PMID-sentid	Pub_year	Sent_text	comp_official_name	comp_offset	protein_name	organism	prot_offset
25205248-3	2015	We inferred that deletion of NTPDase2 would increase local extracellular nucleoside triphosphate concentrations perturbing purinergic signaling and boosting progenitor cell proliferation and neurogenesis.	[[(2R,3S,4R,5S)-3,4-dihydroxy-5-methyloxolan-2-yl]methoxy-hydroxyphosphoryl] phosphono hydrogen phosphate	73-96	ectonucleoside triphosphate diphosphohydrolase 2	Mus musculus	29-37
25205248-2	2015	We have previously noted that stem/progenitor cells in the SVZ and the subgranular layer (SGL) of the dentate gyrus express high levels of plasma membrane-bound nucleoside triphosphate diphosphohydrolase 2 (NTPDase2), an ectoenzyme that hydrolyzes extracellular nucleoside diphosphates and triphosphates.	nucleoside diphosphates	262-285	ectonucleoside triphosphate diphosphohydrolase 2	Mus musculus	161-205
25205248-11	2015	We propose that NTPDase2 has functionality in scavenging mitogenic extracellular nucleoside triphosphates in neurogenic niches of the adult brain, thereby acting as a homeostatic regulator of nucleotide-mediated neural progenitor cell proliferation and expansion.	nucleoside triphosphates	81-105	ectonucleoside triphosphate diphosphohydrolase 2	Mus musculus	16-24
25205248-2	2015	We have previously noted that stem/progenitor cells in the SVZ and the subgranular layer (SGL) of the dentate gyrus express high levels of plasma membrane-bound nucleoside triphosphate diphosphohydrolase 2 (NTPDase2), an ectoenzyme that hydrolyzes extracellular nucleoside diphosphates and triphosphates.	nucleoside diphosphates	262-285	ectonucleoside triphosphate diphosphohydrolase 2	Mus musculus	207-215
25205248-2	2015	We have previously noted that stem/progenitor cells in the SVZ and the subgranular layer (SGL) of the dentate gyrus express high levels of plasma membrane-bound nucleoside triphosphate diphosphohydrolase 2 (NTPDase2), an ectoenzyme that hydrolyzes extracellular nucleoside diphosphates and triphosphates.	triphosphoric acid	290-303	ectonucleoside triphosphate diphosphohydrolase 2	Mus musculus	161-205
23959882-3	2013	In turn, the released ATP is hydrolyzed to ADP by a plasma membrane nucleoside triphosphate previously identified as nucleoside triphosphate diphosphohydrolase-2 (NTPDase2).	[[(2R,3S,4R,5S)-3,4-dihydroxy-5-methyloxolan-2-yl]methoxy-hydroxyphosphoryl] phosphono hydrogen phosphate	68-91	ectonucleoside triphosphate diphosphohydrolase 2	Mus musculus	117-161
25205248-2	2015	We have previously noted that stem/progenitor cells in the SVZ and the subgranular layer (SGL) of the dentate gyrus express high levels of plasma membrane-bound nucleoside triphosphate diphosphohydrolase 2 (NTPDase2), an ectoenzyme that hydrolyzes extracellular nucleoside diphosphates and triphosphates.	triphosphoric acid	290-303	ectonucleoside triphosphate diphosphohydrolase 2	Mus musculus	207-215
25203837-1	2014	The aims of this study were to distinguish between the primary and secondary effects of TGF-beta signalling disruption by Dox treatment in NTPDase2+ cells; and to investigate the interactions between TGF-beta signalling and Jagged2/Notch1 pathway in regulating the expansion of tongue epithelia stem cells.Transgenic mice expressing rtTA from the mouse NTPDase2 promoter or K14 promoter were used to generate an inducible dominant negative TGF-beta receptor type II (Tgfbr2) mutant model.Disruption of TGF-beta signalling in NTPDase2+ cells initially inhibited the formation of filiform papillae but led to their regeneration over time.	Doxorubicin	122-125	ectonucleoside triphosphate diphosphohydrolase 2	Mus musculus	139-147
