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Volumn 13, Issue 2, 2011, Pages 151-162

Identification and Analysis of Muscle-Related Protein Isoforms Expressed in the White Muscle of the Mandarin Fish (Siniperca chuatsi)

Author keywords

ESTs; Isoforms; Mandarin fish; Muscle protein; White muscle

Indexed keywords

ESTS; ISOFORMS; MANDARIN FISH; MUSCLE PROTEIN; WHITE MUSCLE;

EID: 79955533260     PISSN: 14362228     EISSN: None     Source Type: Journal    
DOI: 10.1007/s10126-010-9275-1     Document Type: Article
Times cited : (38)

References (69)
  • 1
    • 12144286775 scopus 로고    scopus 로고
    • Up-regulation of muscle-specific transcription factors during embryonic somitogenesis of zebrafish (Danio rerio) by knock-down of myostatin-1
    • Amali AA, Lin CJ, Chen YH, Wang WL, Gong HY, Lee CY, Ko YL, Lu JK, Her GM, Chen TT, Wu JL (2004) Up-regulation of muscle-specific transcription factors during embryonic somitogenesis of zebrafish (Danio rerio) by knock-down of myostatin-1. Dev Dyn 229: 847-856.
    • (2004) Dev Dyn , vol.229 , pp. 847-856
    • Amali, A.A.1    Lin, C.J.2    Chen, Y.H.3    Wang, W.L.4    Gong, H.Y.5    Lee, C.Y.6    Ko, Y.L.7    Lu, J.K.8    Her, G.M.9    Chen, T.T.10    Wu, J.L.11
  • 3
    • 0033939421 scopus 로고    scopus 로고
    • Calcium ion in skeletal muscle: its crucial role for muscle function, plasticity, and disease
    • Berchtold MW, Brinkmeier H, Muntener M (2000) Calcium ion in skeletal muscle: its crucial role for muscle function, plasticity, and disease. Physiol Rev 80: 1215-1265.
    • (2000) Physiol Rev , vol.80 , pp. 1215-1265
    • Berchtold, M.W.1    Brinkmeier, H.2    Muntener, M.3
  • 4
    • 0037166257 scopus 로고    scopus 로고
    • Exon skipping in cardiac troponin T of turkeys with inherited dilated cardiomyopathy
    • Biesiadecki BJ, Jin JP (2002) Exon skipping in cardiac troponin T of turkeys with inherited dilated cardiomyopathy. J Biol Chem 277: 18459-18468.
    • (2002) J Biol Chem , vol.277 , pp. 18459-18468
    • Biesiadecki, B.J.1    Jin, J.P.2
  • 6
    • 27144498186 scopus 로고    scopus 로고
    • Identification and analysis of teleost slow muscle troponin T (sTnT) and intronless TnT genes
    • Campinho MA, Power DM, Sweeney GE (2005) Identification and analysis of teleost slow muscle troponin T (sTnT) and intronless TnT genes. Gene 361: 67-79.
    • (2005) Gene , vol.361 , pp. 67-79
    • Campinho, M.A.1    Power, D.M.2    Sweeney, G.E.3
  • 7
    • 14644430375 scopus 로고    scopus 로고
    • Troponin T expression in trout red muscle correlates with muscle activation
    • Coughlin DJ, Caputo ND, Bohnert KL, Weaver FE (2005) Troponin T expression in trout red muscle correlates with muscle activation. J Exp Biol 208: 409-417.
    • (2005) J Exp Biol , vol.208 , pp. 409-417
    • Coughlin, D.J.1    Caputo, N.D.2    Bohnert, K.L.3    Weaver, F.E.4
  • 9
    • 0024292932 scopus 로고
    • Crystal structure determination and refinement of pike 4.10 parvalbumin (minor component from Esox lucius)
    • Declercq JP, Tinant B, Parello J, Etienne G, Huber R (1988) Crystal structure determination and refinement of pike 4. 10 parvalbumin (minor component from Esox lucius). J Mol Biol 202: 349-353.
    • (1988) J Mol Biol , vol.202 , pp. 349-353
    • Declercq, J.P.1    Tinant, B.2    Parello, J.3    Etienne, G.4    Huber, R.5
  • 10
    • 3042666256 scopus 로고    scopus 로고
    • MUSCLE: multiple sequence alignment with high accuracy and high throughput
    • Edgar RC (2004) MUSCLE: multiple sequence alignment with high accuracy and high throughput. Nucleic Acids Res 32: 1792-1797.
