Dispatched cleavage, mediated by Furin, regulates Dispatched membrane trafficking and release of Sonic Hedgehog ligand.

SARS-CoV-2 has evolved to cleverly mimic the FURIN-cleavage site in human ENaC-α, unlike any prior coronavirus strain, shedding new light on the Acute Respiratory Distress Syndrome (ARDS) in COVID-19 patients.

Proteolytic activation of a sodium-permeable channel that aids in gas exchange and fluid homeostasis likely evolved at the water to land transition in vertebrates.

Factor Xa and thrombin cleavage activate SARS-CoV-2 spike, widening the scope of host proteases involved in coronavirus entry and demonstrating the potential for dual anticoagulant/antiviral drugs.

The enzyme KPC-1/Furin down-regulates the DMA-1 receptor in neurons, allowing growing dendrites to migrate away from intermediate targets.

SARS-CoV-2 spike protein binding to receptor angiotensin-converting enzyme 2 allosterically enhances furin proteolysis at distal S1/S2 cleavage sites.

A critical role for glycosylation on viral entry and methods to use this knowledge to reduce SARS-CoV-2 infectivity has been demonstrated.

Endogenous BMP2/7 and BMP4/7 heterodimers form in vivo, and are the predominant functional ligand in many, if not all, tissues of developing mouse embryos.

Only three Spike mutations enable murine SARS-CoV-2 infection, which is still strictly ACE2 dependent and causes a COVID-19-like disease in mice with immunopathology-driven lung damage.

Whereas SARS-CoV-2 utilizes cathepsins to enter most cell lines, human airway organoids revealed that entry into relevant cells is dependent on serine proteases, which can be targeted for treatment.