PMID-sentid	Pub_year	Sent_text	comp_official_name	comp_offset	protein_name	organism	prot_offset
32240681-8	2020	KEY FINDINGS: Significant increase of PLD1, not PLD2 was documented in CCl4-induced cirrhotic compared to normal liver tissues.	Carbon Tetrachloride	71-75	phospholipase D1	Rattus norvegicus	38-42
32697411-0	2020	MiR-122-5p and miR-326-3p promote cadmium-induced NRK-52E cell apoptosis by downregulating PLD1.	mir-122-5p	0-10	phospholipase D1	Rattus norvegicus	91-95
32697411-0	2020	MiR-122-5p and miR-326-3p promote cadmium-induced NRK-52E cell apoptosis by downregulating PLD1.	mir-326-3p	15-25	phospholipase D1	Rattus norvegicus	91-95
32697411-0	2020	MiR-122-5p and miR-326-3p promote cadmium-induced NRK-52E cell apoptosis by downregulating PLD1.	Cadmium	34-41	phospholipase D1	Rattus norvegicus	91-95
32697411-3	2020	Phospholipase D1 (PLD1) promotes cell proliferation and inhibits apoptosis, and might be involved in cadmium-induced kidney injury.	Cadmium	101-108	phospholipase D1	Rattus norvegicus	0-16
32697411-3	2020	Phospholipase D1 (PLD1) promotes cell proliferation and inhibits apoptosis, and might be involved in cadmium-induced kidney injury.	Cadmium	101-108	phospholipase D1	Rattus norvegicus	18-22
32697411-4	2020	In this study, we used miRNA microarray assays and bioinformatics analysis to identify miRNAs, which may regulate PLD1 expression and exert an impact on cadmium-induced kidney injury.	Cadmium	153-160	phospholipase D1	Rattus norvegicus	114-118
32697411-7	2020	Cadmium treatment also increased miR-122-5p and miR-326-3p and decreased PLD1 in NRK-52E cells.	Cadmium	0-7	phospholipase D1	Rattus norvegicus	73-77
32697411-9	2020	In conclusion, our results suggest that miR-122-5p and miR-326-3p might enhance cadmium-induced NRK-52E cell apoptosis through downregulating PLD1 expression.	mir-122-5p	40-50	phospholipase D1	Rattus norvegicus	142-146
32697411-9	2020	In conclusion, our results suggest that miR-122-5p and miR-326-3p might enhance cadmium-induced NRK-52E cell apoptosis through downregulating PLD1 expression.	mir-326-3p	55-65	phospholipase D1	Rattus norvegicus	142-146
32697411-9	2020	In conclusion, our results suggest that miR-122-5p and miR-326-3p might enhance cadmium-induced NRK-52E cell apoptosis through downregulating PLD1 expression.	Cadmium	80-87	phospholipase D1	Rattus norvegicus	142-146
32240681-11	2020	Moreover, PLD1 inhibitors not only exhibited similar effects with rapamycin in TGFbeta1-induced fibrogenesis, but also blunted MHY1485 enhanced cell proliferation of HSC-T6.	Sirolimus	66-75	phospholipase D1	Rattus norvegicus	10-14
32240681-11	2020	Moreover, PLD1 inhibitors not only exhibited similar effects with rapamycin in TGFbeta1-induced fibrogenesis, but also blunted MHY1485 enhanced cell proliferation of HSC-T6.	4,6-dimorpholino-N-(4-nitrophenyl)-1,3,5-triazin-2-amine	127-134	phospholipase D1	Rattus norvegicus	10-14
31967386-1	2020	Phosphatidic acid (PA) produced by phospholipase D1 has been shown to contribute to secretory vesicle exocytosis in a large number of cell models.	Phosphatidic Acids	0-17	phospholipase D1	Rattus norvegicus	35-51
31967386-1	2020	Phosphatidic acid (PA) produced by phospholipase D1 has been shown to contribute to secretory vesicle exocytosis in a large number of cell models.	Phosphatidic Acids	19-21	phospholipase D1	Rattus norvegicus	35-51
32337269-0	2020	Phospholipase D1 Ameliorates Apoptosis in Chronic Renal Toxicity Caused by Low-Dose Cadmium Exposure.	Cadmium	84-91	phospholipase D1	Rattus norvegicus	0-16
32337269-5	2020	Bioinformatics analysis indicated that phospholipase D1 (PLD1) was significantly underexpressed and may correlate strongly with Cd-induced chronic kidney impairment.	Cadmium	128-130	phospholipase D1	Rattus norvegicus	39-55
32337269-5	2020	Bioinformatics analysis indicated that phospholipase D1 (PLD1) was significantly underexpressed and may correlate strongly with Cd-induced chronic kidney impairment.	Cadmium	128-130	phospholipase D1	Rattus norvegicus	57-61
