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Volumn 112, Issue 42, 2015, Pages E5660-E5668

An invertebrate smooth muscle with striated muscle myosin filaments

Author keywords

Muscle contraction; Muscle structure; Schistosoma mansoni; Schistosome; Thick filament

Indexed keywords

MYOSIN; MYOSIN II; TROPONIN;

EID: 84947235712     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1513439112     Document Type: Article
Times cited : (47)

References (80)
  • 1
    • 24744432501 scopus 로고    scopus 로고
    • Molecular structure of the sarcomere
    • eds Engel AG, Franzini-Armstrong C (McGraw-Hill, New York)
    • Craig R, Padrón R (2004) Molecular structure of the sarcomere. Myology, eds Engel AG, Franzini-Armstrong C (McGraw-Hill, New York), pp 129-166.
    • (2004) Myology , pp. 129-166
    • Craig, R.1    Padrón, R.2
  • 3
    • 0021327069 scopus 로고
    • Structural apparatus for force transmission in smooth muscles
    • Gabella G (1984) Structural apparatus for force transmission in smooth muscles. Physiol Rev 64(2):455-477.
    • (1984) Physiol Rev , vol.64 , Issue.2 , pp. 455-477
    • Gabella, G.1
  • 4
    • 0007838798 scopus 로고
    • Evolution and diversity of nonstriated muscles
    • eds Bohr DF, Somlyo AP, Sparks HV (American Physiological Society, Bethesda, MD)
    • Prosser CL (1980) Evolution and diversity of nonstriated muscles. Handbook of Physiology: Vascular Smooth Muscle, eds Bohr DF, Somlyo AP, Sparks HV (American Physiological Society, Bethesda, MD), pp 635-670.
    • (1980) Handbook of Physiology: Vascular Smooth Muscle , pp. 635-670
    • Prosser, C.L.1
  • 5
    • 0034650174 scopus 로고    scopus 로고
    • Characterization of several invertebrate muscle cell types: A comparison with vertebrate muscles
    • Royuela M, Fraile B, Arenas MI, Paniagua R (2000) Characterization of several invertebrate muscle cell types: A comparison with vertebrate muscles. Microsc Res Tech 48(2):107-115.
    • (2000) Microsc Res Tech , vol.48 , Issue.2 , pp. 107-115
    • Royuela, M.1    Fraile, B.2    Arenas, M.I.3    Paniagua, R.4
  • 6
    • 33646009721 scopus 로고    scopus 로고
    • Structure and function of myosin filaments
    • Craig R, Woodhead JL (2006) Structure and function of myosin filaments. Curr Opin Struct Biol 16(2):204-212.
    • (2006) Curr Opin Struct Biol , vol.16 , Issue.2 , pp. 204-212
    • Craig, R.1    Woodhead, J.L.2
  • 7
    • 0027519403 scopus 로고
    • Life stage specific expression of a myosin heavy chain in the hydrozoan Podocoryne carnea
    • Schuchert P, Reber-Müller S, Schmid V (1993) Life stage specific expression of a myosin heavy chain in the hydrozoan Podocoryne carnea. Differentiation 54(1): 11-18.
    • (1993) Differentiation , vol.54 , Issue.1 , pp. 11-18
    • Schuchert, P.1    Reber-Müller, S.2    Schmid, V.3
  • 8
    • 0041192909 scopus 로고    scopus 로고
    • Identification of two distinct muscles in the planarian Dugesia japonica by their expression of myosin heavy chain genes
    • Kobayashi C, et al. (1998) Identification of two distinct muscles in the planarian Dugesia japonica by their expression of myosin heavy chain genes. Zoolog Sci 15(6):861-869.
    • (1998) Zoolog Sci , vol.15 , Issue.6 , pp. 861-869
    • Kobayashi, C.1
  • 9
    • 0034059761 scopus 로고    scopus 로고
    • Regulation of contraction in striated muscle
    • Gordon AM, Homsher E, Regnier M (2000) Regulation of contraction in striated muscle. Physiol Rev 80(2):853-924.
    • (2000) Physiol Rev , vol.80 , Issue.2 , pp. 853-924
    • Gordon, A.M.1    Homsher, E.2    Regnier, M.3
  • 10
    • 0038303504 scopus 로고    scopus 로고
    • Protein kinase network in the regulation of phosphorylation and dephosphorylation of smooth muscle myosin light chain
    • Hirano K, Derkach DN, Hirano M, Nishimura J, Kanaide H (2003) Protein kinase network in the regulation of phosphorylation and dephosphorylation of smooth muscle myosin light chain. Mol Cell Biochem 248(1-2):105-114.
