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Alexander A. Vassilevski

Researcher at Russian Academy of Sciences

Publications -  81
Citations -  2150

Alexander A. Vassilevski is an academic researcher from Russian Academy of Sciences. The author has contributed to research in topics: Spider toxin & Peptide. The author has an hindex of 28, co-authored 76 publications receiving 1848 citations. Previous affiliations of Alexander A. Vassilevski include Moscow State University & Moscow Institute of Physics and Technology.

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Molecular diversity of spider venom

TL;DR: Spider venom, a factor that has played a decisive role in the evolution of one of the most successful groups of living organisms, is reviewed and special attention is given to the structure, properties, and biosynthesis of toxins of polypeptide nature.
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Latarcins, Antimicrobial and Cytolytic Peptides from the Venom of the Spider Lachesana tarabaevi (Zodariidae) That Exemplify Biomolecular Diversity

TL;DR: Seven novel short linear antimicrobial and cytolytic peptides named latarcins were purified from the venom of the spider Lachesana tarabaevi and showed to adopt amphipathic α-helical structure in membrane-mimicking environment by CD spectroscopy.
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Disulfide-stabilized Helical Hairpin Structure and Activity of a Novel Antifungal Peptide EcAMP1 from Seeds of Barnyard Grass (Echinochloa crus-galli)

TL;DR: Close spatial structure similarity between EcAMP1, the trypsin inhibitor VhTI from seeds of Veronica hederifolia, and some scorpion and cone snail toxins suggests natural elaboration of different functions on a common fold.
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Cyanogen bromide cleavage of proteins in salt and buffer solutions.

TL;DR: It is shown that the commonly used Tris-HCl, sodium phosphate, NaCl, imidazole, and guanidine-hCl do not interfere with the reaction under acidic conditions and omitting the desalting step does not decrease the final yields of target products, as demonstrated for fusion proteins of different origin and composition.
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A novel antifungal hevein-type peptide from Triticum kiharae seeds with a unique 10-cysteine motif

TL;DR: Two forms of a novel antimicrobial peptide (AMP) that differ by a single C‐terminal amino acid residue and belong to a new structural type of plant AMP were purified from seeds of Triticum kiharae Dorof and successfully produced in Escherichia coli.