메뉴 건너뛰기




Volumn 28, Issue 12, 2004, Pages 885-894

Muscular myosin isoforms of Taenia solium (Cestoda)

Author keywords

ATPase; Isoforms; Muscular proteins; Myosin heavy chain; Myosin II; Taenia solium

Indexed keywords

ADENOSINE TRIPHOSPHATASE; ISOPROTEIN; MUSCLE PROTEIN; MYOSIN HEAVY CHAIN; MYOSIN II;

EID: 9644252662     PISSN: 10656995     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cellbi.2004.09.008     Document Type: Article
Times cited : (8)

References (52)
  • 2
    • 0030924898 scopus 로고    scopus 로고
    • Identification and partial characterization of a myosin-like protein from cysticerci and adults of Taenia solium using a monoclonal antibody
    • J. Ambrosio, M. Cruz-Rivera, J. Allan, E. Moran, K. Ersfeld, and A. Flisser Identification and partial characterization of a myosin-like protein from cysticerci and adults of Taenia solium using a monoclonal antibody Parasitology 114 1997 545 553
    • (1997) Parasitology , vol.114 , pp. 545-553
    • Ambrosio, J.1    Cruz-Rivera, M.2    Allan, J.3    Moran, E.4    Ersfeld, K.5    Flisser, A.6
  • 4
  • 6
    • 0034665405 scopus 로고    scopus 로고
    • Smooth muscle myosin heavy chain isoforms and their role in muscle physiology
    • G.J. Babu, D. Warshaw, and M. Periasamy Smooth muscle myosin heavy chain isoforms and their role in muscle physiology Microsc Res Tech 50 2000 532 540
    • (2000) Microsc Res Tech , vol.50 , pp. 532-540
    • Babu, G.J.1    Warshaw, D.2    Periasamy, M.3
  • 8
    • 9644275773 scopus 로고    scopus 로고
    • Enhanced electrophoretic separation and resolution myosin heavy chains in mammalian and avian skeletal muscles
    • E.R. Blough, E.R. Rennie, F. Zhang, and P.J. Reiser Enhanced electrophoretic separation and resolution myosin heavy chains in mammalian and avian skeletal muscles Electrophoresis 18 1997 64 66
    • (1997) Electrophoresis , vol.18 , pp. 64-66
    • Blough, E.R.1    Rennie, E.R.2    Zhang, F.3    Reiser, P.J.4
  • 9
    • 0017613305 scopus 로고
    • Peptide mapping by limited proteolysis in sodium sulfate and analysis by gel electrophoresis
    • D. Cleveland, S. Fischer, M. Kirschner, and U. Laemmli Peptide mapping by limited proteolysis in sodium sulfate and analysis by gel electrophoresis J Biol Chem 252 1977 1102 1106
    • (1977) J Biol Chem , vol.252 , pp. 1102-1106
    • Cleveland, D.1    Fischer, S.2    Kirschner, M.3    Laemmli, U.4
  • 10
    • 0031692830 scopus 로고    scopus 로고
    • A conserved C-terminal assembly region in paramyosin and myosin rods
    • C. Cohen, and D. Parry A conserved C-terminal assembly region in paramyosin and myosin rods J Struct Biol 122 1998 180 187
    • (1998) J Struct Biol , vol.122 , pp. 180-187
    • Cohen, C.1    Parry, D.2
  • 11
    • 1642333310 scopus 로고    scopus 로고
    • Relating biochemistry and function in the myosin superfamily
    • E.M. De la Cruz, and M.E. Ostap Relating biochemistry and function in the myosin superfamily Curr Opin Cell Biol 16 2004 61 67
    • (2004) Curr Opin Cell Biol , vol.16 , pp. 61-67
    • De La Cruz, E.M.1    Ostap, M.E.2
  • 12
    • 0024290415 scopus 로고
    • Two smooth muscle myosin heavy chains differ in their light meromyosin fragment
    • T.J. Eddinger, and R.A. Murphy Two smooth muscle myosin heavy chains differ in their light meromyosin fragment Biochemistry 27 1988 3807 3811
    • (1988) Biochemistry , vol.27 , pp. 3807-3811
    • Eddinger, T.J.1    Murphy, R.A.2
  • 13
    • 0021964531 scopus 로고
    • Myosin and Paramyosin are organized about a newly identified core structure
    • H.F. Epstein, D.M. Miller III, I. Ortiz, and G.C. Berliner Myosin and Paramyosin are organized about a newly identified core structure J Cell Biol 100 1985 904 915
    • (1985) J Cell Biol , vol.100 , pp. 904-915
    • Epstein, H.F.1    Miller III, D.M.2    Ortiz, I.3    Berliner, G.C.4
  • 14
    • 0028869865 scopus 로고
    • Double staining of Coomassie blue stained polyacrylamide gels by imidazole-sodium dodecyl sulfate-zinc reverse staining: Sensitive detection of Coomassie blue undetected proteins
    • C. Fernandez-Patron, E. Hardy, A. Sosa, J. Seoane, and L. Castellanos Double staining of Coomassie blue stained polyacrylamide gels by imidazole-sodium dodecyl sulfate-zinc reverse staining: sensitive detection of Coomassie blue undetected proteins Anal Biochem 224 1995 263 269
    • (1995) Anal Biochem , vol.224 , pp. 263-269
    • Fernandez-Patron, C.1    Hardy, E.2    Sosa, A.3    Seoane, J.4    Castellanos, L.5
  • 15
    • 0028185763 scopus 로고
    • Taeniasis and cysticercosis due to Taenia solium
    • Tsieh Sun CRC Press, Inc.
