메뉴 건너뛰기




Volumn 94, Issue 11, 2012, Pages 2398-2406

A novel calmodulin-like protein from the liver fluke, Fasciola hepatica

Author keywords

Calcium binding protein; Calmodulin; EF hand; Fascioliasis; Trifluoperazine

Indexed keywords

CALCIUM BINDING PROTEIN; CALCIUM ION; CYSTEINE; EGG PROTEIN; FHCAM3 PROTEIN; HELMINTH PROTEIN; PARASITE ANTIGEN; UNCLASSIFIED DRUG;

EID: 84867405112     PISSN: 03009084     EISSN: 61831638     Source Type: Journal    
DOI: 10.1016/j.biochi.2012.06.015     Document Type: Article
Times cited : (16)

References (71)
  • 2
    • 0034256090 scopus 로고    scopus 로고
    • Calmodulin: A prototypical calcium sensor
    • D. Chin, and A.R. Means Calmodulin: a prototypical calcium sensor Trends Cell Biol. 10 2000 322 328
    • (2000) Trends Cell Biol. , vol.10 , pp. 322-328
    • Chin, D.1    Means, A.R.2
  • 4
    • 0024213513 scopus 로고
    • Structure of calmodulin refined at 2.2 Å resolution
    • Y.S. Babu, C.E. Bugg, and W.J. Cook Structure of calmodulin refined at 2.2 Å resolution J. Mol. Biol. 204 1988 191 204
    • (1988) J. Mol. Biol. , vol.204 , pp. 191-204
    • Babu, Y.S.1    Bugg, C.E.2    Cook, W.J.3
  • 6
    • 0029160568 scopus 로고
    • Calcium-induced conformational transition revealed by the solution structure of apo calmodulin
    • M. Zhang, T. Tanaka, and M. Ikura Calcium-induced conformational transition revealed by the solution structure of apo calmodulin Nat. Struct. Biol. 2 1995 758 767
    • (1995) Nat. Struct. Biol. , vol.2 , pp. 758-767
    • Zhang, M.1    Tanaka, T.2    Ikura, M.3
  • 7
    • 0032469789 scopus 로고    scopus 로고
    • Molecular mechanisms of calmodulin's functional versatility
    • M. Zhang, and T. Yuan Molecular mechanisms of calmodulin's functional versatility Biochem. Cell Biol. 76 1998 313 323
    • (1998) Biochem. Cell Biol. , vol.76 , pp. 313-323
    • Zhang, M.1    Yuan, T.2
  • 8
    • 0021939759 scopus 로고
    • 2+-induced exposure of a hydrophobic region. Separation of active and inactive forms of calmodulin
    • 2+-induced exposure of a hydrophobic region. Separation of active and inactive forms of calmodulin Biochim. Biophys. Acta 844 1985 265 269
    • (1985) Biochim. Biophys. Acta , vol.844 , pp. 265-269
    • Gopalakrishna, R.1    Anderson, W.B.2
  • 9
    • 0026536335 scopus 로고
    • Solution structure of a calmodulin-target peptide complex by multidimensional NMR
    • M. Ikura, G.M. Clore, A.M. Gronenborn, G. Zhu, C.B. Klee, and A. Bax Solution structure of a calmodulin-target peptide complex by multidimensional NMR Science 256 1992 632 638
    • (1992) Science , vol.256 , pp. 632-638
    • Ikura, M.1    Clore, G.M.2    Gronenborn, A.M.3    Zhu, G.4    Klee, C.B.5    Bax, A.6
  • 10
    • 0026794065 scopus 로고
    • Target enzyme recognition by calmodulin: 2.4 Å structure of a calmodulin-peptide complex
    • W.E. Meador, A.R. Means, and F.A. Quiocho Target enzyme recognition by calmodulin: 2.4 Å structure of a calmodulin-peptide complex Science 257 1992 1251 1255
    • (1992) Science , vol.257 , pp. 1251-1255
    • Meador, W.E.1    Means, A.R.2    Quiocho, F.A.3
  • 11
    • 0034636190 scopus 로고    scopus 로고
    • Calmodulin remains extended upon binding to smooth muscle caldesmon: A combined small-angle scattering and Fourier transform infrared spectroscopy study
