ArticleThe Journal of biological chemistry2017
Defining the crucial domain and amino acid residues in bacterial Lon protease for DNA binding and processing of DNA-interacting substrates.
Article in The Journal of biological chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
What it found
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Who cites it
15 citing papers in PubMed, 30 citations in OpenAlex.
- Substrate-dependent activation of LONP1 informs on proteolytic regulation and ATPase motor function.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Article
- Allosteric modulation of the Lon protease by effector binding and local charges.bioRxiv : the preprint server for biology · 2024Article
- Structural and mechanistic studies on human LONP1 redefine the hand-over-hand translocation mechanism.bioRxiv : the preprint server for biology · 2024Article
- G-quadruplexes rescuing protein folding.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Structure, Substrate Specificity and Role of Lon Protease in Bacterial Pathogenesis and Survival.International journal of molecular sciences · 2023Review
- Polyphosphate induces the proteolysis of ADP-bound fraction of initiator to inhibit DNA replication initiation upon stress in Escherichia coli.Nucleic acids research · 2020Article
- Article
- Iron Limitation inFrontiers in microbiology · 2020Article
- DNA and Polyphosphate in Directed Proteolysis for DNA Replication Control.Frontiers in microbiology · 2020Review
- Asymmetric division yields progeny cells with distinct modes of regulating cell cycle-dependent chromosome methylation.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Efficient biosynthesis of heterodimeric CNature communications · 2018Article
- Multiple domains of bacterial and human Lon proteases define substrate selectivity.Emerging microbes & infections · 2018Article
- Regulated Proteolysis in Bacteria.Annual review of biochemistry · 2018Review
- ClpC and MecA, components of a proteolytic machine, prevent Spo0A-P-dependent transcription without degradation.Molecular microbiology · 2018Article
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Lon protease previously has been shown to interact with DNA, but the role of this interaction for Lon proteolytic activity has not been characterized. In this study, we used truncated
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Registered trials
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