General Information of This Target
Target ID
BTDT10180
Target Name
Potassium voltage-gated channel subfamily A member 1
Target Bioclass
Transporter and channel
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N.A.
Toxin Information Related to This Target
                           Toxin Name Activity Data Type Activity Data Reference
 Toxin Info    HgTX1 (A19Y,Y37F) Dissociation constant
0.12 pM
[1]
 Toxin Info    Kunitz-type serine protease inhibitor homolog dendrotoxin K Dissociation constant
0.24 nM
[2- 8]
 Toxin Info    Kunitz-type serine protease inhibitor homolog alpha-dendrotoxin Dissociation constant
2.8 nM
[9], [10], [11], [12]
 Toxin Info    Kappa-actitoxin-Bgr1a Dissociation constant
6 nM
[13- 20]
 Toxin Info    Potassium channel toxin alpha-KTx 3.1 Dissociation constant
41 nM
[21- 28]
 Toxin Info    PBTx3 Dissociation constant
771 nM
[29]
 Toxin Info    Potassium channel toxin kappa-KTx 1.2 Dissociation constant
>150 μM
[30- 34]
 Toxin Info    Potassium channel toxin alpha-KTx 1.10 Dissociation constant
79 μM
[29- 36]
 Toxin Info    Venom peptide Sh41 Effect . [37]
 Toxin Info    Venom peptide Sh42 Effect . [37]
 Toxin Info    U-scoloptoxin(15)-Sm2a Effect . [38], [39]
 Toxin Info    Upsilon-Da2a Inhibition rate . [40]
 Toxin Info    MTX (C31[Abu],[Abu]) Inhibition rate . [41]
 Toxin Info    Mu-thomitoxin-Hme1c Inhibition rate . [42], [43]
 Toxin Info    Neurotoxic enhancer CSTX-13 Inhibition rate . [44], [45], [46], [47]
 Toxin Info    Conotoxin flf14a Inhibition rate . [48]
 Toxin Info    Delta/kappa-actitoxin-Avd4a Inhibition rate . [19- 53]
 Toxin Info    Kappa-theraphotoxin-Ps1a Inhibition rate . [54], [55], [56]
 Toxin Info    Kappa-theraphotoxin-Ps1b Inhibition rate . [54]
 Toxin Info    Potassium channel toxin alpha-KTx 1.11 Inhibition rate . [57]
 Toxin Info    Delta-theraphotoxin-Cg1a 1 Inhibition rate . [58- 64]
 Toxin Info    Kappa-theraphotoxin-Cg2a Inhibition rate . [59- 66]
 Toxin Info    Toxin PhcrTx2 Inhibition rate . [67]
 Toxin Info    U18-theraphotoxin-Cg1a Inhibition rate . [59- 68]
 Toxin Info    U21-theraphotoxin-Cg1b Inhibition rate . [59- 65]
 Toxin Info    Kappa-theraphotoxin-Cg1a 1 Inhibition rate . [59- 70]
 Toxin Info    Kappa-theraphotoxin-Gr1a Inhibition rate . [71- 77]
 Toxin Info    Kappa-actitoxin-Ael2a Inhibition rate . [19- 83]
 Toxin Info    Beta/kappa-theraphotoxin-Cg1a Inhibition rate . [59- 85]
 Toxin Info    Potassium channel toxin alpha-KTx 21.1 Inhibition rate . [86- 90]
 Toxin Info    Potassium channel toxin alpha-KTx 6.1 Inhibition rate . [91- 99]
 Toxin Info    Alpha/kappa-conotoxin pl14a Inhibition rate
5 %
[100]
 Toxin Info    Potassium channel toxin alpha-KTx Ctri9577 Inhibition rate
7 %
[101]
 Toxin Info    Defensin BmKDfsin5 Inhibition rate
8.7 %
[102], [103]
 Toxin Info    Kunitz-type serine protease inhibitor LmKTT-1a Inhibition rate
25 %
[104], [105], [106], [107]
 Toxin Info    Defensin BmKDfsin4 Inhibition rate
25.2 %
[102- 109]
 Toxin Info    Potassium channel toxin alpha-KTx 8.6 Inhibition rate
35 %
[110], [111]
 Toxin Info    Toxin MeKTx13-3 (D33H) Inhibition rate
46 %
[112]
 Toxin Info    Kunitz-type kappaPI-theraphotoxin-Hs1e Inhibition rate
59 %
[113], [114]
 Toxin Info    Kunitz-type kappaPI-theraphotoxin-Hs1e Inhibition rate
59.2 %
[113], [114]
 Toxin Info    Kunitz-type kappaPI-theraphotoxin-Hs1a Inhibition rate
78 %
[113- 118]
 Toxin Info    Kunitz-type kappaPI-theraphotoxin-Hs1a Inhibition rate
78 %
[113- 118]
 Toxin Info    Kunitz-type serine protease inhibitor homolog dendrotoxin K Effective concentration 50
0.6 nM
[2- 8]
 Toxin Info    Kappa-stichotoxin-She3a IC50
6.7 - 87 pM
[15- 131]
 Toxin Info    Kappa-actitoxin-Bcs4a IC50
˜3 nM
[132]
 Toxin Info    Potassium channel toxin alpha-KTx 2.5 IC50
0.031 nM
[1- 133]
 Toxin Info    Kunitz-type serine protease inhibitor homolog dendrotoxin K IC50
0.05 nM
[2- 8]
 Toxin Info    HgTX1 (A19Y,Y37F) IC50
0.067 nM
[1]
