PMID-sentid	Pub_year	Sent_text	comp_official_name	comp_offset	protein_name	organism	prot_offset
9931016-2	1999	The cDNA encoding a human ecto-apyrase (HB6), predicted to have seven N-linked glycosylation sites, was transiently expressed in mammalian COS cells and the resulting membrane preparations were treated with peptide N-glycosidase F (PNGase-F).	Nitrogen	6-7	ectonucleoside triphosphate diphosphohydrolase 3	Homo sapiens	40-43
34416508-6	2021	Similarly, derivative 3b (IC50, 0.77 +- 0.06), 2h (IC50, 0.36 +- 0.01) and 2c (IC50, 0.90 +- 0.08) displayed excellent activity corresponding to NTPDase2, NTPDase3 and NTPdase8.	Deuterium	47-49	ectonucleoside triphosphate diphosphohydrolase 3	Homo sapiens	155-163
28956227-0	2017	Various N-glycoforms differentially upregulate E-NTPDase activity of the NTPDase3/CD39L3 ecto-enzymatic domain.	Nitrogen	8-9	ectonucleoside triphosphate diphosphohydrolase 3	Homo sapiens	73-81
34416508-4	2021	These quinoline derivatives had IC50 (microM) values in the range of 0.20-1.75, 0.77-2.20, 0.36-5.50 and 0.90-1.82 for NTPDase1, NTPDase2, NTPDase3 and NTPDase8, respectively.	quinoline	6-15	ectonucleoside triphosphate diphosphohydrolase 3	Homo sapiens	139-147
32973513-0	2020	Development of Anthraquinone Derivatives as Ectonucleoside Triphosphate Diphosphohydrolase (NTPDase) Inhibitors With Selectivity for NTPDase2 and NTPDase3.	Anthraquinones	15-28	ectonucleoside triphosphate diphosphohydrolase 3	Homo sapiens	146-154
31754326-0	2019	GATA Binding Protein 3 Boosts Extracellular ATP Hydrolysis and Inhibits Metastasis of Breast Cancer by Up-regulating Ectonucleoside Triphosphate Diphosphohydrolase 3.	Adenosine Triphosphate	44-47	ectonucleoside triphosphate diphosphohydrolase 3	Homo sapiens	117-165
31754326-5	2019	Here, we demonstrate that GATA3 reduces the ATP level in the breast cancer microenvironment and inhibits breast cancer metastasis by up-regulating ectonucleoside triphosphate diphosphohydrolase 3 (ENTPD3).	Adenosine Triphosphate	44-47	ectonucleoside triphosphate diphosphohydrolase 3	Homo sapiens	147-195
31754326-5	2019	Here, we demonstrate that GATA3 reduces the ATP level in the breast cancer microenvironment and inhibits breast cancer metastasis by up-regulating ectonucleoside triphosphate diphosphohydrolase 3 (ENTPD3).	Adenosine Triphosphate	44-47	ectonucleoside triphosphate diphosphohydrolase 3	Homo sapiens	197-203
31754326-7	2019	ENTPD3 hydrolyzes ATP in tumor microenvironment and suppresses breast cancer metastasis.	Adenosine Triphosphate	18-21	ectonucleoside triphosphate diphosphohydrolase 3	Homo sapiens	0-6
29273916-5	2018	In oviducts, remarkably, ectonucleoside triphosphate diphosphohydrolase 2 (NTPDase2) and NTPDase3, with the ability to hydrolyze ATP to AMP, are expressed in ciliated epithelial cells but with different subcellular localization.	Adenosine Triphosphate	129-132	ectonucleoside triphosphate diphosphohydrolase 3	Homo sapiens	89-97
29273916-5	2018	In oviducts, remarkably, ectonucleoside triphosphate diphosphohydrolase 2 (NTPDase2) and NTPDase3, with the ability to hydrolyze ATP to AMP, are expressed in ciliated epithelial cells but with different subcellular localization.	Adenosine Monophosphate	136-139	ectonucleoside triphosphate diphosphohydrolase 3	Homo sapiens	89-97
28956227-3	2017	NTPDase3/CD39L3is dominantly expressed in pancreatic islet cells, where it may regulate insulin secretion, and has seven N-linked glycosylation sites with four close to five highly conserved domains called "apyrase conserved regions" (ACRs).	Nitrogen	0-1	ectonucleoside triphosphate diphosphohydrolase 3	Homo sapiens	9-15
