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Volumn 68, Issue , 2002, Pages 1515-1518

Structural and genetic characterization of fish skeletal muscle tropomyosins

Author keywords

cDNA cloning; DSC; fast skeletal muscle; fish; primary structure; tropomyosin

Indexed keywords


EID: 0242404109     PISSN: 09199268     EISSN: 14442906     Source Type: Journal    
DOI: 10.2331/fishsci.68.sup2_1515     Document Type: Article
Times cited : (6)

References (16)
  • 1
    • 0018762433 scopus 로고
    • Structure and functions of tropomyosin from muscle and non-muscle sources.
    • Smillie L. B. Structure and functions of tropomyosin from muscle and non-muscle sources. Trends Biochem. Sci. 1979; 4:151155.
    • (1979) Trends Biochem. Sci. , vol.4 , pp. 151155
    • Smillie, L.B.1
  • 2
    • 0032917668 scopus 로고    scopus 로고
    • Conformational changes of contractile proteins and their role in muscle contraction.
    • Borovikov Y. S. Conformational changes of contractile proteins and their role in muscle contraction. Int. Rev. Cytol. 1999; 189: 267–301.
    • (1999) Int. Rev. Cytol. , vol.189 , pp. 267-301
    • Borovikov, Y.S.1
  • 5
    • 0000185180 scopus 로고    scopus 로고
    • cDNA cloning of tropomyosin from the anterior byssus retractor muscle of mussel and its structural integrity from the deduced amino acid sequence.
    • Iwasaki K., Kikuchi K., Funabara D., Watabe S. cDNA cloning of tropomyosin from the anterior byssus retractor muscle of mussel and its structural integrity from the deduced amino acid sequence. Fisheries Sci. 1997; 63: 731–734.
    • (1997) Fisheries Sci. , vol.63 , pp. 731-734
    • Iwasaki, K.1    Kikuchi, K.2    Funabara, D.3    Watabe, S.4
  • 7
    • 0025933273 scopus 로고
    • The chicken gene encoding the α isoform of tropomyosin of fast-twitch muscle fibers: organization, expression and identification of the major proteins synthesized
    • Lemonnier M., Balvay L., Mouly V., Libri D., Fiszman M. Y. The chicken gene encoding the α isoform of tropomyosin of fast-twitch muscle fibers: organization, expression and identification of the major proteins synthesized. Gene 1991, 107: 229–240.
    • (1991) Gene , vol.107 , pp. 229-240
    • Lemonnier, M.1    Balvay, L.2    Mouly, V.3    Libri, D.4    Fiszman, M.Y.5
  • 9
    • 0028269716 scopus 로고
    • Isolation and characterization of tropomyosins from fish muscles.
    • Heeley D. H., Hong C. Isolation and characterization of tropomyosins from fish muscles. Comp. Biochem. Physiol. 1994; 108B: 95–106.
    • (1994) Comp. Biochem. Physiol. , vol.108B , pp. 95-106
    • Heeley, D.H.1    Hong, C.2
  • 10
    • 0029846301 scopus 로고    scopus 로고
    • Further characterization of fast, slow and cardiac muscle tropomyosins from salmonid fish.
    • Jackman D., Waddleton D. M., Younghusband B., Heeley D. H. Further characterization of fast, slow and cardiac muscle tropomyosins from salmonid fish. Eur. J. Biochem. 1996; 242: 363–371.
    • (1996) Eur. J. Biochem. , vol.242 , pp. 363-371
    • Jackman, D.1    Waddleton, D.M.2    Younghusband, B.3    Heeley, D.H.4
  • 11
    • 0034958956 scopus 로고    scopus 로고
    • cDNA cloning and deduced amino acid sequence of tropomyosin from fast skeletal muscle of white croaker Pennahia argentata.
    • Ochiai Y., Ahmed K., Ahsan M. N., Funabara D.Nakaya M., Watabe S. cDNA cloning and deduced amino acid sequence of tropomyosin from fast skeletal muscle of white croaker Pennahia argentata. Fisheries Sci. 2001; 67: 559–561.
    • (2001) Fisheries Sci. , vol.67 , pp. 559-561
    • Ochiai, Y.1    Ahmed, K.2    Ahsan, M.N.3    Funabara, D.4    Nakaya, M.5    Watabe, S.6
  • 12
    • 0019332511 scopus 로고
    • A comparison of the amino acid sequences of rabbit skeletal muscle α- and β-tropomyosins.
    • Mak A. S., Smillie L. B., Stewart G. B. A comparison of the amino acid sequences of rabbit skeletal muscle α- and β-tropomyosins. J. Biol. Chem. 1980; 255: 3647–3655.
    • (1980) J. Biol. Chem. , vol.255 , pp. 3647-3655
    • Mak, A.S.1    Smillie, L.B.2    Stewart, G.B.3
  • 13
    • 0029591294 scopus 로고
    • The stability of tropomyosin, a two-stranded coiled-coil protein, is primarily a function of the hydrophobicity of residues at the helix-helix interface.
    • Greenfield N. J., Hitchcock-DeGregori S. E. The stability of tropomyosin, a two-stranded coiled-coil protein, is primarily a function of the hydrophobicity of residues at the helix-helix interface. Biochemistry 1995; 34:16797–16805.
    • (1995) Biochemistry , vol.34 , pp. 16797-16805
    • Greenfield, N.J.1    Hitchcock-DeGregori, S.E.2
  • 14
    • 0019975166 scopus 로고
    • Periodic charge distributions in the myosin rod amino acid sequence match cross-bridge spacings in muscle
    • McLachlan A. D., Karn J. Periodic charge distributions in the myosin rod amino acid sequence match cross-bridge spacings in muscle. Nature 1982, 299:226–231.
    • (1982) Nature , vol.299 , pp. 226-231
    • McLachlan, A.D.1    Karn, J.2
  • 15
    • 0001136664 scopus 로고    scopus 로고
    • cDNA cloning of myosin rod and the complete primary structure of myosin heavy chain of walleye pollack fast skeletal muscle.
    • Togashi M., Kakinuma M., Hirayama Y., Fukushima H., Watabe S., Ojima T., Nishita K. cDNA cloning of myosin rod and the complete primary structure of myosin heavy chain of walleye pollack fast skeletal muscle. Fisheries Sci. 2000; 66: 349–357.
    • (2000) Fisheries Sci. , vol.66 , pp. 349-357
    • Togashi, M.1    Kakinuma, M.2    Hirayama, Y.3    Fukushima, H.4    Watabe, S.5    Ojima, T.6    Nishita, K.7
  • 16
    • 18744369369 scopus 로고    scopus 로고
    • cDNA cloning and characterization of the complete structure for myosin heavy chain of white croaker fast skeletal muscle
    • Yoon S. H., Kakinuma M., Hirayama Y., Yamamoto J., Watabe S. cDNA cloning and characterization of the complete structure for myosin heavy chain of white croaker fast skeletal muscle. Fisheries Sci. 2000; 66–1163–1171.
    • (2000) Fisheries Sci. , vol.66 , pp. 1163-1171
    • Yoon, S.H.1    Kakinuma, M.2    Hirayama, Y.3    Yamamoto, J.4    Watabe, S.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.