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Volumn 109, Issue 9, 2011, Pages 1082-1095

Caenorhabditis elegans muscle: A genetic and molecular model for protein interactions in the heart

Author keywords

Caenorhabditis elegans sarcomere structure; cardiomyopathies; model genetics; sarcomere assembly

Indexed keywords

CAENORHABDITIS ELEGANS PROTEIN; PROTEOME;

EID: 80054966402     PISSN: 00097330     EISSN: 15244571     Source Type: Journal    
DOI: 10.1161/CIRCRESAHA.110.237685     Document Type: Review
Times cited : (35)

References (122)
  • 1
    • 0035936792 scopus 로고    scopus 로고
    • The genetic basis for cardiomyopathy: From mutation identification to mechanistic paradigms
    • DOI 10.1016/S0092-8674(01)00242-2
    • Seidman JG, Seidman C. The genetic basis for cardiomyopathy: from mutation identification to mechanistic paradigms. Cell. 2001;104: 557-567. (Pubitemid 32201950)
    • (2001) Cell , vol.104 , Issue.4 , pp. 557-567
    • Seidman, J.G.1    Seidman, C.2
  • 2
    • 77950614614 scopus 로고    scopus 로고
    • Evolving molecular diagnostics for familial cardiomyopathies: At the heart of it all
    • Callis TE, Jensen BC, Weck KE, Willis MS. Evolving molecular diagnostics for familial cardiomyopathies: at the heart of it all. Expert Rev Mol Diagn. 2010;10:329-351.
    • (2010) Expert Rev Mol Diagn , vol.10 , pp. 329-351
    • Callis, T.E.1    Jensen, B.C.2    Weck, K.E.3    Willis, M.S.4
  • 4
    • 0025164036 scopus 로고
    • A molecular basis for familial hypertrophic cardiomyopathy: Aň/acardiac myosin heavy chain hybrid gene
    • Tanigawa G, Jarcho JA, Kass S, Solomon SD, Vosberg H-P, Seidman JG, Seidman CE. A molecular basis for familial hypertrophic cardiomyopathy: aň/acardiac myosin heavy chain hybrid gene. Cell. 1990; 62:991-998.
    • (1990) Cell , vol.62 , pp. 991-998
    • Tanigawa, G.1    Jarcho, J.A.2    Kass, S.3    Solomon, S.D.4    Vosberg, H.-P.5    Seidman, J.G.6    Seidman, C.E.7
  • 8
    • 77949718853 scopus 로고    scopus 로고
    • Hypertrophic cardiomyopathy: From genetics to treatment
    • Marian AJ. Hypertrophic cardiomyopathy: from genetics to treatment. Eur J Clin Invest. 2010;40:360-369.
    • (2010) Eur J Clin Invest , vol.40 , pp. 360-369
    • Marian, A.J.1
  • 9
    • 0021153417 scopus 로고
    • Expression of the cardiac ventricular α- and β-myosin heavy chain genes is developmentally and hormonally regulated
    • Lompre A-M, Nadal-Ginard B, Mahdavi V. Expression of the cardiac ventriculaRf-anD1-myosin heavy chain genes is developmentally and hormonally regulated. J Biol Chem. 1984;259:6437-6446. (Pubitemid 14108193)
    • (1984) Journal of Biological Chemistry , vol.259 , Issue.10 , pp. 6437-6446
    • Lompre, A.-M.1    Nadal-Ginard, B.2    Mahdavi, V.3
  • 10
    • 0021273032 scopus 로고
    • Myosin types in the human heart. An immunofluorescence study of normal and hypertrophied atrial and ventricular myocardium
    • Gorza L, Mercadier JJ, Schwartz K, Thornell LE, Sartore S, Schiaffino S. Myosin types in the human heart: an immunofluorescent study of normal and hypertrophied atrial and ventricular myocardium. Circ Res. 1984;54:694-702. (Pubitemid 14091674)
    • (1984) Circulation Research , vol.54 , Issue.6 , pp. 694-702
    • Gorza, L.1    Mercadier, J.J.2    Schwart, K.3
  • 11
    • 0023764031 scopus 로고
    • Molecular cloning and characterization of human cardiaC2-anD1-form myosin heavy chain complementary DNA clones
    • Kurabayashi M, Tsuchimochi H, Komuro I, Takaku F, Yazaki Y. Molecular cloning and characterization of human cardiaC2-anD1-form myosin heavy chain complementary DNA clones. J Clin Invest. 1988; 82:524-531.
    • (1988) J Clin Invest , vol.82 , pp. 524-531
    • Kurabayashi, M.1    Tsuchimochi, H.2    Komuro, I.3    Takaku, F.4    Yazaki, Y.5
  • 12
  • 13
    • 0019126256 scopus 로고
    • Paramyosin is necessary for determination of nematode thick filament length in vivo
    • Mackenzie JM, Epstein HF. Paramyosin is necessary for determination of nematode thick filament length in vivo. Cell. 1980;22:747-755. (Pubitemid 11218764)
    • (1980) Cell , vol.22 , Issue.3 , pp. 747-755
    • Mackenzie Jr., J.M.1    Epstein, H.F.2
  • 14
    • 0022345717 scopus 로고
    • Muscle organization in Caenorhabditis elegans: Localization of proteins implicated in thin filament attachment and I-band organization
    • DOI 10.1083/jcb.101.4.1532
    • Francis GR, Waterston RH. Muscle organization in Caenorhabditis elegans: localization of proteins implicated in thin filament attachment and I-band organization. J Cell Biol. 1985;101:1532-1549. (Pubitemid 16234180)
    • (1985) Journal of Cell Biology , vol.101 , Issue.4 , pp. 1532-1549
    • Francis, G.R.1    Waterston, R.H.2
  • 17
    • 77952475658 scopus 로고    scopus 로고
    • Molecular structure of sarcomere-to-membrane attachment at M-lines in C elegans muscle
    • Qadota H, Benian GM. Molecular structure of sarcomere-to-membrane attachment at M-lines in C elegans muscle. J Biomed Biotech. 2010; 864749.
