Evidence map›Paper›PMID 24898546›Full record

ArticleJournal of biomedical science2014

Structural and functional characterization of MERS coronavirus papain-like protease.

Min-Han Lin, Shang-Ju Chuang, Chiao-Che Chen, Shu-Chun Cheng, Kai-Wen Cheng, Chao-Hsiung Lin, Chiao-Yin Sun, Chi-Yuan Chou

Open access · diamondAbstract read
In one paragraph

Article in Journal of biomedical science, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
2.9field-weighted citation impact, top 9% 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

30 citing papers in PubMed, 40 citations in OpenAlex.

  1. Utilizing sinapic acid as an inhibitory antiviral agent against MERS-CoV PLpro.Saudi pharmaceutical journal : SPJ : the official publication of the Saudi Pharmaceutical Society · 2024
    Article
  2. Review
  3. Research Advances on Swine Acute Diarrhea Syndrome Coronavirus.Animals : an open access journal from MDPI · 2024
    Review
  4. Interaction between coronaviruses and the autophagic response.Frontiers in cellular and infection microbiology · 2024
    Review
  5. Screening and identification of potential MERS-CoV papain-like protease (PLpro) inhibitors; Steady-state kinetic and Molecular dynamic studies.Saudi pharmaceutical journal : SPJ : the official publication of the Saudi Pharmaceutical Society · 2023
    Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. COVID-19: fighting the invisible enemy with microRNAs.Expert review of anti-infective therapy · 2021
    Review
  11. Review
  12. Article
  13. Computed optical spectra of SARS-CoV-2 proteins.Chemical physics letters · 2020
    Article
  14. Structural and biochemical characterization of SADS-CoV papain-like protease 2.Protein science : a publication of the Protein Society · 2020
    Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. Article
  20. Review
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 2 institutions in 1 country.

Min-Han Lin
Shang-Ju Chuang
Chiao-Che Chen
Shu-Chun Cheng
Kai-Wen Cheng
Chao-Hsiung Lin
Chiao-Yin SunDepartment of Life Sciences and Institute of Genome Sciences, National Yang-Ming University, Taipei 112, Taiwan. fish3970@gmail.com.
Chi-Yuan Chou
National Yang Ming Chiao Tung University · TWKeelung Chang Gung Memorial Hospital · TW

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundsA new highly pathogenic human coronavirus (CoV), Middle East respiratory syndrome coronavirus (MERS-CoV), has emerged in Jeddah and Saudi Arabia and quickly spread to some European countries since September 2012. Until 15 May 2014, it has infected at least 572 people with a fatality rate of about 30% globally. Studies to understand the virus and to develop antiviral drugs or therapy are necessary and urgent. In the present study, MERS-CoV papain-like protease (PLpro) is expressed, and its structural and functional consequences are elucidated.

resultsCircular dichroism and Tyr/Trp fluorescence analyses indicated that the secondary and tertiary structure of MERS-CoV PLpro is well organized and folded. Analytical ultracentrifugation analyses demonstrated that MERS-CoV PLpro is a monomer in solution. The steady-state kinetic and deubiquitination activity assays indicated that MERS-CoV PLpro exhibits potent deubiquitination activity but lower proteolytic activity, compared with SARS-CoV PLpro. A natural mutation, Leu105, is the major reason for this difference.

conclusionsOverall, MERS-CoV PLpro bound by an endogenous metal ion shows a folded structure and potent proteolytic and deubiquitination activity. These findings provide important insights into the structural and functional properties of coronaviral PLpro family, which is applicable to develop strategies inhibiting PLpro against highly pathogenic coronaviruses.

Indexed as

Antiviral AgentsCoronavirus 3C ProteasesCysteine EndopeptidasesEuropeGene Expression Regulation, ViralHumansIonsMetalsProtein Processing, Post-TranslationalProteolysisSevere acute respiratory syndrome-related coronavirusViral ProteinsAntiviral AgentsCoronavirus 3C ProteasesCysteine EndopeptidasesIonsMetalsViral Proteins

Identifiers

PMID24898546
PMCPMC4051379
OpenAlexW2103991539

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.