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

LRRC15 mediates an accessory interaction with the SARS-CoV-2 spike protein

3 Feb 2023

Abstract excerpt

The interactions between Severe Acute Respiratory Syndrome Coronavirus 2 (SARS-CoV-2) and human host factors enable the virus to propagate infections that lead to Coronavirus Disease 2019 (COVID-19). The spike protein is the largest structural component of the virus and mediates interactions essential for infection, including with the primary angiotensin-converting enzyme 2 (ACE2) receptor. We performed two...

Read the complete abstract on PubMed

Topics

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

Share to COVID-19 Clinical Research Studies
Share to Influenza Virus Research Studies
Share to SARS-CoV-2 and COVID-19 Research

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Source

Identifiers

PMID: 36735681
DOI: 10.1371/journal.pbio.3001959

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 8 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

LRRC15 mediates an accessory interaction with the SARS-CoV-2 spike proteinPMID 36735681Read ↗

LRRC15 mediates an accessory interaction with the SARS-CoV-2 spike proteinSemantic proximity Read ↗

LRRC15 inhibits SARS-CoV-2 cellular entry in transSemantic proximity Read ↗

The Host Interactome of Spike Expands the Tropism of SARS-CoV-2Semantic proximity Read ↗

Fibroblast-expressed LRRC15 is a receptor for SARS-CoV-2 spike and controls antiviral and antifibrotic transcriptional programsSemantic proximity Read ↗

Interaction network of SARS-CoV-2 with host receptome through spike proteinSemantic proximity Read ↗

Spike S1 domain interactome in non-pulmonary systems: A role beyond the receptor recognitionSemantic proximity Read ↗

ACE2-Independent Alternative Receptors for SARS-CoV-2Semantic proximity Read ↗

The SARS-CoV-2 spike protein binds and modulates estrogen receptorsSemantic proximity Read ↗

Variations in cell-surface ACE2 levels alter direct binding of SARS-CoV-2 Spike protein and viral infectivity: Implications for measuring Spike protein interactions with animal ACE2 orthologsSemantic proximity Read ↗

Spike protein recognition of mammalian ACE2 predicts the host range and an optimized ACE2 for SARS-CoV-2 infectionSemantic proximity Read ↗

Differential Ability of Spike Protein of SARS-CoV-2 Variants to Downregulate ACE2.Semantic proximity Read ↗

The spike protein of SARS-CoV-2 induces inflammation and EMT of lung epithelial cells and fibroblasts through the upregulation of GADD45ASemantic proximity Read ↗

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