A
Alexei P. Donchenko
Researcher at USSR Academy of Medical Sciences
Publications - 15
Citations - 2815
Alexei P. Donchenko is an academic researcher from USSR Academy of Medical Sciences. The author has contributed to research in topics: RNA & Proteases. The author has an hindex of 9, co-authored 15 publications receiving 2756 citations.
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Two related superfamilies of putative helicases involved in replication, recombination, repair and expression of DNA and RNA genomes
TL;DR: A degree of similarity was revealed between the consensus pattern of conserved amino acid residues derived for the new superfamily and that of another recently described protein superfamily including a different set of prokaryotic, eukaryotic and viral (putative) helicases.
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Cysteine proteases of positive strand RNA viruses and chymotrypsin-like serine proteases. A distinct protein superfamily with a common structural fold.
TL;DR: The His residue previously implicated in catalysis, together with two partially conserved Gly residues, is predicted to constitute part of the substrate‐binding pocket of 3C proteases, providing the first example of relatedness between proteases belonging, by definition, to different classes.
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Coronavirus genome: prediction of putative functional domains in the non-structural polyprotein by comparative amino acid sequence analysis
TL;DR: A partial tentative scheme for the functional organization and expression strategy of the non-structural polyproteins of IBV implies that, despite the general similarity to other positive strand RNA viruses, and particularly to potyviruses, coronaviruses possess a number of unique structural and functional features.
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A novel superfamily of nucleoside triphosphate-binding motif containing proteins which are probably involved in duplex unwinding in DNA and RNA replication and recombination.
TL;DR: A statistically significant similarity was demonstrated between the amino acid sequences of 4 Escherichia coli helicases and helicase subunits, a family of non‐structural proteins of eukaryotic positive‐strand RNA viruses and 2 herpesvirus proteins, and a generalized structural model for the ATP‐binding core is proposed.
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N-terminal domains of putative helicases of flavi- and pestiviruses may be serine proteases
TL;DR: It is suggested that flavivirus NS3 and the respective pestivirus protein contain at least two functional domains, the N-proximal protease and the C- Proximal helicase one, which is probably involved in the processing of viral non-structural proteins.