    • J.K. Krueger, S.C. Gallagher, C.A. Wang, and J. Trewhella Calmodulin remains extended upon binding to smooth muscle caldesmon: a combined small-angle scattering and Fourier transform infrared spectroscopy study Biochemistry 39 2000 3979 3987
    • (2000) Biochemistry , vol.39 , pp. 3979-3987
    • Krueger, J.K.1    Gallagher, S.C.2    Wang, C.A.3    Trewhella, J.4
  • 12
    • 0025264994 scopus 로고
    • Calmodulin dissociation regulates brush border myosin i (110-kD-calmodulin) mechanochemical activity in vitro
    • K. Collins, J.R. Sellers, and P. Matsudaira Calmodulin dissociation regulates brush border myosin I (110-kD-calmodulin) mechanochemical activity in vitro J. Cell Biol. 110 1990 1137 1147
    • (1990) J. Cell Biol. , vol.110 , pp. 1137-1147
    • Collins, K.1    Sellers, J.R.2    Matsudaira, P.3
  • 14
    • 79953811907 scopus 로고    scopus 로고
    • Cloning and functional characterization of two calmodulin genes during larval development in the parasitic flatworm Schistosoma mansoni
    • A.S. Taft, and T.P. Yoshino Cloning and functional characterization of two calmodulin genes during larval development in the parasitic flatworm Schistosoma mansoni J. Parasitol. 97 2011 72 81
    • (2011) J. Parasitol. , vol.97 , pp. 72-81
    • Taft, A.S.1    Yoshino, T.P.2
  • 15
    • 0025101741 scopus 로고
    • Characterisation of Sm20, a 20-kilodalton calcium-binding protein of Schistosoma mansoni
    • J.C. Havercroft, M.C. Huggins, D.W. Dunne, and D.W. Taylor Characterisation of Sm20, a 20-kilodalton calcium-binding protein of Schistosoma mansoni Mol. Biochem. Parasitol. 38 1990 211 219
    • (1990) Mol. Biochem. Parasitol. , vol.38 , pp. 211-219
    • Havercroft, J.C.1    Huggins, M.C.2    Dunne, D.W.3    Taylor, D.W.4
  • 17
    • 51449107159 scopus 로고    scopus 로고
    • Molecular characterization of a calcium-binding protein SjCa8 from Schistosoma japonicum
    • S. Hu, P. Law, Z. Lv, Z. Wu, and M.C. Fung Molecular characterization of a calcium-binding protein SjCa8 from Schistosoma japonicum Parasitol. Res. 103 2008 1047 1053
    • (2008) Parasitol. Res. , vol.103 , pp. 1047-1053
    • Hu, S.1    Law, P.2    Lv, Z.3    Wu, Z.4    Fung, M.C.5
  • 18
    • 65549109772 scopus 로고    scopus 로고
    • Expression profile, localization of an 8-kDa calcium-binding protein from Schistosoma japonicum (SjCa8), and vaccine potential of recombinant SjCa8 (rSjCa8) against infections in mice
    • Z.Y. Lv, L.L. Yang, S.M. Hu, X. Sun, H.J. He, S.J. He, Z.Y. Li, Y.P. Zhou, M.C. Fung, X.B. Yu, H.Q. Zheng, A.L. Cao, and Z.D. Wu Expression profile, localization of an 8-kDa calcium-binding protein from Schistosoma japonicum (SjCa8), and vaccine potential of recombinant SjCa8 (rSjCa8) against infections in mice Parasitol. Res. 104 2009 733 743
    • (2009) Parasitol. Res. , vol.104 , pp. 733-743
    • Lv, Z.Y.1    Yang, L.L.2    Hu, S.M.3    Sun, X.4    He, H.J.5    He, S.J.6    Li, Z.Y.7    Zhou, Y.P.8    Fung, M.C.9    Yu, X.B.10    Zheng, H.Q.11    Cao, A.L.12    Wu, Z.D.13
  • 19
    • 34249988772 scopus 로고    scopus 로고
    • Characterisation of two calmodulin-like proteins from the liver fluke, Fasciola hepatica
    • S.L. Russell, N.V. McFerran, E.M. Hoey, A. Trudgett, and D.J. Timson Characterisation of two calmodulin-like proteins from the liver fluke, Fasciola hepatica Biol. Chem. 388 2007 593 599
