Evidence map›Paper›PMID 38380775›Full record

ArticleProtein science : a publication of the Protein Society2024

An intein-based biosensor to measure protein stability in vivo.

Ahyun Son, John S Smetana, Scott Horowitz, Christopher W Lennon

Open access · greenAbstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.5field-weighted citation impact, top 38% 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

4 citing papers in PubMed, 2 citations in OpenAlex.

  1. Article
  2. Article
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  4. An intein-based biosensor to measure protein stability in vivo.Protein science : a publication of the Protein Society · 2024
    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 2 institutions in 1 country.

Ahyun SonDepartment of Chemistry & Biochemistry, Knoebel Institute for Healthy Aging, University of Denver, Denver, Colorado, USA.ORCID 0000-0002-7979-0409
John S SmetanaDepartment of Biological Sciences, Murray State University, Murray, Kentucky, USA.
Scott HorowitzDepartment of Chemistry & Biochemistry, Knoebel Institute for Healthy Aging, University of Denver, Denver, Colorado, USA.ORCID 0000-0002-1148-0105
Christopher W LennonDepartment of Biological Sciences, Murray State University, Murray, Kentucky, USA.ORCID 0000-0001-9413-180X
Murray State University · USUniversity of Denver · US

Funding

WKU Lead Faculty AwardP20GM103436 · NIGMS · UNIVERSITY OF LOUISVILLE · PI ERIC C ROUCHKA · 2012 to 2026
$60.1M
Nucleic Acids Roles in Protein Folding and AggregationR35GM142442 · NIGMS · UNIVERSITY OF DENVER (COLORADO SEMINARY) · PI Scott Andrew Horowitz · 2021 to 2026
$2.4M
Inteins: Expanding Biological Roles and Biotechnological ApplicationsR15GM143662 · NIGMS · MURRAY STATE UNIVERSITY · PI LENNON, CHRISTOPHER WILLIAM · 2021 to 2025
$811k
NIGMS NIH HHS P20 GM103436NIGMS NIH HHS R15 GM143662NIGMS NIH HHS R35 GM142442NIH HHS P20GM103436NIH HHS R15GM143662NIH HHS R35GM142442
6 · The paper itself

Abstract

Biosensors to measure protein stability in vivo are valuable tools for a variety of applications. Previous work has demonstrated that a tripartite design, whereby a protein of interest (POI) is inserted within a reporter, can link POI stability to reporter activity. Inteins are translated within other proteins and excised in a self-mediated protein splicing reaction. Here, we developed a novel folding biosensor where a POI is inserted within an intein, which is subsequently translated within an antibiotic resistance marker. We showed that protein splicing is required for antibiotic resistance and that housing a stable POI within the intein, compared to an unstable variant, results in a 100,000-fold difference in survival. Further, using a fluorescent protein that matures slowly as the POI, we developed a reporter with two simultaneous readouts for protein folding. Finally, we showed that co-expression of GroEL can significantly increase the activity of both reporters, further verifying that protein folding factors can act on the POI in the biosensor. As a whole, our work provides a new twist on the traditional tripartite approach to measuring protein stability in vivo.

Indexed as

InteinsProtein SplicingProteinsProteinsbiosensorchaperoneinteinprotein foldingprotein splicing

Identifiers

PMID38380775
PMCPMC10880411
OpenAlexW4392004037

What OpenQuestion holds

Textmetadata
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.