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Volumn 386, Issue 4, 2009, Pages 976-988

A LIM-9 (FHL) / SCPL-1 (SCP) Complex Interacts with the C-terminal Protein Kinase Regions of UNC-89 (Obscurin) in Caenorhabditis elegans Muscle

Author keywords

C. elegans; CTD phosphatase; FHL; muscle; obscurin

Indexed keywords

HELMINTH PROTEIN; LIM 9 PROTEIN; SMALL CTD PHOSPHATASE LIKE 1; TERNARY COMPLEX FACTOR; UNC 89 PROTEIN; UNCLASSIFIED DRUG;

EID: 60149098024     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2009.01.016     Document Type: Article
Times cited : (29)

References (50)
  • 1
    • 60149096659 scopus 로고    scopus 로고
    • Moerman, D. G. & Fire, A. (1997). Muscle: structure, function and development. In C. elegans II (Riddle, D. L., Blumenthal, T., Meyer, B. J. & Priess, J. R., eds), pp. 417-470, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
    • Moerman, D. G. & Fire, A. (1997). Muscle: structure, function and development. In C. elegans II (Riddle, D. L., Blumenthal, T., Meyer, B. J. & Priess, J. R., eds), pp. 417-470, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
  • 2
    • 38449083521 scopus 로고    scopus 로고
    • Moerman, D. G. & Williams, B. D. (2006). Sarcomere assembly in C. elegans muscle. WormBook, editor. The C. elegans Research Community, WormBook, doi:10.1895/wormbook.1.81.1, http://www.wormbook.org.
    • Moerman, D. G. & Williams, B. D. (2006). Sarcomere assembly in C. elegans muscle. WormBook, editor. The C. elegans Research Community, WormBook, doi:10.1895/wormbook.1.81.1, http://www.wormbook.org.
  • 4
    • 33745712384 scopus 로고    scopus 로고
    • Titin/connectin-related proteins in C. elegans: a review and new findings
    • Ferrara T.M., Flaherty D.B., and Benian G.M. Titin/connectin-related proteins in C. elegans: a review and new findings. J. Muscle Res. Cell Motil. 26 (2005) 435-447
    • (2005) J. Muscle Res. Cell Motil. , vol.26 , pp. 435-447
    • Ferrara, T.M.1    Flaherty, D.B.2    Benian, G.M.3
  • 5
    • 0024422164 scopus 로고
    • Sequence of an unusually large protein implicated in regulation of myosin activity in C. elegans
    • Benian G.M., Kiff J.E., Neckelmann N., Moerman D.G., and Waterston R.H. Sequence of an unusually large protein implicated in regulation of myosin activity in C. elegans. Nature 342 (1989) 45-50
    • (1989) Nature , vol.342 , pp. 45-50
    • Benian, G.M.1    Kiff, J.E.2    Neckelmann, N.3    Moerman, D.G.4    Waterston, R.H.5
  • 6
    • 0027237468 scopus 로고
    • Additional sequence complexity in the muscle gene, unc-22, and its encoded protein, twitchin, of Caenorhabditis elegans
    • Benian G.M., L'Hernault S.W., and Morris M.E. Additional sequence complexity in the muscle gene, unc-22, and its encoded protein, twitchin, of Caenorhabditis elegans. Genetics 134 (1993) 1097-1104
    • (1993) Genetics , vol.134 , pp. 1097-1104
    • Benian, G.M.1    L'Hernault, S.W.2    Morris, M.E.3
  • 7
    • 0023776666 scopus 로고
    • Identification and intracellular localization of the unc-22 gene product of Caenorhabditis elegans
