General Information of This Target
Target ID
BTDT00050
Target Name
Potassium voltage-gated channel subfamily A member 3 (Kcna3)
Target Bioclass
Transporter and channel
Uniprot ID
P15384
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
29731
Synonym
RCK3; RGK5; Voltage-gated potassium channel subunit Kv1.3; Voltage-gated potassium channel subunit Kv3
Sequence
MTVVPGDHLLEPEAAGGGGGDPPQGGCVSGGGCDRYEPLPPALPAAGEQDCCGERVVINI
SGLRFETQLKTLCQFPETLLGDPKRRMRYFDPLRNEYFFDRNRPSFDAILYYYQSGGRIR
RPVNVPIDIFSEEIRFYQLGEEAMEKFREDEGFLREEERPLPRRDFQRQVWLLFEYPESS
GPARGIAIVSVLVILISIVIFCLETLPEFRDEKDYPASPSQDVFEAANNSTSGASSGASS
FSDPFFVVETLCIIWFSFELLVRFFACPSKATFSRNIMNLIDIVAIIPYFITLGTELAER
QGNGQQAMSLAILRVIRLVRVFRIFKLSRHSKGLQILGQTLKASMRELGLLIFFLFIGVI
LFSSAVYFAEADDPSSGFNSIPDAFWWAVVTMTTVGYGDMHPVTIGGKIVGSLCAIAGVL
TIALPVPVIVSNFNYFYHRETEGEEQAQYMHVGSCQHLSSSAEELRKARSNSTLSKSEYM
VIEEGGMNHSAFPQTPFKTGNSTATCTTNNNPNSCVNIKKIFTDV

    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
10116
        Click to Show/Hide the Complete Species Lineage
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    Potassium channel toxin Bgk (K25[Dab]) . . [1]
 Toxin Info    Potassium channel toxin Bgk (K25[Dap]) . . [1]
 Toxin Info    Potassium channel toxin Bgk (K25[Nle]) . . [1]
 Toxin Info    Potassium channel toxin Bgk (K25[Orn]) Dissociation constant
111 nM
[1]
 Toxin Info    Potassium channel toxin Bgk (K25A,Y26A) Dissociation constant
12 μM
[1]
 Toxin Info    Potassium channel toxin alpha-KTx 1.1 Inhibition constant
0.19 nM
[2- 20]
 Toxin Info    Potassium channel toxin alpha-KTx 3.4 Inhibition constant
1.7 nM
[7- 21]
 Toxin Info    Potassium channel toxin alpha-KTx 3.2 Inhibition constant
4 nM
[7- 23]
 Toxin Info    MTX (G33A) Inhibition rate . [24]
 Toxin Info    MTX (K15Q) Inhibition rate . [24]
 Toxin Info    MTX (P12A,P20A) Inhibition rate . [25]
 Toxin Info    Kappa-conotoxin SrXIA Inhibition rate . [26], [27]
 Toxin Info    Kunitz-type serine protease inhibitor homolog alpha-dendrotoxin Inhibition rate . [28]
 Toxin Info    Potassium channel toxin TsTXK-beta Inhibition rate . [29]
 Toxin Info    Mu-theraphotoxin-Pspp1 Inhibition rate . [30]
 Toxin Info    Potassium channel toxin alpha-KTx 6.4 Inhibition rate . [31]
 Toxin Info    Neurotoxin lambda-MeuTx Inhibition rate . [32]
 Toxin Info    MTX (S2V,C3I,T4G,G5Q,S6R,K7C,D8T,C9G,Y10S,A11K,P12D,R14Y,K15A,Q16P,T17C,G18R,C19K,P20Q,N21T,A22G,K23C,C24P,I25N,N26A,S28C,C29I,K30N,C31K,Y32S,G33C,C34K) Inhibition rate . [33]
 Toxin Info    Potassium channel toxin alpha-KTx 3.6 Inhibition rate
>0 %
[12- 37]
 Toxin Info    Potassium channel toxin Bgk (Y26A) Inhibition rate
4 %
[1]
 Toxin Info    Calcium channel toxin-like peptide-1 Inhibition rate
9 %
[32]
 Toxin Info    Potassium channel toxin Bgk (N19A) Inhibition rate
10 %
[1]
 Toxin Info    Potassium channel toxin Bgk (S23A) Inhibition rate
10 %
[1]
 Toxin Info    Potassium channel toxin MeuTXKalpha3 Inhibition rate
12 %
[38]
 Toxin Info    Kunitz-type conkunitzin-S1 Inhibition rate
15 %
[39], [40], [41]
 Toxin Info    Potassium channel toxin Bgk (K25A) Inhibition rate
24 %
[1]
 Toxin Info    Potassium channel toxin Bgk (F6A) Inhibition rate
25 %
[1]
 Toxin Info    Potassium channel toxin Bgk (N29A) Inhibition rate
25 %
[1]
 Toxin Info    Potassium channel toxin Bgk (Q24A) Inhibition rate
27 %
[1]
 Toxin Info    Kappa-actitoxin-Ael2e Inhibition rate
27 %
[42]
 Toxin Info    Potassium channel toxin Bgk (K7A) Inhibition rate
35 %
[1]
 Toxin Info    Potassium channel toxin alpha-KTx (N30P) Inhibition rate
