General Information of This Target
Target ID
BTDT00131
Target Name
Potassium voltage-gated channel subfamily A member 1 (KCNA1)
Target Bioclass
Transporter and channel
Uniprot ID
Q09470
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
KCNA1
Gene ID
3736
Synonym
Voltage-gated K(+) channel HuKI; Voltage-gated potassium channel HBK1; Voltage-gated potassium channel subunit Kv1.1
Sequence
MTVMSGENVDEASAAPGHPQDGSYPRQADHDDHECCERVVINISGLRFETQLKTLAQFPN
TLLGNPKKRMRYFDPLRNEYFFDRNRPSFDAILYYYQSGGRLRRPVNVPLDMFSEEIKFY
ELGEEAMEKFREDEGFIKEEERPLPEKEYQRQVWLLFEYPESSGPARVIAIVSVMVILIS
IVIFCLETLPELKDDKDFTGTVHRIDNTTVIYNSNIFTDPFFIVETLCIIWFSFELVVRF
FACPSKTDFFKNIMNFIDIVAIIPYFITLGTEIAEQEGNQKGEQATSLAILRVIRLVRVF
RIFKLSRHSKGLQILGQTLKASMRELGLLIFFLFIGVILFSSAVYFAEAEEAESHFSSIP
DAFWWAVVSMTTVGYGDMYPVTIGGKIVGSLCAIAGVLTIALPVPVIVSNFNYFYHRETE
GEEQAQLLHVSSPNLASDSDLSRRSSSTMSKSEYMEIEEDMNNSIAHYRQVNIRTANCTT
ANQNCVNKSKLLTDV

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Family
the potassium channel family
Function
Voltage-gated potassium channel that mediates transmembrane potassium transport in excitable membranes, primarily in the brain and the central nervous system, but also in the kidney. Contributes to the regulation of the membrane potential and nerve signaling, and prevents neuronal hyperexcitability. 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, KCNA5, KCNA6, KCNA7, 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 of delayed rectifier potassium channels. In vivo, membranes probably contain a mixture of heteromeric potassium channel complexes, making it difficult to assign currents observed in intact tissues to any particular potassium channel family member. Homotetrameric KCNA1 forms a delayed-rectifier potassium channel that opens in response to membrane depolarization, followed by slow spontaneous channel closure. In contrast, a heterotetrameric channel formed by KCNA1 and KCNA4 shows rapid inactivation. Regulates neuronal excitability in hippocampus, especially in mossy fibers and medial perforant path axons, preventing neuronal hyperexcitability. Response to toxins that are selective for KCNA1, respectively for KCNA2, suggests that heteromeric potassium channels composed of both KCNA1 and KCNA2 play a role in pacemaking and regulate the output of deep cerebellar nuclear neurons. May function as down-stream effector for G protein-coupled receptors and inhibit GABAergic inputs to basolateral amygdala neurons. May contribute to the regulation of neurotransmitter release, such as gamma-aminobutyric acid (GABA) release. Plays a role in regulating the generation of action potentials and preventing hyperexcitability in myelinated axons of the vagus nerve, and thereby contributes to the regulation of heart contraction. Required for normal neuromuscular responses. Regulates the frequency of neuronal action potential firing in response to mechanical stimuli, and plays a role in the perception of pain caused by mechanical stimuli, but does not play a role in the perception of pain due to heat stimuli. Required for normal responses to auditory stimuli and precise location of sound sources, but not for sound perception. The use of toxins that block specific channels suggest that it contributes to the regulation of the axonal release of the neurotransmitter dopamine. Required for normal postnatal brain development and normal proliferation of neuronal precursor cells in the brain. Plays a role in the reabsorption of Mg(2+) in the distal convoluted tubules in the kidney and in magnesium ion homeostasis, probably via its effect on the membrane potential.

