Powdery mildews are a diverse group of pathogenic fungi that can infect a large number of plant species, including many economically important crops. However, basic and applied research on these devastating diseases has been hampered by the obligate biotrophic lifestyle of the pathogens, which require living host cells for growth and reproduction, and lacking genetic and molecular tools for imp...

Crude extracts and active principles from medicinal plants have shown potential role in controlling plant diseases in glasshouses as well as in fields as one of the safest and ecofriendly methods. The effect of nor-securinine (an alkaloid) isolated from Phyllanthus amarus has been seen against spore germination of some fungi (Alternaria brassicae, A. solani, Curvularia pennisetti, Curvularia sp...

Habrobracon females homozygous for the mutant ebony produce about 5% mosaic progeny among fertilized eggs. The present experiment demonstrates by means of a test-cross method that in the production of these mosaics only one pronucleus is involved, and that this nucleus cleaves before union of one of its daughter nuclei with the sperm nucleus.

Grapevine powdery mildew, caused by the ascomycete Erysiphe necator, is a major threat to grapes worldwide. Despite its global impact on grape production, E. necator is sensitive to adverse environmental conditions, such as excess heat, free water and UV radiation. Using detached leaf co-culture assays, 3-d-old single colonies of E. necator were exposed to 1, 2 or 3 consecutive d of punctuated ...

the erysiphaceae are obligatory parasitic fungi that cause powdery mildew disease of green space plants. during this study, powdery mildew fungi were collected and identified from different localities of ardabil landscape, iran. erysiphe rayssiae (on spartium junceum), erysiphe robiniae var. robiniae (on robinia pseudoacacia) and euoidium cf. agerati (on ageratum houstonianum)are new records fo...

Four positively-charged residues, namely betaLys-155, betaArg-182, betaArg-246, and alphaArg-376 have been identified as Pi binding residues in Escherichia coli ATP synthase. They form a triangular Pi binding site in catalytic site betaE where substrate Pi initially binds for ATP synthesis in oxidative phosphorylation. Positive electrostatic charge in the vicinity of betaArg-246 is shown to be ...