{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Naineni SK"],"funding":["NCATS NIH HHS","National Institutes of Health","NIGMS NIH HHS","Canadian Institutes of Health Research"],"pagination":["826-835"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC10187672"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["29(6)"],"pubmed_abstract":["Inhibition of eukaryotic translation initiation through unscheduled RNA clamping of the DEAD-box (DDX) RNA helicases eIF4A1 and eIF4A2 has been documented for pateamine A (PatA) and rocaglates-two structurally different classes of compounds that share overlapping binding sites on eIF4A. Clamping of eIF4A to RNA causes steric blocks that interfere with ribosome binding and scanning, rationalizing the potency of these molecules since not all eIF4A molecules need to be engaged to elicit a biological effect. In addition to targeting translation, PatA and analogs have also been shown to target the eIF4A homolog, eIF4A3-a helicase necessary for exon junction complex (EJC) formation. EJCs are deposited on mRNAs upstream of exon-exon junctions and, when present downstream from premature terminatio"],"journal":["RNA (New York, N.Y.)"],"pubmed_title":["Exploring the targeting spectrum of rocaglates among eIF4A homologs."],"pmcid":["PMC10187672"],"funding_grant_id":["R35 GM118173","#FDN-148366","R35GM118173","U01 TR002625","U01TR002625"],"pubmed_authors":["Haque M","Pelletier J","Senechal P","Porco JA","Robert F","Cencic R","Brown LE","Scott-Talib J","Schmeing TM","Naineni SK"],"additional_accession":[]},"is_claimable":false,"name":"Exploring the targeting spectrum of rocaglates among eIF4A homologs.","description":"Inhibition of eukaryotic translation initiation through unscheduled RNA clamping of the DEAD-box (DDX) RNA helicases eIF4A1 and eIF4A2 has been documented for pateamine A (PatA) and rocaglates-two structurally different classes of compounds that share overlapping binding sites on eIF4A. Clamping of eIF4A to RNA causes steric blocks that interfere with ribosome binding and scanning, rationalizing the potency of these molecules since not all eIF4A molecules need to be engaged to elicit a biological effect. In addition to targeting translation, PatA and analogs have also been shown to target the eIF4A homolog, eIF4A3-a helicase necessary for exon junction complex (EJC) formation. EJCs are deposited on mRNAs upstream of exon-exon junctions and, when present downstream from premature terminatio","dates":{"release":"2023-01-01T00:00:00Z","publication":"2023 Jun","modification":"2026-07-15T20:09:54.947Z","creation":"2026-07-09T03:10:34.466Z"},"accession":"S-EPMC10187672","cross_references":{"pubmed":["36882295"],"doi":["10.1261/rna.079318.122"]}}