ArticleThe Journal of biological chemistry2012
Activity, specificity, and probe design for the smallpox virus protease K7L.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
What it found
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The trial behind it
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, 20 citations in OpenAlex.
- Dynamic Cap-Mediated Substrate Access and Potent Inhibitor Design of Monkeypox Virus I7L Protease.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Article
- Yeast-Based Screening of Anti-Viral Molecules.Microorganisms · 2024Review
- Targeting the I7L Protease: A Rational Design for Anti-Monkeypox Drugs?International journal of molecular sciences · 2023Article
- Viral proteases as therapeutic targets.Molecular aspects of medicine · 2022Review
- Precursors of Viral Proteases as Distinct Drug Targets.Viruses · 2021Review
- SARS-CoV-2 MNature chemical biology · 2021Article
- Activity profiling and crystal structures of inhibitor-bound SARS-CoV-2 papain-like protease: A framework for anti-COVID-19 drug design.Science advances · 2020Article
- Capsid protein structure, self-assembly, and processing reveal morphogenesis of the marine virophage mavirus.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Article
- Variola virus F1L is a Bcl-2-like protein that unlike its vaccinia virus counterpart inhibits apoptosis independent of Bim.Cell death & disease · 2015Article
- Presentation overrides specificity: probing the plasticity of alphaviral proteolytic activity through mutational analysis.Journal of virology · 2013Article
Corrections and comments
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Authors and funding
9 authors at 1 institution in 1 country.
Funding
Abstract
The K7L gene product of the smallpox virus is a protease implicated in the maturation of viral proteins. K7L belongs to protease Clan CE, which includes distantly related cysteine proteases from eukaryotes, pathogenic bacteria, and viruses. Here, we describe its recombinant high level expression, biochemical mechanism, substrate preference, and regulation. Earlier studies inferred that the orthologous I7L vaccinia protease cleaves at an AG-X motif in six viral proteins. Our data for K7L suggest that the AG-X motif is necessary but not sufficient for optimal cleavage activity. Thus, K7L requires peptides extended into the P7 and P8 positions for efficient substrate cleavage. Catalytic activity of K7L is substantially enhanced by homodimerization, by the substrate protein P25K as well as by glycerol. RNA and DNA also enhance cleavage of the P25K protein but not of synthetic peptides, suggesting that nucleic acids augment the interaction of K7L with its protein substrate. Library-based peptide preference analyses enabled us to design an activity-based probe that covalently and selectively labels K7L in lysates of transfected and infected cells. Our study thus provides proof-of-concept for the design of inhibitors and probes that may contribute both to a better understanding of the role of K7L in the virus life cycle and the design of novel anti-virals.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.