2022
PP1cβ dephosphorylates cardiac myosin by MYPT‐dependent and independent mechanisms
Lee E, Liu Z, Nguyen N, Nairn A, Chang A. PP1cβ dephosphorylates cardiac myosin by MYPT‐dependent and independent mechanisms. The FASEB Journal 2022, 36 DOI: 10.1096/fasebj.2022.36.s1.r3877.Peer-Reviewed Original ResearchMyosin light chain phosphataseRegulatory light chainCardiac myosinSmooth muscleNormal cardiac functionMain catalytic subunitSmooth muscle contractionMyosin light chain kinaseMyosin phosphatase targetCardiac functionPP1cβLight chain kinaseCatalytic subunitAccessory subunitsConstitutive phosphorylationProtein stabilityLight chain phosphataseKnockout animalsMuscle contractionMuscle pathogenesisConditional knockoutCardiac muscle myosinCardiac myocytesCardiac musclePhosphatase activity
2018
Structural and biochemical insights into inhibition of human primase by citrate
Lee JG, Park KR, An JY, Kang JY, Shen H, Wang J, Eom SH. Structural and biochemical insights into inhibition of human primase by citrate. Biochemical And Biophysical Research Communications 2018, 507: 383-388. PMID: 30446220, DOI: 10.1016/j.bbrc.2018.11.047.Peer-Reviewed Original ResearchConceptsDNA replicationSmall catalytic subunitShort RNA segmentReplicative DNA polymerasesPhosphate binding siteMammalian chromosomesReplication forksCatalytic subunitAccessory subunitsBiochemical insightsOkazaki fragmentsRNA primersKey regulatorRNA segmentsBacterial enzymesHuman primasePrimaseDNA templateBase pairsDNA polymeraseInactive formDNA strandsBinding sitesPolymeraseSubunitsA Non-canonical BCOR-PRC1.1 Complex Represses Differentiation Programs in Human ESCs
Wang Z, Gearhart MD, Lee YW, Kumar I, Ramazanov B, Zhang Y, Hernandez C, Lu AY, Neuenkirchen N, Deng J, Jin J, Kluger Y, Neubert TA, Bardwell VJ, Ivanova NB. A Non-canonical BCOR-PRC1.1 Complex Represses Differentiation Programs in Human ESCs. Cell Stem Cell 2018, 22: 235-251.e9. PMID: 29337181, PMCID: PMC5797497, DOI: 10.1016/j.stem.2017.12.002.Peer-Reviewed Original ResearchMeSH KeywordsCell DifferentiationChromatinF-Box ProteinsHistonesHuman Embryonic Stem CellsHumansJumonji Domain-Containing Histone DemethylasesLysineMethylationMultiprotein ComplexesPolycomb Repressive Complex 1Polycomb Repressive Complex 2Promoter Regions, GeneticProtein DomainsProto-Oncogene ProteinsRepressor ProteinsConceptsEmbryonic stem cellsHuman embryonic stem cellsPolycomb domainsNon-canonical PRC1 complexesKey developmental lociNon-canonical complexesPolycomb group (PcG) proteinsE3 ubiquitin ligasesStem cell systemInitiation of differentiationDevelopmental lociPRC1 complexesRepressive chromatinRepressor functionPRC1.1 complexMesoderm lineageGroup proteinsCo-repressorAccessory subunitsDifferentiation programCanonical complexDevelopmental systemsC-terminusGene targetsN-terminus
2010
β4-Subunit increases Slo responsiveness to physiological Ca2+ concentrations and together with β1 reduces surface expression of Slo in hair cells
Bai JP, Surguchev A, Navaratnam D. β4-Subunit increases Slo responsiveness to physiological Ca2+ concentrations and together with β1 reduces surface expression of Slo in hair cells. American Journal Of Physiology - Cell Physiology 2010, 300: c435-c446. PMID: 21178105, PMCID: PMC3063969, DOI: 10.1152/ajpcell.00449.2010.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCalciumCalcium SignalingCell MembraneChickensCochleaDown-RegulationHair Cells, AuditoryIon Channel GatingLarge-Conductance Calcium-Activated Potassium Channel beta SubunitsLarge-Conductance Calcium-Activated Potassium ChannelsMechanotransduction, CellularMembrane PotentialsOocytesXenopus laevisConceptsLow-frequency hair cellsHair cellsLarge-conductance potassium channelsBK channelsSurface expressionBK channel functionNonmammalian vertebratesAccessory subunitsΑ-subunitMolecular underpinningsΒ-subunitChannel functionSubunitsΒ4 subunitPhysiological Ca2Critical rolePotassium channelsCellsBK currentsAdditional mechanismExpressionVertebratesDramatic increaseChicksIntracellular
2003
Characterization of Novel Reverse Transcriptase and Other RNA-associated Catalytic Activities by Human DNA Polymerase γ IMPORTANCE IN MITOCHONDRIAL DNA REPLICATION*
Murakami E, Feng J, Lee H, Hanes J, Johnson K, Anderson K. Characterization of Novel Reverse Transcriptase and Other RNA-associated Catalytic Activities by Human DNA Polymerase γ IMPORTANCE IN MITOCHONDRIAL DNA REPLICATION*. Journal Of Biological Chemistry 2003, 278: 36403-36409. PMID: 12857740, DOI: 10.1074/jbc.m306236200.Peer-Reviewed Original ResearchConceptsMtDNA genomeMtDNA replicationPol gammaInitiation of mtDNA replicationRNA-primed DNA synthesisHuman mitochondrial DNA polymeraseMitochondrial DNA polymeraseReverse transcriptionDNA synthesis activityPhysiologically relevant ratesMitochondrial DNARibonucleotide incorporationProofreading activitySingle ribonucleotidesHeteroduplex intermediatesRibonucleotide triphosphatesRNA templateDNA primersDNA polymeraseReverse transcriptaseDNA excisionMtDNAAccessory subunitsDNA synthesisEnzymatic pathways
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