General Information of This Target
Target ID
BTDT10177
Target Name
Potassium channel
Target Bioclass
Transporter and channel
        Click to Show/Hide the Complete Species Lineage
N.A.
Toxin Information Related to This Target
                           Toxin Name Activity Data Type Activity Data Reference
 Toxin Info    Conotoxin as14b . . [1]
 Toxin Info    Conotoxin MIVA . . [2]
 Toxin Info    Conotoxin SIVB . . [2], [3]
 Toxin Info    Crotamine Ile-19 . . [4]
 Toxin Info    Crotamine-IV-2 . . [5]
 Toxin Info    Crotamine-IV-3 . . [5]
 Toxin Info    Delta-actitoxin-Amc2a . . [6], [7]
 Toxin Info    Kappa-theraphotoxin-Gr2a . . [8]
 Toxin Info    Cysteine-rich venom protein kaouthin-1 . . [9], [10]
 Toxin Info    Kappa-thalatoxin-Cad2a . . [11]
 Toxin Info    Kunitz-type serine protease inhibitor As-fr-19 . . [12], [13]
 Toxin Info    Kunitz-type serine protease inhibitor dendrotoxin E . . [14]
 Toxin Info    Kunitz-type serine protease inhibitor homolog beta-bungarotoxin B4 chain . . [15]
 Toxin Info    Lambda-hexatoxin-Hv1a . . [16]
 Toxin Info    Myotoxin . . [17], [18], [19], [20]
 Toxin Info    Myotoxin . . [21]
 Toxin Info    Myotoxin-1 . . [22]
 Toxin Info    Myotoxin-2 . . [23]
 Toxin Info    Lambda-hexatoxin-Hv1b . . [16]
 Toxin Info    Myotoxin-2 . . [22]
 Toxin Info    Myotoxin-3 . . [23]
 Toxin Info    Myotoxin-A . . [23], [24], [25], [26]
 Toxin Info    PI-stichotoxin-Hcr2h . . [27], [28], [29]
 Toxin Info    Potassium channel toxin AaTXK-beta . . [30], [31]
 Toxin Info    Potassium channel toxin alpha-KTx 14.2 . . [32- 36]
 Toxin Info    Potassium channel toxin alpha-KTx 17.1 . . [32- 38]
 Toxin Info    Potassium channel toxin alpha-KTx 2.18 . . [39]
 Toxin Info    Potassium channel toxin alpha-KTx 2.19 . . [40]
 Toxin Info    Potassium channel toxin alpha-KTx 23.3 . . [41]
 Toxin Info    Potassium channel toxin alpha-KTx 3.16 . . [42]
 Toxin Info    Potassium channel toxin alpha-KTx 4.7 . . [43]
 Toxin Info    Potassium channel toxin alpha-KTx 5.5 . . [44]
 Toxin Info    Potassium channel toxin alpha-KTx 6.11 . . [45]
 Toxin Info    Potassium channel toxin alpha-KTx 8.4 . . [46], [47]
 Toxin Info    Potassium channel toxin alpha-KTx 9.11 . . [42]
 Toxin Info    Potassium channel toxin alpha-KTx 9.3 . . [46], [47]
 Toxin Info    Potassium channel toxin alpha-KTx 9.6 . . [48]
 Toxin Info    Potassium channel toxin alpha-KTx 9.7 . . [48]
 Toxin Info    Potassium channel toxin Hge-beta-KTx . . [49], [50], [51]
 Toxin Info    Potassium channel toxin BmTXK-beta . . [52], [53], [54], [55]
 Toxin Info    Potassium channel toxin MeuTXKbeta3-meucin-24 . . [56], [57], [58]
 Toxin Info    Potassium channel toxin Tdi-beta-KTx . . [50- 60]
 Toxin Info    Potassium channel toxin TdiKIK . . [50- 60]
 Toxin Info    Potassium channel toxin TstKMK . . [61], [62]
 Toxin Info    Tityustoxin-19 . . [63], [64], [65], [66]
 Toxin Info    Toxin BmKK12 . . [35]
 Toxin Info    Toxin BmKK16 . . [35]
