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Volumn 44, Issue 1, 1997, Pages 89-97

Structural comparisons of muscle and nonmuscle actins give insights into the evolution of their functional differences

Author keywords

Evolution; Isoactins; Ligand binding sites; Muscle actins; Nonmuscle actins; Structure function relationship

Indexed keywords

ACTIN; PROTEIN SUBUNIT;

EID: 0031014648     PISSN: 00222844     EISSN: None     Source Type: Journal    
DOI: 10.1007/PL00006125     Document Type: Article
Times cited : (27)

References (24)
  • 2
    • 0026687729 scopus 로고
    • An ATPase domain common to prokaryotic cell cycle proteins, sugar kinases, actin, and hsp70 heat shock proteins
    • Bork P, Sander C, Valencia A (1992) An ATPase domain common to prokaryotic cell cycle proteins, sugar kinases, actin, and hsp70 heat shock proteins. Proc Natl Acad Sci USA 89:7290-7294
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 7290-7294
    • Bork, P.1    Sander, C.2    Valencia, A.3
  • 3
    • 0021952869 scopus 로고
    • Actin and myosin multigene families: Their expression during the formation of skeletal muscle
    • Buckingham ME (1985) Actin and myosin multigene families: their expression during the formation of skeletal muscle. Essays Biochem 20:77-109
    • (1985) Essays Biochem , vol.20 , pp. 77-109
    • Buckingham, M.E.1
  • 5
    • 0028984528 scopus 로고
    • The specific NH2-terminal sequence Ac-EEED of α-smooth muscle actin plays a role in polymerization in vitro and in vivo
    • Chaponnier C, Goethals M, Janmey PA, Gabbiani F, Gabbiani G, Vandekerckhove J (1995) The specific NH2-terminal sequence Ac-EEED of α-smooth muscle actin plays a role in polymerization in vitro and in vivo. J Cell Biol 130:887-895
    • (1995) J Cell Biol , vol.130 , pp. 887-895
    • Chaponnier, C.1    Goethals, M.2    Janmey, P.A.3    Gabbiani, F.4    Gabbiani, G.5    Vandekerckhove, J.6
  • 6
    • 0027547324 scopus 로고
    • Actin isoforms
    • Herman IM (1993) Actin isoforms. Curr Biol 5:48-55
    • (1993) Curr Biol , vol.5 , pp. 48-55
    • Herman, I.M.1
  • 7
    • 0000301384 scopus 로고
    • Muscle proteins: Actin
    • Holmes KC, Kabsch W (1991) Muscle proteins: actin. Curr Biol 1: 270-280
    • (1991) Curr Biol , vol.1 , pp. 270-280
    • Holmes, K.C.1    Kabsch, W.2
  • 12
    • 0024451183 scopus 로고
    • Wild-type and mutant actin genes in Caenorhabditis elegans
    • Krause M, Wild M, Rosenzweig B, Hirsh D (1989) Wild-type and mutant actin genes in Caenorhabditis elegans. J Mol Biol 208:381-392
    • (1989) J Mol Biol , vol.208 , pp. 381-392
    • Krause, M.1    Wild, M.2    Rosenzweig, B.3    Hirsh, D.4
  • 13
    • 0028179144 scopus 로고
    • Ca2+-induced tropomyosin movement in Limulus thin filaments revealed by three dimensional reconstruction
    • Lehman W, Craig R, Vibert P (1994) Ca2+-induced tropomyosin movement in Limulus thin filaments revealed by three dimensional reconstruction. Nature 368:65-67
    • (1994) Nature , vol.368 , pp. 65-67
    • Lehman, W.1    Craig, R.2    Vibert, P.3
  • 14
    • 0027131941 scopus 로고
    • Refinement of the F-actin model against X-ray fiber diffraction data by the use of a directed mutation algorithm
    • Lorenz M, Popp D, Holmes KC (1993) Refinement of the F-actin model against X-ray fiber diffraction data by the use of a directed mutation algorithm. J Mol Biol 234:826-836
    • (1993) J Mol Biol , vol.234 , pp. 826-836
    • Lorenz, M.1    Popp, D.2    Holmes, K.C.3
  • 15
    • 0027251071 scopus 로고
    • Structure of gelsolin segment-1-actin complex and the mechanism of filament severing
    • McLaughlin PJ, Gooch JT, Mannherz HG, Weeds AG (1993) Structure of gelsolin segment-1-actin complex and the mechanism of filament severing. Nature 364:685-692
    • (1993) Nature , vol.364 , pp. 685-692
    • McLaughlin, P.J.1    Gooch, J.T.2    Mannherz, H.G.3    Weeds, A.G.4
  • 17
    • 0026777385 scopus 로고
    • Insect muscle actins differ distinctly from invertebrate and vertebrate cytoplasmic actins
    • Mounier N, Gouy M, Mouchiroud D, Prudhomme JC (1992) Insect muscle actins differ distinctly from invertebrate and vertebrate cytoplasmic actins. J Mol Evol 34:406-415
    • (1992) J Mol Evol , vol.34 , pp. 406-415
    • Mounier, N.1    Gouy, M.2    Mouchiroud, D.3    Prudhomme, J.C.4
  • 19
    • 0025457288 scopus 로고
    • The functional importance of multiple actin isoforms
    • Rubenstein PA (1990) The functional importance of multiple actin isoforms. Bioessays 12:309-315
    • (1990) Bioessays , vol.12 , pp. 309-315
    • Rubenstein, P.A.1
  • 23
    • 0028679210 scopus 로고
    • Actin
    • Sheterline P (ed) Academic Press, London
    • Sheterline P, Sparrow JC (1994) Actin. In: Sheterline P (ed) Protein profile, vol 1. Academic Press, London
    • (1994) Protein Profile , vol.1
    • Sheterline, P.1    Sparrow, J.C.2
  • 24
    • 0009780328 scopus 로고
    • Mammalian cytoplasmic actins are the products of at least two genes and differ in primary structure in at least 25 identified positions from skeletal muscle actins
    • Vandekerckhove J, Weber K (1978) Mammalian cytoplasmic actins are the products of at least two genes and differ in primary structure in at least 25 identified positions from skeletal muscle actins. Proc Natl Acad Sci USA 75:1106-1110
    • (1978) Proc Natl Acad Sci USA , vol.75 , pp. 1106-1110
    • Vandekerckhove, J.1    Weber, K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.