General Information of This Target
Target ID
BTDT00051
Target Name
Potassium voltage-gated channel subfamily A member 4 (Kcna4)
Target Bioclass
Transporter and channel
Uniprot ID
P15385
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
Kcna4
Gene ID
25469
Synonym
RCK4; RHK1; RK3; Voltage-gated potassium channel subunit Kv1.4
Sequence
MEVAMVSAESSGCNSHMPYGYAAQARARERERLAHSRAAAAAAVAAATAAVEGTGGSGGG
PHHHHQTRGAYSSHDPQGSRGSREEEATRTEKKKKLHHRQSSFPHCSDLMPSGSEEKILR
ELSEEEEDEEEEEEEEEEGRFYYSEEDHGDGCSYTDLLPQDDGGGGGYSSVRYSDCCERV
VINVSGLRFETQMKTLAQFPETLLGDPEKRTQYFDPLRNEYFFDRNRPSFDAILYYYQSG
GRLKRPVNVPFDIFTEEVKFYQLGEEALLKFREDEGFVREEEDRALPENEFKKQIWLLFE
YPESSSPARGIAIVSVLVILISIVIFCLETLPEFRDDRDLIMALSAGGHSRLLNDTSAPH
LENSGHTIFNDPFFIVETVCIVWFSFEFVVRCFACPSQALFFKNIMNIIDIVSILPYFIT
LGTDLAQQQGGGNGQQQQAMSFAILRIIRLVRVFRIFKLSRHSKGLQILGHTLRASMREL
GLLIFFLFIGVILFSSAVYFAEADEPTTHFQSIPDAFWWAVVTMTTVGYGDMKPITVGGK
IVGSLCAIAGVLTIALPVPVIVSNFNYFYHRETENEEQTQLTQNAVSCPYLPSNLLKKFR
SSTSSSLGDKSEYLEMEEGVKESLCGKEEKCQGKGDDSETDKNNCSNAKAVETDV

    Click to Show/Hide
Family
the potassium channel family
Function
Voltage-gated potassium channel that mediates transmembrane potassium transport in excitable membranes. 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, 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. 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 KCNA4 forms a potassium channel that opens in response to membrane depolarization, followed by rapid spontaneous channel closure. Likewise, a heterotetrameric channel formed by KCNA1 and KCNA4 shows rapid inactivation.

    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    N.vectensis toxin 4 Effect . [1]
 Toxin Info    N.vectensis toxin 5 Effect . [1]
 Toxin Info    Toxin MeKTx13-3 (G11R,I28M,G30R,D33H) Inhibition rate . [2- 21]
 Toxin Info    Toxin MeKTx13-3 (Q12A,K15A,K18A,D33R) Inhibition rate . [22]
 Toxin Info    Mu-conotoxin CnIIIC Inhibition rate . [23], [24], [25]
 Toxin Info    Crotamine Inhibition rate . [26]
 Toxin Info    Kappa-actitoxin-Bcs3a Inhibition rate . [27]
 Toxin Info    Defensin-like protein 1 Inhibition rate . [28]
 Toxin Info    Kappa-actitoxin-Bcs3b Inhibition rate . [27]
 Toxin Info    Kappa-conotoxin PVIIA Inhibition rate . [29- 40]
 Toxin Info    Kunitz-type serine protease inhibitor homolog alpha-dendrotoxin Inhibition rate . [41]
 Toxin Info    Potassium channel toxin alpha-KTx 1.17 Inhibition rate . [42]
 Toxin Info    Potassium channel toxin alpha-KTx 19.2 Inhibition rate . [43]
 Toxin Info    Potassium channel toxin alpha-KTx 3.13 Inhibition rate . [44]
 Toxin Info    Mu-conotoxin GIIIA Inhibition rate . [45- 57]
 Toxin Info    Mu-conotoxin PIIIA Inhibition rate . [23- 61]
 Toxin Info    Mu-conotoxin SIIIA Inhibition rate . [23- 86]
 Toxin Info    PI-stichotoxin-Hcr2f Inhibition rate . [87]
 Toxin Info    PI-stichotoxin-Hcr2g Inhibition rate . [87]
 Toxin Info    Potassium channel toxin alpha-KTx 1.16 Inhibition rate . [42]
 Toxin Info    Potassium channel toxin alpha-KTx 31.1 Inhibition rate . [88]
 Toxin Info    Toxin PhcrTx2 Inhibition rate . [89]
 Toxin Info    Kappa-LhTx-1 Inhibition rate . [90]
 Toxin Info    Potassium channel toxin alpha-KTx 3.18 Inhibition rate . [2- 21]
