PMID-sentid	Pub_year	Sent_text	comp_official_name	comp_offset	protein_name	organism	prot_offset
26639824-8	2016	Adelmidrol modulated the expression of PEA biosynthetic enzyme, NAPE-PLD, in HaCaT cells, and inhibited the release of the pro-inflammatory chemokine MCP-2 from stimulated HaCaT cells.	adelmidrol	0-10	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	64-72
26585314-5	2016	These substances are released from the membrane precursor, N-acylphosphatidylethanolamine (NAPE), by the action of a NAPE-specific phospholipase D (NAPE-PLD), and in macrophage are primarily deactivated by the lysosomal cysteine amidase, N-acylethanolamine acid amidase (NAAA).	N-acylphosphatidylethanolamine	59-89	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	117-146
26585314-5	2016	These substances are released from the membrane precursor, N-acylphosphatidylethanolamine (NAPE), by the action of a NAPE-specific phospholipase D (NAPE-PLD), and in macrophage are primarily deactivated by the lysosomal cysteine amidase, N-acylethanolamine acid amidase (NAAA).	N-acylphosphatidylethanolamine	59-89	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	148-156
27245898-1	2016	N-acyl-phosphatidylethanolamine (NAPE)-hydrolyzing phospholipase D (NAPE-PLD) is a prominent enzyme involved in the biosynthesis of fatty acid amides (FAAs), a family of bioactive lipids including anandamide (AEA) as the prototypical member.	fatty acid amides	132-149	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	0-66
27245898-1	2016	N-acyl-phosphatidylethanolamine (NAPE)-hydrolyzing phospholipase D (NAPE-PLD) is a prominent enzyme involved in the biosynthesis of fatty acid amides (FAAs), a family of bioactive lipids including anandamide (AEA) as the prototypical member.	fatty acid amides	132-149	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	68-76
27245898-1	2016	N-acyl-phosphatidylethanolamine (NAPE)-hydrolyzing phospholipase D (NAPE-PLD) is a prominent enzyme involved in the biosynthesis of fatty acid amides (FAAs), a family of bioactive lipids including anandamide (AEA) as the prototypical member.	faas	151-155	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	0-66
27245898-1	2016	N-acyl-phosphatidylethanolamine (NAPE)-hydrolyzing phospholipase D (NAPE-PLD) is a prominent enzyme involved in the biosynthesis of fatty acid amides (FAAs), a family of bioactive lipids including anandamide (AEA) as the prototypical member.	faas	151-155	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	68-76
27245898-1	2016	N-acyl-phosphatidylethanolamine (NAPE)-hydrolyzing phospholipase D (NAPE-PLD) is a prominent enzyme involved in the biosynthesis of fatty acid amides (FAAs), a family of bioactive lipids including anandamide (AEA) as the prototypical member.	anandamide	197-207	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	0-66
27245898-1	2016	N-acyl-phosphatidylethanolamine (NAPE)-hydrolyzing phospholipase D (NAPE-PLD) is a prominent enzyme involved in the biosynthesis of fatty acid amides (FAAs), a family of bioactive lipids including anandamide (AEA) as the prototypical member.	anandamide	197-207	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	68-76
27245898-1	2016	N-acyl-phosphatidylethanolamine (NAPE)-hydrolyzing phospholipase D (NAPE-PLD) is a prominent enzyme involved in the biosynthesis of fatty acid amides (FAAs), a family of bioactive lipids including anandamide (AEA) as the prototypical member.	anandamide	209-212	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	0-66
27245898-1	2016	N-acyl-phosphatidylethanolamine (NAPE)-hydrolyzing phospholipase D (NAPE-PLD) is a prominent enzyme involved in the biosynthesis of fatty acid amides (FAAs), a family of bioactive lipids including anandamide (AEA) as the prototypical member.	anandamide	209-212	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	68-76
25975960-5	2015	Levels of two enzymes participating in the biosynthesis and degradation of AEA, N-acyl-phosphatidylethanolamine-hydrolyzing phospholipase D (NPLD) and fatty acid amide hydrolase (FAAH), together with the most abundant ceramide synthases (CerS1, CerS2, CerS5 and CerS6) in the colon were also determined.	aea	75-78	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	80-139
24423290-9	2014	Changes in the immunohistochemical densities of the AEA modifying enzymes N-acylphophatidylethanolamine-phospholipase D (NAPE-PLD) and FAAH, and the cannabinoid receptors (CB1 and CB2) were observed with increased NAPE-PLD, FAAH, and CB1 expression seen in the trophoblast of MTOP patients.	anandamide	52-55	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	74-119
25684574-0	2015	Structure of human N-acylphosphatidylethanolamine-hydrolyzing phospholipase D: regulation of fatty acid ethanolamide biosynthesis by bile acids.	Fatty Acids	93-103	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	19-77
25684574-0	2015	Structure of human N-acylphosphatidylethanolamine-hydrolyzing phospholipase D: regulation of fatty acid ethanolamide biosynthesis by bile acids.	ethanolamide	104-116	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	19-77
25684574-0	2015	Structure of human N-acylphosphatidylethanolamine-hydrolyzing phospholipase D: regulation of fatty acid ethanolamide biosynthesis by bile acids.	Bile Acids and Salts	133-143	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	19-77
25684574-4	2015	NAPE-PLD forms homodimers partly separated by an internal ~ 9-A-wide channel and uniquely adapted to associate with phospholipids.	Phospholipids	116-129	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	0-8
24952959-2	2014	PEA is synthetized from phospholipids through the sequential actions of N-acyltransferase and N-acylphosphatidylethanolamine-preferring phospholipase D (NAPE-PLD), and its actions are terminated by its hydrolysis by two enzymes, fatty acid amide hydrolase (FAAH) and N-acylethanolamine-hydrolysing acid amidase (NAAA).	Phospholipids	24-37	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	94-151
24952959-2	2014	PEA is synthetized from phospholipids through the sequential actions of N-acyltransferase and N-acylphosphatidylethanolamine-preferring phospholipase D (NAPE-PLD), and its actions are terminated by its hydrolysis by two enzymes, fatty acid amide hydrolase (FAAH) and N-acylethanolamine-hydrolysing acid amidase (NAAA).	Phospholipids	24-37	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	153-161
25384256-5	2015	By targeted screening of a library of SERM analogues, additional parallel synthesis, and evaluation in multiple PLD assays, we discovered a novel desketoraloxifene-based scaffold that inhibited not only the two mammalian PLDs but also structurally divergent PldA and NAPE-PLD.	Desketoraloxifene	146-163	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	267-275
24747663-5	2014	The first step is N-acylation of ethanolamine phospholipids catalyzed by Ca(2+)-dependent N-acyltransferase and the second step is the release of NAEs from N-acylated ethanolamine phospholipids by N-acylphosphatidylethanolamine (NAPE)-hydrolyzing phospholipase D (NAPE-PLD).	ethanolamine phospholipids	33-59	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	197-262
