ArticleMethods in molecular biology (Clifton, N.J.)2023
Structural Studies of Modular Nonribosomal Peptide Synthetases.
Article in Methods in molecular biology (Clifton, N.J.), 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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.
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Who cites it
6 citing papers in PubMed, 6 citations in OpenAlex.
- Structure of a stand-alone homodimeric nonribosomal peptide synthetase condensation domain reveals occlusion of the canonical carrier-protein interface.The Journal of biological chemistry · 2026Article
- Structure of a Stand-Alone Homodimeric NRPS Condensation Domain Reveals Occlusion of the Canonical Carrier-Protein Interface.bioRxiv : the preprint server for biology · 2026Article
- Genome mining identifies a diversity of natural product biosynthetic capacity in human respiratorymSphere · 2025Article
- Expanding the Substrate Selectivity of the Fimsbactin Biosynthetic Adenylation Domain, FbsH.ACS chemical biology · 2024Article
- Expanding the substrate selectivity of the fimsbactin biosynthetic adenylation domain, FbsH.bioRxiv : the preprint server for biology · 2024Article
- Structural and functional insights into δ-poly-L-ornithine polymer biosynthesis from Acinetobacter baumannii.Communications biology · 2023Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
The non-ribosomal peptide synthetases (NRPSs) are a family of modular enzymes involved in the production of peptide natural products. Not restricted by the constraints of ribosomal peptide and protein production, the NRPSs are able to incorporate unusual amino acids and other suitable building blocks into the final product. The NRPSs operate with an assembly line strategy in which peptide intermediates are covalently tethered to a peptidyl carrier protein and transported to different catalytic domains for the multiple steps in the biosynthesis. Often the carrier and catalytic domains are joined into a single large multidomain protein. This chapter serves to introduce the NRPS enzymes, using the nocardicin NRPS system as an example that highlights many common features to NRPS biochemistry. We then describe recent advances in the structural biology of NRPSs focusing on large multidomain structures that have been determined.
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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.