    • (2003) Mol Cell Biochem , vol.248 , Issue.1-2 , pp. 105-114
    • Hirano, K.1    Derkach, D.N.2    Hirano, M.3    Nishimura, J.4    Kanaide, H.5
  • 11
    • 0017672926 scopus 로고
    • Assembly of smooth muscle myosin into side-polar filaments
    • Craig R, Megerman J (1977) Assembly of smooth muscle myosin into side-polar filaments. J Cell Biol 75(3):990-996.
    • (1977) J Cell Biol , vol.75 , Issue.3 , pp. 990-996
    • Craig, R.1    Megerman, J.2
  • 12
    • 0029987687 scopus 로고    scopus 로고
    • Myosin filament structure in vertebrate smooth muscle
    • Xu JQ, Harder BA, Uman P, Craig R (1996) Myosin filament structure in vertebrate smooth muscle. J Cell Biol 134(1):53-66.
    • (1996) J Cell Biol , vol.134 , Issue.1 , pp. 53-66
    • Xu, J.Q.1    Harder, B.A.2    Uman, P.3    Craig, R.4
  • 13
    • 77955387555 scopus 로고    scopus 로고
    • Mechanism of catch force: Tethering of thick and thin filaments by twitchin
    • Butler TM, Siegman MJ (2010) Mechanism of catch force: Tethering of thick and thin filaments by twitchin. J Biomed Biotechnol 2010:725207.
    • (2010) J Biomed Biotechnol , vol.2010 , pp. 725207
    • Butler, T.M.1    Siegman, M.J.2
  • 16
    • 84879508835 scopus 로고    scopus 로고
    • Immunoprotection of mice against Schistosomiasis mansoni using solubilized membrane antigens
    • Sulbarán G, Noya O, Brito B, Ballén DE, Cesari IM (2013) Immunoprotection of mice against Schistosomiasis mansoni using solubilized membrane antigens. PLoS Negl Trop Dis 7(6):e2254.
    • (2013) PLoS Negl Trop Dis , vol.7 , Issue.6 , pp. e2254
    • Sulbarán, G.1    Noya, O.2    Brito, B.3    Ballén, D.E.4    Cesari, I.M.5
  • 17
    • 0026458038 scopus 로고
    • Induction of protective immunity in mice using a 62-kDa recombinant fragment of a Schistosoma mansoni surface antigen
    • Soisson LM, et al. (1992) Induction of protective immunity in mice using a 62-kDa recombinant fragment of a Schistosoma mansoni surface antigen. J Immunol 149(11): 3612-3620.
    • (1992) J Immunol , vol.149 , Issue.11 , pp. 3612-3620
    • Soisson, L.M.1
  • 18
    • 0023936918 scopus 로고
    • Paramyosin and actin in schistosomal teguments
    • Matsumoto Y, et al. (1988) Paramyosin and actin in schistosomal teguments. Nature 333(6168):76-78.
    • (1988) Nature , vol.333 , Issue.6168 , pp. 76-78
    • Matsumoto, Y.1
  • 19
    • 0022419384 scopus 로고
    • Arrangement of the heads of myosin in relaxed thick filaments from tarantula muscle
    • Crowther RA, Padrón R, Craig R (1985) Arrangement of the heads of myosin in relaxed thick filaments from tarantula muscle. J Mol Biol 184(3):429-439.
    • (1985) J Mol Biol , vol.184 , Issue.3 , pp. 429-439
    • Crowther, R.A.1    Padrón, R.2    Craig, R.3
  • 20
    • 0022416683 scopus 로고
    • Electron microscopic and optical diffraction analysis of the structure of scorpion muscle thick filaments
    • Kensler RW, Levine RJ, Stewart M (1985) Electron microscopic and optical diffraction analysis of the structure of scorpion muscle thick filaments. J Cell Biol 101(2):395-401.
    • (1985) J Cell Biol , vol.101 , Issue.2 , pp. 395-401
    • Kensler, R.W.1    Levine, R.J.2    Stewart, M.3
  • 21
    • 0019882167 scopus 로고
    • Structure of Limulus telson muscle thick filaments
    • Stewart M, Kensler RW, Levine RJ (1981) Structure of Limulus telson muscle thick filaments. J Mol Biol 153(3):781-790.
    • (1981) J Mol Biol , vol.153 , Issue.3 , pp. 781-790
    • Stewart, M.1    Kensler, R.W.2    Levine, R.J.3
  • 22
    • 24144484776 scopus 로고    scopus 로고
    • Atomic model of a myosin filament in the relaxed state
    • Woodhead JL, et al. (2005) Atomic model of a myosin filament in the relaxed state. Nature 436(7054):1195-1199.
