Target Information

General Information of This Target
Target ID
BTDT00059
Target Name
Potassium voltage-gated channel subfamily A member 3 (Kcna3)
Target Bioclass
Transporter and channel
Uniprot ID
P16390
3D Structure
Download
2D Sequence
3D Structure
Source
Predict by Alphafold2
?
Alphafold Parameters: msa_mode: mmseqs2_uniref_env model_type: auto num_recycles: auto
Gene Name
Kcna3
Gene ID
16491
Synonym
MK3; Voltage-gated potassium channel subunit Kv1.3
Sequence
MTVVPGDHLLEPEAAGGGGGDPPQGGCGSGGGGGGCDRYEPLPPALPAAGEQDCCGERVV
INISGLRFETQLKTLCQFPETLLGDPKRRMRYFDPLRNEYFFDRNRPSFDAILYYYQSGG
RIRRPVNVPIDIFSEEIRFYQLGEEAMEKFREDEGFLREEERPLPRRDFQRQVWLLFEYP
ESSGPARGIAIVSVLVILISIVIFCLETLPEFRDEKDYPASPSQDVFEAANNSTSGAPSG
ASSFSDPFFVVETLCIIWFSFELLVRFFACPSKATFSRNIMNLIDIVAIIPYFITLGTEL
AERQGNGQQAMSLAILRVIRLVRVFRIFKLSRHSKGLQILGQTLKASMRELGLLIFFLFI
GVILFSSAVYFAEADDPSSGFNSIPDAFWWAVVTMTTVGYGDMHPVTIGGKIVGSLCAIA
GVLTIALPVPVIVSNFNYFYHRETEGEEQAQYMHVGSCQHLSSSAEELRKARSNSTLSKS
EYMVIEEGGMNHSAFPQTPFKTGNSTATCTTNNNPNSCVNIKKIFTDV

    Click to Show/Hide
Family
the potassium channel family
Function
Mediates the voltage-dependent potassium ion permeability of excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a potassium-selective channel through which potassium ions may pass in accordance with their electrochemical gradient.

    Click to Show/Hide
Taxonomy ID
10090
        Click to Show/Hide the Complete Species Lineage
Kingdom: Metazoa
Phylum: Chordata
Class: Mammalia
Order: Rodentia
Family: Muridae
Genus: Mus
Species: Mus musculus
Toxin Information Related to This Target
                           Toxin Name Activity Data Type Activity Data Reference
 Toxin Info    Potassium channel toxin alpha-KTx 2.1 Dissociation constant
>25 nM
 [1], [2], [3], [4]
 Toxin Info    Potassium channel toxin ShK ([pTyrMe][AEEA]) Dissociation constant
0.01 nM
 [5]
 Toxin Info    Potassium channel toxin ShK ([pTyr2Me][AEEA]) Dissociation constant
0.024 nM
 [5]
 Toxin Info    Potassium channel toxin ShK (K22[Dap]) Dissociation constant
0.024 nM
 [6]
 Toxin Info    Potassium channel toxin ShK (Y[AEEA] Dissociation constant
0.047 nM
 [5]
 Toxin Info    Potassium channel toxin ShK (K22[Dap]) Dissociation constant
0.052 nM
 [5]
 Toxin Info    Potassium channel toxin ShK ([Apa][AEEA]) Dissociation constant
0.065 nM
 [5]
 Toxin Info    Potassium channel toxin ShK ([pTyr][AEEA]) Dissociation constant
0.069 nM
 [5]
 Toxin Info    Potassium channel toxin ShK ([Pmp2Et]D[AEEA]) Dissociation constant
0.07 nM
 [5]
 Toxin Info    Potassium channel toxin ShK ([Pmp2Et][AEEA]) Dissociation constant
0.071 nM
 [5]
 Toxin Info    Potassium channel toxin ShK ([Cpa][AEEA]) Dissociation constant
0.094 nM
 [5]
 Toxin Info    Potassium channel toxin ShK ([PmpD][AEEA]) Dissociation constant
0.096 nM
 [5]
 Toxin Info    Potassium channel toxin ShK ([Pmp][AEEA]) Dissociation constant
0.293 nM
 [5]
 Toxin Info    Potassium channel toxin ShK ([PmpEtD][AEEA]) Dissociation constant
0.311 nM
 [5]
 Toxin Info    ShK (S20A) Dissociation constant
0.32 nM
 [6]
 Toxin Info    Potassium channel toxin alpha-KTx 2.1 Dissociation constant
1 nM
 [3]
 Toxin Info    Potassium channel toxin alpha-KTx 2.1 Dissociation constant
1 nM
 [1], [2], [3], [4]
 Toxin Info    Potassium channel toxin ShK ([pTyrD][AEEA]) Dissociation constant
1.1 nM
 [5]
 Toxin Info    Potassium channel toxin alpha-KTx 1.1 Dissociation constant