28956227-4	2017	In a manner similar to CD39, NTPDase3/CD39L3 uses ATP as its preferential substrate and also possesses significant activities toward other triphosphate and diphosphate nucleosides.	Adenosine Triphosphate	50-53	ectonucleoside triphosphate diphosphohydrolase 3	Homo sapiens	29-37
28956227-4	2017	In a manner similar to CD39, NTPDase3/CD39L3 uses ATP as its preferential substrate and also possesses significant activities toward other triphosphate and diphosphate nucleosides.	Adenosine Triphosphate	50-53	ectonucleoside triphosphate diphosphohydrolase 3	Homo sapiens	38-44
28956227-4	2017	In a manner similar to CD39, NTPDase3/CD39L3 uses ATP as its preferential substrate and also possesses significant activities toward other triphosphate and diphosphate nucleosides.	triphosphoric acid	139-151	ectonucleoside triphosphate diphosphohydrolase 3	Homo sapiens	29-37
28956227-4	2017	In a manner similar to CD39, NTPDase3/CD39L3 uses ATP as its preferential substrate and also possesses significant activities toward other triphosphate and diphosphate nucleosides.	triphosphoric acid	139-151	ectonucleoside triphosphate diphosphohydrolase 3	Homo sapiens	38-44
28956227-0	2017	Various N-glycoforms differentially upregulate E-NTPDase activity of the NTPDase3/CD39L3 ecto-enzymatic domain.	Nitrogen	8-9	ectonucleoside triphosphate diphosphohydrolase 3	Homo sapiens	82-88
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
28956227-4	2017	In a manner similar to CD39, NTPDase3/CD39L3 uses ATP as its preferential substrate and also possesses significant activities toward other triphosphate and diphosphate nucleosides.	diphosphate nucleosides	156-179	ectonucleoside triphosphate diphosphohydrolase 3	Homo sapiens	29-37
28956227-4	2017	In a manner similar to CD39, NTPDase3/CD39L3 uses ATP as its preferential substrate and also possesses significant activities toward other triphosphate and diphosphate nucleosides.	diphosphate nucleosides	156-179	ectonucleoside triphosphate diphosphohydrolase 3	Homo sapiens	38-44
28956227-5	2017	To understand the mechanism of the ecto-NTPDase activity and substrate specificity, potentially impacted by N-glycans, we have generated soluble enzymatic domains of NTPDase3/CD39L3 in human embryotic kidney cells with four different glycan modifications.	n-glycans	108-117	ectonucleoside triphosphate diphosphohydrolase 3	Homo sapiens	166-174
28956227-5	2017	To understand the mechanism of the ecto-NTPDase activity and substrate specificity, potentially impacted by N-glycans, we have generated soluble enzymatic domains of NTPDase3/CD39L3 in human embryotic kidney cells with four different glycan modifications.	Polysaccharides	110-116	ectonucleoside triphosphate diphosphohydrolase 3	Homo sapiens	166-174
28956227-5	2017	To understand the mechanism of the ecto-NTPDase activity and substrate specificity, potentially impacted by N-glycans, we have generated soluble enzymatic domains of NTPDase3/CD39L3 in human embryotic kidney cells with four different glycan modifications.	Polysaccharides	110-116	ectonucleoside triphosphate diphosphohydrolase 3	Homo sapiens	175-181
28956227-7	2017	Our functional data indicate that the non-glycosylated NTPDase3/CD39L3 ecto-enzymatic domain retains activity, but that N-glycan attachments, such as the GlcNAc-Asn, substantially upregulate specific NTPDase activity by 2-20 fold.	2-acetamido-2-deoxy-4-O-(beta-2-acetamid-2-deoxyglucopyranosyl)glucopyranose	154-160	ectonucleoside triphosphate diphosphohydrolase 3	Homo sapiens	55-63
