General Information of This Target
Target ID
BTDT10186
Target Name
Potassium voltage-gated channel subfamily A member 3
Target Bioclass
Transporter and channel
        Click to Show/Hide the Complete Species Lineage
N.A.
Toxin Information Related to This Target
                           Toxin Name Activity Data Type Activity Data Reference
 Toxin Info    HgTX1 (A19Y,Y37F) Dissociation constant
0.21 pM
[1]
 Toxin Info    Potassium channel toxin alpha-KTx 2.9 Dissociation constant
0.25 nM
[2]
 Toxin Info    Toxin II.11 (S14W) Dissociation constant
0.61 nM
[3]
 Toxin Info    Potassium channel toxin alpha-KTx 3.1 Dissociation constant
0.65 nM
[4- 11]
 Toxin Info    Potassium channel toxin alpha-KTx 2.11 Dissociation constant
0.98 nM
[2]
 Toxin Info    Potassium channel toxin alpha-KTx 32.1 Dissociation constant
1.3 nM
[12]
 Toxin Info    Potassium channel toxin alpha-KTx 2.1 Dissociation constant
6.8 nM
[13], [14], [15]
 Toxin Info    Potassium channel toxin alpha-KTx 2.13 Dissociation constant
7.2 nM
[16]
 Toxin Info    Kappa-actitoxin-Bgr1a Dissociation constant
10 - 39 nM
[17- 24]
 Toxin Info    Potassium channel toxin alpha-KTx 4.6 Dissociation constant
10.7 nM
[25]
 Toxin Info    Toxin II.11 (P10S) Dissociation constant
30 nM
[3]
 Toxin Info    Potassium channel toxin alpha-KTx 2.12 Dissociation constant
69 nM
[2]
 Toxin Info    PBTx3 Dissociation constant
99.4 nM
[26]
 Toxin Info    Toxin II.1 (A25R) Dissociation constant
112 nM
[3]
 Toxin Info    Toxin II.11 (A25) Dissociation constant
166 nM
[3]
 Toxin Info    ChTX (K27[Orn]) Dissociation constant
196 nM
[27]
 Toxin Info    Potassium channel toxin alpha-KTx 2.10 Dissociation constant
366 nM
[2]
 Toxin Info    Potassium channel toxin alpha-KTx 1.10 Dissociation constant
492 nM
[28], [26], [29]
 Toxin Info    Potassium channel toxin kappa-KTx 1.2 Dissociation constant
40 μM
[30- 34]
 Toxin Info    IbTx (S10A,G30N) Inhibition constant
43 nM
[35]
 Toxin Info    Venom peptide Sh41 Effect . [36]
 Toxin Info    Venom peptide Sh42 Effect . [36]
 Toxin Info    U-scoloptoxin(15)-Sm2a Effect . [37], [38]
 Toxin Info    S10A Inhibition rate . [35]
 Toxin Info    IbTx (D4N,D6N,S10A) Inhibition rate . [35]
 Toxin Info    IbTx (D4N,D6N,S10A,D19N,D24N) Inhibition rate . [35]
 Toxin Info    IbTx (D4N,S10A) Inhibition rate . [35]
 Toxin Info    IbTx (S10A,D24N) Inhibition rate . [35]
 Toxin Info    Hemitoxin Inhibition rate . [3]
 Toxin Info    MTX (C31[Abu],[Abu]) Inhibition rate . [39]
 Toxin Info    Leiuropeptide-1 (H9A,N21D) Inhibition rate . [40]
 Toxin Info    Leiuropeptide-1 (K11A,N21D) Inhibition rate . [40]
 Toxin Info    Leiuropeptide-1 (K13A,N21D) Inhibition rate . [40]
 Toxin Info    Mu-thomitoxin-Hme1c Inhibition rate . [41], [42]
 Toxin Info    Neurotoxic enhancer CSTX-13 Inhibition rate . [43], [44], [45], [46]
 Toxin Info    Conotoxin flf14c Inhibition rate . [47], [48]
 Toxin Info    Conopeptide Y-Pl1 Inhibition rate . [49]
 Toxin Info    Kappa-theraphotoxin-Ps1a Inhibition rate . [50], [51], [52]
 Toxin Info    Kappa-theraphotoxin-Ps1b Inhibition rate . [50]
 Toxin Info    Beta/kappa-theraphotoxin-Cg2a Inhibition rate . [53- 59]
 Toxin Info    Beta/kappa-theraphotoxin-Cg2a Inhibition rate . [53- 59]
 Toxin Info    Delta-theraphotoxin-Cg1a 1 Inhibition rate . [54- 64]
 Toxin Info    Kappa-theraphotoxin-Cg2a Inhibition rate . [54- 65]
 Toxin Info    Mambaquaretin-1 Inhibition rate . [66], [67], [68]
 Toxin Info    Toxin PhcrTx2 Inhibition rate . [69]
 Toxin Info    Conopeptide Y-Fe1 Inhibition rate . [49]
 Toxin Info    Alpha/kappa-conotoxin pl14a Inhibition rate . [70]
 Toxin Info    U18-theraphotoxin-Cg1a Inhibition rate . [54- 71]
 Toxin Info    U21-theraphotoxin-Cg1b Inhibition rate . [57], [54]
 Toxin Info    Kappa-theraphotoxin-Cg1a 1 Inhibition rate . [54- 73]
 Toxin Info    Kappa-theraphotoxin-Gr1a Inhibition rate . [74- 80]
 Toxin Info    Kappa-actitoxin-Ael2a Inhibition rate . [23- 86]
 Toxin Info    Beta/kappa-theraphotoxin-Cg1a Inhibition rate . [54- 88]
 Toxin Info    Short neurotoxin 1 Inhibition rate
2.71 %
[89], [90]
 Toxin Info    Kunitz-type serine protease inhibitor Inhibition rate
3.7 %
[91], [90]
 Toxin Info    Defensin BmKDfsin5 Inhibition rate
9 %
[92], [93]
 Toxin Info    Potassium channel toxin alpha-KTx 29.1 Inhibition rate
13.2 %
[94], [95]
 Toxin Info    Potassium channel toxin alpha-KTx 29.3 Inhibition rate
13.2 %
[94], [95]
 Toxin Info    Potassium channel toxin alpha-KTx 29.2 Inhibition rate
13.2 %
[95]
 Toxin Info    Delta/kappa-actitoxin-Avd4a Inhibition rate
17 %
[23- 100]
 Toxin Info    Potassium channel toxin kappa-KTx 5.1 Inhibition rate
20 %
[7- 103]
 Toxin Info    Potassium channel toxin AbeTx1 Inhibition rate
20 %
[104]
 Toxin Info    Kunitz-type kappaPI-theraphotoxin-Hs1a Inhibition rate
28 %
[105- 109]
 Toxin Info    Kunitz-type kappaPI-theraphotoxin-Hs1a Inhibition rate
28 %
[105- 109]
 Toxin Info    Potassium channel toxin kappa-KTx 2.8 Inhibition rate
35.1 %
[95- 110]
 Toxin Info    Cysteine-rich venom protein natrin-1 Inhibition rate
46 %
[111- 116]
 Toxin Info    Defensin BmKDfsin4 Inhibition rate
61 %
[92- 118]
 Toxin Info    Potassium channel toxin alpha-KTx 30.1 Inhibition rate
64.1 %
[95- 119]
 Toxin Info    Kappa-stichotoxin-She3a IC50
10 - 250 pM
[19- 132]
 Toxin Info    Potassium channel toxin ImKTx88 IC50
91 pM
[133]
 Toxin Info    Potassium channel toxin alpha-KTx 6.3 IC50
1129 pM
[29- 140]
 Toxin Info    Potassium channel toxin alpha-KTx 3.7 IC50
0.014 nM
[7- 143]
 Toxin Info    Potassium channel toxin alpha-KTx 2.5 IC50
0.086 nM
[1- 144]
 Toxin Info    HgTX1 (A19Y,Y37F) IC50
0.153 nM
[1]
 Toxin Info    Potassium channel toxin alpha-KTx 2.2 IC50
0.23 nM
[145], [146], [147], [148]
 Toxin Info    Potassium channel toxin alpha-KTx 2.2 IC50
0.23 nM
[1- 151]
 Toxin Info    Potassium channel toxin alpha-KTx Ctri9577 IC50
0.49 nM
[152]
 Toxin Info    Potassium channel toxin alpha-KTx 12.1 IC50
0.55 nM
[145- 161]
 Toxin Info    Potassium channel toxin alpha-KTx 1.2 IC50
1 nM
[162], [163], [164]
 Toxin Info    Kappa-thalatoxin-Tas2a IC50
3.4 nM
[90- 165]
 Toxin Info    Potassium channel toxin alpha-KTx 3.11 IC50
7.2 nM
[34- 166]
 Toxin Info    Potassium channel toxin alpha-KTx 3.19 IC50
8.9 nM
[167], [168]
 Toxin Info    Apamin IC50
13 nM
[169- 188]
 Toxin Info    Potassium channel toxin alpha-KTx 9.5 IC50
15 nM
[189]
 Toxin Info    Defensin BmKDfsin3 IC50
23.4 nM
[92], [93]
 Toxin Info    Potassium channel toxin alpha-KTx 12.5 IC50
28 nM
[94- 190]
 Toxin Info    Potassium channel toxin alpha-KTx 16.7 IC50
118.3 ± 55.8 nM
[191]
 Toxin Info    Kunitz-type serine protease inhibitor IX IC50
120 nM
[192], [193], [194]
 Toxin Info    Potassium channel toxin alpha-KTx 6.2 IC50
150 - 180 nM
[138- 204]
 Toxin Info    Crotamine IC50
287 nM
[205- 222]
 Toxin Info    Defensin BmKDfsin4 IC50
510.2 nM
[92- 118]
 Toxin Info    Conopeptide Y-Pl1 IC50
>50 μM
[49]
 Toxin Info    Conopeptide Y-Fe1 IC50
>50 μM
[49]
 Toxin Info    Potassium channel toxin alpha-KTx 6 hetlaxin IC50
0.48 μM
[223], [224]
 Toxin Info    Scorpine-like peptide Ev37 IC50
0.95 μM
[225]
 Toxin Info    Kappa-actitoxin-Ate1a IC50
3.051 μM
[226]
References
Ref 1 Subunit composition of brain voltage-gated potassium channels determined by hongotoxin-1, a novel peptide derived from Centruroides limbatus venom. J Biol Chem. 1998 Jan 30;273(5):2639-44. doi: 10.1074/jbc.273.5.2639.
