2019
Altered allostery of the left flipper domain underlies the weak ATP response of rat P2X5 receptors
Sun L, Liu Y, Wang J, Huang L, Yang Y, Cheng X, Fan Y, Zhu M, Liang H, Tian Y, Wang H, Guo C, Yu Y. Altered allostery of the left flipper domain underlies the weak ATP response of rat P2X5 receptors. Journal Of Biological Chemistry 2019, 294: 19589-19603. PMID: 31727741, PMCID: PMC6926468, DOI: 10.1074/jbc.ra119.009959.Peer-Reviewed Original ResearchConceptsFuture transgenic studiesFull-length variantATP responseTransmembrane domainTransgenic studiesMammalian speciesP2X5 receptorsAllosteryPathological functionsSingle replacementSingle-channel recordingsSkeletal muscleExon 10Molecular modelingFunctional subtypesATPResiduesNervous systemP2X5ReceptorsDomainMammalsSpeciesTM2Lack of knowledge
2002
Effect of Zinc Ions on Caffeine-Induced Contracture in Vascular Smooth Muscle and Skeletal Mu-scle of Rat
Cheng X, Chen K, Zhang X, Zhu P. Effect of Zinc Ions on Caffeine-Induced Contracture in Vascular Smooth Muscle and Skeletal Mu-scle of Rat. Cellular Physiology And Biochemistry 2002, 12: 119-126. PMID: 12077557, DOI: 10.1159/000063788.Peer-Reviewed Original ResearchConceptsVascular smooth muscleSmooth muscleCaffeine contractureCaffeine exposureSkeletal muscleCaffeine-induced contracturesDose-dependent mannerAortic stripsContractureIntracellular Ca2MuscleActivation dependenceMin intervalsRatsCaffeine concentrationsDepressionExposureMicroMPossible mechanismPotentiationSmall bundles
2001
Inhibition of Ryanodine Binding to Sarcoplasmic Reticulum Vesicles of Cardiac Muscle by Zn2+ Ions
Wang H, Wei Q, Cheng X, Chen K, Zhu P. Inhibition of Ryanodine Binding to Sarcoplasmic Reticulum Vesicles of Cardiac Muscle by Zn2+ Ions. Cellular Physiology And Biochemistry 2001, 11: 83-92. PMID: 11275686, DOI: 10.1159/000047795.Peer-Reviewed Original ResearchConceptsInhibitory effectCardiac muscleModulators of RyRSarcoplasmic reticulumSkeletal muscleSarcoplasmic reticulum vesiclesMuscleScatchard analysisRyanodine receptorRyanodine bindingRyRsThiol-reducing agentsPhysiological significanceReticulum vesiclesHill coefficientObvious changeActivation siteMM dithiothreitol
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