Evidence map›Paper›PMID 34968782›Full record

ArticleBiochemical and biophysical research communications2022

Mutations on RBD of SARS-CoV-2 Omicron variant result in stronger binding to human ACE2 receptor.

Cecylia S Lupala, Yongjin Ye, Hong Chen, Xiao-Dong Su, Haiguang Liu

Abstract read
In one paragraph

Article in Biochemical and biophysical research communications, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 130 papers.

0numbers the graph read from it
0cells of the map it votes in
130citing papers in PubMed
–field-weighted citation impact
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

130 citing papers in PubMed.

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  4. Cancer-associated TRF1 mutations alter PARP1 interaction dynamics: an in silico study.Mammalian genome : official journal of the International Mammalian Genome Society · 2026
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  5. Current pharmaceutical biotechnology · 2026
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70 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

5 authors.

Cecylia S LupalaComplex Systems Division, Beijing Computational Science Research Center, Haidian, Beijing, 100193, People's Republic of China.
Yongjin YeComplex Systems Division, Beijing Computational Science Research Center, Haidian, Beijing, 100193, People's Republic of China.
Hong ChenSchool of Life Sciences, State Key Laboratory of Protein and Plant Gene Research and Biomedical Pioneering Innovation Center (BIOPIC), Peking University, Beijing, 100871, People's Republic of China.
Xiao-Dong SuSchool of Life Sciences, State Key Laboratory of Protein and Plant Gene Research and Biomedical Pioneering Innovation Center (BIOPIC), Peking University, Beijing, 100871, People's Republic of China. Electronic address: xdsu@pku.edu.cn.
Haiguang LiuComplex Systems Division, Beijing Computational Science Research Center, Haidian, Beijing, 100193, People's Republic of China; Physics Department, Beijing Normal University, Haidian, Beijing, 100875, People's Republic of China. Electronic address: hgliu@csrc.ac.cn.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The COVID-19 pandemic caused by the SARS-CoV-2 virus has led to more than 270 million infections and 5.3 million of deaths worldwide. Several major variants of SARS-CoV-2 have emerged and posed challenges in controlling the pandemic. The recently occurred Omicron variant raised serious concerns about reducing the efficacy of vaccines and neutralization antibodies due to its vast mutations. We have modelled the complex structure of the human ACE2 protein and the receptor binding domain (RBD) of Omicron Spike protein (S-protein), and conducted atomistic molecular dynamics simulations to study the binding interactions. The analysis shows that the Omicron RBD binds more strongly to the human ACE2 protein than the original strain. The mutations at the ACE2-RBD interface enhance the tight binding by increasing hydrogen bonding interaction and enlarging buried solvent accessible surface area.

Indexed as

Angiotensin-Converting Enzyme 2Binding SitesCOVID-19Host-Pathogen InteractionsHumansMolecular Docking SimulationMolecular Dynamics SimulationMutationProtein BindingProtein ConformationProtein Interaction Domains and MotifsSARS-CoV-2Spike Glycoprotein, CoronavirusACE2 protein, humanAngiotensin-Converting Enzyme 2Spike Glycoprotein, Coronavirusspike protein, SARS-CoV-2ACE2Molecular dynamics simulationOmicron mutantReceptor binding domainSARS-CoV-2

Identifiers

PMID34968782
PMCPMC8702632

What OpenQuestion holds

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Registered trials

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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.