Ref 2 Novel alpha-KTx peptides from the venom of the scorpion Centruroides elegans selectively blockade Kv1.3 over IKCa1 K+ channels of T cells. Toxicon. 2005 Sep 15;46(4):418-29. doi: 10.1016/j.toxicon.2005.06.001.
Ref 3 Insights into alpha-K toxin specificity for K+ channels revealed through mutations in noxiustoxin. Biochemistry. 2001 Sep 18;40(37):10987-97. doi: 10.1021/bi010227m.
Ref 4 Kaliotoxin, a novel peptidyl inhibitor of neuronal BK-type Ca(2+)-activated K+ channels characterized from Androctonus mauretanicus mauretanicus venom. J Biol Chem. 1992 Jan 25;267(3):1640-7.
Ref 5 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 6 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 7 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 8 Kaliotoxin (1-37) shows structural differences with related potassium channel blockers. Biochemistry. 1994 Nov 29;33(47):14256-63. doi: 10.1021/bi00251a038.
Ref 9 3D structure of kaliotoxin: is residue 34 a key for channel selectivity?. J Pept Sci. 1997 Jul-Aug;3(4):314-9. doi: 10.1002/(SICI)1099-1387(199707)3:4%3C314::AID-PSC117%3E3.0.CO;2-E.
Ref 10 A concept for rapid protein-structure determination by solid-state NMR spectroscopy. Angew Chem Int Ed Engl. 2005 Mar 29;44(14):2089-92. doi: 10.1002/anie.200462516.
Ref 11 Toxin-induced conformational changes in a potassium channel revealed by solid-state NMR. Nature. 2006 Apr 13;440(7086):959-62. doi: 10.1038/nature04649.
Ref 12 Cm28, a scorpion toxin having a unique primary structure, inhibits KV1.2 and KV1.3 with high affinity. J Gen Physiol. 2022 Aug 1;154(8):e202213146. doi: 10.1085/jgp.202213146. Epub 2022 Jun 14.
Ref 13 Charybdotoxin and noxiustoxin, two homologous peptide inhibitors of the K+ (Ca2+) channel. FEBS Lett. 1988 Jan 4;226(2):280-4. doi: 10.1016/0014-5793(88)81439-x.
Ref 14 Synthetic peptides corresponding to the sequence of noxiustoxin indicate that the active site of this K+ channel blocker is located on its amino-terminal portion. J Neural Transm. 1989;77(1):11-20. doi: 10.1007/BF01255815.
Ref 15 Determination of the three-dimensional solution structure of noxiustoxin: analysis of structural differences with related short-chain scorpion toxins. Biochemistry. 1995 Dec 26;34(51):16563-73. doi: 10.1021/bi00051a004.
Ref 16 A selective blocker of Kv1.2 and Kv1.3 potassium channels from the venom of the scorpion Centruroides suffusus suffusus. Biochem Pharmacol. 2008 Oct 30;76(9):1142-54. doi: 10.1016/j.bcp.2008.08.018. Epub 2008 Aug 22.
Ref 17 A potassium channel toxin from the secretion of the sea anemone Bunodosoma granulifera. Isolation, amino acid sequence and biological activity. Biochim Biophys Acta. 1993 May 7;1157(1):86-92. doi: 10.1016/0304-4165(93)90082-j.
Ref 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. Eur J Biochem. 1997 Feb 15;244(1):192-202. doi: 10.1111/j.1432-1033.1997.00192.x.
Ref 19 Structural conservation of the pores of calcium-activated and voltage-gated potassium channels determined by a sea anemone toxin. J Biol Chem. 1999 Jul 30;274(31):21885-92. doi: 10.1074/jbc.274.31.21885.
Ref 20 Mapping the functional anatomy of BgK on Kv1.1, Kv1.2, and Kv1.3. Clues to design analogs with enhanced selectivity. J Biol Chem. 1999 Dec 10;274(50):35653-61. doi: 10.1074/jbc.274.50.35653.
Ref 21 Characterization of a novel radiolabeled peptide selective for a subpopulation of voltage-gated potassium channels in mammalian brain. J Biol Chem. 2002 Feb 8;277(6):3886-93. doi: 10.1074/jbc.M109886200. Epub 2001 Nov 13.
Ref 22 Peptide fingerprinting of the neurotoxic fractions isolated from the secretions of sea anemones Stichodactyla helianthus and Bunodosoma granulifera. New members of the APETx-like family identified by a 454 pyrosequencing approach. Peptides. 2012 Mar;34(1):26-38. doi: 10.1016/j.peptides.2011.10.011. Epub 2011 Oct 12.
Ref 23 Development of a rational nomenclature for naming peptide and protein toxins from sea anemones. Toxicon. 2012 Sep 15;60(4):539-50. doi: 10.1016/j.toxicon.2012.05.020. Epub 2012 Jun 5.
Ref 24 On the convergent evolution of animal toxins. Conservation of a diad of functional residues in potassium channel-blocking toxins with unrelated structures. J Biol Chem. 1997 Feb 14;272(7):4302-9. doi: 10.1074/jbc.272.7.4302.
Ref 25 Tst26, a novel peptide blocker of Kv1.2 and Kv1.3 channels from the venom of Tityus stigmurus. Toxicon. 2009 Sep 15;54(4):379-89. doi: 10.1016/j.toxicon.2009.05.023. Epub 2009 Jun 3.
Ref 26 Evidence for a function-specific mutation in the neurotoxin, parabutoxin 3. Eur J Neurosci. 2003 May;17(9):1786-92. doi: 10.1046/j.1460-9568.2003.02613.x.
Ref 27 Structure-guided transformation of charybdotoxin yields an analog that selectively targets Ca(2+)-activated over voltage-gated K(+) channels. J Biol Chem. 2000 Jan 14;275(2):1201-8. doi: 10.1074/jbc.275.2.1201.