    • (2007) Biol. Chem. , vol.388 , pp. 593-599
    • Russell, S.L.1    McFerran, N.V.2    Hoey, E.M.3    Trudgett, A.4    Timson, D.J.5
  • 22
    • 31144444454 scopus 로고    scopus 로고
    • An analysis of the calcium-binding protein 1 of Fasciola gigantica with a comparison to its homologs in the phylum Platyhelminthes
    • S. Vichasri-Grams, P. Subpipattana, P. Sobhon, V. Viyanant, and R. Grams An analysis of the calcium-binding protein 1 of Fasciola gigantica with a comparison to its homologs in the phylum Platyhelminthes Mol. Biochem. Parasitol. 146 2006 10 23
    • (2006) Mol. Biochem. Parasitol. , vol.146 , pp. 10-23
    • Vichasri-Grams, S.1    Subpipattana, P.2    Sobhon, P.3    Viyanant, V.4    Grams, R.5
  • 23
    • 35448944438 scopus 로고    scopus 로고
    • A novel tegumental protein 31.8 kDa of Clonorchis sinensis: Sequence analysis, expression, and immunolocalization
    • Y. Huang, Z. Zhou, X. Hu, Q. Wei, J. Xu, Z. Wu, and X. Yu A novel tegumental protein 31.8 kDa of Clonorchis sinensis: sequence analysis, expression, and immunolocalization Parasitol. Res. 102 2007 77 81
    • (2007) Parasitol. Res. , vol.102 , pp. 77-81
    • Huang, Y.1    Zhou, Z.2    Hu, X.3    Wei, Q.4    Xu, J.5    Wu, Z.6    Yu, X.7
  • 24
    • 84863423769 scopus 로고    scopus 로고
    • Identification and characterization of a novel 21.6-kDa tegumental protein from Clonorchis sinensis
    • Y.J. Kim, W.G. Yoo, M.R. Lee, D.W. Kim, W.J. Lee, J.M. Kang, B.K. Na, and J.W. Ju Identification and characterization of a novel 21.6-kDa tegumental protein from Clonorchis sinensis Parasitol. Res. 110 2011 2061 2066
    • (2011) Parasitol. Res. , vol.110 , pp. 2061-2066
    • Kim, Y.J.1    Yoo, W.G.2    Lee, M.R.3    Kim, D.W.4    Lee, W.J.5    Kang, J.M.6    Na, B.K.7    Ju, J.W.8
  • 25
    • 84859107051 scopus 로고    scopus 로고
    • Analysis of a calcium-binding EF-hand protein family in Fasciola gigantica
    • P. Subpipattana, R. Grams, and S. Vichasri-Grams Analysis of a calcium-binding EF-hand protein family in Fasciola gigantica Exp. Parasitol. 130 2012 364 373
    • (2012) Exp. Parasitol. , vol.130 , pp. 364-373
    • Subpipattana, P.1    Grams, R.2    Vichasri-Grams, S.3
  • 26
    • 82655172476 scopus 로고    scopus 로고
    • Cloning, expression, and characterization of a novel Opisthorchis viverrini calcium-binding EF-hand protein
    • G. Senawong, T. Laha, A. Loukas, P.J. Brindley, and B. Sripa Cloning, expression, and characterization of a novel Opisthorchis viverrini calcium-binding EF-hand protein Parasitol. Int. 61 2012 94 100
    • (2012) Parasitol. Int. , vol.61 , pp. 94-100
    • Senawong, G.1    Laha, T.2    Loukas, A.3    Brindley, P.J.4    Sripa, B.5
  • 27
    • 0017701494 scopus 로고
    • Binding of trifluoperazine to the calcium-dependent activator of cyclic nucleotide phosphodiesterase
    • R.M. Levin, and B. Weiss Binding of trifluoperazine to the calcium-dependent activator of cyclic nucleotide phosphodiesterase Mol. Pharmacol. 13 1977 690 697
    • (1977) Mol. Pharmacol. , vol.13 , pp. 690-697
    • Levin, R.M.1    Weiss, B.2
  • 29
    • 0028558882 scopus 로고
    • Drug binding by calmodulin: Crystal structure of a calmodulin- trifluoperazine complex