42 %
[38]
 Toxin Info    Potassium channel toxin Bgk (H13A) Inhibition rate
42 %
[1]
 Toxin Info    Potassium channel toxin Bgk (L17A) Inhibition rate
49 %
[1]
 Toxin Info    Potassium channel toxin Bgk (L36A) Inhibition rate
52 %
[1]
 Toxin Info    Potassium channel toxin Bgk (R27A) Inhibition rate
55 %
[1]
 Toxin Info    Potassium channel toxin Bgk (K32A) Inhibition rate
58 %
[1]
 Toxin Info    Potassium channel toxin Bgk (T22A) Inhibition rate
58 %
[1]
 Toxin Info    Potassium channel toxin Bgk (R21A) Inhibition rate
60 %
[1]
 Toxin Info    Potassium channel toxin Bgk (K15A) Inhibition rate
63 %
[1]
 Toxin Info    Potassium channel toxin Bgk (R12A) Inhibition rate
63 %
[1]
 Toxin Info    Potassium channel toxin Bgk (T33A) Inhibition rate
65 %
[1]
 Toxin Info    Potassium channel toxin Bgk (T9A) Inhibition rate
65 %
[1]
 Toxin Info    Potassium channel toxin Bgk (R3A) Inhibition rate
68 %
[1]
 Toxin Info    Potassium channel toxin Bgk (S16A) Inhibition rate
75 %
[1]
 Toxin Info    Potassium channel toxin Bgk (E8A) Inhibition rate
77 %
[1]
 Toxin Info    Potassium channel toxin Bgk (W5A) Inhibition rate
85 %
[1]
 Toxin Info    Potassium channel toxin alpha-KTx 4.1 Inhibition rate
85 %
[43]
 Toxin Info    Potassium channel toxin Bgk (V1A) Inhibition rate
87 %
[1]
 Toxin Info    Potassium channel toxin Bgk (E35A) Inhibition rate
89 %
[1]
 Toxin Info    Potassium channel toxin alpha-KTx 6.3 IC50
0.012 nM
[44- 51]
 Toxin Info    Potassium channel toxin alpha-KTx 12.2 IC50
0.55 nM
[52], [53]
 Toxin Info    Potassium channel toxin alpha-KTx 12.1 IC50
0.55 nM
[43- 62]
 Toxin Info    MgTX IC50
0.825 nM
[63]
 Toxin Info    Potassium channel toxin alpha-KTx 3.12 IC50
1.1 nM
[64]
 Toxin Info    Potassium channel toxin alpha-KTx 1.5 IC50
1.5 nM
[35- 86]
 Toxin Info    Potassium channel toxin alpha-KTx 1.6 IC50
1.6 nM
[35- 87]
 Toxin Info    Potassium channel toxin alpha-KTx 6.15 IC50
2 nM
[88]
 Toxin Info    Potassium channel toxin alpha-KTx 6.15 IC50
2 nM
[88]
 Toxin Info    Potassium channel toxin alpha-KTx 9.1 IC50
7 nM
[89], [90], [91], [92]
 Toxin Info    Potassium channel toxin alpha-KTx 9.5 IC50
15 nM
[93]
 Toxin Info    Potassium channel toxin alpha-KTx 9.2 IC50
85.4 nM
[89- 94]
 Toxin Info    Potassium channel toxin alpha-KTx 6.2 IC50
180 nM
[9- 100]
 Toxin Info    Potassium channel toxin alpha-KTx 8.2 IC50
269 - 467 nM
[90- 103]
 Toxin Info    MTX (C19[Abu],G34[Abu]) IC50
443 nM
[104]
 Toxin Info    Kappa-conotoxin ViTx IC50
2.09 μM
[105], [106]
 Toxin Info    Mesomartoxin IC50
12.5 μM
[107]
 Toxin Info    Mesomartoxin IC50
12.5 μM
[107]
References
Ref 1 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 2 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 3 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 4 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 5 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 6 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 7 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 8 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 9 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 10 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 11 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 12 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 13 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 14 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 15 Molecular structure of charybdotoxin: retraction. Science. 1991 May 3;252(5006):631. doi: 10.1126/science.252.5006.631.b.
