2023
Pain-causing stinging nettle toxins target TMEM233 to modulate NaV1.7 function
Jami S, Deuis J, Klasfauseweh T, Cheng X, Kurdyukov S, Chung F, Okorokov A, Li S, Zhang J, Cristofori-Armstrong B, Israel M, Ju R, Robinson S, Zhao P, Ragnarsson L, Andersson Å, Tran P, Schendel V, McMahon K, Tran H, Chin Y, Zhu Y, Liu J, Crawford T, Purushothamvasan S, Habib A, Andersson D, Rash L, Wood J, Zhao J, Stehbens S, Mobli M, Leffler A, Jiang D, Cox J, Waxman S, Dib-Hajj S, Neely G, Durek T, Vetter I. Pain-causing stinging nettle toxins target TMEM233 to modulate NaV1.7 function. Nature Communications 2023, 14: 2442. PMID: 37117223, PMCID: PMC10147923, DOI: 10.1038/s41467-023-37963-2.Peer-Reviewed Original ResearchConceptsSensory neuronsVoltage-sensing domainNav channelsTransmembrane proteinAccessory proteinsVoltage-gated sodium channelsCritical regulatorPore domainChannel gatingExtracellular loopToxin-mediated effectsNeuronal excitabilityPeptide toxinsProteinSodium channelsPharmacological activitiesNav1.7 functionKnottin peptidesNeuronsImportant insightsToxinSubunitsRegulatorDomainExcelsa
2018
Molecular mechanism underlying the subtype-selectivity of competitive inhibitor NF110 and its distinct potencies in human and rat P2X3 receptors
Li B, Wang J, Cheng X, Liu Y, Yang Y, Yang X, Guo C, Niu Y, Cao P, Lu X, Zhu M, Tian Y, Yu Y. Molecular mechanism underlying the subtype-selectivity of competitive inhibitor NF110 and its distinct potencies in human and rat P2X3 receptors. Science Bulletin 2018, 63: 1616-1625. PMID: 36658853, DOI: 10.1016/j.scib.2018.11.016.Peer-Reviewed Original ResearchP2X3 receptorsP2X receptorsExperimental animalsDifferent P2X receptorsLower bodyRat P2X3 receptorsDistinct potenciesSubtype-selective mannerHuman P2X3 receptorsLF domainInhibitors/modulatorsPreclinical dataClinical trialsAmino acidsEquivalent amino acidsATP-binding pocketClinical researchExtracellular ATPSubstitution of residuesReceptorsCation channelsPharmacological activitiesDorsal fin domainInhibitory efficacyChannel activity