    • W.J. Cook, L.J. Walter, and M.R. Walter Drug binding by calmodulin: crystal structure of a calmodulin-trifluoperazine complex Biochemistry 33 1994 15259 15265
    • (1994) Biochemistry , vol.33 , pp. 15259-15265
    • Cook, W.J.1    Walter, L.J.2    Walter, M.R.3
  • 31
    • 0023548402 scopus 로고
    • Targeting calmodulin for the development of novel cancer chemotherapeutic agents
    • W.N. Hait Targeting calmodulin for the development of novel cancer chemotherapeutic agents Anticancer Drug Des. 2 1987 139 149
    • (1987) Anticancer Drug Des. , vol.2 , pp. 139-149
    • Hait, W.N.1
  • 32
    • 0022996540 scopus 로고
    • Calmodulin: Biochemical, physiological, and morphological effects on Schistosoma mansoni
    • D.P. Thompson, G.Z. Chen, A.K. Sample, D.R. Semeyn, and J.L. Bennett Calmodulin: biochemical, physiological, and morphological effects on Schistosoma mansoni Am. J. Physiol. 251 1986 R1051 R1058
    • (1986) Am. J. Physiol. , vol.251
    • Thompson, D.P.1    Chen, G.Z.2    Sample, A.K.3    Semeyn, D.R.4    Bennett, J.L.5
  • 33
    • 0023033235 scopus 로고
    • Effect of calmodulin inhibitors on viability and mitochondrial potential of Plasmodium falciparum in culture
    • T.G. Geary, A.A. Divo, and J.B. Jensen Effect of calmodulin inhibitors on viability and mitochondrial potential of Plasmodium falciparum in culture Antimicrob. Agents Chemother. 30 1986 785 788
    • (1986) Antimicrob. Agents Chemother. , vol.30 , pp. 785-788
    • Geary, T.G.1    Divo, A.A.2    Jensen, J.B.3
  • 34
    • 70349337145 scopus 로고    scopus 로고
    • Zoonotic helminth infections with particular emphasis on fasciolosis and other trematodiases
    • M.W. Robinson, and J.P. Dalton Zoonotic helminth infections with particular emphasis on fasciolosis and other trematodiases Philos. Trans. R. Soc. Lond. B. Biol. Sci. 364 2009 2763 2776
    • (2009) Philos. Trans. R. Soc. Lond. B. Biol. Sci. , vol.364 , pp. 2763-2776
    • Robinson, M.W.1    Dalton, J.P.2
  • 36
    • 0029331256 scopus 로고
    • Resistance of Fasciola hepatica to triclabendazole
    • D.J. Overend, and F.L. Bowen Resistance of Fasciola hepatica to triclabendazole Aust. Vet. J. 72 1995 275 276
    • (1995) Aust. Vet. J. , vol.72 , pp. 275-276
    • Overend, D.J.1    Bowen, F.L.2
  • 37
    • 0032480579 scopus 로고    scopus 로고
    • Triclabendazole-resistant liver fluke in Scottish sheep
    • G.B. Mitchell, L. Maris, and M.A. Bonniwell Triclabendazole-resistant liver fluke in Scottish sheep Vet. Rec. 143 1998 399
    • (1998) Vet. Rec. , vol.143 , pp. 399
    • Mitchell, G.B.1    Maris, L.2    Bonniwell, M.A.3
  • 38
    • 0034639720 scopus 로고    scopus 로고
    • Triclabendazole-resistant Fasciola hepatica in southwest Wales
    • I. Thomas, G.C. Coles, and K. Duffus Triclabendazole-resistant Fasciola hepatica in southwest Wales Vet. Rec. 146 2000 200
    • (2000) Vet. Rec. , vol.146 , pp. 200
    • Thomas, I.1    Coles, G.C.2    Duffus, K.3
  • 40
    • 23944474052 scopus 로고    scopus 로고
    • Triclabendazole: New skills to unravel an old(ish) enigma
    • I. Fairweather Triclabendazole: new skills to unravel an old(ish) enigma J. Helminthol. 79 2005 227 234
    • (2005) J. Helminthol. , vol.79 , pp. 227-234
    • Fairweather, I.1
  • 41
    • 70350568141 scopus 로고    scopus 로고
    • Triclabendazole progress report, 2005-2009: An advancement of learning?