    • (2010) J Biomed Biotech , pp. 864749
    • Qadota, H.1    Benian, G.M.2
  • 18
    • 0037076211 scopus 로고    scopus 로고
    • C. elegans PAT-4/ILK functions as an adaptor protein within integrin adhesion complexes
    • DOI 10.1016/S0960-9822(02)00810-2, PII S0960982202008102
    • Mackinnon AC, Qadota H, Norman KR, Moerman DG, Williams BD. C elegans PAT-4/ILK functions as an adaptor protein within integrin adhesion complexes. Curr Biol. 2002;12:787-797. (Pubitemid 34514364)
    • (2002) Current Biology , vol.12 , Issue.10 , pp. 787-797
    • Mackinnon A.Craig1    Qadota, H.2    Norman, K.R.3    Moerman, D.G.4    Williams, B.D.5
  • 19
    • 0037850992 scopus 로고    scopus 로고
    • C. elegans PAT-6/actopaxin plays a critical role in the assembly of integrin adhesion complexes in vivo
    • DOI 10.1016/S0960-9822(03)00372-5
    • Lin X, Qadota H, Moerman DG, Williams BD. C elegans PAT-6/actopaxin plays a critical role in the assembly of integrin adhesion complexes in vivo. Curr Biol. 2003;13:922-932. (Pubitemid 36632141)
    • (2003) Current Biology , vol.13 , Issue.11 , pp. 922-932
    • Lin, X.1    Qadota, H.2    Moerman, D.G.3    Williams, B.D.4
  • 20
    • 34548118392 scopus 로고    scopus 로고
    • UNC-97/PINCH is involved in the assembly of integrin cell adhesion complexes in Caenorhabditis elegans body wall muscle
    • DOI 10.1016/j.ydbio.2007.06.014, PII S0012160607011499
    • Norman KR, Cordes S, Qadota H, Rahmani P, Moerman DG. UNC-97/PINCH is involved in the assembly of integrin cell adhesion complexes in Caenorhabditis elegans body wall muscle. Dev Biol. 2007;309: 45-55. (Pubitemid 47302444)
    • (2007) Developmental Biology , vol.309 , Issue.1 , pp. 45-55
    • Norman, K.R.1    Cordes, S.2    Qadota, H.3    Rahmani, P.4    Moerman, D.G.5
  • 21
    • 0037632845 scopus 로고    scopus 로고
    • Caenorhabditis elegans UNC-98, a C2H2 Zn finger protein, is a novel partner of UNC-97/PINCH in muscle adhesion complexes
    • DOI 10.1091/mbc.E02-10-0676
    • Mercer KB, Flaherty DB, Miller RK, Qadota H, Tinley TL, Moerman DG, Benian GM. Caenorhabditis elegans UNC-98, a C2H2 Zn finger protein, is a novel partner of UNC-97/PINCH in muscle adhesion complexes. Mol Biol Cell. 2003;14:2492-2507. (Pubitemid 36724337)
    • (2003) Molecular Biology of the Cell , vol.14 , Issue.6 , pp. 2492-2507
    • Mercer, K.B.1    Flaherty, D.B.2    Miller, R.K.3    Qadota, H.4    Tinley, T.L.5    Moerman, D.G.6    Benian, G.M.7
  • 22
    • 33845700521 scopus 로고    scopus 로고
    • UNC-98 links an integrin-associated complex to thick filaments in Caenorhabditis elegans muscle
    • DOI 10.1083/jcb.200608043
    • Miller RK, Qadota H, Landsverk ML, Mercer KB, Epstein HF, Benian GM. UNC-98 links an integrin-associated complex to thick filaments in Caenorhabditis elegans muscle. J Cell Biol. 2006;175:853-859. (Pubitemid 44969191)
    • (2006) Journal of Cell Biology , vol.175 , Issue.6 , 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
  • 23
    • 35848949782 scopus 로고    scopus 로고
    • Two LIM domain proteins and UNC-96 link UNC-97/PINCH to myosin thick filaments in Caenorhabditis elegans muscle
    • DOI 10.1091/mbc.E07-03-0278
    • Qadota H, Mercer KB, Miller RK, Kaibuchi K, Benian GM. Two LIM domain proteins and UNC-96 link UNC-97/pinch to myosin thick filaments in Caenorhabditis elegans muscle. Mol Biol Cell. 2007;18: 4317-4326. (Pubitemid 350060161)
    • (2007) Molecular Biology of the Cell , vol.18 , Issue.11 , pp. 4317-4326
    • Qadota, H.1    Mercer, K.B.2    Miller, R.K.3    Kaibuchi, K.4    Benian, G.M.5
  • 24
    • 79960293259 scopus 로고    scopus 로고
    • The C elegans paxillin ortholog, PXL-1, is required for pharyngeal muscle contraction and for viability
    • Warner A, Qadota H, Benian GM, Vogl AW, Moerman DG. The C elegans paxillin ortholog, PXL-1, is required for pharyngeal muscle contraction and for viability. Mol Biol Cell. 2011;22:2551-2563.
    • (2011) Mol Biol Cell , vol.22 , pp. 2551-2563
    • Warner, A.1    Qadota, H.2    Benian, G.M.3    Vogl, A.W.4    Moerman, D.G.5
  • 25
    • 0018961312 scopus 로고
    • Mutants with altered muscle structure in Caenorhabditis elegans
    • DOI 10.1016/0012-1606(80)90475-3
    • Waterston RH, Thomson JN, Brenner S. Mutants with altered muscle structure in Caenorhabditis elegans. Dev Biol. 1980;77:271-302. (Pubitemid 10011378)
    • (1980) Developmental Biology , vol.77 , Issue.2 , pp. 271-302
    • Waterston, R.H.1    Thomson, J.N.2    Brenner, S.3
  • 26
    • 0019297123 scopus 로고
    • Identification of genetic elements associated with muscle structure in the nematode Caenorhabditis elegans
    • Zengel JM, Epstein HF. Identification of genetic elements associated with muscle structure in the nematode Caenorhabditis elegans. Cell Motil. 1980;1:73-97. (Pubitemid 12233335)
    • (1980) Cell Motility , vol.1 , Issue.1 , pp. 73-97
    • Zengel, J.M.1    Epstein, H.F.2
  • 27
    • 0028089203 scopus 로고
    • Genes critical for muscle development and function in Caenorhabditis elegans identified through lethal mutations
    • Williams BD, Waterston RH. Genes critical for muscle development and function in Caenorhabditis elegans identified through lethal mutations. J Cell Biol. 1994;124:475-490. (Pubitemid 24064460)
    • (1994) Journal of Cell Biology , vol.124 , Issue.4 , pp. 475-490
    • Williams, B.D.1    Waterston, R.H.2
  • 29
    • 0019975166 scopus 로고
    • Periodic charge distributions in the myosin rod amino acid sequence match cross-bridge spacings in muscle
    • DOI 10.1038/299226a0
    • McLachlan AD, Karn J. Periodic charge distributions in the myosin rod amino acid sequence match cross-bridge spacings in muscle. Nature. 1982;299:226-231. (Pubitemid 12059141)
    • (1982) Nature , vol.299 , Issue.5880 , pp. 226-231
    • McLachlan, A.D.1    Karn, J.2
  • 30
    • 0016345945 scopus 로고
    • A mutant affecting the heavy chain of myosin in Caenorhabditis elegans
    • Epstein HF, Waterston RH, Brenner S. A mutant affecting the heavy chain of myosin in Caenorhabditis elegans. J Mol Biol. 1974;90: 291-300.
