Search Results - "Darbon, H"

Recombinant production and solution structure of PcTx1, the specific peptide inhibitor of ASIC1a proton‐gated cation channels by Escoubas, Pierre, Bernard, Cédric, Lambeau, Gérard, Lazdunski, Michel, Darbon, Hervé

“…Acid‐sensing ion channels (ASICs) are thought to be important ion channels, particularly for the perception of pain. Some of them may also contribute to…”
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Solution structure of APETx2, a specific peptide inhibitor of ASIC3 proton‐gated channels by Chagot, Benjamin, Escoubas, Pierre, Diochot, Sylvie, Bernard, Cédric, Lazdunski, Michel, Darbon, Hervé

“…Acid‐sensing ion channels (ASIC) are proton‐gated sodium channels that have been implicated in pain transduction associated with acidosis in inflamed or…”
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Thermal Unfolding of a Llama Antibody Fragment:  A Two-State Reversible Process by Pérez, Janice M. J, Renisio, Jean G, Prompers, Jeanine J, van Platerink, Chris J, Cambillau, Christian, Darbon, Hervé, Frenken, Leon G. J

“…Camelids produce functional “heavy chain” antibodies which are devoid of light chains and CH1 domains [Hamers-Casterman, C., et al. (1993) Nature 363,…”
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Solution structure of two insect-specific spider toxins and their pharmacological interaction with the insect voltage-gated Na+ channel by Ferrat, G., Bosmans, F., Tytgat, J., Pimentel, C., Chagot, B., Gilles, N., Nakajima, T., Darbon, H., Corzo, G.

“…δ‐PaluIT1 and δ‐paluIT2 are toxins purified from the venom of the spider Paracoelotes luctuosus. Similar in sequence to μ‐agatoxins from Agelenopsis aperta,…”
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Solution structure of APETx1 from the sea anemone Anthopleura elegantissima: A new fold for an HERG toxin by Chagot, Benjamin, Diochot, Sylvie, Pimentel, Cyril, Lazdunski, Michel, Darbon, Hervé

“…APETx1 is a 42‐amino acid toxin purified from the venom of the sea anemone Anthopleura elegantissima. This cysteine‐rich peptide possesses three disulfide…”
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Selective Inhibition of Trypsins by Insect Peptides: Role of P6−P10 Loop by Kellenberger, C, Ferrat, G, Leone, P, Darbon, H, Roussel, A

“…PMP-D2 and HI, two peptides from Locusta migratoria, were shown to belong to the family of tight-binding protease inhibitors. However, they interact weakly…”
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The impact of the fourth disulfide bridge in scorpion toxins of the α-KTx6 subfamily by Carrega, Louis, Mosbah, Amor, Ferrat, Gilles, Beeton, Christine, Andreotti, Nicolas, Mansuelle, Pascal, Darbon, Hervé, De Waard, Michel, Sabatier, Jean-Marc

“…Animal toxins are highly reticulated and structured polypeptides that adopt a limited number of folds. In scorpion species, the most represented fold is the…”
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Solution structure of maurotoxin, a scorpion toxin from Scorpio maurus, with high affinity for voltage-gated potassium channels by Blanc, E., Sabatier, J.M., Kharrat, R., Meunier, S., El Ayeb, M., Van Rietschoten, J., Darbon, H.

“…Maurotoxin (MTX), purified from the scorpionid Scorpio maurus is a potent ligand for potassium channels. It shows a broad specificity as being active on Kv1.1…”
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An Overview of The Three Dimensional Structure of Short Spider Toxins by Ferrat, G., Darbon, H.

“…Arthropods are one of the most diverse animal groups on the Earth. Spiders belong to this phylum and they are ancient animals with a history going back some…”
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Solution Structure of Ptu1, a Toxin from the Assassin Bug Peirates turpis That Blocks the Voltage-Sensitive Calcium Channel N-Type by Bernard, Cédric, Corzo, Gerardo, Mosbah, Amor, Nakajima, Terumi, Darbon, Hervé

“…Ptu1 is a toxin from the assassin bug Peirates turpis which has been demonstrated to bind reversibly the N-type calcium channels and to have lower affinity…”
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Solution structure of HpTX2, a toxin from Heteropoda venatoria spider that blocks Kv4.2 potassium channel by BERNARD, CÉDRIC, LEGROS, CHRISTIAN, FERRAT, GILLES, BISCHOFF, ULRIKE, MARQUARDT, ANNETTE, PONGS, OLAF, DARBON, HERVÉ

“…HpTX2 is a toxin from the venom of Heteropoda venatoria spider that has been demonstrated to bind on Kv4.2 potassium channel. We have determined the solution…”
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Streptomyces matensis laminaripentaose hydrolase is an ‘inverting’ β-1,3-glucanase by Nishimura, T., Bignon, C., Allouch, J., Czjzek, M., Darbon, H., Watanabe, T., Henrissat, B.

