Publications by authors named "P Mikshina"

Celery () can be considered as a model plant for studying pectin-enriched primary cell walls. In addition to parenchyma cells with xyloglucan-deficient walls, celery petioles contain collenchyma, a mechanical tissue with thickened cell walls of similar composition. This study presents a comprehensive analysis of these tissues at both early and late developmental stages, integrating data on polysaccharide yield, composition, localization, and transcriptome analysis.

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Disruption of cholinesterases and, as a consequence, increased levels of acetylcholine lead to serious disturbances in the functioning of the nervous system, including death. The need for rapid administration of an antidote to restore esterase activity is critical, but practical implementation of this is often difficult. One promising solution may be the development of antidote delivery systems that will release the drug only when acetylcholine levels are elevated.

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Many phytopathogens' gene products that contribute to plant-pathogen interactions remain unexplored. In one of the most harmful phytopathogenic bacterium (), phosphonate-related genes have been previously shown to be among the most upregulated following host plant colonization. However, phosphonates, compounds characterized by a carbon-phosphorus bond in their composition, have not been described in species and other phytopathogenic bacteria, with the exception of and .

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Microorganisms produce a wide variety of polysaccharides. Due to biosafety considerations, lactic acid bacteria (LAB) are popular producers of exopolysaccharides (EPS) for various applications. In this study, we analyzed the composition and properties of EPS produced by L.

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Glycan-binding specificity was studied for Jacalin, RCA 120, SBA, PHA-L, PHA-E, WGA, UEA, AAL, LTL, LEL, SNA, DSA, LCA, MAH and Con A, lectins widely used in histochemistry. Oligosaccharide- and polysaccharide-based glycan arrays were applied. Expected specificity was confirmed for only 6 of the 15 lectins and the glycan binding profiles of some lectins were dramatically broader than generally accepted.

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