| Ref 1 |
Purification and characterization of a unique, potent inhibitor of apamin binding from Leiurus quinquestriatus hebraeus venom. J Biol Chem. 1988 Jul 25;263(21):10192-7.
|
| Ref 2 |
Leiurotoxin I (scyllatoxin), a peptide ligand for Ca2(+)-activated K+ channels. Chemical synthesis, radiolabeling, and receptor characterization. J Biol Chem. 1990 Mar 15;265(8):4753-9.
|
| Ref 3 |
Design and characterization of a highly selective peptide inhibitor of the small conductance calcium-activated K+ channel, SkCa2. J Biol Chem. 2001 Nov 16;276(46):43145-51. doi: 10.1074/jbc.M106981200. Epub 2001 Aug 29.
|
| Ref 4 |
Role of disulfide bonds in folding and activity of leiurotoxin I: just two disulfides suffice. Biochemistry. 2002 Sep 24;41(38):11488-94. doi: 10.1021/bi026136m.
|
| Ref 5 |
Moving pieces in a taxonomic puzzle: venom 2D-LC/MS and data clustering analyses to infer phylogenetic relationships in some scorpions from the Buthidae family (Scorpiones). Toxicon. 2006 May;47(6):628-39. doi: 10.1016/j.toxicon.2006.01.015. Epub 2006 Mar 23.
|
| Ref 6 |
Solution conformation of leiurotoxin I (scyllatoxin) by 1H nuclear magnetic resonance. Resonance assignment and secondary structure. FEBS Lett. 1990 Jan 29;260(2):249-53. doi: 10.1016/0014-5793(90)80115-y.
|
| Ref 7 |
Characterization of a new leiurotoxin I-like scorpion toxin. PO5 from Androctonus mauretanicus mauretanicus. FEBS Lett. 1993 Apr 12;320(3):189-92. doi: 10.1016/0014-5793(93)80583-g.
|
| Ref 8 |
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. Biochemistry. 1993 Mar 23;32(11):2763-70. doi: 10.1021/bi00062a005.
|
| Ref 9 |
Solution structure of P05-NH2, a scorpion toxin analog with high affinity for the apamin-sensitive potassium channel. Biochemistry. 1993 Nov 16;32(45):11969-76. doi: 10.1021/bi00096a005.
|
| Ref 10 |
Characterization of a new peptide from Tityus serrulatus scorpion venom which is a ligand of the apamin-binding site. FEBS Lett. 1996 Jul 15;390(1):81-4. doi: 10.1016/0014-5793(96)00616-3.
|
| Ref 11 |
Novel components of Tityus serrulatus venom: A transcriptomic approach. Toxicon. 2021 Jan 15;189:91-104. doi: 10.1016/j.toxicon.2020.11.001. Epub 2020 Nov 10.
|
| Ref 12 |
A common "hot spot" confers hERG blockade activity to alpha-scorpion toxins affecting K+ channels. Biochem Pharmacol. 2008 Sep 15;76(6):805-15. doi: 10.1016/j.bcp.2008.07.008. Epub 2008 Jul 18.
|
| Ref 13 |
Tityus serrulatus scorpion venom and toxins: an overview. Protein Pept Lett. 2009;16(8):920-32. doi: 10.2174/092986609788923329.
|
| Ref 14 |
Solution structure of TsKapa, a charybdotoxin-like scorpion toxin from Tityus serrulatus with high affinity for apamin-sensitive Ca(2+)-activated K+ channels. Proteins. 1997 Nov;29(3):359-69. doi: 10.1002/(sici)1097-0134(199711)29:3<359::aid-prot9>3.0.co;2-5.
|
| Ref 15 |
Screening, large-scale production and structure-based classification of cystine-dense peptides. Nat Struct Mol Biol. 2018 Mar;25(3):270-278. doi: 10.1038/s41594-018-0033-9. Epub 2018 Feb 26.
|
| Ref 16 |
A novel structural class of K+-channel blocking toxin from the scorpion Pandinus imperator. Biochem J. 1996 May 1;315 ( Pt 3)(Pt 3):977-81. doi: 10.1042/bj3150977.
|
| Ref 17 |
Three new toxins from the scorpion Pandinus imperator selectively block certain voltage-gated K+ channels. Mol Pharmacol. 1996 Nov;50(5):1167-77.
|
| Ref 18 |
Block of ShakerB K+ channels by Pi1, a novel class of scorpion toxin. FEBS Lett. 1997 Jan 3;400(2):197-200. doi: 10.1016/s0014-5793(96)01387-7.
|
| Ref 19 |
Pandinus imperator scorpion venom blocks voltage-gated K+ channels in human lymphocytes. Biochem Biophys Res Commun. 1998 Jan 26;242(3):621-5. doi: 10.1006/bbrc.1997.8018.
