Kyle C. Dent
University of Leeds
4 Papers
Kyle C. Dent is an academic researcher from University of Leeds. The author has contributed to research in topics: Genome & Capsid. The author has an hindex of 4, co-authored 4 publications.
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Papers
Nucleocapsid protein structures from orthobunyaviruses reveal insight into ribonucleoprotein architecture and RNA polymerization
Antonio Ariza,Sian J. Tanner,Cheryl T. Walter,Kyle C. Dent,Dale A. Shepherd,Weining Wu,Susan V. Matthews,Julian A. Hiscox,Todd Green,Ming Luo,Richard M. Elliott,Anthony R. Fooks,Alison E. Ashcroft,Nicola J. Stonehouse,Neil A. Ranson,John N. Barr,Thomas A. Edwards +16 more
TL;DR: Comparison between these crystal structures and electron microscopy images of both soluble tetramers and authentic RNPs suggests the N protein does not bind RNA as a repeating monomer; thus, it represents a newly described architecture for bunyavirus RNP assembly, with implications for many other segmented negative-strand RNA viruses.
Direct visualization of the small hydrophobic protein of human respiratory syncytial virus reveals the structural basis for membrane permeability.
Stephen D. Carter,Kyle C. Dent,Elizabeth Atkins,Toshana L. Foster,Mark Verow,Petra Gorny,Mark Harris,Julian A. Hiscox,Neil A. Ranson,Stephen Griffin,John N. Barr +10 more
TL;DR: MINT‐7890784, MINT-7890776: SH (uniprot kb:P04852) and SH ( uniprotkb:P02452) bind (MI:0407) by electron microscopy by electron microscope.
The Asymmetric Structure of an Icosahedral Virus Bound to Its Receptor Suggests a Mechanism for Genome Release
Kyle C. Dent,Rebecca F. Thompson,Amy M. Barker,Julian A. Hiscox,John N. Barr,Peter G. Stockley,Neil A. Ranson +6 more
TL;DR: An asymmetric structure of bacteriophage MS2, attached to its receptor, the F-pilus, is reported, which can fulfill its known biological roles in receptor and genome binding and suggests an exit route for the genome during infection.
Mechanisms of assembly and genome packaging in an RNA virus revealed by high-resolution cryo-EM
Emma L. Hesketh,Yulia Meshcheriakova,Kyle C. Dent,Pooja Saxena,Pooja Saxena,Rebecca F. Thompson,Joseph J.B. Cockburn,George P. Lomonossoff,Neil A. Ranson +8 more
TL;DR: Cryo-electron microscopy reconstructions for the wild-type virus and an empty virus-like particle are determined and built and reveal the C-terminal region of the small coat protein subunit, essential for virus assembly and which was missing from previously determined crystal structures, allowing a new model for genome encapsidation and capsid assembly to be developed.