Evidence map›Paper›PMID 22659295›Full record

ArticleVirus research2012

Short peptides derived from the interaction domain of SARS coronavirus nonstructural protein nsp10 can suppress the 2'-O-methyltransferase activity of nsp10/nsp16 complex.

Min Ke, Yu Chen, Andong Wu, Ying Sun, Ceyang Su, Hao Wu, Xu Jin, Jiali Tao, Yi Wang, Xiao Ma and 2 more

Open access · greenAbstract read
In one paragraph

Article in Virus research, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 papers.

0numbers the graph read from it
0cells of the map it votes in
57citing papers in PubMed
1.2field-weighted citation impact, top 21% 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

57 citing papers in PubMed, 80 citations in OpenAlex.

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  13. Host and Viral Zinc-Finger Proteins in COVID-19.International journal of molecular sciences · 2022
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  15. Structural biology of SARS-CoV-2: open the door for novel therapies.Signal transduction and targeted therapy · 2022
    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

12 authors at 1 institution in 1 country.

Min KeState Key Laboratory of Virology and Modern Virology Research Center, College of Life Sciences, Wuhan University, Wuhan 430072, People's Republic of China.
Yu Chen
Andong Wu
Ying Sun
Ceyang Su
Hao Wu
Xu Jin
Jiali Tao
Yi Wang
Xiao Ma
Ji-An Pan
Deyin Guo
Wuhan University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Coronaviruses are the etiological agents of respiratory and enteric diseases in humans and livestock, exemplified by the life-threatening severe acute respiratory syndrome (SARS) caused by SARS coronavirus (SARS-CoV). However, effective means for combating coronaviruses are still lacking. The interaction between nonstructural protein (nsp) 10 and nsp16 has been demonstrated and the crystal structure of SARS-CoV nsp16/10 complex has been revealed. As nsp10 acts as an essential trigger to activate the 2'-O-methyltransferase activity of nsp16, short peptides derived from nsp10 may have inhibitory effect on viral 2'-O-methyltransferase activity. In this study, we revealed that the domain of aa 65-107 of nsp10 was sufficient for its interaction with nsp16 and the region of aa 42-120 in nsp10, which is larger than the interaction domain, was needed for stimulating the nsp16 2'-O-methyltransferase activity. We further showed that two short peptides derived from the interaction domain of nsp10 could inhibit the 2'-O-methyltransferase activity of SARS-CoV nsp16/10 complex, thus providing a novel strategy and proof-of-principle study for developing peptide inhibitors against SARS-CoV.

Indexed as

Protein Interaction MappingEnzyme InhibitorsMethyltransferasesModels, MolecularPeptidesProtein ConformationProtein Interaction Domains and MotifsSevere acute respiratory syndrome-related coronavirusTwo-Hybrid System TechniquesViral Nonstructural ProteinsEnzyme InhibitorsMethyltransferasesNsp10 protein, SARS virusNsp16 protein, SARS virusPeptidesViral Nonstructural Proteins

Identifiers

PMID22659295
PMCPMC7114426
OpenAlexW2051534962

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.