    • I. Fairweather Triclabendazole progress report, 2005-2009: an advancement of learning? J. Helminthol. 83 2009 139 150
    • (2009) J. Helminthol. , vol.83 , pp. 139-150
    • Fairweather, I.1
  • 47
    • 3242887695 scopus 로고    scopus 로고
    • Protein structure prediction and analysis using the Robetta server
    • D.E. Kim, D. Chivian, and D. Baker Protein structure prediction and analysis using the Robetta server Nucleic Acids Res. 32 2004 W526 W531
    • (2004) Nucleic Acids Res. , vol.32
    • Kim, D.E.1    Chivian, D.2    Baker, D.3
  • 48
    • 32144432437 scopus 로고    scopus 로고
    • The SWISS-MODEL workspace: A web-based environment for protein structure homology modelling
    • K. Arnold, L. Bordoli, J. Kopp, and T. Schwede The SWISS-MODEL workspace: a web-based environment for protein structure homology modelling Bioinformatics 22 2006 195 201
    • (2006) Bioinformatics , vol.22 , pp. 195-201
    • Arnold, K.1    Bordoli, L.2    Kopp, J.3    Schwede, T.4
  • 49
    • 31044452100 scopus 로고    scopus 로고
    • Structure of calmodulin bound to a calcineurin peptide: A new way of making an old binding mode
    • Q. Ye, X. Li, A. Wong, Q. Wei, and Z. Jia Structure of calmodulin bound to a calcineurin peptide: a new way of making an old binding mode Biochemistry 45 2006 738 745
    • (2006) Biochemistry , vol.45 , pp. 738-745
    • Ye, Q.1    Li, X.2    Wong, A.3    Wei, Q.4    Jia, Z.5
  • 50
    • 0020493109 scopus 로고
    • 2+-induced hydrophobic site on calmodulin: Application for purification of calmodulin by phenyl-Sepharose affinity chromatography
    • 2+-induced hydrophobic site on calmodulin: application for purification of calmodulin by phenyl-Sepharose affinity chromatography Biochem. Biophys. Res. Commun. 104 1982 830 836
    • (1982) Biochem. Biophys. Res. Commun. , vol.104 , pp. 830-836
    • Gopalakrishna, R.1    Anderson, W.B.2
  • 51
    • 79953216184 scopus 로고    scopus 로고
    • IQ-motif selectivity in human IQGAP2 and IQGAP3: Binding of calmodulin and myosin essential light chain
    • E. Atcheson, E. Hamilton, S. Pathmanathan, B. Greer, P. Harriott, and D.J. Timson IQ-motif selectivity in human IQGAP2 and IQGAP3: binding of calmodulin and myosin essential light chain Biosci. Rep. 31 2011 371 379
    • (2011) Biosci. Rep. , vol.31 , pp. 371-379
    • Atcheson, E.1    Hamilton, E.2    Pathmanathan, S.3    Greer, B.4    Harriott, P.5    Timson, D.J.6
  • 52
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • M.M. Bradford A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding Anal. Biochem. 72 1976 248 254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 53
    • 0037293916 scopus 로고    scopus 로고
    • Fasciola hepatica: Surface and internal tegumental changes induced by treatment in vitro with the sulphoxide metabolite of albendazole ('Valbazen')