24747663-5	2014	The first step is N-acylation of ethanolamine phospholipids catalyzed by Ca(2+)-dependent N-acyltransferase and the second step is the release of NAEs from N-acylated ethanolamine phospholipids by N-acylphosphatidylethanolamine (NAPE)-hydrolyzing phospholipase D (NAPE-PLD).	ethanolamine phospholipids	33-59	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	264-272
24747663-5	2014	The first step is N-acylation of ethanolamine phospholipids catalyzed by Ca(2+)-dependent N-acyltransferase and the second step is the release of NAEs from N-acylated ethanolamine phospholipids by N-acylphosphatidylethanolamine (NAPE)-hydrolyzing phospholipase D (NAPE-PLD).	N-acylethanolamines	146-150	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	197-262
24747663-5	2014	The first step is N-acylation of ethanolamine phospholipids catalyzed by Ca(2+)-dependent N-acyltransferase and the second step is the release of NAEs from N-acylated ethanolamine phospholipids by N-acylphosphatidylethanolamine (NAPE)-hydrolyzing phospholipase D (NAPE-PLD).	N-acylethanolamines	146-150	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	264-272
24747663-5	2014	The first step is N-acylation of ethanolamine phospholipids catalyzed by Ca(2+)-dependent N-acyltransferase and the second step is the release of NAEs from N-acylated ethanolamine phospholipids by N-acylphosphatidylethanolamine (NAPE)-hydrolyzing phospholipase D (NAPE-PLD).	ethanolamine phospholipids	167-193	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	197-262
24747663-5	2014	The first step is N-acylation of ethanolamine phospholipids catalyzed by Ca(2+)-dependent N-acyltransferase and the second step is the release of NAEs from N-acylated ethanolamine phospholipids by N-acylphosphatidylethanolamine (NAPE)-hydrolyzing phospholipase D (NAPE-PLD).	ethanolamine phospholipids	167-193	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	264-272
24423290-9	2014	Changes in the immunohistochemical densities of the AEA modifying enzymes N-acylphophatidylethanolamine-phospholipase D (NAPE-PLD) and FAAH, and the cannabinoid receptors (CB1 and CB2) were observed with increased NAPE-PLD, FAAH, and CB1 expression seen in the trophoblast of MTOP patients.	anandamide	52-55	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	121-129
24423290-10	2014	CONCLUSIONS: Trophoblast after MTOP demonstrated high AEA concentrations with increased expression of NAPE-PLD, FAAH, and CB1.	5-((5-Methyl-3-thienyl)oxy)-2(1H)-pyrimidinone	31-35	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	102-110
24018423-0	2013	Isolevuglandin-modified phosphatidylethanolamine is metabolized by NAPE-hydrolyzing phospholipase D.	isolevuglandin	0-14	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	67-99
24018423-0	2013	Isolevuglandin-modified phosphatidylethanolamine is metabolized by NAPE-hydrolyzing phospholipase D.	phosphatidylethanolamine	24-48	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	67-99
24018423-8	2013	LC-MS/MS analysis confirmed that recombinant NAPE-PLD hydrolyzed IsoLG-PE to IsoLG-ethanolamine.	isolg-pe	65-73	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	45-53
24018423-8	2013	LC-MS/MS analysis confirmed that recombinant NAPE-PLD hydrolyzed IsoLG-PE to IsoLG-ethanolamine.	isolg-ethanolamine	77-95	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	45-53
24018423-5	2013	Because N-acyl phosphatidylethanolamine-hydrolyzing phospholipase D (NAPE-PLD) has been described as a key enzyme in the hydrolysis of N-acyl phosphatidylethanoamine (NAPE) and both NAPE and IsoLG-PE have large aliphatic headgroups, we considered the possibility that this enzyme might also hydrolyze IsoLG-PE.	n-acyl phosphatidylethanoamine	135-165	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	8-67
24018423-9	2013	These results demonstrate that NAPE-PLD contributes to the degradation of IsoLG-PE and suggest that a major physiological role of NAPE-PLD may be to degrade aldehyde-modified PE, thereby preventing the accumulation of these harmful compounds.	Aldehydes	157-165	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	31-39
24018423-5	2013	Because N-acyl phosphatidylethanolamine-hydrolyzing phospholipase D (NAPE-PLD) has been described as a key enzyme in the hydrolysis of N-acyl phosphatidylethanoamine (NAPE) and both NAPE and IsoLG-PE have large aliphatic headgroups, we considered the possibility that this enzyme might also hydrolyze IsoLG-PE.	n-acyl phosphatidylethanoamine	135-165	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	69-77
24018423-9	2013	These results demonstrate that NAPE-PLD contributes to the degradation of IsoLG-PE and suggest that a major physiological role of NAPE-PLD may be to degrade aldehyde-modified PE, thereby preventing the accumulation of these harmful compounds.	Aldehydes	157-165	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	130-138
23425575-3	2013	In the known metabolic pathway in mammals, anandamide and other bioactive N-acylethanolamines, such as palmitoylethanolamide and oleoylethanolamide, are biosynthesized from glycerophospholipids by a combination of Ca(2+)-dependent N-acyltransferase and N-acyl-phosphatidylethanolamine-hydrolyzing phospholipase D, and are degraded by fatty acid amide hydrolase.	anandamide	43-53	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	253-312
23697839-4	2013	Local AEA levels are regulated by the synthetic and degradative enzymes, NAPE-PLD and FAAH, respectively.	anandamide	6-9	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	73-81
23425575-3	2013	In the known metabolic pathway in mammals, anandamide and other bioactive N-acylethanolamines, such as palmitoylethanolamide and oleoylethanolamide, are biosynthesized from glycerophospholipids by a combination of Ca(2+)-dependent N-acyltransferase and N-acyl-phosphatidylethanolamine-hydrolyzing phospholipase D, and are degraded by fatty acid amide hydrolase.	N-acylethanolamines	74-93	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	253-312
23425575-3	2013	In the known metabolic pathway in mammals, anandamide and other bioactive N-acylethanolamines, such as palmitoylethanolamide and oleoylethanolamide, are biosynthesized from glycerophospholipids by a combination of Ca(2+)-dependent N-acyltransferase and N-acyl-phosphatidylethanolamine-hydrolyzing phospholipase D, and are degraded by fatty acid amide hydrolase.	Glycerophospholipids	173-193	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	253-312
23425575-3	2013	In the known metabolic pathway in mammals, anandamide and other bioactive N-acylethanolamines, such as palmitoylethanolamide and oleoylethanolamide, are biosynthesized from glycerophospholipids by a combination of Ca(2+)-dependent N-acyltransferase and N-acyl-phosphatidylethanolamine-hydrolyzing phospholipase D, and are degraded by fatty acid amide hydrolase.	palmidrol	103-124	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	253-312
