Tatyana V. Pestova

This study identifies structural and evolutionary mechanisms underlying the diversification of viral IRESs through accretion and recombination.

The paper determines high-resolution structures of NediV IRES-mediated translation initiation complexes and their transition to elongation, revealing structural changes and interactions during viral translation.

This study determines cryo-EM structures of GTPBP1 bound to ribosomes and tRNA, revealing its unique architecture and mechanism for slow dissociation and enhanced decoding accuracy.

This study uses structural models to clarify DHX29's role in mRNA scanning, showing it transiently pulls mRNA opposite to scanning direction.

The paper determines the cryo-EM structure of 48S initiation complexes on EMCV IRESs and identifies key interactions essential for ribosomal recruitment.

The paper investigates how TCF25 imposes K48-specificity on Listerin-mediated ubiquitination by interacting with the RING domain and orienting the acceptor ubiquitin.

The paper identifies inconsistencies in rabbit ribosomal rRNA sequences and proposes using the Broad Institute's genome sequence to standardize numbering and improve model consistency.

The paper investigates how SARS-CoV-2 Nsp1 induces mRNA cleavage in vitro using different mRNAs, identifying key domains in Nsp1 and eIF3g essential for the process.

The paper presents cryo-EM structures of Hepatitis C virus IRES initiation complexes, revealing conformational changes during translation initiation.

The paper shows that the Halastavi arva virus IGR IRES initiates translation without initiation factors or an AUG codon by directly placing the first codon in the decoding center.