    • (2004) Nucleic Acids Res , vol.32 , pp. 1792-1797
    • Edgar, R.C.1
  • 11
    • 0029031198 scopus 로고
    • The troponin complex and regulation of muscle contraction
    • Farah CS, Reinach FC (1995) The troponin complex and regulation of muscle contraction. Faseb J 9: 755-767.
    • (1995) Faseb J , vol.9 , pp. 755-767
    • Farah, C.S.1    Reinach, F.C.2
  • 12
    • 58549088169 scopus 로고    scopus 로고
    • Myosin heavy chain genes expressed in juvenile and adult silver carp Hypopthalmichthys molitrix: Novel fast-type myosin heavy chain genes of silver carp
    • Fukushima H, Ikeda D, Tao Y, Watabe S (2009) Myosin heavy chain genes expressed in juvenile and adult silver carp Hypopthalmichthys molitrix: novel fast-type myosin heavy chain genes of silver carp. Gene 432: 102-111.
    • (2009) Gene , vol.432 , pp. 102-111
    • Fukushima, H.1    Ikeda, D.2    Tao, Y.3    Watabe, S.4
  • 13
    • 0036018453 scopus 로고    scopus 로고
    • Beating the cold: the functional evolution of troponin C in teleost fish
    • Gillis TE, Tibbits GF (2002) Beating the cold: the functional evolution of troponin C in teleost fish. Comp Biochem Physiol A Mol Integr Physiol 132: 763-772.
    • (2002) Comp Biochem Physiol A Mol Integr Physiol , vol.132 , pp. 763-772
    • Gillis, T.E.1    Tibbits, G.F.2
  • 14
    • 37449015457 scopus 로고    scopus 로고
    • Functional and evolutionary relationships of troponin C
    • Gillis TE, Marshall CR, Tibbits GF (2007) Functional and evolutionary relationships of troponin C. Physiol Genomics 32: 16-27.
    • (2007) Physiol Genomics , vol.32 , pp. 16-27
    • Gillis, T.E.1    Marshall, C.R.2    Tibbits, G.F.3
  • 15
    • 0033583079 scopus 로고    scopus 로고
    • Specialized conservation of surface loops of myosin: evidence that loops are involved in determining functional characteristics
    • Goodson HV, Warrick HM, Spudich JA (1999) Specialized conservation of surface loops of myosin: evidence that loops are involved in determining functional characteristics. J Mol Biol 287: 173-185.
    • (1999) J Mol Biol , vol.287 , pp. 173-185
    • Goodson, H.V.1    Warrick, H.M.2    Spudich, J.A.3
  • 16
    • 0031955116 scopus 로고    scopus 로고
    • Consed: a graphical tool for sequence finishing
    • Gordon D, Abajian C, Green P (1998) Consed: a graphical tool for sequence finishing. Genome Res 8: 195-202.
    • (1998) Genome Res , vol.8 , pp. 195-202
    • Gordon, D.1    Abajian, C.2    Green, P.3
  • 18
    • 4243073122 scopus 로고    scopus 로고
    • Hedgehog regulation of superficial slow muscle fibres in Xenopus and the evolution of tetrapod trunk myogenesis
    • Grimaldi A, Tettamanti G, Martin BL, Gaffield W, Pownall ME, Hughes SM (2004) Hedgehog regulation of superficial slow muscle fibres in Xenopus and the evolution of tetrapod trunk myogenesis. Development 131: 3249-3262.
    • (2004) Development , vol.131 , pp. 3249-3262
    • Grimaldi, A.1    Tettamanti, G.2    Martin, B.L.3    Gaffield, W.4    Pownall, M.E.5    Hughes, S.M.6
  • 19
    • 0027993246 scopus 로고
    • Myosin subfragment-1 isoforms having different heavy chain structures from fast skeletal muscle of thermally acclimated carp
    • Guo XF, Nakaya M, Watabe S (1994) Myosin subfragment-1 isoforms having different heavy chain structures from fast skeletal muscle of thermally acclimated carp. J Biochem 116: 728-735.
