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Richard Moxon

Researcher at University of Oxford

Publications -  45
Citations -  3150

Richard Moxon is an academic researcher from University of Oxford. The author has contributed to research in topics: Haemophilus influenzae & Nucleic acid. The author has an hindex of 20, co-authored 44 publications receiving 2947 citations. Previous affiliations of Richard Moxon include John Radcliffe Hospital & University of Queensland.

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The minimum information about a genome sequence (MIGS) specification.

Dawn Field, +71 more
- 01 May 2008 - 
TL;DR: Here, the minimum information about a genome sequence (MIGS) specification is introduced with the intent of promoting participation in its development and discussing the resources that will be required to develop improved mechanisms of metadata capture and exchange.
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Bacterial Contingency Loci: The Role of Simple Sequence DNA Repeats in Bacterial Adaptation

TL;DR: How bacterial pathogens exploit localized hypermutation, through polymerase slippage of simple sequence repeats (SSRs), to generate phenotypic variation and enhanced fitness is reviewed.
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Microbiology in the post-genomic era

TL;DR: The evolving field of bacterial typing and the genomic technologies that enable comparative analysis of multiple genomes and the metagenomes of complex microbial environments are reviewed, and the implications of the genomic era for the future of microbiology are addressed.
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Neisseria meningitidis GNA2132, a heparin-binding protein that induces protective immunity in humans

TL;DR: It is shown that GNA2132 induces protective immunity in humans and it is recognized by sera of patients after meningococcal disease, and the protein binds heparin in vitro through an Arg-rich region and this property correlates with increased survival of the unencapped bacterium in human serum.
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Sialic acid transport in Haemophilus influenzae is essential for lipopolysaccharide sialylation and serum resistance and is dependent on a novel tripartite ATP‐independent periplasmic transporter

TL;DR: It is demonstrated that N‐acetylneuraminic acid (Neu5Ac or sialic acid) uptake in H.’influenzae is essential for the subsequent modification of the LPS and that this uptake is mediated through a single transport system which is a member of the tripartite ATP‐independent periplasmic (TRAP) transporter family.