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

Biophysical and structural characterizations of the effects of mutations on the structure-activity relationships of SARS-CoV-2 spike protein.

Methods in enzymology - 1 Jan 2022

Yu Pei-Yu, Yang Tzu-Jing, Hsu Shang-Te Danny

Abstract excerpt

Mutations on the spike (S) protein of SARS-CoV-2 could induce structural changes that help increase viral transmissibility and enhance resistance to antibody neutralization. Here, we report a robust workflow to prepare recombinant S protein variants and its host receptor angiotensin-convert enzyme 2 (ACE2) by using a mammalian cell expression system. The functional states of the S protein variants are...

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 Angiotensins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Cryoelectron Microscopy

Share to Mammals

Share to Peptidyl-Dipeptidase A

Share to Receptors, Virus

Share to SARS-CoV-2

Share to Spike Glycoprotein, Coronavirus

Source

Open in PubMed Open full text

Identifiers

PMID: 36220274
DOI: 10.1016/bs.mie.2022.07.013
PMCID: PMC9388326

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

Biophysical and structural characterizations of the effects of mutations on the structure-activity relationships of SARS-CoV-2 spike protein.PMID 36220274Read ↗

Effect of natural mutations of SARS-CoV-2 on spike structure, conformation, and antigenicity.Semantic proximity Read ↗

Structure and Mutations of SARS-CoV-2 Spike Protein: A Focused Overview.Semantic proximity Read ↗

Evolutionary trajectory of receptor binding specificity and promiscuity of the spike protein of SARS-CoV-2Semantic proximity Read ↗

Structural analysis of receptor binding domain mutations in SARS-CoV-2 variants of concern that modulate ACE2 and antibody binding.Semantic proximity Read ↗

Structural basis for enhanced infectivity and immune evasion of SARS-CoV-2 variants.Semantic proximity Read ↗

Comprehensive Structural and Molecular Comparison of Spike Proteins of SARS-CoV-2, SARS-CoV and MERS-CoV, and Their Interactions with ACE2Semantic proximity Read ↗

Effect of SARS-CoV-2 B.1.1.7 mutations on spike protein structure and function.Semantic proximity Read ↗

Structural and Functional Analysis of the D614G SARS-CoV-2 Spike Protein VariantSemantic proximity Read ↗

Conformational dynamics of SARS-CoV-2 trimeric spike glycoprotein in complex with receptor ACE2 revealed by cryo-EM.Semantic proximity Read ↗

The sequence of human ACE2 is suboptimal for binding the S spike protein of SARS coronavirus 2Semantic proximity Read ↗

Structural basis for enhanced infectivity and immune evasion of SARS-CoV-2 variantsSemantic proximity Read ↗

Cooperative multivalent receptor binding promotes exposure of the SARS-CoV-2 fusion machinery coreSemantic proximity Read ↗

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