PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
19120451-4	2009	Antibody recognition of NTPDase3 is greatly attenuated by denaturation with SDS, and abolished by reducing agents, indicating the significance of the native conformation and the disulfide bonds for epitope recognition.	Disulfides	178-187	ectonucleoside triphosphate diphosphohydrolase 3	Homo sapiens	24-32	
15966724-0	2005	Characterization of disulfide bonds in human nucleoside triphosphate diphosphohydrolase 3 (NTPDase3): implications for NTPDase structural modeling.	Disulfides	20-29	ectonucleoside triphosphate diphosphohydrolase 3	Homo sapiens	45-89	
15966724-0	2005	Characterization of disulfide bonds in human nucleoside triphosphate diphosphohydrolase 3 (NTPDase3): implications for NTPDase structural modeling.	Disulfides	20-29	ectonucleoside triphosphate diphosphohydrolase 3	Homo sapiens	91-99	
15966724-2	2005	To investigate disulfide structure in human NTPDase3, we made single and double mutants of these 10 cysteines, and analyzed their enzymatic activity, glycosylation pattern, trafficking to the cell membrane, and sensitivity to reduction.	Disulfides	15-24	ectonucleoside triphosphate diphosphohydrolase 3	Homo sapiens	44-52	
15966724-10	2005	The resultant theoretical 3-D model of the extracellular portion of NTPDase3, based on homology with this exopolyphosphatase, is consistent with the assignment of the disulfide bonds occurring in regions of good fold similarity between NTPDase3 and the exopolyphosphatase.	Disulfides	167-176	ectonucleoside triphosphate diphosphohydrolase 3	Homo sapiens	68-76	
15966724-10	2005	The resultant theoretical 3-D model of the extracellular portion of NTPDase3, based on homology with this exopolyphosphatase, is consistent with the assignment of the disulfide bonds occurring in regions of good fold similarity between NTPDase3 and the exopolyphosphatase.	Disulfides	167-176	ectonucleoside triphosphate diphosphohydrolase 3	Homo sapiens	236-244