|
| Ref 20 |
Chemical synthesis and characterization of Pi1, a scorpion toxin from Pandinus imperator active on K+ channels. Eur J Biochem. 2000 Aug;267(16):5149-55. doi: 10.1046/j.1432-1327.2000.01577.x.
|
| Ref 21 |
The 'functional' dyad of scorpion toxin Pi1 is not itself a prerequisite for toxin binding to the voltage-gated Kv1.2 potassium channels. Biochem J. 2004 Jan 1;377(Pt 1):25-36. doi: 10.1042/BJ20030115.
|
| Ref 22 |
A novel potassium channel blocking toxin from the scorpion Pandinus imperator: A 1H NMR analysis using a nano-NMR probe. Biochemistry. 1997 Mar 4;36(9):2649-58. doi: 10.1021/bi9617116.
|
| Ref 23 |
The impact of the fourth disulfide bridge in scorpion toxins of the alpha-KTx6 subfamily. Proteins. 2005 Dec 1;61(4):1010-23. doi: 10.1002/prot.20681.
|
| Ref 24 |
Characterization of PO1, a new peptide ligand of the apamin-sensitive Ca2+ activated K+ channel. Int J Pept Protein Res. 1996 Dec;48(6):514-21. doi: 10.1111/j.1399-3011.1996.tb00870.x.
|
| Ref 25 |
Solution structure of P01, a natural scorpion peptide structurally analogous to scorpion toxins specific for apamin-sensitive potassium channel. Proteins. 1996 Mar;24(3):359-69. doi: 10.1002/(SICI)1097-0134(199603)24:3<359::AID-PROT9>3.0.CO;2-B.
|
| Ref 26 |
The Scorpion Toxin Analogue BmKTX-D33H as a Potential Kv1.3 Channel-Selective Immunomodulator for Autoimmune Diseases. Toxins (Basel). 2016 Apr 19;8(4):115. doi: 10.3390/toxins8040115.
|
| Ref 27 |
Slotoxin, alphaKTx1.11, a new scorpion peptide blocker of MaxiK channels that differentiates between alpha and alpha+beta (beta1 or beta4) complexes. FEBS Lett. 2001 Sep 21;505(3):369-73. doi: 10.1016/s0014-5793(01)02791-0.
|
| Ref 28 |
The genome of Mesobuthus martensii reveals a unique adaptation model of arthropods. Nat Commun. 2013;4:2602. doi: 10.1038/ncomms3602.
|
| Ref 29 |
Scorpion Potassium Channel-blocking Defensin Highlights a Functional Link with Neurotoxin. J Biol Chem. 2016 Mar 25;291(13):7097-106. doi: 10.1074/jbc.M115.680611. Epub 2016 Jan 27.
|
| Ref 30 |
A Scorpion Defensin BmKDfsin4 Inhibits Hepatitis B Virus Replication in Vitro. Toxins (Basel). 2016 Apr 27;8(5):124. doi: 10.3390/toxins8050124.
|
| Ref 31 |
Identification of a new specific Kv1.3 channel blocker, Ctri9577, from the scorpion Chaerilus tricostatus. Peptides. 2012 Jul;36(1):94-9. doi: 10.1016/j.peptides.2012.04.023. Epub 2012 May 8.
|
| Ref 32 |
Ion channel modulation by scorpion hemolymph and its defensin ingredients highlights origin of neurotoxins in telson formed in Paleozoic scorpions. Int J Biol Macromol. 2020 Apr 1;148:351-363. doi: 10.1016/j.ijbiomac.2020.01.133. Epub 2020 Jan 15.
|
| Ref 33 |
Tamapin, a venom peptide from the Indian red scorpion (Mesobuthus tamulus) that targets small conductance Ca2+-activated K+ channels and afterhyperpolarization currents in central neurons. J Biol Chem. 2002 Nov 29;277(48):46101-9. doi: 10.1074/jbc.M206465200. Epub 2002 Sep 17.
|
| Ref 34 |
Cytotoxicity of recombinant tamapin and related toxin-like peptides on model cell lines. Chem Res Toxicol. 2014 Jun 16;27(6):960-7. doi: 10.1021/tx4004193. Epub 2014 May 12.
|
| Ref 35 |
Dynamic diversification from a putative common ancestor of scorpion toxins affecting sodium, potassium, and chloride channels. J Mol Evol. 1999 Feb;48(2):187-96. doi: 10.1007/pl00006457.
|
| Ref 36 |
Purification, sequence, and model structure of charybdotoxin, a potent selective inhibitor of calcium-activated potassium channels. Proc Natl Acad Sci U S A. 1988 May;85(10):3329-33. doi: 10.1073/pnas.85.10.3329.