 Toxin Info    Toxin Ct28 . . [67]
 Toxin Info    Toxin NvePTx1 . . [68], [69], [70]
 Toxin Info    Toxin Tx7335 . . [71]
 Toxin Info    U-actitoxin-Bcg2a . . [7- 73]
 Toxin Info    U-AITX-Bg1a . . [74]
 Toxin Info    Peptide 2 . . [75]
 Toxin Info    U-Asilidin(12)-Dg3a . . [76]
 Toxin Info    Potassium channel toxin alpha-KTx 1.18 . . [40]
 Toxin Info    Kunitz-type serine protease inhibitor PPTI . . [77], [78]
 Toxin Info    Peptide LaIT2 . . [79]
 Toxin Info    Delta-aiptatoxin-Adi1a . . [80], [81]
 Toxin Info    U-actitoxin-Bgr3a . . [7- 74]
 Toxin Info    U-actitoxin-Bgr3b . . [7- 74]
 Toxin Info    U-actitoxin-Bgr3c . . [7- 74]
 Toxin Info    U-actitoxin-Bgr3d . . [7- 74]
 Toxin Info    Potassium channel toxin alpha-KTx 18.3 . . [59- 82]
 Toxin Info    Potassium channel toxin kappa-KTx 2.2 . . [83], [84]
 Toxin Info    Conotoxin PIVF . . [85]
 Toxin Info    Heteroscorpine-1 . . [86]
 Toxin Info    Conotoxin as14a . . [1]
 Toxin Info    PI-actitoxin-Aeq3a . . [7]
 Toxin Info    PI-actitoxin-Aeq3b . . [7]
 Toxin Info    Delta-theraphotoxin-Hm1b . . [87], [88]
 Toxin Info    Potassium channel toxin alpha-KTx 3.8 . . [89]
 Toxin Info    Potassium channel toxin kappa-KTx 1.2 . . [90- 94]
 Toxin Info    Kappa-theraphotoxin-Tb1c . . [95], [96]
 Toxin Info    Conotoxin vil14a . . [97], [98]
 Toxin Info    U-actitoxin-Bcs2a . . [7- 99]
 Toxin Info    Potassium channel toxin Ts16 . . [100], [101]
 Toxin Info    Defensin alpha 5 . . [102- 115]
 Toxin Info    Defensin alpha 5 . . [102- 115]
 Toxin Info    Defensin alpha 5 . . [102- 115]
 Toxin Info    Defensin alpha 5 . . [116]
 Toxin Info    Scorpine-like peptide Tco 41.46-2 . . [117]
 Toxin Info    Potassium channel toxin gamma-KTx 4.1 . . [118]
 Toxin Info    Potassium channel toxin gamma-KTx 1.5 . . [118]
 Toxin Info    Delta-theraphotoxin-Cg1a 2 IC50
8.05 μM
[119- 125]
 Toxin Info    Delta-theraphotoxin-Cg1a 3 IC50
8.05 μM
[119- 125]
References
Ref 1 Two new 4-Cys conotoxins (framework 14) of the vermivorous snail Conus austini from the Gulf of Mexico with activity in the central nervous system of mice. Peptides. 2008 Feb;29(2):179-85. doi: 10.1016/j.peptides.2007.09.021. Epub 2007 Dec 5.
Ref 2 The A-superfamily of conotoxins: structural and functional divergence. J Biol Chem. 2004 Apr 23;279(17):17596-606. doi: 10.1074/jbc.M309654200. Epub 2003 Dec 30.
Ref 3 Two toxins from Conus striatus that individually induce tetanic paralysis. Biochemistry. 2006 Nov 28;45(47):14212-22. doi: 10.1021/bi061485s.
Ref 4 Structure of the polypeptide crotamine from the Brazilian rattlesnake Crotalus durissus terrificus. Acta Crystallogr D Biol Crystallogr. 2013 Oct;69(Pt 10):1958-64. doi: 10.1107/S0907444913018003. Epub 2013 Sep 20.
Ref 5 Structural and biological characterization of two crotamine isoforms IV-2 and IV-3 isolated from the Crotalus durissus cumanensis venom. Protein J. 2007 Dec;26(8):533-40. doi: 10.1007/s10930-007-9094-z.
