2022
An RNAi screen of RNA helicases identifies eIF4A3 as a regulator of embryonic stem cell identity
Li D, Yang J, Malik V, Huang Y, Huang X, Zhou H, Wang J. An RNAi screen of RNA helicases identifies eIF4A3 as a regulator of embryonic stem cell identity. Nucleic Acids Research 2022, 50: 12462-12479. PMID: 36416264, PMCID: PMC9757061, DOI: 10.1093/nar/gkac1084.Peer-Reviewed Original ResearchConceptsExon junction complexRNA helicaseRNA interferenceEmbryonic stem cellsPost-transcriptionallyEmbryonic stem cell identityEfficient nuclear exportRNA interference screenCell cycle progression of ESCsPost-transcriptional controlCell cycle regulationStem cell identityCell cycle progressionMaintenance of embryonic stem cellsStem cell pluripotencyLoss of pluripotencyRNA metabolismDEAD-boxCell cycle dysregulationCell identityCycle regulationCell pluripotencyCell cyclePluripotency controlCyclin B1
2014
The UPF1 RNA surveillance gene is commonly mutated in pancreatic adenosquamous carcinoma
Liu C, Karam R, Zhou Y, Su F, Ji Y, Li G, Xu G, Lu L, Wang C, Song M, Zhu J, Wang Y, Zhao Y, Foo W, Zuo M, Valasek M, Javle M, Wilkinson M, Lu Y. The UPF1 RNA surveillance gene is commonly mutated in pancreatic adenosquamous carcinoma. Nature Medicine 2014, 20: 596-598. PMID: 24859531, PMCID: PMC4048332, DOI: 10.1038/nm.3548.Peer-Reviewed Original ResearchMeSH KeywordsAlternative SplicingBase SequenceCarcinoma, AdenosquamousGene ComponentsHEK293 CellsHumansImmunohistochemistryIn Situ Nick-End LabelingMolecular Sequence DataMutagenesisMutationNonsense Mediated mRNA DecayPancreatic NeoplasmsReal-Time Polymerase Chain ReactionReverse Transcriptase Polymerase Chain ReactionRNA HelicasesSequence Analysis, DNATrans-Activators
2012
ATP Utilization and RNA Conformational Rearrangement by DEAD-Box Proteins
Henn A, Bradley MJ, De La Cruz EM. ATP Utilization and RNA Conformational Rearrangement by DEAD-Box Proteins. Annual Review Of Biophysics 2012, 41: 247-267. PMID: 22404686, PMCID: PMC7761782, DOI: 10.1146/annurev-biophys-050511-102243.Peer-Reviewed Original ResearchConceptsDEAD-box proteinsNucleotide-dependent interactionRegulatory partner proteinsMolecular motor proteinsMolecular motor functionPartner proteinsRNA helicasesHelicase coreRNA helicaseRNA metabolismVivo foldingATP bindingDBP functionMotor proteinsCellular RNARNA structureQuantitative mechanistic understandingConformational rearrangementsBiophysical investigationsEnzymatic adaptationLarge familyMechanistic understandingProteinRNAAuxiliary domain
2010
The Yb Body, a Major Site for Piwi-associated RNA Biogenesis and a Gateway for Piwi Expression and Transport to the Nucleus in Somatic Cells*
Qi H, Watanabe T, Ku HY, Liu N, Zhong M, Lin H. The Yb Body, a Major Site for Piwi-associated RNA Biogenesis and a Gateway for Piwi Expression and Transport to the Nucleus in Somatic Cells*. Journal Of Biological Chemistry 2010, 286: 3789-3797. PMID: 21106531, PMCID: PMC3030380, DOI: 10.1074/jbc.m110.193888.Peer-Reviewed Original ResearchConceptsYb bodiesSomatic cellsPiRNA pathwayGerm lineEndo-siRNA pathwaySomatic niche cellsTudor-like domainGonadal somatic cellsPutative RNA helicaseCo-immunoprecipitation experimentsSomatic stem cellsFlamenco locusSomatic piRNAsPiRNA biogenesisEndo-siRNAsRNA biogenesisRNA pathwaysPiwi expressionRNA helicaseNovel proteinPiwiNiche cellsMolecular basisStem cellsBiogenesis
2004
Equilibrium and Kinetic Analysis of Nucleotide Binding to the DEAD-Box RNA Helicase DbpA †
Talavera MA, De La Cruz EM. Equilibrium and Kinetic Analysis of Nucleotide Binding to the DEAD-Box RNA Helicase DbpA †. Biochemistry 2004, 44: 959-970. PMID: 15654752, DOI: 10.1021/bi048253i.Peer-Reviewed Original ResearchConceptsFluorescence resonance energy transferAbsence of RNARNA helicaseATP bindingNucleotide bindingConformational rearrangementsResonance energy transferConformational flexibilityDbpADependent conformationStructural rearrangementsDbpA.Protein AUnfavorable entropic contributionNucleotidesPhysiological temperatureBindingAssociation rate constantsADP
2002
mda-5: An interferon-inducible putative RNA helicase with double-stranded RNA-dependent ATPase activity and melanoma growth-suppressive properties
Kang DC, Gopalkrishnan RV, Wu Q, Jankowsky E, Pyle AM, Fisher PB. mda-5: An interferon-inducible putative RNA helicase with double-stranded RNA-dependent ATPase activity and melanoma growth-suppressive properties. Proceedings Of The National Academy Of Sciences Of The United States Of America 2002, 99: 637-642. PMID: 11805321, PMCID: PMC117358, DOI: 10.1073/pnas.022637199.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphatasesAmino Acid SequenceAnimalsApoptosisCell DifferentiationCell DivisionCloning, MolecularDEAD-box RNA HelicasesDNA, ComplementaryGrowth InhibitorsHumansInterferon Type IInterferon-Induced Helicase, IFIH1MelanomaMolecular Sequence DataRecombinant ProteinsRNA HelicasesRNA, Double-StrandedSequence Homology, Amino AcidTumor Cells, CulturedTumor Stem Cell AssayConceptsRNA-dependent ATPase activityCaspase recruitment domainHelicase motifsHuman melanoma cellsRecruitment domainRNA helicase motifsRNA-dependent ATPaseMDA-5RNA helicase domainPutative RNA helicaseMelanoma cellsEarly response genesATPase activityProtein kinase C activationGrowth-suppressive propertiesMelanoma differentiation-associated gene 5Appropriate pharmacological manipulationKinase C activationHypothetical proteinsRNA helicaseHelicase domainDifferentiation-associated gene 5Mediator of IFNSubtraction hybridizationMda-5 expression
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