23959882-3	2013	In turn, the released ATP is hydrolyzed to ADP by a plasma membrane nucleoside triphosphate previously identified as nucleoside triphosphate diphosphohydrolase-2 (NTPDase2).	[[(2R,3S,4R,5S)-3,4-dihydroxy-5-methyloxolan-2-yl]methoxy-hydroxyphosphoryl] phosphono hydrogen phosphate	68-91	ectonucleoside triphosphate diphosphohydrolase 2	Mus musculus	163-171
23959882-11	2013	We suggest that the excessive levels of extracellular ATP in the Entpd2-knockout animals desensitize the P2X receptors associated with nerve fibers, thereby depressing taste responses.	Adenosine Triphosphate	54-57	ectonucleoside triphosphate diphosphohydrolase 2	Mus musculus	65-71
23959882-3	2013	In turn, the released ATP is hydrolyzed to ADP by a plasma membrane nucleoside triphosphate previously identified as nucleoside triphosphate diphosphohydrolase-2 (NTPDase2).	Adenosine Triphosphate	22-25	ectonucleoside triphosphate diphosphohydrolase 2	Mus musculus	117-161
16476557-7	2006	In contrast, CD39L1/NTPDase2, a preferential nucleoside triphosphatase, activates platelets by preferentially converting ATP to ADP, the major agonist of platelet P2 receptors.	Adenosine Triphosphate	121-124	ectonucleoside triphosphate diphosphohydrolase 2	Mus musculus	13-19
23959882-3	2013	In turn, the released ATP is hydrolyzed to ADP by a plasma membrane nucleoside triphosphate previously identified as nucleoside triphosphate diphosphohydrolase-2 (NTPDase2).	Adenosine Triphosphate	22-25	ectonucleoside triphosphate diphosphohydrolase 2	Mus musculus	163-171
23959882-3	2013	In turn, the released ATP is hydrolyzed to ADP by a plasma membrane nucleoside triphosphate previously identified as nucleoside triphosphate diphosphohydrolase-2 (NTPDase2).	Adenosine Diphosphate	43-46	ectonucleoside triphosphate diphosphohydrolase 2	Mus musculus	117-161
23959882-3	2013	In turn, the released ATP is hydrolyzed to ADP by a plasma membrane nucleoside triphosphate previously identified as nucleoside triphosphate diphosphohydrolase-2 (NTPDase2).	Adenosine Diphosphate	43-46	ectonucleoside triphosphate diphosphohydrolase 2	Mus musculus	163-171
22865704-4	2012	Here we identify the major ectonucleotidase responsible for the hydrolysis of extracellular ATP in the mouse medial habenula as ectonucleoside triphosphate diphosphohydrolase 2 (NTPDase2), using immunostaining and enzyme histochemistry.	Adenosine Triphosphate	92-95	ectonucleoside triphosphate diphosphohydrolase 2	Mus musculus	178-186
23293651-4	2012	Here, using a transgenic mouse expressing rtTA from the mouse NTPDase2 promoter, we generated an inducible model by treatment with Doxycycline.	Doxycycline	131-142	ectonucleoside triphosphate diphosphohydrolase 2	Mus musculus	62-70
18031938-3	2007	NTPDase2 converts ATP and UTP to ADP and UDP, respectively, which are all P2Y receptor agonists.	Adenosine Triphosphate	18-21	ectonucleoside triphosphate diphosphohydrolase 2	Mus musculus	0-8
18031938-3	2007	NTPDase2 converts ATP and UTP to ADP and UDP, respectively, which are all P2Y receptor agonists.	Uridine Triphosphate	26-29	ectonucleoside triphosphate diphosphohydrolase 2	Mus musculus	0-8
18031938-3	2007	NTPDase2 converts ATP and UTP to ADP and UDP, respectively, which are all P2Y receptor agonists.	Adenosine Diphosphate	33-36	ectonucleoside triphosphate diphosphohydrolase 2	Mus musculus	0-8