    • (2005) Nature , vol.436 , Issue.7054 , pp. 1195-1199
    • Woodhead, J.L.1
  • 23
    • 84868462586 scopus 로고    scopus 로고
    • The myosin interacting-heads motif is present in the relaxed thick filament of the striated muscle of scorpion
    • Pinto A, Sánchez F, Alamo L, Padrón R (2012) The myosin interacting-heads motif is present in the relaxed thick filament of the striated muscle of scorpion. J Struct Biol 180(3):469-478.
    • (2012) J Struct Biol , vol.180 , Issue.3 , pp. 469-478
    • Pinto, A.1    Sánchez, F.2    Alamo, L.3    Padrón, R.4
  • 24
    • 58149092608 scopus 로고    scopus 로고
    • Head-head interaction characterizes the relaxed state of Limulus muscle myosin filaments
    • Zhao FQ, Craig R, Woodhead JL (2009) Head-head interaction characterizes the relaxed state of Limulus muscle myosin filaments. J Mol Biol 385(2):423-431.
    • (2009) J Mol Biol , vol.385 , Issue.2 , pp. 423-431
    • Zhao, F.Q.1    Craig, R.2    Woodhead, J.L.3
  • 25
    • 0035836733 scopus 로고    scopus 로고
    • Three-dimensional image reconstruction of dephosphorylated smooth muscle heavy meromyosin reveals asymmetry in the interaction between myosin heads and placement of subfragment 2
    • Wendt T, Taylor D, Trybus KM, Taylor K (2001) Three-dimensional image reconstruction of dephosphorylated smooth muscle heavy meromyosin reveals asymmetry in the interaction between myosin heads and placement of subfragment 2. Proc Natl Acad Sci USA 98(8):4361-4366.
    • (2001) Proc Natl Acad Sci USA , vol.98 , Issue.8 , pp. 4361-4366
    • Wendt, T.1    Taylor, D.2    Trybus, K.M.3    Taylor, K.4
  • 26
    • 21244459182 scopus 로고    scopus 로고
    • Invertebrate muscles: Muscle specific genes and proteins
    • Hooper SL, Thuma JB (2005) Invertebrate muscles: Muscle specific genes and proteins. Physiol Rev 85(3):1001-1060.
    • (2005) Physiol Rev , vol.85 , Issue.3 , pp. 1001-1060
    • Hooper, S.L.1    Thuma, J.B.2
  • 28
    • 0027508927 scopus 로고
    • Molecular evolution of the myosin family: Relationships derived from comparisons of amino acid sequences
    • Goodson HV, Spudich JA (1993) Molecular evolution of the myosin family: Relationships derived from comparisons of amino acid sequences. Proc Natl Acad Sci USA 90(2):659-663.
    • (1993) Proc Natl Acad Sci USA , vol.90 , Issue.2 , pp. 659-663
    • Goodson, H.V.1    Spudich, J.A.2
  • 29
    • 67650789618 scopus 로고    scopus 로고
    • The genome of the blood fluke Schistosoma mansoni
    • Berriman M, et al. (2009) The genome of the blood fluke Schistosoma mansoni. Nature 460(7253):352-358.
    • (2009) Nature , vol.460 , Issue.7253 , pp. 352-358
    • Berriman, M.1
  • 30
    • 0029561337 scopus 로고
    • Chimeric substitutions of the actin-binding loop activate dephosphorylated but not phosphorylated smooth muscle heavy meromyosin
    • Rovner AS, Freyzon Y, Trybus KM (1995) Chimeric substitutions of the actin-binding loop activate dephosphorylated but not phosphorylated smooth muscle heavy meromyosin. J Biol Chem 270(51):30260-30263.
    • (1995) J Biol Chem , vol.270 , Issue.51 , pp. 30260-30263
    • Rovner, A.S.1    Freyzon, Y.2    Trybus, K.M.3
  • 31
    • 0032540958 scopus 로고    scopus 로고
    • The light chain-binding domain of the smooth muscle myosin heavy chain is not the only determinant of regulation
    • Trybus KM, Naroditskaya V, Sweeney HL (1998) The light chain-binding domain of the smooth muscle myosin heavy chain is not the only determinant of regulation. J Biol Chem 273(29):18423-18428.
