Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Impact of mutations in SARS-CoV-2 recombinant sub-variant XBB.1.16 on the binding affinity with human ACE2 receptor.

Journal of molecular graphics & modelling - 1 Sept 2024

Tariq Syeda Sumayya, Zia Komal, Nur-E-Alam Mohammad, Nerukh Dmitry, Farafonov Vladimir S, Ul-Haq Zaheer

Abstract excerpt

Despite the waning threat of the COVID-19 pandemic, its detrimental impact on global health persists. Regardless of natural immunity or immunity obtained through vaccination, emerging variants of the virus continue to undergo mutations and propagate globally. The persistent mutations in SARS-CoV-2, along with the subsequent formation of recombinant sub-variants has become a challenge for researchers and health...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Angiotensin-Converting Enzyme 2
Share to Binding Sites

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to COVID-19

Share to Molecular Docking Simulation

Share to Molecular Dynamics Simulation

Share to Protein Binding

Share to SARS-CoV-2

Share to Spike Glycoprotein, Coronavirus

Source

Identifiers

PMID: 38885553
DOI: 10.1016/j.jmgm.2024.108813

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Impact of mutations in SARS-CoV-2 recombinant sub-variant XBB.1.16 on the binding affinity with human ACE2 receptor.PMID 38885553Read ↗

The XBB.1.5 slightly increase the binding affinity for host receptor ACE2 and exhibit strongest immune escaping features: molecular modeling and free energy calculationSemantic proximity Read ↗

Deciphering the Impact of Mutations on the Binding Efficacy of SARS-CoV-2 Omicron and Delta Variants With Human ACE2 ReceptorSemantic proximity Read ↗

Preliminary Structural Data Revealed That the SARS‐CoV‐2 B.1.617 Variant's RBD Binds to ACE2 Receptor Stronger Than the Wild Type to Enhance the InfectivitySemantic proximity Read ↗

Molecular dynamics study on the strengthening behavior of Delta and Omicron SARS-CoV-2 spike RBD improved receptor-binding affinitySemantic proximity Read ↗

Molecular Dynamics Simulations Studies On The Effects Of Mutations On The Binding Affinities Between SARS-CoV-2 Spike RBD And Human ACE2Semantic proximity Read ↗

Decomposition of the SARS-CoV-2-ACE2 interface reveals a common trend among emerging viral variantsSemantic proximity Read ↗

Comparative Study of the Mutations Observed in the SARS-CoV-2 RBD Variants of Concern and Their Impact on the Interaction with the ACE2 Protein.Semantic proximity Read ↗

Investigating the role of glycans in Omicron sub-lineages XBB.1.5 and XBB.1.16 binding to host receptor using molecular dynamics and binding free energy calculations.Semantic proximity Read ↗

Mutations on RBD of SARS-CoV-2 Omicron variant result in stronger binding to human ACE2 receptorSemantic proximity Read ↗

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

Key mechanistic features of the trade-off between antibody escape and host cell binding in the SARS-CoV-2 Omicron variant spike proteinsSemantic proximity Read ↗

Molecular insights into the differential dynamics of SARS-CoV-2 variants of concern.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.