    • (1974) J Mol Biol , vol.90 , pp. 291-300
    • Epstein, H.F.1    Waterston, R.H.2    Brenner, S.3
  • 31
    • 0021878067 scopus 로고
    • Sequence analysis of mutations that affect the synthesis, assembly and enzymatic activity of unc-54 myosin heavy chain of Caenorhabditis elegans
    • DOI 10.1016/0022-2836(85)90170-6
    • Dibb NJ, Brown DM, Karn J, Moerman DG, Bolten SL, Waterston RH. Sequence analysis of mutations that affect the synthesis, assembly and enzymatic activity of the unc-54 myosin heavy chain of Caenorhabditis elegans. J Mol Biol. 1985;183:543-551. (Pubitemid 15036846)
    • (1985) Journal of Molecular Biology , vol.183 , Issue.4 , pp. 543-551
    • Dibb, N.J.1    Brown, D.M.2    Karn, J.3
  • 32
    • 0024097541 scopus 로고
    • Myosin heavy-chain mutations that disrupt Caenorhabditis elegans thick filament assembly
    • Bejsovec A, Anderson P. Myosin heavy-chain mutations that disrupt Caenorhabditis elegans thick filament assembly. Genes Dev. 1988;2: 1307-1317.
    • (1988) Genes Dev , vol.2 , pp. 1307-1317
    • Bejsovec, A.1    Anderson, P.2
  • 33
    • 0024422164 scopus 로고
    • Sequence of an unusually large protein implicated in regulation of myosin activity in C. elegans
    • DOI 10.1038/342045a0
    • Benian GM, Kiff JE, Neckelmann N, Moerman DG, Waterston RH. The sequence of twitchin: an unusually large protein implicated in regulation of myosin activity in C elegans. Nature. 1989;342:45-50. (Pubitemid 19271116)
    • (1989) Nature , vol.342 , Issue.6245 , pp. 45-50
    • Benian, G.M.1    Kiff, J.E.2    Neckelmann, N.3    Moerman, D.G.4    Waterston, R.H.5
  • 34
    • 0027237468 scopus 로고
    • Additional sequence complexity in the muscle gene, unc-22, and its encoded protein, twitchin, of Caenorhabditis elegans
    • Benian GM, L'Hernault SW, Morris ME. Additional sequence complexity in the muscle gene, unc-22, and its encoded protein, twitchin, of C elegans. Genetics. 1993;134:1097-1104. (Pubitemid 23220032)
    • (1993) Genetics , vol.134 , Issue.4 , pp. 1097-1104
    • Benian, G.M.1    L'Hernault, S.W.2    Morris, M.E.3
  • 35
    • 0028287635 scopus 로고
    • Insights into autoregulation from the crystal structure of twitchin kinase
    • DOI 10.1038/369581a0
    • Hu S-H, Parker MW, Lei J, Wilce MCJ, Benian GM, Kemp BE. Intrasteric regulation of protein kinases: insights from the crystal structure of twitchin kinase. Nature. 1994;369:581-584. (Pubitemid 24192530)
    • (1994) Nature , vol.369 , Issue.6481 , pp. 581-584
    • Hu, S.-H.1    Parker, M.W.2    Lei, J.Y.3    Wilce, M.C.J.4    Benian, G.M.5    Kemp, B.E.6
  • 36
    • 0032578901 scopus 로고    scopus 로고
    • Structural basis for activation of the titin kinase domain during myofibrillogenesis
    • DOI 10.1038/27603
    • Mayans O, van der Ven PF, Wilm M, Mues A, Young P, Furst DO, Wilmanns M, Gautel M. Structural basis for activation of the titin kinase domain during myofibrillogenesis. Nature. 1998;395:863-869. (Pubitemid 28503420)
    • (1998) Nature , vol.395 , Issue.6705 , pp. 863-869
    • Mayans, O.1    Van Der Ven, P.F.M.2    Wilm, M.3    Mues, A.4    Young, P.5    Furst, D.O.6    Wilmanns, M.7    Gautel, M.8
  • 37
    • 0029978282 scopus 로고    scopus 로고
    • The Caenorhabditis elegans gene unc-89, required for muscle M-line assembly, encodes a giant modular protein composed of Ig and signal transduction domains
    • DOI 10.1083/jcb.132.5.835
    • Benian GM, Tinley TL, Tang X, Borodovsky M. The C elegans gene unc-89, required for muscle M-line assembly, encodes a giant modular protein containing Ig and signal transduction domains. J Cell Biol. 1996;132:835-848. (Pubitemid 26085499)
    • (1996) Journal of Cell Biology , vol.132 , Issue.5 , pp. 835-848
    • Benian, G.M.1    Tinley, T.L.2    Tang, X.3    Borodovsky, M.4
  • 38
    • 0035833261 scopus 로고    scopus 로고
    • Obscurin, a giant sarcomeric Rho guanine nucleotide exchange factor protein involved in sarcomere assembly
    • DOI 10.1083/jcb.200102110
    • Young P, Ehler E, Gautel M. Obscurin, a giant sarcomeric Rho guanine nucleotide exchange factor protein involved in sarcomere assembly. J Cell Biol. 2001;154:123-136. (Pubitemid 34289283)
    • (2001) Journal of Cell Biology , vol.154 , Issue.1 , pp. 123-136
    • Young, P.1    Ehler, E.2    Gautel, M.3
  • 39
    • 0035941407 scopus 로고    scopus 로고
    • The complete gene sequence of titin, expression of an unusual ≈700-kDa titin isoform, and its interaction with obscurin identify a novel Z-line to I-band linking system
    • Bang ML, Centner T, Fornoff F, Geach AJ, Gotthardt M, McNabb M, Witt CC, Labeit D, Gregorio CC, Granzier H, Labeit S. 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. Circ Res. 2001;89:1065-1072. (Pubitemid 34640875)
    • (2001) Circulation Research , vol.89 , Issue.11 , pp. 1065-1072
    • Bang, M.-L.1    Centner, T.2    Fornoff, F.3    Geach, A.J.4    Gotthardt, M.5    McNabb, M.6    Witt, C.C.7    Labeit, D.8    Gregorio, C.C.9    Granzier, H.10    Labeit, S.11
  • 40
    • 0016358187 scopus 로고
    • Temperature-sensitive mutation affecting myofilament assembly in Caenorhabditis elegans
    • Epstein HF, Thomson JN. Temperature-sensitive mutation affecting myofilament assembly in Caenorhabditis elegans. Nature. 1974;250: 579-580.