    • (1994) J Biochem , vol.116 , pp. 728-735
    • Guo, X.F.1    Nakaya, M.2    Watabe, S.3
  • 20
    • 0027959627 scopus 로고
    • Binding of the amino-terminal region of myosin alkali 1 light chain to actin and its effect on actin-myosin interaction
    • Hayashibara T, Miyanishi T (1994) Binding of the amino-terminal region of myosin alkali 1 light chain to actin and its effect on actin-myosin interaction. Biochemistry 33: 12821-12827.
    • (1994) Biochemistry , vol.33 , pp. 12821-12827
    • Hayashibara, T.1    Miyanishi, T.2
  • 21
    • 0032191560 scopus 로고    scopus 로고
    • Two types of mRNA encoding myosin regulatory light chain in carp fast skeletal muscle differ in their 3′ non-coding regions and expression patterns following temperature acclimation
    • Hirayama Y, Kobiyama A, Ochiai Y, Watabe S (1998) Two types of mRNA encoding myosin regulatory light chain in carp fast skeletal muscle differ in their 3′ non-coding regions and expression patterns following temperature acclimation. J Exp Biol 201: 2815-2820.
    • (1998) J Exp Biol , vol.201 , pp. 2815-2820
    • Hirayama, Y.1    Kobiyama, A.2    Ochiai, Y.3    Watabe, S.4
  • 22
    • 0034607138 scopus 로고    scopus 로고
    • Structure-function relationships of the two surface loops of myosin heavy chain isoforms from thermally acclimated carp
    • Hirayama Y, Sutoh K, Watabe S (2000) Structure-function relationships of the two surface loops of myosin heavy chain isoforms from thermally acclimated carp. Biochem Biophys Res Commun 269: 237-241.
    • (2000) Biochem Biophys Res Commun , vol.269 , pp. 237-241
    • Hirayama, Y.1    Sutoh, K.2    Watabe, S.3
  • 23
    • 0032849859 scopus 로고    scopus 로고
    • CAP3: a DNA sequence assembly program
    • Huang X, Madan A (1999) CAP3: a DNA sequence assembly program. Genome Res 9: 868-877.
    • (1999) Genome Res , vol.9 , pp. 868-877
    • Huang, X.1    Madan, A.2
  • 24
    • 0017593105 scopus 로고
    • Isolation and characterization of the three light chains from carp white muscle myosin
    • Huriaux F, Focant B (1977) Isolation and characterization of the three light chains from carp white muscle myosin. Arch Int Physiol Biochim 85: 917-929.
    • (1977) Arch Int Physiol Biochim , vol.85 , pp. 917-929
    • Huriaux, F.1    Focant, B.2
  • 25
    • 0031019058 scopus 로고    scopus 로고
    • cDNA cloning of myosin heavy chain isoforms from carp fast skeletal muscle and their gene expression associated with temperature acclimation
    • Imai J, Hirayama Y, Kikuchi K, Kakinuma M, Watabe S (1997) cDNA cloning of myosin heavy chain isoforms from carp fast skeletal muscle and their gene expression associated with temperature acclimation. J Exp Biol 200: 27-34.
    • (1997) J Exp Biol , vol.200 , pp. 27-34
    • Imai, J.1    Hirayama, Y.2    Kikuchi, K.3    Kakinuma, M.4    Watabe, S.5
  • 26
    • 34250818777 scopus 로고    scopus 로고
    • Sequence, annotation and developmental expression of the sea urchin Ca(2+) -ATPase family
    • Jayantha Gunaratne H, Vacquier VD (2007) Sequence, annotation and developmental expression of the sea urchin Ca(2+) -ATPase family. Gene 397: 67-75.
    • (2007) Gene , vol.397 , pp. 67-75
    • Jayantha Gunaratne, H.1    Vacquier, V.D.2
  • 27
    • 0034718455 scopus 로고    scopus 로고
    • Modulation of troponin T molecular conformation and flexibility by metal ion binding to the NH2-terminal variable region
    • Jin JP, Root DD (2000) Modulation of troponin T molecular conformation and flexibility by metal ion binding to the NH2-terminal variable region. Biochemistry 39: 11702-11713.