 Toxin Info    Potassium channel toxin alpha-KTx 4.1 Inhibition rate . [91]
 Toxin Info    Potassium channel toxin alpha-KTx 8.2 Inhibition rate . [92]
 Toxin Info    Potassium channel toxin alpha-KTx 8.5 Inhibition rate . [93]
 Toxin Info    Potassium channel toxin alpha-KTx 8.6 Inhibition rate . [92], [94]
 Toxin Info    Potassium channel toxin alpha-KTx 8.6 Inhibition rate . [92]
 Toxin Info    Kappa-actitoxin-Bcs4a Inhibition rate . [95]
 Toxin Info    Potassium channel toxin AbeTx1 Inhibition rate . [96]
 Toxin Info    Potassium channel toxin AbeTx1 Inhibition rate . [96]
 Toxin Info    Potassium channel toxin alpha-KTx 8.8 Inhibition rate . [97]
 Toxin Info    Potassium channel toxin alpha-KTx 9.1 Inhibition rate . [98]
 Toxin Info    Potassium channel toxin alpha-KTx 9.2 Inhibition rate . [98]
 Toxin Info    Potassium channel toxin epsilon-KTx 1.1 Inhibition rate . [99]
 Toxin Info    Potassium channel toxin kappa-KTx 2.5 Inhibition rate . [100]
 Toxin Info    Potassium channel toxin TsTXK-beta Inhibition rate . [101]
 Toxin Info    Potassium channel toxin alpha-KTx 3.19 Inhibition rate . [22]
 Toxin Info    Apamin Inhibition rate . [102- 119]
 Toxin Info    Potassium channel toxin alpha-KTx 12.2 Inhibition rate . [91]
 Toxin Info    Thrombin-like enzyme collinein-1 Inhibition rate . [120], [121], [122], [123]
 Toxin Info    U-actitoxin-Oulsp1 Inhibition rate . [124]
 Toxin Info    U-actitoxin-Oulsp1 Inhibition rate . [125]
 Toxin Info    Potassium channel toxin alpha-KTx 16.4 Inhibition rate . [126]
 Toxin Info    Potassium channel toxin alpha-KTx 20.1 Inhibition rate . [127]
 Toxin Info    Potassium channel toxin alpha-KTx 3.11 Inhibition rate . [128]
 Toxin Info    Mu-theraphotoxin-Pspp1 Inhibition rate . [129]
 Toxin Info    Kappa-actitoxin-Ate1a Inhibition rate . [130]
 Toxin Info    U-actitoxin-Avd3n Inhibition rate . [131]
 Toxin Info    Potassium channel toxin alpha-KTx 3.2 Inhibition rate . [132]
 Toxin Info    Potassium channel toxin alpha-KTx 3.7 Inhibition rate . [132]
 Toxin Info    Kappa-sparatoxin-Hv1b Inhibition rate . [133]
 Toxin Info    Kappa-sparatoxin-Hv1c Inhibition rate . [134]
 Toxin Info    Potassium channel toxin alpha-KTx 12.1 Inhibition rate . [91]
 Toxin Info    APETx2 Inhibition rate . [135- 144]
 Toxin Info    Potassium channel toxin alpha-KTx 21.1 Inhibition rate . [145]
 Toxin Info    Potassium channel toxin alpha-KTx 3.6 Inhibition rate . [44]
 Toxin Info    Potassium channel toxin alpha-KTx 21.1 Inhibition rate . [145- 149]
 Toxin Info    Neurotoxin lambda-MeuTx Inhibition rate . [150]
 Toxin Info    KappaPI-actitoxin-Ael3a Inhibition rate . [151], [152]
 Toxin Info    Peptide TsPep3 Inhibition rate
20 %
[147- 154]
 Toxin Info    Potassium channel toxin epsilon-KTx 1.2 Inhibition rate
20 %
[99]
 Toxin Info    Calcium channel toxin-like peptide-1 Inhibition rate
36 %
[150]
 Toxin Info    Pi-stichotoxin-Hcr5b Inhibition rate
47 %
[155]
References
Ref 1 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 2 Retraction: Role of mesenchymal stem cells versus angiotensin converting enzyme inhibitor in kidney repair. Nephrology (Carlton). 2024 Apr;29(4):239. doi: 10.1111/nep.14278. Epub 2024 Feb 11.