2 nM
 [7]
 Toxin Info    ChTx-c (E18Q,K19Y,Y21H,K32[Cpa]) Dissociation constant
121 nM
 [7]
 Toxin Info    Toxin II.10.4 (T7P,D9Q) Dissociation constant
260 nM
 [8]
 Toxin Info    ChTx-c (E18Q,K19Y,Y21H,K32D) Dissociation constant
274 nM
 [7]
 Toxin Info    ChTx-c (E18Q,K19Y,Y21H,K32E) Dissociation constant
693 nM
 [7]
 Toxin Info    Potassium channel toxin alpha-KTx 10.1 Dissociation constant
5.3 μM
 [8]
 Toxin Info    Pi1 (K24A,Y33[pTyr]) Inhibition rate . [12]
 Toxin Info    Pi1 (K24A,Y33A) Inhibition rate . [12]
 Toxin Info    Mu-conotoxin GIIIA Inhibition rate . [13- 25]
 Toxin Info    Mu-conotoxin PIIIA Inhibition rate . [14- 30]
 Toxin Info    Scorpine-like peptide Ev37 Inhibition rate . [31]
 Toxin Info    Mu-conotoxin SIIIA Inhibition rate . [21- 56]
 Toxin Info    Scorpine-like peptide Ev37 (G1N,I3C,N4A,E5F,K6N,K7V,V8D,Q9T,Q10V,Y11G,L12M,D13C,E14D,K15A,L16D,P17C,N18K,G19R,V20Q,V21G,G23A,A24K,L25G,K26V,S27C,L28H,V29G,H30T,A32C,A33K,K34C,N35D,Q36V) Inhibition rate . [31]
 Toxin Info    Delta-theraphotoxin-Hm1a Inhibition rate
3 %
 [57], [58], [59], [60]
 Toxin Info    Kappa-theraphotoxin-Hm2a Inhibition rate
6 %
 [57]
 Toxin Info    Potassium channel toxin alpha-KTx 28.1 Inhibition rate
7 %
 [61]
 Toxin Info    Kappa-theraphotoxin-Sc1a Inhibition rate
9 %
 [57]
 Toxin Info    Potassium channel toxin alpha-KTx 29.1 Inhibition rate
13 %
 [61]
 Toxin Info    Potassium channel toxin alpha-KTx 29.2 Inhibition rate
13 %
 [61]
 Toxin Info    Beta-defensin 3 Inhibition rate
14 %
 [62]
 Toxin Info    Kunitz-type serine protease inhibitor BmKTT-3 Inhibition rate
18 %
 [63]
 Toxin Info    Potassium channel toxin alpha-KTx 16.2 Inhibition rate
20 %
 [64]
 Toxin Info    Potassium channel toxin kappa-KTx 2.8 Inhibition rate
35 %
 [61]
 Toxin Info    Kunitz-type serine protease inhibitor LmKTT-1a Inhibition rate
50 %
 [63- 67]
 Toxin Info    Kunitz-type serine protease inhibitor LmKTT-1b Inhibition rate
50 %
 [63- 67]
 Toxin Info    Kunitz-type serine protease inhibitor LmKTT-1c Inhibition rate
50 %
 [63]
 Toxin Info    Potassium channel toxin alpha-KTx 30.1 Inhibition rate
64 %
 [61]
 Toxin Info    Kunitz-type serine protease inhibitor Hg1 Inhibition rate
80 %
 [63- 68]
 Toxin Info    Toxin MeKTx13-3 (G11R,I28T,D33H) IC50
2 pM
 [69]
 Toxin Info    [K16,D20]- OsK1 IC50
3 pM
 [70]
 Toxin Info    Kappa-stichotoxin-She3a IC50
0.011 nM
 [71]
 Toxin Info    Potassium channel toxin alpha-KTx 3.7 IC50
0.014 nM
 [70]
 Toxin Info    Toxin MeKTx13-3 (D33H) IC50
0.015 nM
 [72]
 Toxin Info    Potassium channel toxin ShK (K22[Dap]) IC50
0.023 nM
 [71]
 Toxin Info    Potassium channel toxin ShK ([Pmp][AEEA],M21[Nle]) IC50
0.025 nM
 [73]
 Toxin Info    OsK1 (E15K,K19D) IC50
0.025 nM
 [74]
 Toxin Info    ShK-Lys IC50
0.026 nM
 [75]
 Toxin Info    Toxin MeKTx13-3 (G11R,I28T,D33H,T35A) IC50
0.028 nM
 [69]
 Toxin Info    OsK1 (K20D) IC50
0.037 nM
 [70]
 Toxin Info    Potassium channel toxin ShK (Q16K,36A) IC50
0.037 nM
 [73]
 Toxin Info    Neurotoxin HsTX1 (R14A) IC50
0.045 nM
 [76]
 Toxin Info    Neurotoxin HsTX1 (R14[Abu]) IC50
0.05 nM
 [76]
 Toxin Info    Toxin MeKTx13-3 (K15A) IC50
0.055 nM
 [72]
 Toxin Info    Toxin MeKTx13-3 (G11R,I28A,D33H) IC50
0.058 nM
 [69]
 Toxin Info    [P12,K16,D20]- OsK1 IC50
0.059 nM
 [70]
 Toxin Info    Potassium channel toxin ShK (M21I) IC50
0.062 nM
 [73]
 Toxin Info    OsK1 (E16K) IC50