    • (1998) J Biol Chem , vol.273 , Issue.29 , pp. 18423-18428
    • Trybus, K.M.1    Naroditskaya, V.2    Sweeney, H.L.3
  • 32
    • 0025601653 scopus 로고
    • Skip residues correlate with bends in the myosin tail
    • Offer G (1990) Skip residues correlate with bends in the myosin tail. J Mol Biol 216(2): 213-218.
    • (1990) J Mol Biol , vol.216 , Issue.2 , pp. 213-218
    • Offer, G.1
  • 33
    • 84863655007 scopus 로고    scopus 로고
    • Independent evolution of striated muscles in cnidarians and bilaterians
    • Steinmetz PR, et al. (2012) Independent evolution of striated muscles in cnidarians and bilaterians. Nature 487(7406):231-234.
    • (2012) Nature , vol.487 , Issue.7406 , pp. 231-234
    • Steinmetz, P.R.1
  • 34
    • 26244466046 scopus 로고    scopus 로고
    • Skip residues and charge interactions in myosin II coiled-coils: Implications for molecular packing
    • Straussman R, Squire JM, Ben-Ya'acov A, Ravid S (2005) Skip residues and charge interactions in myosin II coiled-coils: Implications for molecular packing. J Mol Biol 353(3):613-628.
    • (2005) J Mol Biol , vol.353 , Issue.3 , pp. 613-628
    • Straussman, R.1    Squire, J.M.2    Ben-Ya'Acov, A.3    Ravid, S.4
  • 35
    • 0035979730 scopus 로고    scopus 로고
    • Crossbridge and tropomyosin positions observed in native, interacting thick and thin filaments
    • Craig R, Lehman W (2001) Crossbridge and tropomyosin positions observed in native, interacting thick and thin filaments. J Mol Biol 311(5):1027-1036.
    • (2001) J Mol Biol , vol.311 , Issue.5 , pp. 1027-1036
    • Craig, R.1    Lehman, W.2
  • 36
    • 0014502513 scopus 로고
    • Ultrastructural studies of the blood fluke - Schistosoma mansoni. II. The musculature
    • Silk MH, Spence IM (1969) Ultrastructural studies of the blood fluke - Schistosoma mansoni. II. The musculature. S Afr J Med Sci 34(1):11-20.
    • (1969) S Afr J Med Sci , vol.34 , Issue.1 , pp. 11-20
    • Silk, M.H.1    Spence, I.M.2
  • 37
    • 0033811773 scopus 로고    scopus 로고
    • A confocal microscopical study of the musculature of adult Schistosoma mansoni
    • Mair GR, Maule AG, Day TA, Halton DW (2000) A confocal microscopical study of the musculature of adult Schistosoma mansoni. Parasitology 121(2):163-170.
    • (2000) Parasitology , vol.121 , Issue.2 , pp. 163-170
    • Mair, G.R.1    Maule, A.G.2    Day, T.A.3    Halton, D.W.4
  • 38
    • 79953781201 scopus 로고    scopus 로고
    • An atlas for Schistosoma mansoni organs and life-cycle stages using cell type-specific markers and confocal microscopy
    • Collins JJ, 3rd, King RS, Cogswell A, Williams DL, Newmark PA (2011) An atlas for Schistosoma mansoni organs and life-cycle stages using cell type-specific markers and confocal microscopy. PLoS Negl Trop Dis 5(3):e1009.
    • (2011) PLoS Negl Trop Dis , vol.5 , Issue.3 , pp. e1009
    • Collins, J.J.1    King, R.S.2    Cogswell, A.3    Williams, D.L.4    Newmark, P.A.5
  • 40
    • 0016834835 scopus 로고
    • The contractile apparatus of vascular smooth muscle: Intermediate high voltage stereo electron microscopy
    • Ashton FT, Somlyo AV, Somlyo AP (1975) The contractile apparatus of vascular smooth muscle: Intermediate high voltage stereo electron microscopy. J Mol Biol 98(1):17-29.
    • (1975) J Mol Biol , vol.98 , Issue.1 , pp. 17-29
    • Ashton, F.T.1    Somlyo, A.V.2    Somlyo, A.P.3
  • 41
    • 0015924772 scopus 로고
    • The influence of temperature on the thick filaments of vertebrate smooth muscle
    • Shoenberg CF (1973) The influence of temperature on the thick filaments of vertebrate smooth muscle. Philos Trans R Soc Lond B Biol Sci 265(867):197-202.
    • (1973) Philos Trans R Soc Lond B Biol Sci , vol.265 , Issue.867 , pp. 197-202
    • Shoenberg, C.F.1
  • 42
    • 0024961717 scopus 로고
    • Sequence analysis of the complete Caenorhabditis elegans myosin heavy chain gene family
    • Dibb NJ, Maruyama IN, Krause M, Karn J (1989) Sequence analysis of the complete Caenorhabditis elegans myosin heavy chain gene family. J Mol Biol 205(3):603-613.