32337269-6	2020	Previous studies have shown that PLD1 promotes cell proliferation and inhibits apoptosis, indicating that PLD1 may be implicated in the pathogenesis of kidney injury induced by Cd.	Cadmium	177-179	phospholipase D1	Rattus norvegicus	33-37
32337269-6	2020	Previous studies have shown that PLD1 promotes cell proliferation and inhibits apoptosis, indicating that PLD1 may be implicated in the pathogenesis of kidney injury induced by Cd.	Cadmium	177-179	phospholipase D1	Rattus norvegicus	106-110
32337269-7	2020	Studies in vivo and in vitro all demonstrate that the mRNA and protein levels of PLD1 decrease significantly both in kidney tissue and in proximal tubular cell lines exposed to Cd.	Cadmium	177-179	phospholipase D1	Rattus norvegicus	81-85
32337269-8	2020	Overexpression of PLD1 and its downstream product PA could ameliorate Cd-induced apoptosis.	Protactinium	50-52	phospholipase D1	Rattus norvegicus	18-22
32337269-8	2020	Overexpression of PLD1 and its downstream product PA could ameliorate Cd-induced apoptosis.	Cadmium	70-72	phospholipase D1	Rattus norvegicus	18-22
32337269-11	2020	In conclusion, our results indicated that PLD1 and its downstream PA were strongly implicated in Cd-induced chronic kidney impairment and could be a novel player in the defense against Cd-induced nephrotoxicity.	Protactinium	66-68	phospholipase D1	Rattus norvegicus	42-46
32337269-11	2020	In conclusion, our results indicated that PLD1 and its downstream PA were strongly implicated in Cd-induced chronic kidney impairment and could be a novel player in the defense against Cd-induced nephrotoxicity.	Cadmium	97-99	phospholipase D1	Rattus norvegicus	42-46
32337269-11	2020	In conclusion, our results indicated that PLD1 and its downstream PA were strongly implicated in Cd-induced chronic kidney impairment and could be a novel player in the defense against Cd-induced nephrotoxicity.	Cadmium	185-187	phospholipase D1	Rattus norvegicus	42-46
29325932-6	2018	Subsequent LEGO bioinformatics analysis indicated that phospholipid metabolism genes Lpcat2 and Pld1 served as the potential target genes responsible for the LSD1 mediated protective effects.	Phospholipids	55-67	phospholipase D1	Rattus norvegicus	96-100
30207376-6	2019	We observed an early increase in PLD1 gene and protein expression along with the increase in the PLD activity in vascular muscle cell line, during calcification induced by ascorbic acid and beta-glycerophosphate.	Ascorbic Acid	172-185	phospholipase D1	Rattus norvegicus	33-37
30207376-6	2019	We observed an early increase in PLD1 gene and protein expression along with the increase in the PLD activity in vascular muscle cell line, during calcification induced by ascorbic acid and beta-glycerophosphate.	beta-glycerophosphoric acid	190-211	phospholipase D1	Rattus norvegicus	33-37
30207376-7	2019	Inhibition of PLD1 by the selective inhibitor VU0155069, or the pan-PLD inhibitor, halopemide, prevented calcification.	N-(1-(4-(5-chloro-2-oxo-2,3-dihydro-1H-benzo(d)imidazol-1-yl)piperidin-1-yl)propan-2-yl)-2-naphthamide	46-55	phospholipase D1	Rattus norvegicus	14-18
30207376-9	2019	In agreement, we found an increase in Pld1 gene expression and PLD activity in aortic explant cultures treated with high phosphate, whereas PLD inhibition by halopemide decreased calcification.	Phosphates	121-130	phospholipase D1	Rattus norvegicus	38-42
29981815-5	2018	The rPLD1 toxin was converted into toxoid (the first toxoid of H. lepturus PLD) with a 0.25% concentration of formalin and stored for ten days at room temperature.	Formaldehyde	110-118	phospholipase D1	Rattus norvegicus	4-9
24986006-6	2015	Furthermore, treatment with arachidonic acid (AA) which is generated by the action of PLA2 (phospholipase A2) on phosphatidic acid (a PLD1 product), increased the phosphorylation of p38 MAPK and CREB, as well as Bcl-2 expression, indicating that PLA2 is involved in the differentiation process resulting from PLD1 activation.	Arachidonic Acid	28-44	phospholipase D1	Rattus norvegicus	134-138