    • Moerman D.G., Benian G.M., Barstead R.J., Schriefer L.A., and Waterston R.H. Identification and intracellular localization of the unc-22 gene product of Caenorhabditis elegans. Genes Dev. 2 (1988) 93-105
    • (1988) Genes Dev. , vol.2 , pp. 93-105
    • Moerman, D.G.1    Benian, G.M.2    Barstead, R.J.3    Schriefer, L.A.4    Waterston, R.H.5
  • 8
    • 0036406568 scopus 로고    scopus 로고
    • Titins in C. elegans with unusual features: coiled-coil domains, novel regulation of kinase activity and two new possible elastic regions
    • Flaherty D.B., Gernert K.M., Shmeleva N., Tang X., Mercer K.B., Borodovsky M., and Benian G.M. Titins in C. elegans with unusual features: coiled-coil domains, novel regulation of kinase activity and two new possible elastic regions. J. Mol. Biol. 323 (2002) 533-549
    • (2002) J. Mol. Biol. , vol.323 , pp. 533-549
    • Flaherty, D.B.1    Gernert, K.M.2    Shmeleva, N.3    Tang, X.4    Mercer, K.B.5    Borodovsky, M.6    Benian, G.M.7
  • 9
    • 0029978282 scopus 로고    scopus 로고
    • The Caenorhabditis elegans gene unc-89, required fpr muscle M-line assembly, encodes a giant modular protein composed of Ig and signal transduction domains
    • Benian G.M., Tinley T.L., Tang X., and Borodovsky M. The Caenorhabditis elegans gene unc-89, required fpr muscle M-line assembly, encodes a giant modular protein composed of Ig and signal transduction domains. J. Cell Biol. 132 (1996) 835-848
    • (1996) J. Cell Biol. , vol.132 , pp. 835-848
    • Benian, G.M.1    Tinley, T.L.2    Tang, X.3    Borodovsky, M.4
  • 10
    • 4143153989 scopus 로고    scopus 로고
    • Three new isoforms of Caenorhabditis elegans UNC-89 containing MLCK-like protein kinase domains
    • Small T.M., Gernert K.M., Flaherty D.B., Mercer K.B., Borodovsky M., and Benian G.M. Three new isoforms of Caenorhabditis elegans UNC-89 containing MLCK-like protein kinase domains. J. Mol. Biol. 342 (2004) 91-108
    • (2004) J. Mol. Biol. , vol.342 , pp. 91-108
    • Small, T.M.1    Gernert, K.M.2    Flaherty, D.B.3    Mercer, K.B.4    Borodovsky, M.5    Benian, G.M.6
  • 11
    • 0032616278 scopus 로고    scopus 로고
    • The genetics and molecular biology of the titin/connectin-like proteins of invertebrates
    • Benian G.M., Ayme-Southgate A., and Tinley T.L. The genetics and molecular biology of the titin/connectin-like proteins of invertebrates. Rev. Physiol. Biochem. Pharmacol. 138 (1999) 235-268
    • (1999) Rev. Physiol. Biochem. Pharmacol. , vol.138 , pp. 235-268
    • Benian, G.M.1    Ayme-Southgate, A.2    Tinley, T.L.3
  • 12
    • 0018961312 scopus 로고
    • Mutants with altered muscle structure of Caenorhabditis elegans
    • Waterston R.H., Thomson J.N., and Brenner S. Mutants with altered muscle structure of Caenorhabditis elegans. Dev. Biol. 77 (1980) 271-302
    • (1980) Dev. Biol. , vol.77 , pp. 271-302
    • Waterston, R.H.1    Thomson, J.N.2    Brenner, S.3
  • 13
    • 53149141697 scopus 로고    scopus 로고
    • The DH-PH region of the giant protein UNC-89 activates RHO-1 GTPase in Caenorhabditis elegans body wall muscle
    • Qadota H., Blangy A., Xiong G., and Benian G.M. The DH-PH region of the giant protein UNC-89 activates RHO-1 GTPase in Caenorhabditis elegans body wall muscle. J. Mol. Biol. 383 (2008) 747-752
