ArticleNature communications2021
Molecular insights into receptor binding energetics and neutralization of SARS-CoV-2 variants.
Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers, 1 of them a synthesis that pooled 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.
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.
Who cites it
49 citing papers in PubMed, 1 synthesis or guideline pooled it, 80 citations in OpenAlex.
- Newly Emerged Antiviral Strategies for SARS-CoV-2: From Deciphering Viral Protein Structural Function to the Development of Vaccines, Antibodies, and Small Molecules.International journal of molecular sciences · 2022Pooled it
- The Effect of Ligand Reactivity and Carrier Mechanics on Thiol-Mediated Cellular Uptake for miRNA Nano-Drugs.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Structural dynamics and allosteric communication of a SARS-like bat coronavirus spike glycoprotein.Biophysical journal · 2026Article
- Insights into the recruitment of the H3K4me3 reader Spp1 by the meiotic double-strand break protein Mer2.Nucleic acids research · 2026Article
- An optimized contact map for GōMartini 3 enabling conformational changes in protein assemblies.Biophysical journal · 2026Article
- Physical Changes of Biomacromolecules upon Covalent Surface Immobilization.Langmuir : the ACS journal of surfaces and colloids · 2026Article
- Cleaved versus Uncleaved: How furin cleavage reshapes the conformational landscape of SARS-CoV-2 spike.Protein science : a publication of the Protein Society · 2025Article
- Modulation of SARS-CoV-2 spike binding to ACE2 through conformational selection.Nature nanotechnology · 2025Article
- GōMartini 3: From large conformational changes in proteins to environmental bias corrections.Nature communications · 2025Article
- Conformational and Stability Analysis of SARS-CoV-2 Spike Protein Variants by Molecular Simulation.Pathogens (Basel, Switzerland) · 2025Article
- Variant-Specific Interactions at the Plasma Membrane: Heparan Sulfate's Impact on SARS-CoV-2 Binding Kinetics.Analytical chemistry · 2025Article
- From viral assembly to host interaction: AFM's contributions to virology.Journal of virology · 2025Review
- Probing living cell dynamics and molecular interactions using atomic force microscopy.Biophysical reviews · 2024Review
- Widespread exposure to SARS-CoV-2 in wildlife communities.Nature communications · 2024Article
- Micro-second time-resolved X-ray single-molecule internal motions of SARS-CoV-2 spike variants.Biochemistry and biophysics reports · 2024Article
- Single-Molecule Investigation of the Binding Interface Stability of SARS-CoV-2 Variants with ACE2.ACS nanoscience Au · 2024Article
- Single-molecule force stability of the SARS-CoV-2-ACE2 interface in variants-of-concern.Nature nanotechnology · 2024Article
- Molecular-Scale Investigations Reveal the Effect of Natural Polyphenols on BAX/Bcl-2 Interactions.International journal of molecular sciences · 2024Article
- Deciphering the free energy landscapes of SARS-CoV-2 wild type and Omicron variant interacting with human ACE2.The Journal of chemical physics · 2024Article
- Identification of conserved linear epitopes in the SARS-CoV-2 receptor-binding region using monoclonal antibodies.Heliyon · 2023Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 4 institutions in 2 countries.
Funding
Abstract
Despite an unprecedented global gain in knowledge since the emergence of SARS-CoV-2, almost all mechanistic knowledge related to the molecular and cellular details of viral replication, pathology and virulence has been generated using early prototypic isolates of SARS-CoV-2. Here, using atomic force microscopy and molecular dynamics, we investigated how these mutations quantitatively affected the kinetic, thermodynamic and structural properties of RBD-ACE2 complex formation. We observed for several variants of concern a significant increase in the RBD-ACE2 complex stability. While the N501Y and E484Q mutations are particularly important for the greater stability, the N501Y mutation is unlikely to significantly affect antibody neutralization. This work provides unprecedented atomistic detail on the binding of SARS-CoV-2 variants and provides insight into the impact of viral mutations on infection-induced immunity.
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What OpenQuestion holds
Registered trials
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.