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

Cryo-EM structure of infectious bronchitis coronavirus spike protein reveals structural and functional evolution of coronavirus spike proteins

23 Apr 2018

Abstract excerpt

As cell-invading molecular machinery, coronavirus spike proteins pose an evolutionary conundrum due to their high divergence. In this study, we determined the cryo-EM structure of avian infectious bronchitis coronavirus (IBV) spike protein from the γ-genus. The trimeric IBV spike ectodomain contains three receptor-binding S1 heads and a trimeric membrane-fusion S2 stalk. While IBV S2 is structurally similar to...

Read the complete abstract on PubMed

Topics

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

Share to Animal Virus Infections Studies
Share to SARS-CoV-2 and COVID-19 Research
Share to Viral gastroenteritis research and epidemiology

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 29684066
DOI: 10.1371/journal.ppat.1007009

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Cryo-EM structure of infectious bronchitis coronavirus spike protein reveals structural and functional evolution of coronavirus spike proteinsPMID 29684066Read ↗

Cryo-EM structures of HKU2 and SADS-CoV spike glycoproteins and insights into coronavirus evolutionSemantic proximity Read ↗

Structure, Function, and Evolution of Coronavirus Spike ProteinsSemantic proximity Read ↗

Architects of infection: A structural overview of SARS-related coronavirus spike glycoproteinsSemantic proximity Read ↗

Cryo-EM structure of a SARS-CoV-2 omicron spike protein ectodomain.Semantic proximity Read ↗

Cryo-EM structures of HKU2 and SADS-CoV spike glycoproteins provide insights into coronavirus evolutionSemantic proximity Read ↗

Cryo-electron Microscopy Structure of the Swine Acute Diarrhea Syndrome Coronavirus Spike Glycoprotein Provides Insights into Evolution of Unique Coronavirus Spike ProteinsSemantic proximity Read ↗

Bat and pangolin coronavirus spike glycoprotein structures provide insights into SARS-CoV-2 evolutionSemantic proximity Read ↗

Tectonic conformational changes of a coronavirus spike glycoprotein promote membrane fusion.Semantic proximity Read ↗

Cryo-electron microscopy structure of the SADS-CoV spike glycoprotein provides insights into an evolution of unique coronavirus spike proteinsSemantic proximity Read ↗

Structural impact on SARS-CoV-2 spike protein by D614G substitutionSemantic proximity Read ↗

Cryo-EM reveals variation in structural motifs within animal SARS-related coronavirus spike proteinsSemantic proximity Read ↗

Evidence for a Common Evolutionary Origin of Coronavirus Spike Protein Receptor-Binding SubunitsSemantic proximity Read ↗

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