2023
7SK methylation by METTL3 promotes transcriptional activity
Perez-Pepe M, Desotell A, Li H, Li W, Han B, Lin Q, Klein D, Liu Y, Goodarzi H, Alarcón C. 7SK methylation by METTL3 promotes transcriptional activity. Science Advances 2023, 9: eade7500. PMID: 37163588, PMCID: PMC10171809, DOI: 10.1126/sciadv.ade7500.Peer-Reviewed Original ResearchConceptsTranscriptional elongationTranscriptional responseAdaptive transcriptional responseHeterogeneous nuclear ribonucleoproteinsElongation factor complexPositive transcription elongation factor complexGrowth factorExtracellular signalsRNA modificationsRNA 7SKEpidermal growth factorCell signalingInduces phosphorylationMethyltransferase 3Nuclear ribonucleoproteinFactor complexTranscriptional activityUnknown functionMethylationMETTL3RibonucleoproteinPhosphorylationTEFbElongationSignalingPharmacological disruption of mSWI/SNF complex activity restricts SARS-CoV-2 infection
Wei J, Patil A, Collings C, Alfajaro M, Liang Y, Cai W, Strine M, Filler R, DeWeirdt P, Hanna R, Menasche B, Ökten A, Peña-Hernández M, Klein J, McNamara A, Rosales R, McGovern B, Luis Rodriguez M, García-Sastre A, White K, Qin Y, Doench J, Yan Q, Iwasaki A, Zwaka T, Qi J, Kadoch C, Wilen C. Pharmacological disruption of mSWI/SNF complex activity restricts SARS-CoV-2 infection. Nature Genetics 2023, 55: 471-483. PMID: 36894709, PMCID: PMC10011139, DOI: 10.1038/s41588-023-01307-z.Peer-Reviewed Original ResearchConceptsMSWI/SNF complexesAcute respiratory syndrome coronavirus 2 infectionSevere acute respiratory syndrome coronavirus 2 (SARS-CoV-2) infectionHost-directed therapeutic targetSyndrome coronavirus 2 infectionSARS-CoV-2 infectionSWItch/Sucrose Non-Fermentable (SWI/SNF) chromatinSARS-CoV-2 susceptibilityNon-fermentable (SWI/SNF) chromatinCoronavirus 2 infectionEnzyme 2 (ACE2) expressionSARS-CoV-2 variantsHuman cell typesPrimary human cell typesAirway epithelial cellsDrug-resistant variantsNew drug targetsChromatin accessibilitySNF complexACE2 locusACE2 expressionFactor complexHost determinantsTherapeutic targetConfer resistance
2016
Reciprocal stabilization of ABL and TAZ regulates osteoblastogenesis through transcription factor RUNX2
Matsumoto Y, La Rose J, Kent OA, Wagner MJ, Narimatsu M, Levy AD, Omar MH, Tong J, Krieger JR, Riggs E, Storozhuk Y, Pasquale J, Ventura M, Yeganeh B, Post M, Moran MF, Grynpas MD, Wrana JL, Superti-Furga G, Koleske AJ, Pendergast AM, Rottapel R. Reciprocal stabilization of ABL and TAZ regulates osteoblastogenesis through transcription factor RUNX2. Journal Of Clinical Investigation 2016, 126: 4482-4496. PMID: 27797343, PMCID: PMC5127668, DOI: 10.1172/jci87802.Peer-Reviewed Original ResearchConceptsLineage-specifying transcription factorsReciprocal stabilizationAdaptor protein 3BP2TAZ nuclear localizationTranscription factor complexTyrosine kinase AblTranscription factor Runx2Transcriptional coactivator TAZLineage-specific maturationMetazoan organismsCellular identityOsteoblast expansionTranscriptional positive feedbackTranscription factorsSkeletal formationFactor complexNuclear localizationOwn expressionPositive feedback loopGenetic dataOsteoblast lineageMaturation programOsteoblast differentiationDevelopmental networksTAZ
2014
RNA polymerase III transcription factor complexes block transcriptional interference from intergenic RNA polymerase II progression in Saccharomyces cerevisiae (561.3)