    • (1989) J Mol Biol , vol.205 , Issue.3 , pp. 603-613
    • Dibb, N.J.1    Maruyama, I.N.2    Krause, M.3    Karn, J.4
  • 43
    • 0016364724 scopus 로고
    • The fine structure and organization of the tail musculature of the cercaria of Schistosoma mansoni
    • Nuttman CJ (1974) The fine structure and organization of the tail musculature of the cercaria of Schistosoma mansoni. Parasitology 68(2):147-154.
    • (1974) Parasitology , vol.68 , Issue.2 , pp. 147-154
    • Nuttman, C.J.1
  • 44
    • 0016680461 scopus 로고
    • Regulation of muscular contraction. Distribution of actin control and myosin control in the animal kingdom
    • Lehman W, Szent-Györgyi AG (1975) Regulation of muscular contraction. Distribution of actin control and myosin control in the animal kingdom. J Gen Physiol 66(1):1-30.
    • (1975) J Gen Physiol , vol.66 , Issue.1 , pp. 1-30
    • Lehman, W.1    Szent-Györgyi, A.G.2
  • 45
    • 0014196054 scopus 로고
    • Forked tail of the cercaria of Schistosoma mansoni - A rowing device
    • Graefe G, Hohorst W, Dräger H (1967) Forked tail of the cercaria of Schistosoma mansoni - A rowing device. Nature 215(5097):207-208.
    • (1967) Nature , vol.215 , Issue.5097 , pp. 207-208
    • Graefe, G.1    Hohorst, W.2    Dräger, H.3
  • 46
    • 0004161470 scopus 로고    scopus 로고
    • (Oxford Univ Press, Oxford), 2nd Ed
    • Sellers JR (1999) Myosins (Oxford Univ Press, Oxford), 2nd Ed.
    • (1999) Myosins
    • Sellers, J.R.1
  • 47
    • 0024421567 scopus 로고
    • Kinetics of contraction initiated by flash photolysis of caged adenosine triphosphate in tonic and phasic smooth muscles
    • Horiuti K, Somlyo AV, Goldman YE, Somlyo AP (1989) Kinetics of contraction initiated by flash photolysis of caged adenosine triphosphate in tonic and phasic smooth muscles. J Gen Physiol 94(4):769-781.
    • (1989) J Gen Physiol , vol.94 , Issue.4 , pp. 769-781
    • Horiuti, K.1    Somlyo, A.V.2    Goldman, Y.E.3    Somlyo, A.P.4
  • 48
    • 0028786311 scopus 로고
    • Kinetics of prephosphorylation reactions and myosin light chain phosphorylation in smooth muscle. Flash photolysis studies with caged calcium and caged ATP
    • Zimmermann B, Somlyo AV, Ellis-Davies GC, Kaplan JH, Somlyo AP (1995) Kinetics of prephosphorylation reactions and myosin light chain phosphorylation in smooth muscle. Flash photolysis studies with caged calcium and caged ATP. J Biol Chem 270(41):23966-23974.
    • (1995) J Biol Chem , vol.270 , Issue.41 , pp. 23966-23974
    • Zimmermann, B.1    Somlyo, A.V.2    Ellis-Davies, G.C.3    Kaplan, J.H.4    Somlyo, A.P.5
  • 49
    • 0027300234 scopus 로고
    • Myosin light chain phosphorylation in vertebrate striated muscle: Regulation and function
    • Sweeney HL, Bowman BF, Stull JT (1993) Myosin light chain phosphorylation in vertebrate striated muscle: Regulation and function. Am J Physiol 264(5):C1085-C1095.
    • (1993) Am J Physiol , vol.264 , Issue.5 , pp. C1085-C1095
    • Sweeney, H.L.1    Bowman, B.F.2    Stull, J.T.3
  • 50
    • 56249115186 scopus 로고    scopus 로고
    • Three-dimensional reconstruction of tarantula myosin filaments suggests how phosphorylation may regulate myosin activity
    • Alamo L, et al. (2008) Three-dimensional reconstruction of tarantula myosin filaments suggests how phosphorylation may regulate myosin activity. J Mol Biol 384(4): 780-797.
    • (2008) J Mol Biol , vol.384 , Issue.4 , pp. 780-797
    • Alamo, L.1
  • 51
    • 81055155880 scopus 로고    scopus 로고
    • A molecular model of phosphorylation-based activation and potentiation of tarantula muscle thick filaments
    • Brito R, et al. (2011) A molecular model of phosphorylation-based activation and potentiation of tarantula muscle thick filaments. J Mol Biol 414(1):44-61.