Ref 6 Isolation and molecular cloning of novel peptide toxins from the sea anemone Antheopsis maculata. Toxicon. 2005 Jan;45(1):33-41. doi: 10.1016/j.toxicon.2004.09.013.
Ref 7 Development of a rational nomenclature for naming peptide and protein toxins from sea anemones. Toxicon. 2012 Sep 15;60(4):539-50. doi: 10.1016/j.toxicon.2012.05.020. Epub 2012 Jun 5.
Ref 8 Solution structure of peptide toxins that block mechanosensitive ion channels. J Biol Chem. 2002 Sep 13;277(37):34443-50. doi: 10.1074/jbc.M202715200. Epub 2002 Jun 24.
Ref 9 Structural divergence of cysteine-rich secretory proteins in snake venoms. J Biochem. 2009 Mar;145(3):365-75. doi: 10.1093/jb/mvn174. Epub 2008 Dec 23.
Ref 10 Cobra venom contains a pool of cysteine-rich secretory proteins. Biochem Biophys Res Commun. 2005 Mar 4;328(1):177-82. doi: 10.1016/j.bbrc.2004.12.154.
Ref 11 Screening and cDNA cloning of Kv1 potassium channel toxins in sea anemones. Mar Drugs. 2010 Dec 2;8(12):2893-905. doi: 10.3390/md8122893.
Ref 12 Molecular components and toxicity of the venom of the solitary wasp, Anoplius samariensis. Biochem Biophys Res Commun. 2005 May 20;330(4):1048-54. doi: 10.1016/j.bbrc.2005.03.087.
Ref 13 Peptide Toxins in Solitary Wasp Venoms. Toxins (Basel). 2016 Apr 18;8(4):114. doi: 10.3390/toxins8040114.
Ref 14 Snake venoms. The amino-acid sequence of trypsin inhibitor E of Dendroaspis polylepis polylepis (Black Mamba) venom. Eur J Biochem. 1978 Jun 1;87(1):191-8. doi: 10.1111/j.1432-1033.1978.tb12366.x.
Ref 15 Divergence of genes encoding B chains of beta-bungarotoxins. Toxicon. 2006 Mar;47(3):322-9. doi: 10.1016/j.toxicon.2005.11.009. Epub 2006 Feb 2.
Ref 16 Discovery and characterization of a family of insecticidal neurotoxins with a rare vicinal disulfide bridge. Nat Struct Biol. 2000 Jun;7(6):505-13. doi: 10.1038/75921.
Ref 17 The venom-gland transcriptome of the eastern diamondback rattlesnake (Crotalus adamanteus). BMC Genomics. 2012 Jul 16;13:312. doi: 10.1186/1471-2164-13-312.
Ref 18 A high-throughput venom-gland transcriptome for the Eastern Diamondback Rattlesnake (Crotalus adamanteus) and evidence for pervasive positive selection across toxin classes. Toxicon. 2011 Apr;57(5):657-71. doi: 10.1016/j.toxicon.2011.01.008. Epub 2011 Jan 19.
Ref 19 Amino acid sequence of a myotoxin from venom of the eastern diamondback rattlesnake (Crotalus adamanteus). Toxicon. 1991;29(4-5):461-8. doi: 10.1016/0041-0101(91)90020-r.
Ref 20 Linking the transcriptome and proteome to characterize the venom of the eastern diamondback rattlesnake (Crotalus adamanteus). J Proteomics. 2014 Jan 16;96:145-58. doi: 10.1016/j.jprot.2013.11.001. Epub 2013 Nov 12.
Ref 21 Some chemical properties of the venom of the rattlesnake, Crotalus viridis helleri. Toxicon. 1978;16(5):431-41. doi: 10.1016/0041-0101(78)90140-x.
Ref 22 Amino acid sequences of myotoxins from Crotalus viridis concolor venom. Toxicon. 1987;25(6):677-80. doi: 10.1016/0041-0101(87)90115-2.
Ref 23 A new small myotoxin from the venom of the prairie rattlesnake (Crotalus viridis viridis). FEBS Lett. 1990 Nov 12;274(1-2):43-7. doi: 10.1016/0014-5793(90)81325-i.
