Evidence map›Paper›PMID 16546436›Full record

ArticleThe international journal of biochemistry & cell biology2006

Retracted: Nucleocapsid protein of SARS-CoV activates the expression of cyclooxygenase-2 by binding directly to regulatory elements for nuclear factor-kappa B and CCAAT/enhancer binding protein.

Xiaohong Yan, Qian Hao, Yongxin Mu, Khalid Amine Timani, Linbai Ye, Ying Zhu, Jianguo Wu

RetractedOpen access · greenAbstract readRetracted Publication
In one paragraph

Article in The international journal of biochemistry & cell biology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. It has been retracted, and should not be counted. Cited by 85 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
85citing papers in PubMed, 1 pooled it
2.6field-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

85 citing papers in PubMed, 1 synthesis or guideline pooled it, 141 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Review
  4. Article
  5. Review
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Toll-like Receptor Mediation in SARS-CoV-2: A Therapeutic Approach.International journal of molecular sciences · 2022
    Review
  12. Article
  13. Article
  14. Article
  15. Review
  16. Review
  17. Article
  18. Models for COVID-19 Early Cardiac Pathology Following SARS-CoV-2 Infection.International journal of infectious diseases : IJID : official publication of the International Society for Infectious Diseases · 2021
    Article
  19. Article
  20. Hyperactivated Mast Cells Pathogenesis Hypothesis for COVID-19 Cutaneous Manifestations.JID innovations : skin science from molecules to population health · 2021
    Article

25 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

7 authors at 1 institution in 1 country.

Xiaohong YanThe State Key Laboratory of Virology, College of Life Sciences, Wuhan University, Wuhan 430072, PR China.
Qian Hao
Yongxin Mu
Khalid Amine Timani
Linbai Ye
Ying Zhu
Jianguo Wu
Wuhan University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

SARS-associated coronavirus (SARS-CoV) causes inflammation and damage to the lungs resulting in severe acute respiratory syndrome. To evaluate the molecular mechanisms behind this event, we investigated the roles of SARS-CoV proteins in regulation of the proinflammatory factor, cyclooxygenase-2 (COX-2). Individual viral proteins were tested for their abilities to regulate COX-2 gene expression. Results showed that the COX-2 promoter was activated by the nucleocapsid (N) protein in a concentration-dependent manner. Western blot analysis indicated that N protein was sufficient to stimulate the production of COX-2 protein in mammalian cells. COX-2 promoter mutations suggested that activation of COX-2 transcription depended on two regulatory elements, a nuclear factor-kappa B (NF-kappaB) binding site, and a CCAAT/enhancer binding protein (C/EBP) binding site. Electrophoretic mobility shift assay (EMSA) and chromatin immunoprecipitation (ChIP) demonstrated that SARS-CoV N protein bound directly to these regulatory sequences. Protein mutation analysis revealed that a Lys-rich motif of N protein acted as a nuclear localization signal and was essential for the activation of COX-2. In addition, a Leu-rich motif was found to be required for the N protein function. A sequence of 68 residuals was identified as a potential DNA-binding domain essential for activating COX-2 expression. We propose that SARS-CoV N protein causes inflammation of the lungs by activating COX-2 gene expression by binding directly to the promoter resulting in inflammation through multiple COX-2 signaling cascades.

Indexed as

Amino Acid SequenceBinding SitesCCAAT-Enhancer-Binding Protein-betaCell LineChromatin ImmunoprecipitationCyclooxygenase 2Electrophoretic Mobility Shift AssayGene Expression Regulation, EnzymologicHumansMutagenesis, Site-DirectedMutationNF-kappa BNucleocapsid ProteinsPlasmidsPromoter Regions, GeneticProtein BindingCCAAT-Enhancer-Binding Protein-betaCyclooxygenase 2NF-kappa BNucleocapsid Proteins

Identifiers

PMID16546436
PMCPMC7108415
OpenAlexW2083240355

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.