    • (1974) Nature , vol.250 , pp. 579-580
    • Epstein, H.F.1    Thomson, J.N.2
  • 41
    • 0025028910 scopus 로고
    • The unc-45 gene of Caenorhabditis elegans is an essential muscle-affecting gene with maternal expression
    • Venolia L, Waterston RH. The unc-45 gene of Caenorhabditis elegans is an essential muscle-affecting gene with maternal expression. Genetics. 1990;126:345-353. (Pubitemid 20341017)
    • (1990) Genetics , vol.126 , Issue.2 , pp. 345-353
    • Venolia, L.1    Waterston, R.H.2
  • 42
    • 0032583155 scopus 로고    scopus 로고
    • Unc-45 mutations in Caenorhabditis elegans implicate a CRO1/She4p-like domain in myosin assembly
    • DOI 10.1083/jcb.143.5.1215
    • Barral JM, Bauer CC, Ortiz I, Epstein HF. Unc-45 mutations in C elegans implicate a CRO1/She4p-like domain in myosin assembly. J Cell Biol. 1998;143:1215-1225. (Pubitemid 28559823)
    • (1998) Journal of Cell Biology , vol.143 , Issue.5 , pp. 1215-1225
    • Barral, J.M.1    Bauer, C.C.2    Ortiz, I.3    Epstein, H.F.4
  • 43
    • 0037169028 scopus 로고    scopus 로고
    • Role of the myosin assembly protein UNC-45 as a molecular chaperone for myosin
    • DOI 10.1126/science.1066648
    • Barral JM, Hutagalung AH, Brinker A, Hartl FU, Epstein HF. Role of the myosin assembly protein UNC-45 as a molecular chaperone for myosin. Science. 2002;295:669-671. (Pubitemid 34111823)
    • (2002) Science , vol.295 , Issue.5555 , pp. 669-671
    • Barral, J.M.1    Hutagalung, A.H.2    Brinker, A.3    Hartl, F.U.4    Epstein, H.F.5
  • 44
    • 0344527945 scopus 로고    scopus 로고
    • Unc-45 gene of Caenorhabditis elegans encodes a muscle-specific tetratricopeptide repeat-containing protein
    • DOI 10.1002/(SICI)1097-0169(1999)42:3<163::AID-CM1>3.0.CO;2-E
    • Venolia L, Ao W, Kim S, Kim C, Pilgrim D. Unc-45 gene of Caenorhabditis elegans encodes a muscle-specific tetratricopeptide repeatcontaining protein. Cell Motil Cytoskeleton. 1999;42:163-177. (Pubitemid 29142947)
    • (1999) Cell Motility and the Cytoskeleton , vol.42 , Issue.3 , pp. 163-177
    • Lee, V.1    Ao, W.2    Kim, S.3    Kim, C.4    Pilgrim, D.5
  • 45
    • 1842833926 scopus 로고    scopus 로고
    • Two mammalian UNC-45 isoforms are related to distinct cytoskeletal and muscle-specific functions
    • DOI 10.1242/jcs.00108
    • Price MG, Landsverk ML, Barral JM, Epstein HF. Two mammalian UNC-45 isoforms are related to distinct cytoskeletal and muscle-specific function. J Cell Sci. 2002;115:4013-4023. (Pubitemid 35446800)
    • (2002) Journal of Cell Science , vol.115 , Issue.21 , pp. 4013-4023
    • Price, M.G.1    Landsverk, M.L.2    Barral, J.M.3    Epstein, H.F.4
  • 46
    • 0034632070 scopus 로고    scopus 로고
    • The UNC-112 gene in Caenorhabditis elegans encodes a novel component of cell-matrix adhesion structures required for integrin localization in the muscle cell membrane
    • DOI 10.1083/jcb.150.1.253
    • Rogalski TM, Mullen GP, Gilbert MM, Williams BD, Moerman DG. The UNC-112 gene in Caenorhabditis elegans encodes a novel component of cell-matrix adhesion structures required for integrin localization in the muscle cell membrane. J Cell Biol. 2000;150:253-264. (Pubitemid 30480998)
    • (2000) Journal of Cell Biology , vol.150 , Issue.1 , pp. 253-264
    • Rogalski, T.M.1    Mullen, G.P.2    Gilbert, M.M.3    Williams, B.D.4    Moerman, D.G.5
  • 47
    • 0016063911 scopus 로고
    • The genetics of Caenorhabditis elegans
    • Brenner S. The genetics of Caenorhabditis elegans. Genetics. 1974;77: 71-94.
    • (1974) Genetics , vol.77 , pp. 71-94
    • Brenner, S.1
  • 52
    • 0020156343 scopus 로고
    • Mutations in the unc-54 myosin heavy chain gene of Caenorhabditis elegans that alter contractility but not muscle structure
    • Moerman DG, Plurad S, Waterston RH, Baillie DL. Mutations in the unc-54 myosin heavy chain gene of Caenorhabditis elegans that alter contractility but not muscle structure. Cell. 1982;29:773-781.
    • (1982) Cell , vol.29 , pp. 773-781
    • Moerman, D.G.1    Plurad, S.2    Waterston, R.H.3    Baillie, D.L.4
  • 53
    • 9444284320 scopus 로고    scopus 로고
    • The RNA-binding protein SUP-12 controls muscle-specific splicing of the ADF/cofilin pre-mRNA in C. elegans
    • DOI 10.1083/jcb.200407085
    • Anyanful A, Ono K, Johnsen RC, Ly H, Jensen V, Baillie DL, Ono S. The RNA-binding protein SUP-12 controls muscle-specific splicing of the ADF/cofilin pre-mRNA in C elegans. J Cell Biol. 2004;167: 639-647. (Pubitemid 39565145)
    • (2004) Journal of Cell Biology , vol.167 , Issue.4 , pp. 639-647
    • Anyanful, A.1    Ono, K.2    Johnsen, R.C.3    Ly, H.4    Jensen, V.5    Baillie, D.L.6    Ono, S.7
  • 54
    • 0022761252 scopus 로고
    • C elegans unc-105 mutations affect muscle and are suppressed by other mutations that affect muscle
    • Park EC, Horvitz HR. C elegans unc-105 mutations affect muscle and are suppressed by other mutations that affect muscle. Genetics. 1986; 113:853-867.
    • (1986) Genetics , vol.113 , pp. 853-867
    • Park, E.C.1    Horvitz, H.R.2
  • 55
    • 0029890657 scopus 로고    scopus 로고
    • Interaction between a putative mechanosensory membrane channel and a collagen
    • Liu J, Schrank B, Waterston RH. Interaction between a putative mechanosensory membrane channel and a collagen. Science. 1996;273: 361-364. (Pubitemid 26250265)
    • (1996) Science , vol.273 , Issue.5273 , pp. 361-364
    • Liu, J.1    Schrank, B.2    Waterston, R.H.3
  • 56
    • 57449110162 scopus 로고    scopus 로고
    • Computer-enhanced high-throughput genetic screens of C elegans in a microfluidic system
    • Crane MM, Chung K, Lu H. Computer-enhanced high-throughput genetic screens of C elegans in a microfluidic system. Lab Chip. 2009; 9:38-40.