Ref 24 Amino acid sequence and disulfide bond assignment of myotoxin a isolated from the venom of Prairie rattlesnake (Crotalus viridis viridis). Biochemistry. 1979 Feb 20;18(4):678-84. doi: 10.1021/bi00571a020.
Ref 25 Multiple myotoxin sequences from the venom of a single prairie rattlesnake (Crotalus viridis viridis). Toxicon. 1991;29(2):265-8. doi: 10.1016/0041-0101(91)90111-4.
Ref 26 Structure-function relationship of myotoxin a using peptide fragments. Arch Biochem Biophys. 1992 Nov 1;298(2):325-31. doi: 10.1016/0003-9861(92)90418-v.
Ref 27 Kunitz-Type Peptide HCRG21 from the Sea Anemone Heteractis crispa Is a Full Antagonist of the TRPV1 Receptor. Mar Drugs. 2016 Dec 15;14(12):229. doi: 10.3390/md14120229.
Ref 28 Kunitz-Type Peptides from the Sea Anemone Heteractis crispa Demonstrate Potassium Channel Blocking and Anti-Inflammatory Activities. Biomedicines. 2020 Nov 4;8(11):473. doi: 10.3390/biomedicines8110473.
Ref 29 Sea Anemone Kunitz-Type Peptides Demonstrate Neuroprotective Activity in the 6-Hydroxydopamine Induced Neurotoxicity Model. Biomedicines. 2021 Mar 10;9(3):283. doi: 10.3390/biomedicines9030283.
Ref 30 Evidence for a new class of scorpion toxins active against K+ channels. FEBS Lett. 1998 Jul 24;431(3):375-80. doi: 10.1016/s0014-5793(98)00780-7.
Ref 31 Subtype-selective activation of K(v)7 channels by AaTXK????, a novel toxin variant from the Androctonus australis scorpion venom. Mol Pharmacol. 2013 Nov;84(5):763-73. doi: 10.1124/mol.113.088971. Epub 2013 Sep 9.
Ref 32 Molecular cloning and characterization of four scorpion K(+)-toxin-like peptides: a new subfamily of venom peptides (alpha-KTx14) and genomic analysis of a member. Biochimie. 2001 Sep;83(9):883-9. doi: 10.1016/s0300-9084(01)01326-8.
Ref 33 Precursors of three unique cysteine-rich peptides from the scorpion Buthus martensii Karsch. Comp Biochem Physiol B Biochem Mol Biol. 2002 Apr;131(4):749-56. doi: 10.1016/s1096-4959(02)00020-9.
Ref 34 Purification and pharmacological characterization of BmKK2 (alpha-KTx 14.2), a novel potassium channel-blocking peptide, from the venom of Asian scorpion Buthus martensi Karsch. Toxicon. 2004 Jun 15;43(8):895-900. doi: 10.1016/j.toxicon.2003.11.028.
Ref 35 Short-chain peptides identification of scorpion Buthus martensi Karsch venom by employing high orthogonal 2D-HPLC system and tandem mass spectrometry. Proteomics. 2012 Oct;12(19-20):3076-84. doi: 10.1002/pmic.201200224. Epub 2012 Sep 19.
Ref 36 Solution structure of BmKK2, a new potassium channel blocker from the venom of chinese scorpion Buthus martensi Karsch. Proteins. 2004 Jun 1;55(4):835-45. doi: 10.1002/prot.20117.
Ref 37 BmKK4, a novel toxin from the venom of Asian scorpion Buthus martensi Karsch, inhibits potassium currents in rat hippocampal neurons in vitro. Toxicon. 2003 Aug;42(2):199-205. doi: 10.1016/s0041-0101(03)00136-3.
Ref 38 Solution structure of BmKK4, the first member of subfamily alpha-KTx 17 of scorpion toxins. Biochemistry. 2004 Oct 5;43(39):12469-76. doi: 10.1021/bi0490643.
Ref 39 Comparative proteomic analysis of female and male venoms from the Mexican scorpion Centruroides limpidus: Novel components found. Toxicon. 2017 Jan;125:91-98. doi: 10.1016/j.toxicon.2016.11.256. Epub 2016 Nov 24.