23425575-3	2013	In the known metabolic pathway in mammals, anandamide and other bioactive N-acylethanolamines, such as palmitoylethanolamide and oleoylethanolamide, are biosynthesized from glycerophospholipids by a combination of Ca(2+)-dependent N-acyltransferase and N-acyl-phosphatidylethanolamine-hydrolyzing phospholipase D, and are degraded by fatty acid amide hydrolase.	oleoylethanolamide	129-147	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	253-312
22669247-4	2012	The possible endogenous production of the eCB, anandamide (AEA), was investigated in testis by analyzing the expression of its biosynthetic enzyme, Nape-pld.	Endocannabinoids	42-45	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	148-156
22825852-8	2012	Third, when NAPE-hydrolyzing phospholipase D was additionally expressed in PLA/AT-2-expressing cells, accumulating NAPE was efficiently converted to NAE.	N-acylethanolamines	149-152	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	12-44
22669247-4	2012	The possible endogenous production of the eCB, anandamide (AEA), was investigated in testis by analyzing the expression of its biosynthetic enzyme, Nape-pld.	anandamide	47-57	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	148-156
22669247-4	2012	The possible endogenous production of the eCB, anandamide (AEA), was investigated in testis by analyzing the expression of its biosynthetic enzyme, Nape-pld.	anandamide	59-62	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	148-156
20152858-3	2010	In mammalian tissues, NAEs are formed from glycerophospholipids through the phosphodiesterase-transacylation pathway consisting of Ca(2+)-dependent N-acyltransferase and N-acylphosphatidylethanolamine-hydrolyzing phospholipase D.	N-acylethanolamines	22-26	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	170-228
22827915-3	2012	We used microarray with qPCR validation and in situ hybridisation to quantify mRNA for the central endocannabinoid receptor CB(1)R, endocannabinoid synthetic enzymes (DAGLalpha for 2-arachidonylglycerol [2-AG] and NAPE-PLD for anandamide), and inactivating enzymes (MGL and ABHD6 for 2-AG and FAAH for anandamide) in human dorsolateral prefrontal cortex (39 days - 49 years).	glyceryl 2-arachidonate	181-202	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	214-222
22827915-9	2012	After adolescence, higher mRNA levels of the anandamide synthetic and inactivating enzymes NAPE-PLD and FAAH suggest that a late developmental switch may occur where anandamide is more strongly regulated after adolescence than earlier in life.	anandamide	45-55	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	91-99
22827915-9	2012	After adolescence, higher mRNA levels of the anandamide synthetic and inactivating enzymes NAPE-PLD and FAAH suggest that a late developmental switch may occur where anandamide is more strongly regulated after adolescence than earlier in life.	anandamide	166-176	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	91-99
22176552-4	2012	We also measured the expressions and activities of the enzymes responsible for anandamide and 2-AG biosynthesis and degradation, that is, N-acylphosphatidylethanolamine-hydrolysing phospholipase D (NAPE-PLD), fatty acid amide hydrolase (FAAH), monoacylglycerol lipase (MGL), and diacylglycerol lipase-alpha (DGL), in the same samples.	anandamide	79-89	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	138-196
22176552-4	2012	We also measured the expressions and activities of the enzymes responsible for anandamide and 2-AG biosynthesis and degradation, that is, N-acylphosphatidylethanolamine-hydrolysing phospholipase D (NAPE-PLD), fatty acid amide hydrolase (FAAH), monoacylglycerol lipase (MGL), and diacylglycerol lipase-alpha (DGL), in the same samples.	anandamide	79-89	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	198-206
22176552-4	2012	We also measured the expressions and activities of the enzymes responsible for anandamide and 2-AG biosynthesis and degradation, that is, N-acylphosphatidylethanolamine-hydrolysing phospholipase D (NAPE-PLD), fatty acid amide hydrolase (FAAH), monoacylglycerol lipase (MGL), and diacylglycerol lipase-alpha (DGL), in the same samples.	glyceryl 2-arachidonate	94-98	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	138-196
22176552-4	2012	We also measured the expressions and activities of the enzymes responsible for anandamide and 2-AG biosynthesis and degradation, that is, N-acylphosphatidylethanolamine-hydrolysing phospholipase D (NAPE-PLD), fatty acid amide hydrolase (FAAH), monoacylglycerol lipase (MGL), and diacylglycerol lipase-alpha (DGL), in the same samples.	glyceryl 2-arachidonate	94-98	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	198-206
20152858-3	2010	In mammalian tissues, NAEs are formed from glycerophospholipids through the phosphodiesterase-transacylation pathway consisting of Ca(2+)-dependent N-acyltransferase and N-acylphosphatidylethanolamine-hydrolyzing phospholipase D.	Glycerophospholipids	43-63	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	170-228
19419760-2	2009	AEA synthesized by multiple pathways, including NAPE-specific phospholipase D (NAPE-PLD) and degraded by the fatty acid amide hydrolase (FAAH).	anandamide	0-3	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	48-77
19715685-2	2009	These lipids are formed from their respective N-acylated ethanolamine phospholipid (NAPE) precursor by the action of a phospholipase D enzyme (NAPE-PLD).	n-acylated ethanolamine phospholipid	46-82	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	143-151
19715685-7	2009	Furthermore, it was found that NAPE-PLD was activated by phosphatidylethanolamine and inhibited by the beta-lactamase substrate nitrocefin.	phosphatidylethanolamine	57-81	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	31-39
19715685-7	2009	Furthermore, it was found that NAPE-PLD was activated by phosphatidylethanolamine and inhibited by the beta-lactamase substrate nitrocefin.	nitrocefin	128-138	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	31-39
20369362-2	2010	Plasma AEA levels are maintained by the actions of the enzymes fatty acid amide hydrolase (FAAH) and N-acylphosphatidylethanolamine-phospholipase D (NAPE-PLD).	anandamide	7-10	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	101-147
20369362-2	2010	Plasma AEA levels are maintained by the actions of the enzymes fatty acid amide hydrolase (FAAH) and N-acylphosphatidylethanolamine-phospholipase D (NAPE-PLD).	anandamide	7-10	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	149-157
20096328-4	2010	Here, we extended the study of the effect of 15-HAEA on the AEA synthetase (NAPE-PLD) and the AEA-binding vanilloid receptor (TRPV1), showing that 15-HAEA activates the former (up to approximately 140% of controls) and inhibits the latter protein (down to approximately 70%).	15-hydroxyanandamide	45-52	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	76-84
20096328-4	2010	Here, we extended the study of the effect of 15-HAEA on the AEA synthetase (NAPE-PLD) and the AEA-binding vanilloid receptor (TRPV1), showing that 15-HAEA activates the former (up to approximately 140% of controls) and inhibits the latter protein (down to approximately 70%).	15-hydroxyanandamide	147-154	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	76-84
