Evidence map›Paper›PMID 27188239›Full record

ArticleScientific reports2016

An intein-mediated modulation of protein stability system and its application to study human cytomegalovirus essential gene function.

Deng Pan, Baoqin Xuan, Yamei Sun, Shaowu Huang, Maorong Xie, Yadan Bai, Wenjia Xu, Zhikang Qian

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
0.7field-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

6 citing papers in PubMed, 17 citations in OpenAlex.

  1. Int&in: A machine learning-based web server for active split site identification in inteins.Protein science : a publication of the Protein Society · 2024
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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

8 authors at 3 institutions in 1 country.

Deng PanUnit of Herpesvirus and Molecular Virology, Key Laboratory of Molecular Virology &Immunology, Institut Pasteur of Shanghai, Chinese Academy of Sciences, University of the Chinese Academy of Sciences, Shanghai, China.
Baoqin XuanUnit of Herpesvirus and Molecular Virology, Key Laboratory of Molecular Virology &Immunology, Institut Pasteur of Shanghai, Chinese Academy of Sciences, University of the Chinese Academy of Sciences, Shanghai, China.
Yamei SunUnit of Herpesvirus and Molecular Virology, Key Laboratory of Molecular Virology &Immunology, Institut Pasteur of Shanghai, Chinese Academy of Sciences, University of the Chinese Academy of Sciences, Shanghai, China.
Shaowu HuangUnit of Herpesvirus and Molecular Virology, Key Laboratory of Molecular Virology &Immunology, Institut Pasteur of Shanghai, Chinese Academy of Sciences, University of the Chinese Academy of Sciences, Shanghai, China.
Maorong XieUnit of Herpesvirus and Molecular Virology, Key Laboratory of Molecular Virology &Immunology, Institut Pasteur of Shanghai, Chinese Academy of Sciences, University of the Chinese Academy of Sciences, Shanghai, China.
Yadan BaiUnit of Herpesvirus and Molecular Virology, Key Laboratory of Molecular Virology &Immunology, Institut Pasteur of Shanghai, Chinese Academy of Sciences, University of the Chinese Academy of Sciences, Shanghai, China.
Wenjia XuUnit of Herpesvirus and Molecular Virology, Key Laboratory of Molecular Virology &Immunology, Institut Pasteur of Shanghai, Chinese Academy of Sciences, University of the Chinese Academy of Sciences, Shanghai, China.
Zhikang QianUnit of Herpesvirus and Molecular Virology, Key Laboratory of Molecular Virology &Immunology, Institut Pasteur of Shanghai, Chinese Academy of Sciences, University of the Chinese Academy of Sciences, Shanghai, China.
Institut Pasteur of Shanghai · CNChinese Academy of Sciences · CNSoochow University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Functional analysis of the essential proteins encoded by human cytomegalovirus (HCMV) is hindered by the lack of complementing systems. To overcome this difficulty, we have established a novel approach, termed the intein-mediated modulation of protein stability (imPS), in which a destabilizing domain and part of a split intein are fused to the essential protein. The growth of the mutant virus can then be regulated by the degradation and splicing of the protein. We found that an ultrafast gp41-1 split intein was able to rescue or degrade the protein of interest (POI) by removing or adding a strong degron through protein splicing. As a result, the function of the POI was turned on or off during the process. Using HCMV essential gene IE1/IE2, we confirmed that imPS worked remarkably well in conditionally regulating protein stability during viral infection. This conditional approach is likely to be applicable for dissecting the gene functions of HCMV or other viruses.

Indexed as

Genes, EssentialGenes, ViralCytomegalovirusHEK293 CellsHumansInteinsMicrobial ViabilityMolecular BiologyProtein StabilityVirology

Identifiers

PMID27188239
PMCPMC4870628
OpenAlexW2401016120

What Socratic 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 Socratic graph.