Ref 16 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 17 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 18 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 19 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 20 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 21 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 22 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 23 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 24 Maurotoxin versus Pi1/HsTx1 scorpion toxins. Toward new insights in the understanding of their distinct disulfide bridge patterns. J Biol Chem. 2000 Dec 15;275(50):39394-402. doi: 10.1074/jbc.M006810200.
Ref 25 Disulfide bridge reorganization induced by proline mutations in maurotoxin. FEBS Lett. 2001 Feb 2;489(2-3):202-7. doi: 10.1016/s0014-5793(00)02433-9.
Ref 26 I-conotoxins in vermivorous species of the West Atlantic: peptide sr11a from Conus spurius. Peptides. 2007 Jan;28(1):18-23. doi: 10.1016/j.peptides.2006.08.024. Epub 2006 Dec 12.
Ref 27 Peptide sr11a from Conus spurius is a novel peptide blocker for Kv1 potassium channels. Peptides. 2010 Jul;31(7):1287-91. doi: 10.1016/j.peptides.2010.04.007. Epub 2010 Apr 18.
Ref 28 Identification of amino acid residues involved in dendrotoxin block of rat voltage-dependent potassium channels. Mol Pharmacol. 1991 Oct;40(4):572-6.
Ref 29 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 30 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 31 Synthesis and characterization of Pi4, a scorpion toxin from Pandinus imperator that acts on K+ channels. Eur J Biochem. 2003 Sep;270(17):3583-92. doi: 10.1046/j.1432-1033.2003.03743.x.
Ref 32 Functional evolution of scorpion venom peptides with an inhibitor cystine knot fold. Biosci Rep. 2013 Jun 27;33(3):e00047. doi: 10.1042/BSR20130052.
Ref 33 Synthesis, 3-D structure, and pharmacology of a reticulated chimeric peptide derived from maurotoxin and Tsk scorpion toxins. Biochem Biophys Res Commun. 2002 Mar 1;291(3):640-8. doi: 10.1006/bbrc.2002.6496.
Ref 34 Genomic organization of three novel toxins from the scorpion Buthus martensi Karsch that are active on potassium channels. Biochem J. 2000 Mar 15;346 Pt 3(Pt 3):805-9.
Ref 35 Purification, characterization, and synthesis of three novel toxins from the Chinese scorpion Buthus martensi, which act on K+ channels. Biochemistry. 1997 Nov 4;36(44):13473-82. doi: 10.1021/bi971044w.
Ref 36 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 37 Solution structure of BmKTX, a K+ blocker toxin from the Chinese scorpion Buthus Martensi. Proteins. 2000 Jan 1;38(1):70-8. doi: 10.1002/(sici)1097-0134(20000101)38:1<70::aid-prot8>3.0.co;2-5.
Ref 38 A single-point mutation enhances dual functionality of a scorpion toxin. Comp Biochem Physiol C Toxicol Pharmacol. 2016 Jan;179:72-8. doi: 10.1016/j.cbpc.2015.09.002. Epub 2015 Sep 7.
Ref 39 Production of recombinant Conkunitzin-S1 in Escherichia coli. Protein Expr Purif. 2006 Jun;47(2):640-4. doi: 10.1016/j.pep.2006.01.019. Epub 2006 Feb 20.
Ref 40 Conkunitzin-S1 is the first member of a new Kunitz-type neurotoxin family. Structural and functional characterization. J Biol Chem. 2005 Jun 24;280(25):23766-70. doi: 10.1074/jbc.C500064200. Epub 2005 Apr 15.