Korde A, Rosselot J, Donze D. RNA polymerase III transcription factor complexes block transcriptional interference from intergenic RNA polymerase II progression in Saccharomyces cerevisiae (561.3). The FASEB Journal 2014, 28 DOI: 10.1096/fasebj.28.1_supplement.561.3.Peer-Reviewed Original ResearchPol III transcription complexesTranscription complexTransfer RNATranscriptional interferenceRNA polymerase II progressionRNA polymerase II transcriptionRNA polymerase III transcriptionPol III complexesPolymerase II transcriptionTranscription factor complexPolymerase III transcriptionChromosome functionPervasive transcriptionTFIIIB complexChromatin immunoprecipitationGene upstreamFactor complexEnzyme complexTranscriptionGenesSequential assemblyRecent discoveryYeastComplexesRecent studies
2008
A novel genetic strategy reveals unexpected roles of the Swi–Snf–like chromatin-remodeling BAF complex in thymocyte development
Jani A, Wan M, Zhang J, Cui K, Wu J, Preston-Hurlburt P, Khatri R, Zhao K, Chi T. A novel genetic strategy reveals unexpected roles of the Swi–Snf–like chromatin-remodeling BAF complex in thymocyte development. Journal Of Experimental Medicine 2008, 205: 2813-2825. PMID: 18955569, PMCID: PMC2585832, DOI: 10.1084/jem.20080938.Peer-Reviewed Original ResearchConceptsPoint mutantsUnexpected roleImportant gene functionsThymocyte developmentNovel genetic strategyPoint mutationsEarly thymocyte developmentMammalian geneticsChromatin templatesSWI-SNFBAF complexGene functionATPase subunitsDeletion mutantsFactor complexCD4 locusTarget genesGenetic strategiesCD4 activationMutantsNovel activityPhysical interactionDeletionBRGMutations
2004
A BAF-centred view of the immune system
Chi T. A BAF-centred view of the immune system. Nature Reviews Immunology 2004, 4: 965-977. PMID: 15573131, DOI: 10.1038/nri1501.Peer-Reviewed Original ResearchConceptsChromatin-remodelling complexBAF complexRepressive chromatin structureStructure of chromatinHistone-DNA contactsTranscription factor complexPost-translational modificationsTranscriptional start siteIFN-β geneTranscriptional machineryChromatin structureTranscriptional activatorTranscriptional repressorHuman genesResponsive genesExpression of CIITAStart siteDNA sequencesFactor complexHistone octamerNucleosomesOwn replicationGene expressionGenomic DNAIFN-β expressionAncylostoma ceylanicum anticoagulant peptide-1: role of the predicted reactive site amino acid in mediating inhibition of coagulation factors Xa and VIIa
Mieszczanek J, Harrison LM, Cappello M. Ancylostoma ceylanicum anticoagulant peptide-1: role of the predicted reactive site amino acid in mediating inhibition of coagulation factors Xa and VIIa. Molecular And Biochemical Parasitology 2004, 137: 151-159. PMID: 15279961, DOI: 10.1016/j.molbiopara.2004.05.011.Peer-Reviewed Original ResearchConceptsCoagulation factor XaAmino acid sequence similarityFactor XaGastrointestinal blood lossIron deficiency anemiaSite amino acid residuesAmino acid residuesSite amino acidsMechanism of actionBlood lossHookworm infectionSequence similarityDeficiency anemiaLeading causeFactor VIIa/tissue factor complexFactor complexCoagulation inhibitorsPeptide-1Ancylostoma caninum anticoagulant peptide 5Coagulation responseAcid residuesNon-active siteA. ceylanicumAnticoagulantsTissue factor complex
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