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Showing 1–19 of 19 results
Advanced filters: Author: Ronald Micura Clear advanced filters
  • The reliable design of small-molecule binders to target RNAs remains challenging. Recognizing hidden pockets that are transiently occupied by intramolecular nucleobase intercalation brings us closer to achieving this goal.

    • Alexander K. Pichler
    • Przemyslaw Wanat
    • Ronald Micura
    News & Views
    Nature Chemical Biology
    P: 1-2
  • How do pathogens survive temperature variations? At a molecular level, one bacterial species seems to regulate gene expression in response to temperature through structural equilibria in corresponding RNA sequences. See Letter p.355

    • Ronald Micura
    News & Views
    Nature
    Volume: 499, P: 289-290
  • Small-molecule ligands have been developed that covalently attach to their cognate RNA aptamers in vitro and in living cells. This strategy opens up new avenues for RNA imaging applications (for example, FRAP), for direct fluorescence detection of RNA pull-downs or for covalent RNA-targeted drug design.

    • Raphael Bereiter
    • Laurin Flemmich
    • Ronald Micura
    ResearchOpen Access
    Nature Chemical Biology
    Volume: 21, P: 843-854
  • In humans, protein methyltransferase is responsible for RNA methylation using S-adenosylmethionine as a methyl group donor. Here the authors report a self-methylation activity of a bacterial riboswitch.

    • Laurin Flemmich
    • Sarah Heel
    • Ronald Micura
    ResearchOpen Access
    Nature Communications
    Volume: 12, P: 1-10
  • Riboswitches are conserved RNA domains located in the non-coding region of mRNA that recognize cellular metabolites and, in turn, regulate gene expression. Here the authors report the structure of the recently identified SAM-VI riboswitch and provide insight into its mechanism of ligand discrimination.

    • Aiai Sun
    • Catherina Gasser
    • Aiming Ren
    ResearchOpen Access
    Nature Communications
    Volume: 10, P: 1-13
  • Twisters ribozymes are a recently discovered class of non-coding, site-specific self-cleaving RNAs. Here Ren et al. describe a crystal structure of the env22twister ribozyme, propose an ion coordination and catalytic mechanism, and contrast their findings with those of two recently reported twister structures.

    • Aiming Ren
    • Marija Košutić
    • Dinshaw J. Patel
    Research
    Nature Communications
    Volume: 5, P: 1-10
  • Structural and biochemical analysis of the recently discovered env25 pistol ribozyme reveal an active site containing a pseudoknot that enforces in-line nucleophilic attack at the scissile phosphate and positions nucleotides for general acid and general base catalysis.

    • Aiming Ren
    • Nikola Vušurović
    • Dinshaw J Patel
    Research
    Nature Chemical Biology
    Volume: 12, P: 702-708
  • Twister-sister is a self-cleaving ribozyme. Here, the authors report the 2.0 Å crystal structure of the four-way junctional twister-sister ribozyme in the pre-catalytic state and discuss mechanistic implications based on their mutagenesis experiments and comparisons with other ribozyme structures.

    • Luqian Zheng
    • Elisabeth Mairhofer
    • Aiming Ren
    ResearchOpen Access
    Nature Communications
    Volume: 8, P: 1-12
  • SAM riboswitches are RNA elements that regulate bacterial gene expression in response to binding of the small-molecule metabolite, S-adenosylmethionine. The SAM-II riboswitch binds its ligand through a conformational capture mechanism that is dependent on formation of a transient pseudoknot.

    • Andrea Haller
    • Ulrike Rieder
    • Ronald Micura
    Research
    Nature Chemical Biology
    Volume: 7, P: 393-400
  • The recognition of the mRNA codon by the tRNA anticodon is crucial for protein synthesis. Here the authors introduce non-standard nucleotides in bacterial and eukaryotic mRNA to reveal the minimal hydrogen bond requirement of codon-anticodon interaction for efficient and accurate translation.

    • Thomas Philipp Hoernes
    • Klaus Faserl
    • Matthias David Erlacher
    ResearchOpen Access
    Nature Communications
    Volume: 9, P: 1-12
  • Modified chromosome conformation capture (Hi-C) technology is used to characterize the interactions between sister chromatids, despite their identical DNA sequences.

    • Michael Mitter
    • Catherina Gasser
    • Daniel W. Gerlich
    Research
    Nature
    Volume: 586, P: 139-144
  • The innate immune system relies on a series of specific receptors that recognize RNAs that might come from viruses. The structure of the C terminal domain of one such receptor, RIG-I, in complex with 5'ppp-dsRNA, now indicates the basis of recognition of the observable 5'pp-RNA, through interactions that are shown to be needed for tight binding and a cellular response to this trigger.

    • Yanli Wang
    • Janos Ludwig
    • Dinshaw J Patel
    Research
    Nature Structural & Molecular Biology
    Volume: 17, P: 781-787
  • Elongation factor G (EF-G) is an essential GTPase involved in translation, but how the translocating ribosome activates EF-G remains an open question. Nucleotide functional group mutagenesis implicates A2660 of 23S rRNA as the trigger of GTPase hydrolysis by EF-G.

    • Nina Clementi
    • Anna Chirkova
    • Norbert Polacek
    Research
    Nature Chemical Biology
    Volume: 6, P: 344-351
  • The combination of single-cell RNA sequencing with metabolic RNA labelling enables a time-resolved view of transcriptional responses in individual cells. In this Primer, Erhard and Saliba et al. discuss metabolic labelling approaches and how to assess the temporal dynamics of transcriptional responses in different conditions.

    • Florian Erhard
    • Antoine-Emmanuel Saliba
    • Lars Dölken
    Reviews
    Nature Reviews Methods Primers
    Volume: 2, P: 1-18
  • This protocol combines in situ chromosome conformation capture with labeling of nascent DNA with the synthetic nucleoside 4-thio-thymidine to generate genome-wide contact probability maps within and across sister chromatids in mammalian cells.

    • Michael Mitter
    • Zsuzsanna Takacs
    • Daniel W. Gerlich
    Protocols
    Nature Protocols
    Volume: 17, P: 1486-1517