Ref 41 Structure of conkunitzin-S1, a neurotoxin and Kunitz-fold disulfide variant from cone snail. Acta Crystallogr D Biol Crystallogr. 2006 Sep;62(Pt 9):980-90. doi: 10.1107/S0907444906021123. Epub 2006 Aug 19.
Ref 42 APETx4, a Novel Sea Anemone Toxin and a Modulator of the Cancer-Relevant Potassium Channel K(V)10.1. Mar Drugs. 2017 Sep 13;15(9):287. doi: 10.3390/md15090287.
Ref 43 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 44 A four-disulphide-bridged toxin, with high affinity towards voltage-gated K+ channels, isolated from Heterometrus spinnifer (Scorpionidae) venom. Biochem J. 1997 Nov 15;328 ( Pt 1)(Pt 1):321-7. doi: 10.1042/bj3280321.
Ref 45 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 46 Free energy simulations of binding of HsTx1 toxin to Kv1 potassium channels: the basis of Kv1.3/Kv1.1 selectivity. J Phys Chem B. 2014 Jan 23;118(3):707-16. doi: 10.1021/jp410950h. Epub 2014 Jan 13.
Ref 47 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 48 Prolonged immunomodulation in inflammatory arthritis using the selective Kv1.3 channel blocker HsTX1[R14A] and its PEGylated analog. Clin Immunol. 2017 Jul;180:45-57. doi: 10.1016/j.clim.2017.03.014. Epub 2017 Apr 4.
Ref 49 Structural and functional consequences of the presence of a fourth disulfide bridge in the scorpion short toxins: solution structure of the potassium channel inhibitor HsTX1. Protein Sci. 1999 Dec;8(12):2672-85. doi: 10.1110/ps.8.12.2672.
Ref 50 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 51 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 52 Disulfide bridges and blockage of Shaker B K(+)-channels by another butantoxin peptide purified from the Argentinean scorpion Tityus trivittatus. Toxicon. 2003 Feb;41(2):173-9. doi: 10.1016/s0041-0101(02)00247-7.
Ref 53 NMR solution structure of butantoxin. Arch Biochem Biophys. 2000 Jul 1;379(1):18-27. doi: 10.1006/abbi.2000.1858.
Ref 54 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 55 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 56 TsTX-IV, a short chain four-disulfide-bridged neurotoxin from Tityus serrulatus venom which acts on Ca2+-activated K+ channels. Toxicon. 1999 Apr;37(4):651-60. doi: 10.1016/s0041-0101(98)00206-2.
Ref 57 Covalent structure and some pharmacological features of native and cleaved alpha-KTx12-1, a four disulfide-bridged toxin from Tityus serrulatus venom. J Pept Sci. 2003 Feb;9(2):132-40. doi: 10.1002/psc.440.
Ref 58 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 59 Tityus serrulatus venom and toxins Ts1, Ts2 and Ts6 induce macrophage activation and production of immune mediators. Toxicon. 2011 Jun;57(7-8):1101-8. doi: 10.1016/j.toxicon.2011.04.017. Epub 2011 Apr 29.
Ref 60 Ts6 and Ts2 from Tityus serrulatus venom induce inflammation by mechanisms dependent on lipid mediators and cytokine production. Toxicon. 2013 Jan;61:1-10. doi: 10.1016/j.toxicon.2012.10.002. Epub 2012 Oct 22.
Ref 61 Probing the pH-dependent structural features of alpha-KTx12.1, a potassium channel blocker from the scorpion Tityus serrulatus. Protein Sci. 2005 Apr;14(4):1025-38. doi: 10.1110/ps.041131205.
Ref 62 Increasing the molecular contacts between maurotoxin and Kv1.2 channel augments ligand affinity. Proteins. 2005 Aug 15;60(3):401-11. doi: 10.1002/prot.20509.
Ref 63 Olfactory bulb-targeted quantum dot (QD) bioconjugate and Kv1.3 blocking peptide improve metabolic health in obese male mice. J Neurochem. 2021 Jun;157(6):1876-1896. doi: 10.1111/jnc.15200. Epub 2020 Oct 20.
Ref 64 A new Kaliotoxin selective towards Kv1.3 and Kv1.2 but not Kv1.1 channels expressed in oocytes. Biochem Biophys Res Commun. 2008 Nov 21;376(3):525-30. doi: 10.1016/j.bbrc.2008.09.033. Epub 2008 Sep 18.