Ref 3 Photogeneration and quenching of singlet molecular oxygen by bacterial C(40) carotenoids with long chain of conjugated double bonds. Photosynth Res. 2024 Mar;159(2-3):291-301. doi: 10.1007/s11120-023-01070-6. Epub 2024 Feb 5.
Ref 4 Density Functional Theory, Molecular Dynamics and AlteQ Studies Approaches of Baimantuoluoamide A and Baimantuoluoamide B to Identify Potential Inhibitors of M(pro) Proteins: a Novel Target for the Treatment of SARS COVID-19. JETP Lett. 2023 May 15:1-10. doi: 10.1134/S0021364023600039. Online ahead of print.
Ref 5 Melatonin Confers NaCl Tolerance in Withaniacoagulans L. by Maintaining Na(+)/K(+) Homeostasis, Strengthening the Antioxidant Defense System and Modulating Withanolides Synthesis-Related Genes. Russ J Plant Physiol. 2023;70(3):52. doi: 10.1134/S1021443723600125. Epub 2023 May 23.
Ref 6 Rhodococcus rhodochrous IEGM 1360, an Effective Biocatalyst of C3 Oxidative Transformation of Oleanane Triterpenoids. Microbiology (N Y). 2023;92(2):204-214. doi: 10.1134/S0026261722603360. Epub 2023 Apr 21.
Ref 7 Quaternary Ammonium Salt Strategy and Molecular Docking Studies of Novel 5-Acyl-8-(Arylamino)-Quinolines by Acetyl and Methanesulfonyl Chloride for Dual Evaluation Bioactivity. Russ J Bioorg Chem. 2023;49(2):367-375. doi: 10.1134/S1068162023020097. Epub 2023 Feb 21.
Ref 8 Erratum to: Prospects for the Use of Marine Sulfated Fucose-Rich Polysaccharides in Treatment and Prevention of COVID-19 and Post-COVID-19 Syndrome. Russ J Bioorg Chem. 2022;48(6):1372. doi: 10.1134/S1068162022340015. Epub 2022 Dec 23.
Ref 9 Current Trends and Approaches to the Search for Genetic Determinants of Aging and Longevity. Russ J Genet. 2022;58(12):1427-1443. doi: 10.1134/S1022795422120067. Epub 2022 Dec 28.
Ref 10 Design, Synthesis, Anti-Tubercular Evaluation and Teratogenicity Studies of Furanyl Pyrazolo[3,4-b] Quinoline-5-Ones. Russ J Bioorg Chem. 2023;49(1):127-138. doi: 10.1134/S1068162023010053. Epub 2022 Dec 22.
Ref 11 Rapid Assessment of Neutralizing Antibodies Using Influenza Viruses with a Luciferase Reporter. Appl Biochem Microbiol. 2022;58(7):878-886. doi: 10.1134/S0003683822070067. Epub 2022 Dec 6.
Ref 12 Analysis of adiabatic trapping phenomena for quasi-integrable area-preserving maps in the presence of time-dependent exciters. Phys Rev E. 2022 Sep;106(3-1):034204. doi: 10.1103/PhysRevE.106.034204.
Ref 13 Synthesis, Antiviral, and Antibacterial Activity of the Glycyrrhizic Acid and Glycyrrhetinic Acid Derivatives. Russ J Bioorg Chem. 2022;48(5):906-918. doi: 10.1134/S1068162022050132. Epub 2022 Jul 28.
Ref 14 Erratum to: Evaluation of the Effects of Favipiravir Combined with Vitamin C on Alveolar Bone in Rats. J Evol Biochem Physiol. 2022;58(3):941. doi: 10.1134/S0022093022030280. Epub 2022 Jun 29.
Ref 15 Design, Synthesis, and Molecular Docking Studies of Some New Quinoxaline Derivatives as EGFR Targeting Agents. Russ J Bioorg Chem. 2022;48(3):565-575. doi: 10.1134/S1068162022030220. Epub 2022 Jun 21.
Ref 16 Identification of Some Promising Heterocycles Useful in Treatment of Allergic Rhinitis: Virtual Screening, Pharmacophore Mapping, Molecular Docking, and Molecular Dynamics. Russ J Bioorg Chem. 2022;48(2):438-456. doi: 10.1134/S1068162022330019. Epub 2022 May 26.