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Taxonomy ID
9606
TCDB ID
1.A.1.2.12
        Click to Show/Hide the Complete Species Lineage
Kingdom: Metazoa
Phylum: Chordata
Class: Mammalia
Order: Primates
Family: Hominidae
Genus: Homo
Species: Homo sapiens
Toxin Information Related to This Target
                           Toxin Name Activity Data Type Activity Data Reference
 Toxin Info    U-AITX-Bg1c . . [1]
 Toxin Info    Toxin APETx1 (P3T) . . [2]
 Toxin Info    Toxin APETx1 (D42A) . . [2]
 Toxin Info    Toxin APETx1 (F33A) . . [2]
 Toxin Info    Toxin APETx1 (K18A) . . [2]
 Toxin Info    Toxin APETx1 (L34A) . . [2]
 Toxin Info    Toxin APETx1 (N23A) . . [2]
 Toxin Info    Toxin APETx1 (R24A) . . [2]
 Toxin Info    Toxin APETx1 (S22A) . . [2]
 Toxin Info    Toxin APETx1 (S29A) . . [2]
 Toxin Info    Toxin APETx1 (T19A) . . [2]
 Toxin Info    Toxin APETx1 (T27A) . . [2]
 Toxin Info    Toxin APETx1 (Y32A) . . [2]
 Toxin Info    Toxin APETx1 (Y5A . . [2]
 Toxin Info    Toxin APETx4 . . [2]
 Toxin Info    Toxin APETx4 (K8A,A15F) . . [2]
 Toxin Info    Toxin APETx2 . . [1]
 Toxin Info    Toxin APETx2_A33F_L34A . . [1]
 Toxin Info    Potassium channel toxin gamma-KTx 1.1 Dissociation constant
4.5 nM
[3]
 Toxin Info    BeKm1 (E9A) Dissociation constant
4.8 nM
[4]
 Toxin Info    BeKm1 (D34A) Dissociation constant
7.2 nM
[4]
 Toxin Info    BeKm1 (V29A) Dissociation constant
7.4 nM
[4]
 Toxin Info    Potassium channel toxin gamma-KTx 2.1 Dissociation constant
7.7 nM
[3]
 Toxin Info    BeKm1 (F32A) Dissociation constant
9.1 nM
[4]
 Toxin Info    BeKm1 (P2A) Dissociation constant
10.9 nM
[4]
 Toxin Info    Potassium channel toxin gamma-KTx 1.7 Dissociation constant
12.8 nM
[5]
 Toxin Info    CeErg4 Dissociation constant
14.2 nM
[6]
 Toxin Info    BeKm1 (Q12A) Dissociation constant
14.3 nM
[4]
 Toxin Info    BeKm1 (K6A) Dissociation constant
17.2 nM
[4]
 Toxin Info    BeKm1 (F36A) Dissociation constant
20.2 nM
[4]
 Toxin Info    BeKm1 (D4A) Dissociation constant
21.2 nM
[4]
 Toxin Info    BeKm1 (R1A) Dissociation constant
41.9 nM
[4]
 Toxin Info    BeKm1 (R27A) Dissociation constant
46.7 nM
[4]
 Toxin Info    BeKm1 (F14A) Dissociation constant
51.9 nM
[4]
 Toxin Info    ErgTx1 (Q18A,A35M) Dissociation constant
72.9 nM
[6]
 Toxin Info    BeKm1 (K23A) Dissociation constant
92.2 nM
[4]
 Toxin Info    BeKm1 (Y11A) Dissociation constant
92.4 nM
[4]
 Toxin Info    ErgTx1 Dissociation constant
303.4 nM
[7]
 Toxin Info    BeKm1 (F21A) Dissociation constant
328.6 nM
[4]
 Toxin Info    BeKm1 (R20A) Dissociation constant
444.8 nM
[4]
 Toxin Info    BeKm1 (K18A) Dissociation constant
544.3 nM
[4]
 Toxin Info    Potassium channel toxin alpha-KTx 15.2 Dissociation constant
1.9 μM
[8]
 Toxin Info    N.vectensis toxin 4 Effect . [9]
 Toxin Info    N.vectensis toxin 5 Effect . [9]
 Toxin Info    OsK1 (R12P,E16K,K20D) Inhibition rate . [10]
 Toxin Info    OsK1 (E16K) Inhibition rate . [10]
