Evidence map›Paper›PMID 33674802›Full record

ArticleNature structural & molecular biology2021

Structural basis for inhibition of the SARS-CoV-2 RNA polymerase by suramin.

Wanchao Yin, Xiaodong Luan, Zhihai Li, Ziwei Zhou, Qingxing Wang, Minqi Gao, Xiaoxi Wang, Fulai Zhou, Jingjing Shi, Erli You and 9 more

Open access · bronzeAbstract read
PubMed Publisher
In one paragraph

Article in Nature structural & molecular biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 95 papers.

0numbers the graph read from it
0cells of the map it votes in
95citing papers in PubMed
9.6field-weighted citation impact, top 2% 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

95 citing papers in PubMed, 180 citations in OpenAlex.

  1. Trial
  2. Review
  3. Article
  4. Review
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. RedefiningMolecular therapy. Nucleic acids · 2025
    Article

35 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

19 authors at 3 institutions in 2 countries.

Wanchao Yin *The CAS Key Laboratory of Receptor Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai, China.ORCID http://orcid.org/0000-0002-6889-4907
Xiaodong Luan *School of Medicine, Tsinghua University, Haidian District, Beijing, China.ORCID http://orcid.org/0000-0002-1279-5432
Zhihai Li *The CAS Key Laboratory of Receptor Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai, China.ORCID http://orcid.org/0000-0002-2816-6243
Ziwei Zhou *The CAS Key Laboratory of Receptor Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai, China.
Qingxing Wang *University of Chinese Academy of Sciences, Beijing, China.ORCID http://orcid.org/0000-0003-1028-1267
Minqi GaoWuxiBiortus Biosciences Co. Ltd, Jiangyin, China.
Xiaoxi WangThe CAS Key Laboratory of Receptor Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai, China.
Fulai ZhouThe CAS Key Laboratory of Receptor Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai, China.
Jingjing ShiThe CAS Key Laboratory of Receptor Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai, China.
Erli YouThe CAS Key Laboratory of Receptor Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai, China.
Mingliang LiuThe CAS Key Laboratory of Receptor Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai, China.
Qingxia WangThe CAS Key Laboratory of Receptor Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai, China.
Yi JiangThe CAS Key Laboratory of Receptor Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai, China.ORCID http://orcid.org/0000-0002-0723-1413
Hualiang JiangThe CAS Key Laboratory of Receptor Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai, China.ORCID http://orcid.org/0000-0003-0656-6315
Gengfu XiaoState Key Laboratory of Virology, Wuhan Institute of Virology, Center for Biosafety Mega-Science, Chinese Academy of Sciences, Wuhan, Hubei, China.
Leike ZhangUniversity of Chinese Academy of Sciences, Beijing, China. zhangleike@wh.iov.cn.ORCID http://orcid.org/0000-0002-2593-2571
Xuekui YuThe CAS Key Laboratory of Receptor Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai, China. xkyu@simm.ac.cn.ORCID http://orcid.org/0000-0002-4434-2040
Shuyang ZhangSchool of Medicine, Tsinghua University, Haidian District, Beijing, China. shuyangzhang103@nrdrs.org.ORCID http://orcid.org/0000-0002-1532-0029
H Eric XuThe CAS Key Laboratory of Receptor Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai, China. eric.xu@simm.ac.cn.ORCID http://orcid.org/0000-0002-6829-8144
Chinese Academy of Sciences · CNChinese Academy of Medical Sciences & Peking Union Medical College · CNBiortus (China) · CN

Funding

Science and Technology Commission of Shanghai Municipality (Shanghai Municipal Science and Technology Commission) 2019SHZDZX02
6 · The paper itself

Abstract

The COVID-19 pandemic caused by nonstop infections of SARS-CoV-2 has continued to ravage many countries worldwide. Here we report that suramin, a 100-year-old drug, is a potent inhibitor of the SARS-CoV-2 RNA-dependent RNA polymerase (RdRp) and acts by blocking the binding of RNA to the enzyme. In biochemical assays, suramin and its derivatives are at least 20-fold more potent than remdesivir, the currently approved nucleotide drug for treatment of COVID-19. The 2.6 Å cryo-electron microscopy structure of the viral RdRp bound to suramin reveals two binding sites. One site directly blocks the binding of the RNA template strand and the other site clashes with the RNA primer strand near the RdRp catalytic site, thus inhibiting RdRp activity. Suramin blocks viral replication in Vero E6 cells, although the reasons underlying this effect are likely various. Our results provide a structural mechanism for a nonnucleotide inhibitor of the SARS-CoV-2 RdRp.

Indexed as

AnimalsAntiviral AgentsBinding SitesCatalytic DomainChlorocebus aethiopsCoronavirus RNA-Dependent RNA PolymeraseCryoelectron MicroscopyEnzyme InhibitorsProtein ConformationRNA, ViralSARS-CoV-2SuraminVero CellsVirus ReplicationAntiviral AgentsCoronavirus RNA-Dependent RNA PolymeraseEnzyme InhibitorsNSP12 protein, SARS-CoV-2RNA, ViralSuramin

Identifiers

PMID33674802
OpenAlexW3133499696

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.