    • (2009) Lab Chip , vol.9 , pp. 38-40
    • Crane, M.M.1    Chung, K.2    Lu, H.3
  • 58
    • 79952313987 scopus 로고    scopus 로고
    • PKN-1, a homologue of mammalian PKN, is involved in the regulation of muscle contraction and force transmission in C elegans
    • Qadota H, Miyauchi T, Nahabedian JF, Stirman JN, Lu H, Amano M, Benian GM, Kaibuchi K. PKN-1, a homologue of mammalian PKN, is involved in the regulation of muscle contraction and force transmission in C elegans. J Mol Biol. 2011;407:222-231.
    • (2011) J Mol Biol , vol.407 , pp. 222-231
    • Qadota, H.1    Miyauchi, T.2    Nahabedian, J.F.3    Stirman, J.N.4    Lu, H.5    Amano, M.6    Benian, G.M.7    Kaibuchi, K.8
  • 59
    • 4043096960 scopus 로고    scopus 로고
    • Regulation of the myosin-directed chaperone UNC-45 by a novel E3/E4-multiubiquitylation complex in C. elegans
    • DOI 10.1016/j.cell.2004.07.014, PII S0092867404007032
    • Hoppe T, Cassata G, Barral JM, Springer W, Hutagalung AH, Epstein HF, Baumeister R. Regulation of the myosin-directed chaperone UNC-45 by a novel E3/E4-multiubiquitylation complex in C elegans. Cell. 2004;118:337-349. (Pubitemid 39061114)
    • (2004) Cell , vol.118 , Issue.3 , pp. 337-349
    • Hoppe, T.1    Cassata, G.2    Barral, J.M.3    Springer, W.4    Hutagalung, A.H.5    Epstein, H.F.6    Baumeister, R.7
  • 60
    • 34247466028 scopus 로고    scopus 로고
    • The UNC-45 chaperone mediates sarcomere assembly through myosin degradation in Caenorhabditis elegans
    • DOI 10.1083/jcb.200607084
    • Landsverk ML, Li S, Hutagalung AH, Najafov A, Hoppe T, Barral JM, Epstein HF. The UNC-45 chaperone mediates sarcomere assembly through myosin degradation in Caenorhabditis elegans. J Cell Biol. 2007;177:205-210. (Pubitemid 46658632)
    • (2007) Journal of Cell Biology , vol.177 , Issue.2 , pp. 205-210
    • Landsverk, M.L.1    Li, S.2    Hutagalung, A.H.3    Najafov, A.4    Hoppe, T.5    Barral, J.M.6    Epstein, H.F.7
  • 61
    • 77649170228 scopus 로고    scopus 로고
    • Molecular basis of hereditary cardiomyopathy: Abnormalities in calcium sensitivity, stretch response, stress response and beyond
    • Kimura A. Molecular basis of hereditary cardiomyopathy: abnormalities in calcium sensitivity, stretch response, stress response and beyond. J Hum Gen. 2010;55:81-90.
    • (2010) J Hum Gen , vol.55 , pp. 81-90
    • Kimura, A.1
  • 62
    • 41949127144 scopus 로고    scopus 로고
    • Kindlin-2 is an essential component of intercalated discs and is required for vertebrate cardiac structure and function
    • DOI 10.1161/CIRCRESAHA.107.161489
    • Dowling JJ, Gibbs E, Russell M, Goldman D, Minarcik J, Golden JA, Feldman EL. Kindlin-2 is an essential component of intercalated discs and is required for vertebrate cardiac structure and function. Circ Res. 2008;102:423-431. (Pubitemid 351651103)
    • (2008) Circulation Research , vol.102 , Issue.4 , pp. 423-431
    • Dowling, J.J.1    Gibbs, E.2    Russell, M.3    Goldman, D.4    Minarcik, J.5    Golden, J.A.6    Feldman, E.L.7
  • 63
    • 0033545214 scopus 로고    scopus 로고
    • A conserved LIM protein that affects muscular adherens junction integrity and mechanosensory function in Caenorhabditis elegans
    • DOI 10.1083/jcb.144.1.45
    • Hobert O, Moerman DG, Clark KA, Beckerle MC, Ruvkun G. A conserved LIM protein that affects muscular adherens junction integrity and mechanosensory function in Caenorhabditis elegans. J Cell Biol. 1999;144:45-57. (Pubitemid 29047010)
    • (1999) Journal of Cell Biology , vol.144 , Issue.1 , pp. 45-57
    • Hobert, O.1    Moerman, D.G.2    Clark, K.A.3    Beckerle, M.C.4    Ruvkun, G.5
  • 65
    • 33847392824 scopus 로고    scopus 로고
    • The myosin co-chaperone UNC-45 is required for skeletal and cardiac muscle function in zebrafish
    • DOI 10.1016/j.ydbio.2006.11.027, PII S0012160606013790
    • Wohlgemuth SL, Crawford BD, Pilgrim DB. The myosin co-chaperone UNC-45 is required for skeletal and cardiac muscle function in zebrafish. Dev Biol. 2007;303:483-492. (Pubitemid 46341278)
    • (2007) Developmental Biology , vol.303 , Issue.2 , pp. 483-492
    • Wohlgemuth, S.L.1    Crawford, B.D.2    Pilgrim, D.B.3
  • 66
    • 34547103542 scopus 로고    scopus 로고
    • The UCS factor Steif/Unc-45b interacts with the heat shock protein Hsp90a during myofibrillogenesis
    • DOI 10.1016/j.ydbio.2007.05.014, PII S0012160607009104
    • Etard C, Behra M, Fischer N, Hutcheson D, Geisler R, Strähle U. The UCS factor Steif/Unc-45b interacts with the heat shock protein Hsp90a during myofibrillogenesis. Dev Biol. 2007;308:133-143. (Pubitemid 47096642)
    • (2007) Developmental Biology , vol.308 , Issue.1 , pp. 133-143
    • Etard, C.1    Behra, M.2    Fischer, N.3    Hutcheson, D.4    Geisler, R.5    Strahle, U.6
  • 67
    • 79960707770 scopus 로고    scopus 로고
    • The UNC-45 chaperone is critical for establishing myosin-based myofibrillar organization and cardiac contractility in the Drosophila heart model
    • Melkani GC, Bodmer R, Ocorr K, Bernstein SI. The UNC-45 chaperone is critical for establishing myosin-based myofibrillar organization and cardiac contractility in the Drosophila heart model. PLOS ONE. 2011; 7:e22579.
    • (2011) Plos One , vol.7
    • Melkani, G.C.1    Bodmer, R.2    Ocorr, K.3    Bernstein, S.I.4
  • 68
    • 74249111371 scopus 로고    scopus 로고
    • Caenorhabditis elegans unc-82 encodes a serine/threonine kinase important for myosin filament organization in muscle during growth
    • Hoppe PE, Chau J, Flanagan KA, Reedy AR, Schriefer LA. Caenorhabditis elegans unc-82 encodes a serine/threonine kinase important for myosin filament organization in muscle during growth. Genetics. 2010; 184:79-90.