19608651-3	2009	Protein expression was revealed for CB1 ( approximately 56 kDa), TRPV1 ( approximately 95 kDa), AEA-synthesizing phospholipase D (NAPE-PLD) ( approximately 46 kDa), and AEA-hydrolyzing enzyme [fatty acid amide hydrolase (FAAH), approximately 66 kDa].	anandamide	96-99	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	130-138
19419760-2	2009	AEA synthesized by multiple pathways, including NAPE-specific phospholipase D (NAPE-PLD) and degraded by the fatty acid amide hydrolase (FAAH).	anandamide	0-3	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	79-87
18806270-5	2008	FAAH and the NAE-forming enzyme N-acylphosphatidylethanolamine-hydrolysing phospholipase D (NAPE-PLD) were also detected in these cells.	N-acylphosphatidylethanolamine	32-62	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	92-100
16515464-6	2006	Recently, the N-acylphosphatidylethanolamine-specific phospholipase D (NAPE-PLD), which synthesizes AEA from N-arachidonoylphosphatidylethanolamine (NArPE), and the diacylglycerol lipase (DAGL), which generates 2-AG from diacylglycerol (DAG) substrates, have been characterized.	anandamide	100-103	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	71-79
18234884-6	2008	In contrast to its predicted role in retrograde signaling, here we show that N-acylphosphatidylethanolamine-hydrolyzing phospholipase D (NAPE-PLD), a biosynthetic enzyme of anandamide and its related bioactive congeners, the N-acylethanolamines (NAEs), is concentrated presynaptically in several types of hippocampal excitatory axon terminals.	anandamide	173-183	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	77-135
18234884-6	2008	In contrast to its predicted role in retrograde signaling, here we show that N-acylphosphatidylethanolamine-hydrolyzing phospholipase D (NAPE-PLD), a biosynthetic enzyme of anandamide and its related bioactive congeners, the N-acylethanolamines (NAEs), is concentrated presynaptically in several types of hippocampal excitatory axon terminals.	anandamide	173-183	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	137-145
18234884-6	2008	In contrast to its predicted role in retrograde signaling, here we show that N-acylphosphatidylethanolamine-hydrolyzing phospholipase D (NAPE-PLD), a biosynthetic enzyme of anandamide and its related bioactive congeners, the N-acylethanolamines (NAEs), is concentrated presynaptically in several types of hippocampal excitatory axon terminals.	N-acylethanolamines	225-244	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	77-135
18234884-6	2008	In contrast to its predicted role in retrograde signaling, here we show that N-acylphosphatidylethanolamine-hydrolyzing phospholipase D (NAPE-PLD), a biosynthetic enzyme of anandamide and its related bioactive congeners, the N-acylethanolamines (NAEs), is concentrated presynaptically in several types of hippocampal excitatory axon terminals.	N-acylethanolamines	225-244	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	137-145
18234884-6	2008	In contrast to its predicted role in retrograde signaling, here we show that N-acylphosphatidylethanolamine-hydrolyzing phospholipase D (NAPE-PLD), a biosynthetic enzyme of anandamide and its related bioactive congeners, the N-acylethanolamines (NAEs), is concentrated presynaptically in several types of hippocampal excitatory axon terminals.	N-acylethanolamines	246-250	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	77-135
18234884-6	2008	In contrast to its predicted role in retrograde signaling, here we show that N-acylphosphatidylethanolamine-hydrolyzing phospholipase D (NAPE-PLD), a biosynthetic enzyme of anandamide and its related bioactive congeners, the N-acylethanolamines (NAEs), is concentrated presynaptically in several types of hippocampal excitatory axon terminals.	N-acylethanolamines	246-250	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	137-145
17346227-2	2007	The in vivo biosynthesis of AEA has been shown to occur through several pathways mediated by N-acylphosphatidylethanolamide-phospholipase D (NAPE-PLD), a secretory PLA(2) and PLC.	anandamide	28-31	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	93-139
17346227-2	2007	The in vivo biosynthesis of AEA has been shown to occur through several pathways mediated by N-acylphosphatidylethanolamide-phospholipase D (NAPE-PLD), a secretory PLA(2) and PLC.	anandamide	28-31	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	141-149
16515464-6	2006	Recently, the N-acylphosphatidylethanolamine-specific phospholipase D (NAPE-PLD), which synthesizes AEA from N-arachidonoylphosphatidylethanolamine (NArPE), and the diacylglycerol lipase (DAGL), which generates 2-AG from diacylglycerol (DAG) substrates, have been characterized.	anandamide	100-103	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	14-69
17965731-6	2008	KEY RESULTS: Under basal conditions, the endogenous cannabinoid AEA was present in both lipid raft and specific non-lipid raft fractions as was one of its biosynthetic enzymes, NAPE-PLD.	Cannabinoids	52-63	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	177-185
17965731-6	2008	KEY RESULTS: Under basal conditions, the endogenous cannabinoid AEA was present in both lipid raft and specific non-lipid raft fractions as was one of its biosynthetic enzymes, NAPE-PLD.	aea	64-67	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	177-185
16515464-6	2006	Recently, the N-acylphosphatidylethanolamine-specific phospholipase D (NAPE-PLD), which synthesizes AEA from N-arachidonoylphosphatidylethanolamine (NArPE), and the diacylglycerol lipase (DAGL), which generates 2-AG from diacylglycerol (DAG) substrates, have been characterized.	N-arachidonylphosphatidylethanolamine	149-154	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	14-69
16515464-6	2006	Recently, the N-acylphosphatidylethanolamine-specific phospholipase D (NAPE-PLD), which synthesizes AEA from N-arachidonoylphosphatidylethanolamine (NArPE), and the diacylglycerol lipase (DAGL), which generates 2-AG from diacylglycerol (DAG) substrates, have been characterized.	N-arachidonylphosphatidylethanolamine	149-154	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	71-79
16515464-6	2006	Recently, the N-acylphosphatidylethanolamine-specific phospholipase D (NAPE-PLD), which synthesizes AEA from N-arachidonoylphosphatidylethanolamine (NArPE), and the diacylglycerol lipase (DAGL), which generates 2-AG from diacylglycerol (DAG) substrates, have been characterized.	glyceryl 2-arachidonate	211-215	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	14-69
16515464-6	2006	Recently, the N-acylphosphatidylethanolamine-specific phospholipase D (NAPE-PLD), which synthesizes AEA from N-arachidonoylphosphatidylethanolamine (NArPE), and the diacylglycerol lipase (DAGL), which generates 2-AG from diacylglycerol (DAG) substrates, have been characterized.	glyceryl 2-arachidonate	211-215	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	71-79
16515464-6	2006	Recently, the N-acylphosphatidylethanolamine-specific phospholipase D (NAPE-PLD), which synthesizes AEA from N-arachidonoylphosphatidylethanolamine (NArPE), and the diacylglycerol lipase (DAGL), which generates 2-AG from diacylglycerol (DAG) substrates, have been characterized.	Diglycerides	165-179	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	71-79