Ref 17 Erratum to: Experimental Search for New Means of Pathogenetic Therapy COVID-19: Inhibitor of H2-Receptors Famotidine Increases the Effect of Oseltamivir on Survival and Immune Status of Mice Infected by A/PR/8/34 (H1N1). J Evol Biochem Physiol. 2022;58(2):623. doi: 10.1134/S0022093022020284. Epub 2022 May 16.
Ref 18 MicroRNAs as the Potential Regulators of SARS-CoV-2 Infection and Modifiers of the COVID-19 Clinical Features. Mol Biol. 2022;56(1):29-45. doi: 10.1134/S0026893322010034. Epub 2022 Feb 12.
Ref 19 Predators as Control Agents of Mosquito Larvae in Micro-Reservoirs (Review). Inland Water Biol. 2022;15(1):39-53. doi: 10.1134/S1995082922010138. Epub 2022 Mar 12.
Ref 20 Molecular Beacon DNA Probes with Fluorescein Bifluorophore. Russ J Bioorg Chem. 2021;47(3):734-740. doi: 10.1134/S1068162021030055. Epub 2021 Jun 11.
Ref 21 Synthesis, Molecular Docking, In Silico ADME Predictions, and Toxicity Studies of N-Substituted-5-(4-Chloroquinolin-2-yl)-1,3,4-Thiadiazol-2-Amine Derivatives as COVID-19 Inhibitors. Russ J Bioorg Chem. 2021;47(1):158-165. doi: 10.1134/S1068162021010155. Epub 2021 Mar 20.
Ref 22 Tuning Scorpion Toxin Selectivity: Switching From K(V)1.1 to K(V)1.3. Front Pharmacol. 2020 Jul 7;11:1010. doi: 10.3389/fphar.2020.01010. eCollection 2020.
Ref 23 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 24 Large-scale discovery of conopeptides and conoproteins in the injectable venom of a fish-hunting cone snail using a combined proteomic and transcriptomic approach. J Proteomics. 2012 Sep 18;75(17):5215-25. doi: 10.1016/j.jprot.2012.06.001. Epub 2012 Jun 13.
Ref 25 Peptide therapeutics from venom: Current status and potential. Bioorg Med Chem. 2018 Jun 1;26(10):2738-2758. doi: 10.1016/j.bmc.2017.09.029. Epub 2017 Sep 23.
Ref 26 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 27 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 28 The antifungal plant defensin AtPDF2.3 from Arabidopsis thaliana blocks potassium channels. Sci Rep. 2016 Aug 30;6:32121. doi: 10.1038/srep32121.
Ref 29 kappa-Conotoxin PVIIA is a peptide inhibiting the shaker K+ channel. J Biol Chem. 1998 Jan 2;273(1):33-8. doi: 10.1074/jbc.273.1.33.
Ref 30 Strategy for rapid immobilization of prey by a fish-hunting marine snail. Nature. 1996 May 9;381(6578):148-51. doi: 10.1038/381148a0.
Ref 31 The block of Shaker K+ channels by kappa-conotoxin PVIIA is state dependent. J Gen Physiol. 1999 Jul;114(1):125-40. doi: 10.1085/jgp.114.1.125.
Ref 32 Single amino acid substitutions in kappa-conotoxin PVIIA disrupt interaction with the shaker K+ channel. J Biol Chem. 2000 Aug 11;275(32):24639-44. doi: 10.1074/jbc.C900990199.
Ref 33 Molecular simulation of the interaction of kappa-conotoxin-PVIIA with the Shaker potassium channel pore. Eur Biophys J. 2001 Dec;30(7):528-36. doi: 10.1007/s00249-001-0189-8.
Ref 34 Inhibition of single Shaker K channels by kappa-conotoxin-PVIIA. Biophys J. 2002 Jun;82(6):3003-11. doi: 10.1016/S0006-3495(02)75641-5.
Ref 35 Electrostatic recognition and induced fit in the kappa-PVIIA toxin binding to Shaker potassium channel. J Am Chem Soc. 2005 May 11;127(18):6836-49. doi: 10.1021/ja042641q.
Ref 36 Postischemic administration of CGX-1051, a peptide from cone snail venom, reduces infarct size in both rat and dog models of myocardial ischemia and reperfusion. J Cardiovasc Pharmacol. 2005 Aug;46(2):141-6. doi: 10.1097/01.fjc.0000167015.84715.27.
