scispace - formally typeset
J

Jonathan D. Dinman

Researcher at University of Maryland, College Park

Publications -  166
Citations -  8337

Jonathan D. Dinman is an academic researcher from University of Maryland, College Park. The author has contributed to research in topics: Translational frameshift & Ribosome. The author has an hindex of 52, co-authored 158 publications receiving 7404 citations. Previous affiliations of Jonathan D. Dinman include University of Maryland, Baltimore & Medical University of South Carolina.

Papers
More filters
Journal ArticleDOI

A -1 ribosomal frameshift in a double-stranded RNA virus of yeast forms a gag-pol fusion protein.

TL;DR: Analysis of the "slippery site" suggests that a low probability of unpairing of the aminoacyl-tRNA from the 0-frame codon at the ribosomal A site reduces the efficiency of frameshifting more than the reluctance of a given tRNA to have its wobble base mispaired.
Journal ArticleDOI

rRNA pseudouridylation defects affect ribosomal ligand binding and translational fidelity from yeast to human cells.

TL;DR: Describing ribosomes isolated from a yeast strain in which Cbf5p, the yeast homolog of DKC1, is catalytically impaired through a D95A mutation reveals specific roles for Ψ modification in ribosome-ligand interactions that are conserved in yeast, mouse, and humans.
Journal ArticleDOI

Ribosomal frameshifting efficiency and gag/gag-pol ratio are critical for yeast M1 double-stranded RNA virus propagation.

TL;DR: In this paper, the importance of frameshifting efficiency for viral propagation was tested in a system where the M1 (killer toxin-encoding) satellite RNA is supported by a full-length L-A cDNA clone.
Journal ArticleDOI

Trajectories of the ribosome as a Brownian nanomachine.

TL;DR: This work presents a new analytical approach capable of determining the free-energy landscape and the continuous trajectories of molecular machines from a large number of snapshots obtained by cryogenic electron microscopy and allows model-free quantitative analysis of the degrees of freedom and the energy landscape underlying continuous conformational changes in nanomachines, including those important for biological function.