0.067 nM
 [70]
 Toxin Info    Potassium channel toxin ShK ([pTyr][AEEA]) IC50
0.06899 nM
 [77]
 Toxin Info    Potassium channel toxin ShK ([pTyr][AEEA]) IC50
0.069 nM
 [78]
 Toxin Info    Potassium channel toxin ShK ([pTyr][AEEA]) IC50
0.071 nM
 [78]
 Toxin Info    Toxin MeKTx13-3 (G11R,I28T,D33A) IC50
0.077 nM
 [69]
 Toxin Info    Potassium channel toxin ShK ([pTyr][AEEA],M21[Nle]) IC50
0.109 nM
 [78]
 Toxin Info    [K16,D20]- OsK1 IC50
0.122 nM
 [70]
 Toxin Info    Toxin MeKTx13-3 (T35A) IC50
0.134 nM
 [72]
 Toxin Info    Potassium channel toxin ShK ([Ppa][AEEA],M21[Nle]) IC50
0.14 nM
 [78]
 Toxin Info    Potassium channel toxin ShK ([Pmp][AEEA]) IC50
0.149 nM
 [78]
 Toxin Info    ([Pmp][AEEA])- ShK(Q16K) IC50
0.164 nM
 [73]
 Toxin Info    Potassium channel toxin alpha-KTX 12 Sp2 IC50
0.3 - 30 nM
 [79]
 Toxin Info    Defensin, beta 104 IC50
0.311 nM
 [80]
 Toxin Info    Toxin MeKTx13-3 (G11A,I28T,D33A) IC50
0.336 nM
 [69]
 Toxin Info    Toxin MeKTx13-3 (T35A,D33H) IC50
0.34 nM
 [72]
 Toxin Info    Toxin MeKTx13-3 (D19K) IC50
0.375 nM
 [81]
 Toxin Info    Toxin MeKTx13-3 (K8A) IC50
0.41 nM
 [72]
 Toxin Info    Toxin MeKTx13-3 (D33A) IC50
0.43 nM
 [72]
 Toxin Info    Toxin MeKTx13-3 (N4A) IC50
0.437 nM
 [72]
 Toxin Info    Toxin MeKTx13-3 (G11R,I28T,N29A,D33H) IC50
0.454 nM
 [69]
 Toxin Info    Toxin MeKTx13-3 (M22A) IC50
0.454 nM
 [72]
 Toxin Info    Toxin MeKTx13-3 (K6A) IC50
0.581 nM
 [72]
 Toxin Info    PBTx3 (N24F) IC50
0.657 nM
 [80]
 Toxin Info    Toxin MeKTx13-3 (I28A,D33H) IC50
0.721 nM
 [72]
 Toxin Info    Potassium channel toxin alpha-KTx J123 IC50
0.8 nM
 [82]
 Toxin Info    Toxin MeKTx13-3 (K31A) IC50
0.821 nM
 [72]
 Toxin Info    Toxin MeKTx13-3 (Q12A) IC50
0.93 nM
 [72]
 Toxin Info    Toxin MeKTx13-3 (G11R,K26A,I28T,D33H) IC50
0.9674 nM
 [69]
 Toxin Info    Toxin MeKTx13-3 (P36A) IC50
1.46 nM
 [72]
 Toxin Info    OsK1 (E16A,K20D) IC50
1.85 nM
 [74]
 Toxin Info    Toxin MeKTx13-3 (H9A) IC50
2.14 nM
 [72]
 Toxin Info    Toxin MeKTx13-3 (K18A) IC50
3.898 nM
 [72]
 Toxin Info    MTX (N21Y,A22G,I25M,K27R,S28K,Y32N,G33R) IC50
4 nM
 [83]
 Toxin Info    Toxin MeKTx13-3 (G11R,F24A,I28T,D33H) IC50
4.013 nM
 [69]
 Toxin Info    Toxin MeKTx13-3 (K26A) IC50
4.555 nM
 [72]
 Toxin Info    Toxin MeKTx13-3 (K26N) IC50
5.457 nM
 [72]
 Toxin Info    Toxin MeKTx13-3 (N29A,D33H) IC50
6.164 nM
 [72]
 Toxin Info    Kunitz-type serine protease inhibitor Hg1 IC50
6.2 nM
 [63]
 Toxin Info    Kunitz-type serine protease inhibitor Hg1 IC50
6.2 nM
 [63- 68]
 Toxin Info    Toxin MeKTx13-3 (K6D,D19K) IC50
7.3 nM
 [81]
 Toxin Info    Toxin MeKTx13-3 (G11R,R23A,I28T,D33H) IC50
7.344 nM
 [69]
 Toxin Info    Toxin MeKTx13-3 (F24A) IC50
9.7 nM
 [72]
 Toxin Info    Potassium channel toxin alpha-KTX 12 Sp2 IC50
14.7 nM
 [79]
 Toxin Info    Toxin MeKTx13-3 (F24A,D33H) IC50
20.998 nM
 [72]
 Toxin Info    ScyTx (F2V,R6K,Q9E,D24V) IC50
22 nM
 [84]
 Toxin Info    Potassium channel toxin Sp4 IC50
24.73 nM
 [85]
 Toxin Info    Potassium channel toxin Sp4 IC50
24.73 nM
 [85]
 Toxin Info    Toxin KTx8 IC50
26.4 nM
 [86]
 Toxin Info    Toxin MeKTx13-3 (R23A,D33H) IC50
27.218 nM
 [72]
 Toxin Info    Leiurotoxin I-like toxin P05 (R6K,Q9E,R13A,E27K) IC50
47 nM
 [84]
 Toxin Info    Kunitz-type serine protease inhibitor IX IC50
120 nM
 [87], [88], [89]
 Toxin Info    Kunitz-type serine protease inhibitor BmKTT-1 IC50
129.7 nM