Ref 40 Comparative proteomic analysis of male and female venoms from the Cuban scorpion Rhopalurus junceus. Toxicon. 2015 Dec 1;107(Pt B):327-34. doi: 10.1016/j.toxicon.2015.06.026. Epub 2015 Jul 10.
Ref 41 St20, a new venomous animal derived natural peptide with immunosuppressive and anti-inflammatory activities. Toxicon. 2017 Mar 1;127:37-43. doi: 10.1016/j.toxicon.2017.01.005. Epub 2017 Jan 8.
Ref 42 Novel potassium channel blocker venom peptides from Mesobuthus gibbosus (Scorpiones: Buthidae). Toxicon. 2013 Jan;61:72-82. doi: 10.1016/j.toxicon.2012.10.010. Epub 2012 Nov 7.
Ref 43 Molecular basis of Tityus stigmurus alpha toxin and potassium channel kV1.2 interactions. J Mol Graph Model. 2019 Mar;87:197-203. doi: 10.1016/j.jmgm.2018.11.012. Epub 2018 Nov 28.
Ref 44 Tamapin, a venom peptide from the Indian red scorpion (Mesobuthus tamulus) that targets small conductance Ca2+-activated K+ channels and afterhyperpolarization currents in central neurons. J Biol Chem. 2002 Nov 29;277(48):46101-9. doi: 10.1074/jbc.M206465200. Epub 2002 Sep 17.
Ref 45 Solution structure of IsTX. A male scorpion toxin from Opisthacanthus madagascariensis (Ischnuridae). Eur J Biochem. 2004 Oct;271(19):3855-64. doi: 10.1111/j.1432-1033.2004.04322.x.
Ref 46 Characterization of a new family of toxin-like peptides from the venom of the scorpion Leiurus quinquestriatus hebraeus. 1H-NMR structure of leiuropeptide II. J Pept Res. 1997 Jun;49(6):545-55. doi: 10.1111/j.1399-3011.1997.tb01162.x.
Ref 47 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 48 Activation of skeletal ryanodine receptors by two novel scorpion toxins from Buthotus judaicus. J Biol Chem. 2004 Jun 18;279(25):26588-96. doi: 10.1074/jbc.M403284200. Epub 2004 Apr 5.
Ref 49 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 50 Wide phylogenetic distribution of Scorpine and long-chain beta-KTx-like peptides in scorpion venoms: identification of "orphan" components. Peptides. 2007 Jan;28(1):31-7. doi: 10.1016/j.peptides.2006.06.012. Epub 2006 Dec 1.
Ref 51 Cytolytic and K+ channel blocking activities of beta-KTx and scorpine-like peptides purified from scorpion venoms. Cell Mol Life Sci. 2008 Jan;65(1):187-200. doi: 10.1007/s00018-007-7370-x.
Ref 52 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 53 A naturally occurring non-coding fusion transcript derived from scorpion venom gland: implication for the regulation of scorpion toxin gene expression. FEBS Lett. 2001 Nov 16;508(2):241-4. doi: 10.1016/s0014-5793(01)03067-8.
Ref 54 Evidence that BmTXK beta-BmKCT cDNA from Chinese scorpion Buthus martensii Karsch is an artifact generated in the reverse transcription process. FEBS Lett. 2002 Jun 5;520(1-3):183-4; author reply 185. doi: 10.1016/s0014-5793(02)02812-0.
Ref 55 Expression, purification and functional characterization of a recombinant scorpion venom peptide BmTXKbeta. Peptides. 2003 Feb;24(2):187-92. doi: 10.1016/s0196-9781(03)00025-1.
Ref 56 Characterization of two linear cationic antimalarial peptides in the scorpion Mesobuthus eupeus. Biochimie. 2010 Apr;92(4):350-9. doi: 10.1016/j.biochi.2010.01.011. Epub 2010 Jan 22.
Ref 57 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 58 Scorpion venom peptides with no disulfide bridges: a review. Peptides. 2014 Jan;51:35-45. doi: 10.1016/j.peptides.2013.10.021. Epub 2013 Oct 31.