Ref 37 Why the Drosophila Shaker K+ channel is not a good model for ligand binding to voltage-gated Kv1 channels. Biochemistry. 2013 Mar 5;52(9):1631-40. doi: 10.1021/bi301257p. Epub 2013 Feb 20.
Ref 38 Efficient enzymatic cyclization of an inhibitory cystine knot-containing peptide. Biotechnol Bioeng. 2016 Oct;113(10):2202-12. doi: 10.1002/bit.25993. Epub 2016 Aug 9.
Ref 39 Solution structure and proposed binding mechanism of a novel potassium channel toxin kappa-conotoxin PVIIA. Structure. 1997 Dec 15;5(12):1585-97. doi: 10.1016/s0969-2126(97)00307-9.
Ref 40 Three-dimensional structure of kappa-conotoxin PVIIA, a novel potassium channel-blocking toxin from cone snails. Biochemistry. 1998 Apr 21;37(16):5407-16. doi: 10.1021/bi9730341.
Ref 41 Molecular basis of functional diversity of voltage-gated potassium channels in mammalian brain. EMBO J. 1989 Nov;8(11):3235-44. doi: 10.1002/j.1460-2075.1989.tb08483.x.
Ref 42 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 43 Characterization of Kbot21 Reveals Novel Side Chain Interactions of Scorpion Toxins Inhibiting Voltage-Gated Potassium Channels. PLoS One. 2015 Sep 23;10(9):e0137611. doi: 10.1371/journal.pone.0137611. eCollection 2015.
Ref 44 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 45 Evolution of separate predation- and defence-evoked venoms in carnivorous cone snails. Nat Commun. 2014 Mar 24;5:3521. doi: 10.1038/ncomms4521.
Ref 46 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 47 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 48 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 49 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 50 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 51 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 52 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 53 -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 54 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 55 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 56 Tertiary structure of conotoxin GIIIA in aqueous solution. Biochemistry. 1991 Jul 16;30(28):6908-16. doi: 10.1021/bi00242a014.
Ref 57 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 58 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 59 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 60 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 61 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 62 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 63 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 64 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 65 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 66 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 67 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 68 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 69 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 70 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 71 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 72 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 73 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 74 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 75 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 76 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 77 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 78 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 79 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 80 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 81 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 82 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 83 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 84 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 85 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 86 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 87 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 88 Kbot55, purified from Buthus occitanus tunetanus venom, represents the first member of a novel -KTx subfamily. Peptides. 2016 Jun;80:4-8. doi: 10.1016/j.peptides.2015.05.015. Epub 2015 Jun 14.
Ref 89 PhcrTx2, a New Crab-Paralyzing Peptide Toxin from the Sea Anemone Phymanthus crucifer. Toxins (Basel). 2018 Feb 7;10(2):72. doi: 10.3390/toxins10020072.
Ref 90 Variation of Two S3b Residues in K(V)4.1-4.3 Channels Underlies Their Different Modulations by Spider Toxin -LhTx-1. Front Pharmacol. 2021 Jun 10;12:692076. doi: 10.3389/fphar.2021.692076. eCollection 2021.
Ref 91 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 92 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 93 The first potassium channel toxin from the venom of the Iranian scorpion Odonthobuthus doriae. FEBS Lett. 2006 Nov 13;580(26):6254-8. doi: 10.1016/j.febslet.2006.10.029. Epub 2006 Oct 20.
Ref 94 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 95 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 96 AbeTx1 Is a Novel Sea Anemone Toxin with a Dual Mechanism of Action on Shaker-Type K? Channels Activation. Mar Drugs. 2018 Oct 1;16(10):360. doi: 10.3390/md16100360.
Ref 97 C-Terminal residues in small potassium channel blockers OdK1 and OSK3 from scorpion venom fine-tune the selectivity. Biochim Biophys Acta Proteins Proteom. 2017 May;1865(5):465-472. doi: 10.1016/j.bbapap.2017.02.001. Epub 2017 Feb 4.
Ref 98 Two dyad-free Shaker-type K? channel blockers from scorpion venom. Toxicon. 2012 Mar 1;59(3):402-7. doi: 10.1016/j.toxicon.2011.11.016. Epub 2012 Jan 4.
