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Page 1
Charybdotoxin and its effects on potassium channels.
Garcia ML, Knaus HG, Munujos P, Slaughter RS, Kaczorowski GJ. Garcia ML, et al. Am J Physiol. 1995 Jul;269(1 Pt 1):C1-10. doi: 10.1152/ajpcell.1995.269.1.C1. Am J Physiol. 1995. PMID: 7543240 Review.
Different areas of research have contributed to knowledge in this field. Charybdotoxin (ChTX), a 37-amino acid peptide isolated from venom of the scorpion Leiurus quinquestriatus var. hebraeus, represents a remarkable tool for studying K+ channels. ...
Different areas of research have contributed to knowledge in this field. Charybdotoxin (ChTX), a 37-amino acid peptide isolated from …
Development of charybdotoxin Q18F variant as a selective peptide blocker of neuronal BK(alpha + beta4) channel for the treatment of epileptic seizures.
Liu X, Tao J, Zhang S, Lan W, Yao Y, Wang C, Xue H, Ji Y, Li G, Cao C. Liu X, et al. Protein Sci. 2022 Dec;31(12):e4506. doi: 10.1002/pro.4506. Protein Sci. 2022. PMID: 36369672 Free PMC article.
Here, by nuclear magnetic resonance (NMR) and other biochemical techniques, we found that charybdotoxin might interact with the extracellular loop of human beta4 subunit (i.e., hbeta4-loop) of BK(alpha + beta4) channel at a molar ratio 4:1 (hbeta4-loop vs. charybdotoxin …
Here, by nuclear magnetic resonance (NMR) and other biochemical techniques, we found that charybdotoxin might interact with the extra …
Trans-toxin ion-sensitivity of charybdotoxin-blocked potassium-channels reveals unbinding transitional states.
Moldenhauer H, Díaz-Franulic I, Poblete H, Naranjo D. Moldenhauer H, et al. Elife. 2019 Jul 4;8:e46170. doi: 10.7554/eLife.46170. Elife. 2019. PMID: 31271355 Free PMC article.
Protein-protein complexes, lasting from microseconds to years, often involve induced-fit, challenging computational or kinetic analysis. Charybdotoxin (CTX), a peptide from the Leiurus scorpion venom, blocks voltage-gated K(+)-channels in a unique example of binding/unbind …
Protein-protein complexes, lasting from microseconds to years, often involve induced-fit, challenging computational or kinetic analysis. …
Charybdotoxin unbinding from the mKv1.3 potassium channel: a combined computational and experimental study.
Khabiri M, Nikouee A, Cwiklik L, Grissmer S, Ettrich R. Khabiri M, et al. J Phys Chem B. 2011 Oct 6;115(39):11490-500. doi: 10.1021/jp2061909. Epub 2011 Sep 13. J Phys Chem B. 2011. PMID: 21877740
Charybdotoxin, belonging to the group of so-called scorpion toxins, is a short peptide able to block many voltage-gated potassium channels, such as mKv1.3, with high affinity. We use a reliable homology model based on the high-resolution crystal structure of the 94% sequen …
Charybdotoxin, belonging to the group of so-called scorpion toxins, is a short peptide able to block many voltage-gated potassium cha …
Charybdotoxin blocks dendrotoxin-sensitive voltage-activated K+ channels.
Schweitz H, Stansfeld CE, Bidard JN, Fagni L, Maes P, Lazdunski M. Schweitz H, et al. FEBS Lett. 1989 Jul 3;250(2):519-22. doi: 10.1016/0014-5793(89)80788-4. FEBS Lett. 1989. PMID: 2473923 Free article.
Charybdotoxin, a short scorpion venom neurotoxin, which was thought to be specific for the blockade of Ca2+-activated K+ channels also blocks a class of voltage-sensitive K+ channels that are known to be the target of other peptide neurotoxins from snake and bee venoms suc …
Charybdotoxin, a short scorpion venom neurotoxin, which was thought to be specific for the blockade of Ca2+-activated K+ channels als …
Charybdotoxin-sensitive small conductance K(Ca) channel activated by bradykinin and substance P in endothelial cells.
Sollini M, Frieden M, Bény JL. Sollini M, et al. Br J Pharmacol. 2002 Aug;136(8):1201-9. doi: 10.1038/sj.bjp.0704819. Br J Pharmacol. 2002. PMID: 12163354 Free PMC article.
Charybdotoxin inhibited by 75% the bradykinin-induced current and by 80% the substance P-induced current. Charybdotoxin plus iberiotoxin (50 nM each) inhibited by 97% the bradykinin-response. ...
Charybdotoxin inhibited by 75% the bradykinin-induced current and by 80% the substance P-induced current. Charybdotoxin plus i …
Charybdotoxin binding in the I(Ks) pore demonstrates two MinK subunits in each channel complex.
Chen H, Kim LA, Rajan S, Xu S, Goldstein SA. Chen H, et al. Neuron. 2003 Sep 25;40(1):15-23. doi: 10.1016/s0896-6273(03)00570-1. Neuron. 2003. PMID: 14527430 Free article.
Here, I(Ks) channels assembled naturally by monomer subunits are compared to those with linked subunits that force defined stoichiometries. Two strategies that exploit charybdotoxin (CTX)-sensitive subunit variants are applied. First, CTX on rate, off rate, and equilibrium …
Here, I(Ks) channels assembled naturally by monomer subunits are compared to those with linked subunits that force defined stoichiometries. …
Charybdotoxin and margatoxin acting on the human voltage-gated potassium channel hKv1.3 and its H399N mutant: an experimental and computational comparison.
Nikouee A, Khabiri M, Grissmer S, Ettrich R. Nikouee A, et al. J Phys Chem B. 2012 May 3;116(17):5132-40. doi: 10.1021/jp2102463. Epub 2012 Apr 19. J Phys Chem B. 2012. PMID: 22490327
The effect of the pore-blocking peptides charybdotoxin and margatoxin, both scorpion toxins, on currents through human voltage-gated hK(v)1.3 wild-type and hK(v)1.3_H399N mutant potassium channels was characterized by the whole-cell patch clamp technique. ...
The effect of the pore-blocking peptides charybdotoxin and margatoxin, both scorpion toxins, on currents through human voltage-gated …
2,477 results