2023
Discovery of the first unconventional myosin: Acanthamoeba myosin-I
Pollard T, Korn E. Discovery of the first unconventional myosin: Acanthamoeba myosin-I. Frontiers In Physiology 2023, 14: 1324623. PMID: 38046947, PMCID: PMC10693453, DOI: 10.3389/fphys.2023.1324623.Peer-Reviewed Original ResearchUnconventional myosinActin filamentsMyosin heavy chain kinaseFirst unconventional myosinsEvolution of eukaryotesClass I MyosinHeavy chain kinaseNovel unconventional myosinPhylogenetic analysisSlime moldMembrane lipidsChain kinaseProteolytic fragmentsHeavy chainMuscle myosinMyosinCofactorEnzymeMg-ATPaseMg-ATPase activityEukaryotesFilamentsCrude enzymeKinaseActin
2022
Myosin light chain phosphatase catalytic subunit dephosphorylates cardiac myosin via mechanisms dependent and independent of the MYPT regulatory subunits
Lee E, Liu Z, Nguyen N, Nairn A, Chang AN. Myosin light chain phosphatase catalytic subunit dephosphorylates cardiac myosin via mechanisms dependent and independent of the MYPT regulatory subunits. Journal Of Biological Chemistry 2022, 298: 102296. PMID: 35872014, PMCID: PMC9418503, DOI: 10.1016/j.jbc.2022.102296.Peer-Reviewed Original ResearchConceptsMyosin light chain phosphataseRegulatory light chainRegulatory subunitCatalytic subunitPhosphatase catalytic subunitMain catalytic subunitSmooth muscle myosin light chain phosphataseNon-muscle cellsMuscle myosin light chain phosphataseMyosin regulatory light chainMyosin light chain kinaseLight chain kinasePP1cβTrimeric proteinConditional knockout miceLight chain phosphatasePhosphatase activitySubunitsPhosphate/Chain kinaseMuscle pathogenesisPhysiological regulationKnockout animalsMain isoformsProtein
2011
Use of a tandem affinity purification assay to detect interactions between West Nile and dengue viral proteins and proteins of the mosquito vector
Colpitts TM, Cox J, Nguyen A, Feitosa F, Krishnan MN, Fikrig E. Use of a tandem affinity purification assay to detect interactions between West Nile and dengue viral proteins and proteins of the mosquito vector. Virology 2011, 417: 179-187. PMID: 21700306, PMCID: PMC3166580, DOI: 10.1016/j.virol.2011.06.002.Peer-Reviewed Original ResearchConceptsWest Nile virus infectionWest NileMosquito vectorsWest Nile virus envelope proteinMosquito proteinsSignificant morbidityFlavivirus infectionDengue viral proteinsVirus envelope proteinVirus infectionMosquito factorsDengue virusNovel targetInfectionMosquito cellsDengueEnvelope proteinMyosin light chain kinaseViral proteinsFlavivirusesLight chain kinasePI3-kinaseChain kinaseNS2B proteinCells
1994
Calcium/calmodulin-dependent protein kinases.
Nairn AC, Picciotto MR. Calcium/calmodulin-dependent protein kinases. Seminars In Cancer Biology 1994, 5: 295-303. PMID: 7803766.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsCalcium-Calmodulin-Dependent Protein Kinase Type 1Calcium-Calmodulin-Dependent Protein Kinase Type 2Calcium-Calmodulin-Dependent Protein Kinase Type 4Calcium-Calmodulin-Dependent Protein KinasesElongation Factor 2 KinaseHumansMolecular Sequence DataMyosin-Light-Chain KinasePhosphorylationConceptsProtein kinaseSecond messenger-regulated protein kinasesCaM-dependent protein kinaseEssential intracellular second messengerEF-2 kinaseCaM kinase ICaM kinase IVCaM kinase IIIntracellular second messengerMyosin light chain kinaseEukaryotic systemsProtein phosphorylationKinase ILight chain kinaseKinase IIPhosphorylase kinaseGene expressionKinase IVSecond messengerKinaseChain kinaseImportant familyCell proliferationNeurotransmitter releaseRegulation
1984
The amino acid sequence of rabbit skeletal muscle calmodulin
Nairn A, Grand R, Perry S. The amino acid sequence of rabbit skeletal muscle calmodulin. FEBS Letters 1984, 167: 215-220. PMID: 6698209, DOI: 10.1016/0014-5793(84)80129-5.Peer-Reviewed Original ResearchConceptsSingle polypeptide chainMyosin light chain kinaseBlocked N terminusRabbit skeletal muscleLight chain kinasePhosphorylase kinaseMammalian calmodulinN-terminusPolypeptide chainResidues 48Chain kinaseAmide assignmentsCalmodulinLow ionic strength bufferKinaseSkeletal muscleIonic strength bufferSequenceN-terminal tripeptideStrength bufferTerminal tripeptideTerminusSubunitsProteinResidues
1982
Ca++-calmodulin-dependent phosphorylation of myosin, and its role in brush border contraction in vitro.
Keller T, Mooseker M. Ca++-calmodulin-dependent phosphorylation of myosin, and its role in brush border contraction in vitro. Journal Of Cell Biology 1982, 95: 943-959. PMID: 6897550, PMCID: PMC2112925, DOI: 10.1083/jcb.95.3.943.Peer-Reviewed Original ResearchConceptsBrush border contractionBrush borderIntestinal epithelial cellsEpithelial cellsCalmodulin activityBrush border proteinsMyosin light chain kinaseContractionDegrees CLight chain kinaseLight chainCalmodulin-dependent phosphorylationBrush border myosinPhosphorylationDalton light chainChain kinaseTerminal web
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