Ref 65 Modelling Alzheimer's disease in a dish: dissecting amyloid- metabolism in human neurons. Neuronal Signal. 2024 Jan 11;8(1):NS20230020. doi: 10.1042/NS20230020. eCollection 2024 Jan.
Ref 66 A commentary on the paper, 'Development and validation of a novel automatable assay for cholesterol efflux capacity'. Biosci Rep. 2023 Jun 28;43(6):BSR20230124. doi: 10.1042/BSR20230124.
Ref 67 Retracted: Chen, Y, Zhang, W, Kadier, A, Zhang, H, Yao, X. MicroRNA-769-5p suppresses cell growth and migration via targeting NUSAP1 in bladder cancer. J Clin Lab Anal. 2020; 34:e23193. J Clin Lab Anal. 2023 Apr;37(8):e24893. doi: 10.1002/jcla.24893. Epub 2023 May 14.
Ref 68 New mechanisms for the kidney-protective effect of alkali in chronic kidney disease. Clin Sci (Lond). 2022 Oct 28;136(20):1433-1437. doi: 10.1042/CS20220395.
Ref 69 ANGPTL1, Foxo3a-Sox2, and colorectal cancer metastasis. Clin Sci (Lond). 2022 Sep 30;136(18):1367-1370. doi: 10.1042/CS20220394.
Ref 70 Microglia-Mediated Neuroinflammation: A Potential Target for the Treatment of Cardiovascular Diseases. J Inflamm Res. 2022 May 25;15:3083-3094. doi: 10.2147/JIR.S350109. eCollection 2022.
Ref 71 Angiotensin receptors - affinitiy and beyond. Clin Sci (Lond). 2022 May 27;136(10):799-802. doi: 10.1042/CS20220024.
Ref 72 Utility of preclinical models of altered maternal nutrition to support the developmental origins of health and disease hypothesis. Clin Sci (Lond). 2022 May 27;136(10):711-714. doi: 10.1042/CS20211175.
Ref 73 SARS-CoV-2 spike protein causes cardiovascular disease independent of viral infection. Clin Sci (Lond). 2022 Mar 31;136(6):431-434. doi: 10.1042/CS20220028.
Ref 74 Microbiota transplantation in portal hypertension: promises and pitfalls. Clin Sci (Lond). 2022 Mar 31;136(6):425-429. doi: 10.1042/CS20220029.
Ref 75 Paradoxical effects of osteoprotegerin on vascular function: inhibiting inflammation while promoting oxidative stress?. Clin Sci (Lond). 2022 Mar 18;136(5):379-382. doi: 10.1042/CS20211096.
Ref 76 MicroRNAs as messengers of liver diseases: has the message finally been decrypted?. Clin Sci (Lond). 2022 Mar 18;136(5):323-328. doi: 10.1042/CS20211177.
Ref 77 Commentary on: Xbp1s-Ddit3, DNA damage and pulmonary hypertension. Clin Sci (Lond). 2022 Jan 14;136(1):163-166. doi: 10.1042/CS20211095.
Ref 78 A commentary on the paper: 'Evaluation of spice and herb as phytoderived selective modulators of human retinaldehyde dehydrogenases using a simple in vitro method'. Biosci Rep. 2022 Jan 28;42(1):BSR20211522. doi: 10.1042/BSR20211522.
Ref 79 Countering the classical renin-angiotensin system. Clin Sci (Lond). 2021 Dec 10;135(23):2619-2623. doi: 10.1042/CS20211043.
Ref 80 Commentary on: Screening of immunosuppressive cells from colorectal adenocarcinoma and identification of prognostic markers. Biosci Rep. 2021 Dec 22;41(12):BSR20211096. doi: 10.1042/BSR20211096.
Ref 81 Double agent indole-3-acetic acid: mechanistic analysis of indole-3-acetaldehyde dehydrogenase AldA that synthesizes IAA, an auxin that aids bacterial virulence. Biosci Rep. 2021 Aug 27;41(8):BSR20210598. doi: 10.1042/BSR20210598.
Ref 82 Targeting the 'garbage-bin' to fight cancer: HDAC6 inhibitor WT161 has an anti-tumor effect on osteosarcoma and synergistically interacts with 5-FU. Biosci Rep. 2021 Aug 27;41(8):BSR20210952. doi: 10.1042/BSR20210952.
