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M

Mikhail A. Belozersky

Researcher at Moscow State University

Publications -  65
Citations -  1556

Mikhail A. Belozersky is an academic researcher from Moscow State University. The author has contributed to research in topics: Proteolytic enzymes & Protease. The author has an hindex of 23, co-authored 63 publications receiving 1393 citations. Previous affiliations of Mikhail A. Belozersky include Laboratory of Molecular Biology.

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Trypsin-like proteins of the fungi as possible markers of pathogenicity

TL;DR: The hypothesis that the expression of trypsin-like peptidases in fungi represents a marker of fungal phytopathogenicity is supported and the changes that occurred in STP of pathogenic fungi in the course of evolution represent specific adaptations to proteins of their respective hosts.
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Protein Bodies from Buckwheat Seed Cotyledons: Isolation and Characteristics

TL;DR: Cet article presente une methode d'isolement de grains d'aleurone intacts a partir de cotyledons de semences seches de sarrasin a partIR ofre de purete obtenu est eleve.
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Fungal proteolytic enzymes: Features of the extracellular proteases of xylotrophic basidiomycetes

TL;DR: In the present review, the features of the extracellular proteases of xylotrophic basidiomycetes are discussed and their biochemical characteristics and physiological role, as well as the regulation of their activity in the course of fungal growth are stressed.
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Localization of a metalloproteinase and its inhibitor in the protein bodies of buckwheat seeds

TL;DR: Cotyledons of dry buckwheat seeds were used to study the cellular localization of a metalloproteinase which performs in vitro the initial limited proteolysis of the main storage protein of the seed, and of its proteinaceous inhibitor.
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Fungal inhibitors of proteolytic enzymes: classification, properties, possible biological roles, and perspectives for practical use.

TL;DR: Fungal inhibitors extend the spectrum of known peptidase inhibitors potentially suitable for use in medicine and agriculture, and can be used for selective inhibition of peptidases responsible for initiation and development of pathogenic processes.