PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
8942978-8	1996	These structural features are unique to CA IV and provide a framework for the design of sulfonamide inhibitors selective for this particular isozyme.	Sulfonamides	88-99	carbonic anhydrase 4	Homo sapiens	40-45	
10995069-0	2000	Carbonic anhydrase inhibitors: synthesis of sulfonamides incorporating 2,4,6-trisubstituted-pyridinium-ethylcarboxamido moieties possessing membrane-impermeability and in vivo selectivity for the membrane-bound (CA IV) versus the cytosolic (CA I and CA II) isozymes.	Sulfonamides	44-56	carbonic anhydrase 4	Homo sapiens	212-217	
10488246-4	1999	Potent inhibition was observed against all three isozymes but especially against CA I, which is generally 10-75 times less susceptible to inhibition by the classical sulfonamides in clinical use as compared to the other major red cell isozyme, CA II, or the membrane-bound one, CA IV.	Sulfonamides	166-178	carbonic anhydrase 4	Homo sapiens	278-283	
9054574-11	1997	Finally, the affinity of CA IV for sulfonamide inhibitors is decreased up to 65-fold compared to CA II as demonstrated by fluorescence titration.	Sulfonamides	35-46	carbonic anhydrase 4	Homo sapiens	25-30	
8037456-5	1994	The enzyme also resembles mammalian CA IV in its relative sensitivity to inhibition by sulfonamides and the resistance to inhibition by halide ions.	Sulfonamides	87-99	carbonic anhydrase 4	Homo sapiens	36-41	
31476557-1	2019	By exploiting the power of multicomponent chemistry, a relatively small, diverse set of primary sulfonamides was synthesized and screened against a panel of human carbonic anhydrases to reveal a low-nanomolar, albeit non-selective hCA IV lead inhibitor.	Sulfonamides	96-108	carbonic anhydrase 4	Homo sapiens	231-237	
2111324-5	1990	CA IV resembles CA II in being a "high activity" isozyme, relatively resistant to inhibition by halide ions and sensitive to inhibition by sulfonamides.	Sulfonamides	139-151	carbonic anhydrase 4	Homo sapiens	0-5	
30380448-5	2019	Most screened sulfonamides exhibited great potency in inhibiting CA isoforms II, widely involved in glaucoma and other pathologies (KIs in the range of 0.7-62.3 nM), and IX, that is a validated anti-tumor target (KIs in the range of 3.0-50.9 nM), whereas interesting hydrophilicity-dependent inhibitory profiles were measured against isoform CA IV (KIs in the range of 3.9-428.6 nM).	Sulfonamides	14-26	carbonic anhydrase 4	Homo sapiens	342-347	
27160030-3	2016	The separation of the CA II and CA IV (both of which are catalytically active isoforms, highly sensitive to sulfonamide-type inhibitors) is particularly remarkable and is adding significantly to the global body of data on the chemical biology of carbonic anhydrases.	Sulfonamides	108-119	carbonic anhydrase 4	Homo sapiens	32-37	
28975383-8	2018	Sulfonamide inhibitor binding to CA IV is linked to several reactions-the deprotonation of the sulfonamide amino group, the protonation of CA-Zn(II)-bound hydroxide at the active site of CA IV, and the compensating reactions of the buffer.	Sulfonamides	0-11	carbonic anhydrase 4	Homo sapiens	33-38	
28975383-8	2018	Sulfonamide inhibitor binding to CA IV is linked to several reactions-the deprotonation of the sulfonamide amino group, the protonation of CA-Zn(II)-bound hydroxide at the active site of CA IV, and the compensating reactions of the buffer.	Sulfonamides	0-11	carbonic anhydrase 4	Homo sapiens	187-192	
28975383-8	2018	Sulfonamide inhibitor binding to CA IV is linked to several reactions-the deprotonation of the sulfonamide amino group, the protonation of CA-Zn(II)-bound hydroxide at the active site of CA IV, and the compensating reactions of the buffer.	Sulfonamides	95-106	carbonic anhydrase 4	Homo sapiens	33-38	
28975383-8	2018	Sulfonamide inhibitor binding to CA IV is linked to several reactions-the deprotonation of the sulfonamide amino group, the protonation of CA-Zn(II)-bound hydroxide at the active site of CA IV, and the compensating reactions of the buffer.	Sulfonamides	95-106	carbonic anhydrase 4	Homo sapiens	187-192	
28975383-9	2018	The dissection of binding-linked reactions yielded the intrinsic thermodynamic parameters, characterizing the interaction between CA IV and the sulfonamides in the binding-able protonation forms, including Gibbs energy, enthalpy, and entropy, that could be used for the characterization of binding to any CA in the process of drug design.	Sulfonamides	144-156	carbonic anhydrase 4	Homo sapiens	130-135