28956227-7	2017	Our functional data indicate that the non-glycosylated NTPDase3/CD39L3 ecto-enzymatic domain retains activity, but that N-glycan attachments, such as the GlcNAc-Asn, substantially upregulate specific NTPDase activity by 2-20 fold.	2-acetamido-2-deoxy-4-O-(beta-2-acetamid-2-deoxyglucopyranosyl)glucopyranose	154-160	ectonucleoside triphosphate diphosphohydrolase 3	Homo sapiens	64-70
28956227-7	2017	Our functional data indicate that the non-glycosylated NTPDase3/CD39L3 ecto-enzymatic domain retains activity, but that N-glycan attachments, such as the GlcNAc-Asn, substantially upregulate specific NTPDase activity by 2-20 fold.	Asparagine	161-164	ectonucleoside triphosphate diphosphohydrolase 3	Homo sapiens	55-63
28956227-7	2017	Our functional data indicate that the non-glycosylated NTPDase3/CD39L3 ecto-enzymatic domain retains activity, but that N-glycan attachments, such as the GlcNAc-Asn, substantially upregulate specific NTPDase activity by 2-20 fold.	Asparagine	161-164	ectonucleoside triphosphate diphosphohydrolase 3	Homo sapiens	64-70
28956227-9	2017	Structural modeling analysis based on putative structures derived from bacterial-originated CD39 domain proteins suggests that N-glycan modifications at Asn149 next to ACR2 and/or Asn454, N-terminal to ACR5 have critical roles in regulating the catalytic pocket of NTPDase3/CD39L3.	n-glycan	127-135	ectonucleoside triphosphate diphosphohydrolase 3	Homo sapiens	265-273
28956227-9	2017	Structural modeling analysis based on putative structures derived from bacterial-originated CD39 domain proteins suggests that N-glycan modifications at Asn149 next to ACR2 and/or Asn454, N-terminal to ACR5 have critical roles in regulating the catalytic pocket of NTPDase3/CD39L3.	n-glycan	127-135	ectonucleoside triphosphate diphosphohydrolase 3	Homo sapiens	274-280
21103216-8	2010	Taken together, these results suggest a role for proline residues 53 and 481 in the linker regions of human NTPDase3 for coupling nucleotide binding at the enzyme active site to movements and/or rearrangements of the transmembrane helices necessary for optimal nucleotide hydrolysis.	Proline	49-56	ectonucleoside triphosphate diphosphohydrolase 3	Homo sapiens	108-116
20190036-2	2010	The present study shows that the obstructive disease cystic fibrosis (CF) affects the activity, expression, and tissue distribution of two ectonucleotidases found critical for the regulation of ATP on airway surfaces: NTPDase1 and NTPDase3.	Adenosine Triphosphate	194-197	ectonucleoside triphosphate diphosphohydrolase 3	Homo sapiens	231-239
19743837-2	2009	To investigate the structural and functional roles of the conserved polar residues in the N- and C-terminal transmembrane helices of human nucleoside triphosphate diphosphohydrolase 3 (NTPDase3) (N-terminus, S33, S39, T41, and Q44; C-terminus, T490, T495, and C501), each was singly mutated to alanine.	Alanine	294-301	ectonucleoside triphosphate diphosphohydrolase 3	Homo sapiens	185-193
19743837-8	2009	Lastly, Tween 20 substantially and selectively increases NTPDase3 activity, mediated by the transmembrane helices containing the conserved polar residues.	Polysorbates	8-16	ectonucleoside triphosphate diphosphohydrolase 3	Homo sapiens	57-65
19743837-9	2009	Taken together, the data suggest a model for putative hydrogen bond interactions of the conserved polar residues in the transmembrane domain of native, oligomeric NTPDase3.	Hydrogen	54-62	ectonucleoside triphosphate diphosphohydrolase 3	Homo sapiens	163-171
18693757-9	2008	These data suggest that ER-targeted NTPDase3 significantly depletes ATP in ER, whereas wild-type NTPDase3 is likely to acquire ATPase activity in a post-ER, but pre-Golgi, compartment, thus avoiding unproductive ATP hydrolysis and interference with protein folding in the ER.	Adenosine Triphosphate	68-71	ectonucleoside triphosphate diphosphohydrolase 3	Homo sapiens	36-44
