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

Integrate structural analysis, isoform diversity, and interferon-inductive propensity of ACE2 to predict SARS-CoV2 susceptibility in vertebrates

31 Aug 2020

Abstract excerpt

The current new coronavirus disease (COVID-19) has caused globally over 0.4/6 million confirmed deaths/infected cases across more than 200 countries. As the etiological coronavirus (a.k.a. SARS-CoV2) may putatively have a bat origin, our understanding about its intermediate reservoir between bats and humans, especially its tropism in wild and domestic animals are mostly unknown. This constitutes major concerns in...

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 COVID-19 epidemiological studies
Share to SARS-CoV-2 and COVID-19 Research

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 32904785
DOI: 10.1016/j.heliyon.2020.e04818

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

Integrate structural analysis, isoform diversity, and interferon-inductive propensity of ACE2 to predict SARS-CoV2 susceptibility in vertebratesPMID 32904785Read ↗

ACE2 isoform diversity predicts the host susceptibility of SARS-CoV-2.Semantic proximity Read ↗

Broad Host Range of SARS-CoV-2 Predicted by Comparative and Structural Analysis of ACE2 in VertebratesSemantic proximity Read ↗

Broad host range of SARS-CoV-2 predicted by comparative and structural analysis of ACE2 in vertebrates.Semantic proximity Read ↗

Predicting susceptibility to SARS-CoV-2 infection based on structural differences in ACE2 across species.Semantic proximity Read ↗

A novel structure-based approach for identification of vertebrate susceptibility to SARS-CoV-2: implications for future surveillance programmesSemantic proximity Read ↗

ACE2-Variants Indicate Potential SARS-CoV-2-Susceptibility in Animals: An Extensive Molecular Dynamics StudySemantic proximity Read ↗

ACE2 models of frequently contacted animals provide clues of their SARS‐CoV‐2 S protein affinity and viral susceptibilitySemantic proximity Read ↗

ACE2 partially dictates the host range and tropism of SARS-CoV-2Semantic proximity Read ↗

In silico comparison of SARS-CoV-2 spike protein-ACE2 binding affinities across species and implications for virus originSemantic proximity Read ↗

The SARS-CoV-2 Spike protein has a broad tropism for mammalian ACE2 proteinsSemantic proximity Read ↗

The ancient cardioprotective mechanisms of ACE2 bestow SARS-CoV-2 with a wide host rangeSemantic proximity Read ↗

Interspecies transmission of SARS CoV-2 with special emphasis on viral mutations and ACE-2 receptor homology rolesSemantic proximity Read ↗

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