Ref 28 Purification, characterization and biosynthesis of parabutoxin 3, a component of Parabuthus transvaalicus venom. Eur J Biochem. 2002 Apr;269(7):1854-65. doi: 10.1046/j.1432-1033.2002.02833.x.
Ref 29 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 30 kappa-Hefutoxin1, a novel toxin from the scorpion Heterometrus fulvipes with unique structure and function. Importance of the functional diad in potassium channel selectivity. J Biol Chem. 2002 Aug 16;277(33):30040-7. doi: 10.1074/jbc.M111258200. Epub 2002 May 28.
Ref 31 Synthesis and characterization of amino acid deletion analogs of -hefutoxin 1, a scorpion toxin on potassium channels. Toxicon. 2013 Sep;71:25-30. doi: 10.1016/j.toxicon.2013.05.010. Epub 2013 May 29.
Ref 32 Expanding the pharmacological profile of -hefutoxin 1 and analogues: A focus on the inhibitory effect on the oncogenic channel K(v)10.1. Peptides. 2017 Dec;98:43-50. doi: 10.1016/j.peptides.2016.08.008. Epub 2016 Aug 28.
Ref 33 Assignment of voltage-gated potassium channel blocking activity to kappa-KTx1.3, a non-toxic homologue of kappa-hefutoxin-1, from Heterometrus spinifer venom. Biochem Pharmacol. 2005 Feb 15;69(4):669-78. doi: 10.1016/j.bcp.2004.10.018. Epub 2004 Dec 29.
Ref 34 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 35 Glycine 30 in iberiotoxin is a critical determinant of its specificity for maxi-K versus K(V) channels. FEBS Lett. 2002 Sep 11;527(1-3):298-302. doi: 10.1016/s0014-5793(02)03256-8.
Ref 36 Isolation and characterization of FMRFamide-like peptides in the venoms of solitary sphecid wasps. Peptides. 2021 Aug;142:170575. doi: 10.1016/j.peptides.2021.170575. Epub 2021 May 20.
Ref 37 Clawing through evolution: toxin diversification and convergence in the ancient lineage Chilopoda (centipedes). Mol Biol Evol. 2014 Aug;31(8):2124-48. doi: 10.1093/molbev/msu162. Epub 2014 May 20.
Ref 38 A Centipede Toxin Family Defines an Ancient Class of CS Defensins. Structure. 2019 Feb 5;27(2):315-326.e7. doi: 10.1016/j.str.2018.10.022. Epub 2018 Dec 13.
Ref 39 Maurotoxin and the Kv1.1 channel: voltage-dependent binding upon enantiomerization of the scorpion toxin disulfide bridge Cys31-Cys34. J Pept Res. 2000 Mar;55(3):246-54. doi: 10.1034/j.1399-3011.2000.00170.x.
Ref 40 Mapping the Interaction Anatomy of BmP02 on Kv1.3 Channel. Sci Rep. 2016 Jul 11;6:29431. doi: 10.1038/srep29431.
Ref 41 Structure of membrane-active toxin from crab spider Heriaeus melloteei suggests parallel evolution of sodium channel gating modifiers in Araneomorphae and Mygalomorphae. J Biol Chem. 2015 Jan 2;290(1):492-504. doi: 10.1074/jbc.M114.595678. Epub 2014 Oct 28.
Ref 42 Spider toxin inhibits gating pore currents underlying periodic paralysis. Proc Natl Acad Sci U S A. 2018 Apr 24;115(17):4495-4500. doi: 10.1073/pnas.1720185115. Epub 2018 Apr 10.
Ref 43 The Dual Prey-Inactivation Strategy of Spiders-In-Depth Venomic Analysis of Cupiennius salei. Toxins (Basel). 2019 Mar 19;11(3):167. doi: 10.3390/toxins11030167.
Ref 44 CSTX-13, a highly synergistically acting two-chain neurotoxic enhancer in the venom of the spider Cupiennius salei (Ctenidae). Proc Natl Acad Sci U S A. 2004 Aug 3;101(31):11251-6. doi: 10.1073/pnas.0402226101. Epub 2004 Jul 22.
Ref 45 Spider venom: enhancement of venom efficacy mediated by different synergistic strategies in Cupiennius salei. J Exp Biol. 2005 Jun;208(Pt 11):2115-21. doi: 10.1242/jeb.01594.
Ref 46 Neurotoxin Merging: A Strategy Deployed by the Venom of the Spider Cupiennius salei to Potentiate Toxicity on Insects. Toxins (Basel). 2020 Apr 12;12(4):250. doi: 10.3390/toxins12040250.
Ref 47 Definition of the R-superfamily of conotoxins: Structural convergence of helix-loop-helix peptidic scaffolds. Peptides. 2018 Sep;107:75-82. doi: 10.1016/j.peptides.2018.06.002. Epub 2018 Jul 21.
Ref 48 A novel conotoxin framework with a helix-loop-helix (Cs alpha/alpha) fold. Biochemistry. 2005 Dec 13;44(49):15986-96. doi: 10.1021/bi0511181.
Ref 49 Tyrosine-rich conopeptides affect voltage-gated K+ channels. J Biol Chem. 2008 Aug 22;283(34):23026-32. doi: 10.1074/jbc.M800084200. Epub 2008 May 27.
Ref 50 Effects of phrixotoxins on the Kv4 family of potassium channels and implications for the role of Ito1 in cardiac electrogenesis. Br J Pharmacol. 1999 Jan;126(1):251-63. doi: 10.1038/sj.bjp.0702283.
Ref 51 Studies examining the relationship between the chemical structure of protoxin II and its activity on voltage gated sodium channels. J Med Chem. 2014 Aug 14;57(15):6623-31. doi: 10.1021/jm500687u. Epub 2014 Jul 24.
Ref 52 Solution structure of Phrixotoxin 1, a specific peptide inhibitor of Kv4 potassium channels from the venom of the theraphosid spider Phrixotrichus auratus. Protein Sci. 2004 May;13(5):1197-208. doi: 10.1110/ps.03584304.
Ref 53 Isolation and characterization of Jingzhaotoxin-V, a novel neurotoxin from the venom of the spider Chilobrachys jingzhao. Toxicon. 2007 Mar 1;49(3):388-99. doi: 10.1016/j.toxicon.2006.10.012. Epub 2006 Nov 6.
Ref 54 Proteomic and peptidomic analysis of the venom from Chinese tarantula Chilobrachys jingzhao. Proteomics. 2007 Jun;7(11):1892-907. doi: 10.1002/pmic.200600785.
Ref 55 [Inhibition of Jingzhaotoxin-V on Kv4.3 channel]. Sheng Li Xue Bao. 2010 Jun 25;62(3):255-60.
Ref 56 Effects and mechanism of Chinese tarantula toxins on the Kv2.1 potassium channels. Biochem Biophys Res Commun. 2007 Jan 19;352(3):799-804. doi: 10.1016/j.bbrc.2006.11.086. Epub 2006 Nov 27.
Ref 57 Molecular diversity and evolution of cystine knot toxins of the tarantula Chilobrachys jingzhao. Cell Mol Life Sci. 2008 Aug;65(15):2431-44. doi: 10.1007/s00018-008-8135-x.
Ref 58 Molecular surface of JZTX-V (-Theraphotoxin-Cj2a) interacting with voltage-gated sodium channel subtype NaV1.4. Toxins (Basel). 2014 Jul 23;6(7):2177-93. doi: 10.3390/toxins6072177.
Ref 59 Pharmacological characterization of potent and selective NaV1.7 inhibitors engineered from Chilobrachys jingzhao tarantula venom peptide JzTx-V. PLoS One. 2018 May 3;13(5):e0196791. doi: 10.1371/journal.pone.0196791. eCollection 2018.
Ref 60 Jingzhaotoxin-I, a novel spider neurotoxin preferentially inhibiting cardiac sodium channel inactivation. J Biol Chem. 2005 Apr 1;280(13):12069-76. doi: 10.1074/jbc.M411651200. Epub 2004 Nov 17.
Ref 61 Characterization of the excitatory mechanism induced by Jingzhaotoxin-I inhibiting sodium channel inactivation. Toxicon. 2007 Sep 15;50(4):507-17. doi: 10.1016/j.toxicon.2007.04.018. Epub 2007 May 3.
