Daniel Benhalevy
National Institutes of Health
13 Papers
3 Citations
Daniel Benhalevy is an academic researcher from National Institutes of Health. The author has contributed to research in topics: RNA & Translation (biology). The author has an hindex of 6, co-authored 9 publications. Previous affiliations of Daniel Benhalevy include Weizmann Institute of Science.
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Papers
DHX36 prevents the accumulation of translationally inactive mRNAs with G4-structures in untranslated regions.
Markus Sauer,Markus Sauer,Markus Sauer,Stefan Juranek,James Marks,Alessio De Magis,Hinke G. Kazemier,Daniel Hilbig,Daniel Benhalevy,Xiantao Wang,Markus Hafner,Katrin Paeschke,Katrin Paeschke,Katrin Paeschke +13 more
TL;DR: It is revealed that loss of DHX36 helicase activity leads to an accumulation of translationally inactive target mRNAs with G-rich structures in untranslated regions, which may be involved in resolution of rG4 induced cellular stress.
The Human CCHC-type Zinc Finger Nucleic Acid-Binding Protein Binds G-Rich Elements in Target mRNA Coding Sequences and Promotes Translation
Daniel Benhalevy,Sanjay K. Gupta,Charles H. Danan,Suman Ghosal,Hong-Wei Sun,Hinke G. Kazemier,Katrin Paeschke,Markus Hafner,Stefan Juranek,Stefan Juranek +9 more
TL;DR: Functional analyses revealed that CNBP binding did not influence target mRNA abundance but rather increased their translational efficiency, and it is hypothesize that CN BP is supporting translation by resolving stable structures on mRNAs.
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PAR-CLIP and streamlined small RNA cDNA library preparation protocol for the identification of RNA binding protein target sites
TL;DR: A streamlined protocol for Photoactivatable-Ribonucleoside-Enhanced Crosslinking and Immunoprecipitation (PAR-CLIP), a technique that allows for the characterization of RBP binding sites on target RNAs at nucleotide resolution and transcriptome-wide scale.
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Model Uracil-Rich RNAs and Membrane Protein mRNAs Interact Specifically with Cold Shock Proteins in Escherichia coli
TL;DR: The results suggest that the evolutionarily conserved cold shock proteins may have a role, possibly as promiscuous chaperons, in the biogenesis of MPRs.
Evidence for a cytoplasmic pool of ribosome-free mRNAs encoding inner membrane proteins in Escherichia coli.
TL;DR: The possibility that the effects of CspE overexpression may link the intriguing subcellular localization of MPRs to the cytosolic ribosome-free fraction with their translation into membrane proteins and that the ribosomes-free pool of M PRs may represent a stage during their targeting to the membrane, which precedes translation.