identified through lethal mutations
    • Williams B.D., Waterston R.H. Genes critical for muscle development and function in Caenorhabditis elegans identified through lethal mutations. J. Cell Biol. 124:1994;475-490.
    • (1994) J. Cell Biol. , vol.124 , pp. 475-490
    • Williams, B.D.1    Waterston, R.H.2
  • 64
    • 0003139634 scopus 로고
    • The phenogenetics of the embryonic mutant, lethal myospheroid, in Drosophila melanogaster
    • Wright T.R.F. The phenogenetics of the embryonic mutant, lethal myospheroid, in Drosophila melanogaster. J. Exp. Zool. 143:1960;77-99.
    • (1960) J. Exp. Zool. , vol.143 , pp. 77-99
    • Wright, T.R.F.1
  • 65
    • 0031929760 scopus 로고    scopus 로고
    • Vinculin knockout results in heart and brain defects during embryonic development
    • Xu W., Baribault H., Adamson E.D. Vinculin knockout results in heart and brain defects during embryonic development. Development. 125:1998;327-337.
    • (1998) Development , vol.125 , pp. 327-337
    • Xu, W.1    Baribault, H.2    Adamson, E.D.3
  • 66
    • 0027179696 scopus 로고
    • γ, expressed in the midgut of Drosophila melanogaster
    • γ, expressed in the midgut of Drosophila melanogaster. Development. 118:1993;845-858.
    • (1993) Development , vol.118 , pp. 845-858
    • Yee, G.H.1    Hynes, R.O.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.