Ref 62 Molecular determinants for the tarantula toxin jingzhaotoxin-I interacting with potassium channel Kv2.1. Toxicon. 2013 Mar 1;63:129-36. doi: 10.1016/j.toxicon.2012.12.001. Epub 2012 Dec 13.
Ref 63 Molecular determinant for the tarantula toxin Jingzhaotoxin-I slowing the fast inactivation of voltage-gated sodium channels. Toxicon. 2016 Mar 1;111:13-21. doi: 10.1016/j.toxicon.2015.12.009. Epub 2015 Dec 23.
Ref 64 Sequence-specific assignment of 1H-NMR resonance and determination of the secondary structure of Jingzhaotoxin-I. Acta Biochim Biophys Sin (Shanghai). 2005 Aug;37(8):567-72. doi: 10.1111/j.1745-7270.2005.00078.x.
Ref 65 Jingzhaotoxin-XII, a gating modifier specific for Kv4.1 channels. Toxicon. 2007 Oct;50(5):646-52. doi: 10.1016/j.toxicon.2007.05.009. Epub 2007 Jun 3.
Ref 66 Green mamba peptide targets type-2 vasopressin receptor against polycystic kidney disease. Proc Natl Acad Sci U S A. 2017 Jul 3;114(27):7154-7159. doi: 10.1073/pnas.1620454114. Epub 2017 Jun 19.
Ref 67 A snake toxin as a theranostic agent for the type 2 vasopressin receptor. Theranostics. 2020 Sep 18;10(25):11580-11594. doi: 10.7150/thno.47485. eCollection 2020.
Ref 68 A new Kunitz-type snake toxin family associated with an original mode of interaction with the vasopressin 2 receptor. Br J Pharmacol. 2022 Jul;179(13):3470-3481. doi: 10.1111/bph.15814. Epub 2022 Feb 28.
Ref 69 PhcrTx2, a New Crab-Paralyzing Peptide Toxin from the Sea Anemone Phymanthus crucifer. Toxins (Basel). 2018 Feb 7;10(2):72. doi: 10.3390/toxins10020072.
Ref 70 A novel conotoxin inhibitor of Kv1.6 channel and nAChR subtypes defines a new superfamily of conotoxins. Biochemistry. 2006 Jul 11;45(27):8331-40. doi: 10.1021/bi060263r.
Ref 71 Jingzhaotoxin-IX, a novel gating modifier of both sodium and potassium channels from Chinese tarantula Chilobrachys jingzhao. Neuropharmacology. 2009 Aug;57(2):77-87. doi: 10.1016/j.neuropharm.2009.04.009. Epub 2009 May 4.
Ref 72 Solution structure and functional characterization of jingzhaotoxin-XI: a novel gating modifier of both potassium and sodium channels. Biochemistry. 2006 Dec 26;45(51):15591-600. doi: 10.1021/bi061457+.
Ref 73 The tarantula toxin jingzhaotoxin-XI (-theraphotoxin-Cj1a) regulates the activation and inactivation of the voltage-gated sodium channel Nav1.5. Toxicon. 2014 Dec 15;92:6-13. doi: 10.1016/j.toxicon.2014.09.002. Epub 2014 Sep 18.
Ref 74 An inhibitor of the Kv2.1 potassium channel isolated from the venom of a Chilean tarantula. Neuron. 1995 Oct;15(4):941-9. doi: 10.1016/0896-6273(95)90184-1.
Ref 75 Hanatoxin modifies the gating of a voltage-dependent K+ channel through multiple binding sites. Neuron. 1997 Apr;18(4):665-73. doi: 10.1016/s0896-6273(00)80306-2.
Ref 76 Mapping the receptor site for hanatoxin, a gating modifier of voltage-dependent K+ channels. Neuron. 1997 Apr;18(4):675-82. doi: 10.1016/s0896-6273(00)80307-4.
Ref 77 Gating modifier toxins reveal a conserved structural motif in voltage-gated Ca2+ and K+ channels. Proc Natl Acad Sci U S A. 1998 Jul 21;95(15):8585-9. doi: 10.1073/pnas.95.15.8585.
Ref 78 Voltage-sensor activation with a tarantula toxin as cargo. Nature. 2005 Aug 11;436(7052):857-60. doi: 10.1038/nature03873.
Ref 79 Gating modifier peptides as probes of pancreatic beta-cell physiology. Toxicon. 2007 Feb;49(2):231-8. doi: 10.1016/j.toxicon.2006.09.012. Epub 2006 Sep 23.
Ref 80 Solution structure of hanatoxin1, a gating modifier of voltage-dependent K(+) channels: common surface features of gating modifier toxins. J Mol Biol. 2000 Mar 31;297(3):771-80. doi: 10.1006/jmbi.2000.3609.
Ref 81 APETx1, a new toxin from the sea anemone Anthopleura elegantissima, blocks voltage-gated human ether-a-go-go-related gene potassium channels. Mol Pharmacol. 2003 Jul;64(1):59-69. doi: 10.1124/mol.64.1.59.
Ref 82 Species diversity and peptide toxins blocking selectivity of ether-a-go-go-related gene subfamily K+ channels in the central nervous system. Mol Pharmacol. 2006 May;69(5):1673-83. doi: 10.1124/mol.105.019729. Epub 2006 Feb 23.
Ref 83 APETx1 from sea anemone Anthopleura elegantissima is a gating modifier peptide toxin of the human ether-a-go-go- related potassium channel. Mol Pharmacol. 2007 Aug;72(2):259-68. doi: 10.1124/mol.107.035840. Epub 2007 May 1.
Ref 84 A natural point mutation changes both target selectivity and mechanism of action of sea anemone toxins. FASEB J. 2012 Dec;26(12):5141-51. doi: 10.1096/fj.12-218479. Epub 2012 Sep 12.
Ref 85 Defensin-neurotoxin dyad in a basally branching metazoan sea anemone. FEBS J. 2017 Oct;284(19):3320-3338. doi: 10.1111/febs.14194. Epub 2017 Sep 6.
Ref 86 Solution structure of APETx1 from the sea anemone Anthopleura elegantissima: a new fold for an HERG toxin. Proteins. 2005 May 1;59(2):380-6. doi: 10.1002/prot.20425.
Ref 87 Jingzhaotoxin-III, a novel spider toxin inhibiting activation of voltage-gated sodium channel in rat cardiac myocytes. J Biol Chem. 2004 Jun 18;279(25):26220-6. doi: 10.1074/jbc.M401387200. Epub 2004 Apr 14.
Ref 88 Solution structure of Jingzhaotoxin-III, a peptide toxin inhibiting both Nav1.5 and Kv2.1 channels. Toxicon. 2007 Jul;50(1):135-43. doi: 10.1016/j.toxicon.2007.03.006. Epub 2007 Mar 16.
Ref 89 Neurotoxins from the venoms of the sea snakes Hydrophis ornatus and Hydrophis lapemoides. Biochem J. 1983 Jul 1;213(1):31-8. doi: 10.1042/bj2130031.
Ref 90 Identification of novel Kv1.3 targeting venom peptides by a single round of autocrine-based selection. Biochem Biophys Res Commun. 2019 Feb 19;509(4):954-959. doi: 10.1016/j.bbrc.2019.01.014. Epub 2019 Jan 14.
Ref 91 Purification and characterization of a Kunitz-type trypsin inhibitor from Leaf-nosed viper venom. FEBS Lett. 1991 Dec 2;294(1-2):141-3. doi: 10.1016/0014-5793(91)81361-b.
Ref 92 The genome of Mesobuthus martensii reveals a unique adaptation model of arthropods. Nat Commun. 2013;4:2602. doi: 10.1038/ncomms3602.
Ref 93 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 94 Comparative venom gland transcriptome analysis of the scorpion Lychas mucronatus reveals intraspecific toxic gene diversity and new venomous components. BMC Genomics. 2010 Jul 28;11:452. doi: 10.1186/1471-2164-11-452.
Ref 95 Structural and functional diversity of acidic scorpion potassium channel toxins. PLoS One. 2012;7(4):e35154. doi: 10.1371/journal.pone.0035154. Epub 2012 Apr 12.