18031938-3	2007	NTPDase2 converts ATP and UTP to ADP and UDP, respectively, which are all P2Y receptor agonists.	Uridine Diphosphate	41-44	ectonucleoside triphosphate diphosphohydrolase 2	Mus musculus	0-8
18404455-9	2007	The data suggest that NTPDase2 is the major ATP-degrading ectonucleotidase of the retinal parenchyma.	Adenosine Triphosphate	44-47	ectonucleoside triphosphate diphosphohydrolase 2	Mus musculus	22-30
18404455-10	2007	NTPDase2 expressed by Muller cells can be implicated in the regulation of purinergic calcium responses and cellular volume.	Calcium	85-92	ectonucleoside triphosphate diphosphohydrolase 2	Mus musculus	0-8
16476557-7	2006	In contrast, CD39L1/NTPDase2, a preferential nucleoside triphosphatase, activates platelets by preferentially converting ATP to ADP, the major agonist of platelet P2 receptors.	Adenosine Triphosphate	121-124	ectonucleoside triphosphate diphosphohydrolase 2	Mus musculus	20-28
16476557-7	2006	In contrast, CD39L1/NTPDase2, a preferential nucleoside triphosphatase, activates platelets by preferentially converting ATP to ADP, the major agonist of platelet P2 receptors.	Adenosine Diphosphate	128-131	ectonucleoside triphosphate diphosphohydrolase 2	Mus musculus	13-19
16476557-7	2006	In contrast, CD39L1/NTPDase2, a preferential nucleoside triphosphatase, activates platelets by preferentially converting ATP to ADP, the major agonist of platelet P2 receptors.	Adenosine Diphosphate	128-131	ectonucleoside triphosphate diphosphohydrolase 2	Mus musculus	20-28
16436623-1	2006	We have previously shown that the extracellular nucleoside triphosphate-hydrolyzing enzyme NTPDase2 is highly expressed in situ by stem/progenitor cells of the two neurogenic regions of the adult murine brain: the subventricular zone (type B cells) and the dentate gyrus of the hippocampus (residual radial glia).	[[(2R,3S,4R,5S)-3,4-dihydroxy-5-methyloxolan-2-yl]methoxy-hydroxyphosphoryl] phosphono hydrogen phosphate	48-71	ectonucleoside triphosphate diphosphohydrolase 2	Mus musculus	91-99
12392715-6	2002	TCDD increased expression of the NTPDase2 gene but only in the mouse and not in the human hepatoma cells.	Polychlorinated Dibenzodioxins	0-4	ectonucleoside triphosphate diphosphohydrolase 2	Mus musculus	33-41
15632415-5	2005	NTPDase1 has identity with CD39, a B lymphocyte activation marker, and hydrolyzes extracellular ATP and ADP to AMP within the vasculature, whereas NTPDase2/CD39L(ike)1 preferentially converts ATP to ADP outside of blood vessels.	Adenosine Triphosphate	192-195	ectonucleoside triphosphate diphosphohydrolase 2	Mus musculus	147-155
12417608-3	2002	Our previous studies have implicated CD39/NTPDase1 and CD39L1/NTPDase2, members of the ectonucleoside triphosphate diphosphohydrolase (E-NTPDase) family, as major ATP-hydrolyzing enzymes in the tissues lining the cochlear endolymphatic and perilymphatic compartments.	Adenosine Triphosphate	163-166	ectonucleoside triphosphate diphosphohydrolase 2	Mus musculus	55-61
12417608-3	2002	Our previous studies have implicated CD39/NTPDase1 and CD39L1/NTPDase2, members of the ectonucleoside triphosphate diphosphohydrolase (E-NTPDase) family, as major ATP-hydrolyzing enzymes in the tissues lining the cochlear endolymphatic and perilymphatic compartments.	Adenosine Triphosphate	163-166	ectonucleoside triphosphate diphosphohydrolase 2	Mus musculus	62-70