Ref 59 Molecular cloning and nucleotide sequence analysis of genes from a cDNA library of the scorpion Tityus discrepans. Biochimie. 2009 Aug;91(8):1010-9. doi: 10.1016/j.biochi.2009.05.005. Epub 2009 May 24.
Ref 60 Proteomic analysis of Tityus discrepans scorpion venom and amino acid sequence of novel toxins. Proteomics. 2006 Jun;6(12):3718-27. doi: 10.1002/pmic.200500525.
Ref 61 Molecular approaches for structural characterization of a new potassium channel blocker from Tityus stigmurus venom: cDNA cloning, homology modeling, dynamic simulations and docking. Biochem Biophys Res Commun. 2013 Jan 4;430(1):113-8. doi: 10.1016/j.bbrc.2012.11.044. Epub 2012 Nov 27.
Ref 62 Proteomic analysis of the venom from the scorpion Tityus stigmurus: biochemical and physiological comparison with other Tityus species. Comp Biochem Physiol C Toxicol Pharmacol. 2007 Jul-Aug;146(1-2):147-157. doi: 10.1016/j.cbpc.2006.12.004. Epub 2006 Dec 16.
Ref 63 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 64 Isolation and characterization of Ts19 Fragment II, a new long-chain potassium channel toxin from Tityus serrulatus venom. Peptides. 2016 Jun;80:9-17. doi: 10.1016/j.peptides.2015.06.004. Epub 2015 Jun 25.
Ref 65 Tityus serrulatus venom peptidomics: assessing venom peptide diversity. Toxicon. 2008 Oct;52(5):611-8. doi: 10.1016/j.toxicon.2008.07.010. Epub 2008 Jul 31.
Ref 66 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 67 Mass fingerprinting of the venom and transcriptome of venom gland of scorpion Centruroides tecomanus. PLoS One. 2013 Jun 20;8(6):e66486. doi: 10.1371/journal.pone.0066486. Print 2013.
Ref 68 Sea anemone genome reveals ancestral eumetazoan gene repertoire and genomic organization. Science. 2007 Jul 6;317(5834):86-94. doi: 10.1126/science.1139158.
Ref 69 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.
Ref 70 Dynamics of venom composition across a complex life cycle. Elife. 2018 Feb 9;7:e35014. doi: 10.7554/eLife.35014.
Ref 71 Discovery and characterisation of a novel toxin from Dendroaspis angusticeps, named Tx7335, that activates the potassium channel KcsA. Sci Rep. 2016 Apr 5;6:23904. doi: 10.1038/srep23904.
Ref 72 Proteomics of the neurotoxic fraction from the sea anemone Bunodosoma cangicum venom: Novel peptides belonging to new classes of toxins. Comp Biochem Physiol Part D Genomics Proteomics. 2008 Sep;3(3):219-25. doi: 10.1016/j.cbd.2008.04.002. Epub 2008 Apr 26.
Ref 73 Sea anemone peptide with uncommon -hairpin structure inhibits acid-sensing ion channel 3 (ASIC3) and reveals analgesic activity. J Biol Chem. 2013 Aug 9;288(32):23116-27. doi: 10.1074/jbc.M113.485516. Epub 2013 Jun 25.
Ref 74 Peptide fingerprinting of the neurotoxic fractions isolated from the secretions of sea anemones Stichodactyla helianthus and Bunodosoma granulifera. New members of the APETx-like family identified by a 454 pyrosequencing approach. Peptides. 2012 Mar;34(1):26-38. doi: 10.1016/j.peptides.2011.10.011. Epub 2011 Oct 12.
Ref 75 Characterization of two different peptides from the venom of the scorpion Buthus sindicus. FEBS Lett. 1989 Nov 6;257(2):260-2. doi: 10.1016/0014-5793(89)81548-0.
Ref 76 Buzz Kill: Function and Proteomic Composition of Venom from the Giant Assassin Fly Dolopus genitalis (Diptera: Asilidae). Toxins (Basel). 2018 Nov 5;10(11):456. doi: 10.3390/toxins10110456.