Ref 99 Structural and Functional Elucidation of Peptide Ts11 Shows Evidence of a Novel Subfamily of Scorpion Venom Toxins. Toxins (Basel). 2016 Sep 30;8(10):288. doi: 10.3390/toxins8100288.
Ref 100 The new kappa-KTx 2.5 from the scorpion Opisthacanthus cayaporum. Peptides. 2011 Jul;32(7):1509-17. doi: 10.1016/j.peptides.2011.05.017. Epub 2011 May 23.
Ref 101 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 102 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 103 The peptide components of bee venom. Eur J Biochem. 1976 Jan 15;61(2):369-76. doi: 10.1111/j.1432-1033.1976.tb10030.x.
Ref 104 Apamin as a selective blocker of the calcium-dependent potassium channel in neuroblastoma cells: voltage-clamp and biochemical characterization of the toxin receptor. Proc Natl Acad Sci U S A. 1982 Feb;79(4):1308-12. doi: 10.1073/pnas.79.4.1308.
Ref 105 Apamin, a blocker of the calcium-activated potassium channel, induces neurodegeneration of Purkinje cells exclusively. Brain Res. 1997 Dec 19;778(2):405-8. doi: 10.1016/s0006-8993(97)01165-7.
Ref 106 Determinants of apamin and d-tubocurarine block in SK potassium channels. J Biol Chem. 1997 Sep 12;272(37):23195-200. doi: 10.1074/jbc.272.37.23195.
Ref 107 Pharmacological characterization of small-conductance Ca(2+)-activated K(+) channels stably expressed in HEK 293 cells. Br J Pharmacol. 2000 Mar;129(5):991-9. doi: 10.1038/sj.bjp.0703120.
Ref 108 SK3 is an important component of K(+) channels mediating the afterhyperpolarization in cultured rat SCG neurones. J Physiol. 2001 Sep 1;535(Pt 2):323-34. doi: 10.1111/j.1469-7793.2001.00323.x.
Ref 109 Apamin interacts with all subtypes of cloned small-conductance Ca2+-activated K+ channels. Pflugers Arch. 2001 Jan;441(4):544-50. doi: 10.1007/s004240000447.
Ref 110 An amino acid outside the pore region influences apamin sensitivity in small conductance Ca2+-activated K+ channels. J Biol Chem. 2007 Feb 9;282(6):3478-86. doi: 10.1074/jbc.M607213200. Epub 2006 Dec 1.
Ref 111 Apamin reduces neuromuscular transmission by activating inhibitory muscarinic M(2) receptors on motor nerve terminals. Eur J Pharmacol. 2010 Jan 25;626(2-3):239-43. doi: 10.1016/j.ejphar.2009.09.064. Epub 2009 Oct 8.
Ref 112 Allosteric block of KCa2 channels by apamin. J Biol Chem. 2010 Aug 27;285(35):27067-27077. doi: 10.1074/jbc.M110.110072. Epub 2010 Jun 18.
Ref 113 The small neurotoxin apamin blocks not only small conductance Ca(2+) activated K(+) channels (SK type) but also the voltage dependent Kv1.3 channel. Eur Biophys J. 2017 Sep;46(6):517-523. doi: 10.1007/s00249-016-1196-0. Epub 2017 Jan 20.
Ref 114 Apamin inhibits TNF-- and IFN--induced inflammatory cytokines and chemokines via suppressions of NF-B signaling pathway and STAT in human keratinocytes. Pharmacol Rep. 2017 Oct;69(5):1030-1035. doi: 10.1016/j.pharep.2017.04.006. Epub 2017 Apr 18.
Ref 115 Apamin Suppresses LPS-Induced Neuroinflammatory Responses by Regulating SK Channels and TLR4-Mediated Signaling Pathways. Int J Mol Sci. 2020 Jun 17;21(12):4319. doi: 10.3390/ijms21124319.
Ref 116 Apamin from bee venom suppresses inflammation in a murine model of gouty arthritis. J Ethnopharmacol. 2020 Jul 15;257:112860. doi: 10.1016/j.jep.2020.112860. Epub 2020 Apr 11.
Ref 117 Antioxidative, Antiapoptotic, and Anti-Inflammatory Effects of Apamin in a Murine Model of Lipopolysaccharide-Induced Acute Kidney Injury. Molecules. 2020 Dec 3;25(23):5717. doi: 10.3390/molecules25235717.