    • (2011) J Mol Biol , vol.414 , Issue.1 , pp. 44-61
    • Brito, R.1
  • 52
    • 51249105761 scopus 로고    scopus 로고
    • Invertebrate muscles: Thin and thick filament structure; Molecular basis of contraction and its regulation, catch and asynchronous muscle
    • Hooper SL, Hobbs KH, Thuma JB (2008) Invertebrate muscles: Thin and thick filament structure; molecular basis of contraction and its regulation, catch and asynchronous muscle. Prog Neurobiol 86(2):72-127.
    • (2008) Prog Neurobiol , vol.86 , Issue.2 , pp. 72-127
    • Hooper, S.L.1    Hobbs, K.H.2    Thuma, J.B.3
  • 53
    • 84878128694 scopus 로고    scopus 로고
    • Structural basis of the relaxed state of a Ca2+-regulated myosin filament and its evolutionary implications
    • Woodhead JL, Zhao FQ, Craig R (2013) Structural basis of the relaxed state of a Ca2+-regulated myosin filament and its evolutionary implications. Proc Natl Acad Sci USA 110(21):8561-8566.
    • (2013) Proc Natl Acad Sci USA , vol.110 , Issue.21 , pp. 8561-8566
    • Woodhead, J.L.1    Zhao, F.Q.2    Craig, R.3
  • 54
    • 40649098633 scopus 로고    scopus 로고
    • Three-dimensional structure of vertebrate cardiac muscle myosin filaments
    • Zoghbi ME, Woodhead JL, Moss RL, Craig R (2008) Three-dimensional structure of vertebrate cardiac muscle myosin filaments. Proc Natl Acad Sci USA 105(7):2386-2390.
    • (2008) Proc Natl Acad Sci USA , vol.105 , Issue.7 , pp. 2386-2390
    • Zoghbi, M.E.1    Woodhead, J.L.2    Moss, R.L.3    Craig, R.4
  • 56
    • 34548478783 scopus 로고    scopus 로고
    • Structures of smooth muscle myosin and heavy meromyosin in the folded, shutdown state
    • Burgess SA, et al. (2007) Structures of smooth muscle myosin and heavy meromyosin in the folded, shutdown state. J Mol Biol 372(5):1165-1178.
    • (2007) J Mol Biol , vol.372 , Issue.5 , pp. 1165-1178
    • Burgess, S.A.1
  • 57
    • 47049110451 scopus 로고    scopus 로고
    • Head-head and head-tail interaction: A general mechanism for switching off myosin II activity in cells
    • Jung HS, Komatsu S, Ikebe M, Craig R (2008) Head-head and head-tail interaction: A general mechanism for switching off myosin II activity in cells. Mol Biol Cell 19(8): 3234-3242.
    • (2008) Mol Biol Cell , vol.19 , Issue.8 , pp. 3234-3242
    • Jung, H.S.1    Komatsu, S.2    Ikebe, M.3    Craig, R.4
  • 58
    • 84962114870 scopus 로고    scopus 로고
    • The inhibited, interacting-heads motif characterizes myosin II from the earliest animals with muscle
    • Sulbarán G, et al. (2015) The inhibited, interacting-heads motif characterizes myosin II from the earliest animals with muscle. Biophys J 108(2):301a.
    • (2015) Biophys J , vol.108 , Issue.2 , pp. 301a
    • Sulbarán, G.1
  • 59
    • 84924763994 scopus 로고    scopus 로고
    • Can systems biology help to separate evolutionary analogies (convergent homoplasies) from homologies?
    • Gordon MS, Notar JC (2015) Can systems biology help to separate evolutionary analogies (convergent homoplasies) from homologies? Prog Biophys Mol Biol 117(1): 19-29.
    • (2015) Prog Biophys Mol Biol , vol.117 , Issue.1 , pp. 19-29
    • Gordon, M.S.1    Notar, J.C.2
  • 60
    • 0024571893 scopus 로고
    • Bilaterians of the Precambrian-Cambrian transition and the annelid-arthropod relationship
    • Valentine JW (1989) Bilaterians of the Precambrian-Cambrian transition and the annelid-arthropod relationship. Proc Natl Acad Sci USA 86(7):2272-2275.
    • (1989) Proc Natl Acad Sci USA , vol.86 , Issue.7 , pp. 2272-2275
    • Valentine, J.W.1
  • 61
    • 84862814389 scopus 로고    scopus 로고
    • Molecular phylogenetics: Principles and practice
    • Yang Z, Rannala B (2012) Molecular phylogenetics: Principles and practice. Nat Rev Genet 13(5):303-314.