18693757-9	2008	These data suggest that ER-targeted NTPDase3 significantly depletes ATP in ER, whereas wild-type NTPDase3 is likely to acquire ATPase activity in a post-ER, but pre-Golgi, compartment, thus avoiding unproductive ATP hydrolysis and interference with protein folding in the ER.	Adenosine Triphosphate	127-130	ectonucleoside triphosphate diphosphohydrolase 3	Homo sapiens	97-105
18693757-10	2008	ER-targeted NTPDase3 may be a useful experimental tool to study the effects of ER ATP depletion on ER function under normal and stress conditions.	Adenosine Triphosphate	82-85	ectonucleoside triphosphate diphosphohydrolase 3	Homo sapiens	12-20
16997558-2	2006	The most potent compound was K(6)H(2)[TiW(11)CoO(40)], exhibiting K(i) values of 0.140 microM (NTPDase1), 0.910 microM (NTPDase2), and 0.563 microM (NTPDase3).	k(6)h(2)	29-37	ectonucleoside triphosphate diphosphohydrolase 3	Homo sapiens	149-157
16997558-2	2006	The most potent compound was K(6)H(2)[TiW(11)CoO(40)], exhibiting K(i) values of 0.140 microM (NTPDase1), 0.910 microM (NTPDase2), and 0.563 microM (NTPDase3).	carboxyl radical	45-48	ectonucleoside triphosphate diphosphohydrolase 3	Homo sapiens	149-157
18404511-0	2005	Identification of a tyrosine residue responsible for N-acetylimidazole-induced increase of activity of ecto-nucleoside triphosphate diphosphohydrolase 3.	Tyrosine	20-28	ectonucleoside triphosphate diphosphohydrolase 3	Homo sapiens	103-152
18404511-0	2005	Identification of a tyrosine residue responsible for N-acetylimidazole-induced increase of activity of ecto-nucleoside triphosphate diphosphohydrolase 3.	N-acetylimidazole	53-70	ectonucleoside triphosphate diphosphohydrolase 3	Homo sapiens	103-152
18404511-1	2005	Chemical modification in combination with site-directed mutagenesis was used to identify a tyrosine residue responsible for the increase in ecto-nucleoside triphosphate diphosphohydrolase 3 (NTPDase3) nucleotidase activity after acetylation with a tyrosine-selective reagent, N-acetylimidazole.	Tyrosine	91-99	ectonucleoside triphosphate diphosphohydrolase 3	Homo sapiens	140-189
18404511-1	2005	Chemical modification in combination with site-directed mutagenesis was used to identify a tyrosine residue responsible for the increase in ecto-nucleoside triphosphate diphosphohydrolase 3 (NTPDase3) nucleotidase activity after acetylation with a tyrosine-selective reagent, N-acetylimidazole.	Tyrosine	91-99	ectonucleoside triphosphate diphosphohydrolase 3	Homo sapiens	191-199
18404511-1	2005	Chemical modification in combination with site-directed mutagenesis was used to identify a tyrosine residue responsible for the increase in ecto-nucleoside triphosphate diphosphohydrolase 3 (NTPDase3) nucleotidase activity after acetylation with a tyrosine-selective reagent, N-acetylimidazole.	Tyrosine	248-256	ectonucleoside triphosphate diphosphohydrolase 3	Homo sapiens	140-189
18404511-1	2005	Chemical modification in combination with site-directed mutagenesis was used to identify a tyrosine residue responsible for the increase in ecto-nucleoside triphosphate diphosphohydrolase 3 (NTPDase3) nucleotidase activity after acetylation with a tyrosine-selective reagent, N-acetylimidazole.	Tyrosine	248-256	ectonucleoside triphosphate diphosphohydrolase 3	Homo sapiens	191-199
18404511-1	2005	Chemical modification in combination with site-directed mutagenesis was used to identify a tyrosine residue responsible for the increase in ecto-nucleoside triphosphate diphosphohydrolase 3 (NTPDase3) nucleotidase activity after acetylation with a tyrosine-selective reagent, N-acetylimidazole.	N-acetylimidazole	276-293	ectonucleoside triphosphate diphosphohydrolase 3	Homo sapiens	140-189