32473244-7	2020	In silico analysis showed that the ectonucleotidases were modulated after induction of conditions that can lead to vascular diseases such as, hypertensive and hypotensive mice models (Nt5e); exposition to high-fat (Entpd1 and Entpd2) or high-phosphate (Nt5e) diet; mechanical stretch (Entpd1, Entpd2 and Nt5e); and myocardial infarction (Entpd1).	Phosphates	242-251	ectonucleoside triphosphate diphosphohydrolase 2	Mus musculus	293-299
11929769-4	2002	In contrast, we now show that NTPDase2 (CD39L1, 75 kd), a preferential nucleoside triphosphatase, activates platelet aggregation by converting adenosine triphosphate (ATP) to ADP, the specific agonist of P2Y(1) and P2Y(12) receptors.	Adenosine Triphosphate	143-165	ectonucleoside triphosphate diphosphohydrolase 2	Mus musculus	30-38
11929769-4	2002	In contrast, we now show that NTPDase2 (CD39L1, 75 kd), a preferential nucleoside triphosphatase, activates platelet aggregation by converting adenosine triphosphate (ATP) to ADP, the specific agonist of P2Y(1) and P2Y(12) receptors.	Adenosine Triphosphate	143-165	ectonucleoside triphosphate diphosphohydrolase 2	Mus musculus	40-46
11929769-4	2002	In contrast, we now show that NTPDase2 (CD39L1, 75 kd), a preferential nucleoside triphosphatase, activates platelet aggregation by converting adenosine triphosphate (ATP) to ADP, the specific agonist of P2Y(1) and P2Y(12) receptors.	Adenosine Triphosphate	167-170	ectonucleoside triphosphate diphosphohydrolase 2	Mus musculus	30-38
11929769-4	2002	In contrast, we now show that NTPDase2 (CD39L1, 75 kd), a preferential nucleoside triphosphatase, activates platelet aggregation by converting adenosine triphosphate (ATP) to ADP, the specific agonist of P2Y(1) and P2Y(12) receptors.	Adenosine Triphosphate	167-170	ectonucleoside triphosphate diphosphohydrolase 2	Mus musculus	40-46
11929769-4	2002	In contrast, we now show that NTPDase2 (CD39L1, 75 kd), a preferential nucleoside triphosphatase, activates platelet aggregation by converting adenosine triphosphate (ATP) to ADP, the specific agonist of P2Y(1) and P2Y(12) receptors.	Adenosine Diphosphate	175-178	ectonucleoside triphosphate diphosphohydrolase 2	Mus musculus	30-38
11929769-4	2002	In contrast, we now show that NTPDase2 (CD39L1, 75 kd), a preferential nucleoside triphosphatase, activates platelet aggregation by converting adenosine triphosphate (ATP) to ADP, the specific agonist of P2Y(1) and P2Y(12) receptors.	Adenosine Diphosphate	175-178	ectonucleoside triphosphate diphosphohydrolase 2	Mus musculus	40-46
31188623-12	2019	Here, we used Entpd1- and Entpd2-deficient mice to show that the differential and cell-selective regulation of purine hydrolysis by NTPDase1 and -2 plays important roles in barrier function, gut motility, and neuromuscular communication in health and disease.	purine	111-117	ectonucleoside triphosphate diphosphohydrolase 2	Mus musculus	26-32
32825435-0	2020	Ecto-Nucleotide Triphosphate Diphosphohydrolase-2 (NTPDase2) Deletion Increases Acetaminophen-Induced Hepatotoxicity.	Acetaminophen	80-93	ectonucleoside triphosphate diphosphohydrolase 2	Mus musculus	51-59
32825435-1	2020	Ecto-nucleotidase triphosphate diphosphohydrolase-2 (NTPDase2) is an ecto-enzyme that is expressed on portal fibroblasts in the liver that modulates P2 receptor signaling by regulating local concentrations of extracellular ATP and ADP.	Adenosine Triphosphate	223-226	ectonucleoside triphosphate diphosphohydrolase 2	Mus musculus	0-51
32825435-1	2020	Ecto-nucleotidase triphosphate diphosphohydrolase-2 (NTPDase2) is an ecto-enzyme that is expressed on portal fibroblasts in the liver that modulates P2 receptor signaling by regulating local concentrations of extracellular ATP and ADP.	Adenosine Triphosphate	223-226	ectonucleoside triphosphate diphosphohydrolase 2	Mus musculus	53-61
