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Vadim I. Agol

Researcher at Moscow State University

Publications -  195
Citations -  8768

Vadim I. Agol is an academic researcher from Moscow State University. The author has contributed to research in topics: RNA & Virus. The author has an hindex of 52, co-authored 195 publications receiving 8497 citations. Previous affiliations of Vadim I. Agol include Russian Academy of Sciences & Laboratory of Molecular Biology.

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Molecular mechanisms of translation initiation in eukaryotes.

TL;DR: Encephalomyocarditis virus (EMCV) and hepatitis C virus epitomize distinct mechanisms of internal ribosomal entry site (IRES)-mediated initiation, and initiation on some EMCV-like IRESs requires additional noncanonical initiation factors, which alter IRES conformation and promote binding of eIF4A/4G.
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La autoantigen enhances and corrects aberrant translation of poliovirus RNA in reticulocyte lysate.

TL;DR: The results suggest that La protein is involved in poliovirus internal initiation of translation and might function through a similar mechanism in the translation of cellular mRNAs.
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A cell cycle-dependent protein serves as a template-specific translation initiation factor.

TL;DR: The data indicate that PTB and ITAF act as RNA chaperones that control the functional state of a particular IRES and that their cell-specific distribution may constitute a basis for cell- specific translational control of certain mRNAs.
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Prokaryotic-like cis elements in the cap-independent internal initiation of translation on picornavirus RNA.

TL;DR: It is shown that efficient function of this element involves two appropriately spaced smaller elements: UUUCC and an AUG, which is similar to the prokaryotic translation initiation mechanism, but in the picornavirus system the position of the UUU CC must be strictly fixed relative to upstream cis-acting elements, and the AUG may not necessarily serve as an initiation codon.
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Conserved structural domains in the 5'-untranslated region of picornaviral genomes: an analysis of the segment controlling translation and neurovirulence.

TL;DR: No major changes in the conformation of the Sabin vaccine poliovirus type 3 5'-UTR due to the transition in position 472 were observed, and the biological relevance of the conserved primary and secondary structure elements in the picornaviral5'-UTRs is discussed.