Evidence map›Paper›PMID 25732088›Full record

ArticleBiochemical and biophysical research communications2015

VHL negatively regulates SARS coronavirus replication by modulating nsp16 ubiquitination and stability.

Xiao Yu, Shuliang Chen, Panpan Hou, Min Wang, Yu Chen, Deyin Guo

Open access · greenAbstract read
In one paragraph

Article in Biochemical and biophysical research communications, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
0.6field-weighted citation impact, top 31% 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

9 citing papers in PubMed, 18 citations in OpenAlex.

  1. Article
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  6. Review
  7. The long form of pVHL is artifactually modified by serine protease inhibitor AEBSF.Protein science : a publication of the Protein Society · 2020
    Article
  8. Review
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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

6 authors at 1 institution in 1 country.

Xiao YuCollege of Life Sciences, Wuhan University, Wuhan 430072, PR China.
Shuliang ChenSchool of Basic Medical Sciences, Wuhan University Wuhan, 430072, PR China.
Panpan HouCollege of Life Sciences, Wuhan University, Wuhan 430072, PR China.
Min WangSchool of Basic Medical Sciences, Wuhan University Wuhan, 430072, PR China.
Yu ChenCollege of Life Sciences, Wuhan University, Wuhan 430072, PR China.
Deyin GuoCollege of Life Sciences, Wuhan University, Wuhan 430072, PR China; School of Basic Medical Sciences, Wuhan University Wuhan, 430072, PR China. Electronic address: dguo@whu.edu.cn.
Wuhan University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Eukaryotic cellular and most viral RNAs carry a 5'-terminal cap structure, a 5'-5' triphosphate linkage between the 5' end of the RNA and a guanosine nucleotide (cap-0). SARS coronavirus (SARS-CoV) nonstructural protein nsp16 functions as a methyltransferase, to methylate mRNA cap-0 structure at the ribose 2'-O position of the first nucleotide to form cap-1 structures. However, whether there is interplay between nsp16 and host proteins was not yet clear. In this report, we identified several potential cellular nsp16-interacting proteins from a human thymus cDNA library by yeast two-hybrid screening. VHL, one of these proteins, was proven to interact with nsp16 both in vitro and in vivo. Further studies showed that VHL can inhibit SARS-CoV replication by regulating nsp16 ubiquitination and promoting its degradation. Our results have revealed the role of cellular VHL in the regulation of SARS-CoV replication.

Indexed as

AnimalsChlorocebus aethiopsExoribonucleasesHost-Pathogen InteractionsHumansMethyltransferasesProtein StabilityProteolysisRecombinant Fusion ProteinsSevere acute respiratory syndrome-related coronavirusTwo-Hybrid System TechniquesUbiquitinationVero CellsViral Nonstructural ProteinsVirus ReplicationVon Hippel-Lindau Tumor Suppressor ProteinExoribonucleasesMethyltransferasesnsp14 protein, SARS coronavirusNsp16 protein, SARS virusRecombinant Fusion ProteinsVHL protein, humanViral Nonstructural ProteinsVon Hippel-Lindau Tumor Suppressor Proteinnsp16ReplicationSARS-CoVUbiquitinationVHL

Identifiers

PMID25732088
PMCPMC7092858
OpenAlexW2028216660

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.