Ref 77 Characterization of a new member of kunitz-type protein family from the venom of Persian false-horned viper, Pseudocerastes persicus. Arch Biochem Biophys. 2019 Feb 15;662:1-6. doi: 10.1016/j.abb.2018.11.017. Epub 2018 Nov 16.
Ref 78 Structural characterization of PPTI, a kunitz-type protein from the venom of Pseudocerastes persicus. PLoS One. 2019 Apr 11;14(4):e0214657. doi: 10.1371/journal.pone.0214657. eCollection 2019.
Ref 79 Purification and cDNA cloning of LaIT2, a novel insecticidal toxin from venom of the scorpion Liocheles australasiae. Biosci Biotechnol Biochem. 2009 Dec;73(12):2769-72. doi: 10.1271/bbb.90509. Epub 2009 Dec 7.
Ref 80 AdE-1, a new inotropic Na(+) channel toxin from Aiptasia diaphana, is similar to, yet distinct from, known anemone Na(+) channel toxins. Biochem J. 2013 Apr 1;451(1):81-90. doi: 10.1042/BJ20121623.
Ref 81 The sea anemone toxin AdE-1 modifies both sodium and potassium currents of rat cardiomyocytes. Biochem J. 2014 Jul 1;461(1):51-9. doi: 10.1042/BJ20131454.
Ref 82 Looking over toxin-K(+) channel interactions. Clues from the structural and functional characterization of -KTx toxin Tc32, a Kv1.3 channel blocker. Biochemistry. 2012 Mar 6;51(9):1885-94. doi: 10.1021/bi201713z. Epub 2012 Feb 27.
Ref 83 An unusual fold for potassium channel blockers: NMR structure of three toxins from the scorpion Opisthacanthus madagascariensis. Biochem J. 2005 May 15;388(Pt 1):263-71. doi: 10.1042/BJ20041705.
Ref 84 Purification, molecular cloning and functional characterization of HelaTx1 (Heterometrus laoticus): the first member of a new -KTX subfamily. Biochem Pharmacol. 2012 May 1;83(9):1307-17. doi: 10.1016/j.bcp.2012.01.021. Epub 2012 Jan 24.
Ref 85 Discovery and characterization of the short kappaA-conotoxins: a novel subfamily of excitatory conotoxins. Toxicon. 2007 Mar 1;49(3):318-28. doi: 10.1016/j.toxicon.2006.10.001. Epub 2006 Oct 14.
Ref 86 Purification and characterization of Heteroscorpine-1 (HS-1) toxin from Heterometrus laoticus scorpion venom. Toxicon. 2007 Jan;49(1):19-29. doi: 10.1016/j.toxicon.2006.09.003. Epub 2006 Sep 14.
Ref 87 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 88 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 89 Purification and primary structure of low molecular mass peptides from scorpion (Buthus sindicus) venom. Comp Biochem Physiol A Mol Integr Physiol. 1998 Dec;121(4):323-32. doi: 10.1016/s1095-6433(98)10140-x.
Ref 90 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 91 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 92 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 93 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 94 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 95 Nanospray analysis of the venom of the tarantula Theraphosa leblondi: a powerful method for direct venom mass fingerprinting and toxin sequencing. Rapid Commun Mass Spectrom. 2004;18(10):1024-32. doi: 10.1002/rcm.1442.
Ref 96 Modulation of Kv4.2 channels by a peptide isolated from the venom of the giant bird-eating tarantula Theraphosa leblondi. Toxicon. 2004 Jun 15;43(8):923-32. doi: 10.1016/j.toxicon.2003.12.012.
Ref 97 Definition of the R-superfamily of conotoxins: Structural convergence of helix-loop-helix peptidic scaffolds. Peptides. 2018 Sep;107:75-82. doi: 10.1016/j.peptides.2018.06.002. Epub 2018 Jul 21.
Ref 98 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 99 BcIV, a new paralyzing peptide obtained from the venom of the sea anemone Bunodosoma caissarum. A comparison with the Na+ channel toxin BcIII. Biochim Biophys Acta. 2006 Oct;1764(10):1592-600. doi: 10.1016/j.bbapap.2006.08.010. Epub 2006 Aug 26.
