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

Glycosylation and Serological Reactivity of an Expression-enhanced SARS-CoV-2 Viral Spike Mimetic

28 Oct 2021

Abstract excerpt

Extensive glycosylation of viral glycoproteins is a key feature of the antigenic surface of viruses and yet glycan processing can also be influenced by the manner of their recombinant production. The low yields of the soluble form of the trimeric spike (S) glycoprotein from SARS-CoV-2 has prompted advances in protein engineering that have greatly enhanced the stability and yields of the glycoprotein. The latest...

Read the complete abstract on PubMed

Topics

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

Share to Bacteriophages and microbial interactions
Share to SARS-CoV-2 and COVID-19 Research
Share to Virus-based gene therapy research

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 34717971
DOI: 10.1016/j.jmb.2021.167332

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Glycosylation and Serological Reactivity of an Expression-enhanced SARS-CoV-2 Viral Spike MimeticPMID 34717971Read ↗

Glycans of SARS-CoV-2 Spike Protein in Virus Infection and Antibody ProductionSemantic proximity Read ↗

Site Specific N- and O-glycosylation mapping of the Spike Proteins of SARS-CoV-2 Variants of ConcernSemantic proximity Read ↗

Site specific N- and O-glycosylation mapping of the spike proteins of SARS-CoV-2 variants of concernSemantic proximity Read ↗

Assessing Antigen Structural Integrity through Glycosylation Analysis of the SARS-CoV-2 Viral SpikeSemantic proximity Read ↗

Site-Specific Steric Control of SARS-CoV-2 Spike GlycosylationSemantic proximity Read ↗

SARS-CoV2 envelop proteins reshape the serological responses of COVID-19 patientsSemantic proximity Read ↗

Site-specific analysis of the SARS-CoV-2 glycan shieldSemantic proximity Read ↗

N-glycosylation profiles of the SARS-CoV-2 spike D614G mutant and its ancestral protein characterized by advanced mass spectrometrySemantic proximity Read ↗

N-Glycome Profile of the Spike Protein S1: Systemic and Comparative Analysis from Eleven Variants of SARS-CoV-2Semantic proximity Read ↗

Protein <i>N</i> -glycosylation is essential for SARS-CoV-2 infectionSemantic proximity Read ↗

Variations in O-Glycosylation Patterns Influence Viral Pathogenicity, Infectivity, and Transmissibility in SARS-CoV-2 VariantsSemantic proximity Read ↗

N-glycosylation profiles of the SARS-CoV-2 spike D614G mutant and its ancestral protein characterized by advanced mass spectrometry.Semantic proximity Read ↗

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