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Article

Identification and characterization of hippuristanol-resistant mutants reveals eIF4A1 dependencies within mRNA 5' leader regions.

Nucleic acids research - 25 Sept 2020

Steinberger Jutta, Shen Leo, J Kiniry Stephen, Naineni Sai Kiran, Cencic Regina, Amiri Mehdi, Aboushawareb Sarah A E, Chu Jennifer, Maïga Rayelle Itoua, Yachnin Brahm J, Robert Francis, Sonenberg Nahum, Baranov Pavel V, Pelletier Jerry

Abstract excerpt

Hippuristanol (Hipp) is a natural product that selectively inhibits protein synthesis by targeting eukaryotic initiation factor (eIF) 4A, a DEAD-box RNA helicase required for ribosome recruitment to mRNA templates. Hipp binds to the carboxyl-terminal domain of eIF4A, locks it in a closed conformation, and inhibits its RNA binding. The dependencies of mRNAs for eIF4A during initiation is contingent on the degree...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 32766783
DOI: 10.1093/nar/gkaa662
PMCID: PMC7515738

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

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