    • (2000) Biochemistry , vol.39 , pp. 11702-11713
    • Jin, J.P.1    Root, D.D.2
  • 28
    • 0033696205 scopus 로고    scopus 로고
    • Conformational modulation of slow skeletal muscle troponin T by an NH(2)-terminal metal-binding extension
    • Jin JP, Chen A, Ogut O, Huang QQ (2000) Conformational modulation of slow skeletal muscle troponin T by an NH(2)-terminal metal-binding extension. Am J Physiol Cell Physiol 279: C1067-1077.
    • (2000) Am J Physiol Cell Physiol , vol.279
    • Jin, J.P.1    Chen, A.2    Ogut, O.3    Huang, Q.Q.4
  • 29
    • 0014144052 scopus 로고
    • 3-methylhistidine in actin and other muscle proteins
    • Johnson P, Harris CI, Perry SV (1967) 3-methylhistidine in actin and other muscle proteins. Biochem J 105: 361-370.
    • (1967) Biochem J , vol.105 , pp. 361-370
    • Johnson, P.1    Harris, C.I.2    Perry, S.V.3
  • 30
    • 0033930401 scopus 로고    scopus 로고
    • Differential scanning calorimetry of light meromyosin fragments having various lengths of carp fast skeletal muscle isoforms
    • Kakinuma M, Hatanaka A, Fukushima H, Nakaya M, Maeda K, Doi Y, Ooi T, Watabe S (2000a) Differential scanning calorimetry of light meromyosin fragments having various lengths of carp fast skeletal muscle isoforms. J Biochem 128: 11-20.
    • (2000) J Biochem , vol.128 , pp. 11-20
    • Kakinuma, M.1    Hatanaka, A.2    Fukushima, H.3    Nakaya, M.4    Maeda, K.5    Doi, Y.6    Ooi, T.7    Watabe, S.8
  • 31
    • 0033930401 scopus 로고    scopus 로고
    • Differential scanning calorimetry of light meromyosin fragments having various lengths of carp fast skeletal muscle isoforms
    • Kakinuma M, Hatanaka A, Fukushima H, Nakaya M, Maeda K, Doi Y, Ooi T, Watabe S (2000b) Differential scanning calorimetry of light meromyosin fragments having various lengths of carp fast skeletal muscle isoforms. J Biochem (Tokyo) 128: 11-20.
    • (2000) J Biochem (Tokyo) , vol.128 , pp. 11-20
    • Kakinuma, M.1    Hatanaka, A.2    Fukushima, H.3    Nakaya, M.4    Maeda, K.5    Doi, Y.6    Ooi, T.7    Watabe, S.8
  • 32
    • 0033522188 scopus 로고    scopus 로고
    • Characterization of the carp myosin heavy chain multigene family
    • Kikuchi K, Muramatsu M, Hirayama Y, Watabe S (1999) Characterization of the carp myosin heavy chain multigene family. Gene 228: 189-196.
    • (1999) Gene , vol.228 , pp. 189-196
    • Kikuchi, K.1    Muramatsu, M.2    Hirayama, Y.3    Watabe, S.4
  • 37
    • 2442671523 scopus 로고    scopus 로고
    • Evolution of sarcomeric myosin heavy chain genes: evidence from fish
    • McGuigan K, Phillips PC, Postlethwait JH (2004) Evolution of sarcomeric myosin heavy chain genes: evidence from fish. Mol Biol Evol 21: 1042-1056.
    • (2004) Mol Biol Evol , vol.21 , pp. 1042-1056
    • McGuigan, K.1    Phillips, P.C.2    Postlethwait, J.H.3
  • 38
    • 23144455729 scopus 로고    scopus 로고
    • OrfPredictor: predicting protein-coding regions in EST-derived sequences
    • Min XJ, Butler G, Storms R, Tsang A (2005a) OrfPredictor: predicting protein-coding regions in EST-derived sequences. Nucleic Acids Res 33: W677-680.
    • (2005) Nucleic Acids Res , vol.33
    • Min, X.J.1    Butler, G.2    Storms, R.3    Tsang, A.4
  • 39
    • 23144435719 scopus 로고    scopus 로고
    • TargetIdentifier: a webserver for identifying full-length cDNAs from EST sequences
    • Min XJ, Butler G, Storms R, Tsang A (2005b) TargetIdentifier: a webserver for identifying full-length cDNAs from EST sequences. Nucleic Acids Res 33: W669-672.
