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Showing 1–9 of 9 results
Advanced filters: Author: Natalia Demeshkina Clear advanced filters

  • The anticodon loops of almost all tRNAs contain modifications known to be important for their function. Here the authors use crystallography to provide new mechanistic insights into how the modification at the wobble position of the E. coli tRNALysUUUassists in discrimination between cognate and near-cognate codons.

    • Alexey Rozov
    • Natalia Demeshkina
    • Gulnara Yusupova
    ResearchOpen Access
    Nature Communications
    Volume: 7, P: 1-10

  • Translation of mRNA into proteins is the least accurate process during genetic information transfer. Here the authors suggest—based on 11 high-resolution ribosome crystal structures—that the origin of protein missense errors involves molecular mimicry via tautomerism or ionization.

    • Alexey Rozov
    • Natalia Demeshkina
    • Gulnara Yusupova
    ResearchOpen Access
    Nature Communications
    Volume: 6, P: 1-9

  • Ensuring the ribosome accepts a correct tRNA is key to fidelity of translation. The structures of the 70S ribosome carrying correct and incorrect tRNAs are now presented, giving mechanistic insight into the tRNA proofreading process where ribosomal proteins are shown to play an active role.

    • Lasse Jenner
    • Natalia Demeshkina
    • Marat Yusupov
    Research
    Nature Structural & Molecular Biology
    Volume: 17, P: 1072-1078

  • An integrated mechanism for decoding is proposed, based on six X-ray structures of the 70S ribosome determined at 3.1–3.4 Å resolution, modelling cognate or near-cognate states of the decoding centre at the proofreading step.

    • Natalia Demeshkina
    • Lasse Jenner
    • Gulnara Yusupova
    Research
    Nature
    Volume: 484, P: 256-259

  • Structural analysis of the Saccharomyces cerevisiae 80S ribosome trapped in an intermediate translocation state shows stabilization of codon–anticodon interactions by eukaryote-specific elements of the 80S ribosome, eEF2 and tRNA and demonstrates a major role for eEF2 in maintaining the directionality of translocation.

    • Muminjon Djumagulov
    • Natalia Demeshkina
    • Gulnara Yusupova
    ResearchOpen Access
    Nature
    Volume: 600, P: 543-546

  • DHX36 is a G-quadruplex (G4) resolving helicase that targets both DNA-G4 and RNA-G4. Here the authors use single molecule FRET measurements and show that DHX36 resolves RNA-G4 structures by a mechanism involving an ATP-dependent, highly repetitive and stepwise refolding of RNA-G4 that differs from its DNA-G4 structures resolving mechanism.

    • Ramreddy Tippana
    • Michael C. Chen
    • Sua Myong
    ResearchOpen Access
    Nature Communications
    Volume: 10, P: 1-10

  • An important aspect of translational fidelity is that the reading frame of a translating mRNA be maintained on the ribosome. Structures representing the initiating and elongating ribosome now show that a tunnel narrows to facilitate a network of interactions that may hold the message in frame in the latter complex.

    • Lasse B Jenner
    • Natalia Demeshkina
    • Marat Yusupov
    Research
    Nature Structural & Molecular Biology
    Volume: 17, P: 555-560

  • A crystal structure of the RNA aptamer Mango bound to a thiazole orange–derived fluorophore reveals a three-tiered G-quadruplex structure, which, together with three flap-like nucleotides, constrains the fluorophore into its active conformation.

    • Robert J Trachman III
    • Natalia A Demeshkina
    • Adrian R Ferré-D'Amaré
    Research
    Nature Chemical Biology
    Volume: 13, P: 807-813