Ref 118 Solution structure of apamin determined by nuclear magnetic resonance and distance geometry. Biochemistry. 1988 Nov 1;27(22):8491-8. doi: 10.1021/bi00422a029.
Ref 119 Binding and toxicity of apamin. Characterization of the active site. Eur J Biochem. 1991 Mar 28;196(3):639-45. doi: 10.1111/j.1432-1033.1991.tb15860.x.
Ref 120 Expression of a new serine protease from Crotalus durissus collilineatus venom in Pichia pastoris and functional comparison with the native enzyme. Appl Microbiol Biotechnol. 2015 Dec;99(23):9971-86. doi: 10.1007/s00253-015-6836-2. Epub 2015 Jul 31.
Ref 121 Functional and biological insights of rCollinein-1, a recombinant serine protease from Crotalus durissus collilineatus. J Venom Anim Toxins Incl Trop Dis. 2019 Apr 8;25:e147118. doi: 10.1590/1678-9199-JVATITD-1471-18. eCollection 2019.
Ref 122 Beyond hemostasis: a snake venom serine protease with potassium channel blocking and potential antitumor activities. Sci Rep. 2020 Mar 11;10(1):4476. doi: 10.1038/s41598-020-61258-x.
Ref 123 Towards toxin PEGylation: The example of rCollinein-1, a snake venom thrombin-like enzyme, as a PEGylated biopharmaceutical prototype. Int J Biol Macromol. 2021 Nov 1;190:564-573. doi: 10.1016/j.ijbiomac.2021.09.004. Epub 2021 Sep 7.
Ref 124 Sunanda, Punnepalli, et al. "Identification, chemical synthesis, structure, and function of a new KV1 channel blocking peptide from Oulactis sp." Peptide Science 110.4 (2018): e24073.
Ref 125 Structure, folding and stability of a minimal homologue from Anemonia sulcata of the sea anemone potassium channel blocker ShK. Peptides. 2018 Jan;99:169-178. doi: 10.1016/j.peptides.2017.10.001. Epub 2017 Oct 6.
Ref 126 Molecular divergence of two orthologous scorpion toxins affecting potassium channels. Comp Biochem Physiol A Mol Integr Physiol. 2011 Jul;159(3):313-21. doi: 10.1016/j.cbpa.2011.03.027. Epub 2011 Apr 3.
Ref 127 A novel toxin from the venom of the scorpion Tityus trivittatus, is the first member of a new alpha-KTX subfamily. FEBS Lett. 2006 Jan 23;580(2):592-6. doi: 10.1016/j.febslet.2005.12.073. Epub 2006 Jan 4.
Ref 128 OdK2, a Kv1.3 channel-selective toxin from the venom of the Iranian scorpion Odonthobuthus doriae. Toxicon. 2008 Jun 15;51(8):1424-30. doi: 10.1016/j.toxicon.2008.03.027. Epub 2008 Mar 29.
Ref 129 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 130 PHAB toxins: a unique family of predatory sea anemone toxins evolving via intra-gene concerted evolution defines a new peptide fold. Cell Mol Life Sci. 2018 Dec;75(24):4511-4524. doi: 10.1007/s00018-018-2897-6. Epub 2018 Aug 14.
Ref 131 AsKC11, a Kunitz Peptide from Anemonia sulcata, Is a Novel Activator of G Protein-Coupled Inward-Rectifier Potassium Channels. Mar Drugs. 2022 Feb 15;20(2):140. doi: 10.3390/md20020140.
Ref 132 Fluorescent protein-scorpion toxin chimera is a convenient molecular tool for studies of potassium channels. Sci Rep. 2016 Sep 21;6:33314. doi: 10.1038/srep33314.
Ref 133 Heteropoda toxin 2 is a gating modifier toxin specific for voltage-gated K+ channels of the Kv4 family. Toxicon. 2005 Mar 15;45(4):431-42. doi: 10.1016/j.toxicon.2004.11.015.
Ref 134 Heteropodatoxins: peptides isolated from spider venom that block Kv4.2 potassium channels. Mol Pharmacol. 1997 Mar;51(3):491-8.
Ref 135 A new sea anemone peptide, APETx2, inhibits ASIC3, a major acid-sensitive channel in sensory neurons. EMBO J. 2004 Apr 7;23(7):1516-25. doi: 10.1038/sj.emboj.7600177. Epub 2004 Mar 25.