|
| Ref 37 |
Charybdotoxin is a new member of the K+ channel toxin family that includes dendrotoxin I and mast cell degranulating peptide. Biochemistry. 1989 Dec 12;28(25):9708-14. doi: 10.1021/bi00451a025.
|
| Ref 38 |
Analysis of the blocking activity of charybdotoxin homologs and iodinated derivatives against Ca2+-activated K+ channels. J Membr Biol. 1989 Aug;109(3):269-81. doi: 10.1007/BF01870284.
|
| Ref 39 |
Solution synthesis of charybdotoxin (ChTX), a K+ channel blocker. Biochem Biophys Res Commun. 1990 Jul 31;170(2):684-90. doi: 10.1016/0006-291x(90)92145-p.
|
| Ref 40 |
Synthesis and structural characterization of charybdotoxin, a potent peptidyl inhibitor of the high conductance Ca2(+)-activated K+ channel. J Biol Chem. 1990 Nov 5;265(31):18745-8.
|
| Ref 41 |
Purification and characterization of three inhibitors of voltage-dependent K+ channels from Leiurus quinquestriatus var. hebraeus venom. Biochemistry. 1994 Jun 7;33(22):6834-9. doi: 10.1021/bi00188a012.
|
| Ref 42 |
Pharmacological characterization of five cloned voltage-gated K+ channels, types Kv1.1, 1.2, 1.3, 1.5, and 3.1, stably expressed in mammalian cell lines. Mol Pharmacol. 1994 Jun;45(6):1227-34.
|
| Ref 43 |
BeKm-1 is a HERG-specific toxin that shares the structure with ChTx but the mechanism of action with ErgTx1. Biophys J. 2003 May;84(5):3022-36. doi: 10.1016/S0006-3495(03)70028-9.
|
| Ref 44 |
Maurotoxin: a potent inhibitor of intermediate conductance Ca2+-activated potassium channels. Mol Pharmacol. 2003 Feb;63(2):409-18. doi: 10.1124/mol.63.2.409.
|
| Ref 45 |
Multidimensional signatures in antimicrobial peptides. Proc Natl Acad Sci U S A. 2004 May 11;101(19):7363-8. doi: 10.1073/pnas.0401567101. Epub 2004 Apr 26.
|
| Ref 46 |
A designer ligand specific for Kv1.3 channels from a scorpion neurotoxin-based library. Proc Natl Acad Sci U S A. 2009 Dec 29;106(52):22211-6. doi: 10.1073/pnas.0910123106. Epub 2009 Dec 10.
|
| Ref 47 |
Scorpion toxins interact with nicotinic acetylcholine receptors. FEBS Lett. 2019 Oct;593(19):2779-2789. doi: 10.1002/1873-3468.13530. Epub 2019 Jul 18.
|
| Ref 48 |
Molecular structure of charybdotoxin, a pore-directed inhibitor of potassium ion channels. Science. 1990 Aug 3;249(4968):521-4. doi: 10.1126/science.1696395.
|
| Ref 49 |
Molecular structure of charybdotoxin: retraction. Science. 1991 May 3;252(5006):631. doi: 10.1126/science.252.5006.631.b.
|
| Ref 50 |
Three-dimensional structure of natural charybdotoxin in aqueous solution by 1H-NMR. Charybdotoxin possesses a structural motif found in other scorpion toxins. Eur J Biochem. 1991 Feb 26;196(1):19-28. doi: 10.1111/j.1432-1033.1991.tb15780.x.
|
| Ref 51 |
Refined structure of charybdotoxin: common motifs in scorpion toxins and insect defensins. Science. 1991 Dec 6;254(5037):1521-3. doi: 10.1126/science.1720574.
|
| Ref 52 |
Analysis of side-chain organization on a refined model of charybdotoxin: structural and functional implications. Biochemistry. 1992 Sep 1;31(34):7756-64. doi: 10.1021/bi00149a003.
|
| Ref 53 |
Progress in multidimensional NMR investigations of peptide and protein 3-D structures in solution. From structure to functional aspects. Biochimie. 1992 Sep-Oct;74(9-10):825-36. doi: 10.1016/0300-9084(92)90065-m.
|
| Ref 54 |
NMR solution structure of a two-disulfide derivative of charybdotoxin: structural evidence for conservation of scorpion toxin alpha/beta motif and its hydrophobic side chain packing. Biochemistry. 1997 Apr 1;36(13):3760-6. doi: 10.1021/bi962720h.
|
| Ref 55 |
Mechanisms Underlying the Inhibition of KV1.3 Channel by Scorpion Toxin ImKTX58. Mol Pharmacol. 2022 Sep;102(3):150-160. doi: 10.1124/molpharm.121.000480. Epub 2022 Jun 28.
|
