메뉴 건너뛰기




Volumn 29, Issue 6, 2008, Pages 985-991

Identification of a novel class of conotoxins defined as V-conotoxins with a unique cysteine pattern and signal peptide sequence

Author keywords

Conotoxin; Cysteine framework; Diversity; V superfamily

Indexed keywords

COMPLEMENTARY DNA; CONOTOXIN; CONOTOXIN VI15A; CYSTEINE; SIGNAL PEPTIDE;

EID: 43049092974     PISSN: 01969781     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.peptides.2008.01.007     Document Type: Article
Times cited : (32)

References (36)
  • 1
    • 23944450557 scopus 로고    scopus 로고
    • A novel conotoxin from Conus delessertii with posttranslationally modified lysine residues
    • Aguilar M.B., Lopez-Vera E., Ortiz E., Becerril B., Possani L.D., Olivera B.M., et al. A novel conotoxin from Conus delessertii with posttranslationally modified lysine residues. Biochemistry 44 (2005) 11130-11136
    • (2005) Biochemistry , vol.44 , pp. 11130-11136
    • Aguilar, M.B.1    Lopez-Vera, E.2    Ortiz, E.3    Becerril, B.4    Possani, L.D.5    Olivera, B.M.6
  • 2
    • 20444459479 scopus 로고    scopus 로고
    • Conotoxins as research tools and drug leads
    • Armishaw C.J., and Alewood P.F. Conotoxins as research tools and drug leads. Curr Protein Pept Sci 6 (2005) 221-240
    • (2005) Curr Protein Pept Sci , vol.6 , pp. 221-240
    • Armishaw, C.J.1    Alewood, P.F.2
  • 3
  • 4
    • 21744458595 scopus 로고    scopus 로고
    • Precursors of novel Gla-containing conotoxins contain a carboxy-terminal recognition site that directs gamma-carboxylation
    • Brown M.A., Begley G.S., Czerwiec E., Stenberg L.M., Jacobs M., Kalume D.E., et al. Precursors of novel Gla-containing conotoxins contain a carboxy-terminal recognition site that directs gamma-carboxylation. Biochemistry 44 (2005) 9150-9159
    • (2005) Biochemistry , vol.44 , pp. 9150-9159
    • Brown, M.A.1    Begley, G.S.2    Czerwiec, E.3    Stenberg, L.M.4    Jacobs, M.5    Kalume, D.E.6
  • 5
    • 29344443859 scopus 로고    scopus 로고
    • Conotoxins and the posttranslational modification of secreted gene products
    • Buczek O., Bulaj G., and Olivera B.M. Conotoxins and the posttranslational modification of secreted gene products. Cell Mol Life Sci 62 (2005) 3067-3079
    • (2005) Cell Mol Life Sci , vol.62 , pp. 3067-3079
    • Buczek, O.1    Bulaj, G.2    Olivera, B.M.3
  • 6
    • 34548490740 scopus 로고    scopus 로고
    • Structure and sodium channel activity of an excitatory I(1)-superfamily conotoxin
    • Buczek O., Wei D., Babon J.J., Yang X., Fiedler B., Chen P., et al. Structure and sodium channel activity of an excitatory I(1)-superfamily conotoxin. Biochemistry 46 (2007) 9929-9940
    • (2007) Biochemistry , vol.46 , pp. 9929-9940
    • Buczek, O.1    Wei, D.2    Babon, J.J.3    Yang, X.4    Fiedler, B.5    Chen, P.6
  • 7
    • 14244259287 scopus 로고    scopus 로고
    • Post-translational amino acid isomerization: a functionally important d-amino acid in an excitatory peptide
    • Buczek O., Yoshikami D., Bulaj G., Jimenez E.C., and Olivera B.M. Post-translational amino acid isomerization: a functionally important d-amino acid in an excitatory peptide. J Biol Chem 280 (2005) 4247-4253
    • (2005) J Biol Chem , vol.280 , pp. 4247-4253
    • Buczek, O.1    Yoshikami, D.2    Bulaj, G.3    Jimenez, E.C.4    Olivera, B.M.5