    • (2008) J. Mol. Biol. , vol.383 , pp. 747-752
    • Qadota, H.1    Blangy, A.2    Xiong, G.3    Benian, G.M.4
  • 14
    • 20644440418 scopus 로고    scopus 로고
    • The kinase domain of titin controls muscle gene expression and protein turnover
    • Lange S., Xiang F., Yakovenko A., Vihola A., Hackman P., Rostkova E., et al. The kinase domain of titin controls muscle gene expression and protein turnover. Science 308 (2005) 1599-1603
    • (2005) Science , vol.308 , pp. 1599-1603
    • Lange, S.1    Xiang, F.2    Yakovenko, A.3    Vihola, A.4    Hackman, P.5    Rostkova, E.6
  • 15
    • 18844398202 scopus 로고    scopus 로고
    • Mechanically induced titin kinase activation studied by force-probe molecular dynamics simulations
    • Grater F., Shen J., Jiang H., Gautel M., and Grubmuller H. Mechanically induced titin kinase activation studied by force-probe molecular dynamics simulations. Biophys. J. 88 (2005) 790-804
    • (2005) Biophys. J. , vol.88 , pp. 790-804
    • Grater, F.1    Shen, J.2    Jiang, H.3    Gautel, M.4    Grubmuller, H.5
  • 16
    • 44449085063 scopus 로고    scopus 로고
    • Single-molecule force spectroscopy reveals a stepwise unfolding of Caenorhabditis elegans giant protein kinase domains
    • Greene D.N., Garcia T., Sutton R.B., Gernert K.M., Benian G.M., and Oberhauser A.F. Single-molecule force spectroscopy reveals a stepwise unfolding of Caenorhabditis elegans giant protein kinase domains. Biophys. J. 95 (2008) 1360-1370
    • (2008) Biophys. J. , vol.95 , pp. 1360-1370
    • Greene, D.N.1    Garcia, T.2    Sutton, R.B.3    Gernert, K.M.4    Benian, G.M.5    Oberhauser, A.F.6
  • 18
    • 48749118801 scopus 로고    scopus 로고
    • A novel protein phosphatase is a binding partner for the protein kinase domains of UNC-89 (Obscurin) in Caenorhabditis elegans
    • Qadota H., McGaha L.A., Mercer K.B., Stark T.J., Ferrara T.M., and Benian G.M. A novel protein phosphatase is a binding partner for the protein kinase domains of UNC-89 (Obscurin) in Caenorhabditis elegans. Mol. Biol. Cell 19 (2008) 2424-2432
    • (2008) Mol. Biol. Cell , vol.19 , pp. 2424-2432
    • Qadota, H.1    McGaha, L.A.2    Mercer, K.B.3    Stark, T.J.4    Ferrara, T.M.5    Benian, G.M.6
  • 19
    • 33745726378 scopus 로고    scopus 로고
    • Complete human gene structure of obscurin: implications for isoform generation by differential splicing
    • Fukuzawa A., Idowu S., and Gautel M. Complete human gene structure of obscurin: implications for isoform generation by differential splicing. J. Muscle Res. Cell Motil. 26 (2005) 427-434
    • (2005) J. Muscle Res. Cell Motil. , vol.26 , pp. 427-434
    • Fukuzawa, A.1    Idowu, S.2    Gautel, M.3
  • 20
    • 0035833261 scopus 로고    scopus 로고
    • Obscurin, a giant sarcomeric Rho guanine nucleotide exchange factor protein involved in sarcomere assembly
    • Young P., Ehler E., and Gautel M. Obscurin, a giant sarcomeric Rho guanine nucleotide exchange factor protein involved in sarcomere assembly. J. Cell Biol. 154 (2001) 123-136
    • (2001) J. Cell Biol. , vol.154 , pp. 123-136
    • Young, P.1    Ehler, E.2    Gautel, M.3
  • 22
    • 0035941407 scopus 로고    scopus 로고
