General Information of This Target
Target ID
BTDT00061
Target Name
Potassium voltage-gated channel subfamily A member 6 (Kcna6)
Target Bioclass
Transporter and channel
Uniprot ID
P17659
3D Structure
Download
2D Sequence
3D Structure
Source
Predict by Alphafold2
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Alphafold Parameters: msa_mode: mmseqs2_uniref_env model_type: auto num_recycles: auto
Gene Name
Kcna6
Synonym
RCK2; Voltage-gated potassium channel subunit Kv1.6; Voltage-gated potassium channel subunit Kv2
Sequence
MRSEKSLTLAAPGEVRGPEGEQQDAGEFQEAEGGGGCCSSERLVINISGLRYETQLRTLS
LFPDTLLGDPGRRVRFFDPLRNEYFFDRNRPSFDAILYYYQSGGRLRRPVNVPLDIFMEE
IRFYQLGDEALAAFREDEGCLPEGGEDEKPLPSQPFQRQVWLLFEYPESSGPARGIAIVS
VLVILISIVIFCLETLPQFRADGRGGSNEGSGTRMSPASRGSHEEEDEDEDSYAFPGSIP
SGGLGTGGTSSFSTLGGSFFTDPFFLVETLCIVWFTFELLVRFSACPSKAAFFRNIMNII
DLVAIFPYFITLGTELVQRHEQQPVSGGSGQNRQQAMSLAILRVIRLVRVFRIFKLSRHS
KGLQILGKTLQASMRELGLLIFFLFIGVILFSSAVYFAEADDVDSLFPSIPDAFWWAVVT
MTTVGYGDMYPMTVGGKIVGSLCAIAGVLTIALPVPVIVSNFNYFYHRETEQEEQGQYTH
VTCGQPTPDLKATDNGLGKPDFAEASRERRSSYLPTPHRAYAEKRMLTEV

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Family
the potassium channel family
Function
Voltage-gated potassium channel that mediates transmembrane potassium transport in excitable membranes. Forms tetrameric potassium- selective channels through which potassium ions pass in accordance with their electrochemical gradient. The channel alternates between opened and closed conformations in response to the voltage difference across the membrane. Can form functional homotetrameric channels and heterotetrameric channels that contain variable proportions of KCNA1, KCNA2, KCNA4, KNCA5, KCNA6, and possibly other family members as well; channel properties depend on the type of alpha subunits that are part of the channel. Channel properties are modulated by cytoplasmic beta subunits that regulate the subcellular location of the alpha subunits and promote rapid inactivation (Probable). Homotetrameric channels display rapid activation and slow inactivation.

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Taxonomy ID
10116
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Kingdom: Metazoa
Phylum: Chordata
Class: Mammalia
Order: Rodentia
Family: Muridae
Genus: Rattus
Species: Rattus norvegicus
Toxin Information Related to This Target
                           Toxin Name Activity Data Type Activity Data Reference
 Toxin Info    Kunitz-type serine protease inhibitor homolog delta-dendrotoxin Dissociation constant
23 nM
[1], [2]
 Toxin Info    Potassium channel toxin alpha-KTx 3.2 Inhibition constant
0.037 nM
[3- 7]
 Toxin Info    Potassium channel toxin alpha-KTx 1.1 Inhibition constant
22 nM
[3- 23]
 Toxin Info    Potassium channel toxin alpha-KTx 3.4 Inhibition constant
149 nM
[3- 24]
 Toxin Info    N.vectensis toxin 4 Effect . [25]
 Toxin Info    N.vectensis toxin 5 Effect . [25]
 Toxin Info    Mu-conotoxin CnIIIC Inhibition rate . [26], [27], [28]
 Toxin Info    Crotamine Inhibition rate . [29]
 Toxin Info    Toxin PhcrTx2 Inhibition rate . [30]
 Toxin Info    Kunitz-type serine protease inhibitor homolog dendrotoxin K Inhibition rate . [31]
 Toxin Info    Potassium channel toxin alpha-KTx 8.2 Inhibition rate . [32]
 Toxin Info    Potassium channel toxin alpha-KTx 8.6 Inhibition rate . [32], [33]
 Toxin Info    Potassium channel toxin alpha-KTx 8.6 Inhibition rate . [32]
 Toxin Info    Potassium channel toxin epsilon-KTx 1.1 Inhibition rate . [34]
 Toxin Info    Potassium channel toxin epsilon-KTx 1.2 Inhibition rate . [34]