  • 8
    • 23844444145 scopus 로고    scopus 로고
    • Characterization of d-amino-acid-containing excitatory conotoxins and redefinition of the I-conotoxin superfamily
    • Buczek O., Yoshikami D., Watkins M., Bulaj G., Jimenez E.C., and Olivera B.M. Characterization of d-amino-acid-containing excitatory conotoxins and redefinition of the I-conotoxin superfamily. FEBS J 272 (2005) 4178-4188
    • (2005) FEBS J , vol.272 , pp. 4178-4188
    • Buczek, O.1    Yoshikami, D.2    Watkins, M.3    Bulaj, G.4    Jimenez, E.C.5    Olivera, B.M.6
  • 9
    • 0038645850 scopus 로고    scopus 로고
    • A novel conotoxin from Conus betulinus, kappa-BtX, unique in cysteine pattern and in function as a specific BK channel modulator
    • Fan C.X., Chen X.K., Zhang C., Wang L.X., Duan K.L., He L.L., et al. A novel conotoxin from Conus betulinus, kappa-BtX, unique in cysteine pattern and in function as a specific BK channel modulator. J Biol Chem 278 (2003) 12624-12633
    • (2003) J Biol Chem , vol.278 , pp. 12624-12633
    • Fan, C.X.1    Chen, X.K.2    Zhang, C.3    Wang, L.X.4    Duan, K.L.5    He, L.L.6
  • 10
    • 3442894756 scopus 로고    scopus 로고
    • Conotoxins and structural biology: a prospective paradigm for drug discovery
    • Grant M.A., Morelli X.J., and Rigby A.C. Conotoxins and structural biology: a prospective paradigm for drug discovery. Curr Protein Pept Sci 5 (2004) 235-248
    • (2004) Curr Protein Pept Sci , vol.5 , pp. 235-248
    • Grant, M.A.1    Morelli, X.J.2    Rigby, A.C.3
  • 11
    • 2942605083 scopus 로고    scopus 로고
    • Isolation and characterization of three novel Gla-containing Conus marmoreus venom peptides, one with a novel cysteine pattern
    • Hansson K., Furie B., Furie B.C., and Stenflo J. Isolation and characterization of three novel Gla-containing Conus marmoreus venom peptides, one with a novel cysteine pattern. Biochem Biophys Res Commun 319 (2004) 1081-1087
    • (2004) Biochem Biophys Res Commun , vol.319 , pp. 1081-1087
    • Hansson, K.1    Furie, B.2    Furie, B.C.3    Stenflo, J.4
  • 12
    • 0033543581 scopus 로고    scopus 로고
    • Crystal structures of two alpha-like scorpion toxins: non-proline cis peptide bonds and implications for new binding site selectivity on the sodium channel
    • He X.L., Li H.M., Zeng Z.H., Liu X.Q., Wang M., and Wang D.C. Crystal structures of two alpha-like scorpion toxins: non-proline cis peptide bonds and implications for new binding site selectivity on the sodium channel. J Mol Biol 292 (1999) 125-135
    • (1999) J Mol Biol , vol.292 , pp. 125-135
    • He, X.L.1    Li, H.M.2    Zeng, Z.H.3    Liu, X.Q.4    Wang, M.5    Wang, D.C.6
  • 14
    • 0033865588 scopus 로고    scopus 로고
    • Conotoxins-new vistas for peptide therapeutics
    • Jones R.M., and Bulaj G. Conotoxins-new vistas for peptide therapeutics. Curr Pharm Des 6 (2000) 1249-1285
    • (2000) Curr Pharm Des , vol.6 , pp. 1249-1285
    • Jones, R.M.1    Bulaj, G.2
  • 15
    • 4644305653 scopus 로고    scopus 로고
    • Novel conopeptides of the I-superfamily occur in several clades of cone snails
    • Kauferstein S., Huys I., Kuch U., Melaun C., Tytgat J., and Mebs D. Novel conopeptides of the I-superfamily occur in several clades of cone snails. Toxicon 44 (2004) 539-548
    • (2004) Toxicon , vol.44 , pp. 539-548