16515464-6	2006	Recently, the N-acylphosphatidylethanolamine-specific phospholipase D (NAPE-PLD), which synthesizes AEA from N-arachidonoylphosphatidylethanolamine (NArPE), and the diacylglycerol lipase (DAGL), which generates 2-AG from diacylglycerol (DAG) substrates, have been characterized.	Diglycerides	188-191	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	14-69
16515464-6	2006	Recently, the N-acylphosphatidylethanolamine-specific phospholipase D (NAPE-PLD), which synthesizes AEA from N-arachidonoylphosphatidylethanolamine (NArPE), and the diacylglycerol lipase (DAGL), which generates 2-AG from diacylglycerol (DAG) substrates, have been characterized.	Diglycerides	188-191	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	71-79
15890658-0	2005	N-acylphosphatidylethanolamine-hydrolyzing phospholipase D is an important determinant of uterine anandamide levels during implantation.	anandamide	98-108	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	0-58
15760304-1	2005	In animal tissues, NAEs (N-acylethanolamines), including N-arachidonoylethanolamine (anandamide), are primarily formed from their corresponding NAPEs (N-acylphosphatidylethanolamines) by a phosphodiesterase of the PLD (phospholipase D) type (NAPE-PLD).	aea	57-83	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	242-250
15760304-1	2005	In animal tissues, NAEs (N-acylethanolamines), including N-arachidonoylethanolamine (anandamide), are primarily formed from their corresponding NAPEs (N-acylphosphatidylethanolamines) by a phosphodiesterase of the PLD (phospholipase D) type (NAPE-PLD).	anandamide	85-95	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	242-250
15760304-7	2005	The overexpression of NAPE-PLD caused a decrease in the total amount of NAPEs by 50-90% with a 1.5-fold increase in the total amount of NAEs, suggesting that the recombinant NAPE-PLD utilizes endogenous NAPE as a substrate in the cell.	N-acylphosphatidylethanolamine	72-77	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	22-30
15760304-7	2005	The overexpression of NAPE-PLD caused a decrease in the total amount of NAPEs by 50-90% with a 1.5-fold increase in the total amount of NAEs, suggesting that the recombinant NAPE-PLD utilizes endogenous NAPE as a substrate in the cell.	N-acylphosphatidylethanolamine	72-77	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	174-182
15760304-7	2005	The overexpression of NAPE-PLD caused a decrease in the total amount of NAPEs by 50-90% with a 1.5-fold increase in the total amount of NAEs, suggesting that the recombinant NAPE-PLD utilizes endogenous NAPE as a substrate in the cell.	N-acylethanolamines	136-140	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	22-30
15760304-7	2005	The overexpression of NAPE-PLD caused a decrease in the total amount of NAPEs by 50-90% with a 1.5-fold increase in the total amount of NAEs, suggesting that the recombinant NAPE-PLD utilizes endogenous NAPE as a substrate in the cell.	N-acylethanolamines	136-140	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	174-182
15760304-7	2005	The overexpression of NAPE-PLD caused a decrease in the total amount of NAPEs by 50-90% with a 1.5-fold increase in the total amount of NAEs, suggesting that the recombinant NAPE-PLD utilizes endogenous NAPE as a substrate in the cell.	N-acylphosphatidylethanolamine	22-26	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	174-182
15760304-9	2005	These results confirm that overexpressed NAPE-PLD is capable of forming NAEs, including anandamide, in living cells.	N-acylethanolamines	72-76	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	41-49
15760304-9	2005	These results confirm that overexpressed NAPE-PLD is capable of forming NAEs, including anandamide, in living cells.	anandamide	88-98	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	41-49
16144868-3	2005	In this study we report unprecedented evidence that boar sperm cells have the biochemical machinery to bind and degrade AEA, i.e. type-1 cannabinoid receptors (CB1R), vanilloid receptors (TRPV1), AEA-synthesizing phospholipase D (NAPE-PLD), AEA transporter (AMT) and AEA hydrolase (FAAH).	anandamide	120-123	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	230-238
15760304-1	2005	In animal tissues, NAEs (N-acylethanolamines), including N-arachidonoylethanolamine (anandamide), are primarily formed from their corresponding NAPEs (N-acylphosphatidylethanolamines) by a phosphodiesterase of the PLD (phospholipase D) type (NAPE-PLD).	N-acylethanolamines	19-23	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	242-250
15760304-1	2005	In animal tissues, NAEs (N-acylethanolamines), including N-arachidonoylethanolamine (anandamide), are primarily formed from their corresponding NAPEs (N-acylphosphatidylethanolamines) by a phosphodiesterase of the PLD (phospholipase D) type (NAPE-PLD).	N-acylethanolamines	25-44	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	242-250
15890658-5	2005	Using multiple approaches, we show here that uterine anandamide levels conducive to implantation are primarily regulated by spatiotemporal expression of Nape-Pld, the gene encoding N-acylphosphatidylethanolamine-hydrolyzing phospholipase D that generates anandamide.	anandamide	53-63	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	153-161
15890658-5	2005	Using multiple approaches, we show here that uterine anandamide levels conducive to implantation are primarily regulated by spatiotemporal expression of Nape-Pld, the gene encoding N-acylphosphatidylethanolamine-hydrolyzing phospholipase D that generates anandamide.	anandamide	53-63	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	181-239
15890658-5	2005	Using multiple approaches, we show here that uterine anandamide levels conducive to implantation are primarily regulated by spatiotemporal expression of Nape-Pld, the gene encoding N-acylphosphatidylethanolamine-hydrolyzing phospholipase D that generates anandamide.	anandamide	255-265	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	153-161
15890658-5	2005	Using multiple approaches, we show here that uterine anandamide levels conducive to implantation are primarily regulated by spatiotemporal expression of Nape-Pld, the gene encoding N-acylphosphatidylethanolamine-hydrolyzing phospholipase D that generates anandamide.	anandamide	255-265	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	181-239
15974992-8	2005	Considering cannabimimetic activities of anandamide, the enzymes involved in the biosynthesis and degradation of anandamide, including NAPE-PLD, may be promising targets for therapeutic agents.	anandamide	41-51	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	135-143
15974992-8	2005	Considering cannabimimetic activities of anandamide, the enzymes involved in the biosynthesis and degradation of anandamide, including NAPE-PLD, may be promising targets for therapeutic agents.	anandamide	113-123	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	135-143