Ref 100 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 101 New tricks of an old pattern: structural versatility of scorpion toxins with common cysteine spacing. J Biol Chem. 2012 Apr 6;287(15):12321-30. doi: 10.1074/jbc.M111.329607. Epub 2012 Jan 10.
Ref 102 DNA sequence and analysis of human chromosome 8. Nature. 2006 Jan 19;439(7074):331-5. doi: 10.1038/nature04406.
Ref 103 The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. doi: 10.1101/gr.2596504.
Ref 104 Paneth cell trypsin is the processing enzyme for human defensin-5. Nat Immunol. 2002 Jun;3(6):583-90. doi: 10.1038/ni797. Epub 2002 May 20.
Ref 105 Protection against enteric salmonellosis in transgenic mice expressing a human intestinal defensin. Nature. 2003 Apr 3;422(6931):522-6. doi: 10.1038/nature01520. Epub 2003 Mar 19.
Ref 106 Antibacterial activity and specificity of the six human {alpha}-defensins. Antimicrob Agents Chemother. 2005 Jan;49(1):269-75. doi: 10.1128/AAC.49.1.269-275.2005.
Ref 107 Human alpha defensin 5 expression in the human kidney and urinary tract. PLoS One. 2012;7(2):e31712. doi: 10.1371/journal.pone.0031712. Epub 2012 Feb 16.
Ref 108 Paneth cell -defensin 6 (HD-6) is an antimicrobial peptide. Mucosal Immunol. 2015 May;8(3):661-71. doi: 10.1038/mi.2014.100. Epub 2014 Nov 5.
Ref 109 Paneth cell -defensins HD-5 and HD-6 display differential degradation into active antimicrobial fragments. Proc Natl Acad Sci U S A. 2019 Feb 26;116(9):3746-3751. doi: 10.1073/pnas.1817376116. Epub 2019 Feb 11.
Ref 110 Crystal structures of human alpha-defensins HNP4, HD5, and HD6. Protein Sci. 2006 Dec;15(12):2749-60. doi: 10.1110/ps.062336606. Epub 2006 Nov 6.
Ref 111 Selective arginines are important for the antibacterial activity and host cell interaction of human alpha-defensin 5. FEBS Lett. 2009 Aug 6;583(15):2507-12. doi: 10.1016/j.febslet.2009.06.051. Epub 2009 Jul 7.
Ref 112 NMR solution structure and condition-dependent oligomerization of the antimicrobial peptide human defensin 5. Biochemistry. 2012 Dec 4;51(48):9624-37. doi: 10.1021/bi301255u. Epub 2012 Nov 19.
Ref 113 Functional determinants of human enteric -defensin HD5: crucial role for hydrophobicity at dimer interface. J Biol Chem. 2012 Jun 22;287(26):21615-27. doi: 10.1074/jbc.M112.367995. Epub 2012 May 9.
Ref 114 Design of a potent antibiotic peptide based on the active region of human defensin 5. J Med Chem. 2015 Apr 9;58(7):3083-93. doi: 10.1021/jm501824a. Epub 2015 Mar 20.
Ref 115 Human Enteric -Defensin 5 Promotes Shigella Infection by Enhancing Bacterial Adhesion and Invasion. Immunity. 2018 Jun 19;48(6):1233-1244.e6. doi: 10.1016/j.immuni.2018.04.014. Epub 2018 May 29.
Ref 116 Human -defensins are immune-related Kv1.3 channel inhibitors: new support for their roles in adaptive immunity. FASEB J. 2015 Oct;29(10):4324-33. doi: 10.1096/fj.15-274787. Epub 2015 Jul 6.
Ref 117 The Brazilian scorpion Tityus costatus Karsch: genes, peptides and function. Toxicon. 2005 Mar 1;45(3):273-83. doi: 10.1016/j.toxicon.2004.10.014. Epub 2004 Dec 10.
Ref 118 A large number of novel Ergtoxin-like genes and ERG K+-channels blocking peptides from scorpions of the genus Centruroides. FEBS Lett. 2002 Dec 4;532(1-2):121-6. doi: 10.1016/s0014-5793(02)03652-9.
Ref 119 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 120 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 121 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 122 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 123 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 124 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 125 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.
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.