2018
Druggable negative allosteric site of P2X3 receptors
Wang J, Wang Y, Cui W, Huang Y, Yang Y, Liu Y, Zhao W, Cheng X, Sun W, Cao P, Zhu M, Wang R, Hattori M, Yu Y. Druggable negative allosteric site of P2X3 receptors. Proceedings Of The National Academy Of Sciences Of The United States Of America 2018, 115: 4939-4944. PMID: 29674445, PMCID: PMC5948998, DOI: 10.1073/pnas.1800907115.Peer-Reviewed Original ResearchMeSH KeywordsAllosteric RegulationCrystallography, X-RayHEK293 CellsHumansModels, MolecularPhenyl EthersProtein DomainsPyrimidinesReceptors, Purinergic P2X3SulfonamidesConceptsAllosteric siteNegative allosteric siteDruggable allosteric sitesG protein-coupled receptorsAllosteric modulationLeft flipperProtein-coupled receptorsNew drug targetsDorsal fin domainLB domainsClinical trialsP2X receptorsAllosteric changesAllosteric inhibitorsChannel mutantsDrug targetsPhase II clinical trialFunctional studiesFin domainRefractory chronic coughIdiopathic pulmonary fibrosisIon channelsLower bodyX-ray crystallographyNegative allosteric modulation
2014
Relative motions between left flipper and dorsal fin domains favour P2X4 receptor activation
Zhao W, Wang J, Ma X, Yang Y, Liu Y, Huang L, Fan Y, Cheng X, Chen H, Wang R, Yu Y. Relative motions between left flipper and dorsal fin domains favour P2X4 receptor activation. Nature Communications 2014, 5: 4189. PMID: 24943126, DOI: 10.1038/ncomms5189.Peer-Reviewed Original ResearchConceptsAllosteric changesChannel gatingLeft flipperP2X4 receptorDorsal fin domainAllosteric eventsP2X4 receptor activationPhysiological functionsResidues leadFin domainHydrophobic interactionsEssential roleExtracellular ATPFundamental processesZinc bridgesChannel activationReceptor activationDorsal finP2X receptorsReceptorsGatingDomainActivationL217V291Inherent Dynamics of Head Domain Correlates with ATP-Recognition of P2X4 Receptors: Insights Gained from Molecular Simulations
Huang L, Fan Y, Tian Y, Yang Y, Liu Y, Wang J, Zhao W, Zhou W, Cheng X, Cao P, Lu X, Yu Y. Inherent Dynamics of Head Domain Correlates with ATP-Recognition of P2X4 Receptors: Insights Gained from Molecular Simulations. PLOS ONE 2014, 9: e97528. PMID: 24878662, PMCID: PMC4039465, DOI: 10.1371/journal.pone.0097528.Peer-Reviewed Original Research
2000
Biphasic modulation of ryanodine binding to sarcoplasmic reticulum vesicles of skeletal muscle by Zn2+ ions
XIA R, CHENG X, Hui W, CHEN K, WEI Q, ZHANG X, ZHU P. Biphasic modulation of ryanodine binding to sarcoplasmic reticulum vesicles of skeletal muscle by Zn2+ ions. Biochemical Journal 2000, 345: 279-286. PMID: 10620505, PMCID: PMC1220757, DOI: 10.1042/bj3450279.Peer-Reviewed Original ResearchConceptsSarcoplasmic reticulum vesiclesReticulum vesiclesBiphasic modulationSkeletal muscle ryanodine receptorPeak bindingInhibitory effectMuscle ryanodine receptorHeavy sarcoplasmic reticulum vesiclesSkeletal muscleScatchard analysisRyanodine receptorBiphasic time courseRyanodine bindingTime courseMicroMThiol-reducing agentsPhysiological significanceInactivation site