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Boris Vishnepolsky

Publications -  21
Citations -  632

Boris Vishnepolsky is an academic researcher. The author has contributed to research in topics: Antimicrobial peptides & Substitution matrix. The author has an hindex of 7, co-authored 18 publications receiving 365 citations.

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DBAASP v.2: an enhanced database of structure and antimicrobial/cytotoxic activity of natural and synthetic peptides.

TL;DR: A new version of the Database of Antimicrobial Activity and Structure of Peptides (DBAASPv.2), which is freely accessible at http://dbaasp.org, reports chemical structures and empirically-determined activities against more than 4200 specific target microbes for more than 2000 ribosomal, 80 non-ribosomal and 5700 synthetic peptides.
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DBAASP v3: database of antimicrobial/cytotoxic activity and structure of peptides as a resource for development of new therapeutics.

TL;DR: The Database of Antimicrobial Activity and Structure of Peptides (DBAASP) is an open-access, comprehensive database containing information on amino acid sequences, chemical modifications, 3D structures, bioactivities and toxicities of peptides that possess antimicrobial properties.
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DBAASP: database of antimicrobial activity and structure of peptides.

TL;DR: The Database of Antimicrobial Activity and Structure of Peptides (DBAASP) is a manually curated database for those peptides for which antimicrobial activity against particular targets has been evaluated experimentally.
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Predictive Model of Linear Antimicrobial Peptides Active against Gram-Negative Bacteria.

TL;DR: A predictive model of linear AMPs being active against particular Gram-negative strains relying on a semi-supervised machine-learning approach with a density-based clustering algorithm is presented.
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Prediction of linear cationic antimicrobial peptides based on characteristics responsible for their interaction with the membranes.

TL;DR: A new simple algorithm of prediction is developed and evaluation of efficacies of the characteristics as descriptors performed show that three descriptors, hydrophobic moment, charge density and location of the peptide along the membranes, can be used as discriminators of LCAPs.