    • A. Flisser Taeniasis and cysticercosis due to Taenia solium Tsieh Sun Progress in clinical parasitology 1994 CRC Press, Inc.
    • (1994) Progress in Clinical Parasitology
    • Flisser, A.1
  • 16
    • 9644301372 scopus 로고
    • Taenia solium, Taenia saginata and Hymenolepis nana
    • M.J.G. Farthing G.T. Keusch D. Wakelin Chapman and Hall Medical
    • A. Flisser Taenia solium, Taenia saginata and Hymenolepis nana M.J.G. Farthing G.T. Keusch D. Wakelin Enteric infection 2. Intestinal helminths vol. 13 1995 Chapman and Hall Medical 173 189
    • (1995) Enteric Infection 2. Intestinal Helminths , vol.13 , pp. 173-189
    • Flisser, A.1
  • 17
    • 0008937084 scopus 로고    scopus 로고
    • Epidemiological studies of taeniosis and cysticercosis in Latin America
    • P. Craig Z. Pawlowski Cestode zoonoses: echinococcosis and cysticercosis. An emergent and global problem
    • A. Flisser Epidemiological studies of taeniosis and cysticercosis in Latin America P. Craig Z. Pawlowski Cestode zoonoses: echinococcosis and cysticercosis. An emergent and global problem Nato Science Series vol. 341 2002 IOS Press Ohmsha 3 11
    • (2002) Nato Science Series , vol.341 , pp. 3-11
    • Flisser, A.1
  • 18
    • 0018891302 scopus 로고
    • Human cysticercosis: Antigens, antibodies and non responders
    • A. Flisser, E. Woodhouse, and C. Larralde Human cysticercosis: antigens, antibodies and non responders Clin Exp Immunol 39 1980 27 37
    • (1980) Clin Exp Immunol , vol.39 , pp. 27-37
    • Flisser, A.1    Woodhouse, E.2    Larralde, C.3
  • 19
    • 0003142767 scopus 로고
    • Biochemical and immunological characterization of antigen B purified from cysticerci of Taenia solium
    • A. Flisser K. Willms J.P. Laclette C. Larralde C. Ridaura F. Beltran Academic press New York
    • G. Guerra, A. Flisser, L. Cañedo, and J.P. Laclette Biochemical and immunological characterization of antigen B purified from cysticerci of Taenia solium A. Flisser K. Willms J.P. Laclette C. Larralde C. Ridaura F. Beltran Cysticercosis: present states knowledge and perspectives 1982 Academic press New York 437 451
    • (1982) Cysticercosis: Present States Knowledge and Perspectives , pp. 437-451
    • Guerra, G.1    Flisser, A.2    Cañedo, L.3    Laclette, J.P.4
  • 21
    • 0029915379 scopus 로고    scopus 로고
    • Structural stability of chloroplast coupling factor I as determined by differential scanning calorimetry and cold inactivation
    • K.E. Hightower, and R.E. McCarty Structural stability of chloroplast coupling factor I as determined by differential scanning calorimetry and cold inactivation Biochemistry 35 1996 4852 4857
    • (1996) Biochemistry , vol.35 , pp. 4852-4857
    • Hightower, K.E.1    McCarty, R.E.2
  • 22
    • 0030444538 scopus 로고    scopus 로고
    • Muscle proteins - Their actions and interactions
    • K. Holmes Muscle proteins - their actions and interactions Curr Opin Struct Biol 6 1996 781 789
    • (1996) Curr Opin Struct Biol , vol.6 , pp. 781-789
    • Holmes, K.1
  • 24
    • 0035071665 scopus 로고    scopus 로고
    • Functional specificity of actin isoforms
    • S.Y. Khaitlina Functional specificity of actin isoforms Int Rev Cytol 202 2001 35 98
    • (2001) Int Rev Cytol , vol.202 , pp. 35-98
    • Khaitlina, S.Y.1
  • 25
    • 0026090875 scopus 로고
    • Tissue-specific and non-tissue-specific heavy-chain isoforms of myosin in the brain as revealed by monoclonal antibodies
