Target Information

General Information of This Target
Target ID
BTDT00069
Target Name
Potassium voltage-gated channel subfamily A member 5 (KCNA5)
Target Bioclass
Transporter and channel
Uniprot ID
P22460
3D Structure
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2D Sequence
3D Structure
Source
Predict by Alphafold2
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Alphafold Parameters: msa_mode: mmseqs2_uniref_env model_type: auto num_recycles: auto
Gene Name
KCNA5
Gene ID
3741
Synonym
HPCN1; Voltage-gated potassium channel HK2; Voltage-gated potassium channel subunit Kv1.5
Sequence
MEIALVPLENGGAMTVRGGDEARAGCGQATGGELQCPPTAGLSDGPKEPAPKGRGAQRDA
DSGVRPLPPLPDPGVRPLPPLPEELPRPRRPPPEDEEEEGDPGLGTVEDQALGTASLHHQ
RVHINISGLRFETQLGTLAQFPNTLLGDPAKRLRYFDPLRNEYFFDRNRPSFDGILYYYQ
SGGRLRRPVNVSLDVFADEIRFYQLGDEAMERFREDEGFIKEEEKPLPRNEFQRQVWLIF
EYPESSGSARAIAIVSVLVILISIITFCLETLPEFRDERELLRHPPAPHQPPAPAPGANG
SGVMAPPSGPTVAPLLPRTLADPFFIVETTCVIWFTFELLVRFFACPSKAGFSRNIMNII
DVVAIFPYFITLGTELAEQQPGGGGGGQNGQQAMSLAILRVIRLVRVFRIFKLSRHSKGL
QILGKTLQASMRELGLLIFFLFIGVILFSSAVYFAEADNQGTHFSSIPDAFWWAVVTMTT
VGYGDMRPITVGGKIVGSLCAIAGVLTIALPVPVIVSNFNYFYHRETDHEEPAVLKEEQG
TQSQGPGLDRGVQRKVSGSRGSFCKAGGTLENADSARRGSCPLEKCNVKAKSNVDLRRSL
YALCLDTSRETDL

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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. Homotetrameric channels display rapid activation and slow inactivation. May play a role in regulating the secretion of insulin in normal pancreatic islets. Isoform 2 exhibits a voltage-dependent recovery from inactivation and an excessive cumulative inactivation.

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Taxonomy ID
9606
TCDB ID
1.A.1.2.4
        Click to Show/Hide the Complete Species Lineage
Kingdom: Metazoa
Phylum: Chordata
Class: Mammalia
Order: Primates
Family: Hominidae
Genus: Homo
Species: Homo sapiens
Toxin Information Related to This Target
                           Toxin Name Activity Data Type Activity Data Reference
 Toxin Info    Uro (K25A) . . [1]
 Toxin Info    Toxin TdK3 . . [1]
 Toxin Info    Potassium channel toxin alpha-KTx 2.1 Dissociation constant
>25 nM
 [2], [3], [4], [5]
 Toxin Info    OsK1 (R12P,E16K,K20D) Inhibition rate . [6]
 Toxin Info    OsK1 (E16K,K20D,T36Y) Inhibition rate . [6]
 Toxin Info    OsK1 (E16K) Inhibition rate . [6]
 Toxin Info    Potassium channel toxin ShK ([Ppa][AEEA],M21[Nle]) Inhibition rate . [10]
 Toxin Info    Potassium channel toxin ShK ([pTyr][AEEA]) Inhibition rate . [11]
 Toxin Info    Potassium channel toxin ShK (M21M[Dap]) Inhibition rate . [12]
 Toxin Info    Toxin II.10.4 (T7P,D9Q) Inhibition rate . [13]
 Toxin Info    OsK1 (E14A,K18D) Inhibition rate . [14]
 Toxin Info    OsK1 (E15A,K19D) Inhibition rate . [14]
 Toxin Info    Neurotoxin HsTX1 Inhibition rate . [15]
 Toxin Info    Neurotoxin HsTX1 (A14R,C19[Abu],C34[Abu]) Inhibition rate . [16]
 Toxin Info    Beta/omega-theraphotoxin-Tp2a Inhibition rate . [17- 36]
 Toxin Info    Kappa-conotoxin RIIIK Inhibition rate . [37]
 Toxin Info    Kappa-stichotoxin-She3a Inhibition rate . [12]
 Toxin Info    Kunitz-type conkunitzin-S1 Inhibition rate . [38], [39], [40]
 Toxin Info    Potassium channel toxin alpha-KTx 4.6 Inhibition rate . [41]
 Toxin Info    Potassium channel toxin alpha-KTx 4.8 Inhibition rate . [42]
