Id |
Subject |
Object |
Predicate |
Lexical cue |
T1 |
0-90 |
Sentence |
denotes |
High affinity binding of SARS-CoV-2 spike protein enhances ACE2 carboxypeptidase activity. |
T2 |
91-225 |
Sentence |
denotes |
The novel severe acute respiratory syndrome coronavirus (SARS-CoV-2) has emerged to a pandemic and caused global public health crisis. |
T3 |
226-322 |
Sentence |
denotes |
Human angiotensin-converting enzyme 2(ACE2) was identified as the entry receptor for SARS-CoV-2. |
T4 |
323-461 |
Sentence |
denotes |
As a carboxypeptidase, ACE2 cleaves many biological substrates besides angiotensin II to control vasodilatation and vascular permeability. |
T5 |
462-620 |
Sentence |
denotes |
Given the nanomolar high affinity between ACE2 and SARS-CoV-2 spike protein, we investigated how this interaction would affect the enzymatic activity of ACE2. |
T6 |
621-800 |
Sentence |
denotes |
Surprisingly, SARS-CoV-2 trimeric spike protein increased ACE2 proteolytic activity ~3-10 fold against model peptide substrates, such as caspase-1 substrate and Bradykinin-analog. |
T7 |
801-903 |
Sentence |
denotes |
The enhancement in ACE2 enzymatic function was mediated by the binding of SARS-CoV-2 spike RBD domain. |
T8 |
904-1073 |
Sentence |
denotes |
These results highlighted the potential for SARS-CoV-2 infection to enhance ACE2 activity, which may be relevant to the cardiovascular symptoms associated with COVID-19. |