scispace - formally typeset
A

A. Lesley Jones

Researcher at University of Wales

Publications -  19
Citations -  925

A. Lesley Jones is an academic researcher from University of Wales. The author has contributed to research in topics: Fatty acid synthesis & Lipid metabolism. The author has an hindex of 10, co-authored 19 publications receiving 902 citations. Previous affiliations of A. Lesley Jones include Cardiff University.

Papers
More filters
Journal ArticleDOI

Aberrant interactions of transcriptional repressor proteins with the Huntington's disease gene product, huntingtin.

TL;DR: It is found that in Huntington's disease (HD) cortex and caudate, the cellular localization of these proteins is exclusively cytoplasmic whilst in control brain they are localized in the nucleus as well as the cy toplasm; mSin3A immunoreactivity also occurred in a subset of huntingtin positive intranuclear inclusions.
Book ChapterDOI

Lipid metabolism in algae.

TL;DR: This chapter focuses on groups of organisms (algae) that have been studied in reasonable detail and deals with organisms of increasing complexity, from the primitive cyanobacteria to marine macroalgae.
Journal ArticleDOI

Huntingtin interacts with cystathionine beta-synthase

TL;DR: An interaction with cystathionine beta-synthase (CBS) is detected in vitro using His-tagged CBS expressed in Escherichia coli, which was able to specifically bind both rat and human full-length huntingtin, suggesting a mechanism for such excitotoxic damage.
Journal ArticleDOI

Partial Characterisation of Murine Huntingtin and Apparent Variations in the Subcellular Localisation of Huntingtin in Human, Mouse and Rat Brain

TL;DR: Differences in the subcellular localisation of huntingtin between mouse and human brain are important in the context of mouse models for HD.
Journal ArticleDOI

Insoluble TATA-binding protein accumulation in Huntington's disease cortex.

TL;DR: TATA-binding protein labelling was relatively more abundant than huntingtin labelling and increased with the grade of the disease, suggesting that at least a proportion of this accumulated TBP exists as insoluble protein.