Covering: up to June 2020 Ribosomally-synthesized and post-translationally modified
peptides (RiPPs) are a large group of natural products. A community-driven review in 2013 …

Our ever‐increasing understanding of biological systems is providing a range of exciting
novel biological targets, whose modulation may enable novel therapeutic options for many …

Covering: 2014. Previous review: Nat. Prod. Rep., 2015, 32, 116–211 This review covers the
literature published in 2014 for marine natural products (MNPs), with 1116 citations (753 for …

Ribosomally synthesized and post-translationally modified peptides (RiPPs) are a large
group of structurally diverse natural products. Their biological activities and unique …

With advances in sequencing technology, uncharacterized proteins and domains of
unknown function (DUFs) are rapidly accumulating in sequence databases and offer an …

In this article we describe the production and screening of a genetically encoded library of
106 lanthipeptides in Escherichia coli using the substrate-tolerant lanthipeptide synthetase …

Thiopeptides are potent antibiotics that inhibit protein synthesis. They are made by a
remarkable post-translational modification process that transforms a linear peptide into a …

This review covers the literature published in 2015 for marine natural products (MNPs), with
1220 citations (792 for the period January to December 2015) referring to compounds …

Regioselective modification of amino acids within the context of a peptide is common to a
number of biosynthetic pathways, and many of the resulting products have potential as …

mRNA display is revolutionizing peptide drug discovery through its ability to quickly identify
potent peptide binders of therapeutic protein targets. Methods to expand the chemical …