ReviewBeilstein journal of organic chemistry2016
Cyclisation mechanisms in the biosynthesis of ribosomally synthesised and post-translationally modified peptides.
Review in Beilstein journal of organic chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed.
- Exploring RiPP-derivedRSC chemical biology · 2026Article
- Discovery and development of penicillin-binding protein-type thioesterases as biocatalysts.Current opinion in biotechnology · 2026Review
- Peptide and Protein Cyclization by a Promiscuous Graspetide Synthetase.ACS central science · 2025Article
- Whole genome analysis and biocontrol potential of endophytic Bacillus cereus EMS1 against Fusarium wilt in banana.World journal of microbiology & biotechnology · 2025Article
- Article
- Article
- Insights into the structure and function of the histidine kinase ComP from Bacillus amyloliquefaciens based on molecular modeling.Bioscience reports · 2022Article
- Article
- Complex peptide natural products: Biosynthetic principles, challenges and opportunities for pathway engineering.Synthetic and systems biotechnology · 2022Article
- Discovery and characterisation of an amidine-containing ribosomally-synthesised peptide that is widely distributed in nature.Chemical science · 2021Article
- Review
- Recent Advances and Perspectives on Expanding the Chemical Diversity of Lasso Peptides.Frontiers in bioengineering and biotechnology · 2021Review
- Recent advances in the biosynthesis of RiPPs from multicore-containing precursor peptides.Journal of industrial microbiology & biotechnology · 2020Review
- Architecture of Microcin B17 Synthetase: An Octameric Protein Complex Converting a Ribosomally Synthesized Peptide into a DNA Gyrase Poison.Molecular cell · 2019Article
- Article
- Ribosomal Natural Products, Tailored To Fit.Accounts of chemical research · 2017Article
- Ribosomally synthesized and post-translationally modified peptide natural product discovery in the genomic era.Current opinion in chemical biology · 2017Review
- Elucidating and engineering thiopeptide biosynthesis.World journal of microbiology & biotechnology · 2017Review
Corrections and comments
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Authors and funding
1 author.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Ribosomally synthesised and post-translationally modified peptides (RiPPs) are a large class of natural products that are remarkably chemically diverse given an intrinsic requirement to be assembled from proteinogenic amino acids. The vast chemical space occupied by RiPPs means that they possess a wide variety of biological activities, and the class includes antibiotics, co-factors, signalling molecules, anticancer and anti-HIV compounds, and toxins. A considerable amount of RiPP chemical diversity is generated from cyclisation reactions, and the current mechanistic understanding of these reactions will be discussed here. These cyclisations involve a diverse array of chemical reactions, including 1,4-nucleophilic additions, [4 + 2] cycloadditions, ATP-dependent heterocyclisation to form thiazolines or oxazolines, and radical-mediated reactions between unactivated carbons. Future prospects for RiPP pathway discovery and characterisation will also be highlighted.
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