30611738-12	2019	Colonic levels of N-acyl-phosphatidylethanolamine-specific phospholipase D (NAPE-PLD), which is responsible for synthesis of AEA, significantly declined after chronic treatment with 5-HT and this effect was reversed by the 5-HT3 and 5-HT4 receptor antagonists.	anandamide	125-128	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	18-74
12182959-5	2002	Formation of NAPE and NAE is catalyzed by an N-acyltransferase and an NAPE-hydrolyzing phospholipase D, respectively, two enzymes that have been characterized only preliminary.	N-acylethanolamines	22-25	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	70-102
11106787-1	2000	The present review focuses on the relationship between formation of N-acylethanolamine phospholipids (NAPEs) and N-acyletransferase (NAEs) catalyzed by N-acyltranferase and NAPE-hydrolyzing phospholipase D, respectively, and cell injury in tissues like brain, heart, and testis.	n-acylethanolamine phospholipids	68-100	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	173-205
11106787-1	2000	The present review focuses on the relationship between formation of N-acylethanolamine phospholipids (NAPEs) and N-acyletransferase (NAEs) catalyzed by N-acyltranferase and NAPE-hydrolyzing phospholipase D, respectively, and cell injury in tissues like brain, heart, and testis.	N-(4-aminophenethyl)spiroperidol	102-107	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	173-205
34843683-0	2022	Selective measurement of NAPE-PLD activity via a PLA1/2-resistant fluorogenic N-acyl-phosphatidylethanolamine analog.	N-acylphosphatidylethanolamine	78-109	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	25-33
34843683-1	2022	N-acyl-phosphatidylethanolamine (NAPE)-hydrolyzing phospholipase D (NAPE-PLD) is a zinc metallohydrolase enzyme that converts NAPEs to bioactive N-acyl-ethanolamides (NAEs).	n-acyl-ethanolamides	145-165	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	0-66
34843683-1	2022	N-acyl-phosphatidylethanolamine (NAPE)-hydrolyzing phospholipase D (NAPE-PLD) is a zinc metallohydrolase enzyme that converts NAPEs to bioactive N-acyl-ethanolamides (NAEs).	n-acyl-ethanolamides	145-165	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	68-76
34843683-1	2022	N-acyl-phosphatidylethanolamine (NAPE)-hydrolyzing phospholipase D (NAPE-PLD) is a zinc metallohydrolase enzyme that converts NAPEs to bioactive N-acyl-ethanolamides (NAEs).	naes	167-171	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	0-66
34843683-1	2022	N-acyl-phosphatidylethanolamine (NAPE)-hydrolyzing phospholipase D (NAPE-PLD) is a zinc metallohydrolase enzyme that converts NAPEs to bioactive N-acyl-ethanolamides (NAEs).	naes	167-171	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	68-76
34843683-5	2022	Recently, NAPE-PLD activity in cells has been assayed using the fluorogenic NAPE analogs PED-A1 and PED6, but these substrates also detect the activity of serine hydrolase-type lipases PLA1 and PLA2.	Serine	155-161	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	10-18
32954972-6	2022	These changes were accompanied by an increase in the expression of the genes for the cannabinoid receptor (Cnr1) and Nape-pld, an enzyme involved in endocannabinoid synthesis, in females and a decrease in the endocannabinoid degradation enzyme Faah in males.	Endocannabinoids	149-164	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	117-125
31921630-2	2019	It is widely accepted that plasma levels of these three NAEs are regulated by the actions of the rate-limiting enzymes N-acylphoshatidylethanolamine-specific phospholipase D (NAPE-PLD) and fatty acid amide hydrolase (FAAH), which are synthesizing and degradative, respectively.	N-acylethanolamines	56-60	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	119-173
31921630-2	2019	It is widely accepted that plasma levels of these three NAEs are regulated by the actions of the rate-limiting enzymes N-acylphoshatidylethanolamine-specific phospholipase D (NAPE-PLD) and fatty acid amide hydrolase (FAAH), which are synthesizing and degradative, respectively.	N-acylethanolamines	56-60	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	175-183
31921630-2	2019	It is widely accepted that plasma levels of these three NAEs are regulated by the actions of the rate-limiting enzymes N-acylphoshatidylethanolamine-specific phospholipase D (NAPE-PLD) and fatty acid amide hydrolase (FAAH), which are synthesizing and degradative, respectively.	Fatty Acids	189-205	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	119-173
31921630-6	2019	Concentrations of the three NAEs also measured in plasma and tissues were correlated with lymphocytic FAAH activity and the NAPE-PLD and FAAH transcript and protein levels.	N-acylethanolamines	28-32	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	124-132
31921630-10	2019	Correlation analyses also confirmed that tissue NAE concentrations were inversely related to FAAH expression and directly correlated to NAPE-PLD expression and the NAPE-PLD/FAAH ratio.	3,4-dihydro-N-isopropyl-3-(N-isopropyl-N-propylamino)-2H-1-benzopyran-5-carboxamide	48-51	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	136-144
31921630-10	2019	Correlation analyses also confirmed that tissue NAE concentrations were inversely related to FAAH expression and directly correlated to NAPE-PLD expression and the NAPE-PLD/FAAH ratio.	3,4-dihydro-N-isopropyl-3-(N-isopropyl-N-propylamino)-2H-1-benzopyran-5-carboxamide	48-51	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	164-172
31685899-6	2019	Furthermore, NAPE-PLD silencing protects cathecolamine-producing SH-SY5Y cells from 6-OHDA-induced reactive oxygen species formation, caspase-3 activation and death.	Oxidopamine	84-90	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	13-21
31685899-6	2019	Furthermore, NAPE-PLD silencing protects cathecolamine-producing SH-SY5Y cells from 6-OHDA-induced reactive oxygen species formation, caspase-3 activation and death.	Oxygen	108-114	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	13-21
30659320-5	2019	We demonstrate that THC (10-40 microM) impairs placental endocannabinoid system by disrupting the endocannabinoid anandamide (AEA) levels and the expression of AEA synthetic and degrading enzymes N-arachidonoylphosphatidylethanolamine-specific phospholipase D (NAPE-PLD) and fatty acid amide hydrolase (FAAH), respectively.	Dronabinol	20-23	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	196-259
30659320-5	2019	We demonstrate that THC (10-40 microM) impairs placental endocannabinoid system by disrupting the endocannabinoid anandamide (AEA) levels and the expression of AEA synthetic and degrading enzymes N-arachidonoylphosphatidylethanolamine-specific phospholipase D (NAPE-PLD) and fatty acid amide hydrolase (FAAH), respectively.	Dronabinol	20-23	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	261-269
30659320-5	2019	We demonstrate that THC (10-40 microM) impairs placental endocannabinoid system by disrupting the endocannabinoid anandamide (AEA) levels and the expression of AEA synthetic and degrading enzymes N-arachidonoylphosphatidylethanolamine-specific phospholipase D (NAPE-PLD) and fatty acid amide hydrolase (FAAH), respectively.	aea	160-163	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	196-259