Ref 96 Sea anemone peptides with a specific blocking activity against the fast inactivating potassium channel Kv3.4. J Biol Chem. 1998 Mar 20;273(12):6744-9. doi: 10.1074/jbc.273.12.6744.
Ref 97 Modulation of Kv3 subfamily potassium currents by the sea anemone toxin BDS: significance for CNS and biophysical studies. J Neurosci. 2005 Sep 21;25(38):8735-45. doi: 10.1523/JNEUROSCI.2119-05.2005.
Ref 98 Modulation of neuronal sodium channels by the sea anemone peptide BDS-I. J Neurophysiol. 2012 Jun;107(11):3155-67. doi: 10.1152/jn.00785.2011. Epub 2012 Mar 21.
Ref 99 A proton nuclear magnetic resonance study of the antihypertensive and antiviral protein BDS-I from the sea anemone Anemonia sulcata: sequential and stereospecific resonance assignment and secondary structure. Biochemistry. 1989 Mar 7;28(5):2178-87. doi: 10.1021/bi00431a032.
Ref 100 Determination of the three-dimensional solution structure of the antihypertensive and antiviral protein BDS-I from the sea anemone Anemonia sulcata: a study using nuclear magnetic resonance and hybrid distance geometry-dynamical simulated annealing. Biochemistry. 1989 Mar 7;28(5):2188-98. doi: 10.1021/bi00431a033.
Ref 101 Purification, molecular cloning and functional characterization of HelaTx1 (Heterometrus laoticus): the first member of a new -KTX subfamily. Biochem Pharmacol. 2012 May 1;83(9):1307-17. doi: 10.1016/j.bcp.2012.01.021. Epub 2012 Jan 24.
Ref 102 Effects of deletion and insertion of amino acids on the activity of HelaTx1, a scorpion toxin on potassium channels. Toxicon. 2016 Mar 1;111:1-5. doi: 10.1016/j.toxicon.2015.12.014. Epub 2015 Dec 24.
Ref 103 Solution structure and functional analysis of HelaTx1: the first toxin member of the -KTx5 subfamily. BMB Rep. 2020 May;53(5):260-265. doi: 10.5483/BMBRep.2020.53.5.256.
Ref 104 AbeTx1 Is a Novel Sea Anemone Toxin with a Dual Mechanism of Action on Shaker-Type K? Channels Activation. Mar Drugs. 2018 Oct 1;16(10):360. doi: 10.3390/md16100360.
Ref 105 Genomic organization and cloning of novel genes encoding toxin-like peptides of three superfamilies from the spider Orinithoctonus huwena. Peptides. 2008 Oct;29(10):1679-84. doi: 10.1016/j.peptides.2008.06.001. Epub 2008 Jun 12.
Ref 106 Discovery of a distinct superfamily of Kunitz-type toxin (KTT) from tarantulas. PLoS One. 2008;3(10):e3414. doi: 10.1371/journal.pone.0003414. Epub 2008 Oct 15.
Ref 107 Molecular diversification based on analysis of expressed sequence tags from the venom glands of the Chinese bird spider Ornithoctonus huwena. Toxicon. 2008 Jun 15;51(8):1479-89. doi: 10.1016/j.toxicon.2008.03.024. Epub 2008 Mar 27.
Ref 108 An overview of peptide toxins from the venom of the Chinese bird spider Selenocosmia huwena Wang [=Ornithoctonus huwena (Wang)]. Toxicon. 2004 Apr;43(5):575-85. doi: 10.1016/j.toxicon.2004.02.005.
Ref 109 Nuclear magnetic resonance studies on huwentoxin-XI from the Chinese bird spider Ornithoctonus huwena: 15N labeling and sequence-specific 1H, 15N nuclear magnetic resonance assignments. Acta Biochim Biophys Sin (Shanghai). 2006 Jul;38(7):457-66. doi: 10.1111/j.1745-7270.2006.00191.x.
Ref 110 Molecular diversity of toxic components from the scorpion Heterometrus petersii venom revealed by proteomic and transcriptome analysis. Proteomics. 2010 Jul;10(13):2471-85. doi: 10.1002/pmic.200900763.
Ref 111 Purification and cloning of cysteine-rich proteins from Trimeresurus jerdonii and Naja atra venoms. Toxicon. 2003 Oct;42(5):539-47. doi: 10.1016/s0041-0101(03)00234-4.
Ref 112 Purification and characterization of Taiwan cobra venom proteins with weak toxicity. Toxicon. 2005 Jan;45(1):21-5. doi: 10.1016/j.toxicon.2004.09.002.
Ref 113 Structural and functional analysis of natrin, a venom protein that targets various ion channels. Biochem Biophys Res Commun. 2006 Dec 15;351(2):443-8. doi: 10.1016/j.bbrc.2006.10.067. Epub 2006 Oct 20.
Ref 114 Structural and functional characterization of ryanodine receptor-natrin toxin interaction. Biophys J. 2008 Nov 1;95(9):4289-99. doi: 10.1529/biophysj.108.137224. Epub 2008 Jul 25.
Ref 115 Purification, crystallization and preliminary X-ray crystallographic analysis of a cysteine-rich secretory protein (CRISP) from Naja atra venom. Acta Crystallogr D Biol Crystallogr. 2004 Oct;60(Pt 10):1912-5. doi: 10.1107/S0907444904019766. Epub 2004 Sep 23.
Ref 116 Blocking effect and crystal structure of natrin toxin, a cysteine-rich secretory protein from Naja atra venom that targets the BKCa channel. Biochemistry. 2005 Aug 2;44(30):10145-52. doi: 10.1021/bi050614m.
Ref 117 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 118 A Scorpion Defensin BmKDfsin4 Inhibits Hepatitis B Virus Replication in Vitro. Toxins (Basel). 2016 Apr 27;8(5):124. doi: 10.3390/toxins8050124.
Ref 119 Extreme diversity of scorpion venom peptides and proteins revealed by transcriptomic analysis: implication for proteome evolution of scorpion venom arsenal. J Proteomics. 2012 Feb 16;75(5):1563-76. doi: 10.1016/j.jprot.2011.11.029. Epub 2011 Dec 7.
Ref 120 Characterization of a potassium channel toxin from the Caribbean Sea anemone Stichodactyla helianthus. Toxicon. 1995 May;33(5):603-13. doi: 10.1016/0041-0101(95)00013-c.
Ref 121 Chemical synthesis and characterization of ShK toxin: a potent potassium channel inhibitor from a sea anemone. Int J Pept Protein Res. 1995 Nov;46(5):354-8. doi: 10.1111/j.1399-3011.1995.tb01068.x.
Ref 122 Identification of three separate binding sites on SHK toxin, a potent inhibitor of voltage-dependent potassium channels in human T-lymphocytes and rat brain. Biochem Biophys Res Commun. 1996 Feb 27;219(3):696-701. doi: 10.1006/bbrc.1996.0297.
Ref 123 Targeting effector memory T cells with a selective peptide inhibitor of Kv1.3 channels for therapy of autoimmune diseases. Mol Pharmacol. 2005 Apr;67(4):1369-81. doi: 10.1124/mol.104.008193. Epub 2005 Jan 21.
Ref 124 Development of a sea anemone toxin as an immunomodulator for therapy of autoimmune diseases. Toxicon. 2012 Mar 15;59(4):529-46. doi: 10.1016/j.toxicon.2011.07.016. Epub 2011 Aug 12.
Ref 125 Sea Anemones: Quiet Achievers in the Field of Peptide Toxins. Toxins (Basel). 2018 Jan 8;10(1):36. doi: 10.3390/toxins10010036.
Ref 126 Solution structure of ShK toxin, a novel potassium channel inhibitor from a sea anemone. Nat Struct Biol. 1996 Apr;3(4):317-20. doi: 10.1038/nsb0496-317.
Ref 127 ShK-Dap22, a potent Kv1.3-specific immunosuppressive polypeptide. J Biol Chem. 1998 Dec 4;273(49):32697-707. doi: 10.1074/jbc.273.49.32697.
Ref 128 Role of disulfide bonds in the structure and potassium channel blocking activity of ShK toxin. Biochemistry. 1999 Nov 2;38(44):14549-58. doi: 10.1021/bi991282m.
