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Showing 1–8 of 8 results
Advanced filters: Author: Gracjan Michlewski Clear advanced filters
  • hnRNP A1 is an auxiliary factor that promotes the Microprocessor-mediated processing of pri-mir-18a, of the oncomiR-1 cluster. Here the authors employ an integrative structural biology approach and provide insights into the molecular mechanism of how hnRNP A1 facilitates pri-mir-18a biogenesis.

    • Hamed Kooshapur
    • Nila Roy Choudhury
    • Michael Sattler
    ResearchOpen Access
    Nature Communications
    Volume: 9, P: 1-17
  • The RNA-binding ubiquitin E3 ligase TRIM25 plays a critical role in antiviral immunity. Here the authors identify key RNA-binding residues of TRIM25, link RNA binding to antiviral activity, reveal RNA structural and sequence preferences, and investigate binding to the viral genome.

    • Lucía Álvarez
    • Kevin Haubrich
    • Janosch Hennig
    ResearchOpen Access
    Nature Communications
    Volume: 15, P: 1-15
  • microRNAs regulate gene expression and control cell fate and differentiation processes. In this work, Nowak et al. reveal that brain-specific miR-9 is under post-transcriptional control and that the pre-miR-9 binding protein Lin28a decreases the levels of mature miR-9 during retinoic acid-mediated neuronal differentiation.

    • Jakub S. Nowak
    • Nila Roy Choudhury
    • Gracjan Michlewski
    ResearchOpen Access
    Nature Communications
    Volume: 5, P: 1-12
  • The Drosha–DGCR8, or Microprocessor, complex, is required for microRNA biogenesis. DGCR8 recognizes the RNA substrates, whereas Drosha functions as an endonuclease. High-throughput sequencing and cross-linking immunoprecipitation (HITS-CLIP) analyses reveal many other RNA targets of DGCR8 besides microRNAs, including snoRNAs, which are processed in a Drosha-independent manner, as well as long noncoding RNAs and mRNAs of protein-coding genes.

    • Sara Macias
    • Mireya Plass
    • Javier F Cáceres
    Research
    Nature Structural & Molecular Biology
    Volume: 19, P: 760-766
  • let-7a, a miRNA involved in differentiation, was known to be regulated by Lin-28. Now work reveals another factor that could control let-7a levels in vivo: hnRNP A1 binds to unprocessed pri-let-7a and inhibits its processing by Drosha. The inhibitory effect of hnRNP A1 is further shown to occur via antagonizing the binding of KSRP to pri-let-7a, which is known to promote biogenesis.

    • Gracjan Michlewski
    • Javier F Cáceres
    Research
    Nature Structural & Molecular Biology
    Volume: 17, P: 1011-1018