 Toxin Info    Apamin Inhibition rate . [35- 52]
 Toxin Info    Potassium channel toxin alpha-KTx 3.11 Inhibition rate . [53]
 Toxin Info    Mu-theraphotoxin-Pspp1 Inhibition rate . [54]
 Toxin Info    Potassium channel toxin kappa-KTx 2.5 Inhibition rate . [55]
 Toxin Info    Potassium channel toxin TsTXK-beta Inhibition rate . [56]
 Toxin Info    Potassium channel toxin alpha-KTx 16.4 Inhibition rate . [57]
 Toxin Info    KappaPI-actitoxin-Ael3a Inhibition rate . [58], [59]
 Toxin Info    Kappa-hefutoxin 2 (C1A,Y2C,R3Y,N4R,C5N,W6C,R7W,E8R,G9E,N10G,D11N,E12D,T14E,C15T,K16C,E17K,R18E,C19R) Inhibition rate
8.8 %
[60]
 Toxin Info    Kappa-hefutoxin 2 (C1H,Y2A,R3C,N4Y,C5R,W6N,R7C,E8W,G9R,N10E,D11G,E12N,E13D,T14E,C15E,K16T,E17C,R18K,C19E) Inhibition rate
13.6 %
[60]
 Toxin Info    U-actitoxin-Avd3n Inhibition rate
14 %
[61]
 Toxin Info    Kunitz-type proteinase inhibitor AEPI-I Inhibition rate
18.7 %
[60]
 Toxin Info    Potassium channel toxin alpha-KTx 12.2 Inhibition rate
20 %
[62]
 Toxin Info    Potassium channel toxin alpha-KTx 12.1 Inhibition rate
20 %
[62]
 Toxin Info    Potassium channel toxin alpha-KTx 21.1 Inhibition rate
20 %
[63]
 Toxin Info    Potassium channel toxin alpha-KTx 31.1 Inhibition rate
21 %
[64]
 Toxin Info    Potassium channel toxin alpha-KTx 31.1 Inhibition rate
21 %
[64]
 Toxin Info    Potassium channel toxin alpha-KTx 21.1 Inhibition rate
22 %
[63- 68]
 Toxin Info    Kunitz-type serine protease inhibitor homolog dendrotoxin I Inhibition rate
26 %
[31]
 Toxin Info    Pi-stichotoxin-Hcr5b Inhibition rate
32 %
[69]
 Toxin Info    Potassium channel toxin kappa-KTx 5.1 Inhibition rate
59.8 %
[70]
 Toxin Info    Potassium channel toxin alpha-KTx 3.6 Inhibition rate
91 %
[71]
 Toxin Info    Potassium channel toxin alpha-KTx 3.13 Inhibition rate
93 %
[71]
 Toxin Info    Potassium channel toxin alpha-KTx 4.1 Inhibition rate
94 %
[62]
 Toxin Info    AgTx2 (K27M) IC50
1.3 nM
[72]
 Toxin Info    Kappa-actitoxin-Bcs3a IC50
1.31 nM
[73]
 Toxin Info    Kappa-actitoxin-Bcs3a IC50
1.31 nM
[73]
 Toxin Info    Kappa-actitoxin-Bcs3b IC50
7.76 nM
[73]
 Toxin Info    Kappa-actitoxin-Bcs3b IC50
7.76 nM
[73]
 Toxin Info    Kunitz-type serine protease inhibitor homolog alpha-dendrotoxin IC50
9 nM
[1- 76]
 Toxin Info    MeuKTx (G11R,G30R,D33H) IC50
16.3 nM
[77- 96]
 Toxin Info    PI-stichotoxin-Hcr2g IC50
43.9 nM
[97]
 Toxin Info    PI-stichotoxin-Hcr2g IC50
43.9 nM
[98], [97], [99]
 Toxin Info    Potassium channel toxin alpha-KTx 3.19 IC50
63.4 nM
[100]
 Toxin Info    Potassium channel toxin alpha-KTx 3.7 IC50
71 nM
[6- 103]
 Toxin Info    Potassium channel toxin alpha-KTx 19.2 IC50
75.9 nM
[104]
 Toxin Info    Potassium channel toxin alpha-KTx 19.2 IC50
75.9 nM
[104]
 Toxin Info    Potassium channel toxin alpha-KTx 3.2 IC50
92 nM
[3- 7]
 Toxin Info    Potassium channel toxin AbeTx1 IC50
116 nM
[105]
 Toxin Info    Plant defensin 2.3 (G36N) IC50
138 nM
[106]
 Toxin Info    PI-stichotoxin-Hcr2f IC50
154.9 nM
[97]
 Toxin Info    PI-stichotoxin-Hcr2f IC50
154.9 nM
[98], [97], [99]
 Toxin Info    Kappa-actitoxin-Ate1a IC50
191 nM
[107]
 Toxin Info    Potassium channel toxin alpha-KTx 3.18 IC50
266.3 nM
[77- 96]
 Toxin Info    Plant defensin 2.3 (K33A,G36N) IC50
366 nM
[106]
 Toxin Info    Potassium channel toxin AbeTx1 (R,R10A) IC50
811 nM
[105]
 Toxin Info    Potassium channel toxin AbeTx1 (R,K6A) IC50
852 nM
[105]
 Toxin Info    Potassium channel toxin alpha-KTx 1.17 IC50
910 nM
[108]
 Toxin Info    Potassium channel toxin alpha-KTx 1.17 IC50
910 nM
[33- 108]
 Toxin Info    Defensin-like protein 1 IC50
