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Antoni R. Slabas

Researcher at Durham University

Publications -  171
Citations -  7580

Antoni R. Slabas is an academic researcher from Durham University. The author has contributed to research in topics: Acyl carrier protein & Reductase. The author has an hindex of 49, co-authored 171 publications receiving 7194 citations. Previous affiliations of Antoni R. Slabas include University of London.

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Immunological detection of NADH-specific enoyl-ACP reductase from rape seed (Brassica napus) — induction, relationship of α and β polypeptides, mRNA translation and interaction with ACP

TL;DR: In vitro translation experiments show that the enzyme is nuclear coded and synthesized as a precursor form and it is shown that ACP-Sepharose may be used as a matrix in the purification of enoyl-ACP reductase.
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A Zea mays GTP-binding protein of the ARF family complements an Escherichia coli mutant with a temperature-sensitive malonyl-coenzyme A:acyl carrier protein transacylase.

TL;DR: Complementation of a mutation affecting bacterial membrane lipid biosynthesis by a plant ARF protein, could indicate the existence of as yet unidentified bacterial equivalents of this ubiquitous eucaryotic GTP-binding protein.
Journal ArticleDOI

Biosynthesis and regulation of fatty acids and triglycerides in oil seed rape. Current status and future trends

TL;DR: Le recent sequencage du genome entier de l'Arabidopsis (plante de la famille de cruciferes comme le colza) constitue un outil puissant pour les chercheurs qui etudient la biosynthese of l'huile and sa regulation.
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A Novel Function for Arabidopsis CYCLASE1 in Programmed Cell Death Revealed by Isobaric Tags for Relative and Absolute Quantitation (iTRAQ) Analysis of Extracellular Matrix Proteins

TL;DR: CYCLASE1, which had no known function hitherto, is a negative regulator of cell death and regulates pathogen-induced symptom development in Arabidopsis and is selected for further analysis using reverse genetics.
Patent

Recombinant plant enzyme

TL;DR: In this paper, a nucleotide sequence encoding an enzyme having acyl-ACP thioesterase activity comprising nucleotides 169-1269 of the sequence shown in Figure 1 or functional equivalents thereof was disclosed.