34843683-8	2022	Furthermore, fluorescence in HepG2 cells using PED-A1 could be partially blocked by either biothionol (a selective NAPE-PLD inhibitor) or tetrahydrolipstatin (an inhibitor of a broad spectrum of serine hydrolase-type lipases).	biothionol	91-101	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	115-123
30842391-6	2019	RESULTS FAAH expression was significantly lower in fibroids, resulting in a NAPE-PLD: FAAH ratio that favors higher AEA levels in pre-menopausal tissues, whilst PEA levels were significantly lower, particularly in post-menopausal women, suggesting PEA protects against fibroid pathogenesis.	aea	116-119	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	76-84
30611738-12	2019	Colonic levels of N-acyl-phosphatidylethanolamine-specific phospholipase D (NAPE-PLD), which is responsible for synthesis of AEA, significantly declined after chronic treatment with 5-HT and this effect was reversed by the 5-HT3 and 5-HT4 receptor antagonists.	anandamide	125-128	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	76-84
27571266-0	2016	Bile Acid Recognition by NAPE-PLD.	Bile Acids and Salts	0-9	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	25-33
29143042-1	2017	N-Acylphosphatidylethanolamine phospholipase D (NAPE-PLD) is a membrane-associated zinc enzyme that catalyzes the hydrolysis of N-acylphosphatidylethanolamines (NAPEs) into fatty acid ethanolamides (FAEs).	N-acylphosphatidylethanolamine	128-159	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	0-46
29143042-1	2017	N-Acylphosphatidylethanolamine phospholipase D (NAPE-PLD) is a membrane-associated zinc enzyme that catalyzes the hydrolysis of N-acylphosphatidylethanolamines (NAPEs) into fatty acid ethanolamides (FAEs).	N-acylphosphatidylethanolamine	128-159	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	48-56
29143042-1	2017	N-Acylphosphatidylethanolamine phospholipase D (NAPE-PLD) is a membrane-associated zinc enzyme that catalyzes the hydrolysis of N-acylphosphatidylethanolamines (NAPEs) into fatty acid ethanolamides (FAEs).	N-acylphosphatidylethanolamine	161-166	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	0-46
29143042-1	2017	N-Acylphosphatidylethanolamine phospholipase D (NAPE-PLD) is a membrane-associated zinc enzyme that catalyzes the hydrolysis of N-acylphosphatidylethanolamines (NAPEs) into fatty acid ethanolamides (FAEs).	N-acylphosphatidylethanolamine	161-166	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	48-56
29143042-1	2017	N-Acylphosphatidylethanolamine phospholipase D (NAPE-PLD) is a membrane-associated zinc enzyme that catalyzes the hydrolysis of N-acylphosphatidylethanolamines (NAPEs) into fatty acid ethanolamides (FAEs).	Fatty Acids	173-183	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	0-46
29143042-1	2017	N-Acylphosphatidylethanolamine phospholipase D (NAPE-PLD) is a membrane-associated zinc enzyme that catalyzes the hydrolysis of N-acylphosphatidylethanolamines (NAPEs) into fatty acid ethanolamides (FAEs).	Fatty Acids	173-183	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	48-56
29143042-1	2017	N-Acylphosphatidylethanolamine phospholipase D (NAPE-PLD) is a membrane-associated zinc enzyme that catalyzes the hydrolysis of N-acylphosphatidylethanolamines (NAPEs) into fatty acid ethanolamides (FAEs).	ethanolamides	184-197	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	0-46
29143042-1	2017	N-Acylphosphatidylethanolamine phospholipase D (NAPE-PLD) is a membrane-associated zinc enzyme that catalyzes the hydrolysis of N-acylphosphatidylethanolamines (NAPEs) into fatty acid ethanolamides (FAEs).	ethanolamides	184-197	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	48-56
29143042-1	2017	N-Acylphosphatidylethanolamine phospholipase D (NAPE-PLD) is a membrane-associated zinc enzyme that catalyzes the hydrolysis of N-acylphosphatidylethanolamines (NAPEs) into fatty acid ethanolamides (FAEs).	faes	199-203	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	0-46
29143042-1	2017	N-Acylphosphatidylethanolamine phospholipase D (NAPE-PLD) is a membrane-associated zinc enzyme that catalyzes the hydrolysis of N-acylphosphatidylethanolamines (NAPEs) into fatty acid ethanolamides (FAEs).	faes	199-203	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	48-56
29143042-2	2017	Here, we describe the identification of the first small-molecule NAPE-PLD inhibitor, the quinazoline sulfonamide derivative 2,4-dioxo-N-[4-(4-pyridyl)phenyl]-1H-quinazoline-6-sulfonamide, ARN19874.	quinazoline sulfonamide	89-112	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	65-73
29143042-2	2017	Here, we describe the identification of the first small-molecule NAPE-PLD inhibitor, the quinazoline sulfonamide derivative 2,4-dioxo-N-[4-(4-pyridyl)phenyl]-1H-quinazoline-6-sulfonamide, ARN19874.	2,4-dioxo-N-(4-(4-pyridyl)phenyl)-1H-quinazoline-6-sulfonamide	124-186	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	65-73
29143042-2	2017	Here, we describe the identification of the first small-molecule NAPE-PLD inhibitor, the quinazoline sulfonamide derivative 2,4-dioxo-N-[4-(4-pyridyl)phenyl]-1H-quinazoline-6-sulfonamide, ARN19874.	2,4-dioxo-N-(4-(4-pyridyl)phenyl)-1H-quinazoline-6-sulfonamide	188-196	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	65-73
30399323-0	2019	NAPE-PLD controls OEA synthesis and fat absorption by regulating lipoprotein synthesis in an in vitro model of intestinal epithelial cells.	oleoylethanolamide	18-21	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	0-8
30399323-4	2019	In this study, we assessed the involvement of NAPE-specific phospholipase D (NAPE-PLD), which can directly release FAEs from NAPE, in intestinal OEA synthesis and lipid metabolism.	oleoylethanolamide	145-148	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	46-75
30399323-4	2019	In this study, we assessed the involvement of NAPE-specific phospholipase D (NAPE-PLD), which can directly release FAEs from NAPE, in intestinal OEA synthesis and lipid metabolism.	oleoylethanolamide	145-148	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	77-85
30399323-5	2019	Clustered regularly interspaced short palindromic repeats (CRISPR)/CRISPER-associated protein 9 (Cas9)-mediated deletion of the NAPE-PLD gene in intestinal epithelial-like Caco-2 cells reduced OEA levels, regardless of their differentiation states.	oleoylethanolamide	193-196	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	128-136
30399323-9	2019	Overall, these results indicate that NAPE-PLD plays important roles in OEA synthesis and fat absorption by regulating lipoprotein production in the intestinal epithelial cells.-Igarashi, M., Watanabe, K., Tsuduki, T., Kimura, I., Kubota, N. NAPE-PLD controls OEA synthesis and fat absorption by regulating lipoprotein synthesis in an in vitro model of intestinal epithelial cells.	oleoylethanolamide	71-74	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	37-45