    • J.F. Buchanan, I. Fairweather, G.P. Brennan, A. Trudgett, and E.M. Hoey Fasciola hepatica: surface and internal tegumental changes induced by treatment in vitro with the sulphoxide metabolite of albendazole ('Valbazen') Parasitology 126 2003 141 153
    • (2003) Parasitology , vol.126 , pp. 141-153
    • Buchanan, J.F.1    Fairweather, I.2    Brennan, G.P.3    Trudgett, A.4    Hoey, E.M.5
  • 55
    • 0018741289 scopus 로고
    • Troponin C-like proteins (calmodulins) from mammalian smooth muscle and other tissues
    • R.J. Grand, S.V. Perry, and R.A. Weeks Troponin C-like proteins (calmodulins) from mammalian smooth muscle and other tissues Biochem. J. 177 1979 521 529
    • (1979) Biochem. J. , vol.177 , pp. 521-529
    • Grand, R.J.1    Perry, S.V.2    Weeks, R.A.3
  • 57
    • 0018959292 scopus 로고
    • Calcium-induced exposure of a hydrophobic surface on calmodulin
    • D.C. LaPorte, B.M. Wierman, and D.R. Storm Calcium-induced exposure of a hydrophobic surface on calmodulin Biochemistry 19 1980 3814 3819
    • (1980) Biochemistry , vol.19 , pp. 3814-3819
    • Laporte, D.C.1    Wierman, B.M.2    Storm, D.R.3
  • 64
    • 0030059923 scopus 로고    scopus 로고
    • Characterization of the actin cross-linking properties of the scruin-calmodulin complex from the acrosomal process of Limulus sperm
    • M.C. Sanders, M. Way, J. Sakai, and P. Matsudaira Characterization of the actin cross-linking properties of the scruin-calmodulin complex from the acrosomal process of Limulus sperm J. Biol. Chem. 271 1996 2651 2657
    • (1996) J. Biol. Chem. , vol.271 , pp. 2651-2657
    • Sanders, M.C.1    Way, M.2    Sakai, J.3    Matsudaira, P.4
  • 66
    • 0026536216 scopus 로고
    • A stage-specific calcium-binding protein expressed in eggs of Schistosoma mansoni
    • D. Moser, M.J. Doenhoff, and M.Q. Klinkert A stage-specific calcium-binding protein expressed in eggs of Schistosoma mansoni Mol. Biochem. Parasitol. 51 1992 229 238
    • (1992) Mol. Biochem. Parasitol. , vol.51 , pp. 229-238
    • Moser, D.1    Doenhoff, M.J.2    Klinkert, M.Q.3
  • 67
    • 0031837346 scopus 로고    scopus 로고
    • Observations on the mechanism of eggshell formation in the liver fluke, Fasciola hepatica
    • L.M. Colhoun, I. Fairweather, and G.P. Brennan Observations on the mechanism of eggshell formation in the liver fluke, Fasciola hepatica Parasitology 116 Pt 6 1998 555 567
    • (1998) Parasitology , vol.116 , Issue.PART 6 , pp. 555-567
    • Colhoun, L.M.1    Fairweather, I.2    Brennan, G.P.3
  • 68
    • 0026245459 scopus 로고
    • Schistosoma mansoni: Eggshell formation is regulated by pH and calcium
    • K.E. Wells, and J.S. Cordingley Schistosoma mansoni: eggshell formation is regulated by pH and calcium Exp. Parasitol. 73 1991 295 310
    • (1991) Exp. Parasitol. , vol.73 , pp. 295-310
    • Wells, K.E.1    Cordingley, J.S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.