    • (2010) Genetics , vol.184 , pp. 79-90
    • Hoppe, P.E.1    Chau, J.2    Flanagan, K.A.3    Reedy, A.R.4    Schriefer, L.A.5
  • 69
    • 0035872209 scopus 로고    scopus 로고
    • 2 subunit of AMP-activated protein kinase cause familial hypertrophic cardiomyopathy: Evidence for the central role of energy compromise in disease pathogenesis
    • Blair E, Redwood C, Ashrafian H, Oliveira M, Broxholme J, Kerr B, Salmon A, Ostman-Smith I, Watkins H. Mutations in the gamma (2) subunit of AMP-activated protein kinase cause familial hypertrophic cardiomyopathy: evidence for the central role of energy compromise in disease pathogenesis. Hum Mol Genet. 2001;10:1215-1220. (Pubitemid 32487544)
    • (2001) Human Molecular Genetics , vol.10 , Issue.11 , pp. 1215-1220
    • Blair, E.1    Redwood, C.2    Ashrafian, H.3    Oliveira, M.4    Broxholme, J.5    Kerr, B.6    Salmon, A.7    Ostman-Smith, I.8    Watkins, H.9
  • 70
    • 0034654362 scopus 로고    scopus 로고
    • Characterization of AMP-activated protein kinase γ-subunit isoforms and their role in AMP binding
    • DOI 10.1042/0264-6021:3460659
    • Cheung PC, Salt IP, Davies DG, Hardie DG, Carling D. Characterization of AMP-activated protein kinase gamma-subunit isoforms and their role in AMP binding. Biochem J. 2000;346:659-669. (Pubitemid 30171026)
    • (2000) Biochemical Journal , vol.346 , Issue.3 , pp. 659-669
    • Cheung, P.C.F.1    Salt, I.P.2    Davies, S.P.3    Hardie, D.G.4    Carling, D.5
  • 71
    • 63849162173 scopus 로고    scopus 로고
    • AMP-activated protein kinase: A core signaling pathway in the heart
    • Kim AS, Miller EJ, Young LH. AMP-activated protein kinase: a core signaling pathway in the heart. Acta Physiol (Oxf). 2009;196:37-53.
    • (2009) Acta Physiol (Oxf) , vol.196 , pp. 37-53
    • Kim, A.S.1    Miller, E.J.2    Young, L.H.3
  • 73
    • 0029848345 scopus 로고    scopus 로고
    • Twitchin and related giant Ig superfamily members of C. elegans and other invertebrates
    • DOI 10.1016/0065-227X(96)81674-1
    • Benian GM, Tang X, Tinley TL. Twitchin and related giant Ig superfamily members of C elegans and other invertebrates. Adv Biophys. 1996;33:183-197. (Pubitemid 26371191)
    • (1996) Advances in Biophysics , vol.33 , pp. 183-197
    • Benian, G.M.1    Tang, X.2    Tinley, T.L.3
  • 74
  • 75
    • 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 LA, Mercer KB, Stark TJ, Ferrara TM, Benian GM. A novel protein phosphatase is a binding partner for the protein kinase domains of UNC-89 (Obscurin) in Caenorhabditis elegans. Mol Biol Cell. 2008a;19:2424-2432.
    • (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
  • 76
    • 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, Benian GM. The DH-PH region of the giant protein UNC-89 activates RHO-1 GTPase in Caenorhabditis elegans body wall muscle. J Mol Biol. 2008b;383:747-752.
    • (2008) J Mol Biol , vol.383 , pp. 747-752
    • Qadota, H.1    Blangy, A.2    Xiong, G.3    Benian, G.M.4
  • 77
    • 60149098024 scopus 로고    scopus 로고
    • A LIM-9 (FHL)/SCPL-1 (SCP) complex interacts with the C-terminal protein kinase regions of UNC-89 (obscurin) in C elegans muscle
    • Xiong G, Qadota H, Mercer KB, McGaha LA, Oberhauser AF, Benian GM. A LIM-9 (FHL)/SCPL-1 (SCP) complex interacts with the C-terminal protein kinase regions of UNC-89 (obscurin) in C elegans muscle. J Mol Biol. 2009;386:976-988.
    • (2009) J Mol Biol , vol.386 , pp. 976-988
    • Xiong, G.1    Qadota, H.2    Mercer, K.B.3    McGaha, L.A.4    Oberhauser, A.F.5    Benian, G.M.6
  • 78
    • 39749137483 scopus 로고    scopus 로고
    • Sense and stretchability: The role of titin and titin-associated proteins in myocardial stress-sensing and mechanical dysfunction
    • DOI 10.1016/j.cardiores.2007.03.029
    • Linke WA. Sense and stretchability: The role of titin and titin-associated proteins in myocardial stress-sensing and mechanical dysfunction. Cardiovas Res. 2008;77:637-648. (Pubitemid 351301882)
    • (2008) Cardiovascular Research , vol.77 , Issue.4 , pp. 637-648
    • Linke, W.A.1
  • 80
    • 0036623918 scopus 로고    scopus 로고
    • Cardiac titin: An adjustable multi-functional spring
    • DOI 10.1113/jphysiol.2001.014381
    • Granzier H, Labeit S. Cardiac titin: an adjustable multi-functional spring. J Physiol. 2002;541:335-342. (Pubitemid 35190203)
    • (2002) Journal of Physiology , vol.541 , Issue.2 , pp. 335-342
    • Granzier, H.1    Labeit, S.2
  • 82
    • 30444458378 scopus 로고    scopus 로고
    • From A to Z and back? Multicompartment proteins in the sarcomere
    • DOI 10.1016/j.tcb.2005.11.007, PII S0962892405003028
    • Lange S, Ehler E, Gautel M. From A to Z and back? Multicompartment proteins in the sarcomere. Trends Cell Biol. 2006;16:11-18. (Pubitemid 43077090)
    • (2006) Trends in Cell Biology , vol.16 , Issue.1 , pp. 11-18
    • Lange, S.1    Ehler, E.2    Gautel, M.3
  • 83
    • 8744221697 scopus 로고    scopus 로고
    • Properties of titin immunoglobulin and fibronectin-3 domains
    • DOI 10.1074/jbc.R400023200
    • Tskhovrebova L, Trinick J. Properties of titin immunoglobulin and fibronectin-3 domains. J Biol Chem. 2004;279:46351-46354. (Pubitemid 39518273)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.45 , pp. 46351-46354
    • Tskhovrebova, L.1    Trinick, J.2
  • 84
    • 0026582867 scopus 로고
    • Towards a molecular understanding of titin
    • Labeit S, Gautel M, Lakey A, Trinick J. Towards a molecular understanding of titin. EMBO J. 1992;11:1711-1716.