 Toxin Info    Peptide 2 Inhibition rate . [43]
 Toxin Info    Mu-conotoxin GIIIA Inhibition rate . [44- 56]
 Toxin Info    Mu-conotoxin PIIIA Inhibition rate . [45- 61]
 Toxin Info    Mu-conotoxin SIIIA Inhibition rate . [52- 86]
 Toxin Info    Potassium channel toxin alpha-KTx 2.1 Inhibition rate . [4]
 Toxin Info    Potassium channel toxin alpha-KTx 6.3 Inhibition rate . [16]
 Toxin Info    Kappa-LhTx-1 Inhibition rate . [87]
 Toxin Info    Potassium channel toxin alpha-KTx 32.1 Inhibition rate . [88]
 Toxin Info    Potassium channel toxin alpha-KTx 6.21 Inhibition rate . [89]
 Toxin Info    Toxin VmKTx1 Inhibition rate . [90]
 Toxin Info    Potassium channel toxin alpha-KTx 23.1 Inhibition rate . [43- 91]
 Toxin Info    Potassium channel toxin alpha-KTx 3.7 Inhibition rate . [6]
 Toxin Info    Kappa-theraphotoxin-Pg1a Inhibition rate . [92], [93], [94], [95]
 Toxin Info    Potassium channel toxin alpha-KTx 2.13 Inhibition rate . [96]
 Toxin Info    Potassium channel toxin ShK ([pTyr][AEEA]) Inhibition rate . [10]
 Toxin Info    OsK1 (E16K,K20D) Inhibition rate . [6]
 Toxin Info    [D20]- OsK1 Inhibition rate . [6]
 Toxin Info    Conorfamide-Sr3 Inhibition rate
5 %
 [97]
 Toxin Info    Beta/omega-theraphotoxin-Tp1a Inhibition rate
7 %
 [17- 101]
 Toxin Info    Kappa-lycotoxin-Os1a Inhibition rate
10 %
 [102]
 Toxin Info    Kappa-actitoxin-Ael2e Inhibition rate
17 %
 [103]
 Toxin Info    Kappa-conotoxin RIIIJ IC50
70 μM
 [37]
References
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Ref 2 Charybdotoxin and noxiustoxin, two homologous peptide inhibitors of the K+ (Ca2+) channel. FEBS Lett. 1988 Jan 4;226(2):280-4. doi: 10.1016/0014-5793(88)81439-x.
Ref 3 Synthetic peptides corresponding to the sequence of noxiustoxin indicate that the active site of this K+ channel blocker is located on its amino-terminal portion. J Neural Transm. 1989;77(1):11-20. doi: 10.1007/BF01255815.
Ref 4 Pharmacological characterization of five cloned voltage-gated K+ channels, types Kv1.1, 1.2, 1.3, 1.5, and 3.1, stably expressed in mammalian cell lines. Mol Pharmacol. 1994 Jun;45(6):1227-34.
Ref 5 Determination of the three-dimensional solution structure of noxiustoxin: analysis of structural differences with related short-chain scorpion toxins. Biochemistry. 1995 Dec 26;34(51):16563-73. doi: 10.1021/bi00051a004.
Ref 6 K+ channel types targeted by synthetic OSK1, a toxin from Orthochirus scrobiculosus scorpion venom. Biochem J. 2005 Jan 1;385(Pt 1):95-104. doi: 10.1042/BJ20041379.
Ref 7 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 8 Letter: An anti-inflammatory peptide from bee venom. Nature. 1973 Sep 21;245(5421):163-4. doi: 10.1038/245163a0.
Ref 9 Mast cell degranulating peptide: a multi-functional neurotoxin. J Pharm Pharmacol. 1990 Jul;42(7):457-61. doi: 10.1111/j.2042-7158.1990.tb06595.x.
Ref 10 Engineering a stable and selective peptide blocker of the Kv1.3 channel in T lymphocytes. Mol Pharmacol. 2009 Apr;75(4):762-73. doi: 10.1124/mol.108.052704. Epub 2009 Jan 2.
Ref 11 Targeting effector memory T cells with a selective peptide inhibitor of Kv1.3 channels for therapy of autoimmune diseases. Mol Pharmacol. 2005 Apr;67(4):1369-81. doi: 10.1124/mol.104.008193. Epub 2005 Jan 21.