18404511-1	2005	Chemical modification in combination with site-directed mutagenesis was used to identify a tyrosine residue responsible for the increase in ecto-nucleoside triphosphate diphosphohydrolase 3 (NTPDase3) nucleotidase activity after acetylation with a tyrosine-selective reagent, N-acetylimidazole.	N-acetylimidazole	276-293	ectonucleoside triphosphate diphosphohydrolase 3	Homo sapiens	191-199
18404511-10	2005	Thus, we speculate that the acetylation of tyrosine 252 might induce a subtle conformational change in NTPDase3, resulting in the observed increase in activity.	Tyrosine	43-51	ectonucleoside triphosphate diphosphohydrolase 3	Homo sapiens	103-111
26336160-7	2015	Furthermore, we have consistently observed differential ATP lifetime kinetics in the mucosal and serosal chambers, which is consistent with our immunofluorescent localization data, showing that ATP-converting enzymes ENTPD3 and alkaline phosphatase are expressed on urothelial basal surface, but not on the apical membrane.	Adenosine Triphosphate	56-59	ectonucleoside triphosphate diphosphohydrolase 3	Homo sapiens	217-223
25372046-5	2015	NTPDase3 and -8 yield AMP and ADP, while NTPDase2 results mainly in the formation of ADP.	Adenosine Monophosphate	22-25	ectonucleoside triphosphate diphosphohydrolase 3	Homo sapiens	0-8
25372046-5	2015	NTPDase3 and -8 yield AMP and ADP, while NTPDase2 results mainly in the formation of ADP.	Adenosine Diphosphate	30-33	ectonucleoside triphosphate diphosphohydrolase 3	Homo sapiens	0-8
25372046-5	2015	NTPDase3 and -8 yield AMP and ADP, while NTPDase2 results mainly in the formation of ADP.	Adenosine Diphosphate	85-88	ectonucleoside triphosphate diphosphohydrolase 3	Homo sapiens	0-8
25100739-3	2014	To devise a different strategy, we engineered and optimized the apyrase activity of human nucleoside triphosphate diphosphohydrolase-3 (CD39L3) to enhance scavenging of extracellular adenosine diphosphate, a predominant ligand of P2Y12 receptors.	Adenosine Diphosphate	183-204	ectonucleoside triphosphate diphosphohydrolase 3	Homo sapiens	136-142
25180024-10	2014	Weak inhibition (10-20%) of NTPDase3 and -8 was observed at 1 mM ticlopidine.	Ticlopidine	65-76	ectonucleoside triphosphate diphosphohydrolase 3	Homo sapiens	28-36
21103216-0	2010	Proline residues link the active site to transmembrane domain movements in human nucleoside triphosphate diphosphohydrolase 3 (NTPDase3).	Proline	0-7	ectonucleoside triphosphate diphosphohydrolase 3	Homo sapiens	81-125
21103216-0	2010	Proline residues link the active site to transmembrane domain movements in human nucleoside triphosphate diphosphohydrolase 3 (NTPDase3).	Proline	0-7	ectonucleoside triphosphate diphosphohydrolase 3	Homo sapiens	127-135
21103216-2	2010	Using site-directed mutagenesis, the roles of the conserved proline residues (N-terminal: P52 and P53; C-terminal: P472, P476, P481, P484, and P485) of human NTPDase3, located in the "linker regions" that connect the N- and C-terminal transmembrane helices with the extracellular active site, were examined.	Proline	60-67	ectonucleoside triphosphate diphosphohydrolase 3	Homo sapiens	158-166
21103216-4	2010	These "sensor" background mutant proteins (V42C and G489C NTPDase3) are enzymatically active and are cross-linked by copper phenanthroline less efficiently in the presence of adenosine triphosphate (ATP).	1,10-phenanthroline	117-138	ectonucleoside triphosphate diphosphohydrolase 3	Homo sapiens	58-66