    • (1992) EMBO J , vol.11 , pp. 1711-1716
    • Labeit, S.1    Gautel, M.2    Lakey, A.3    Trinick, J.4
  • 85
    • 0027536473 scopus 로고
    • A survey of interactions made by the giant protein titin
    • Soteriou A, Gamage M, Trinick J. A survey of interactions made by the giant protein titin. J Cell Sci. 1993;104:119-123. (Pubitemid 23073174)
    • (1993) Journal of Cell Science , vol.104 , Issue.1 , pp. 119-123
    • Soteriou, A.1    Gamage, M.2    Trinick, J.3
  • 86
    • 0029593486 scopus 로고
    • Studies of the interaction between titin and myosin
    • DOI 10.1083/jcb.131.6.1471
    • Houmeida A, Holt J, Tskhovrebova L, Trinick J. Studies of the interaction between titin and myosin. J Cell Biol. 1995;131:1471-1481. (Pubitemid 26001751)
    • (1995) Journal of Cell Biology , vol.131 , Issue.6 , pp. 1471-1481
    • Houmeida, A.1    Holt, J.2    Tskhovrebova, L.3    Trinick, J.4
  • 87
    • 0026672810 scopus 로고
    • Studies on the interaction between titin and myosin
    • Wang SM, Jeng CJ, Sun MC. Studies on the interaction between titin and myosin. Histol Histopathol. 1992;7:333-337.
    • (1992) Histol Histopathol , vol.7 , pp. 333-337
    • Wang, S.M.1    Jeng, C.J.2    Sun, M.C.3
  • 88
    • 0035914471 scopus 로고    scopus 로고
    • Structural and Functional Studies of Titin's fn3 Modules Reveal Conserved Surface Patterns and Binding to Myosin S1 - A Possible Role in the Frank-Starling Mechanism of the Heart
    • DOI 10.1006/jmbi.2001.5017, PII S002228360195017X
    • Muhle-Goll C, Habeck M, Cazorla O, Nilges M, Labeit S, Granzier H. Structural and functional studies of titin's fn3 modules reveal conserved surface patterns and binding to myosin S1: a possible role in the Frank-Starling mechanism of the heart. J Mol Biol. 2001;313:431-447. (Pubitemid 33587198)
    • (2001) Journal of Molecular Biology , vol.313 , Issue.2 , pp. 431-447
    • Muhle-Goll, C.1    Habeck, M.2    Cazorla, O.3    Nilges, M.4    Labeit, S.5    Granzier, H.6
  • 89
    • 0028824480 scopus 로고
    • Titins: Giant proteins in charge of muscle ultrastructure and elasticity
    • Labeit S, Kolmerer B. Titins: giant proteins in charge of muscle ultrastructure and elasticity. Science. 1995;270:293-296.
    • (1995) Science , vol.270 , pp. 293-296
    • Labeit, S.1    Kolmerer, B.2
  • 92
    • 0025246301 scopus 로고
    • Isolation and characterization of a cDNA clone encoding avian skeletal muscle C-protein: An intracellular member of the immunoglobulin superfamily
    • Einheber S, Fischman DA. Isolation and characterization of a cDNA clone encoding avian skeletal muscle C-protein: an intracellular member of the immunoglobulin superfamily. Proc Natl Acad Sci USA. 1990; 87:2157-2161.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 2157-2161
    • Einheber, S.1    Fischman, D.A.2
  • 94
    • 0021259458 scopus 로고
    • Localization of C-protein isoforms in chicken skeletal muscle: Ultrastructural detection using monoclonal antibodies
    • Dennis JE, Shimizu T, Reinach FC, Fischman DA. Localization of C-protein isoforms in chicken skeletal muscle: ultrastructural detection using monoclonal antibodies. J Cell Biol. 1984;98:1514-1522. (Pubitemid 14126981)
    • (1984) Journal of Cell Biology , vol.98 , Issue.4 , pp. 1514-1522
    • Dennis, J.E.1    Shimizu, T.2    Reinach, F.C.3    Fischman, D.A.4
  • 97
    • 0032609762 scopus 로고    scopus 로고
    • The C-protein (myosin binding protein C) family: Regulators of contraction and sarcomere formation?
    • Bennett PM, Furst DO, Gautel M. The C-protein (myosin binding protein C) family: regulators of contraction and sarcomere formation? Rev Physiol Biochem Pharm. 1999;138:203-234.
    • (1999) Rev Physiol Biochem Pharm , vol.138 , pp. 203-234
    • Bennett, P.M.1    Furst, D.O.2    Gautel, M.3
  • 98
    • 0021964531 scopus 로고
    • Myosin and paramyosin are organized about a newly identified core structure
    • Epstein HF, Miller DM, Ortiz I, Berliner GC. Myosin and paramyosin are organized about a newly identified core structure. J Cell Biol. 1985;100:905-915.
    • (1985) J Cell Biol , vol.100 , pp. 905-915
    • Epstein, H.F.1    Miller, D.M.2    Ortiz, I.3    Berliner, G.C.4
  • 99
    • 0027515217 scopus 로고
    • The major myosin-binding domain of skeletal muscle MyBP-C (C protein) resides in the COOH-terminal, immunoglobulin C2 motif
    • DOI 10.1083/jcb.123.3.619
    • Okagaki T, Weber FE, Fischman DA, Vaughan KT, Mikawa T, Reinach FC. The major myosin-binding domain of skeletal muscle MyBP-C (C protein) resides in the COOH-terminal, immunoglobulin C2 motif. J Cell Biol. 1993;123:619-626. (Pubitemid 23324919)
    • (1993) Journal of Cell Biology , vol.123 , Issue.3 , pp. 619-626
    • Okagaki, T.1    Weber, F.E.2    Fischman, D.A.3    Vaughan, K.T.4    Mikawa, T.5    Reinach, F.C.6
  • 103
    • 0018126953 scopus 로고
    • The binding of skeletal muscle C-protein to F-actin, and its relation to the interaction of actin with myosin subfragment-1
    • Moos C, Mason CM, Besterman JM, Feng IM, Dubin JH. The binding of skeletal muscle C-protein to F-actin and its relation to the interaction of actin with myosin subfragment-1. J Mol Biol. 1978;124:571-586. (Pubitemid 9034571)
    • (1978) Journal of Molecular Biology , vol.124 , Issue.5 , pp. 571-586
    • Moos, C.1    Mason, C.M.2    Besterman, J.M.3
  • 104
    • 0042093724 scopus 로고    scopus 로고
    • Structural evidence for the interaction of C-protein (MyBP-C) with actin and sequence identification of a possible actin-binding domain
    • DOI 10.1016/S0022-2836(03)00781-2
    • Squire JM, Luther PK, Knupp C. Structural evidence for the interaction of C-protein (MyBP-C) with actin and sequence identification of a possible actin-binding domain. J Mol Biol. 2003;331:713-724. (Pubitemid 36937155)
    • (2003) Journal of Molecular Biology , vol.331 , Issue.3 , pp. 713-724
    • Squire, J.M.1    Luther, P.K.2    Knupp, C.3
  • 105
    • 33846021648 scopus 로고    scopus 로고
    • Effects of the N-terminal domains of myosin binding protein-C in an in vitro motility assay: Evidence for long-lived cross-bridges
    • DOI 10.1074/jbc.M606949200
    • Razumova MV, Shaffer JF, Tu A-Y, Flint GV, Regnier M, Harris SP. Effects of the N-terminal domains of myosin binding protein-C in an in vitro motility assay. J Biol Chem. 2006;281:35846-35854. (Pubitemid 46041316)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.47 , pp. 35846-35854
    • Razumova, M.V.1    Shaffer, J.F.2    Tu, A.-Y.3    Flint, G.V.4    Regnier, M.5    Harris, S.P.6
  • 106
    • 79952454934 scopus 로고    scopus 로고
    • Binding of the N-terminal fragment C0-C2 of cardiac MyBP-C to cardiac F-actin
    • Kensler RW, Shaffer JF, Harris SP. Binding of the N-terminal fragment C0-C2 of cardiac MyBP-C to cardiac F-actin. J Struct Biol. 2011;174: 44-51.
