Evidence map›Paper›PMID 31067766›Full record

ArticleInternational journal of molecular sciences2019

C1 Compound Biosensors: Design, Functional Study, and Applications.

Jin-Young Lee, Bong Hyun Sung, So-Hyung Oh, Kil Koang Kwon, Hyewon Lee, Haseong Kim, Dae-Hee Lee, Soo-Jin Yeom, Seung-Goo Lee

Open access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 2019. 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
0.9field-weighted citation impact, top 26% 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, 21 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Review
  10. Biosensor-Based Directed Evolution of Methanol Dehydrogenase fromInternational journal of molecular sciences · 2021
    Article
  11. Article
  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

9 authors at 1 institution in 1 country.

Jin-Young LeeSynthetic Biology & Bioengineering Research Center, KRIBB, Daejeon 34141, Korea. jylee84@kribb.re.kr.
Bong Hyun SungSynthetic Biology & Bioengineering Research Center, KRIBB, Daejeon 34141, Korea. bhsung@kribb.re.kr.
So-Hyung OhSynthetic Biology & Bioengineering Research Center, KRIBB, Daejeon 34141, Korea. sohyungoh@kribb.re.kr.
Kil Koang KwonSynthetic Biology & Bioengineering Research Center, KRIBB, Daejeon 34141, Korea. kkkwon@kribb.re.kr.
Hyewon LeeSynthetic Biology & Bioengineering Research Center, KRIBB, Daejeon 34141, Korea. hlee@kribb.re.kr.
Haseong KimSynthetic Biology & Bioengineering Research Center, KRIBB, Daejeon 34141, Korea. haseong@kribb.re.kr.
Dae-Hee LeeSynthetic Biology & Bioengineering Research Center, KRIBB, Daejeon 34141, Korea. dhlee@kribb.re.kr.ORCID 0000-0002-0423-9057
Soo-Jin YeomSynthetic Biology & Bioengineering Research Center, KRIBB, Daejeon 34141, Korea. sujin258@kribb.re.kr.ORCID 0000-0001-7307-237X
Seung-Goo LeeSynthetic Biology & Bioengineering Research Center, KRIBB, Daejeon 34141, Korea. sglee@kribb.re.kr.
Intelligent Synthetic Biology Center · KR

Funding

Korea Research Institute of Bioscience and Biotechnology Research Initiative Program KGM5401911National Research Foundation of Korea 2018M3D3A1A01055732National Research Foundation of Korea 2018M3D3A1A01056181National Research Foundation of Korea 2018R1C1B6004086
6 · The paper itself

Abstract

The microbial assimilation of one-carbon (C1) gases is a topic of interest, given that products developed using this pathway have the potential to act as promising substrates for the synthesis of valuable chemicals via enzymatic oxidation or C-C bonding. Despite extensive studies on C1 gas assimilation pathways, their key enzymes have yet to be subjected to high-throughput evolution studies on account of the lack of an efficient analytical tool for C1 metabolites. To address this challenging issue, we attempted to establish a fine-tuned single-cell-level biosensor system constituting a combination of transcription factors (TFs) and several C1-converting enzymes that convert target compounds to the ligand of a TF. This enzymatic conversion broadens the detection range of ligands by the genetic biosensor systems. In this study, we presented new genetic enzyme screening systems (GESSs) to detect formate, formaldehyde, and methanol from specific enzyme activities and pathways, named FA-GESS, Frm-GESS, and MeOH-GESS, respectively. All the biosensors displayed linear responses to their respective C1 molecules, namely, formate (1.0-250 mM), formaldehyde (1.0-50 μM), and methanol (5-400 mM), and they did so with high specificity. Consequently, the helper enzymes, including formaldehyde dehydrogenase and methanol dehydrogenase, were successfully combined to constitute new versatile combinations of the C1-biosensors.

Indexed as

Alcohol OxidoreductasesAldehyde OxidoreductasesBacterial ProteinsBiosensing TechniquesEscherichia coliFormaldehydeFormatesGenes, ReporterGreen Fluorescent ProteinsMethanolTranscription Factorsalcohol dehydrogenase (acceptor)Alcohol OxidoreductasesAldehyde OxidoreductasesBacterial ProteinsFormaldehydeformaldehyde dehydrogenase, glutathione-independentFormatesGreen Fluorescent ProteinsMethanolTranscription FactorsC1 compound biosensorgenetic enzyme screening systemone-carbon compound

Identifiers

PMID31067766
PMCPMC6540204
OpenAlexW2944261393

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.