    • The complete gene sequence of titin, expression of an unusual approximately 700-kDa titin isoform, and its interaction with obscurin identify a novel Z-line to I-band linking system
    • Bang M.L., Centner T., Fornoff F., Geach A.J., Gotthardt M., McNabb M., et al. The complete gene sequence of titin, expression of an unusual approximately 700-kDa titin isoform, and its interaction with obscurin identify a novel Z-line to I-band linking system. Circulat. Res. 89 (2001) 1065-1072
    • (2001) Circulat. Res. , vol.89 , pp. 1065-1072
    • Bang, M.L.1    Centner, T.2    Fornoff, F.3    Geach, A.J.4    Gotthardt, M.5    McNabb, M.6
  • 23
    • 0037455559 scopus 로고    scopus 로고
    • Binding of an ankyrin-1 isoform to obscurin suggests a molecular link between the sarcoplasmic reticulum and myofibrils in striated muscles
    • Bagnato P., Barone V., Giacomello E., Rossi D., and Sorrentino V. Binding of an ankyrin-1 isoform to obscurin suggests a molecular link between the sarcoplasmic reticulum and myofibrils in striated muscles. J. Cell Biol. 160 (2003) 245-253
    • (2003) J. Cell Biol. , vol.160 , pp. 245-253
    • Bagnato, P.1    Barone, V.2    Giacomello, E.3    Rossi, D.4    Sorrentino, V.5
  • 27
    • 55549103030 scopus 로고    scopus 로고
    • The rho-guanine nucleotide exchange factor domain of obscurin regulates assembly of titin at the Z-disk through interactions with Ran binding protein 9
    • Bowman A.L., Catino D.H., Strong J.C., Randall W.R., Kontrogianni-Konstantopoulos A., and Bloch R.J. The rho-guanine nucleotide exchange factor domain of obscurin regulates assembly of titin at the Z-disk through interactions with Ran binding protein 9. Mol. Biol. Cell 19 (2008) 3782-3792
    • (2008) Mol. Biol. Cell , vol.19 , pp. 3782-3792
    • Bowman, A.L.1    Catino, D.H.2    Strong, J.C.3    Randall, W.R.4    Kontrogianni-Konstantopoulos, A.5    Bloch, R.J.6
  • 28
    • 46749123127 scopus 로고    scopus 로고
    • Interactions with titin and myomesin target obscurin and obscurin-like 1 to the M-band: implications for hereditary myopathies
    • Fukuzawa A., Lange S., Holt M., Vihola A., Carmignac V., Ferreiro A., et al. Interactions with titin and myomesin target obscurin and obscurin-like 1 to the M-band: implications for hereditary myopathies. J. Cell Sci. 121 (2008) 1841-1851
    • (2008) J. Cell Sci. , vol.121 , pp. 1841-1851
    • Fukuzawa, A.1    Lange, S.2    Holt, M.3    Vihola, A.4    Carmignac, V.5    Ferreiro, A.6
  • 29
    • 35848949782 scopus 로고    scopus 로고
    • Two LIM domain proteins and UNC-96 link UNC-97/pinch to myosin thick filaments in Caenorhabditis elegans muscle
    • Qadota H., Mercer K.B., Miller R.K., Kaibuchi K., and Benian G.M. Two LIM domain proteins and UNC-96 link UNC-97/pinch to myosin thick filaments in Caenorhabditis elegans muscle. Mol. Biol. Cell 18 (2007) 4317-4326
    • (2007) Mol. Biol. Cell , vol.18 , pp. 4317-4326
    • Qadota, H.1    Mercer, K.B.2    Miller, R.K.3    Kaibuchi, K.4    Benian, G.M.5
  • 30
    • 0041620131 scopus 로고    scopus 로고
    • NORSp: Predictions of long regions without regular secondary structure