    • Kauferstein, S.1    Huys, I.2    Kuch, U.3    Melaun, C.4    Tytgat, J.5    Mebs, D.6
  • 16
    • 0141767100 scopus 로고    scopus 로고
    • A novel conotoxin inhibiting vertebrate voltage-sensitive potassium channels
    • Kauferstein S., Huys I., Lamthanh H., Stocklin R., Sotto F., Menez A., et al. A novel conotoxin inhibiting vertebrate voltage-sensitive potassium channels. Toxicon 42 (2003) 43-52
    • (2003) Toxicon , vol.42 , pp. 43-52
    • Kauferstein, S.1    Huys, I.2    Lamthanh, H.3    Stocklin, R.4    Sotto, F.5    Menez, A.6
  • 17
    • 0024962351 scopus 로고
    • Determination of the three-dimensional solution structure of the C-terminal domain of cellobiohydrolase I from Trichoderma reesei. A study using nuclear magnetic resonance and hybrid distance geometry-dynamical simulated annealing
    • Kraulis J., Clore G.M., Nilges M., Jones T.A., Pettersson G., Knowles J., et al. Determination of the three-dimensional solution structure of the C-terminal domain of cellobiohydrolase I from Trichoderma reesei. A study using nuclear magnetic resonance and hybrid distance geometry-dynamical simulated annealing. Biochemistry 28 (1989) 7241-7257
    • (1989) Biochemistry , vol.28 , pp. 7241-7257
    • Kraulis, J.1    Clore, G.M.2    Nilges, M.3    Jones, T.A.4    Pettersson, G.5    Knowles, J.6
  • 18
    • 3042631514 scopus 로고    scopus 로고
    • Drugs from the sea: conopeptides as potential therapeutics
    • Livett B.G., Gayler K.R., and Khalil Z. Drugs from the sea: conopeptides as potential therapeutics. Curr Med Chem 11 (2004) 1715-1723
    • (2004) Curr Med Chem , vol.11 , pp. 1715-1723
    • Livett, B.G.1    Gayler, K.R.2    Khalil, Z.3
  • 19
    • 0034894357 scopus 로고    scopus 로고
    • Cone venom-from accidental stings to deliberate injection
    • McIntosh J.M., and Jones R.M. Cone venom-from accidental stings to deliberate injection. Toxicon 39 (2001) 1447-1451
    • (2001) Toxicon , vol.39 , pp. 1447-1451
    • McIntosh, J.M.1    Jones, R.M.2
  • 22
    • 0025894164 scopus 로고
    • Relaxation matrix refinement of the solution structure of squash trypsin inhibitor
    • Nilges M., Habazettl J., Brunger A.T., and Holak T.A. Relaxation matrix refinement of the solution structure of squash trypsin inhibitor. J Mol Biol 219 (1991) 499-510
    • (1991) J Mol Biol , vol.219 , pp. 499-510
    • Nilges, M.1    Habazettl, J.2    Brunger, A.T.3    Holak, T.A.4
  • 23
    • 33751049816 scopus 로고    scopus 로고
    • Conotoxins down under
    • Norton R.S., and Olivera B.M. Conotoxins down under. Toxicon 48 (2006) 780-798
    • (2006) Toxicon , vol.48 , pp. 780-798
    • Norton, R.S.1    Olivera, B.M.2
  • 24
    • 0031796848 scopus 로고    scopus 로고
    • The cystine knot structure of ion channel toxins and related polypeptides
    • Norton R.S., and Pallaghy P.K. The cystine knot structure of ion channel toxins and related polypeptides. Toxicon 36 (1998) 1573-1583
    • (1998) Toxicon , vol.36 , pp. 1573-1583
    • Norton, R.S.1    Pallaghy, P.K.2
  • 25
    • 0036930324 scopus 로고    scopus 로고
    • Conus venom peptides: reflections from the biology of clades and species
    • Olivera B.M. Conus venom peptides: reflections from the biology of clades and species. Ann Rev Ecol System 33 (2002) 25-47
    • (2002) Ann Rev Ecol System , vol.33 , pp. 25-47