“…The laminaripentaose-producing β-1,3-glucanase of Streptomyces matensis is a member of the glycoside hydrolase family GH-64. We have constructed and purified a…”
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Solution structure of TsKapa, a charybdotoxin-like scorpion toxin from Tityus serrulatus with high affinity for apamin-sensitive Ca2+-activated K+ channels by Blanc, E., Lecomte, C., Van Rietschoten, J., Sabatier, J.M., Darbon, H.

“…TsKapa (TsK), purified from the Buthidae Tityus serrulatus is a very high potent ligand for small‐conductance apamin‐sensitive calcium‐activated potassium…”
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Solution structure of TsKapa, a charybdotoxin-like scorpion toxin from Tityus serrulatus with high affinity for apamin-sensitive Ca(2+)-activated K+ channels by Blanc, E., Hassani, O., Meunier, S., Mansuelle, P., Sampieri, F., Rochat, H., Darbon, H., Lecomte, C., Rietschoten, J. V., Sabatier, J. M.

“…TsKapa (TsK), purified from the Buthidae Tityus serrulatus is a very high potent ligand for small-conductance apamin-sensitive calcium-activated potassium…”
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P05, a new leiurotoxin I-like scorpion toxin: synthesis and structure-activity relationships of the alpha-amidated analog, a ligand of Ca(2+)-activated K+ channels with increased affinity by Sabatier, J M, Zerrouk, H, Darbon, H, Mabrouk, K, Benslimane, A, Rochat, H, Martin-Eauclaire, M F, Van Rietschoten, J

“…The venom of the scorpion Androctonus mauretanicus mauretanicus contains a toxin, P05, which is structurally and functionally similar to scorpion leiurotoxin I…”
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Disulfide bridge reorganization induced by proline mutations in maurotoxin by Carlier, E., Fajloun, Z., Mansuelle, P., Fathallah, M., Mosbah, A., Oughideni, R., Sandoz, G., Di Luccio, E., Geib, S., Regaya, I., Brocard, J., Rochat, H., Darbon, H., Devaux, C., Sabatier, J.M., de Waard, M.

“…Maurotoxin (MTX) is a 34-residue toxin that has been isolated from the venom of the chactidae scorpion Scorpio maurus palmatus, and characterized. Together…”
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Solution structure of P05-NH2, a scorpion toxin analog with high affinity for the apamin-sensitive potassium channel by Meunier, S, Bernassau, J. M, Sabatier, J. M, Martin-Eauclaire, M. F, Van Rietschoten, J, Cambillau, C, Darbon, H

“…The venom of the scorpion Androctonus mauretanicus mauretanicus contains a toxin--PO5--which is structurally and functionally similar to scorpion leiurotoxin I…”
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Solution structure of P01, a natural scorpion peptide structurally analogous to scorpion toxins specific for apamin-sensitive potassium channel by Blanc, E., Fremont, V., Sizun, P., Meunier, S., Van Rietschoten, J., Thevand, A., Bernassau, J.-M., Darbon, H.

“…The venom of the North African scorpion Androctonus mauretanicus mauretanicus possesses numerous highly active neurotoxins that specifically bind to various…”
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Determination of the Three-Dimensional Structure of CC Chemokine Monocyte Chemoattractant Protein 3 by 1H Two-Dimensional NMR Spectroscopy by Meunier, S, Bernassau, J.-M, Guillemot, J.-C, Ferrara, P, Darbon, H

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Synthesis and Characterization of Leiurotoxin I Analogs Lacking One Disulfide Bridge:  Evidence That Disulfide Pairing 3−21 Is Not Required for Full Toxin Activity by Sabatier, J.-M, Lecomte, C, Mabrouk, K, Darbon, H, Oughideni, R, Canarelli, S, Rochat, H, Martin-Eauclaire, M.-F, Van Rietschoten, J

“…Leiurotoxin I (Lei-NH2), a toxin isolated from the venom of the scorpion Leiurus quinquestriatus hebraeus, is a blocker of the apamin-sensitive Ca2+-activated…”
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