 Toxin Info    Kunitz-type serine protease inhibitor homolog dendrotoxin I IC50
0.13 - 50 nM
[4- 136]
 Toxin Info    Potassium channel toxin alpha-KTx 2.2 IC50
0.144 nM
[87- 138]
 Toxin Info    Potassium channel toxin alpha-KTx 2.2 IC50
0.144 nM
[1- 141]
 Toxin Info    Kunitz-type serine protease inhibitor homolog alpha-dendrotoxin IC50
0.4 - 150 nM
[9], [10], [11], [12]
 Toxin Info    Potassium channel toxin alpha-KTx 3.7 IC50
0.6 nM
[24- 144]
 Toxin Info    Potassium channel toxin alpha-KTx 1.2 IC50
1 nM
[145], [146], [147]
 Toxin Info    Potassium channel toxin alpha-KTx 6.2 IC50
37 - 45 nM
[96- 159]
 Toxin Info    Potassium channel toxin alpha-KTx 9.5 IC50
145 nM
[160]
 Toxin Info    Hge-scorpine IC50
185 nM
[161], [162], [163], [164]
 Toxin Info    Kunitz-type serine protease inhibitor dendrotoxin DaE1 IC50
300 nM
[165]
 Toxin Info    Kunitz-type serine protease inhibitor dendrotoxin DaE1 IC50
300 nM
[165]
 Toxin Info    Upsilon-Da2a (S3K) IC50
308 nM
[40]
 Toxin Info    Kappa-actitoxin-Ate1a IC50
353 nM
[166]
 Toxin Info    Crotamine IC50
369 nM
[167- 184]
 Toxin Info    Kunitz-type serine protease inhibitor HWTX-XI-IS5 IC50
530 nM
[113]
 Toxin Info    AsKC11 IC50
650 nM
[113]
 Toxin Info    Potassium channel toxin AbeTx1 IC50
671.95 nM
[185]
 Toxin Info    Potassium channel toxin alpha-KTx 6.3 IC50
711 nM
[36- 189]
 Toxin Info    Beta-theraphotoxin-Gr1a IC50
>200 μM
[190], [191], [192], [193]
 Toxin Info    Beta-theraphotoxin-Gr1b IC50
>200 μM
[191], [192], [193]
 Toxin Info    Kappa-theraphotoxin-Gr2c IC50
>200 μM
[194], [191], [192], [193]
 Toxin Info    Kappa-theraphotoxin-Gr3a IC50
>200 μM
[191- 199]
 Toxin Info    Potassium channel toxin kappa-KTx 5.1 IC50
0.5785 - 9.9 μM
[24- 202]
 Toxin Info    Potassium channel toxin alpha-KTx 12.5 IC50
1.7 μM
[104- 203]
 Toxin Info    Kunitz-type serine protease inhibitor huwentoxin-11 (A1P,A2R,K3I,Y4D,C5T,R6C,L7R,P8L,S9P,D10S,R11D,G12R,R13G,C14R,K15C,A16K,S17A,F18S,E19F,R20E,W21R,Y22W,F23Y,N24F,G25N,R26G,T27R,C28T,A29C,K30A,F31K,I32F,Y33I,G34Y,C36G,G37C,N39G,G40N,N41G,K42N,F43K,P44F,T45P,Q46T,E47Q,A48E,C49A,M50C,K51M,R52K,C53R,A54C,K55A,A56K) IC50
2.46 μM
[113]
 Toxin Info    Kunitz-type serine protease inhibitor huwentoxin-11 (T3Y) IC50
2.49 μM
[113]
 Toxin Info    Kunitz-type serine protease inhibitor HWTX-XI-IS4 IC50
2.53 μM
[113]
 Toxin Info    Kunitz-type serine protease inhibitor huwentoxin-11 (G24W) IC50
2.55 μM
[113]
 Toxin Info    Kunitz-type kappaPI-theraphotoxin-Hs1a IC50
2.57 μM
[113- 118]
 Toxin Info    Kunitz-type serine protease inhibitor huwentoxin-11 (R25A) IC50
2.61 μM
[113]
 Toxin Info    Kunitz-type serine protease inhibitor huwentoxin-11 (S16R) IC50
2.61 μM
[113]
 Toxin Info    Kunitz-type serine protease inhibitor huwentoxin-11 (L6Y) IC50
2.66 μM
[113]
 Toxin Info    Kunitz-type serine protease inhibitor huwentoxin-11 (R10T) IC50
2.81 μM
[113]
 Toxin Info    Kunitz-type serine protease inhibitor huwentoxin-11 (K14N) IC50
3.07 μM
[113]
 Toxin Info    Pi4_T3Y_Y6L IC50
3.15 μM
[113]
 Toxin Info    Kunitz-type serine protease inhibitor huwentoxin-11 (L6A) IC50
3.42 μM
[113]
 Toxin Info    Kunitz-type serine protease inhibitor huwentoxin-11 IC50
4.62 μM
[113]
 Toxin Info    Potassium channel toxin alpha-KTx 6 hetlaxin IC50
6.7 μM
[204], [205]
 Toxin Info    Mambaquaretin-1 IC50
8.2 μM
[40- 207]
 Toxin Info    Mambaquaretin-1 IC50
8.2 μM
[40- 207]
 Toxin Info    Kunitz-type serine protease inhibitor huwentoxin-11 (K50A) IC50
10.8 μM
[113]
 Toxin Info    Kunitz-type serine protease inhibitor huwentoxin-11 (R12P) IC50
36.5 μM
[113]
 Toxin Info    M-theraphotoxin-Gr1a IC50
53 - 85 μM
[191- 218]
 Toxin Info    Pi4 IC50
481 μM
[113]
 Toxin Info    Kunitz-type serine protease inhibitor huwentoxin-11 (K14A) IC50
500 μM
[113]
References
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Ref 2 Cloning and functional expression of dendrotoxin K from black mamba, a K+ channel blocker. Biochemistry. 1993 Jun 1;32(21):5692-7. doi: 10.1021/bi00072a026.