21103216-4	2010	These "sensor" background mutant proteins (V42C and G489C NTPDase3) are enzymatically active and are cross-linked by copper phenanthroline less efficiently in the presence of adenosine triphosphate (ATP).	Adenosine Triphosphate	175-197	ectonucleoside triphosphate diphosphohydrolase 3	Homo sapiens	58-66
21103216-4	2010	These "sensor" background mutant proteins (V42C and G489C NTPDase3) are enzymatically active and are cross-linked by copper phenanthroline less efficiently in the presence of adenosine triphosphate (ATP).	Adenosine Triphosphate	199-202	ectonucleoside triphosphate diphosphohydrolase 3	Homo sapiens	58-66
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
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.	Sodium Dodecyl Sulfate	76-79	ectonucleoside triphosphate diphosphohydrolase 3	Homo sapiens	24-32
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	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
18404400-4	2004	This conserved lysine is located between apyrase conserved region 1 (ACR1) and an invariant glycosylation site (N81), in a region previously hypothesized to be important for NTPDase3 oligomeric structure.	Lysine	15-21	ectonucleoside triphosphate diphosphohydrolase 3	Homo sapiens	174-182
18404504-6	2005	In contrast, NTPDases 2, 3 and 8 are expected to promote the activation of ADP specific receptors, because in the presence of ATP they produce a sustained (NTPDase2) or transient (NTPDases 3 and 8) accumulation of ADP.	Adenosine Triphosphate	126-129	ectonucleoside triphosphate diphosphohydrolase 3	Homo sapiens	180-196
18404504-6	2005	In contrast, NTPDases 2, 3 and 8 are expected to promote the activation of ADP specific receptors, because in the presence of ATP they produce a sustained (NTPDase2) or transient (NTPDases 3 and 8) accumulation of ADP.	Adenosine Diphosphate	75-78	ectonucleoside triphosphate diphosphohydrolase 3	Homo sapiens	180-196
18404400-0	2004	Conserved lysine 79 is important for activity of ecto-nucleoside triphosphate diphosphohydrolase 3 (NTPDase3).	Lysine	10-16	ectonucleoside triphosphate diphosphohydrolase 3	Homo sapiens	49-98
18404400-0	2004	Conserved lysine 79 is important for activity of ecto-nucleoside triphosphate diphosphohydrolase 3 (NTPDase3).	Lysine	10-16	ectonucleoside triphosphate diphosphohydrolase 3	Homo sapiens	100-108
12706347-0	2003	Asparagine 81, an invariant glycosylation site near apyrase conserved region 1, is essential for full enzymatic activity of ecto-nucleoside triphosphate diphosphohydrolase 3.	Asparagine	0-10	ectonucleoside triphosphate diphosphohydrolase 3	Homo sapiens	124-173
18404400-2	2004	In this study, we mutated lysine 79 in human ecto-nucleoside triphosphate diphosphohydrolase 3 (NTPDase3).	Lysine	26-32	ectonucleoside triphosphate diphosphohydrolase 3	Homo sapiens	45-94
18404400-2	2004	In this study, we mutated lysine 79 in human ecto-nucleoside triphosphate diphosphohydrolase 3 (NTPDase3).	Lysine	26-32	ectonucleoside triphosphate diphosphohydrolase 3	Homo sapiens	96-104
18404400-3	2004	The residue corresponding to lysine 79 in NTPDase3 is conserved in all known cell surface membrane NTPDases (NTPDase1, 2, 3, and 8), but not in the soluble, monomeric NTPDases (NTPDase5 and 6), or in the intracellular, two transmembrane NTPDases (NTPDase4 and 7).	Lysine	29-35	ectonucleoside triphosphate diphosphohydrolase 3	Homo sapiens	42-50
12706347-4	2003	Only one of these putative glycosylation sites, asparagine 81 in NTPDase3, which is located near apyrase conserved region 1 (ACR1), is invariant in all the cell surface membrane eNTPDases.	Asparagine	48-58	ectonucleoside triphosphate diphosphohydrolase 3	Homo sapiens	65-73
