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

Understanding the Driving Forces That Trigger Mutations in SARS-CoV-2: Mutational Energetics and the Role of Arginine Blockers in COVID-19 Therapy.

Viruses - 11 May 2022

Ridgway Harry, Chasapis Christos T, Kelaidonis Konstantinos, Ligielli Irene, Moore Graham J, Gadanec Laura Kate, Zulli Anthony, Apostolopoulos Vasso, Mavromoustakos Thomas, Matsoukas John M

Abstract excerpt

SARS-CoV-2 is a global challenge due to its ability to mutate into variants that spread more rapidly than the wild-type virus. Because the molecular biology of this virus has been studied in such great detail, it represents an archetypal paradigm for research into new antiviral drug therapies. The rapid evolution of SARS-CoV-2 in the human population is driven, in part, by mutations in the receptor-binding domain...

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 Arginine

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to COVID-19 Drug Treatment

Share to Receptors, Virus

Share to SARS-CoV-2

Share to Spike Glycoprotein, Coronavirus

Share to Viral Envelope Proteins

Source

Open in PubMed Open full text

Identifiers

PMID: 35632769
DOI: 10.3390/v14051029
PMCID: PMC9143829

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

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

Understanding the Driving Forces That Trigger Mutations in SARS-CoV-2: Mutational Energetics and the Role of Arginine Blockers in COVID-19 Therapy.PMID 35632769Read ↗

Molecular Epidemiology of SARS-CoV-2: The Dominant Role of Arginine in Mutations and Infectivity.Semantic proximity Read ↗

Inhibition of SARS-CoV-2 pathogenesis by potent peptides designed by the mutation of ACE2 binding region.Semantic proximity Read ↗

A multi-tier computational screening framework to effectively search the mutational space of SARS-CoV-2 receptor binding motif to identify mutants with enhanced ACE2 binding abilities.Semantic proximity Read ↗

Comparative analysis of ACE2 mutations and their impact on SARS-CoV-2 susceptibility within diverse ethnic groups.Semantic proximity Read ↗

Comparative molecular dynamics study of the receptor-binding domains in SARS-CoV-2 and SARS-CoV and the effects of mutations on the binding affinity.Semantic proximity Read ↗

Comprehensive Deep Mutational Scanning Reveals the Immune-Escaping Hotspots of SARS-CoV-2 Receptor-Binding Domain Targeting Neutralizing AntibodiesSemantic proximity Read ↗

Differences between Omicron SARS-CoV-2 RBD and other variants in their ability to interact with cell receptors and monoclonal antibodiesSemantic proximity Read ↗

S19W, T27W, and N330Y mutations in ACE2 enhance SARS-CoV-2 S-RBD binding toward both wild-type and antibody-resistant viruses and its molecular basisSemantic proximity Read ↗

E484K mutation in SARS-CoV-2 RBD enhances binding affinity with hACE2 but reduces interactions with neutralizing antibodies and nanobodies: Binding free energy calculation studiesSemantic proximity Read ↗

SARS-CoV-2 variants impact RBD conformational dynamics and ACE2 accessibilitySemantic proximity Read ↗

E484K mutation in SARS-CoV-2 RBD enhances binding affinity with hACE2 but reduces interactions with neutralizing antibodies and nanobodies: Binding free energy calculation studies.Semantic proximity Read ↗

Mutational Effect of Some Major COVID-19 Variants on Binding of the S Protein to ACE2.Semantic proximity Read ↗

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