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Cited by 255

The DOI matches its Crossref record; 27 of the 27 references it cites were found in a registry or an index.

N-terminal domains of putative helicases of flavi- and pestiviruses may be serine proteases

Open access
Gorbalenya, Alexander E., Donchenko, Alexei P., Koonin, Eugene V., Blinov, Vladimir M.·1989·Nucleic Acids Research

Abstract

Recently we tentatively identified, by sequence comparison, central domains of the NS3 proteins of flaviviruses and the respective portion of the pestivirus polyprotein as RNA helicases (A.E.G. et al., submitted). Alignment of the N-proximal domains of the same proteins revealed conservation of short sequence stretches resembling those around the catalytic Ser, His and Asp residues of chymotrypsin-like proteases. A statistically significant similarity has been detected between the sequences of these domains and those of the C-terminal serine protease domains of alphavirus capsid proteins. 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. The protease domain is probably involved in the processing of viral non-structural proteins.

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Crossref · 10.1093/nar/17.10.3889

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Metadata

Authors
Gorbalenya, A. E., Donchenko, A. P., Koonin, E. V., & Blinov, V. M.
Venue
Nucleic Acids Research
Published
1989
Volume
17
Issue
10
Pages
3889-3897
ISSN
  • 0305-1048 (ISSN-L)
  • 1362-4962
OpenAlex
W2078798933
Cited by
255
References
27
FWCI
21.05
Type
journal article
Language
en
Open access
green

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CoChat. (2026). Citation check: N-terminal domains of putative helicases of flavi- and pestiviruses may be serine proteases. https://app.cochat.ai/papers/10.1093/nar/17.10.3889
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Gorbalenya, A. E., Donchenko, A. P., Koonin, E. V., & Blinov, V. M. (1989). N-terminal domains of putative helicases of flavi- and pestiviruses may be serine proteases. Nucleic Acids Research. https://doi.org/10.1093/nar/17.10.3889

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

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