Heike Hofmann-Winkler

TL;DR: In this article, the authors show that SARS-CoV-2/COVID-19 variants B.1.7 (UK), B.351 (South Africa), and P.1 (Brazil) harbor mutations in the viral spike (S) protein that may alter virus-host cell interactions and confer resistance to inhibitors and antibodies.

TL;DR: It is shown that arginine and lysine residues within ACE2 amino acids 697 to 716 are essential for cleavage by TMPRSS2 and HAT and that ACE2 processing is required for augmentation of SARS-S-driven entry by these proteases.

TL;DR: The results indicate that chloroquine targets a pathway for viral activation that is not active in lung cells and is unlikely to protect against the spread of SARS-CoV-2 in and between patients.

TL;DR: Results indicate that HCoV-229E can employ redundant proteolytic pathways to ensure its activation in host cells, and suggest that diverse human respiratory viruses are activated by TMPRSS2, which may constitute a target for antiviral intervention.

TL;DR: In this article, the authors showed that several TMPRSS2-related proteases activate SARS-CoV-2 and that two of them are robustly expressed in the upper respiratory tract and can be blocked by Camostat mesylate and its metabolite GBPA.