Evidence map›Paper›PMID 41451912›Full record

ArticleACS synthetic biology2026

Artificial Multidomain Ribosomally Synthesized and Post-translationally Modified Peptide Enzymes for Farnesylated Peptide Library Generation.

Noel Lacerna, Eric W Schmidt

Abstract read
In one paragraph

Article in ACS synthetic biology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

0 citing papers in PubMed.

No citing paper in PubMed yet.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

2 authors.

Noel LacernaDepartment of Medicinal Chemistry, College of Pharmacy, University of Utah, Salt Lake City, Utah 84112, United States.
Eric W SchmidtDepartment of Medicinal Chemistry, College of Pharmacy, University of Utah, Salt Lake City, Utah 84112, United States.ORCID 0000-0001-5839-694X

Funding

Symbiosis and Chemical Diversity GenerationR35GM148283 · NIGMS · UTAH STATE HIGHER EDUCATION SYSTEM--UNIVERSITY OF UTAH · PI Eric W Schmidt · 2023 to 2026
$2.2M
NIGMS NIH HHS R35 GM148283
6 · The paper itself

Abstract

Cyanobactin biosynthetic pathways are used in synthetic biology approaches to create large, peptide-based chemical libraries with drug-like features such as N-C macrocyclization and prenylation. It remains challenging to express enzymes from multiple RiPP pathways to rationally produce the desired products. Here, we designed a simple yet robust method aimed to produce and assess multiple enzymes, fusing biosynthetic genes together in a well-expressed, soluble construct that enables production of macrocyclic peptides and selectively appends C

Indexed as

Peptide LibraryPeptidesRibosomesBacterial ProteinsBiosynthetic PathwaysPeptides, CyclicProtein Processing, Post-TranslationalSynthetic BiologyBacterial ProteinscyanobactinsPeptide LibraryPeptidesPeptides, Cycliccyanobactinscyclic peptide libraryfusion proteinspeptide farnesylationprotein engineeringRiPPs

Identifiers

PMID41451912
PMCPMC12814516

What OpenQuestion holds

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Registered trials

None linked

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.