    • Olivera, B.M.1
  • 26
    • 33845992556 scopus 로고    scopus 로고
    • Conus peptides: biodiversity-based discovery and exogenomics
    • Olivera B.M. Conus peptides: biodiversity-based discovery and exogenomics. J Biol Chem 281 (2006) 31173-31177
    • (2006) J Biol Chem , vol.281 , pp. 31173-31177
    • Olivera, B.M.1
  • 27
    • 0035239229 scopus 로고    scopus 로고
    • Conotoxins, in retrospect
    • Olivera B.M., and Cruz L.J. Conotoxins, in retrospect. Toxicon 39 (2001) 7-14
    • (2001) Toxicon , vol.39 , pp. 7-14
    • Olivera, B.M.1    Cruz, L.J.2
  • 28
    • 0031451746 scopus 로고    scopus 로고
    • Solution structure of robustoxin, the lethal neurotoxin from the funnel-web spider Atrax robustus
    • Pallaghy P.K., Alewood D., Alewood P.F., and Norton R.S. Solution structure of robustoxin, the lethal neurotoxin from the funnel-web spider Atrax robustus. FEBS Lett 419 (1997) 191-196
    • (1997) FEBS Lett , vol.419 , pp. 191-196
    • Pallaghy, P.K.1    Alewood, D.2    Alewood, P.F.3    Norton, R.S.4
  • 29
    • 33751118759 scopus 로고    scopus 로고
    • Diversity and evolution of conotoxins based on gene expression profiling of Conus litteratus
    • Pi C., Liu J., Peng C., Liu Y., Jiang X., Zhao Y., et al. Diversity and evolution of conotoxins based on gene expression profiling of Conus litteratus. Genomics 88 (2006) 809-819
    • (2006) Genomics , vol.88 , pp. 809-819
    • Pi, C.1    Liu, J.2    Peng, C.3    Liu, Y.4    Jiang, X.5    Zhao, Y.6
  • 30
    • 0029243371 scopus 로고
    • The solution structure of omega-Aga-IVB, a P-type calcium channel antagonist from venom of the funnel web spider, Agelenopsis aperta
    • Reily M.D., Thanabal V., and Adams M.E. The solution structure of omega-Aga-IVB, a P-type calcium channel antagonist from venom of the funnel web spider, Agelenopsis aperta. J Biomol NMR 5 (1995) 122-132
    • (1995) J Biomol NMR , vol.5 , pp. 122-132
    • Reily, M.D.1    Thanabal, V.2    Adams, M.E.3
  • 32
    • 0347989461 scopus 로고    scopus 로고
    • Conus venoms: a rich source of novel ion channel-targeted peptides
    • Terlau H., and Olivera B.M. Conus venoms: a rich source of novel ion channel-targeted peptides. Physiol Rev 84 (2004) 41-68
    • (2004) Physiol Rev , vol.84 , pp. 41-68
    • Terlau, H.1    Olivera, B.M.2
  • 35
    • 0034043512 scopus 로고    scopus 로고
    • Discovery and characterization of a family of insecticidal neurotoxins with a rare vicinal disulfide bridge
    • Wang X., Connor M., Smith R., Maciejewski M.W., Howden M.E., Nicholson G.M., et al. Discovery and characterization of a family of insecticidal neurotoxins with a rare vicinal disulfide bridge. Nat Struct Biol 7 (2000) 505-513
    • (2000) Nat Struct Biol , vol.7 , pp. 505-513
    • Wang, X.1    Connor, M.2    Smith, R.3    Maciejewski, M.W.4    Howden, M.E.5    Nicholson, G.M.6
  • 36
    • 23244431760 scopus 로고    scopus 로고
    • An intrathecally administered N-type calcium channel antagonist for the treatment of chronic pain
    • Wermeling D.P., and Ziconotide. An intrathecally administered N-type calcium channel antagonist for the treatment of chronic pain. Pharmacotherapy 25 (2005) 1084-1094
    • (2005) Pharmacotherapy , vol.25 , pp. 1084-1094
    • Wermeling, D.P.1    Ziconotide2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.