 [63]
 Toxin Info    Kunitz-type serine protease inhibitor BmKTT-1 IC50
129.7 nM
 [63]
 Toxin Info    Potassium channel toxin alpha-KTx 26.3 IC50
150 nM
 [90]
 Toxin Info    Potassium channel toxin alpha-KTx 26.1 IC50
150 nM
 [91], [92]
 Toxin Info    Potassium channel toxin alpha-KTx 26.1 IC50
150 nM
 [91]
 Toxin Info    Toxin MeKTx13-3 (R23A) IC50
175.7 nM
 [72]
 Toxin Info    MgTX (K28A) IC50
216 nM
 [93]
 Toxin Info    Leiurotoxin I-like toxin P05 (R6K,Q9E,K20A,E27K) IC50
222 nM
 [84]
 Toxin Info    ScyTx (F2V,R6A,Q9E,D24V) IC50
246 nM
 [84]
 Toxin Info    Potassium channel toxin alpha-KTx 8.2 IC50
269 - 467 nM
 [61- 98]
 Toxin Info    Delta-KTx 1.1 (R57A) IC50
305 nM
 [63]
 Toxin Info    Leiurotoxin I-like toxin P05 (R6K,Q9E,E27K,K30A) IC50
308 nM
 [84]
 Toxin Info    Delta-KTx 1.1 IC50
360 nM
 [63]
 Toxin Info    Kunitz-type serine protease inhibitor BmKTT-2 IC50
371.3 nM
 [63]
 Toxin Info    Kunitz-type serine protease inhibitor BmKTT-2 IC50
371.3 nM
 [66], [63]
 Toxin Info    Leiurotoxin I-like toxin P05 (R6K,Q9E,E27A) IC50
448 nM
 [84]
 Toxin Info    Delta-KTx 1.1_A61F_K63A IC50
457 nM
 [63]
 Toxin Info    Delta-KTx 1.1 (R57A,K56A,A57R) IC50
582 nM
 [63]
 Toxin Info    Scorpine-like peptide Ev37 IC50
950 nM
 [31]
 Toxin Info    SdPII (C51A) IC50
1 μM
 [66]
 Toxin Info    Kunitz-type serine protease inhibitor LmKTT-1c IC50
1 μM
 [63]
 Toxin Info    Kunitz-type serine protease inhibitor LmKTT-1a IC50
1 μM
 [63]
 Toxin Info    Kunitz-type serine protease inhibitor LmKTT-1b IC50
1 μM
 [63]
 Toxin Info    Leiurotoxin I-like toxin P05 (R6K,Q9E,K25A,E27K) IC50
1.2 μM
 [84]
 Toxin Info    Kunitz-type serine protease inhibitor LmKTT-1a IC50
1.58 μM
 [63- 67]
 Toxin Info    Potassium channel toxin KTx1 IC50
1.7 μM
 [99]
 Toxin Info    Potassium channel toxin KTx1 IC50
1.7 μM
 [99]
 Toxin Info    Kunitz-type serine protease inhibitor homolog dendrotoxin I IC50
4.533 μM
 [100]
 Toxin Info    Leiurotoxin I-like toxin P05 (R6K,Q9E,K20V,K25A,E27K) IC50
8.58 μM
 [84]
 Toxin Info    Beta-defensin 1 IC50
13.2 μM
 [101]
References
Ref 1 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 2 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 3 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 4 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 5 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 6 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 7 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 8 Cobatoxin 1 from Centruroides noxius scorpion venom: chemical synthesis, three-dimensional structure in solution, pharmacology and docking on K+ channels. Biochem J. 2004 Jan 1;377(Pt 1):37-49. doi: 10.1042/BJ20030977.
Ref 9 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 10 Letter: An anti-inflammatory peptide from bee venom. Nature. 1973 Sep 21;245(5421):163-4. doi: 10.1038/245163a0.
Ref 11 Mast cell degranulating peptide: a multi-functional neurotoxin. J Pharm Pharmacol. 1990 Jul;42(7):457-61. doi: 10.1111/j.2042-7158.1990.tb06595.x.
Ref 12 The 'functional' dyad of scorpion toxin Pi1 is not itself a prerequisite for toxin binding to the voltage-gated Kv1.2 potassium channels. Biochem J. 2004 Jan 1;377(Pt 1):25-36. doi: 10.1042/BJ20030115.
Ref 13 Evolution of separate predation- and defence-evoked venoms in carnivorous cone snails. Nat Commun. 2014 Mar 24;5:3521. doi: 10.1038/ncomms4521.