Ref 12 ShK-Dap22, a potent Kv1.3-specific immunosuppressive polypeptide. J Biol Chem. 1998 Dec 4;273(49):32697-707. doi: 10.1074/jbc.273.49.32697.
Ref 13 Cobatoxin 1 from Centruroides noxius scorpion venom: chemical synthesis, three-dimensional structure in solution, pharmacology and docking on K+ channels. Biochem J. 2004 Jan 1;377(Pt 1):37-49. doi: 10.1042/BJ20030977.
Ref 14 Pharmacological profiling of Orthochirus scrobiculosus toxin 1 analogs with a trimmed N-terminal domain. Mol Pharmacol. 2006 Jan;69(1):354-62. doi: 10.1124/mol.105.017210. Epub 2005 Oct 18.
Ref 15 A Fluorescent Peptide Toxin for Selective Visualization of the Voltage-Gated Potassium Channel K(V)1.3. Bioconjug Chem. 2022 Nov 16;33(11):2197-2212. doi: 10.1021/acs.bioconjchem.2c00436. Epub 2022 Nov 4.
Ref 16 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 17 Two tarantula peptides inhibit activation of multiple sodium channels. Biochemistry. 2002 Dec 17;41(50):14734-47. doi: 10.1021/bi026546a.
Ref 18 Differential phospholipid binding by site 3 and site 4 toxins. Implications for structural variability between voltage-sensitive sodium channel domains. J Biol Chem. 2005 Mar 25;280(12):11127-33. doi: 10.1074/jbc.M412552200. Epub 2005 Jan 4.
Ref 19 Molecular interactions of the gating modifier toxin ProTx-II with NaV 1.5: implied existence of a novel toxin binding site coupled to activation. J Biol Chem. 2007 Apr 27;282(17):12687-97. doi: 10.1074/jbc.M610462200. Epub 2007 Mar 5.
Ref 20 ProTx-I and ProTx-II: gating modifiers of voltage-gated sodium channels. Toxicon. 2007 Feb;49(2):194-201. doi: 10.1016/j.toxicon.2006.09.014. Epub 2006 Sep 27.
Ref 21 Inhibition of sodium channel gating by trapping the domain II voltage sensor with protoxin II. Mol Pharmacol. 2008 Mar;73(3):1020-8. doi: 10.1124/mol.107.041046. Epub 2007 Dec 21.
Ref 22 ProTx-II, a selective inhibitor of NaV1.7 sodium channels, blocks action potential propagation in nociceptors. Mol Pharmacol. 2008 Nov;74(5):1476-84. doi: 10.1124/mol.108.047670. Epub 2008 Aug 26.
Ref 23 Evidence for multiple effects of ProTxII on activation gating in Na(V)1.5. Toxicon. 2008 Sep 1;52(3):489-500. doi: 10.1016/j.toxicon.2008.06.023. Epub 2008 Jul 9.
Ref 24 The tarantula toxins ProTx-II and huwentoxin-IV differentially interact with human Nav1.7 voltage sensors to inhibit channel activation and inactivation. Mol Pharmacol. 2010 Dec;78(6):1124-34. doi: 10.1124/mol.110.066332. Epub 2010 Sep 20.
Ref 25 Inhibition of the activation pathway of the T-type calcium channel Ca(V)3.1 by ProTxII. Toxicon. 2010 Sep 15;56(4):624-36. doi: 10.1016/j.toxicon.2010.06.009. Epub 2010 Jun 23.
Ref 26 Crystallographic insights into sodium-channel modulation by the 4 subunit. Proc Natl Acad Sci U S A. 2013 Dec 17;110(51):E5016-24. doi: 10.1073/pnas.1314557110. Epub 2013 Dec 2.
Ref 27 Block of T-type calcium channels by protoxins I and II. Mol Brain. 2014 May 9;7:36. doi: 10.1186/1756-6606-7-36.
Ref 28 High Proteolytic Resistance of Spider-Derived Inhibitor Cystine Knots. Int J Pept. 2015;2015:537508. doi: 10.1155/2015/537508. Epub 2015 Dec 30.
Ref 29 Engineering potent and selective analogues of GpTx-1, a tarantula venom peptide antagonist of the Na(V)1.7 sodium channel. J Med Chem. 2015 Mar 12;58(5):2299-314. doi: 10.1021/jm501765v. Epub 2015 Feb 19.
Ref 30 Binary architecture of the Nav1.2-2 signaling complex. Elife. 2016 Feb 19;5:e10960. doi: 10.7554/eLife.10960.
Ref 31 Insensitivity to pain induced by a potent selective closed-state Nav1.7 inhibitor. Sci Rep. 2017 Jan 3;7:39662. doi: 10.1038/srep39662.
