Evidence map›Paper›PMID 32081428›Full record

ArticleBiochemical and biophysical research communications2020

Structure analysis of the receptor binding of 2019-nCoV.

Yun Chen, Yao Guo, Yihang Pan, Zhizhuang Joe Zhao

Open access · hybridAbstract read
In one paragraph

Article in Biochemical and biophysical research communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 402 papers, 2 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
402citing papers in PubMed, 2 pooled it
20.4field-weighted citation impact, top 1% 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

402 citing papers in PubMed, 2 syntheses or guidelines pooled it, 853 citations in OpenAlex.

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  17. Stoichiometric insights into SARS-CoV-2 spike-ACE2 binding across variants.Computational and structural biotechnology journal · 2025
    Article
  18. Article
  19. Article
  20. Exploring Prehospital Data for Pandemic Preparedness: A Western Brazilian Amazon Case Study on COVID-19.International journal of environmental research and public health · 2024
    Article

342 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

4 authors at 1 institution in 2 countries.

Yun ChenEdmond H. Fischer Translational Medical Research Laboratory, Precision Medicine Center, The Seventh Affiliated Hospital, Sun Yat-sen University, Shenzhen, 518107, Guangdong, China.
Yao GuoEdmond H. Fischer Translational Medical Research Laboratory, Precision Medicine Center, The Seventh Affiliated Hospital, Sun Yat-sen University, Shenzhen, 518107, Guangdong, China.
Yihang PanEdmond H. Fischer Translational Medical Research Laboratory, Precision Medicine Center, The Seventh Affiliated Hospital, Sun Yat-sen University, Shenzhen, 518107, Guangdong, China. Electronic address: yihang73@hotmail.com.
Zhizhuang Joe ZhaoEdmond H. Fischer Translational Medical Research Laboratory, Precision Medicine Center, The Seventh Affiliated Hospital, Sun Yat-sen University, Shenzhen, 518107, Guangdong, China; Department of Pathology, University of Oklahoma Health Sciences Center, 940 Stanton L. Young Blvd, Oklahoma City, OK, 73104, USA. Electronic address: joe-zhao@ouhsc.edu.
Sun Yat-sen University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

2019-nCoV is a newly identified coronavirus with high similarity to SARS-CoV. We performed a structural analysis of the receptor binding domain (RBD) of spike glycoprotein responsible for entry of coronaviruses into host cells. The RBDs from the two viruses share 72% identity in amino acid sequences, and molecular simulation reveals highly similar ternary structures. However, 2019-nCoV has a distinct loop with flexible glycyl residues replacing rigid prolyl residues in SARS-CoV. Molecular modeling revealed that 2019-nCoV RBD has a stronger interaction with angiotensin converting enzyme 2 (ACE2). A unique phenylalanine F486 in the flexible loop likely plays a major role because its penetration into a deep hydrophobic pocket in ACE2. ACE2 is widely expressed with conserved primary structures throughout the animal kingdom from fish, amphibians, reptiles, birds, to mammals. Structural analysis suggests that ACE2 from these animals can potentially bind RBD of 2019-nCoV, making them all possible natural hosts for the virus. 2019-nCoV is thought to be transmitted through respiratory droplets. However, since ACE2 is predominantly expressed in intestines, testis, and kidney, fecal-oral and other routes of transmission are also possible. Finally, antibodies and small molecular inhibitors that can block the interaction of ACE2 with RBD should be developed to combat the virus.

Indexed as

CoronavirusMolecular modelingSequence analysisStructure analysis

Identifiers

PMID32081428
PMCPMC7092824
OpenAlexW3006594788

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.