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 insightsToxinSubunitsRegulatorDomainExcelsaVoltage-gated sodium channels (Na<sub>V</sub>) in GtoPdb v.2023.1
Catterall W, Goldin A, Waxman S. Voltage-gated sodium channels (NaV) in GtoPdb v.2023.1. IUPHAR/BPS Guide To Pharmacology CITE 2023, 2023 DOI: 10.2218/gtopdb/f82/2023.1.Peer-Reviewed Original ResearchTransmembrane segmentsLarge extracellular N-terminal domainSingle transmembrane segmentPotassium channel structureShort cytoplasmic domainFourth transmembrane segmentN-terminal domainExtracellular N-terminal domainSodium channelsMost excitable cellsNC-IUPHAR SubcommitteeGlutamate side chainCytoplasmic domainFatty acyl chainsHomologous domainsNovel structural featuresVoltage-gated sodium channelsShort selectivity filterSodium-selective ion channelsΒ-subunitChannel gatingSelectivity filterIon channelsSubunitsPore region
2021
Voltage-gated sodium channels (Na<sub>V</sub>) in GtoPdb v.2021.3
Catterall W, Goldin A, Waxman S. Voltage-gated sodium channels (NaV) in GtoPdb v.2021.3. IUPHAR/BPS Guide To Pharmacology CITE 2021, 2021 DOI: 10.2218/gtopdb/f82/2021.3.Peer-Reviewed Original ResearchTransmembrane segmentsLarge extracellular N-terminal domainSingle transmembrane segmentPotassium channel structureShort cytoplasmic domainFourth transmembrane segmentN-terminal domainExtracellular N-terminal domainSodium channelsMost excitable cellsNC-IUPHAR SubcommitteeGlutamate side chainCytoplasmic domainFatty acyl chainsHomologous domainsNovel structural featuresVoltage-gated sodium channelsShort selectivity filterSodium-selective ion channelsΒ-subunitChannel gatingSelectivity filterIon channelsSubunitsPore region
2019
Voltage-gated sodium channels (version 2019.4) in the IUPHAR/BPS Guide to Pharmacology Database
Catterall W, Goldin A, Waxman S. Voltage-gated sodium channels (version 2019.4) in the IUPHAR/BPS Guide to Pharmacology Database. IUPHAR/BPS Guide To Pharmacology CITE 2019, 2019 DOI: 10.2218/gtopdb/f82/2019.4.Peer-Reviewed Original ResearchTransmembrane segmentsLarge extracellular N-terminal domainSingle transmembrane segmentPotassium channel structureShort cytoplasmic domainFourth transmembrane segmentN-terminal domainExtracellular N-terminal domainSodium channelsMost excitable cellsNC-IUPHAR SubcommitteeGlutamate side chainCytoplasmic domainFatty acyl chainsHomologous domainsNovel structural featuresShort selectivity filterVoltage-gated sodium channelsSodium-selective ion channelsΒ-subunitChannel gatingSelectivity filterIUPHAR/BPS GuideIon channelsSubunits