Ref 14 Definition of the M-conotoxin superfamily: characterization of novel peptides from molluscivorous Conus venoms. Biochemistry. 2005 Jun 7;44(22):8176-86. doi: 10.1021/bi047541b.
Ref 15 The amino acid sequences of homologous hydroxyproline-containing myotoxins from the marine snail Conus geographus venom. FEBS Lett. 1983 May 8;155(2):277-80. doi: 10.1016/0014-5793(82)80620-0.
Ref 16 Disulfide pairings in geographutoxin I, a peptide neurotoxin from Conus geographus. FEBS Lett. 1990 May 7;264(1):29-32. doi: 10.1016/0014-5793(90)80756-9.
Ref 17 Action of derivatives of mu-conotoxin GIIIA on sodium channels. Single amino acid substitutions in the toxin separately affect association and dissociation rates. Biochemistry. 1992 Sep 8;31(35):8229-38. doi: 10.1021/bi00150a016.
Ref 18 Distinction among neuronal subtypes of voltage-activated sodium channels by mu-conotoxin PIIIA. J Neurosci. 2000 Jan 1;20(1):76-80. doi: 10.1523/JNEUROSCI.20-01-00076.2000.
Ref 19 Role of hydroxyprolines in the in vitro oxidative folding and biological activity of conotoxins. Biochemistry. 2008 Feb 12;47(6):1741-51. doi: 10.1021/bi701934m. Epub 2008 Jan 12.
Ref 20 Pruning nature: Biodiversity-derived discovery of novel sodium channel blocking conotoxins from Conus bullatus. Toxicon. 2009 Jan;53(1):90-8. doi: 10.1016/j.toxicon.2008.10.017. Epub 2008 Nov 20.
Ref 21 -Conotoxins that differentially block sodium channels NaV1.1 through 1.8 identify those responsible for action potentials in sciatic nerve. Proc Natl Acad Sci U S A. 2011 Jun 21;108(25):10302-7. doi: 10.1073/pnas.1107027108. Epub 2011 Jun 7.
Ref 22 NMR Structure of -Conotoxin GIIIC: Leucine 18 Induces Local Repacking of the N-Terminus Resulting in Reduced Na(V) Channel Potency. Molecules. 2018 Oct 22;23(10):2715. doi: 10.3390/molecules23102715.
Ref 23 Solution structure of mu-conotoxin GIIIA analysed by 2D-NMR and distance geometry calculations. FEBS Lett. 1991 Jan 28;278(2):160-6. doi: 10.1016/0014-5793(91)80107-e.
Ref 24 Tertiary structure of conotoxin GIIIA in aqueous solution. Biochemistry. 1991 Jul 16;30(28):6908-16. doi: 10.1021/bi00242a014.
Ref 25 Structure-activity relationships of mu-conotoxin GIIIA: structure determination of active and inactive sodium channel blocker peptides by NMR and simulated annealing calculations. Biochemistry. 1992 Dec 22;31(50):12577-84. doi: 10.1021/bi00165a006.
Ref 26 mu-Conotoxin PIIIA, a new peptide for discriminating among tetrodotoxin-sensitive Na channel subtypes. J Neurosci. 1998 Jun 15;18(12):4473-81. doi: 10.1523/JNEUROSCI.18-12-04473.1998.
Ref 27 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 28 Co-expression of Na(V) subunits alters the kinetics of inhibition of voltage-gated sodium channels by pore-blocking -conotoxins. Br J Pharmacol. 2013 Apr;168(7):1597-610. doi: 10.1111/bph.12051.
Ref 29 Structurally diverse -conotoxin PIIIA isomers block sodium channel NaV 1.4. Angew Chem Int Ed Engl. 2012 Apr 23;51(17):4058-61. doi: 10.1002/anie.201107011. Epub 2012 Mar 12.
Ref 30 Solution structure of mu-conotoxin PIIIA, a preferential inhibitor of persistent tetrodotoxin-sensitive sodium channels. J Biol Chem. 2002 Jul 26;277(30):27247-55. doi: 10.1074/jbc.M201611200. Epub 2002 May 2.
Ref 31 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 32 A novel conotoxin from Conus striatus, mu-SIIIA, selectively blocking rat tetrodotoxin-resistant sodium channels. Toxicon. 2006 Jan;47(1):122-32. doi: 10.1016/j.toxicon.2005.10.008. Epub 2005 Dec 1.
Ref 33 Novel conotoxins from Conus striatus and Conus kinoshitai selectively block TTX-resistant sodium channels. Biochemistry. 2005 May 17;44(19):7259-65. doi: 10.1021/bi0473408.
Ref 34 A Lewis Acid-Controlled Enantiodivergent Epoxidation of Aldehydes. ACS Catal. 2023 Oct 6;13(19):13117-13126. doi: 10.1021/acscatal.3c03929. Epub 2023 Sep 25.
Ref 35 Retraction of "Effect of Fluoride Layer Growth on the Deposition Rate under Different Microchannel Structures". ACS Omega. 2024 Feb 28;9(10):12291. doi: 10.1021/acsomega.4c01652. eCollection 2024 Mar 12.