    • (2011) J Struct Biol , vol.174 , pp. 44-51
    • Kensler, R.W.1    Shaffer, J.F.2    Harris, S.P.3
  • 108
    • 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
    • DOI 10.1016/S0022-2836(02)00970-1
    • Flaherty DB, Gernert KM, Shmeleva N, Tang X, Mercer KB, Borodovsky M, Benian GM. Titins in C elegans with unusual features: coiled-coil domains, novel regulation of kinase activity and two new possible elastic regions. J Mol Biol. 2002;323:533-549. (Pubitemid 35283678)
    • (2002) Journal of Molecular Biology , vol.323 , Issue.3 , 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
  • 109
    • 77952318258 scopus 로고    scopus 로고
    • Extensive and modular intrinsically disordered segments in C elegans TTN-1 and implications in filament binding, elasticity and oblique striation
    • Forbes JG, Flaherty DB, Ma K, Qadota H, Benian GM, Wang K. Extensive and modular intrinsically disordered segments in C elegans TTN-1 and implications in filament binding, elasticity and oblique striation. J Mol Biol. 2010;398:672-689.
    • (2010) J Mol Biol , vol.398 , pp. 672-689
    • Forbes, J.G.1    Flaherty, D.B.2    Ma, K.3    Qadota, H.4    Benian, G.M.5    Wang, K.6
  • 110
    • 0032616278 scopus 로고    scopus 로고
    • The genetics and molecular biology of the titin/connectin-like proteins of invertebrates
    • Benian GM, Ayme-Southgate A, Tinley TL. The genetics and molecular biology of the titin/connectin-like proteins of invertebrates. Rev Physiol Biochem Pharm. 1999;138:235-268.
    • (1999) Rev Physiol Biochem Pharm , vol.138 , pp. 235-268
    • Benian, G.M.1    Ayme-Southgate, A.2    Tinley, T.L.3
  • 112
    • 33745712384 scopus 로고    scopus 로고
    • Titin/connectin-related proteins in C elegans: A review and new findings
    • Ferrara TM, Flaherty DB, Benian GM. Titin/connectin-related proteins in C elegans: a review and new findings. J Muscle Res Cell Motil. 2005;26:435-447.
    • (2005) J Muscle Res Cell Motil , vol.26 , pp. 435-447
    • Ferrara, T.M.1    Flaherty, D.B.2    Benian, G.M.3
  • 113
    • 33745726378 scopus 로고    scopus 로고
    • Complete human gene structure of obscurin: Implications for isoform generation by differential splicing
    • Fukuzawa A, Idowu S, Gautel M. Complete human gene structure of obscurin: implications for isoform generation by differential splicing. J Muscle Res Cell Motil. 2005;26:427-434.
    • (2005) J Muscle Res Cell Motil , vol.26 , pp. 427-434
    • Fukuzawa, A.1    Idowu, S.2    Gautel, M.3
  • 115
    • 70349342804 scopus 로고    scopus 로고
    • The rho-guanine nucleotide exchange domain of obscurin activates rhoA signaling in skeletal muscle
    • Ford-Speelman DL, Roche JA, Bowman AL, Bloch RJ. The rho-guanine nucleotide exchange domain of obscurin activates rhoA signaling in skeletal muscle. Mol Biol Cell. 2009;20:3905-3917.
    • (2009) Mol Biol Cell , vol.20 , pp. 3905-3917
    • Ford-Speelman, D.L.1    Roche, J.A.2    Bowman, A.L.3    Bloch, R.J.4
  • 117
    • 0033005291 scopus 로고    scopus 로고
    • The effects of the selective ROCK inhibitor, Y27632, on ET-1-induced hypertrophic response in neonatal rat cardiac myocytes - Possible involvement of Rho/ROCK pathway in cardiac muscle cell hypertrophy
    • DOI 10.1016/S0014-5793(99)00680-8, PII S0014579399006808
    • Kuwahara K, Saito Y, Nakagawa O, Kishimoto I, Harada M, Ogawa E, Miyamoto Y, Hamanaka I, Kajiyama N, Takahashi N, Izumi T, Kawakami R, Tamura N, Ogawa Y, Nakao K. The effects of the selective ROCK inhibitor, Y27632, on ET-1-induced hypertrophic response in neonatal rat cardiac myocytes: possible involvement of Rho/ROCK pathway in cardiac muscle cell hypertrophy. FEBS Lett. 1999;452:314-318. (Pubitemid 29301767)
    • (1999) FEBS Letters , vol.452 , Issue.3 , pp. 314-318
    • Kuwahara, K.1    Saito, Y.2    Nakagawa, O.3    Kishimoto, I.4    Harada, M.5    Ogawa, E.6    Miyamoto, Y.7    Hamanaka, I.8    Kajiyama, N.9    Takahashi, N.10    Izumi, T.11    Kawakami, R.12    Tamura, N.13    Ogawa, Y.14    Nakao, K.15
  • 122
    • 0018036480 scopus 로고
    • Muscle development in Caenorhabditis elegans: Mutants exhibiting retarded sarcomere construction
    • Mackenzie JM, Garcea RL, Zengel JM, Epstein HF. Muscle development in Caenorhabditis elegans: mutants exhibiting retarded sarcomere construction. Cell. 1978;15:751-762.
    • (1978) Cell , vol.15 , pp. 751-762
    • MacKenzie, J.M.1    Garcea, R.L.2    Zengel, J.M.3    Epstein, H.F.4


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