978 nM
[106]
 Toxin Info    Potassium channel toxin AbeTx1 (R,K12A) IC50
1.077 μM
[105]
 Toxin Info    Toxin MeKTx13-3 (Q12A,K15A,K18A,D33R) IC50
1.522 μM
[100]
 Toxin Info    Kappa-actitoxin-Bcs4a IC50
2.24593 μM
[109]
 Toxin Info    Kappa-actitoxin-Bcs4a IC50
2.24593 μM
[109]
 Toxin Info    Potassium channel toxin AbeTx1 (R,R8A) IC50
2.442 μM
[105]
 Toxin Info    Plant defensin 2.3 (K33A) IC50
3.5 μM
[106]
 Toxin Info    Potassium channel toxin AbeTx1 (A) IC50
3.531 μM
[105]
 Toxin Info    Toxin MeKTx11-3 (V9G) IC50
6 μM
[108]
 Toxin Info    U-actitoxin-Oulsp1 IC50
6.542 μM
[110]
 Toxin Info    Toxin MeKTx11-3 (S37P) IC50
6.9 μM
[108]
 Toxin Info    Potassium channel toxin alpha-KTx 1.16 IC50
8.9 μM
[33- 108]
 Toxin Info    Potassium channel toxin alpha-KTx 1.16 IC50
8.9 μM
[108]
 Toxin Info    Potassium channel toxin alpha-KTx 8.8 IC50
9.983 μM
[111]
 Toxin Info    Potassium channel toxin alpha-KTx 8.8 IC50
9.983 μM
[111]
 Toxin Info    Potassium channel toxin AbeTx1 (R,K2A) IC50
18.857 μM
[105]
References
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Ref 2 Energetic and structural interactions between delta-dendrotoxin and a voltage-gated potassium channel. J Mol Biol. 2000 Mar 10;296(5):1283-94. doi: 10.1006/jmbi.2000.3522.
Ref 3 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 4 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 5 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 6 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 7 Solution structure of the potassium channel inhibitor agitoxin 2: caliper for probing channel geometry. Protein Sci. 1995 Aug;4(8):1478-89. doi: 10.1002/pro.5560040805.
Ref 8 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 9 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 10 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 11 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 12 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 13 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 14 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 15 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 16 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 17 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 18 Molecular structure of charybdotoxin: retraction. Science. 1991 May 3;252(5006):631. doi: 10.1126/science.252.5006.631.b.
Ref 19 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 20 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 21 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 22 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 23 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 24 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 25 The Birth and Death of Toxins with Distinct Functions: A Case Study in the Sea Anemone Nematostella. Mol Biol Evol. 2019 Sep 1;36(9):2001-2012. doi: 10.1093/molbev/msz132.
Ref 26 A novel -conopeptide, CnIIIC, exerts potent and preferential inhibition of NaV1.2/1.4 channels and blocks neuronal nicotinic acetylcholine receptors. Br J Pharmacol. 2012 Jul;166(5):1654-68. doi: 10.1111/j.1476-5381.2012.01837.x.
Ref 27 Large-scale discovery of conopeptides and conoproteins in the injectable venom of a fish-hunting cone snail using a combined proteomic and transcriptomic approach. J Proteomics. 2012 Sep 18;75(17):5215-25. doi: 10.1016/j.jprot.2012.06.001. Epub 2012 Jun 13.
Ref 28 Peptide therapeutics from venom: Current status and potential. Bioorg Med Chem. 2018 Jun 1;26(10):2738-2758. doi: 10.1016/j.bmc.2017.09.029. Epub 2017 Sep 23.