    • (2012) Nat Rev Genet , vol.13 , Issue.5 , pp. 303-314
    • Yang, Z.1    Rannala, B.2
  • 62
    • 0037143719 scopus 로고    scopus 로고
    • A phylogenetic analysis of myosin heavy chain type II sequences corroborates that Acoela and Nemertodermatida are basal bilaterians
    • Ruiz-Trillo I, et al. (2002) A phylogenetic analysis of myosin heavy chain type II sequences corroborates that Acoela and Nemertodermatida are basal bilaterians. Proc Natl Acad Sci USA 99(17):11246-11251.
    • (2002) Proc Natl Acad Sci USA , vol.99 , Issue.17 , pp. 11246-11251
    • Ruiz-Trillo, I.1
  • 63
    • 0018328198 scopus 로고
    • Structure of the backbone in myosin filaments of muscle
    • Wray JS (1979) Structure of the backbone in myosin filaments of muscle. Nature 277(5691):37-40.
    • (1979) Nature , vol.277 , Issue.5691 , pp. 37-40
    • Wray, J.S.1
  • 64
    • 0015506180 scopus 로고
    • Structure of insect fibrillar flight muscle in the presence and absence of ATP
    • Miller A, Tregear RT (1972) Structure of insect fibrillar flight muscle in the presence and absence of ATP. J Mol Biol 70(1):85-104.
    • (1972) J Mol Biol , vol.70 , Issue.1 , pp. 85-104
    • Miller, A.1    Tregear, R.T.2
  • 65
    • 0018112325 scopus 로고
    • Structure and function of chicken gizzard myosin
    • Suzuki H, Onishi H, Takahashi K, Watanabe S (1978) Structure and function of chicken gizzard myosin. J Biochem 84(6):1529-1542.
    • (1978) J Biochem , vol.84 , Issue.6 , pp. 1529-1542
    • Suzuki, H.1    Onishi, H.2    Takahashi, K.3    Watanabe, S.4
  • 66
    • 0017091125 scopus 로고
    • Paramyosin in invertebrate muscles. II. Content in relation to structure and function
    • Levine RJ, Elfvin M, Dewey MM, Walcott B (1976) Paramyosin in invertebrate muscles. II. Content in relation to structure and function. J Cell Biol 71(1):273-279.
    • (1976) J Cell Biol , vol.71 , Issue.1 , pp. 273-279
    • Levine, R.J.1    Elfvin, M.2    Dewey, M.M.3    Walcott, B.4
  • 67
    • 42449127767 scopus 로고    scopus 로고
    • Scallop adductor muscles: Structure and function
    • eds Shumway SE, Parsons GJ (Elsevier, Amsterdam)
    • Chantler PD (2006) Scallop adductor muscles: Structure and function. Scallops: Biology, Ecology and Aquaculture, eds Shumway SE, Parsons GJ (Elsevier, Amsterdam), pp 231-320.
    • (2006) Scallops: Biology, Ecology and Aquaculture , pp. 231-320
    • Chantler, P.D.1
  • 68
    • 0021104531 scopus 로고
    • Structure of myosin/paramyosin filaments from a molluscan smooth muscle
    • Castellani L, Vibert P, Cohen C (1983) Structure of myosin/paramyosin filaments from a molluscan smooth muscle. J Mol Biol 167(4):853-872.
    • (1983) J Mol Biol , vol.167 , Issue.4 , pp. 853-872
    • Castellani, L.1    Vibert, P.2    Cohen, C.3
  • 69
    • 0028574171 scopus 로고
    • Scallop striated and smooth muscle myosin heavy-chain isoforms are produced by alternative RNA splicing from a single gene
    • Nyitray L, Jancsó A, Ochiai Y, Gráf L, Szent-Györgyi AG (1994) Scallop striated and smooth muscle myosin heavy-chain isoforms are produced by alternative RNA splicing from a single gene. Proc Natl Acad Sci USA 91(26):12686-12690.
    • (1994) Proc Natl Acad Sci USA , vol.91 , Issue.26 , pp. 12686-12690
    • Nyitray, L.1    Jancsó, A.2    Ochiai, Y.3    Gráf, L.4    Szent-Györgyi, A.G.5
  • 70
    • 84863088849 scopus 로고    scopus 로고
    • Independent specialisation of myosin II paralogues in muscle vs. Non-muscle functions during early animal evolution: A ctenophore perspective
    • Dayraud C, et al. (2012) Independent specialisation of myosin II paralogues in muscle vs. non-muscle functions during early animal evolution: A ctenophore perspective. BMC Evol Biol 12(1):107.