    • A. Kimura, T. Tsuji, R. Matoba, N. Fujitani, K. Ohmori, and S. Matsumura Tissue-specific and non-tissue-specific heavy-chain isoforms of myosin in the brain as revealed by monoclonal antibodies Biochem Biophys Acta 1118 1991 59 69
    • (1991) Biochem Biophys Acta , vol.1118 , pp. 59-69
    • Kimura, A.1    Tsuji, T.2    Matoba, R.3    Fujitani, N.4    Ohmori, K.5    Matsumura, S.6
  • 26
    • 0029620631 scopus 로고
    • Protease-susceptible sites and properties of fragments of aortic smooth-muscle myosin
    • L. King, M.J. Jiang, T.S. Huang, and G.C. Sheu Protease-susceptible sites and properties of fragments of aortic smooth-muscle myosin Biochem J 312 1995 511 518
    • (1995) Biochem J , vol.312 , pp. 511-518
    • King, L.1    Jiang, M.J.2    Huang, T.S.3    Sheu, G.C.4
  • 27
    • 0022497304 scopus 로고
    • The initial burst in ATP hydrolysis by myosin and subfragment-1 as studied by a modified malachite green method for determination of inorganic phosphate
    • T. Kodama, K. Fukui, and K. Kometani The initial burst in ATP hydrolysis by myosin and subfragment-1 as studied by a modified malachite green method for determination of inorganic phosphate J Biochem 99 1986 1465 1472
    • (1986) J Biochem , vol.99 , pp. 1465-1472
    • Kodama, T.1    Fukui, K.2    Kometani, K.3
  • 28
    • 0345305831 scopus 로고    scopus 로고
    • Observations on the musculature and isolated muscle fibres of the liver fluke, Fasciola hepatica
    • D. Kumar, J.G. McGeown, O. Reynoso-Ducoing, J.R. Ambrosio, and I. Fairweather Observations on the musculature and isolated muscle fibres of the liver fluke, Fasciola hepatica Parasitology 127 2003 457 473
    • (2003) Parasitology , vol.127 , pp. 457-473
    • Kumar, D.1    McGeown, J.G.2    Reynoso-Ducoing, O.3    Ambrosio, J.R.4    Fairweather, I.5
  • 29
    • 0026057376 scopus 로고
    • Paramyosin is the Schistosoma mansoni (Trematoda) homologue of antigen B from Taenia solium (Cestoda)
    • J.P. Laclette, A. Landa, L. Arcos, K. Willms, E.A. Davis, and C.B. Shoemaker Paramyosin is the Schistosoma mansoni (Trematoda) homologue of antigen B from Taenia solium (Cestoda) Mol Biochem Parasitol 44 1991 287 296
    • (1991) Mol Biochem Parasitol , vol.44 , pp. 287-296
    • Laclette, J.P.1    Landa, A.2    Arcos, L.3    Willms, K.4    Davis, E.A.5    Shoemaker, C.B.6
  • 30
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • U.K. Laemmli Cleavage of structural proteins during the assembly of the head of bacteriophage T4 Nature 227 1970 680 685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 31
    • 0033615971 scopus 로고    scopus 로고
    • A structural model for phosphorylation control of Dictyostelium myosin II thick filament assembly
    • W. Liang, H.M. Warrick, and J.A. Spudich A structural model for phosphorylation control of Dictyostelium myosin II thick filament assembly J Cell Biol 147 5 1999 1039 1048
    • (1999) J Cell Biol , vol.147 , Issue.5 , pp. 1039-1048
    • Liang, W.1    Warrick, H.M.2    Spudich, J.A.3
  • 32
    • 0003028204 scopus 로고
    • The ultrastructure of invertebrate smooth muscles
    • J. Lowy, and J. Hanson The ultrastructure of invertebrate smooth muscles Physiol Rev 42 1962 34 47
    • (1962) Physiol Rev , vol.42 , pp. 34-47
    • Lowy, J.1    Hanson, J.2
  • 33
  • 34
    • 0032428682 scopus 로고    scopus 로고
    • Primary peptide sequences from squid muscle and optic lobe myosin IIs: Strategy to identify and organelle myosin
    • N.A. Medeiros, T.S. Reese, T.H. Jaffe, J.A. Degiorgis, and E.L. Bearer Primary peptide sequences from squid muscle and optic lobe myosin IIs: strategy to identify and organelle myosin Cell Biol Intl 22 1998 161 173
