Disease relevance of Avena sativa

• Toxicity of methyl tert-butyl ether to plants (Avena sativa, Zea mays, Triticum aestivum, and Lactuca sativa) [1].

High impact information on Avena sativa

• The subunit organization of the tonoplast H+-pumping ATPase from oat roots (Avena sativa L. var. Lang) was investigated [2].
• We have investigated the role of inositol 1,4,5-trisphosphate (InsP(3)) in the gravitropic response of oat (Avena sativa) shoot pulvini [3].
• We investigated the effects of light-dependent growth on the relative steady-state levels of the mRNAs and protein levels of alpha-tubulin and the epsilon-subunit of the chaperonin containing tailless complex protein-1 in oat (Avena sativa) coleoptiles, which were grown in different light conditions to establish different growth responses [4].
• We have further resolved these functional regions by analysis of N-terminal deletion and alanine-scanning mutants of oat (Avena sativa) phyA in transgenic tobacco (Nicotiana tabacum) [5].
• Four cereals, Hordeum vulgare (barley), Triticum aestivum (wheat), Secale cereal (rye), and Avena sativa (oat), were grown in a defined nutritional medium with and without the arbuscular mycorrhizal fungus Glomus intraradices [6].

Biological context of Avena sativa

• Gravitropism of oat (Avena sativa L.) and wheat (Triticum aestivum L.) coleoptiles was investigated in relation to the displacement angle or to the initially set stimulation angle (SA) [7].
• Thus, germination rate, biomass growth and antioxidative enzyme activity (i.e. superoxide dismutase, peroxidase, catalase and glutathione reductase) in three terrestrial plants (Avena sativa L., Brassica campestris L. cv. Chinensis, Lactuca sativa L. cv. hanson) were analyzed [8].
• Nucleotide sequence of oat (Avena sativa L.) cDNA encoding an auxin-binding protein (ABP1) [9].

Anatomical context of Avena sativa

• To assess the general importance of such Spd-protein complexes, we attempted bulk isolation from protoplasts of Petunia and oat (Avena sativa) [10].
• The effect of an in vivo and in vitro treatment with cadmium on transport activities of root plasma membrane enriched vesicles was studied in oat (Avena sativa L. cv. Argentina) plants [11].
• A suspension in dichloromethane-water (18:1, v/v) of various fractions containing hydroxycinnamic acid ester-ether bridges between lignin and polysaccharides prepared from cell walls of matured oat (Avena sativa L.) intemodes, and a solution of their acetates in the same solvent, were treated with 2,3-dichloro-5,6-dicyano-1,4-benzoquinone (DDQ) [12].

Associations of Avena sativa with chemical compounds

• The inhibitor N,N'-dicyclohexylcarbodiimide (DCCD) was used to probe the structure and function of the vacuolar H+-translocating ATPase from oat roots (Avena sativa var. Lang) [13].
• To distinguish between these theories, the pH dependence for auxin-induced growth of oat (Avena sativa L.) coleoptiles has been determined early and late in the elongation process [14].
• We solubilized 90% of the FCBP from oat (Avena sativa L. cv Victory) root PM in an active form with 1% octyl-glucoside [15].
• I examined the ability of frozen-thawed Avena sativa L. coleoptile sections under applied load to extend in response to the calcium chelators ethyleneglycol-bis-(beta-aminoethylether)-N,N,N',N'-tetraacetic acid (EGTA) and 2-[(2-bis-[carboxymethyl]amino-5-methylphenoxy)methyl]-6-methoxy-8-bis[carboxymethyl]aminoquinoline (Quin II) [16].
• Six chloroform/methanol-soluble proteins from oat endosperm (Avena sativa) have been isolated and characterized by a purification procedure based on extraction with volatile solvents, followed by reversed-phase high performance liquid chromatography [17].

Gene context of Avena sativa

• Here we describe removal of FMN from the LOV2 domain of Avena sativa using a hydrophobic matrix and successful incorporation of flavin adenine dinucleotide (FAD), riboflavin, and 5'-malonyl-riboflavin into the resulting apoprotein; 5-deaza-FMN was not incorporated under the applied conditions [18].
• In the C-terminal LOV2 domain of Avena sativa phototropin 1, formation of this bond triggers a conformational change that results in unfolding of a helix external to this domain called Jalpha [Harper, S. M., et al. (2003) Science 301, 1541-1545] [19].
• The influence of glycerol and chloroplast lipids on the spectral shifts of pigments associated with NADPH: protochlorophyllide oxidoreductase from Avena sativa L [20].
• A 60 kDa protein (P60) co-purified with phytochrome was identified as avenacosidase, a beta-glucosidase which is part of the defense system of Avena sativa [21].
• Here, we describe a simple procedure for purification of pigment-free POR from etioplasts of Avena sativa seedlings [22].

Analytical, diagnostic and therapeutic context of Avena sativa

• Europium uptake and partitioning in oat (Avena sativa) roots as studied by laser-induced fluorescence spectroscopy and confocal microscopy profiling technique [23].
• NAD-dependent BADH was purified from Avena sativa shoots by DEAE Sephacel, hydroxyapatite, 5'-AMP Sepharose 4B, Mono Q and TSK-GEL column chromatographies to homogeneity by the criterion of native PAGE, and the properties of BADH were compared with those of aminoaldehyde dehydrogenase purified to homogeneity from A. sativa [24].

References