    • (2005) Nucleic Acids Res , vol.33
    • Min, X.J.1    Butler, G.2    Storms, R.3    Tsang, A.4
  • 40
    • 0029894659 scopus 로고    scopus 로고
    • Green fluorescent protein marks skeletal muscle in murine cell lines and zebrafish
    • Moss JB, Price AL, Raz E, Driever W, Rosenthal N (1996) Green fluorescent protein marks skeletal muscle in murine cell lines and zebrafish. Gene 173: 89-98.
    • (1996) Gene , vol.173 , pp. 89-98
    • Moss, J.B.1    Price, A.L.2    Raz, E.3    Driever, W.4    Rosenthal, N.5
  • 41
    • 84934435729 scopus 로고    scopus 로고
    • Structural basis for calcium-regulated relaxation of striated muscles at interaction sites of troponin with actin and tropomyosin
    • Murakami K, Yumoto F, Ohki SY, Yasunaga T, Tanokura M, Wakabayashi T (2007) Structural basis for calcium-regulated relaxation of striated muscles at interaction sites of troponin with actin and tropomyosin. Adv Exp Med Biol 592: 71-86.
    • (2007) Adv Exp Med Biol , vol.592 , pp. 71-86
    • Murakami, K.1    Yumoto, F.2    Ohki, S.Y.3    Yasunaga, T.4    Tanokura, M.5    Wakabayashi, T.6
  • 42
    • 0344132053 scopus 로고    scopus 로고
    • Relation of nebulin and connectin (titin) to dynamics of actin in nascent myofibrils of cultured skeletal muscle cells
    • Nwe TM, Maruyama K, Shimada Y (1999) Relation of nebulin and connectin (titin) to dynamics of actin in nascent myofibrils of cultured skeletal muscle cells. Exp Cell Res 252: 33-40.
    • (1999) Exp Cell Res , vol.252 , pp. 33-40
    • Nwe, T.M.1    Maruyama, K.2    Shimada, Y.3
  • 44
    • 67649371176 scopus 로고    scopus 로고
    • Structure and orientation of troponin in the thin filament
    • Paul DM, Morris EP, Kensler RW, Squire JM (2009) Structure and orientation of troponin in the thin filament. J Biol Chem 284: 15007-15015.
    • (2009) J Biol Chem , vol.284 , pp. 15007-15015
    • Paul, D.M.1    Morris, E.P.2    Kensler, R.W.3    Squire, J.M.4
  • 45
    • 0021679054 scopus 로고
    • Fast skeletal muscle myosin light chains 1 and 3 are produced from a single gene by a combined process of differential RNA transcription and splicing
    • Periasamy M, Strehler EE, Garfinkel LI, Gubits RM, Ruiz-Opazo N, Nadal-Ginard B (1984) Fast skeletal muscle myosin light chains 1 and 3 are produced from a single gene by a combined process of differential RNA transcription and splicing. J Biol Chem 259: 13595-13604.
    • (1984) J Biol Chem , vol.259 , pp. 13595-13604
    • Periasamy, M.1    Strehler, E.E.2    Garfinkel, L.I.3    Gubits, R.M.4    Ruiz-Opazo, N.5    Nadal-Ginard, B.6
  • 48
    • 0021470717 scopus 로고
    • Muscle fiber activity in carp as a function of swimming speed and muscle temperature
    • Rome LC, Loughna PT, Goldspink G (1984) Muscle fiber activity in carp as a function of swimming speed and muscle temperature. Am J Physiol 247: R272-279.
    • (1984) Am J Physiol , vol.247
    • Rome, L.C.1    Loughna, P.T.2    Goldspink, G.3
  • 51
    • 33749520665 scopus 로고    scopus 로고
    • A new compartment at stereocilia tips defined by spatial and temporal patterns of myosin IIIa expression
    • Schneider ME, Dose AC, Salles FT, Chang W, Erickson FL, Burnside B, Kachar B (2006) A new compartment at stereocilia tips defined by spatial and temporal patterns of myosin IIIa expression. J Neurosci 26: 10243-10252.
