2015
HOTAIR Forms an Intricate and Modular Secondary Structure
Somarowthu S, Legiewicz M, Chillón I, Marcia M, Liu F, Pyle AM. HOTAIR Forms an Intricate and Modular Secondary Structure. Molecular Cell 2015, 58: 353-361. PMID: 25866246, PMCID: PMC4406478, DOI: 10.1016/j.molcel.2015.03.006.Peer-Reviewed Original ResearchConceptsFunctional secondary structureFundamental cellular processesSecondary structureProtein-binding motifsProtein-binding domainsGroup II intronsMetastasis suppressor geneSecondary structure elementsCellular processesPhylogenetic analysisLncRNA moleculesEpidermal developmentChemical probingMolecular mechanismsSuppressor geneCancer progressionStructural organizationKey playersLncRNA HOTAIRHOTAIRStructure elementsRNAHomogenous formReceptor activatorIntrons
2002
The hepatitis C viral NS3 protein is a processive DNA helicase with cofactor enhanced RNA unwinding
Pang PS, Jankowsky E, Planet PJ, Pyle AM. The hepatitis C viral NS3 protein is a processive DNA helicase with cofactor enhanced RNA unwinding. The EMBO Journal 2002, 21: 1168-1176. PMID: 11867545, PMCID: PMC125889, DOI: 10.1093/emboj/21.5.1168.Peer-Reviewed Original ResearchConceptsRNA unwindingHelicase activityDNA helicase activityCytoplasmic RNA virusesProcessive DNA helicaseImportant drug targetsReplicative DNA intermediatesNS3 helicase activityViral NS3 proteinDNA helicaseDuplex unwindingPhylogenetic analysisReplicative roleProcessive helicaseDNA intermediatesHelicaseHost DNARNA virusesRNA activityRNA replicationDrug targetsNS3 proteinUnwindingCentral roleDNA