    • Liu J., and Rost B. NORSp: Predictions of long regions without regular secondary structure. Nucleic Acids Res. 31 (2003) 3833-3835
    • (2003) Nucleic Acids Res. , vol.31 , pp. 3833-3835
    • Liu, J.1    Rost, B.2
  • 31
    • 0036968309 scopus 로고    scopus 로고
    • Loopy proteins appear conserved in evolution
    • Liu J., Tan H., and Rost B. Loopy proteins appear conserved in evolution. J. Mol. Biol. 322 (2002) 53-64
    • (2002) J. Mol. Biol. , vol.322 , pp. 53-64
    • Liu, J.1    Tan, H.2    Rost, B.3
  • 32
    • 0029901640 scopus 로고    scopus 로고
    • Analysis of compositionally biased regions in sequence databases
    • Wootton J.C., and Federhen S. Analysis of compositionally biased regions in sequence databases. Methods Enzymol. 266 (1996) 554-571
    • (1996) Methods Enzymol. , vol.266 , pp. 554-571
    • Wootton, J.C.1    Federhen, S.2
  • 33
    • 0037850992 scopus 로고    scopus 로고
    • C. elegans PAT-6/actopaxin plays a critical role in the assembly of integrin adhesion complexes in vivo
    • Lin X., Qadota H., Moerman D.G., and Williams B.D. C. elegans PAT-6/actopaxin plays a critical role in the assembly of integrin adhesion complexes in vivo. Curr. Biol. 13 (2003) 922-932
    • (2003) Curr. Biol. , vol.13 , pp. 922-932
    • Lin, X.1    Qadota, H.2    Moerman, D.G.3    Williams, B.D.4
  • 34
    • 0037076211 scopus 로고    scopus 로고
    • C. elegans PAT-4/ILK functions as an adaptor protein within integrin adhesion complexes
    • Mackinnon A.C., Qadota H., Norman K.R., Moerman D.G., and Williams B.D. C. elegans PAT-4/ILK functions as an adaptor protein within integrin adhesion complexes. Curr. Biol. 12 (2002) 787-797
    • (2002) Curr. Biol. , vol.12 , pp. 787-797
    • Mackinnon, A.C.1    Qadota, H.2    Norman, K.R.3    Moerman, D.G.4    Williams, B.D.5
  • 35
    • 33845700521 scopus 로고    scopus 로고
    • UNC-98 links an integrin-associated complex to thick filaments in Caenorhabditis elegans muscle
    • Miller R.K., Qadota H., Landsverk M.L., Mercer K.B., Epstein H.F., and Benian G.M. UNC-98 links an integrin-associated complex to thick filaments in Caenorhabditis elegans muscle. J. Cell Biol. 175 (2006) 853-859
    • (2006) J. Cell Biol. , vol.175 , pp. 853-859
    • Miller, R.K.1    Qadota, H.2    Landsverk, M.L.3    Mercer, K.B.4    Epstein, H.F.5    Benian, G.M.6
  • 36
    • 34548118392 scopus 로고    scopus 로고
    • UNC-97/PINCH is involved in the assembly of integrin cell adhesion complexes in Caenorhabditis elegans body wall muscle
    • Norman K.R., Cordes S., Qadota H., Rahmani P., and Moerman D.G. UNC-97/PINCH is involved in the assembly of integrin cell adhesion complexes in Caenorhabditis elegans body wall muscle. Dev. Biol. 309 (2007) 45-55
    • (2007) Dev. Biol. , vol.309 , pp. 45-55
    • Norman, K.R.1    Cordes, S.2    Qadota, H.3    Rahmani, P.4    Moerman, D.G.5
  • 37
    • 3142581436 scopus 로고    scopus 로고
    • The LIM-only proteins FHL2 and FHL3 interact with alpha- and beta-subunits of the muscle alpha7 beta1 integrin receptor
    • Samson T., Smyth N., Janetzky S., Wendler O., Müller J.M., Schüle R., et al. The LIM-only proteins FHL2 and FHL3 interact with alpha- and beta-subunits of the muscle alpha7 beta1 integrin receptor. J. Biol. Chem. 279 (2004) 28641-28652
