Evidence map›Paper›PMID 21533772›Full record

ReviewProtein & cell2011

Activation and maturation of SARS-CoV main protease.

Bin Xia, Xue Kang

Open access · bronzeAbstract readReview
In one paragraph

Review in Protein & cell, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 81 papers.

0numbers the graph read from it
0cells of the map it votes in
81citing papers in PubMed
0.5field-weighted citation impact, top 37% 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

81 citing papers in PubMed, 154 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Journal of chemical information and modeling · 2025
    Article
  5. Article
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  7. Frustration in physiology and molecular medicine.Molecular aspects of medicine · 2025
    Review
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  11. Article
  12. Review
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  17. Review
  18. Article
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21 more citing papers are in PubMed but not listed here.

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

2 authors at 1 institution in 1 country.

Bin XiaBeijing Nuclear Magnetic Resonance Center, College of Chemistry and Molecular Engineering, and School of Life Sciences, Peking University, Beijing 100871, China. binxia@pku.edu.cn
Xue Kang
Peking University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The worldwide outbreak of the severe acute respiratory syndrome (SARS) in 2003 was due to the transmission of SARS coronavirus (SARS-CoV). The main protease (M(pro)) of SARS-CoV is essential for the viral life cycle, and is considered to be an attractive target of anti-SARS drug development. As a key enzyme for proteolytic processing of viral polyproteins to produce functional non-structure proteins, M(pro) is first auto-cleaved out of polyproteins. The monomeric form of M(pro) is enzymatically inactive, and it is activated through homo-dimerization which is strongly affected by extra residues to both ends of the mature enzyme. This review provides a summary of the related literatures on the study of the quaternary structure, activation, and self-maturation of M(pro) over the past years.

Indexed as

Cysteine EndopeptidasesViral ProteinsCoronavirus 3C ProteasesCrystallography, X-RayEnzyme ActivationHumansModels, MolecularPolyproteinsProtein MultimerizationProtein Structure, TertiarySevere Acute Respiratory SyndromeSevere acute respiratory syndrome-related coronavirusCoronavirus 3C ProteasesCysteine EndopeptidasesPolyproteinsViral Proteins

Identifiers

PMID21533772
PMCPMC4875205
OpenAlexW2008428711

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.