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

TMEM106B is a receptor mediating ACE2-independent SARS-CoV-2 cell entry

7 Jul 2023

Abstract excerpt

SARS-CoV-2 is associated with broad tissue tropism, a characteristic often determined by the availability of entry receptors on host cells. Here, we show that TMEM106B, a lysosomal transmembrane protein, can serve as an alternative receptor for SARS-CoV-2 entry into angiotensin-converting enzyme 2 (ACE2)-negative cells. Spike substitution E484D increased TMEM106B binding, thereby enhancing TMEM106B-mediated...

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 Long-Term Effects of COVID-19
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: 37421949
DOI: 10.1016/j.cell.2023.06.005

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 10 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

TMEM106B is a receptor mediating ACE2-independent SARS-CoV-2 cell entryPMID 37421949Read ↗

TMEM106B mediates ACE2-independent replication of the SARS-CoV-2 S-E484D variant in airway-derived cell modelsSemantic proximity Read ↗

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

SARS-CoV-2 mechanisms of cell tropism in various organs considering host factorsSemantic proximity Read ↗

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

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

Atypical N-glycosylation of SARS-CoV-2 impairs the efficient binding of Spike-RBM to the human-host receptor hACE2Semantic proximity Read ↗

SARS-CoV-2 Entry Inhibitors: Small Molecules and Peptides Targeting Virus or Host CellsSemantic proximity Read ↗

TMEM106B-mediated SARS-CoV-2 infection allows for robust ACE2-independent infection in vitro but not in vivoSemantic proximity Read ↗

Rationally Designed, ACE2 Mimetic Binder to the SARS Cov-2 Associated Spike Protein for COVID-19 Therapeutics and BeyondSemantic proximity Read ↗

The Sialoside-Binding Pocket of SARS-CoV-2 Spike Glycoprotein Structurally Resembles MERS-CoVSemantic proximity Read ↗

Visualizing the Rapid Degradation and Differential Binding of Membrane-Bound Human ACE2 Protein Upon Binding and Internalization of the SARS-CoV-2 Spike RBD ProteinSemantic proximity Read ↗

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

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