Ref 83 Soluble (pro)renin receptor: a novel ligand for angiotensin II type 1 receptor?. Clin Sci (Lond). 2021 Jul 16;135(13):1627-1630. doi: 10.1042/CS20210227.
Ref 84 Promyelocytic leukemia protein: an atherosclerosis suppressor protein?. Clin Sci (Lond). 2021 Jul 16;135(13):1557-1561. doi: 10.1042/CS20210314.
Ref 85 Solution structure of two new toxins from the venom of the Chinese scorpion Buthus martensi Karsch blockers of potassium channels. Biochemistry. 1998 Sep 8;37(36):12412-8. doi: 10.1021/bi9809371.
Ref 86 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 87 Molecular cloning and genomic organization of a K(+) channel toxin from the Chinese scorpion Buthus martensii Karsch. Toxicon. 2001 Feb-Mar;39(2-3):407-10. doi: 10.1016/s0041-0101(00)00130-6.
Ref 88 Hemitoxin, the first potassium channel toxin from the venom of the Iranian scorpion Hemiscorpius lepturus. FEBS J. 2008 Sep;275(18):4641-50. doi: 10.1111/j.1742-4658.2008.06607.x. Epub 2008 Aug 11.
Ref 89 Molecular cloning and sequencing of two 'short chain' and two 'long chain' K(+) channel-blocking peptides from the Chinese scorpion Buthus martensii Karsch. FEBS Lett. 1999 Sep 3;457(3):509-14. doi: 10.1016/s0014-5793(99)01101-1.
Ref 90 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 91 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 92 Solution structure of BmP02, a new potassium channel blocker from the venom of the Chinese scorpion Buthus martensi Karsch. Biochemistry. 2000 Nov 14;39(45):13669-75. doi: 10.1021/bi000860s.
Ref 93 Kbot1, a three disulfide bridges toxin from Buthus occitanus tunetanus venom highly active on both SK and Kv channels. Peptides. 2004 Apr;25(4):637-45. doi: 10.1016/j.peptides.2004.02.017.
Ref 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 Chemical synthesis and characterization of maurotoxin, a short scorpion toxin with four disulfide bridges that acts on K+ channels. Eur J Biochem. 1996 Dec 15;242(3):491-8. doi: 10.1111/j.1432-1033.1996.0491r.x.
Ref 96 Maurotoxin, a four disulfide bridge toxin from Scorpio maurus venom: purification, structure and action on potassium channels. FEBS Lett. 1997 Apr 14;406(3):284-90. doi: 10.1016/s0014-5793(97)00285-8.
Ref 97 Maurotoxin, a four disulfide bridges scorpion toxin acting on K+ channels. Toxicon. 1998 Nov;36(11):1609-11. doi: 10.1016/s0041-0101(98)00153-6.
Ref 98 Mechanisms of maurotoxin action on Shaker potassium channels. Biophys J. 2000 Aug;79(2):776-87. doi: 10.1016/S0006-3495(00)76335-1.
Ref 99 Effect of maurotoxin, a four disulfide-bridged toxin from the chactoid scorpion Scorpio maurus, on Shaker K+ channels. J Pept Res. 2000 Jun;55(6):419-27. doi: 10.1034/j.1399-3011.2000.00715.x.
Ref 100 Design and characterization of a highly selective peptide inhibitor of the small conductance calcium-activated K+ channel, SkCa2. J Biol Chem. 2001 Nov 16;276(46):43145-51. doi: 10.1074/jbc.M106981200. Epub 2001 Aug 29.
Ref 101 Scorpion Toxin, BmP01, Induces Pain by Targeting TRPV1 Channel. Toxins (Basel). 2015 Sep 14;7(9):3671-87. doi: 10.3390/toxins7093671.
Ref 102 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 103 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 104 Synthesis, 1H NMR structure, and activity of a three-disulfide-bridged maurotoxin analog designed to restore the consensus motif of scorpion toxins. J Biol Chem. 2000 May 5;275(18):13605-12. doi: 10.1074/jbc.275.18.13605.
Ref 105 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 106 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 107 Mesomartoxin, a new K(v)1.2-selective scorpion toxin interacting with the channel selectivity filter. Biochem Pharmacol. 2015 Jan 15;93(2):232-9. doi: 10.1016/j.bcp.2014.12.002. Epub 2014 Dec 13.
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.