32825435-1	2020	Ecto-nucleotidase triphosphate diphosphohydrolase-2 (NTPDase2) is an ecto-enzyme that is expressed on portal fibroblasts in the liver that modulates P2 receptor signaling by regulating local concentrations of extracellular ATP and ADP.	Adenosine Diphosphate	231-234	ectonucleoside triphosphate diphosphohydrolase 2	Mus musculus	0-51
32825435-1	2020	Ecto-nucleotidase triphosphate diphosphohydrolase-2 (NTPDase2) is an ecto-enzyme that is expressed on portal fibroblasts in the liver that modulates P2 receptor signaling by regulating local concentrations of extracellular ATP and ADP.	Adenosine Diphosphate	231-234	ectonucleoside triphosphate diphosphohydrolase 2	Mus musculus	53-61
32825435-7	2020	We found that Entpd2 expression is significantly upregulated after acetaminophen-induced hepatotoxicity.	Acetaminophen	67-80	ectonucleoside triphosphate diphosphohydrolase 2	Mus musculus	14-20
32473244-7	2020	In silico analysis showed that the ectonucleotidases were modulated after induction of conditions that can lead to vascular diseases such as, hypertensive and hypotensive mice models (Nt5e); exposition to high-fat (Entpd1 and Entpd2) or high-phosphate (Nt5e) diet; mechanical stretch (Entpd1, Entpd2 and Nt5e); and myocardial infarction (Entpd1).	Phosphates	242-251	ectonucleoside triphosphate diphosphohydrolase 2	Mus musculus	226-232
30319684-10	2018	Thirty high priority candidate genes, including Entpd2, Per3, and Fto were nominated for early and sustained alcohol intake QTLs.	Alcohols	109-116	ectonucleoside triphosphate diphosphohydrolase 2	Mus musculus	48-54
30891559-4	2018	Methods: We employed a system using doxycycline to conditionally ablate NTPDase2+ cells in lingual epithelia and papillae by regulated expression of the diphtheria toxin A (DTA) gene.	Doxycycline	36-47	ectonucleoside triphosphate diphosphohydrolase 2	Mus musculus	72-80
30891559-9	2018	Results: After 15 days of Dox induction, the expression of NTPDase2, Sox2 and K14 was ablated from lingual epithelia.	Doxycycline	26-29	ectonucleoside triphosphate diphosphohydrolase 2	Mus musculus	59-67
26924460-9	2016	The endothelial expressions of NTPDases 2 and 3 were significantly increased in the infected group, increasing extracellular ATP hydrolysis and ADP formation by endothelial cells.	Adenosine Triphosphate	125-128	ectonucleoside triphosphate diphosphohydrolase 2	Mus musculus	31-47
28472257-8	2017	When compared with wild type, DSS-induced colitis was exacerbated in Entpd2, and to a lesser extent, Entpd3 null mice as measured by disease activity score and histology, and marked anaemia was seen in both.	dss	30-33	ectonucleoside triphosphate diphosphohydrolase 2	Mus musculus	69-75
26924460-9	2016	The endothelial expressions of NTPDases 2 and 3 were significantly increased in the infected group, increasing extracellular ATP hydrolysis and ADP formation by endothelial cells.	Adenosine Diphosphate	144-147	ectonucleoside triphosphate diphosphohydrolase 2	Mus musculus	31-47
26924460-10	2016	Therefore, mesenteric endothelial cells are primed by schistosomiasis to a pro-inflammatory phenotype characterized by an increased expression of NTPDases 2 and 3, favoring ADP accumulation and mononuclear cell adhesion, possibly contributing to mesenteric inflammation and schistosomiasis morbidity.	Adenosine Diphosphate	173-176	ectonucleoside triphosphate diphosphohydrolase 2	Mus musculus	146-162