    • (2012) BMC Evol Biol , vol.12 , Issue.1 , pp. 107
    • Dayraud, C.1
  • 71
    • 0023601047 scopus 로고
    • Structural changes accompanying phosphorylation of tarantula muscle myosin filaments
    • Craig R, Padrón R, Kendrick-Jones J (1987) Structural changes accompanying phosphorylation of tarantula muscle myosin filaments. J Cell Biol 105(3):1319-1327.
    • (1987) J Cell Biol , vol.105 , Issue.3 , pp. 1319-1327
    • Craig, R.1    Padrón, R.2    Kendrick-Jones, J.3
  • 72
    • 84858033359 scopus 로고    scopus 로고
    • Isolation, electron microscopy and 3D reconstruction of invertebrate muscle myofilaments
    • Craig R (2012) Isolation, electron microscopy and 3D reconstruction of invertebrate muscle myofilaments. Methods 56(1):33-43.
    • (2012) Methods , vol.56 , Issue.1 , pp. 33-43
    • Craig, R.1
  • 73
    • 0029975088 scopus 로고    scopus 로고
    • SPIDER and WEB: Processing and visualization of images in 3D electron microscopy and related fields
    • Frank J, et al. (1996) SPIDER and WEB: Processing and visualization of images in 3D electron microscopy and related fields. J Struct Biol 116(1):190-199.
    • (1996) J Struct Biol , vol.116 , Issue.1 , pp. 190-199
    • Frank, J.1
  • 74
    • 0034564239 scopus 로고    scopus 로고
    • A robust algorithm for the reconstruction of helical filaments using single-particle methods
    • Egelman EH (2000) A robust algorithm for the reconstruction of helical filaments using single-particle methods. Ultramicroscopy 85(4):225-234.
    • (2000) Ultramicroscopy , vol.85 , Issue.4 , pp. 225-234
    • Egelman, E.H.1
  • 75
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227(5259):680-685.
    • (1970) Nature , vol.227 , Issue.5259 , pp. 680-685
    • Laemmli, U.K.1
  • 76
    • 84897442958 scopus 로고    scopus 로고
    • Serological screening of the Schistosoma mansoni adult worm proteome
    • Ludolf F, et al. (2014) Serological screening of the Schistosoma mansoni adult worm proteome. PLoS Negl Trop Dis 8(3):e2745.
    • (2014) PLoS Negl Trop Dis , vol.8 , Issue.3 , pp. e2745
    • Ludolf, F.1
  • 77
    • 65449188232 scopus 로고    scopus 로고
    • Jalview version 2 - A multiple sequence alignment editor and analysis workbench
    • Waterhouse AM, Procter JB, Martin DM, Clamp M, Barton GJ (2009) Jalview version 2 - A multiple sequence alignment editor and analysis workbench. Bioinformatics 25(9):1189-1191.
    • (2009) Bioinformatics , vol.25 , Issue.9 , pp. 1189-1191
    • Waterhouse, A.M.1    Procter, J.B.2    Martin, D.M.3    Clamp, M.4    Barton, G.J.5
  • 78
    • 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(5):1792-1797.
    • (2004) Nucleic Acids Res , vol.32 , Issue.5 , pp. 1792-1797
    • Edgar, R.C.1
  • 79
    • 85018074558 scopus 로고
    • Estudio por microscopía electrónica de los filamentos gruesos aislados de músculo de Schistosoma mansoni
    • Martelo MJ, Granados M, Cesari I, Padrón R (1987) Estudio por microscopía electrónica de los filamentos gruesos aislados de músculo de Schistosoma mansoni. Acta Cient Venez 38(1):227.
    • (1987) Acta Cient Venez , vol.38 , Issue.1 , pp. 227
    • Martelo, M.J.1    Granados, M.2    Cesari, I.3    Padrón, R.4
  • 80
    • 0027404430 scopus 로고
    • Cloning and sequencing of a complete myosin heavy chain cDNA from Schistosoma mansoni
    • Weston D, Schmitz J, Kemp WM, Kunz W (1993) Cloning and sequencing of a complete myosin heavy chain cDNA from Schistosoma mansoni. Mol Biochem Parasitol 58(1):161-164.
    • (1993) Mol Biochem Parasitol , vol.58 , Issue.1 , pp. 161-164
    • Weston, D.1    Schmitz, J.2    Kemp, W.M.3    Kunz, W.4


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