Ref 36 Retraction of "Assessing the Weathering Performance and Functionality of Nanoparticle-Enhanced High-Pressure Laminates for Building Facade Applications". ACS Omega. 2024 Mar 1;9(10):12290. doi: 10.1021/acsomega.4c01411. eCollection 2024 Mar 12.
Ref 37 Correction to "Digoxin-Mediated Inhibition of Potential Hypoxia-Related Angiogenic Repair in Modulated Electro-Hyperthermia (mEHT)-Treated Murine Triple-Negative Breast Cancer Model". ACS Pharmacol Transl Sci. 2024 Feb 28;7(3):904. doi: 10.1021/acsptsci.4c00094. eCollection 2024 Mar 8.
Ref 38 Correction to 1,2,3-Triazole Tethered Hybrid Capsaicinoids as Antiproliferative Agents Active against Lung Cancer Cells (A549). ACS Omega. 2024 Feb 20;9(9):11026. doi: 10.1021/acsomega.4c00155. eCollection 2024 Mar 5.
Ref 39 Correction to "Dual-Surfactant-Capped Ag Nanoparticles as a Highly Selective and Sensitive Colorimetric Sensor for Citrate Detection". ACS Omega. 2024 Feb 22;9(9):11025. doi: 10.1021/acsomega.3c09929. eCollection 2024 Mar 5.
Ref 40 Colloidal Stability of PFSA-Ionomer Dispersions. Part I. Single-Ion Electrostatic Interaction Potential Energies. Langmuir. 2024 Apr 2;40(13):6654-6665. doi: 10.1021/acs.langmuir.3c03903. Epub 2024 Mar 8.
Ref 41 Correction to "Searching for the Rules of Electrochemical Nitrogen Fixation". ACS Catal. 2024 Feb 14;14(5):3169-3170. doi: 10.1021/acscatal.4c00448. eCollection 2024 Mar 1.
Ref 42 Correction to "Quantification and Mapping of Alkylation in the Human Genome Reveal Single Nucleotide Resolution Precursors of Mutational Signatures". ACS Cent Sci. 2024 Jan 25;10(2):487. doi: 10.1021/acscentsci.3c01597. eCollection 2024 Feb 28.
Ref 43 Correction to "Characterization of Proteins Extracted from Ulva sp., Padina sp., and Laurencia sp. Macroalgae Using Green Technology: Effect of In Vitro Digestion on Antioxidant and ACE-I Inhibitory Activity". ACS Omega. 2024 Feb 16;9(8):9848. doi: 10.1021/acsomega.4c00407. eCollection 2024 Feb 27.
Ref 44 Erratum: Antibacterial Efficacy of ZnO/Bentonite (Clay) Nanocomposites against Multidrug-Resistant Escherichia coli. ACS Omega. 2024 Feb 15;9(8):9847. doi: 10.1021/acsomega.4c00630. eCollection 2024 Feb 27.
Ref 45 Low-Cost Nonfused-Ring Electron Acceptors Enabled by Noncovalent Conformational Locks. Acc Chem Res. 2024 Mar 19;57(6):981-991. doi: 10.1021/acs.accounts.3c00813. Epub 2024 Mar 3.
Ref 46 Retraction of "Hydrogenolysis of Polyethylene and Polypropylene into Propane over Cobalt-Based Catalysts". JACS Au. 2024 Feb 7;4(2):865. doi: 10.1021/jacsau.4c00090. eCollection 2024 Feb 26.
Ref 47 Correction to "Comprehensive Study of Preparation of Carboxy Group-Containing Cellulose Fibers from Dry-Lap Kraft Pulps by Catalytic Oxidation with Solid NaOCl". ACS Sustain Chem Eng. 2024 Feb 6;12(7):2921-2923. doi: 10.1021/acssuschemeng.4c00215. eCollection 2024 Feb 19.
Ref 48 Correction to "Dissolution Behavior of Polycyclic Aromatic Hydrocarbons in Heavy Oil in the Presence of Supercritical Cyclohexane". ACS Omega. 2024 Jan 31;9(6):7269. doi: 10.1021/acsomega.4c00064. eCollection 2024 Feb 13.
Ref 49 Retraction of "Fe(3)O(4) Nanoparticles Grown on Cellulose/GO Hydrogels as Advanced Catalytic Materials for the Heterogeneous Fenton-like Reaction". ACS Omega. 2024 Jan 31;9(6):7270. doi: 10.1021/acsomega.4c00561. eCollection 2024 Feb 13.
Ref 50 Correction to "Ligand Chromophore Modification Approach for Predictive Incremental Tuning of Metal-Organic Framework Color". Chem Mater. 2024 Jan 19;36(3):1773. doi: 10.1021/acs.chemmater.3c03160. eCollection 2024 Feb 13.
Ref 51 Correction to "Electrospun Nanofibrous UV Filters with Bidirectional Actuation Properties Based on Salmon Sperm DNA/Silk Fibroin for Biomedical Applications". ACS Omega. 2024 Jan 25;9(5):6025. doi: 10.1021/acsomega.4c00072. eCollection 2024 Feb 6.