 Toxin Info    OsK1 (E16K) Inhibition rate . [10]
 Toxin Info    Potassium channel toxin alpha-KTx 23.1 Inhibition rate . [11]
 Toxin Info    Potassium channel toxin ShK ([Ppa][AEEA],M21[Nle]) Inhibition rate . [12]
 Toxin Info    Potassium channel toxin ShK ([pTyr][AEEA]) Inhibition rate . [13]
 Toxin Info    DiscrepinK6V) Inhibition rate . [14]
 Toxin Info    Toxin MeKTx13-3 (D19K) Inhibition rate . [15]
 Toxin Info    Toxin MeKTx13-3 (K6D,D19K) Inhibition rate . [15]
 Toxin Info    OsK1 (E14A,K18D) Inhibition rate . [16]
 Toxin Info    OsK1 (E15A,K19D) Inhibition rate . [16]
 Toxin Info    Defensin domain protein Inhibition rate . [17]
 Toxin Info    U-actitoxin-Oulsp2 Inhibition rate . [18]
 Toxin Info    Defensin-like protein 1 Inhibition rate . [19]
 Toxin Info    Crotamine Inhibition rate . [20]
 Toxin Info    Kappa-actitoxin-Bcs3a Inhibition rate . [21]
 Toxin Info    Kappa-actitoxin-Bcs3b Inhibition rate . [21]
 Toxin Info    Kappa-conotoxin ViTx Inhibition rate . [22], [23]
 Toxin Info    Mambaquaretin-1 Inhibition rate . [24], [25], [26]
 Toxin Info    Potassium channel toxin alpha-KTx 1.11 Inhibition rate . [27]
 Toxin Info    Potassium channel toxin alpha-KTx 1.15 Inhibition rate . [28]
 Toxin Info    Potassium channel toxin alpha-KTx 1.16 Inhibition rate . [29]
 Toxin Info    Potassium channel toxin alpha-KTx 1.17 Inhibition rate . [29]
 Toxin Info    Potassium channel toxin alpha-KTx 15.6 Inhibition rate . [14]
 Toxin Info    Potassium channel toxin alpha-KTx 2.14 Inhibition rate . [30]
 Toxin Info    Potassium channel toxin alpha-KTx 3.13 Inhibition rate . [31]
 Toxin Info    Potassium channel toxin alpha-KTx 19.1 Inhibition rate . [32]
 Toxin Info    Potassium channel toxin alpha-KTx 4.1 Inhibition rate . [14]
 Toxin Info    Potassium channel toxin alpha-KTx 4.6 Inhibition rate . [33]
 Toxin Info    Potassium channel toxin alpha-KTx 8.2 Inhibition rate . [34]
 Toxin Info    Potassium channel toxin alpha-KTx 8.6 Inhibition rate . [34], [35]
 Toxin Info    Potassium channel toxin alpha-KTx 8.6 Inhibition rate . [34]
 Toxin Info    Kappa-actitoxin-Bcs4a Inhibition rate . [36]
 Toxin Info    Potassium channel toxin AbeTx1 Inhibition rate . [37]
 Toxin Info    Potassium channel toxin AbeTx1 Inhibition rate . [37]
 Toxin Info    Potassium channel toxin alpha-KTx 8.8 Inhibition rate . [38]
 Toxin Info    Potassium channel toxin kappa-KTx 2.5 Inhibition rate . [39]
 Toxin Info    U-actitoxin-Oulsp1 Inhibition rate . [40]
 Toxin Info    Mu-scoloptoxin(15)-Ssm1a Inhibition rate . [41]
 Toxin Info    Kappa-actitoxin-Ael2e Inhibition rate . [42]
 Toxin Info    Potassium channel toxin alpha-KTx 32.1 Inhibition rate . [43]
 Toxin Info    Apamin Inhibition rate . [44- 61]
 Toxin Info    Potassium channel toxin alpha-KTx 20.1 Inhibition rate . [62]
 Toxin Info    Potassium channel toxin alpha-KTx 3.11 Inhibition rate . [63]
 Toxin Info    Mu-theraphotoxin-Pspp1 Inhibition rate . [64]
