PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
35549865-9	2022	Of interest, restoration of NO by L-arginine may attenuate SARS-CoV-2 infection through different mechanisms, including reduction binding of SARS-CoV-2 to ACE2, inhibition of transmembrane protease serine type 2 (TMPRSS2) a critical for activation of SARS-CoV-2 spike protein and cellular entry, inhibition proliferation and replication of SARS-CoV-2, and prevention of SARS-CoV-2-induced coagulopathy.	Arginine	34-44	transmembrane serine protease 2	Homo sapiens	213-220	
34209110-1	2021	Positively charged groups that mimic arginine or lysine in a natural substrate of trypsin are necessary for drugs to inhibit the trypsin-like serine protease TMPRSS2 that is involved in the viral entry and spread of coronaviruses, including SARS-CoV-2.	Arginine	37-45	transmembrane serine protease 2	Homo sapiens	158-165	
30413791-11	2018	These findings suggest that cleavage at S2" is carried out by proteases recognizing a single arginine, most likely TMPRSS2 and cathepsin L.	Arginine	93-101	transmembrane serine protease 2	Homo sapiens	115-122	
24600012-3	2014	The type II transmembrane serine protease TMPRSS2 is expressed in the respiratory tract and is capable of activating a variety of respiratory viruses, including low-pathogenic (LP) IAVs possessing a single arginine residue at the cleavage site.	Arginine	206-214	transmembrane serine protease 2	Homo sapiens	42-49	
26095298-5	2015	Most influenza virus strains contain a HA sequence with a single arginine at the cleavage site suitable for processing by the trypsin-like serine proteases human airway trypsin-like protease (HAT) and transmembrane protease serine 2 (TMPRSS2), albeit a minority of viruses possesses HA cleavage site motifs that are processed by other proteases.	Arginine	65-73	transmembrane serine protease 2	Homo sapiens	201-232	
24227843-4	2014	Here, we show 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.	Arginine	19-27	transmembrane serine protease 2	Homo sapiens	113-120