    • (1998) Cell Biol Intl , vol.22 , pp. 161-173
    • Medeiros, N.A.1    Reese, T.S.2    Jaffe, T.H.3    Degiorgis, J.A.4    Bearer, E.L.5
  • 35
    • 0031816794 scopus 로고    scopus 로고
    • Taenia solium: Description of the intestinal implantation sites in experimental hamster infections
    • M.T. Merchant, L. Aguilar, G. Avila, L. Robert, A. Flisser, and K. Willms Taenia solium: description of the intestinal implantation sites in experimental hamster infections J Parasitol 84 1998 681 685
    • (1998) J Parasitol , vol.84 , pp. 681-685
    • Merchant, M.T.1    Aguilar, L.2    Avila, G.3    Robert, L.4    Flisser, A.5    Willms, K.6
  • 36
    • 0026718384 scopus 로고
    • Analysis of the chicken fast myosin heavy chain family. Localization of isoform-specific antibody epitopes and regions of divergence
    • L.A. Moore, M.J. Arrizubieta, W.E. Tidyman, L.A. Herman, and E. Bandman Analysis of the chicken fast myosin heavy chain family. Localization of isoform-specific antibody epitopes and regions of divergence J Mol Biol 225 1992 1143 1151
    • (1992) J Mol Biol , vol.225 , pp. 1143-1151
    • Moore, L.A.1    Arrizubieta, M.J.2    Tidyman, W.E.3    Herman, L.A.4    Bandman, E.5
  • 37
    • 0026004295 scopus 로고
    • Studies on the distribution of cellular myosin with antibodies to isoform-specific synthetic peptides
    • N. Murakami, P. Mehta, and M. Elzinga Studies on the distribution of cellular myosin with antibodies to isoform-specific synthetic peptides FEBS 278 1991 23 25
    • (1991) FEBS , vol.278 , pp. 23-25
    • Murakami, N.1    Mehta, P.2    Elzinga, M.3
  • 38
    • 0025992841 scopus 로고
    • Taenia solium: Inhibition of spontaneous evagination of cysticerci by the host inflammatory capsule
    • L. Ostrosky, D. Correa, R. Faradji, H. Garcia, and A. Flisser Taenia solium: inhibition of spontaneous evagination of cysticerci by the host inflammatory capsule Int J Parasitol 21 1991 603 604
    • (1991) Int J Parasitol , vol.21 , pp. 603-604
    • Ostrosky, L.1    Correa, D.2    Faradji, R.3    Garcia, H.4    Flisser, A.5
  • 39
    • 77956984659 scopus 로고
    • Myosin adenosinetriphosphatase
    • S.V. Perry Myosin adenosinetriphosphatase Methods Enzymol 2 1955 582 588
    • (1955) Methods Enzymol , vol.2 , pp. 582-588
    • Perry, S.V.1
  • 40
    • 0034665188 scopus 로고    scopus 로고
    • Myosin isoforms, muscle fiber types, and transitions
    • D. Pette, and R. Staron Myosin isoforms, muscle fiber types, and transitions Microsc Res Tech 50 2000 500 509
    • (2000) Microsc Res Tech , vol.50 , pp. 500-509
    • Pette, D.1    Staron, R.2
  • 42
    • 0028986754 scopus 로고
    • Concentrated tris solutions for the preparation, depolymerization and assay of actin: Application to erythroid actin
    • J.C. Pinder, J.A. Sleep, P.M. Bennett, and W.B. Gratzer Concentrated tris solutions for the preparation, depolymerization and assay of actin: application to erythroid actin Anal Biochem 225 1995 291 295
    • (1995) Anal Biochem , vol.225 , pp. 291-295
    • Pinder, J.C.1    Sleep, J.A.2    Bennett, P.M.3    Gratzer, W.B.4
  • 43
    • 0031872677 scopus 로고    scopus 로고
    • Actomyosin motor in the merozoite of the malaria parasite, Plasmodium falciparum: Implications for red cell invasion
    • J.C. Pinder, R.E. Fowier, A.R. Diuzewski, L.H. Bannister, F.M. Lavin, and G.H. Mitchell Actomyosin motor in the merozoite of the malaria parasite, Plasmodium falciparum: implications for red cell invasion J Cell Sci 111 1998 1831 1839
