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

A disintegrin and metalloproteinase domain 9 facilitates SARS-CoV-2 entry into cells with low ACE2 expression

15 Sept 2023

Abstract excerpt

ABSTRACT Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), the etiological agent of the Coronavirus disease-19 (COVID-19) pandemic, utilizes angiotensin-converting enzyme 2 (ACE2) as a receptor for virus infection. However, the expression pattern of ACE2 does not coincide with the tissue tropism of SARS-CoV-2, hinting that other host proteins might be involved in facilitating SARS-CoV-2 entry. To...

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 SARS-CoV-2 and COVID-19 Research
Share to SARS-CoV-2 detection and testing

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 37713503
DOI: 10.1128/spectrum.03854-22

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

A disintegrin and metalloproteinase domain 9 facilitates SARS-CoV-2 entry into cells with low ACE2 expressionPMID 37713503Read ↗

Metalloproteinase-dependent and TMPRSS2-independnt cell surface entry pathway of SARS-CoV-2 requires the furin-cleavage site and the S2 domain of spike proteinSemantic proximity Read ↗

Control of SARS-CoV-2 infection by MT1-MMP-mediated shedding of ACE2Semantic proximity Read ↗

Identification of a SARS-CoV-2 host metalloproteinase-dependent entry pathway differentially used by SARS-CoV-2 and variants of concern Alpha, Delta, and OmicronSemantic proximity Read ↗

SARS-CoV-2 Cell Entry Depends on ACE2 and TMPRSS2 and Is Blocked by a Clinically Proven Protease InhibitorSemantic proximity Read ↗

TMPRSS11D and TMPRSS13 Activate the SARS-CoV-2 Spike ProteinSemantic proximity Read ↗

A Review on Expression, Pathological Roles, and Inhibition of TMPRSS2, the Serine Protease Responsible for SARS-CoV-2 Spike Protein ActivationSemantic proximity Read ↗

Potential COVID‐19 therapeutic approaches targeting angiotensin‐converting enzyme 2; An updated reviewSemantic proximity Read ↗

ADAM10 and ADAM17 promote SARS‐CoV‐2 cell entry and spike protein‐mediated lung cell fusionSemantic proximity Read ↗

SARS-CoV-2-Specific Immune Response and the Pathogenesis of COVID-19Semantic proximity Read ↗

SARS-CoV-2 infection suppresses ACE2 function and antiviral immune response in the upper respiratory tract of infected patientsSemantic proximity Read ↗

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

Downregulation of Membrane-bound Angiotensin Converting Enzyme 2 (ACE2) Receptor has a Pivotal Role in COVID-19 ImmunopathologySemantic proximity Read ↗

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