Filter By:

Journal Check one or more journals to show results from those journals only.

Choose more journals

Article type Check one or more article types to show results from those article types only.
Subject Check one or more subjects to show results from those subjects only.
Date Choose a date option to show results from those dates only.

Custom date range

Clear all filters
Sort by:
Showing 1–5 of 5 results
Advanced filters: Author: Jeffrey A Pleiss Clear advanced filters
  • Branch point selection is required for pre-mRNA splicing, and its mis-regulation is associated with many diseases. Two structural studies provide insights into the dynamics of active site formation and the spliceosomal proteins that may contribute to activation of the correct branch point in eukaryotic introns.

    • Sara R. Downs
    • Bec Grace
    • Jeffrey A. Pleiss
    News & Views
    Nature Structural & Molecular Biology
    Volume: 31, P: 732-734
  • The spliceosome is a complex small nuclear RNA–protein machine that removes introns from pre-mRNAs. A single-molecule fluorescence resonance emission transfer (FRET) assay using the efficiently spliced yeast pre-mRNA, Ubc4, reveals many reversible, time- and ATP-dependent changes in conformation for individual pre-mRNAs and indicates that spliceosome assembly occurs close to thermal equilibrium.

    • John Abelson
    • Mario Blanco
    • Nils G Walter
    Research
    Nature Structural & Molecular Biology
    Volume: 17, P: 504-512
  • In this comment, the authors discuss the potentially widespread problem of selection bias in drawing biological conclusions from RNA sequencing data.

    • Zachary W. Dwyer
    • Jeffrey A. Pleiss
    Comments & OpinionOpen Access
    Nature Communications
    Volume: 14, P: 1-5
  • The Brr2 ATPase is a large DExD/H-box helicase required for key snRNA-remodeling steps during the splicing reaction. The structure of part of Brr2, in conjunction with modeling and functional analysis, indicates that it probably resembles the Hel308 DNA helicase and may share a similar helicase mechanism.

    • Lingdi Zhang
    • Tao Xu
    • Rui Zhao
    Research
    Nature Structural & Molecular Biology
    Volume: 16, P: 731-739