 Toxin Info    Potassium channel toxin alpha-KTx 16.4 Inhibition rate . [65]
 Toxin Info    Kappa-actitoxin-Ate1a Inhibition rate . [66]
 Toxin Info    Toxin VmKTx1 Inhibition rate . [67]
 Toxin Info    Potassium channel toxin alpha-KTx 1.10 Inhibition rate . [14]
 Toxin Info    Potassium channel toxin alpha-KTx 6.13 Inhibition rate . [14]
 Toxin Info    Potassium channel toxin alpha-KTx 2.13 Inhibition rate . [68]
 Toxin Info    Potassium channel toxin alpha-KTx 21.1 Inhibition rate . [69]
 Toxin Info    Potassium channel toxin alpha-KTx 3.6 Inhibition rate . [31]
 Toxin Info    Potassium channel toxin ShK ([pTyr][AEEA]) Inhibition rate . [12]
 Toxin Info    OsK1 (E16K,K20D) Inhibition rate . [16]
 Toxin Info    KappaPI-actitoxin-Ael3a Inhibition rate . [70], [71]
 Toxin Info    Toxin AmmTX3 (R18A) Inhibition rate . [14]
 Toxin Info    Toxin AmmTX3 (R18A,A18R,K19A) Inhibition rate . [14]
 Toxin Info    Discrepin (V6K,R19I,K20D,V21R Inhibition rate . [14]
 Toxin Info    Potassium channel toxin alpha-KTx 3.7 Inhibition rate . [10]
 Toxin Info    OsK1 (E16K,K20D) Inhibition rate . [10]
 Toxin Info    [D20]- OsK1 Inhibition rate . [10]
 Toxin Info    Fungal defensin plectasin Inhibition rate
4 %
[72]
 Toxin Info    Thrombin-like enzyme collinein-1 Inhibition rate
5 %
[73], [74], [75], [76]
 Toxin Info    Neutrophil defensin 1 Inhibition rate
6 %
[77]
 Toxin Info    Defensin BmKDfsin5 Inhibition rate
9 %
[78]
 Toxin Info    Mu-theraphotoxin-Cg2a 3 Inhibition rate
9 %
[79]
 Toxin Info    Defensin alpha 5 Inhibition rate
9 %
[77]
 Toxin Info    Potassium channel toxin alpha-KTx 12.2 Inhibition rate
11 %
[80]
 Toxin Info    Potassium channel toxin alpha-KTx 12.1 Inhibition rate
11 %
[80]
 Toxin Info    Beta/kappa-theraphotoxin-Cg1a Inhibition rate
11 %
[81- 85]
 Toxin Info    Defensin BmKDfsin4 Inhibition rate
12 %
[86]
 Toxin Info    Potassium channel toxin epsilon-KTx 1.1 Inhibition rate
12 %
[87]
 Toxin Info    Beta-defensin 1 Inhibition rate
13 %
[88]
 Toxin Info    BmK86-P1 Inhibition rate
13 %
[89]
 Toxin Info    Defensin domain protein Inhibition rate
15 %
[17]
 Toxin Info    U20-theraphotoxin-Cg1a 1 Inhibition rate
15 %
[79]
 Toxin Info    Discrepin (K20D,V21R Inhibition rate
18.5 %
[14]
 Toxin Info    Potassium channel toxin alpha-KTx Ctri9577 Inhibition rate
19 %
[90]
 Toxin Info    Discrepin (R19I,D20K) Inhibition rate
20.2 %
[14]
 Toxin Info    Potassium channel toxin epsilon-KTx 1.2 Inhibition rate
24 %
[87]
 Toxin Info    Potassium channel toxin alpha-KTx 15.1 Inhibition rate
25 %
[14]
 Toxin Info    Beta/kappa-theraphotoxin-Hlv1a Inhibition rate
25 %
[91]
 Toxin Info    Defensin BmKDfsin3 Inhibition rate
30 %
[78- 92]
 Toxin Info    Potassium channel toxin alpha-KTx 6.3 Inhibition rate
35 %
[14]
 Toxin Info    ProTx2 Inhibition rate
40 %
[91]
 Toxin Info    Pi-stichotoxin-Hcr5b Inhibition rate
52 %
[93]
 Toxin Info    Potassium channel toxin alpha-KTx 4.2 Inhibition rate