    • (2004) J. Biol. Chem. , vol.279 , pp. 28641-28652
    • Samson, T.1    Smyth, N.2    Janetzky, S.3    Wendler, O.4    Müller, J.M.5    Schüle, R.6
  • 38
    • 0034721855 scopus 로고    scopus 로고
    • The LIM-only protein DRAL/FHL2 binds to the cytoplasmic domain of several alpha and beta integrin chains and is recruited to adhesion complexes
    • Wixler V., Geerts D., Laplantine E., Westhoff D., Smyth N., Aumailley M., et al. The LIM-only protein DRAL/FHL2 binds to the cytoplasmic domain of several alpha and beta integrin chains and is recruited to adhesion complexes. J. Biol. Chem. 275 (2000) 33669-33678
    • (2000) J. Biol. Chem. , vol.275 , pp. 33669-33678
    • Wixler, V.1    Geerts, D.2    Laplantine, E.3    Westhoff, D.4    Smyth, N.5    Aumailley, M.6
  • 39
    • 38749136299 scopus 로고    scopus 로고
    • X-linked dominant scapuloperoneal myopathy is due to a mutation in the gene encoding four-and-a-half-LIM protein 1
    • Quinzii C.M., Vu T.H., Min K.C., Tanji K., Barral S., Grewal R.P., et al. X-linked dominant scapuloperoneal myopathy is due to a mutation in the gene encoding four-and-a-half-LIM protein 1. Am. J. Hum. Genet. 82 (2008) 208-213
    • (2008) Am. J. Hum. Genet. , vol.82 , pp. 208-213
    • Quinzii, C.M.1    Vu, T.H.2    Min, K.C.3    Tanji, K.4    Barral, S.5    Grewal, R.P.6
  • 40
    • 38749121773 scopus 로고    scopus 로고
    • An X-linked myopathy with postural muscle atrophy and generalized hypertrophy,termed XMPMA, is caused by mutations in FHL1
    • Windpassinger C., Schoser B., Straub V., Hochmeister S., Noor A., Lohberger B., et al. An X-linked myopathy with postural muscle atrophy and generalized hypertrophy,termed XMPMA, is caused by mutations in FHL1. Am. J. Hum. Genet. 82 (2008) 88-99
    • (2008) Am. J. Hum. Genet. , vol.82 , pp. 88-99
    • Windpassinger, C.1    Schoser, B.2    Straub, V.3    Hochmeister, S.4    Noor, A.5    Lohberger, B.6
  • 41
    • 40549108276 scopus 로고    scopus 로고
    • Proteomic identification of FHL1 as the protein mutated in human reducing body myopathy
    • Schessl J., Zou Y., McGrath M.J., Cowling B.S., Maiti B., Chin S.S., et al. Proteomic identification of FHL1 as the protein mutated in human reducing body myopathy. J. Clin. Invest. 118 (2008) 904-912
    • (2008) J. Clin. Invest. , vol.118 , pp. 904-912
    • Schessl, J.1    Zou, Y.2    McGrath, M.J.3    Cowling, B.S.4    Maiti, B.5    Chin, S.S.6
  • 42
    • 0034735595 scopus 로고    scopus 로고
    • DRAL is a p53-responsive gene whose four and a half LIM domain protein product induces apoptosis
    • Scholl F.A., McLoughlin P., Ehler E., de Giovanni C., and Schäfer B.W. DRAL is a p53-responsive gene whose four and a half LIM domain protein product induces apoptosis. J. Cell Biol. 151 (2000) 495-506
    • (2000) J. Cell Biol. , vol.151 , pp. 495-506
    • Scholl, F.A.1    McLoughlin, P.2    Ehler, E.3    de Giovanni, C.4    Schäfer, B.W.5
  • 43
    • 58249091742 scopus 로고    scopus 로고
    • Identification of FHL1 as a regulator of skeletal muscle mass: implications for human myopathy