Ref 129 Engineering a stable and selective peptide blocker of the Kv1.3 channel in T lymphocytes. Mol Pharmacol. 2009 Apr;75(4):762-73. doi: 10.1124/mol.108.052704. Epub 2009 Jan 2.
Ref 130 Native chemical ligation at Asx-Cys, Glx-Cys: chemical synthesis and high-resolution X-ray structure of ShK toxin by racemic protein crystallography. J Am Chem Soc. 2013 Aug 14;135(32):11911-9. doi: 10.1021/ja4046795. Epub 2013 Aug 6.
Ref 131 Pharmaceutical Optimization of Peptide Toxins for Ion Channel Targets: Potent, Selective, and Long-Lived Antagonists of Kv1.3. J Med Chem. 2015 Sep 10;58(17):6784-802. doi: 10.1021/acs.jmedchem.5b00495. Epub 2015 Aug 31.
Ref 132 Inversion of the Side-Chain Stereochemistry of Indvidual Thr or Ile Residues in a Protein Molecule: Impact on the Folding, Stability, and Structure of the ShK Toxin. Angew Chem Int Ed Engl. 2017 Mar 13;56(12):3324-3328. doi: 10.1002/anie.201612398. Epub 2017 Feb 14.
Ref 133 ImKTx88, a novel selective Kv1.3 channel blocker derived from the scorpion Isometrus maculates. Toxicon. 2011 Feb;57(2):348-55. doi: 10.1016/j.toxicon.2010.12.015. Epub 2010 Dec 29.
Ref 134 A four-disulphide-bridged toxin, with high affinity towards voltage-gated K+ channels, isolated from Heterometrus spinnifer (Scorpionidae) venom. Biochem J. 1997 Nov 15;328 ( Pt 1)(Pt 1):321-7. doi: 10.1042/bj3280321.
Ref 135 Free energy simulations of binding of HsTx1 toxin to Kv1 potassium channels: the basis of Kv1.3/Kv1.1 selectivity. J Phys Chem B. 2014 Jan 23;118(3):707-16. doi: 10.1021/jp410950h. Epub 2014 Jan 13.
Ref 136 A potent and Kv1.3-selective analogue of the scorpion toxin HsTX1 as a potential therapeutic for autoimmune diseases. Sci Rep. 2014 Mar 28;4:4509. doi: 10.1038/srep04509.
Ref 137 Prolonged immunomodulation in inflammatory arthritis using the selective Kv1.3 channel blocker HsTX1[R14A] and its PEGylated analog. Clin Immunol. 2017 Jul;180:45-57. doi: 10.1016/j.clim.2017.03.014. Epub 2017 Apr 4.
Ref 138 Structural and functional consequences of the presence of a fourth disulfide bridge in the scorpion short toxins: solution structure of the potassium channel inhibitor HsTX1. Protein Sci. 1999 Dec;8(12):2672-85. doi: 10.1110/ps.8.12.2672.
Ref 139 Evidence for domain-specific recognition of SK and Kv channels by MTX and HsTx1 scorpion toxins. J Biol Chem. 2004 Dec 31;279(53):55690-6. doi: 10.1074/jbc.M410055200. Epub 2004 Oct 21.
Ref 140 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 141 K+ channel types targeted by synthetic OSK1, a toxin from Orthochirus scrobiculosus scorpion venom. Biochem J. 2005 Jan 1;385(Pt 1):95-104. doi: 10.1042/BJ20041379.
Ref 142 Pharmacological profiling of Orthochirus scrobiculosus toxin 1 analogs with a trimmed N-terminal domain. Mol Pharmacol. 2006 Jan;69(1):354-62. doi: 10.1124/mol.105.017210. Epub 2005 Oct 18.
Ref 143 Three-dimensional structure of toxin OSK1 from Orthochirus scrobiculosus scorpion venom. Biochemistry. 1997 Feb 11;36(6):1223-32. doi: 10.1021/bi9614390.
Ref 144 Synthesis, characterization, and application of cy-dye- and alexa-dye-labeled hongotoxin(1) analogues. The first high affinity fluorescence probes for voltage-gated K+ channels. Bioconjug Chem. 2002 May-Jun;13(3):416-25. doi: 10.1021/bc015543s.
Ref 145 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 146 Isolation and characterization of Ts19 Fragment II, a new long-chain potassium channel toxin from Tityus serrulatus venom. Peptides. 2016 Jun;80:9-17. doi: 10.1016/j.peptides.2015.06.004. Epub 2015 Jun 25.
Ref 147 Tityus serrulatus venom peptidomics: assessing venom peptide diversity. Toxicon. 2008 Oct;52(5):611-8. doi: 10.1016/j.toxicon.2008.07.010. Epub 2008 Jul 31.
Ref 148 Influence of post-starvation extraction time and prey-specific diet in Tityus serrulatus scorpion venom composition and hyaluronidase activity. Toxicon. 2014 Nov;90:326-36. doi: 10.1016/j.toxicon.2014.08.064. Epub 2014 Sep 6.
Ref 149 Purification, characterization, and biosynthesis of margatoxin, a component of Centruroides margaritatus venom that selectively inhibits voltage-dependent potassium channels. J Biol Chem. 1993 Sep 5;268(25):18866-74.
Ref 150 Chemical synthesis and structure-function studies of margatoxin, a potent inhibitor of voltage-dependent potassium channel in human T lymphocytes. Biochem Biophys Res Commun. 1994 Jan 28;198(2):619-25. doi: 10.1006/bbrc.1994.1090.
Ref 151 Determination of the three-dimensional structure of margatoxin by 1H, 13C, 15N triple-resonance nuclear magnetic resonance spectroscopy. Biochemistry. 1994 Dec 20;33(50):15061-70. doi: 10.1021/bi00254a015.
Ref 152 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 153 Proteomic endorsed transcriptomic profiles of venom glands from Tityus obscurus and T. serrulatus scorpions. PLoS One. 2018 Mar 21;13(3):e0193739. doi: 10.1371/journal.pone.0193739. eCollection 2018.
Ref 154 TsTX-IV, a short chain four-disulfide-bridged neurotoxin from Tityus serrulatus venom which acts on Ca2+-activated K+ channels. Toxicon. 1999 Apr;37(4):651-60. doi: 10.1016/s0041-0101(98)00206-2.
Ref 155 NMR solution structure of butantoxin. Arch Biochem Biophys. 2000 Jul 1;379(1):18-27. doi: 10.1006/abbi.2000.1858.
Ref 156 Covalent structure and some pharmacological features of native and cleaved alpha-KTx12-1, a four disulfide-bridged toxin from Tityus serrulatus venom. J Pept Sci. 2003 Feb;9(2):132-40. doi: 10.1002/psc.440.
Ref 157 Electrophysiological characterization of Ts6 and Ts7, K? channel toxins isolated through an improved Tityus serrulatus venom purification procedure. Toxins (Basel). 2014 Feb 28;6(3):892-913. doi: 10.3390/toxins6030892.
Ref 158 Tityus serrulatus venom and toxins Ts1, Ts2 and Ts6 induce macrophage activation and production of immune mediators. Toxicon. 2011 Jun;57(7-8):1101-8. doi: 10.1016/j.toxicon.2011.04.017. Epub 2011 Apr 29.
Ref 159 Ts6 and Ts2 from Tityus serrulatus venom induce inflammation by mechanisms dependent on lipid mediators and cytokine production. Toxicon. 2013 Jan;61:1-10. doi: 10.1016/j.toxicon.2012.10.002. Epub 2012 Oct 22.
Ref 160 Probing the pH-dependent structural features of alpha-KTx12.1, a potassium channel blocker from the scorpion Tityus serrulatus. Protein Sci. 2005 Apr;14(4):1025-38. doi: 10.1110/ps.041131205.
Ref 161 Increasing the molecular contacts between maurotoxin and Kv1.2 channel augments ligand affinity. Proteins. 2005 Aug 15;60(3):401-11. doi: 10.1002/prot.20509.
Ref 162 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 163 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 164 Neuromuscular effects of some potassium channel blocking toxins from the venom of the scorpion Leiurus quinquestriatus hebreus. Toxicon. 1994 Nov;32(11):1433-43. doi: 10.1016/0041-0101(94)90415-4.