    • (2006) J Neurosci , vol.26 , pp. 10243-10252
    • Schneider, M.E.1    Dose, A.C.2    Salles, F.T.3    Chang, W.4    Erickson, F.L.5    Burnside, B.6    Kachar, B.7
  • 53
    • 0017280755 scopus 로고
    • The relationship between biological activity and primary structure of troponin I from white skeletal muscle of the rabbit
    • Syska H, Wilkinson JM, Grand RJ, Perry SV (1976) The relationship between biological activity and primary structure of troponin I from white skeletal muscle of the rabbit. Biochem J 153: 375-387.
    • (1976) Biochem J , vol.153 , pp. 375-387
    • Syska, H.1    Wilkinson, J.M.2    Grand, R.J.3    Perry, S.V.4
  • 54
    • 0033603493 scopus 로고    scopus 로고
    • Size and charge requirements for kinetic modulation and actin binding by alkali 1-type myosin essential light chains
    • Timson DJ, Trayer HR, Smith KJ, Trayer IP (1999) Size and charge requirements for kinetic modulation and actin binding by alkali 1-type myosin essential light chains. J Biol Chem 274: 18271-18277.
    • (1999) J Biol Chem , vol.274 , pp. 18271-18277
    • Timson, D.J.1    Trayer, H.R.2    Smith, K.J.3    Trayer, I.P.4
  • 55
    • 0023150397 scopus 로고
    • Evidence that the N-terminal region of A1-light chain of myosin interacts directly with the C-terminal region of actin
    • Trayer IP, Trayer HR, Levine BA (1987) Evidence that the N-terminal region of A1-light chain of myosin interacts directly with the C-terminal region of actin. Eur J Biochem 164: 259-266.
    • (1987) Eur J Biochem , vol.164 , pp. 259-266
    • Trayer, I.P.1    Trayer, H.R.2    Levine, B.A.3
  • 56
    • 0030596507 scopus 로고    scopus 로고
    • Isolation, characterization and evolution of nine pufferfish (Fugu rubripes) actin genes
    • Venkatesh B, Tay BH, Elgar G, Brenner S (1996) Isolation, characterization and evolution of nine pufferfish (Fugu rubripes) actin genes. J Mol Biol 259: 655-665.
    • (1996) J Mol Biol , vol.259 , pp. 655-665
    • Venkatesh, B.1    Tay, B.H.2    Elgar, G.3    Brenner, S.4
  • 58
    • 0032514716 scopus 로고    scopus 로고
    • Conformational modulation of troponin T by configuration of the NH2-terminal variable region and functional effects
    • Wang J, Jin JP (1998) Conformational modulation of troponin T by configuration of the NH2-terminal variable region and functional effects. Biochemistry 37: 14519-14528.
    • (1998) Biochemistry , vol.37 , pp. 14519-14528
    • Wang, J.1    Jin, J.P.2
  • 59
  • 61
    • 37349081254 scopus 로고    scopus 로고
    • cDNA cloning and characterization of temperature-acclimation-associated light meromyosins from grass carp fast skeletal muscle
    • Wang SY, Tao Y, Liang CS, Fukushima H, Watabe S (2008b) cDNA cloning and characterization of temperature-acclimation-associated light meromyosins from grass carp fast skeletal muscle. Comp Biochem Physiol B Biochem Mol Biol 149: 378-387.
    • (2008) Comp Biochem Physiol B Biochem Mol Biol , vol.149 , pp. 378-387
    • Wang, S.Y.1    Tao, Y.2    Liang, C.S.3    Fukushima, H.4    Watabe, S.5
  • 62
    • 0035575655 scopus 로고    scopus 로고
    • Myosin heavy chain expression in the red, white, and ventricular muscle of juvenile stages of rainbow trout
    • Weaver FE, Stauffer KA, Coughlin DJ (2001) Myosin heavy chain expression in the red, white, and ventricular muscle of juvenile stages of rainbow trout. J Exp Zool 290: 751-758.
    • (2001) J Exp Zool , vol.290 , pp. 751-758
    • Weaver, F.E.1    Stauffer, K.A.2    Coughlin, D.J.3
  • 63
    • 0016249984 scopus 로고
    • Structural homology of myosin alkali light chains, troponin C and carp calcium binding protein
    • Weeds AG, McLachlan AD (1974) Structural homology of myosin alkali light chains, troponin C and carp calcium binding protein. Nature 252: 646-649.
