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Journal Abstract Search

350 related items for PubMed ID: 12815161

  • 1. APETx1, a new toxin from the sea anemone Anthopleura elegantissima, blocks voltage-gated human ether-a-go-go-related gene potassium channels.
    Diochot S, Loret E, Bruhn T, Béress L, Lazdunski M.
    Mol Pharmacol; 2003 Jul; 64(1):59-69. PubMed ID: 12815161
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  • 2. APETx1 from sea anemone Anthopleura elegantissima is a gating modifier peptide toxin of the human ether-a-go-go- related potassium channel.
    Zhang M, Liu XS, Diochot S, Lazdunski M, Tseng GN.
    Mol Pharmacol; 2007 Aug; 72(2):259-68. PubMed ID: 17473056
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  • 5. A natural point mutation changes both target selectivity and mechanism of action of sea anemone toxins.
    Peigneur S, Béress L, Möller C, Marí F, Forssmann WG, Tytgat J.
    FASEB J; 2012 Dec; 26(12):5141-51. PubMed ID: 22972919
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  • 6. Solution structure of APETx1 from the sea anemone Anthopleura elegantissima: a new fold for an HERG toxin.
    Chagot B, Diochot S, Pimentel C, Lazdunski M, Darbon H.
    Proteins; 2005 May 01; 59(2):380-6. PubMed ID: 15726634
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  • 7. Mechanism of hERG inhibition by gating-modifier toxin, APETx1, deduced by functional characterization.
    Matsumura K, Shimomura T, Kubo Y, Oka T, Kobayashi N, Imai S, Yanase N, Akimoto M, Fukuda M, Yokogawa M, Ikeda K, Kurita JI, Nishimura Y, Shimada I, Osawa M.
    BMC Mol Cell Biol; 2021 Jan 07; 22(1):3. PubMed ID: 33413079
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  • 11. Novel peptide toxins recently isolated from sea anemones.
    Shiomi K.
    Toxicon; 2009 Dec 15; 54(8):1112-8. PubMed ID: 19269303
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  • 14. Structural conservation of the pores of calcium-activated and voltage-gated potassium channels determined by a sea anemone toxin.
    Rauer H, Pennington M, Cahalan M, Chandy KG.
    J Biol Chem; 1999 Jul 30; 274(31):21885-92. PubMed ID: 10419508
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  • 16. Sea anemone peptides with a specific blocking activity against the fast inactivating potassium channel Kv3.4.
    Diochot S, Schweitz H, Béress L, Lazdunski M.
    J Biol Chem; 1998 Mar 20; 273(12):6744-9. PubMed ID: 9506974
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  • 17. BeKm-1 is a HERG-specific toxin that shares the structure with ChTx but the mechanism of action with ErgTx1.
    Zhang M, Korolkova YV, Liu J, Jiang M, Grishin EV, Tseng GN.
    Biophys J; 2003 May 20; 84(5):3022-36. PubMed ID: 12719233
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  • 18. A potassium-channel toxin from the sea anemone Bunodosoma granulifera, an inhibitor for Kv1 channels. Revision of the amino acid sequence, disulfide-bridge assignment, chemical synthesis, and biological activity.
    Cotton J, Crest M, Bouet F, Alessandri N, Gola M, Forest E, Karlsson E, Castañeda O, Harvey AL, Vita C, Ménez A.
    Eur J Biochem; 1997 Feb 15; 244(1):192-202. PubMed ID: 9063464
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  • 19. A new sea anemone peptide, APETx2, inhibits ASIC3, a major acid-sensitive channel in sensory neurons.
    Diochot S, Baron A, Rash LD, Deval E, Escoubas P, Scarzello S, Salinas M, Lazdunski M.
    EMBO J; 2004 Apr 07; 23(7):1516-25. PubMed ID: 15044953
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  • 20. Characterization of a potassium channel toxin from the Caribbean Sea anemone Stichodactyla helianthus.
    Castañeda O, Sotolongo V, Amor AM, Stöcklin R, Anderson AJ, Harvey AL, Engström A, Wernstedt C, Karlsson E.
    Toxicon; 1995 May 07; 33(5):603-13. PubMed ID: 7660365
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