    • (1998) J Cell Sci , vol.111 , pp. 1831-1839
    • Pinder, J.C.1    Fowier, R.E.2    Diuzewski, A.R.3    Bannister, L.H.4    Lavin, F.M.5    Mitchell, G.H.6
  • 44
    • 0033105962 scopus 로고    scopus 로고
    • Protein purification from polyacrylamide gels by sonication extraction
    • C.A. Retamal, P. Thiebaut, and E.W. Alves Protein purification from polyacrylamide gels by sonication extraction Anal Biochem 268 1999 15 20
    • (1999) Anal Biochem , vol.268 , pp. 15-20
    • Retamal, C.A.1    Thiebaut, P.2    Alves, E.W.3
  • 45
    • 0029896830 scopus 로고    scopus 로고
    • Molecular diversity of myofibrillar proteins: Gene regulation and functional significance
    • S. Schiaffino, and C. Reggiani Molecular diversity of myofibrillar proteins: gene regulation and functional significance Physiol Rev 76 2 1996 371 423
    • (1996) Physiol Rev , vol.76 , Issue.2 , pp. 371-423
    • Schiaffino, S.1    Reggiani, C.2
  • 46
    • 9644301371 scopus 로고    scopus 로고
    • Introduction. Functional properties of myosin
    • Oxford University Press New York
    • J.R. Sellers Introduction. Functional properties of myosin Myosins. Protein profile 1999 Oxford University Press New York p. 31-35, 57-68
    • (1999) Myosins. Protein Profile
    • Sellers, J.R.1
  • 47
    • 0034677906 scopus 로고    scopus 로고
    • Myosins: A diverse superfamily
    • J.R. Sellers Myosins: a diverse superfamily Biochim Biophys Acta 1496 2000 3 22
    • (2000) Biochim Biophys Acta , vol.1496 , pp. 3-22
    • Sellers, J.R.1
  • 48
    • 0015222719 scopus 로고
    • Paramyosin and the filaments of molluscan catch muscles. II Native filaments: Isolation and characterization
    • A. Szent-Györgyi, C. Cohen, and J. Kendrick-Jones Paramyosin and the filaments of molluscan catch muscles. II Native filaments: isolation and characterization J Mol Biol 56 1971 239 258
    • (1971) J Mol Biol , vol.56 , pp. 239-258
    • Szent-Györgyi, A.1    Cohen, C.2    Kendrick-Jones, J.3
  • 49
    • 0027452352 scopus 로고
    • Electrophoretic separation of rat skeletal muscle myosin heavy-chain isoforms
    • R.J. Talmadge, and R.R. Roy Electrophoretic separation of rat skeletal muscle myosin heavy-chain isoforms J Appl Physiol 75 1993 2337 2341
    • (1993) J Appl Physiol , vol.75 , pp. 2337-2341
    • Talmadge, R.J.1    Roy, R.R.2
  • 50
    • 0021854926 scopus 로고
    • Two chymotrypsin-susceptible sites of myosin rod from chicken gizzard
    • Y. Tashiro, A. Kumon, S. Yasuda, N. Murakami, and S. Matsumura Two chymotrypsin-susceptible sites of myosin rod from chicken gizzard Eur J Biochem 148 1985 521 528
    • (1985) Eur J Biochem , vol.148 , pp. 521-528
    • Tashiro, Y.1    Kumon, A.2    Yasuda, S.3    Murakami, N.4    Matsumura, S.5
  • 51
    • 0034428543 scopus 로고    scopus 로고
    • Biochemical studies of myosin
    • K.M. Trybus Biochemical studies of myosin Methods 22 2000 327 335
    • (2000) Methods , vol.22 , pp. 327-335
    • Trybus, K.M.1
  • 52
    • 0020620657 scopus 로고
    • Monoclonal antibodies localize changes on myosin heavy chain isozymes during avian myogenesis
    • D.A. Winkelmann, S. Lowey, and J.L. Press Monoclonal antibodies localize changes on myosin heavy chain isozymes during avian myogenesis Cell 34 1983 295 306
    • (1983) Cell , vol.34 , pp. 295-306
    • Winkelmann, D.A.1    Lowey, S.2    Press, J.L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.