    • (1974) Nature , vol.252 , pp. 646-649
    • Weeds, A.G.1    McLachlan, A.D.2
  • 64
    • 0032481313 scopus 로고    scopus 로고
    • In mouse brain profilin I and profilin II associate with regulators of the endocytic pathway and actin assembly
    • Witke W, Podtelejnikov AV, Di Nardo A, Sutherland JD, Gurniak CB, Dotti C, Mann M (1998) In mouse brain profilin I and profilin II associate with regulators of the endocytic pathway and actin assembly. Embo J 17: 967-976.
    • (1998) Embo J , vol.17 , pp. 967-976
    • Witke, W.1    Podtelejnikov, A.V.2    di Nardo, A.3    Sutherland, J.D.4    Gurniak, C.B.5    Dotti, C.6    Mann, M.7
  • 65
    • 44949214943 scopus 로고    scopus 로고
    • Transcriptome analyses of amoebic gill disease-affected Atlantic salmon (Salmo salar) tissues reveal localized host gene suppression
    • Wynne JW, O'Sullivan MG, Cook MT, Stone G, Nowak BF, Lovell DR, Elliott NG (2008) Transcriptome analyses of amoebic gill disease-affected Atlantic salmon (Salmo salar) tissues reveal localized host gene suppression. Mar Biotechnol (NY) 10: 388-403.
    • (2008) Mar Biotechnol (NY) , vol.10 , pp. 388-403
    • Wynne, J.W.1    O'Sullivan, M.G.2    Cook, M.T.3    Stone, G.4    Nowak, B.F.5    Lovell, D.R.6    Elliott, N.G.7
  • 66
    • 0033774310 scopus 로고    scopus 로고
    • Asynchronous activation of 10 muscle-specific protein (MSP) genes during zebrafish somitogenesis
    • Xu Y, He J, Wang X, Lim TM, Gong Z (2000) Asynchronous activation of 10 muscle-specific protein (MSP) genes during zebrafish somitogenesis. Dev Dyn 219: 201-215.
    • (2000) Dev Dyn , vol.219 , pp. 201-215
    • Xu, Y.1    He, J.2    Wang, X.3    Lim, T.M.4    Gong, Z.5
  • 67
    • 79955536408 scopus 로고    scopus 로고
    • Gene expression profiles of the muscle tissues of the mandarin fish, Siniperca chuatsi with cDNA microarray
    • Zhang JS, Xia XJ, Chu WY, Chen DG, Fu GH, Liu Z, Chen J, Liu F, Lu SQ (2009a) Gene expression profiles of the muscle tissues of the mandarin fish, Siniperca chuatsi with cDNA microarray. Acta Hydrobiol Sin 33(1): 52-59.
    • (2009) Acta Hydrobiol Sin , vol.33 , Issue.1 , pp. 52-59
    • Zhang, J.S.1    Xia, X.J.2    Chu, W.Y.3    Chen, D.G.4    Fu, G.H.5    Liu, Z.6    Chen, J.7    Liu, F.8    Lu, S.Q.9
  • 68
    • 60649105618 scopus 로고    scopus 로고
    • cDNA cloning and expression analysis of myosin heavy chain gene (MHC) of the Mandarin fish, Sniperca kneri
    • Zhang JS, Fu GH, Chu WY, Chen J, Liu Z, Liu F, Lu SQ, Liang P (2009b) cDNA cloning and expression analysis of myosin heavy chain gene (MHC) of the Mandarin fish, Sniperca kneri. Aquac Res 40: 412-418.
    • (2009) Aquac Res , vol.40 , pp. 412-418
    • Zhang, J.S.1    Fu, G.H.2    Chu, W.Y.3    Chen, J.4    Liu, Z.5    Liu, F.6    Lu, S.Q.7    Liang, P.8
  • 69
    • 0023071735 scopus 로고
    • Structural aspects of troponin-tropomyosin regulation of skeletal muscle contraction
    • Zot AS, Potter JD (1987) Structural aspects of troponin-tropomyosin regulation of skeletal muscle contraction. Annu Rev Biophys Biophys Chem 16: 535-559.
    • (1987) Annu Rev Biophys Biophys Chem , vol.16 , pp. 535-559
    • Zot, A.S.1    Potter, J.D.2


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