12706347-5	2003	Using site-directed mutagenesis, mutants were constructed to eliminate this highly conserved N-glycosylation site in NTPDase3.	Nitrogen	93-94	ectonucleoside triphosphate diphosphohydrolase 3	Homo sapiens	117-125
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
11300774-6	2001	Mutagenesis of arginine 146 to proline (R146P) essentially converted the eNTPDase-3 ecto-apyrase to an ecto-ATPase (eNTPDase-2), mainly by decreasing the hydrolysis rates for nucleoside diphosphates.	nucleoside diphosphates	175-198	ectonucleoside triphosphate diphosphohydrolase 3	Homo sapiens	73-83
11300774-9	2001	We conclude that the residues corresponding to eNTPDase-3 glutamate 182 in ACR3 and serine 224 in ACR4 are essential for the enzymatic activity of eNTPDases in general, and that arginine 67, arginine 146, asparagine 191, and glutamine 226 are important for determining substrate specificity for human ecto-nucleoside triphosphate diphosphohydrolase 3.	Glutamic Acid	58-67	ectonucleoside triphosphate diphosphohydrolase 3	Homo sapiens	47-57
11300774-9	2001	We conclude that the residues corresponding to eNTPDase-3 glutamate 182 in ACR3 and serine 224 in ACR4 are essential for the enzymatic activity of eNTPDases in general, and that arginine 67, arginine 146, asparagine 191, and glutamine 226 are important for determining substrate specificity for human ecto-nucleoside triphosphate diphosphohydrolase 3.	Arginine	178-186	ectonucleoside triphosphate diphosphohydrolase 3	Homo sapiens	47-57
11300774-9	2001	We conclude that the residues corresponding to eNTPDase-3 glutamate 182 in ACR3 and serine 224 in ACR4 are essential for the enzymatic activity of eNTPDases in general, and that arginine 67, arginine 146, asparagine 191, and glutamine 226 are important for determining substrate specificity for human ecto-nucleoside triphosphate diphosphohydrolase 3.	Arginine	191-199	ectonucleoside triphosphate diphosphohydrolase 3	Homo sapiens	47-57
11300774-9	2001	We conclude that the residues corresponding to eNTPDase-3 glutamate 182 in ACR3 and serine 224 in ACR4 are essential for the enzymatic activity of eNTPDases in general, and that arginine 67, arginine 146, asparagine 191, and glutamine 226 are important for determining substrate specificity for human ecto-nucleoside triphosphate diphosphohydrolase 3.	Asparagine	205-215	ectonucleoside triphosphate diphosphohydrolase 3	Homo sapiens	47-57
11300774-9	2001	We conclude that the residues corresponding to eNTPDase-3 glutamate 182 in ACR3 and serine 224 in ACR4 are essential for the enzymatic activity of eNTPDases in general, and that arginine 67, arginine 146, asparagine 191, and glutamine 226 are important for determining substrate specificity for human ecto-nucleoside triphosphate diphosphohydrolase 3.	Glutamine	225-234	ectonucleoside triphosphate diphosphohydrolase 3	Homo sapiens	47-57
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.	p-chloromercuriphenylsulfonic acid	171-205	ectonucleoside triphosphate diphosphohydrolase 3	Homo sapiens	76-85
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.	PCMBS	207-212	ectonucleoside triphosphate diphosphohydrolase 3	Homo sapiens	76-85
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
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.	Water	162-167	ectonucleoside triphosphate diphosphohydrolase 3	Homo sapiens	110-119
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.	Water	202-207	ectonucleoside triphosphate diphosphohydrolase 3	Homo sapiens	110-119
11343793-0	2001	The importance of histidine residues in human ecto-nucleoside triphosphate diphosphohydrolase-3 as determined by site-directed mutagenesis.	Histidine	18-27	ectonucleoside triphosphate diphosphohydrolase 3	Homo sapiens	46-95