Ref 52 Correction to "Iterative Dual-Metal and Energy Transfer Catalysis Enables Stereodivergence in Alkyne Difunctionalization: Carboboration as Case Study". ACS Catal. 2024 Jan 22;14(3):1976. doi: 10.1021/acscatal.4c00200. eCollection 2024 Feb 2.
Ref 53 Correction to "Nanotechnology Impact on Chemical-Enhanced Oil Recovery: A Review and Bibliometric Analysis of Recent Developments". ACS Omega. 2024 Jan 15;9(4):5083. doi: 10.1021/acsomega.3c10450. eCollection 2024 Jan 30.
Ref 54 Neuronally micro-conotoxins from Conus striatus utilize an alpha-helical motif to target mammalian sodium channels. J Biol Chem. 2008 Aug 1;283(31):21621-8. doi: 10.1074/jbc.M802852200. Epub 2008 Jun 3.
Ref 55 N- and C-terminal extensions of -conotoxins increase potency and selectivity for neuronal sodium channels. Biopolymers. 2012;98(2):161-5. doi: 10.1002/bip.22032. Epub 2012 Feb 10.
Ref 56 Structure, dynamics, and selectivity of the sodium channel blocker mu-conotoxin SIIIA. Biochemistry. 2008 Oct 14;47(41):10940-9. doi: 10.1021/bi801010u. Epub 2008 Sep 18.
Ref 57 Novel tarantula toxins for subtypes of voltage-dependent potassium channels in the Kv2 and Kv4 subfamilies. Mol Pharmacol. 2002 Jul;62(1):48-57. doi: 10.1124/mol.62.1.48.
Ref 58 Selective spider toxins reveal a role for the Nav1.1 channel in mechanical pain. Nature. 2016 Jun 23;534(7608):494-9. doi: 10.1038/nature17976. Epub 2016 Jun 6.
Ref 59 A selective Na(V)1.1 activator with potential for treatment of Dravet syndrome epilepsy. Biochem Pharmacol. 2020 Nov;181:113991. doi: 10.1016/j.bcp.2020.113991. Epub 2020 Apr 23.
Ref 60 Selective Na(V)1.1 activation rescues Dravet syndrome mice from seizures and premature death. Proc Natl Acad Sci U S A. 2018 Aug 21;115(34):E8077-E8085. doi: 10.1073/pnas.1804764115. Epub 2018 Aug 3.
Ref 61 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 62 Mouse -Defensin 3, A Defensin Inhibitor of Both Its Endogenous and Exogenous Potassium Channels. Molecules. 2018 Jun 20;23(6):1489. doi: 10.3390/molecules23061489.
Ref 63 Hg1, novel peptide inhibitor specific for Kv1.3 channels from first scorpion Kunitz-type potassium channel toxin family. J Biol Chem. 2012 Apr 20;287(17):13813-21. doi: 10.1074/jbc.M112.343996. Epub 2012 Feb 21.
Ref 64 Recombinant expression and functional characterization of martentoxin: a selective inhibitor for BK channel ( + 4). Toxins (Basel). 2014 Apr 22;6(4):1419-33. doi: 10.3390/toxins6041419.
Ref 65 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 66 Genomic and structural characterization of Kunitz-type peptide LmKTT-1a highlights diversity and evolution of scorpion potassium channel toxins. PLoS One. 2013;8(4):e60201. doi: 10.1371/journal.pone.0060201. Epub 2013 Apr 3.
Ref 67 SdPI, the first functionally characterized Kunitz-type trypsin inhibitor from scorpion venom. PLoS One. 2011;6(11):e27548. doi: 10.1371/journal.pone.0027548. Epub 2011 Nov 8.
Ref 68 Transcriptome analysis of the venom gland of the Mexican scorpion Hadrurus gertschi (Arachnida: Scorpiones). BMC Genomics. 2007 May 16;8:119. doi: 10.1186/1471-2164-8-119.
Ref 69 Structural basis of a potent peptide inhibitor designed for Kv1.3 channel, a therapeutic target of autoimmune disease. J Biol Chem. 2008 Jul 4;283(27):19058-65. doi: 10.1074/jbc.M802054200. Epub 2008 May 14.
Ref 70 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 71 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 72 Unusual binding mode of scorpion toxin BmKTX onto potassium channels relies on its distribution of acidic residues. Biochem Biophys Res Commun. 2014 Apr 25;447(1):70-6. doi: 10.1016/j.bbrc.2014.03.101. Epub 2014 Apr 3.
Ref 73 Development of highly selective Kv1.3-blocking peptides based on the sea anemone peptide ShK. Mar Drugs. 2015 Jan 16;13(1):529-42. doi: 10.3390/md13010529.
Ref 74 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 75 A C-terminally amidated analogue of ShK is a potent and selective blocker of the voltage-gated potassium channel Kv1.3. FEBS Lett. 2012 Nov 16;586(22):3996-4001. doi: 10.1016/j.febslet.2012.09.038. Epub 2012 Oct 9.
Ref 76 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 77 Durable pharmacological responses from the peptide ShK-186, a specific Kv1.3 channel inhibitor that suppresses T cell mediators of autoimmune disease. J Pharmacol Exp Ther. 2012 Sep;342(3):642-53. doi: 10.1124/jpet.112.191890. Epub 2012 May 25.