Ref 165 Screening and cDNA cloning of Kv1 potassium channel toxins in sea anemones. Mar Drugs. 2010 Dec 2;8(12):2893-905. doi: 10.3390/md8122893.
Ref 166 OdK2, a Kv1.3 channel-selective toxin from the venom of the Iranian scorpion Odonthobuthus doriae. Toxicon. 2008 Jun 15;51(8):1424-30. doi: 10.1016/j.toxicon.2008.03.027. Epub 2008 Mar 29.
Ref 167 Variability of Potassium Channel Blockers in Mesobuthus eupeus Scorpion Venom with Focus on Kv1.1: AN INTEGRATED TRANSCRIPTOMIC AND PROTEOMIC STUDY. J Biol Chem. 2015 May 8;290(19):12195-209. doi: 10.1074/jbc.M115.637611. Epub 2015 Mar 19.
Ref 168 Tuning Scorpion Toxin Selectivity: Switching From K(V)1.1 to K(V)1.3. Front Pharmacol. 2020 Jul 7;11:1010. doi: 10.3389/fphar.2020.01010. eCollection 2020.
Ref 169 The precursors of the bee venom constituents apamin and MCD peptide are encoded by two genes in tandem which share the same 3'-exon. J Biol Chem. 1995 May 26;270(21):12704-8. doi: 10.1074/jbc.270.21.12704.
Ref 170 [Sequence analysis of bee venom neurotoxin (apamine) from its tryptic and chymotryptic cleavage products]. Hoppe Seylers Z Physiol Chem. 1967 Jun;348(6):737-8.
Ref 171 The peptide components of bee venom. Eur J Biochem. 1976 Jan 15;61(2):369-76. doi: 10.1111/j.1432-1033.1976.tb10030.x.
Ref 172 Apamin as a selective blocker of the calcium-dependent potassium channel in neuroblastoma cells: voltage-clamp and biochemical characterization of the toxin receptor. Proc Natl Acad Sci U S A. 1982 Feb;79(4):1308-12. doi: 10.1073/pnas.79.4.1308.
Ref 173 Apamin, a blocker of the calcium-activated potassium channel, induces neurodegeneration of Purkinje cells exclusively. Brain Res. 1997 Dec 19;778(2):405-8. doi: 10.1016/s0006-8993(97)01165-7.
Ref 174 Determinants of apamin and d-tubocurarine block in SK potassium channels. J Biol Chem. 1997 Sep 12;272(37):23195-200. doi: 10.1074/jbc.272.37.23195.
Ref 175 Pharmacological characterization of small-conductance Ca(2+)-activated K(+) channels stably expressed in HEK 293 cells. Br J Pharmacol. 2000 Mar;129(5):991-9. doi: 10.1038/sj.bjp.0703120.
Ref 176 SK3 is an important component of K(+) channels mediating the afterhyperpolarization in cultured rat SCG neurones. J Physiol. 2001 Sep 1;535(Pt 2):323-34. doi: 10.1111/j.1469-7793.2001.00323.x.
Ref 177 Apamin interacts with all subtypes of cloned small-conductance Ca2+-activated K+ channels. Pflugers Arch. 2001 Jan;441(4):544-50. doi: 10.1007/s004240000447.
Ref 178 An amino acid outside the pore region influences apamin sensitivity in small conductance Ca2+-activated K+ channels. J Biol Chem. 2007 Feb 9;282(6):3478-86. doi: 10.1074/jbc.M607213200. Epub 2006 Dec 1.
Ref 179 Apamin reduces neuromuscular transmission by activating inhibitory muscarinic M(2) receptors on motor nerve terminals. Eur J Pharmacol. 2010 Jan 25;626(2-3):239-43. doi: 10.1016/j.ejphar.2009.09.064. Epub 2009 Oct 8.
Ref 180 Allosteric block of KCa2 channels by apamin. J Biol Chem. 2010 Aug 27;285(35):27067-27077. doi: 10.1074/jbc.M110.110072. Epub 2010 Jun 18.
Ref 181 The small neurotoxin apamin blocks not only small conductance Ca(2+) activated K(+) channels (SK type) but also the voltage dependent Kv1.3 channel. Eur Biophys J. 2017 Sep;46(6):517-523. doi: 10.1007/s00249-016-1196-0. Epub 2017 Jan 20.
Ref 182 Apamin inhibits TNF-- and IFN--induced inflammatory cytokines and chemokines via suppressions of NF-B signaling pathway and STAT in human keratinocytes. Pharmacol Rep. 2017 Oct;69(5):1030-1035. doi: 10.1016/j.pharep.2017.04.006. Epub 2017 Apr 18.
Ref 183 Apamin Suppresses LPS-Induced Neuroinflammatory Responses by Regulating SK Channels and TLR4-Mediated Signaling Pathways. Int J Mol Sci. 2020 Jun 17;21(12):4319. doi: 10.3390/ijms21124319.
Ref 184 Apamin from bee venom suppresses inflammation in a murine model of gouty arthritis. J Ethnopharmacol. 2020 Jul 15;257:112860. doi: 10.1016/j.jep.2020.112860. Epub 2020 Apr 11.
Ref 185 Antioxidative, Antiapoptotic, and Anti-Inflammatory Effects of Apamin in a Murine Model of Lipopolysaccharide-Induced Acute Kidney Injury. Molecules. 2020 Dec 3;25(23):5717. doi: 10.3390/molecules25235717.
Ref 186 Solution structure of apamin determined by nuclear magnetic resonance and distance geometry. Biochemistry. 1988 Nov 1;27(22):8491-8. doi: 10.1021/bi00422a029.
Ref 187 [Spatial structure of apamin in solution]. Mol Biol (Mosk). 1991 Jul-Aug;25(4):937-45.
Ref 188 Binding and toxicity of apamin. Characterization of the active site. Eur J Biochem. 1991 Mar 28;196(3):639-45. doi: 10.1111/j.1432-1033.1991.tb15860.x.
Ref 189 Kbot1, a three disulfide bridges toxin from Buthus occitanus tunetanus venom highly active on both SK and Kv channels. Peptides. 2004 Apr;25(4):637-45. doi: 10.1016/j.peptides.2004.02.017.
Ref 190 Molecular cloning and functional identification of a new K(+) channel blocker, LmKTx10, from the scorpion Lychas mucronatus. Peptides. 2009 Apr;30(4):675-80. doi: 10.1016/j.peptides.2008.11.015. Epub 2008 Dec 3.
Ref 191 Novel potassium channel blocker venom peptides from Mesobuthus gibbosus (Scorpiones: Buthidae). Toxicon. 2013 Jan;61:72-82. doi: 10.1016/j.toxicon.2012.10.010. Epub 2012 Nov 7.
Ref 192 Complete amino acid sequences of two protease inhibitors in the venom of Bungarus fasciatus. Int J Pept Protein Res. 1983 Feb;21(2):209-15. doi: 10.1111/j.1399-3011.1983.tb03095.x.
Ref 193 BF9, the first functionally characterized snake toxin peptide with Kunitz-type protease and potassium channel inhibiting properties. J Biochem Mol Toxicol. 2014 Feb;28(2):76-83. doi: 10.1002/jbt.21538. Epub 2013 Nov 14.
Ref 194 Solution structure of a Kunitz-type chymotrypsin inhibitor isolated from the elapid snake Bungarus fasciatus. J Biol Chem. 2001 Nov 30;276(48):45079-87. doi: 10.1074/jbc.M106182200. Epub 2001 Sep 18.
Ref 195 Chemical synthesis and characterization of maurotoxin, a short scorpion toxin with four disulfide bridges that acts on K+ channels. Eur J Biochem. 1996 Dec 15;242(3):491-8. doi: 10.1111/j.1432-1033.1996.0491r.x.
Ref 196 Maurotoxin, a four disulfide bridge toxin from Scorpio maurus venom: purification, structure and action on potassium channels. FEBS Lett. 1997 Apr 14;406(3):284-90. doi: 10.1016/s0014-5793(97)00285-8.
Ref 197 Maurotoxin, a four disulfide bridges scorpion toxin acting on K+ channels. Toxicon. 1998 Nov;36(11):1609-11. doi: 10.1016/s0041-0101(98)00153-6.
