PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
11748229-1	2002	Cysteine-to-serine mutations were constructed to test the functional and structural significance of the three non-extracellular cysteine residues in ecto-nucleoside-triphosphate diphosphohydrolase 3 (eNTPDase3).	Cysteine	0-8	ectonucleoside triphosphate diphosphohydrolase 3	Homo sapiens	200-209	
11748229-1	2002	Cysteine-to-serine mutations were constructed to test the functional and structural significance of the three non-extracellular cysteine residues in ecto-nucleoside-triphosphate diphosphohydrolase 3 (eNTPDase3).	Cysteine	128-136	ectonucleoside triphosphate diphosphohydrolase 3	Homo sapiens	149-198	
11748229-1	2002	Cysteine-to-serine mutations were constructed to test the functional and structural significance of the three non-extracellular cysteine residues in ecto-nucleoside-triphosphate diphosphohydrolase 3 (eNTPDase3).	Cysteine	128-136	ectonucleoside triphosphate diphosphohydrolase 3	Homo sapiens	200-209	
11748229-5	2002	Cys(501), located in the hydrophobic C-terminal membrane-spanning domain of eNTPDase3, was found to be the site of chemical modification by a sulfhydryl-specific reagent, p-chloromercuriphenylsulfonic acid (pCMPS), leading to inhibition of enzyme activity.	Cysteine	0-3	ectonucleoside triphosphate diphosphohydrolase 3	Homo sapiens	76-85	
20511214-8	2010	Using homology modeling, we built a 3D structure of NTPDase3 and designed 21 single cysteine mutations distributed over the surface of the enzyme.	Cysteine	84-92	ectonucleoside triphosphate diphosphohydrolase 3	Homo sapiens	52-60	
20511214-10	2010	Tethering NTPDase3 via cysteine residues located in a surface patch near the active site cleft masked the epitope and blocked antibody binding, as evaluated by enzyme inhibition assay and by ELISA.	Cysteine	23-31	ectonucleoside triphosphate diphosphohydrolase 3	Homo sapiens	10-18	
11748229-7	2002	Because Cys(501) is accessible for modification by the membrane-impermeant reagent pCMPS, we hypothesize that eNTPDase3 (and possibly other eNTPDases) contains a water-filled crevice allowing access of water and hydrophilic compounds to at least part of the protein"s C-terminal membrane-spanning helix.	Cysteine	8-11	ectonucleoside triphosphate diphosphohydrolase 3	Homo sapiens	110-119