    • Cowling B.S., McGrath M.J., Nguyen M.A., Cottle D.L., Kee A.J., Brown S., et al. Identification of FHL1 as a regulator of skeletal muscle mass: implications for human myopathy. J. Cell Biol. 183 (2008) 1033-1048
    • (2008) J. Cell Biol. , vol.183 , pp. 1033-1048
    • Cowling, B.S.1    McGrath, M.J.2    Nguyen, M.A.3    Cottle, D.L.4    Kee, A.J.5    Brown, S.6
  • 45
    • 0016063911 scopus 로고
    • The genetics of Caenorhabditis elegans
    • Brenner S. The genetics of Caenorhabditis elegans. Genetics 77 (1974) 71-94
    • (1974) Genetics , vol.77 , pp. 71-94
    • Brenner, S.1
  • 46
    • 33748289980 scopus 로고    scopus 로고
    • Caenorhabditis elegans UNC-96 is a new component of M-lines that interacts with UNC-98 and paramyosin and is required in adult muscle for assembly and/or maintenance of thick filaments
    • Mercer K.B., Miller R.K., Tinley T.L., Sheth S., Qadota H., and Benian G.M. Caenorhabditis elegans UNC-96 is a new component of M-lines that interacts with UNC-98 and paramyosin and is required in adult muscle for assembly and/or maintenance of thick filaments. Mol. Biol. Cell 17 (2006) 3832-3847
    • (2006) Mol. Biol. Cell , vol.17 , pp. 3832-3847
    • Mercer, K.B.1    Miller, R.K.2    Tinley, T.L.3    Sheth, S.4    Qadota, H.5    Benian, G.M.6
  • 47
    • 0027319325 scopus 로고
    • Synaptic function is impaired but not eliminated in C. elegans mutants lacking synaptotagmin
    • Nonet M.L., Grundahl K., Meyer B.J., and Rand J.B. Synaptic function is impaired but not eliminated in C. elegans mutants lacking synaptotagmin. Cell 73 (1993) 1291-1305
    • (1993) Cell , vol.73 , pp. 1291-1305
    • Nonet, M.L.1    Grundahl, K.2    Meyer, B.J.3    Rand, J.B.4
  • 48
    • 0037031152 scopus 로고    scopus 로고
    • Loss of the putative RNA-directed RNA polymerase RRF-3 makes C. elegans hypersensitive to RNAi
    • Simmer F., Tijsterman M., Parrish S., Koushika S.P., Nonet M.L., Fire A., et al. Loss of the putative RNA-directed RNA polymerase RRF-3 makes C. elegans hypersensitive to RNAi. Curr. Biol. 12 (2002) 1317-1319
    • (2002) Curr. Biol. , vol.12 , pp. 1317-1319
    • Simmer, F.1    Tijsterman, M.2    Parrish, S.3    Koushika, S.P.4    Nonet, M.L.5    Fire, A.6
  • 49
    • 0035941485 scopus 로고    scopus 로고
    • Ingestion of bacterially expressed dsRNAs can produce specific and potent genetic interference in Caenorhabditis elegans
    • Timmons L., Court D.L., and Fire A. Ingestion of bacterially expressed dsRNAs can produce specific and potent genetic interference in Caenorhabditis elegans. Gene 263 (2001) 103-112
    • (2001) Gene , vol.263 , pp. 103-112
    • Timmons, L.1    Court, D.L.2    Fire, A.3
  • 50
    • 0031877935 scopus 로고    scopus 로고
    • A new marker for mosaic analysis in Caenorhabditis elegans indicates a fusion between hyp6 and hyp7, two major components of the hypodermis
    • Yochem J., Gu T., and Han M. A new marker for mosaic analysis in Caenorhabditis elegans indicates a fusion between hyp6 and hyp7, two major components of the hypodermis. Genetics 149 (1998) 1323-1334
    • (1998) Genetics , vol.149 , pp. 1323-1334
    • Yochem, J.1    Gu, T.2    Han, M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.