Ref 198 Mechanisms of maurotoxin action on Shaker potassium channels. Biophys J. 2000 Aug;79(2):776-87. doi: 10.1016/S0006-3495(00)76335-1.
Ref 199 Maurotoxin versus Pi1/HsTx1 scorpion toxins. Toward new insights in the understanding of their distinct disulfide bridge patterns. J Biol Chem. 2000 Dec 15;275(50):39394-402. doi: 10.1074/jbc.M006810200.
Ref 200 Effect of maurotoxin, a four disulfide-bridged toxin from the chactoid scorpion Scorpio maurus, on Shaker K+ channels. J Pept Res. 2000 Jun;55(6):419-27. doi: 10.1034/j.1399-3011.2000.00715.x.
Ref 201 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 202 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 203 Chemical synthesis and 1H-NMR 3D structure determination of AgTx2-MTX chimera, a new potential blocker for Kv1.2 channel, derived from MTX and AgTx2 scorpion toxins. Protein Sci. 2008 Jan;17(1):107-18. doi: 10.1110/ps.073122908. Epub 2007 Nov 27.
Ref 204 Solution structure of maurotoxin, a scorpion toxin from Scorpio maurus, with high affinity for voltage-gated potassium channels. Proteins. 1997 Nov;29(3):321-33.
Ref 205 Nucleotide sequence of crotamine isoform precursors from a single South American rattlesnake (Crotalus durissus terrificus). Toxicon. 1999 Jul;37(7):973-84. doi: 10.1016/s0041-0101(98)00226-8.
Ref 206 Structure and chromosomal localization of the gene for crotamine, a toxin from the South American rattlesnake, Crotalus durissus terrificus. Toxicon. 2003 Dec;42(7):747-52. doi: 10.1016/j.toxicon.2003.10.019.
Ref 207 [The primary structure of crotamine (author's transl)]. Hoppe Seylers Z Physiol Chem. 1975 Feb;356(2):213-5.
Ref 208 Crotamine pharmacology revisited: novel insights based on the inhibition of KV channels. Mol Pharmacol. 2012 Jul;82(1):90-6. doi: 10.1124/mol.112.078188. Epub 2012 Apr 12.
Ref 209 Effect of crotamine, a toxin of South American rattlesnake venom, on the sodium channel of murine skeletal muscle. Br J Pharmacol. 1978 Jul;63(3):551-9. doi: 10.1111/j.1476-5381.1978.tb07811.x.
Ref 210 The analgesic activity of crotamine, a neurotoxin from Crotalus durissus terrificus (South American rattlesnake) venom: a biochemical and pharmacological study. Toxicon. 1998 Dec;36(12):1927-37. doi: 10.1016/s0041-0101(98)00117-2.
Ref 211 Crotamine is a novel cell-penetrating protein from the venom of rattlesnake Crotalus durissus terrificus. FASEB J. 2004 Sep;18(12):1407-9. doi: 10.1096/fj.03-1459fje. Epub 2004 Jul 1.
Ref 212 Crotamine mediates gene delivery into cells through the binding to heparan sulfate proteoglycans. J Biol Chem. 2007 Jul 20;282(29):21349-60. doi: 10.1074/jbc.M604876200. Epub 2007 May 9.
Ref 213 Crotamine inhibits preferentially fast-twitching muscles but is inactive on sodium channels. Toxicon. 2007 Sep 15;50(4):553-62. doi: 10.1016/j.toxicon.2007.04.026. Epub 2007 May 18.
Ref 214 Cytotoxic effects of crotamine are mediated through lysosomal membrane permeabilization. Toxicon. 2008 Sep 1;52(3):508-17. doi: 10.1016/j.toxicon.2008.06.029. Epub 2008 Jul 10.
Ref 215 Selective reciprocity in antimicrobial activity versus cytotoxicity of hBD-2 and crotamine. Proc Natl Acad Sci U S A. 2009 Sep 1;106(35):14972-7. doi: 10.1073/pnas.0904465106. Epub 2009 Aug 13.
Ref 216 Crotamine toxicity and efficacy in mouse models of melanoma. Expert Opin Investig Drugs. 2011 Sep;20(9):1189-200. doi: 10.1517/13543784.2011.602064.
Ref 217 In vitro antibacterial and hemolytic activities of crotamine, a small basic myotoxin from rattlesnake Crotalus durissus. J Antibiot (Tokyo). 2011 Apr;64(4):327-31. doi: 10.1038/ja.2011.10. Epub 2011 Mar 9.
Ref 218 The natural cell-penetrating peptide crotamine targets tumor tissue in vivo and triggers a lethal calcium-dependent pathway in cultured cells. Mol Pharm. 2012 Feb 6;9(2):211-21. doi: 10.1021/mp2000605. Epub 2011 Dec 23.
Ref 219 Unraveling the antifungal activity of a South American rattlesnake toxin crotamine. Biochimie. 2013 Feb;95(2):231-40. doi: 10.1016/j.biochi.2012.09.019. Epub 2012 Sep 26.
Ref 220 Biological versatility of crotamine--a cationic peptide from the venom of a South American rattlesnake. Expert Opin Investig Drugs. 2010 Dec;19(12):1515-25. doi: 10.1517/13543784.2010.534457. Epub 2010 Nov 10.
Ref 221 Solution structure of crotamine, a Na+ channel affecting toxin from Crotalus durissus terrificus venom. Eur J Biochem. 2003 May;270(9):1969-79. doi: 10.1046/j.1432-1033.2003.03563.x.
Ref 222 Automated NMR structure determination and disulfide bond identification of the myotoxin crotamine from Crotalus durissus terrificus. Toxicon. 2005 Dec 1;46(7):759-67. doi: 10.1016/j.toxicon.2005.07.018. Epub 2005 Sep 26.
Ref 223 Vietnamese Heterometrus laoticus scorpion venom: evidence for analgesic and anti-inflammatory activity and isolation of new polypeptide toxin acting on Kv1.3 potassium channel. Toxicon. 2014 Jan;77:40-8. doi: 10.1016/j.toxicon.2013.10.027. Epub 2013 Nov 1.
Ref 224 Hetlaxin, a new toxin from the Heterometrus laoticus scorpion venom, interacts with voltage-gated potassium channel Kv1.3. Dokl Biochem Biophys. 2013 Mar-Apr;449:109-11. doi: 10.1134/S1607672913020142. Epub 2013 May 9.
Ref 225 Expression and characterization of a novel scorpine-like peptide Ev37, from the scorpion Euscorpiops validus. Protein Expr Purif. 2013 Mar;88(1):127-33. doi: 10.1016/j.pep.2012.12.004. Epub 2012 Dec 20.
Ref 226 PHAB toxins: a unique family of predatory sea anemone toxins evolving via intra-gene concerted evolution defines a new peptide fold. Cell Mol Life Sci. 2018 Dec;75(24):4511-4524. doi: 10.1007/s00018-018-2897-6. Epub 2018 Aug 14.
Ref 227 Inhibition of Kv2.1 Potassium Channels by MiDCA1, A Pre-Synaptically Active PLA(2)-Type Toxin from Micrurus dumerilii carinicauda Coral Snake Venom. Toxins (Basel). 2019 Jun 12;11(6):335. doi: 10.3390/toxins11060335.
Ref 228 Engineered specific and high-affinity inhibitor for a subtype of inward-rectifier K+ channels. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10774-8. doi: 10.1073/pnas.0802850105. Epub 2008 Jul 31.
Ref 229 Venom-derived peptides inhibiting Kir channels: Past, present, and future. Neuropharmacology. 2017 Dec;127:161-172. doi: 10.1016/j.neuropharm.2017.07.011. Epub 2017 Jul 14.
Ref 230 Anti-inflammatory effects of FS48, the first potassium channel inhibitor from the salivary glands of the flea Xenopsylla cheopis. J Biol Chem. 2021 Jan-Jun;296:100670. doi: 10.1016/j.jbc.2021.100670. Epub 2021 Apr 15.
Data Quality & Feedback

Help us maintain data quality by reporting any errors or inaccuracies you may find.

samedaypayday.com visits since 2024

If you find any error in data or bug in web service, please kindly report it to biodb_contact@163.com et al.