ArticleJournal of chemical sciences (Bangalore, India)2015
Modeling the structure of SARS 3a transmembrane protein using a minimum unfavorable contact approach.
Article in Journal of chemical sciences (Bangalore, India), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
2 citing papers in PubMed, 7 citations in OpenAlex.
- SARS-CoV-2 ORF3a drives dynamic dense body formation for optimal viral infectivity.Nature communications · 2025Article
- Urea-aromatic interactions in biology.Biophysical reviews · 2020Review
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
3a is an accessory protein from SARS coronavirus that is known to play a significant role in the proliferation of the virus by forming tetrameric ion channels. Although the monomeric units are known to consist of three transmembrane (TM) domains, there are no solved structures available for the complete monomer. The present study proposes a structural model for the transmembrane region of the monomer by employing our previously tested approach, which predicts potential orientations of TM ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (doi:10.1007/s12039-015-0982-z) contains supplementary material, which is available to authorized users.
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