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Ahmed Faik

Researcher at Ohio University

Publications -  42
Citations -  1850

Ahmed Faik is an academic researcher from Ohio University. The author has contributed to research in topics: Xyloglucan & Cell wall. The author has an hindex of 22, co-authored 41 publications receiving 1681 citations. Previous affiliations of Ahmed Faik include Michigan State University & Centre national de la recherche scientifique.

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An Arabidopsis gene encoding an α-xylosyltransferase involved in xyloglucan biosynthesis

TL;DR: It is reported that etiolated pea microsomes contain an α-xylosyltransferase that catalyzes the transfer of xylose from UDP-[14C]xylose onto β(1,4)-linked glucan chains, and it is concluded that this Arabidopsis gene encodes an β-glucan synthase activity involved in xyloglucan biosynthesis.
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Supercritical carbon dioxide pretreatment of corn stover and switchgrass for lignocellulosic ethanol production.

TL;DR: The pretreatment method showed very limited improvement in glucose yield for switchgrass and X-ray diffraction results indicated no change in crystallinity of the SC-CO(2) treated corn stover when compared to the untreated, while SEM images showed an increase in surface area.
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Arabidopsis thaliana RGXT1 and RGXT2 Encode Golgi-Localized (1,3)-α-d-Xylosyltransferases Involved in the Synthesis of Pectic Rhamnogalacturonan-II

TL;DR: Results suggest that RGXT1 and RGXT2 encode Golgi-localized (1,3)-α-d-xylosyltransferases involved in the biosynthesis of pectic rhamnogalacturonan-II, a complex polysaccharide essential to vascular plants.
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A Glucurono(arabino)xylan Synthase Complex from Wheat Contains Members of the GT43, GT47, and GT75 Families and Functions Cooperatively

TL;DR: The results provide a direct link of the involvement of TaGT43-4, TaGT47-13, and TaGT75-4 proteins (as a core complex) in the synthesis of GAX polymer in wheat.
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Biochemical Characterization and Molecular Cloning of an α-1,2-Fucosyltransferase That Catalyzes the Last Step of Cell Wall Xyloglucan Biosynthesis in Pea

TL;DR: Kinetic analysis indicates that GDP-fucose and xyloglucan associate with the enzyme in a random order, although several other amino acid-modifying reagents strongly inhibited activity.