2019
Podocyte histone deacetylase activity regulates murine and human glomerular diseases
Inoue K, Gan G, Ciarleglio M, Zhang Y, Tian X, Pedigo CE, Cavanaugh C, Tate J, Wang Y, Cross E, Groener M, Chai N, Wang Z, Justice A, Zhang Z, Parikh CR, Wilson FP, Ishibe S. Podocyte histone deacetylase activity regulates murine and human glomerular diseases. Journal Of Clinical Investigation 2019, 129: 1295-1313. PMID: 30776024, PMCID: PMC6391095, DOI: 10.1172/jci124030.Peer-Reviewed Original ResearchConceptsEarly growth response 1Histone deacetylase 1Proteinuric patientsKidney diseaseHDAC2 activityValproic acidVeterans Aging Cohort StudyEnd-stage kidney diseaseDegree of proteinuriaGlomerular filtration rateAging Cohort StudyInhibition of HDAC1Proteinuric kidney diseaseHuman glomerular diseasesGlomerular disease modelsConnectivity Map databaseCohort studyFiltration rateGlomerular diseaseHistone deacetylase activityProteinuric kidneysHDAC inhibitorsProteinuriaMRNA expressionGenetic ablation
2011
Intracellular energy status regulates activity in hypocretin/orexin neurones: a link between energy and behavioural states
Liu Z, Gan G, Suyama S, Gao X. Intracellular energy status regulates activity in hypocretin/orexin neurones: a link between energy and behavioural states. The Journal Of Physiology 2011, 589: 4157-4166. PMID: 21727218, PMCID: PMC3180576, DOI: 10.1113/jphysiol.2011.212514.Peer-Reviewed Original Research
2008
Lysine-Rich Extracellular Rings Formed by hβ2 Subunits Confer the Outward Rectification of BK Channels
Chen M, Gan G, Wu Y, Wang L, Wu Y, Ding J. Lysine-Rich Extracellular Rings Formed by hβ2 Subunits Confer the Outward Rectification of BK Channels. PLOS ONE 2008, 3: e2114. PMID: 18461166, PMCID: PMC2346552, DOI: 10.1371/journal.pone.0002114.Peer-Reviewed Original ResearchAmino Acid SequenceAnimalsCalciumCharybdotoxinEpitopesLarge-Conductance Calcium-Activated Potassium Channel alpha SubunitsLarge-Conductance Calcium-Activated Potassium Channel beta SubunitsLarge-Conductance Calcium-Activated Potassium ChannelsLysinePatch-Clamp TechniquesPeptide FragmentsPotassiumProtein SubunitsStatic Electricity
2007
Four-turn α-Helical Segment Prevents Surface Expression of the Auxiliary hβ2 Subunit of BK-type Channel*
Lv C, Chen M, Gan G, Wang L, Xu T, Ding J. Four-turn α-Helical Segment Prevents Surface Expression of the Auxiliary hβ2 Subunit of BK-type Channel*. Journal Of Biological Chemistry 2007, 283: 2709-2715. PMID: 17991741, DOI: 10.1074/jbc.m704440200.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsCell LineEndoplasmic ReticulumGene ExpressionHumansLarge-Conductance Calcium-Activated Potassium ChannelsMicroscopy, FluorescenceModels, MolecularMolecular Sequence DataMutagenesis, Site-DirectedPatch-Clamp TechniquesProtein Structure, SecondaryProtein SubunitsRatsRecombinant Fusion ProteinsSequence Homology, Amino AcidConceptsBK-type channelsSurface expressionRat chromaffin cellsExtracellular loopPancreatic beta cellsTrafficking mechanismsN-terminusDRG neuronsHelical segmentsToxin sensitivityBeta cellsClamp techniqueHelp of immunofluorescenceAuxiliary beta subunitsAlpha-helical segmentsChromaffin cellsBeta2 subunitBK channelsHbeta2Retention signalChannel regulatorRegulatory mechanismsBeta subunitEndoplasmic reticulumLarge conductanceMolecular cloning and electrophysiological studies on the first K+ channel toxin (LmKTx8) derived from scorpion Lychas mucronatus
Wu W, Yin S, Ma Y, Wu Y, Zhao R, Gan G, Ding J, Cao Z, Li W. Molecular cloning and electrophysiological studies on the first K+ channel toxin (LmKTx8) derived from scorpion Lychas mucronatus. Peptides 2007, 28: 2306-2312. PMID: 18006119, DOI: 10.1016/j.peptides.2007.10.009.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBase SequenceCell LineCloning, MolecularDNA PrimersDNA, ComplementaryElectrophysiologyHumansKv1.3 Potassium ChannelModels, MolecularMolecular Sequence DataMolecular WeightPatch-Clamp TechniquesPotassium Channel BlockersRecombinant Fusion ProteinsScorpion VenomsScorpionsSequence Homology, Amino AcidSpectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
2006
Residue Phe266 in S5-S6 loop is not critical for Charybdotoxin binding to Ca2+-activated K+ (mSlo1) channels
Yao J, Li H, Gan G, Wu Y, Ding J. Residue Phe266 in S5-S6 loop is not critical for Charybdotoxin binding to Ca2+-activated K+ (mSlo1) channels. Acta Pharmacologica Sinica 2006, 27: 945-949. PMID: 16787581, DOI: 10.1111/j.1745-7254.2006.00385.x.Peer-Reviewed Original Research