Ref 136 ASIC3, a sensor of acidic and primary inflammatory pain. EMBO J. 2008 Nov 19;27(22):3047-55. doi: 10.1038/emboj.2008.213. Epub 2008 Oct 16.
Ref 137 Chemical synthesis and folding of APETx2, a potent and selective inhibitor of acid sensing ion channel 3. Toxicon. 2009 Jul;54(1):56-61. doi: 10.1016/j.toxicon.2009.03.014. Epub 2009 Mar 21.
Ref 138 Expression in Pichia pastoris and characterization of APETx2, a specific inhibitor of acid sensing ion channel 3. Toxicon. 2010 Dec;56(8):1388-97. doi: 10.1016/j.toxicon.2010.08.004. Epub 2010 Sep 9.
Ref 139 Inhibition of voltage-gated Na(+) currents in sensory neurones by the sea anemone toxin APETx2. Br J Pharmacol. 2012 Apr;165(7):2167-77. doi: 10.1111/j.1476-5381.2011.01674.x.
Ref 140 A natural point mutation changes both target selectivity and mechanism of action of sea anemone toxins. FASEB J. 2012 Dec;26(12):5141-51. doi: 10.1096/fj.12-218479. Epub 2012 Sep 12.
Ref 141 Cyclisation increases the stability of the sea anemone peptide APETx2 but decreases its activity at acid-sensing ion channel 3. Mar Drugs. 2012 Jul;10(7):1511-1527. doi: 10.3390/md10071511. Epub 2012 Jul 16.
Ref 142 Functional expression in Escherichia coli of the disulfide-rich sea anemone peptide APETx2, a potent blocker of acid-sensing ion channel 3. Mar Drugs. 2012 Jul;10(7):1605-1618. doi: 10.3390/md10071605. Epub 2012 Jul 23.
Ref 143 Solution structure of APETx2, a specific peptide inhibitor of ASIC3 proton-gated channels. Protein Sci. 2005 Aug;14(8):2003-10. doi: 10.1110/ps.051378905. Epub 2005 Jun 29.
Ref 144 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 145 Purification and characterization of Ts15, the first member of a new -KTX subfamily from the venom of the Brazilian scorpion Tityus serrulatus. Toxicon. 2011 Jul;58(1):54-61. doi: 10.1016/j.toxicon.2011.05.001. Epub 2011 May 13.
Ref 146 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 147 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 148 Moving pieces in a venomic puzzle: unveiling post-translationally modified toxins from Tityus serrulatus. J Proteome Res. 2013 Jul 5;12(7):3460-70. doi: 10.1021/pr4003068. Epub 2013 Jun 13.
Ref 149 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 150 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 151 A bifunctional sea anemone peptide with Kunitz type protease and potassium channel inhibiting properties. Biochem Pharmacol. 2011 Jul 1;82(1):81-90. doi: 10.1016/j.bcp.2011.03.023. Epub 2011 Apr 6.
Ref 152 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 153 Novel structural class of four disulfide-bridged peptides from Tityus serrulatus venom. Biochem Biophys Res Commun. 2003 Feb 21;301(4):1086-92. doi: 10.1016/s0006-291x(03)00082-2.
Ref 154 Tityus serrulatus scorpion venom and toxins: an overview. Protein Pept Lett. 2009;16(8):920-32. doi: 10.2174/092986609788923329.
Ref 155 A Tale of Toxin Promiscuity: The Versatile Pharmacological Effects of Hcr 1b-2 Sea Anemone Peptide on Voltage-Gated Ion Channels. Mar Drugs. 2022 Feb 17;20(2):147. doi: 10.3390/md20020147.
Ref 156 First report on BaltCRP, a cysteine-rich secretory protein (CRISP) from Bothrops alternatus venom: Effects on potassium channels and inflammatory processes. Int J Biol Macromol. 2019 Nov 1;140:556-567. doi: 10.1016/j.ijbiomac.2019.08.108. Epub 2019 Aug 14.
Ref 157 Structural similarity between defense peptide from wheat and scorpion neurotoxin permits rational functional design. J Biol Chem. 2014 May 16;289(20):14331-40. doi: 10.1074/jbc.M113.530477. Epub 2014 Mar 26.
Ref 158 Experimental conversion of a defensin into a neurotoxin: implications for origin of toxic function. Mol Biol Evol. 2014 Mar;31(3):546-59. doi: 10.1093/molbev/msu038. Epub 2014 Jan 14.
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.