Ref 3 Snake venom toxins. The amino acid sequence of toxin Vi2, a homologue of pancreatic trypsin inhibitor, from Dendroaspis polylepis polylepis (black mamba) venom. Biochim Biophys Acta. 1977 Apr 25;491(2):361-9. doi: 10.1016/0005-2795(77)90279-3.
Ref 4 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 5 Site-directed mutagenesis of dendrotoxin K reveals amino acids critical for its interaction with neuronal K+ channels. Biochemistry. 1997 Jun 24;36(25):7690-6. doi: 10.1021/bi963105g.
Ref 6 The relative potencies of dendrotoxins as blockers of the cloned voltage-gated K+ channel, mKv1.1 (MK-1), when stably expressed in Chinese hamster ovary cells. Br J Pharmacol. 1997 Mar;120(6):1029-34. doi: 10.1038/sj.bjp.0701004.
Ref 7 Identification of residues in dendrotoxin K responsible for its discrimination between neuronal K+ channels containing Kv1.1 and 1.2 alpha subunits. Eur J Biochem. 1999 Jul;263(1):222-9. doi: 10.1046/j.1432-1327.1999.00494.x.
Ref 8 Nuclear magnetic resonance solution structure of dendrotoxin K from the venom of Dendroaspis polylepis polylepis. J Mol Biol. 1993 Dec 5;234(3):735-50. doi: 10.1006/jmbi.1993.1623.
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Ref 11 Protease inhibitors from marine venomous animals and their counterparts in terrestrial venomous animals. Mar Drugs. 2013 Jun 14;11(6):2069-112. doi: 10.3390/md11062069.
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Ref 15 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 16 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 17 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.
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Ref 26 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.
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Ref 28 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.
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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 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 36 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 37 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 38 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 39 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 40 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 41 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 42 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 43 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 44 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 45 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 46 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 47 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 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 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 50 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 51 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 52 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 53 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 54 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 55 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 56 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 57 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 58 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 59 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 60 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 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 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 66 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 67 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 68 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 69 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 70 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 71 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.
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