53 %
[14]
 Toxin Info    Potassium channel toxin alpha-KTx 1.6 Inhibition rate
60 %
[14]
 Toxin Info    Potassium channel toxin gamma-KTx 1.8 Inhibition rate
90 %
[5]
 Toxin Info    BeKm1 IC50
0.014 nM
[94]
 Toxin Info    Potassium channel toxin gamma-KTx 1.10 IC50
3.4 nM
[95]
 Toxin Info    Potassium channel toxin gamma-KTx 1.10 IC50
3.4 nM
[95]
 Toxin Info    Potassium channel toxin gamma-KTx 2.2 IC50
6.7 nM
[96]
 Toxin Info    Potassium channel toxin gamma-KTx 2.1 IC50
7.7 nM
[97]
 Toxin Info    Potassium channel gamma toxin gamma-KTx 1.9 IC50
16.9 nM
[98]
 Toxin Info    Potassium channel gamma toxin gamma-KTx 1.9 IC50
16.9 nM
[98]
 Toxin Info    BeKm1 IC50
27 nM
[94]
 Toxin Info    Kappa-actitoxin-Ael2a IC50
34 nM
[3- 103]
 Toxin Info    BeKm1 IC50
64.1 nM
[104]
 Toxin Info    BeKm1_R27K IC50
80.5 nM
[104]
 Toxin Info    BeKm1 IC50
88.6 nM
[104]
 Toxin Info    BeKm1 IC50
280 nM
[104]
 Toxin Info    U21-theraphotoxin-Cg1b IC50
612.6 nM
[79]
 Toxin Info    Delta-theraphotoxin-Cg1a 1 IC50
626.9 nM
[83- 109]
 Toxin Info    U-Asilidin(12)-Dg3b IC50
1 μM
[110], [111]
 Toxin Info    APETx2 IC50
1.21 μM
[1- 119]
 Toxin Info    APETx2 IC50
1.21 μM
[1- 119]
 Toxin Info    Toxin AmmTX3 (K6V) IC50
3.2 μM
[14]
 Toxin Info    Discrepin (I19R,D20K,R21V) IC50
3.5 μM
[14]
 Toxin Info    Beta/kappa-theraphotoxin-Gi1a IC50
3.695 μM
[120]
 Toxin Info    Beta-theraphotoxin-Gr1a IC50
4.2 μM
[121], [122], [123], [124]
 Toxin Info    Kappa-theraphotoxin-Gr2c IC50
4.7 μM
[125], [122], [123], [124]
 Toxin Info    Beta-theraphotoxin-Gr1b IC50
4.8 μM
[122], [123], [124]
 Toxin Info    Kappa-theraphotoxin-Gr3a IC50
7.4 μM
[122- 130]
 Toxin Info    Potassium channel toxin alpha-KTx 15.3 IC50
7.9 μM
[14]
 Toxin Info    Potassium channel toxin alpha-KTx 15.7 IC50
7.9 μM
[14]
 Toxin Info    Mu/kappa-theraphotoxin-Ap1a IC50
8.197 μM
[131]
 Toxin Info    Kappa-theraphotoxin-Aa1a IC50
8.511 μM
[131]
 Toxin Info    M-theraphotoxin-Gr1a IC50
11 μM
[122- 142]
References
Ref 1 Understanding the molecular basis of toxin promiscuity: the analgesic sea anemone peptide APETx2 interacts with acid-sensing ion channel 3 and hERG channels via overlapping pharmacophores. J Med Chem. 2014 Nov 13;57(21):9195-203. doi: 10.1021/jm501400p. Epub 2014 Nov 4.
Ref 2 Mechanism of hERG inhibition by gating-modifier toxin, APETx1, deduced by functional characterization. BMC Mol Cell Biol. 2021 Jan 7;22(1):3. doi: 10.1186/s12860-020-00337-3.
Ref 3 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 4 New binding site on common molecular scaffold provides HERG channel specificity of scorpion toxin BeKm-1. J Biol Chem. 2002 Nov 8;277(45):43104-9. doi: 10.1074/jbc.M204083200. Epub 2002 Jul 31.
Ref 5 Two novel ergtoxins, blockers of K+-channels, purified from the Mexican scorpion Centruroides elegans elegans. Neurochem Res. 2008 Aug;33(8):1525-33. doi: 10.1007/s11064-008-9634-8. Epub 2008 Mar 13.
