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Showing 1–12 of 12 results
Advanced filters: Author: Shintaro Aibara Clear advanced filters

  • Chloroplasts of plants have ribosomes that are important for translation of core proteins involved in photosynthesis. Here, Perez Boerema et al. report a high-resolution cryo-EM structure of the spinach chlororibosome in complex with its accessory factors.

    • Annemarie Perez Boerema
    • Shintaro Aibara
    • A. Amunts
    Research
    Nature Plants
    Volume: 4, P: 212-217

  • Cardiac amyloidosis is caused by misfolded protein fibrils in the heart. Here, authors describe the structure of ApoAIV amyloid found together with TTR amyloid in patient heart tissue, underscoring the need for broad spectrum therapies.

    • Shintaro Aibara
    • Astrid Kassner
    • Taiana Maia de Oliveira
    ResearchOpen Access
    Nature Communications
    Volume: 16, P: 1-6

  • The high-resolution structure of the mammalian pre-initiation complex in different functional states provides detailed insights into the mechanism of transcription initiation.

    • Shintaro Aibara
    • Sandra Schilbach
    • Patrick Cramer
    Research
    Nature
    Volume: 594, P: 124-128

  • 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

  • Under conditions of nutrient limitation, bacterial ribosomes undergo dimerization, forming a 100S complex that is translationally inactive. Here the authors present the structural basis for formation of the 100S complexes in Gram-positive bacteria, shedding light on the mechanism of translation suppression by the ribosome-silencing factors.

    • Donna Matzov
    • Shintaro Aibara
    • Ada E. Yonath
    ResearchOpen Access
    Nature Communications
    Volume: 8, P: 1-7

  • Mitochondrial ribosome biogenesis requires the assistance of multiple assembly factors. Here, the authors provide insights into the essential role of the GTPase MTG3 during small subunit biogenesis and a potential coupling to translation initiation.

    • Marleen Heinrichs
    • Anna Franziska Finke
    • Ricarda Richter-Dennerlein
    ResearchOpen Access
    Nature Communications
    Volume: 16, P: 1-16

  • Cryo-EM structures of two late-stage assembly intermediates of the human mitoribosomal large subunit reveal the timing of rRNA folding and protein incorporation during the final steps of ribosomal maturation and identify two new assembly factors.

    • Alan Brown
    • Sorbhi Rathore
    • V Ramakrishnan
    Research
    Nature Structural & Molecular Biology
    Volume: 24, P: 866-869

  • Assembly of the small ribosomal subunit from an RNA strand and 33 proteins is an intricate and dynamic process. Two cryo-EM studies now provide insight into a complicated complex of at least 51 trans-factors that act on the preribosomal small subunit to sequentially fold it into a 3D molecular machine.

    • Joanna Rorbach
    • Shintaro Aibara
    • Alexey Amunts
    News & Views
    Nature Structural & Molecular Biology
    Volume: 24, P: 879-881

  • RNA polymerase II needs to be imported into the nucleus to perform transcription. Fianu et al. show that RPAP2 binds to Pol II and enters the nucleus with it, before releasing it to perform transcription and returning to the cytoplasm.

    • Isaac Fianu
    • Christian Dienemann
    • Patrick Cramer
    ResearchOpen Access
    Communications Biology
    Volume: 4, P: 1-7