The Effect of Bean Seed Treatment with Entomopathogenic Fungus on Soil Microarthropods (Acari, Collembola).

The treatment of agricultural crops with entomopathogenic fungi may disturb the structure of soil microarthropod communities, which can have an adverse impact on soil fertility and, ultimately, on the yield. The effect of the treatment of broad bean ( L.) seeds, with the entomopathogenic fungus , on the abundance and community structure of soil microarthropods in the rhizosphere was assessed in different phases of plant vegetation in a two-year experiment.

Effect of the Entomopathogenic Fungus Beauveria bassiana on the Development of Faba Bean (Vicia faba) Diseases in the Field Conditions.

Several ascomycetous entomopathogenic fungi, including species in the genera Beauveria, are plant symbionts/endophytes and are termed as endophytic insect-pathogenic fungi. It was shown that the fungus Beauveria bassiana (BBK-1 strain) successfully colonized Vicia faba bean plants in laboratory and field conditions of Western Siberia. The B.

Desialylation of surface receptors as a new dimension in cell signaling.

Terminal sialic acid residues are found in abundance in glycan chains of glycoproteins and glycolipids on the surface of all live cells forming an outer layer of the cell originally known as glycocalyx. Their presence affects the molecular properties and structure of glycoconjugates, modifying their function and interactions with other molecules. Consequently, the sialylation state of glycoproteins and glycolipids has been recognized as a critical factor modulating molecular recognitions inside the cell, between the cells, between the cells and the extracellular matrix, and between the cells and certain exogenous pathogens.

The stoichiometry of protein phosphorylation in adipocyte lipid droplets: analysis by N-terminal isotope tagging and enzymatic dephosphorylation.

Most phosphoproteomic studies to date have been limited to the identification of phosphoproteins and their phosphorylation sites, and have not assessed the stoichiometry of protein phosphorylation, a critical parameter reflecting the dynamic equilibrium between phosphorylated and non-phosphorylated pools of proteins. Here, we used a method for measuring phosphorylation stoichiometry through isotope tagging and enzymatic dephosphorylation of tryptic peptides. Using this method, protein digests are divided into two equal aliquots that are modified with either light or heavy isotope tags.