ReviewACS bio & med chem Au2024
Proteases Involved in Leader Peptide Removal during RiPP Biosynthesis.
Review in ACS bio & med chem Au, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers, 1 of them a synthesis that pooled it.
What it found
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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.
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
26 citing papers in PubMed, 1 synthesis or guideline pooled it, 29 citations in OpenAlex.
- Advancements in the Application of Ribosomally Synthesized and Post-Translationally Modified Peptides (RiPPs).Biomolecules · 2024Pooled it
- Structure and Activity of Class II Lanthipeptides From a Thermophilic Bacterium.Chembiochem : a European journal of chemical biology · 2026Article
- TMcin RiPP biosynthesis in the cellular membrane.bioRxiv : the preprint server for biology · 2026Article
- Structure and Activity of Class II Lanthipeptides from a Thermophilic Bacterium.bioRxiv : the preprint server for biology · 2026Article
- RiPP recognition elements evolved to prevent pathway interference through leader peptide discrimination.Nature communications · 2026Article
- A Bifunctional Protease Cleaves the Leader Peptide in the Biosynthesis of Class I Microviridins.Chembiochem : a European journal of chemical biology · 2026Article
- An Unusual Ring Pattern in the Rosβ Lanthipeptide of the Two-Component Lantibiotic Roseocin.Journal of natural products · 2026Article
- Myxarylin: TotalJournal of the American Chemical Society · 2026Article
- Leaderless RiPPs expand the repertoire of fungal secondary metabolites.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- S9 protease WprPCommunications chemistry · 2026Article
- Oxidative Peptide Backbone Cleavage by a HEXXH Enzyme during RiPP Biosynthesis.Journal of the American Chemical Society · 2026Article
- Tandem solubility enhancing tags enable the heterologous expression andFrontiers in microbiology · 2026Article
- Oxidative Peptide Backbone Cleavage by a HEXXH Enzyme During RiPP Biosynthesis.bioRxiv : the preprint server for biology · 2025Article
- Article
- An antimicrobial daptide from human skin commensal Staphylococcus hominis protects against skin pathogens.Nature communications · 2025Article
- Promiscuity of lanthipeptide enzymes: new challenges and applications.World journal of microbiology & biotechnology · 2025Review
- Combatting virulent gut bacteria by inhibiting the biosynthesis of a two-component lanthipeptide toxin.Nature communications · 2025Article
- Characterization of a novel glycocin from a thermophile.bioRxiv : the preprint server for biology · 2025Article
- Enabling Access to Novel Bacterial Biosynthetic Potential From ONT Draft Genomic Data.Microbial biotechnology · 2025Article
- Characterization of S-glycosylated glycocins containing three disulfides.Journal of industrial microbiology & biotechnology · 2024Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 2 institutions in 1 country.
Funding
Abstract
Ribosomally synthesized and post-translationally modified peptides (RiPPs) have received much attention in recent years because of their promising bioactivities and the portability of their biosynthetic pathways. Heterologous expression studies of RiPP biosynthetic enzymes identified by genome mining often leave a leader peptide on the final product to prevent toxicity to the host and to allow the attachment of a genetically encoded affinity purification tag. Removal of the leader peptide to produce the mature natural product is then carried out in vitro with either a commercial protease or a protease that fulfills this task in the producing organism. This review covers the advances in characterizing these latter cognate proteases from bacterial RiPPs and their utility as sequence-dependent proteases. The strategies employed for leader peptide removal have been shown to be remarkably diverse. They include one-step removal by a single protease, two-step removal by two dedicated proteases, and endoproteinase activity followed by aminopeptidase activity by the same protease. Similarly, the localization of the proteolytic step varies from cytoplasmic cleavage to leader peptide removal during secretion to extracellular leader peptide removal. Finally, substrate recognition ranges from highly sequence specific with respect to the leader and/or modified core peptide to nonsequence specific mechanisms.
Identifiers
What OpenQuestion holds
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.