Ref 32 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 33 Studies examining the relationship between the chemical structure of protoxin II and its activity on voltage gated sodium channels. J Med Chem. 2014 Aug 14;57(15):6623-31. doi: 10.1021/jm500687u. Epub 2014 Jul 24.
Ref 34 Interaction of Tarantula Venom Peptide ProTx-II with Lipid Membranes Is a Prerequisite for Its Inhibition of Human Voltage-gated Sodium Channel NaV1.7. J Biol Chem. 2016 Aug 12;291(33):17049-65. doi: 10.1074/jbc.M116.729095. Epub 2016 Jun 16.
Ref 35 Structural Basis of Nav1.7 Inhibition by a Gating-Modifier Spider Toxin. Cell. 2019 Feb 7;176(4):702-715.e14. doi: 10.1016/j.cell.2018.12.018. Epub 2019 Jan 17.
Ref 36 Structures of human Na(v)1.7 channel in complex with auxiliary subunits and animal toxins. Science. 2019 Mar 22;363(6433):1303-1308. doi: 10.1126/science.aaw2493. Epub 2019 Feb 14.
Ref 37 Biochemical characterization of kappaM-RIIIJ, a Kv1.2 channel blocker: evaluation of cardioprotective effects of kappaM-conotoxins. J Biol Chem. 2010 May 14;285(20):14882-14889. doi: 10.1074/jbc.M109.068486. Epub 2010 Mar 10.
Ref 38 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 39 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 40 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 41 Tst26, a novel peptide blocker of Kv1.2 and Kv1.3 channels from the venom of Tityus stigmurus. Toxicon. 2009 Sep 15;54(4):379-89. doi: 10.1016/j.toxicon.2009.05.023. Epub 2009 Jun 3.
Ref 42 Characterization and Chemical Synthesis of Cm39 (-KTx 4.8): A Scorpion Toxin That Inhibits Voltage-Gated K(+) Channel K(V)1.2 and Small- and Intermediate-Conductance Ca(2+)-Activated K(+) Channels K(Ca)2.2 and K(Ca)3.1. Toxins (Basel). 2023 Jan 5;15(1):41. doi: 10.3390/toxins15010041.
Ref 43 Vm24, a natural immunosuppressive peptide, potently and selectively blocks Kv1.3 potassium channels of human T cells. Mol Pharmacol. 2012 Sep;82(3):372-82. doi: 10.1124/mol.112.078006. Epub 2012 May 23.
Ref 44 Evolution of separate predation- and defence-evoked venoms in carnivorous cone snails. Nat Commun. 2014 Mar 24;5:3521. doi: 10.1038/ncomms4521.
Ref 45 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 46 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 47 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 48 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 49 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 50 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 51 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 52 -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 53 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 54 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 55 Tertiary structure of conotoxin GIIIA in aqueous solution. Biochemistry. 1991 Jul 16;30(28):6908-16. doi: 10.1021/bi00242a014.
Ref 56 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 57 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 58 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 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.
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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.
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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.
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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 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 88 Cm28, a scorpion toxin having a unique primary structure, inhibits KV1.2 and KV1.3 with high affinity. J Gen Physiol. 2022 Aug 1;154(8):e202213146. doi: 10.1085/jgp.202213146. Epub 2022 Jun 14.
Ref 89 Structure, molecular modeling, and function of the novel potassium channel blocker urotoxin isolated from the venom of the Australian scorpion Urodacus yaschenkoi. Mol Pharmacol. 2014 Jul;86(1):28-41. doi: 10.1124/mol.113.090183. Epub 2014 Apr 10.
Ref 90 sVmKTx, a transcriptome analysis-based synthetic peptide analogue of Vm24, inhibits Kv1.3 channels of human T cells with improved selectivity. Biochem Pharmacol. 2022 May;199:115023. doi: 10.1016/j.bcp.2022.115023. Epub 2022 Mar 28.
Ref 91 Structure, function, and chemical synthesis of Vaejovis mexicanus peptide 24: a novel potent blocker of Kv1.3 potassium channels of human T lymphocytes. Biochemistry. 2012 May 15;51(19):4049-61. doi: 10.1021/bi300060n. Epub 2012 May 7.
Ref 92 Blockers of the delayed-rectifier potassium current in pancreatic beta-cells enhance glucose-dependent insulin secretion. Diabetes. 2006 Apr;55(4):1034-42. doi: 10.2337/diabetes.55.04.06.db05-0788.
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