PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
16710859-3	2006	Among the enzymes for which sulfamide-based inhibitors were designed, are the carbonic anhydrases (CAs), a large number of proteases belonging to the aspartic protease (HIV-1 protease, gamma-secretase), serine protease (elastase, chymase, tryptase, and thrombin among others), and metalloprotease (carboxypeptidase A (CPA) and matrix metalloproteinases (MMP)) families.	fusarubin	28-37	carboxypeptidase A1	Homo sapiens	318-321	
15080932-0	2004	Sulfamide derivatives as transition state analogue inhibitors for carboxypeptidase A.	fusarubin	0-9	carboxypeptidase A1	Homo sapiens	66-84	
20141508-2	2006	Amongst the enzymes for which sulfamide-based inhibitors were designed are the carbonic anhydrases (CAs), and a large number of proteases belonging to the aspartic protease (HIV-1 protease, gamma-secretase), serine protease (elastase, chymase, tryptase and thrombin, among others) and metalloproteinase (carboxypeptidase A [CPA] and matrix metalloproteinase [MMP]) families.	fusarubin	30-39	carboxypeptidase A1	Homo sapiens	324-327	
20141508-5	2006	This is achieved either by directly coordinating to the metal ion found in some metalloenzymes (CAs, CPA, STS), usually by means of one of the nitrogen atoms present in the sulfamide motif, or, as in the case of the cyclic sulfamides, acting as HIV protease inhibitors interacting with the catalytically critical aspartic acid residues of the active site by means of an oxygen atom belonging to the HN-SO(2)-NH motif that substitutes a catalytically essential water molecule.	fusarubin	173-182	carboxypeptidase A1	Homo sapiens	101-104	
12431056-0	2002	Sulfamide-based inhibitors for carboxypeptidase A.	fusarubin	0-9	carboxypeptidase A1	Homo sapiens	31-49