Ref 6 Positive selection-guided mutational analysis revealing two key functional sites of scorpion ERG K(+) channel toxins. Biochem Biophys Res Commun. 2012 Dec 7;429(1-2):111-6. doi: 10.1016/j.bbrc.2012.10.065. Epub 2012 Oct 24.
Ref 7 Recombinant expression of the toxic peptide ErgTx1 and role of Met35 on its stability and function. Peptides. 2011 Mar;32(3):560-7. doi: 10.1016/j.peptides.2010.06.018. Epub 2010 Jun 30.
Ref 8 BmTx3, a scorpion toxin with two putative functional faces separately active on A-type K+ and HERG currents. Biochem J. 2004 Mar 15;378(Pt 3):745-52. doi: 10.1042/BJ20031324.
Ref 9 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 10 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 11 Vm24, a natural immunosuppressive peptide, potently and selectively blocks Kv1.3 potassium channels of human T cells. Mol Pharmacol. 2012 Sep;82(3):372-82. doi: 10.1124/mol.112.078006. Epub 2012 May 23.
Ref 12 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 13 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 14 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 15 Toxin acidic residue evolutionary function-guided design of de novo peptide drugs for the immunotherapeutic target, the Kv1.3 channel. Sci Rep. 2015 May 8;5:9881. doi: 10.1038/srep09881.
Ref 16 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 17 Genome and Transcriptome Sequences Reveal the Specific Parasitism of the Nematophagous Purpureocillium lilacinum 36-1. Front Microbiol. 2016 Jul 19;7:1084. doi: 10.3389/fmicb.2016.01084. eCollection 2016.
Ref 18 Synthesis, folding, structure and activity of a predicted peptide from the sea anemone Oulactis sp. with an ShKT fold. Toxicon. 2018 Aug;150:50-59. doi: 10.1016/j.toxicon.2018.05.006. Epub 2018 May 19.
Ref 19 The antifungal plant defensin AtPDF2.3 from Arabidopsis thaliana blocks potassium channels. Sci Rep. 2016 Aug 30;6:32121. doi: 10.1038/srep32121.
Ref 20 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 21 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 22 A novel conotoxin inhibiting vertebrate voltage-sensitive potassium channels. Toxicon. 2003 Jul;42(1):43-52. doi: 10.1016/s0041-0101(03)00099-0.
Ref 23 Novel conopeptides of the I-superfamily occur in several clades of cone snails. Toxicon. 2004 Oct;44(5):539-48. doi: 10.1016/j.toxicon.2004.07.006.
Ref 24 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 25 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 26 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 27 Slotoxin, alphaKTx1.11, a new scorpion peptide blocker of MaxiK channels that differentiates between alpha and alpha+beta (beta1 or beta4) complexes. FEBS Lett. 2001 Sep 21;505(3):369-73. doi: 10.1016/s0014-5793(01)02791-0.
Ref 28 Different pharmacological properties between scorpion toxin BmKcug2 and its degraded analogs highlight the diversity of K(+) channel blockers from thermally processed scorpions. Int J Biol Macromol. 2021 May 1;178:143-153. doi: 10.1016/j.ijbiomac.2021.02.155. Epub 2021 Feb 23.
Ref 29 K(V)1.2 channel-specific blocker from Mesobuthus eupeus scorpion venom: Structural basis of selectivity. Neuropharmacology. 2018 Dec;143:228-238. doi: 10.1016/j.neuropharm.2018.09.030. Epub 2018 Sep 22.
Ref 30 A K? channel blocking peptide from the Cuban scorpion Rhopalurus garridoi. Peptides. 2014 Mar;53:42-7. doi: 10.1016/j.peptides.2013.10.010. Epub 2013 Oct 25.
Ref 31 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 32 BmBKTx1, a novel Ca2+-activated K+ channel blocker purified from the Asian scorpion Buthus martensi Karsch. J Biol Chem. 2004 Aug 13;279(33):34562-9. doi: 10.1074/jbc.M312798200. Epub 2004 Jun 3.
Ref 33 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 34 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 35 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 36 BcsTx3 is a founder of a novel sea anemone toxin family of potassium channel blocker. FEBS J. 2013 Oct;280(19):4839-52. doi: 10.1111/febs.12456. Epub 2013 Aug 23.
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