ArticleMethods in molecular biology (Clifton, N.J.)2025
Guidelines for High-Throughput Engineering of Nonribosomal Peptide Synthetase Libraries.
Article in Methods in molecular biology (Clifton, N.J.), 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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
0 citing papers in PubMed.
No citing paper in PubMed yet.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Nonribosomal peptide synthetases (NRPS) are highly versatile enzymatic machineries responsible for the synthesis of complex peptides. These enzymes' characteristic modular architecture and synthesis pathway have prompted considerable research into their manipulation to generate new-to-nature peptides. Recent advances in the engineering of NRPS offer new avenues for application as a sustainable approach for the production of defined complex peptides, providing a viable alternative to the conventional chemical synthesis methods currently employed. In this protocol, we provide detailed guidelines for the modular assembly of different NRPS by using the eXchange Unit Thiolation domain (XUT) concept to generate hybrid NRPS. The engineering concept was adapted to modern Golden Gate assembly cloning that provides a flexible and sustainable way to assemble NRPS in high-throughput that produces predictable peptides.
Indexed as
Identifiers
40663333What 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.