Evidence map›Paper›PMID 26562751›Full record

ArticleACS synthetic biology2016

Development of an Unnatural Amino Acid Incorporation System in the Actinobacterial Natural Product Producer Streptomyces venezuelae ATCC 15439.

Jingxuan He, Briana Van Treeck, Han B Nguyen, Charles E Melançon

Open access · greenAbstract read
In one paragraph

Article in ACS synthetic biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
2.8field-weighted citation impact, top 10% of its field
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

12 citing papers in PubMed, 23 citations in OpenAlex.

  1. Review
  2. Review
  3. Review
  4. Article
  5. Article
  6. Genetic Code Expansion inACS synthetic biology · 2022
    Article
  7. Article
  8. Review
  9. Upgrading aminoacyl-tRNA synthetases for genetic code expansion.Current opinion in chemical biology · 2018
    Review
  10. Article
  11. Review
  12. Article
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

4 authors at 1 institution in 1 country.

Jingxuan HeDepartment of Chemistry and Chemical Biology, ‡Department of Biology, and §Center for Biomedical Engineering, University of New Mexico , Albuquerque, New Mexico 87131-0001, United States.
Briana Van TreeckDepartment of Chemistry and Chemical Biology, ‡Department of Biology, and §Center for Biomedical Engineering, University of New Mexico , Albuquerque, New Mexico 87131-0001, United States.
Han B NguyenDepartment of Chemistry and Chemical Biology, ‡Department of Biology, and §Center for Biomedical Engineering, University of New Mexico , Albuquerque, New Mexico 87131-0001, United States.
Charles E MelançonDepartment of Chemistry and Chemical Biology, ‡Department of Biology, and §Center for Biomedical Engineering, University of New Mexico , Albuquerque, New Mexico 87131-0001, United States.
University of New Mexico · US

Funding

NM-INBRE Sequencing and Bioinformatics CoreP20GM103451 · NIGMS · NEW MEXICO STATE UNIVERSITY LAS CRUCES · PI SHELLEY LUSETTI · 2012 to 2026
$61.2M
NIGMS NIH HHS P20 GM103451
6 · The paper itself

Abstract

Many Actinobacteria, most notably Streptomyces, produce structurally diverse bioactive natural products, including ribosomally synthesized peptides, by multistep enzymatic pathways. The use of site-specific genetic incorporation of unnatural amino acids to investigate and manipulate the functions of natural product biosynthetic enzymes, enzyme complexes, and ribosomally derived peptides in these organisms would have important implications for drug discovery and development efforts. Here, we have designed, constructed, and optimized unnatural amino acid systems capable of incorporating p-iodo-l-phenylalanine and p-azido-l-phenylalanine site-specifically into proteins in the model natural product producer Streptomyces venezuelae ATCC 15439. We observed notable differences in the fidelity and efficiency of these systems between S. venezuelae and previously used hosts. Our findings serve as a foundation for using an expanded genetic code in Streptomyces to address questions related to natural product biosynthesis and mechanism of action that are relevant to drug discovery and development.

Indexed as

Bacterial ProteinsPhenylalanineStreptomycesBacterial ProteinsPhenylalaninegreen fluorescent proteinnatural productsp-azido-l-phenylalaninep-iodo-l-phenylalanineStreptomycesunnatural amino acids

Identifiers

PMID26562751
PMCPMC4765998
OpenAlexW2304218012

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

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.