Ref 78 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 79 Immunosuppressive effects of a novel potassium channel toxin Ktx-Sp2 from Scorpiops Pocoki. Cell Biosci. 2019 Dec 16;9:99. doi: 10.1186/s13578-019-0364-1. eCollection 2019.
Ref 80 N-Terminally extended analogues of the K? channel toxin from Stichodactyla helianthus as potent and selective blockers of the voltage-gated potassium channel Kv1.3. FEBS J. 2015 Jun;282(12):2247-59. doi: 10.1111/febs.13294. Epub 2015 Apr 23.
Ref 81 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 82 Characterization of a new Kv1.3 channel-specific blocker, J123, from the scorpion Buthus martensii Karsch. Peptides. 2008 Sep;29(9):1514-20. doi: 10.1016/j.peptides.2008.04.021. Epub 2008 May 13.
Ref 83 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 84 Protein-protein recognition control by modulating electrostatic interactions. J Proteome Res. 2010 Jun 4;9(6):3118-25. doi: 10.1021/pr100027k.
Ref 85 Cloning, expression and identification of KTX-Sp4, a selective Kv1.3 peptidic blocker from Scorpiops pococki. Cell Biosci. 2017 Nov 6;7:60. doi: 10.1186/s13578-017-0187-x. eCollection 2017.
Ref 86 Molecular cloning and electrophysiological studies on the first K(+) channel toxin (LmKTx8) derived from scorpion Lychas mucronatus. Peptides. 2007 Dec;28(12):2306-12. doi: 10.1016/j.peptides.2007.10.009. Epub 2007 Oct 22.
Ref 87 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 88 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 89 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 90 The Mediterranean scorpion Mesobuthus gibbosus (Scorpiones, Buthidae): transcriptome analysis and organization of the genome encoding chlorotoxin-like peptides. BMC Genomics. 2014 Apr 21;15:295. doi: 10.1186/1471-2164-15-295.
Ref 91 Cloning and characterization of BmK86, a novel K+ -channel blocker from scorpion venom. Biochem Biophys Res Commun. 2007 Sep 7;360(4):728-34. doi: 10.1016/j.bbrc.2007.06.108. Epub 2007 Jul 2.
Ref 92 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 93 Recombinant expression of margatoxin and agitoxin-2 in Pichia pastoris: an efficient method for production of KV1.3 channel blockers. PLoS One. 2012;7(12):e52965. doi: 10.1371/journal.pone.0052965. Epub 2012 Dec 26.
Ref 94 Genomic organization of three neurotoxins active on small conductance Ca2+-activated potassium channels from the scorpion Buthus martensi Karsch. FEBS Lett. 1999 Jun 11;452(3):360-4. doi: 10.1016/s0014-5793(99)00651-1.
Ref 95 Scorpion Toxin, BmP01, Induces Pain by Targeting TRPV1 Channel. Toxins (Basel). 2015 Sep 14;7(9):3671-87. doi: 10.3390/toxins7093671.
Ref 96 Characterization of four toxins from Buthus martensi scorpion venom, which act on apamin-sensitive Ca2+-activated K+ channels. Eur J Biochem. 1997 Apr 15;245(2):457-64. doi: 10.1111/j.1432-1033.1997.00457.x.
Ref 97 Solution structure of BmP01 from the venom of scorpion Buthus martensii Karsch. Biochem Biophys Res Commun. 2000 Oct 5;276(3):1148-54. doi: 10.1006/bbrc.2000.3435.
Ref 98 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 99 ImKTx1, a new Kv1.3 channel blocker with a unique primary structure. J Biochem Mol Toxicol. 2011 Jul-Aug;25(4):244-51. doi: 10.1002/jbt.20382. Epub 2011 Feb 9.
Ref 100 Both N- and C-terminal regions contribute to the assembly and functional expression of homo- and heteromultimeric voltage-gated K+ channels. J Neurosci. 1994 Mar;14(3 Pt 1):1385-93. doi: 10.1523/JNEUROSCI.14-03-01385.1994.
Ref 101 Human beta-defensin 1, a new animal toxin-like blocker of potassium channel. Toxicon. 2016 Apr;113:1-6. doi: 10.1016/j.toxicon.2016.02.007. Epub 2016 Feb 5.
Ref 102 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 103 Engineering a peptide inhibitor towards the KCNQ1/KCNE1 potassium channel (IKs). Peptides. 2015 Sep;71:77-83. doi: 10.1016/j.peptides.2015.07.002. Epub 2015 Jul 15.
Ref 104 Mechanisms Underlying the Inhibition of KV1.3 Channel by Scorpion Toxin ImKTX58. Mol Pharmacol. 2022 Sep;102(3):150-160. doi: 10.1124/molpharm.121.000480. Epub 2022 Jun 28.
Ref 105 Cloning and identification of a new multifunctional Ascaris-type peptide from the hemolymph of Buthus martensii Karsch. Toxicon. 2020 Sep;184:167-174. doi: 10.1016/j.toxicon.2020.06.008. Epub 2020 Jun 18.
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.