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Showing 1–10 of 10 results
Advanced filters: Author: Yuliya Gordiyenko Clear advanced filters

  • Eukaryotic Initiation Factor 2 (eIF2) initiates protein synthesis aided by its partner eIF2B, which stimulates guanine nucleotide exchange on eIF2. Here, Gordiyenko et al. show that eIF2B exists as a decamer and propose a model for its subunit arrangement that provides new insight into its function.

    • Yuliya Gordiyenko
    • Carla Schmidt
    • Carol V. Robinson
    ResearchOpen Access
    Nature Communications
    Volume: 5, P: 1-12

  • During stress, protein synthesis is inhibited through phosphorylation of the initiation factor eIF2 on its alpha subunit and its interaction with eIF2B. Here the authors describe a structure of the yeast eIF2B in complex with its substrate - the GDP-bound phosphorylated eIF2, providing insights into how phosphorylation results in a tighter interaction with eIF2B.

    • Yuliya Gordiyenko
    • José Luis Llácer
    • V. Ramakrishnan
    ResearchOpen Access
    Nature Communications
    Volume: 10, P: 1-11

  • Transcription and RNA splicing are tightly coupled in eukaryotic cells. Here, authors report the multivalent interaction between U1 snRNP and the transcription elongation complex which may allow efficient co-transcriptional spliceosome assembly.

    • Luojia Zhang
    • Christopher Batters
    • Suyang Zhang
    ResearchOpen Access
    Nature Communications
    Volume: 16, P: 1-10

  • The identification of Escherichia coli ycfD and human MINA53 and NO66 as ribosomal amino acid hydroxylases defines a role for 2-oxoglutarate/iron-dependent oxygenases in translational regulation.

    • Wei Ge
    • Alexander Wolf
    • Christopher J Schofield
    Research
    Nature Chemical Biology
    Volume: 8, P: 960-962

  • Trans-splicing-based methods that are independent of bacterial sequences and that allow the incorporation of RNA modifications enable the reliable synthesis of circular RNAs and enhance the efficiency of rolling circle translation.

    • Yifei Du
    • Philipp Konrad Zuber
    • V. Ramakrishnan
    ResearchOpen Access
    Nature Biomedical Engineering
    Volume: 9, P: 1062-1074

  • The authors report the structure of a human 48S translation initiation complex, finding a second molecule of eIF4A at the mRNA entry site, apart from the one present within the cap-binding complex eIF4F. This second entry-site eIF4A may be responsible for unwinding mRNA secondary structure.

    • Jailson Brito Querido
    • Masaaki Sokabe
    • V. Ramakrishnan
    ResearchOpen Access
    Nature Structural & Molecular Biology
    Volume: 31, P: 455-464

  • The structure of a bacterial ribosome–RelA complex reveals that RelA, a protein recruited to the ribosome in the case of scarce amino acids, binds in a different location to translation factors, and that this binding event suppresses auto-inhibition to activate synthesis of the (p)ppGpp secondary messenger, thus initiating stringent control.

    • Alan Brown
    • Israel S. Fernández
    • V. Ramakrishnan
    Research
    Nature
    Volume: 534, P: 277-280