30399323-9	2019	Overall, these results indicate that NAPE-PLD plays important roles in OEA synthesis and fat absorption by regulating lipoprotein production in the intestinal epithelial cells.-Igarashi, M., Watanabe, K., Tsuduki, T., Kimura, I., Kubota, N. NAPE-PLD controls OEA synthesis and fat absorption by regulating lipoprotein synthesis in an in vitro model of intestinal epithelial cells.	oleoylethanolamide	259-262	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	37-45
28843504-3	2017	The classical "transacylation-phosphodiesterase" pathway proceeds via N-acyl-phosphatidylethanolamine (NAPE), which involves the actions of two enzymes, NAPE-generating Ca2+-dependent N-acyltransferase (Ca-NAT) and NAPE-hydrolyzing phospholipase D (NAPE-PLD).	N-acylphosphatidylethanolamine	70-101	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	215-247
28843504-3	2017	The classical "transacylation-phosphodiesterase" pathway proceeds via N-acyl-phosphatidylethanolamine (NAPE), which involves the actions of two enzymes, NAPE-generating Ca2+-dependent N-acyltransferase (Ca-NAT) and NAPE-hydrolyzing phospholipase D (NAPE-PLD).	N-acylphosphatidylethanolamine	70-101	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	249-257
27571266-1	2016	The membrane-associated enzyme NAPE-PLD (N-acyl phosphatidylethanolamine specific-phospholipase D) generates the endogenous cannabinoid arachidonylethanolamide and other lipid signaling amides, including oleoylethanolamide and palmitoylethanolamide.	Cannabinoids	124-135	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	31-39
27571266-1	2016	The membrane-associated enzyme NAPE-PLD (N-acyl phosphatidylethanolamine specific-phospholipase D) generates the endogenous cannabinoid arachidonylethanolamide and other lipid signaling amides, including oleoylethanolamide and palmitoylethanolamide.	Cannabinoids	124-135	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	41-97
27571266-1	2016	The membrane-associated enzyme NAPE-PLD (N-acyl phosphatidylethanolamine specific-phospholipase D) generates the endogenous cannabinoid arachidonylethanolamide and other lipid signaling amides, including oleoylethanolamide and palmitoylethanolamide.	anandamide	136-159	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	31-39
27571266-1	2016	The membrane-associated enzyme NAPE-PLD (N-acyl phosphatidylethanolamine specific-phospholipase D) generates the endogenous cannabinoid arachidonylethanolamide and other lipid signaling amides, including oleoylethanolamide and palmitoylethanolamide.	anandamide	136-159	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	41-97
27571266-1	2016	The membrane-associated enzyme NAPE-PLD (N-acyl phosphatidylethanolamine specific-phospholipase D) generates the endogenous cannabinoid arachidonylethanolamide and other lipid signaling amides, including oleoylethanolamide and palmitoylethanolamide.	Amides	186-192	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	31-39
27571266-1	2016	The membrane-associated enzyme NAPE-PLD (N-acyl phosphatidylethanolamine specific-phospholipase D) generates the endogenous cannabinoid arachidonylethanolamide and other lipid signaling amides, including oleoylethanolamide and palmitoylethanolamide.	Amides	186-192	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	41-97
27571266-1	2016	The membrane-associated enzyme NAPE-PLD (N-acyl phosphatidylethanolamine specific-phospholipase D) generates the endogenous cannabinoid arachidonylethanolamide and other lipid signaling amides, including oleoylethanolamide and palmitoylethanolamide.	oleoylethanolamide	204-222	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	31-39
27571266-1	2016	The membrane-associated enzyme NAPE-PLD (N-acyl phosphatidylethanolamine specific-phospholipase D) generates the endogenous cannabinoid arachidonylethanolamide and other lipid signaling amides, including oleoylethanolamide and palmitoylethanolamide.	oleoylethanolamide	204-222	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	41-97
27571266-1	2016	The membrane-associated enzyme NAPE-PLD (N-acyl phosphatidylethanolamine specific-phospholipase D) generates the endogenous cannabinoid arachidonylethanolamide and other lipid signaling amides, including oleoylethanolamide and palmitoylethanolamide.	palmidrol	227-248	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	31-39
27571266-1	2016	The membrane-associated enzyme NAPE-PLD (N-acyl phosphatidylethanolamine specific-phospholipase D) generates the endogenous cannabinoid arachidonylethanolamide and other lipid signaling amides, including oleoylethanolamide and palmitoylethanolamide.	palmidrol	227-248	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	41-97
27571266-3	2016	Recently, we reported the crystal structure of human NAPE-PLD and discovered specific binding sites for the bile acid deoxycholic acid.	Bile Acids and Salts	108-117	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	53-61
27571266-3	2016	Recently, we reported the crystal structure of human NAPE-PLD and discovered specific binding sites for the bile acid deoxycholic acid.	Deoxycholic Acid	118-134	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	53-61
27571266-4	2016	In this study, we demonstrate that in the presence of this secondary bile acid, the stiffness of the protein measured by elastic neutron scattering increases, and NAPE-PLD is ~7 times faster to catalyze the hydrolysis of the more unsaturated substrate N-arachidonyl-phosphatidylethanolamine, compared with N-palmitoyl-phosphatidylethanolamine.	Bile Acids and Salts	69-78	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	163-171
27571266-4	2016	In this study, we demonstrate that in the presence of this secondary bile acid, the stiffness of the protein measured by elastic neutron scattering increases, and NAPE-PLD is ~7 times faster to catalyze the hydrolysis of the more unsaturated substrate N-arachidonyl-phosphatidylethanolamine, compared with N-palmitoyl-phosphatidylethanolamine.	N-arachidonylphosphatidylethanolamine	252-290	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	163-171
27571266-4	2016	In this study, we demonstrate that in the presence of this secondary bile acid, the stiffness of the protein measured by elastic neutron scattering increases, and NAPE-PLD is ~7 times faster to catalyze the hydrolysis of the more unsaturated substrate N-arachidonyl-phosphatidylethanolamine, compared with N-palmitoyl-phosphatidylethanolamine.	1-palmitoylphosphatidylethanolamine	306-342	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	163-171
27571266-5	2016	Chenodeoxycholic acid and glyco- or tauro-dihydroxy conjugates can also bind to NAPE-PLD and drive its activation.	Chenodeoxycholic Acid	0-21	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	80-88
27571266-5	2016	Chenodeoxycholic acid and glyco- or tauro-dihydroxy conjugates can also bind to NAPE-PLD and drive its activation.	glyco- or tauro-dihydroxy conjugates	26-62	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	80-88
27571266-7	2016	Overall, these findings provide important insights into the allosteric regulation of the enzyme mediated by bile acid cofactors and reveal that NAPE-PLD responds primarily to the number and position of their hydroxyl groups.	Bile Acids and Salts	108-117	N-acyl phosphatidylethanolamine phospholipase D	Homo sapiens	144-152