ArticleVirology1999
Further requirements for cleavage by the murine coronavirus 3C-like proteinase: identification of a cleavage site within ORF1b.
Article in Virology, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 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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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
12 citing papers in PubMed.
- Molecular mechanisms of human coronavirus NL63 infection and replication.Virus research · 2023Review
- Proteolytic Processing of the Coronavirus Replicase Nonstructural Protein 14 Exonuclease Is Not Required for Virus Replication but Alters RNA Synthesis and Viral Fitness.Journal of virology · 2022Article
- Precision therapeutic targets for COVID-19.Virology journal · 2021Review
- The structure and functions of coronavirus genomic 3' and 5' ends.Virus research · 2015Review
- Murine coronaviruses encoding nsp2 at different genomic loci have altered replication, protein expression, and localization.Journal of virology · 2008Article
- Suppression of coronavirus replication by inhibition of the MEK signaling pathway.Journal of virology · 2007Article
- Human coronavirus NL63, a new respiratory virus.FEMS microbiology reviews · 2006Review
- Viral and cellular proteins involved in coronavirus replication.Current topics in microbiology and immunology · 2005Review
- The coronavirus replicase.Current topics in microbiology and immunology · 2005Review
- Identification of the murine coronavirus MP1 cleavage site recognized by papain-like proteinase 2.Journal of virology · 2003Article
- RNA replication of mouse hepatitis virus takes place at double-membrane vesicles.Journal of virology · 2002Article
- Further characterization of the coronavirus infectious bronchitis virus 3C-like proteinase and determination of a new cleavage site.Virology · 2000Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors.
Funding
Abstract
The coronavirus mouse hepatitis virus strain A59 (MHV-A59) encodes a 3C-like proteinase (3CLpro) that is proposed to be responsible for the majority of the processing events that take place within the replicase polyproteins pp1a and pp1ab. In this study we demonstrate that the Q939/S940 peptide bond, located between the polymerase and Zn-finger regions of pp1ab (the POL/Zn site), is processed by the 3CLpro, albeit inefficiently. Mutagenesis of the POL/Zn site, as well as the previously identified HD1/3C site in the 1a region of pp1a and pp1ab, demonstrated that the amino acid residues at the P2 and P1 positions of the cleavage site, occupied by L and Q, respectively, were important determinants of 3CLpro substrate specificity. Finally, a direct comparison of the 3CLpro-mediated cleavages at the HD1/3C and POL/Zn sites was made by determining the rate constants using synthetic peptides. The results show that while a larger polypeptide substrate carrying the HD1/3C site was processed more efficiently than a polypeptide substrate carrying the POL/Zn site, cleavage of the synthetic peptide substrates containing these two cleavage sites occurred at similar efficiencies. This indicates that the overall conformation of a large polyprotein substrate is important in the accessibility of the cleavage site to the proteinase.
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