Ref 29 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 30 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 31 Novel effects of dendrotoxin homologues on subtypes of mammalian Kv1 potassium channels expressed in Xenopus oocytes. FEBS Lett. 1996 Mar 25;383(1-2):26-30. doi: 10.1016/0014-5793(96)00211-6.
Ref 32 Molecular diversity and functional evolution of scorpion potassium channel toxins. Mol Cell Proteomics. 2011 Feb;10(2):M110.002832. doi: 10.1074/mcp.M110.002832. Epub 2010 Sep 30.
Ref 33 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 34 Structural and Functional Elucidation of Peptide Ts11 Shows Evidence of a Novel Subfamily of Scorpion Venom Toxins. Toxins (Basel). 2016 Sep 30;8(10):288. doi: 10.3390/toxins8100288.
Ref 35 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 36 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 37 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 38 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 39 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 40 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 41 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 42 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 43 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 44 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 45 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 46 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 47 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 48 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 49 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 50 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 51 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 52 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 53 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 54 Chemical Synthesis, Proper Folding, Na(v) Channel Selectivity Profile and Analgesic Properties of the Spider Peptide Phlotoxin 1. Toxins (Basel). 2019 Jun 21;11(6):367. doi: 10.3390/toxins11060367.
Ref 55 The new kappa-KTx 2.5 from the scorpion Opisthacanthus cayaporum. Peptides. 2011 Jul;32(7):1509-17. doi: 10.1016/j.peptides.2011.05.017. Epub 2011 May 23.
Ref 56 Ts8 scorpion toxin inhibits the Kv4.2 channel and produces nociception in?vivo. Toxicon. 2016 Sep 1;119:244-52. doi: 10.1016/j.toxicon.2016.06.014. Epub 2016 Jun 23.
Ref 57 Molecular divergence of two orthologous scorpion toxins affecting potassium channels. Comp Biochem Physiol A Mol Integr Physiol. 2011 Jul;159(3):313-21. doi: 10.1016/j.cbpa.2011.03.027. Epub 2011 Apr 3.
Ref 58 A bifunctional sea anemone peptide with Kunitz type protease and potassium channel inhibiting properties. Biochem Pharmacol. 2011 Jul 1;82(1):81-90. doi: 10.1016/j.bcp.2011.03.023. Epub 2011 Apr 6.
Ref 59 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 60 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 61 AsKC11, a Kunitz Peptide from Anemonia sulcata, Is a Novel Activator of G Protein-Coupled Inward-Rectifier Potassium Channels. Mar Drugs. 2022 Feb 15;20(2):140. doi: 10.3390/md20020140.
Ref 62 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 63 Purification and characterization of Ts15, the first member of a new -KTX subfamily from the venom of the Brazilian scorpion Tityus serrulatus. Toxicon. 2011 Jul;58(1):54-61. doi: 10.1016/j.toxicon.2011.05.001. Epub 2011 May 13.
Ref 64 Kbot55, purified from Buthus occitanus tunetanus venom, represents the first member of a novel -KTx subfamily. Peptides. 2016 Jun;80:4-8. doi: 10.1016/j.peptides.2015.05.015. Epub 2015 Jun 14.
Ref 65 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 66 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 67 Moving pieces in a venomic puzzle: unveiling post-translationally modified toxins from Tityus serrulatus. J Proteome Res. 2013 Jul 5;12(7):3460-70. doi: 10.1021/pr4003068. Epub 2013 Jun 13.
Ref 68 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 69 A Tale of Toxin Promiscuity: The Versatile Pharmacological Effects of Hcr 1b-2 Sea Anemone Peptide on Voltage-Gated Ion Channels. Mar Drugs. 2022 Feb 17;20(2):147. doi: 10.3390/md20020147.
Ref 70 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 71 A potent potassium channel blocker from Mesobuthus eupeus scorpion venom. Biochimie. 2010 Dec;92(12):1847-53. doi: 10.1016/j.biochi.2010.08.003. Epub 2010 Aug 14.
Ref 72 AgTx2-GFP, Fluorescent Blocker Targeting Pharmacologically Important K(v)1.x (x = 1, 3, 6) Channels. Toxins (Basel). 2023 Mar 18;15(3):229. doi: 10.3390/toxins15030229.
Ref 73 Biochemical and electrophysiological characterization of two sea anemone type 1 potassium toxins from a geographically distant population of Bunodosoma caissarum. Mar Drugs. 2013 Mar 6;11(3):655-79. doi: 10.3390/md11030655.
Ref 74 Twenty years of dendrotoxins. Toxicon. 2001 Jan;39(1):15-26. doi: 10.1016/s0041-0101(00)00162-8.
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