Evidence map›Paper›PMID 36317101›Full record

ArticleScience bulletin2022

Antiviral drug design based on structural insights into the N-terminal domain and C-terminal domain of the SARS-CoV-2 nucleocapsid protein.

Xiaodong Luan, Xinming Li, Yufan Li, Gengchen Su, Wanchao Yin, Yi Jiang, Ning Xu, Feng Wang, Wang Cheng, Ye Jin and 4 more

Open access · hybridAbstract read
In one paragraph

Article in Science bulletin, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
3.0field-weighted citation impact, top 7% 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

15 citing papers in PubMed, 33 citations in OpenAlex.

  1. Article
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  12. Molecular characterization of SARS-CoV-2 nucleocapsid protein.Frontiers in cellular and infection microbiology · 2024
    Review
  13. Article
  14. Article
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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

14 authors at 7 institutions in 1 country.

Xiaodong LuanSchool of Medicine, Tsinghua University, Beijing 100084, China.
Xinming LiTsinghua-Peking Center for Life Sciences, Tsinghua University, Beijing 100084, China.
Yufan LiSchool of Medicine, Tsinghua University, Beijing 100084, China.
Gengchen SuSchool of Medicine, Tsinghua University, Beijing 100084, China.
Wanchao YinThe CAS Key Laboratory of Receptor Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai 201203, China.
Yi JiangThe CAS Key Laboratory of Receptor Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai 201203, China.
Ning XuSchool of Life Science, Tsinghua University, Beijing 100084, China.
Feng WangWuxiBiortus Biosciences Co., Ltd., Jiangyin 214437, China.
Wang ChengWuxiBiortus Biosciences Co., Ltd., Jiangyin 214437, China.
Ye JinDepartment of Cardiology, Peking Union Medical College Hospital, Peking Union Medical College and Chinese Academy of Medical Sciences, Beijing 100730, China.
Leike ZhangState Key Laboratory of Virology, Wuhan Institute of Virology, Center for Biosafety Mega-Science, Chinese Academy of Sciences, Wuhan 430071, China.
H Eric XuThe CAS Key Laboratory of Receptor Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai 201203, China.
Yi XueTsinghua-Peking Center for Life Sciences, Tsinghua University, Beijing 100084, China.
Shuyang ZhangDepartment of Cardiology, Peking Union Medical College Hospital, Peking Union Medical College and Chinese Academy of Medical Sciences, Beijing 100730, China.
Center for Life Sciences · CNChinese Academy of Medical Sciences & Peking Union Medical College · CNChinese Academy of Sciences · CNBiortus (China) · CNPeking Union Medical College Hospital · CNTsinghua University · CNUniversity of Chinese Academy of Sciences · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Nucleocapsid (N) protein plays crucial roles in the life cycle of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), including the formation of ribonucleoprotein (RNP) complex with the viral RNA. Here we reported the crystal structures of the N-terminal domain (NTD) and C-terminal domain (CTD) of the N protein and an NTD-RNA complex. Our structures reveal a unique tetramer organization of NTD and identify a distinct RNA binding mode in the NTD-RNA complex, which could contribute to the formation of the RNP complex. We also screened small molecule inhibitors of N-NTD and N-CTD and discovered that ceftriaxone sodium, an antibiotic, can block the binding of RNA to NTD and inhibit the formation of the RNP complex. These results together could facilitate the further research of antiviral drug design targeting N protein.

Indexed as

Ceftriaxone sodiumN-terminal domainNucleocapsid proteinSARS-CoV-2

Identifiers

PMID36317101
PMCPMC9605790
OpenAlexW4307346067

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.