24986006-6	2015	Furthermore, treatment with arachidonic acid (AA) which is generated by the action of PLA2 (phospholipase A2) on phosphatidic acid (a PLD1 product), increased the phosphorylation of p38 MAPK and CREB, as well as Bcl-2 expression, indicating that PLA2 is involved in the differentiation process resulting from PLD1 activation.	Arachidonic Acid	28-44	phospholipase D1	Rattus norvegicus	309-313
24986006-6	2015	Furthermore, treatment with arachidonic acid (AA) which is generated by the action of PLA2 (phospholipase A2) on phosphatidic acid (a PLD1 product), increased the phosphorylation of p38 MAPK and CREB, as well as Bcl-2 expression, indicating that PLA2 is involved in the differentiation process resulting from PLD1 activation.	Phosphatidic Acids	113-130	phospholipase D1	Rattus norvegicus	134-138
24728967-0	2014	The role of phospholipase D1 in liver fibrosis induced by dimethylnitrosamine in vivo.	Dimethylnitrosamine	58-77	phospholipase D1	Rattus norvegicus	12-28
25489735-0	2014	PED/PEA-15 inhibits hydrogen peroxide-induced apoptosis in Ins-1E pancreatic beta-cells via PLD-1.	Hydrogen Peroxide	20-37	phospholipase D1	Rattus norvegicus	92-97
25489735-11	2014	Interestingly, the preincubation with propranolol, an inhibitor of the pathway of PLD-1, a known interactor of PED/PEA-15, responsible for its deleterious effects on glucose tolerance, abolishes the antiapoptotic effects of PED/PEA-15 overexpression in Ins-1E beta-cells.	Propranolol	38-49	phospholipase D1	Rattus norvegicus	82-87
25489735-11	2014	Interestingly, the preincubation with propranolol, an inhibitor of the pathway of PLD-1, a known interactor of PED/PEA-15, responsible for its deleterious effects on glucose tolerance, abolishes the antiapoptotic effects of PED/PEA-15 overexpression in Ins-1E beta-cells.	Glucose	166-173	phospholipase D1	Rattus norvegicus	82-87
25489735-13	2014	These results show that PED/PEA-15 overexpression is sufficient to block hydrogen peroxide-induced apoptosis in Ins-1E cells through a PLD-1 mediated mechanism.	Hydrogen Peroxide	73-90	phospholipase D1	Rattus norvegicus	135-140
24728967-7	2014	The activity of PLD and PLD1, alpha-SMA expression level in the MEA-intervention group was much lower than those in the DMN model group.	N-methylaminoethanol	64-67	phospholipase D1	Rattus norvegicus	24-28
24336713-6	2013	NGF-triggered RSK2-dependent phosphorylation of PLD1 led to its activation and the synthesis of phosphatidic acid at sites of neurite growth.	Phosphatidic Acids	96-113	phospholipase D1	Rattus norvegicus	48-52
24262632-4	2014	Downregulation of PLD1 and exposure to the PLD1 inhibitor VU0359595 attenuated PLD activity and strongly reduced the mitogenic activity of serum and IGF-1.	VU0359595	58-67	phospholipase D1	Rattus norvegicus	43-47
24269608-5	2014	We provide evidence that the 5-HT(1B)R activates PLD1 to subsequently activate PIP 5-kinase and generate PIP2, an allosteric enhancer of TRPM8, achieving a several-fold increase in potency of TRPM8 activation.	Phosphatidylinositol 4,5-Diphosphate	105-109	phospholipase D1	Rattus norvegicus	49-53
23525454-3	2013	Fal-002-2 attenuated the interaction of PLD1 with ADP-ribosylation factor (Arf) 6, Ras homology (Rho) A and protein kinase C (PKC) isoforms (alpha, betaI, and betaII), and also inhibited the membrane recruitment of Arf6 and RhoA in fMLP-stimulated neutrophils, but not in GTPgammaS-stimulated cell-free system.	Guanosine 5'-O-(3-Thiotriphosphate)	272-281	phospholipase D1	Rattus norvegicus	40-44
20954081-5	2010	The phthalate, DEHP (500 mg/kg/d), was administered orally, daily to prepubertal rats (4 wk of age, weighing approximately 70-90 g) for 1, 7, or 28 d. In this study, protein expression levels of PLD1/2, peroxisome proliferator-activated receptor (PPAR), and cytochrome P-450 (CYP) were determined by Western blot analysis using specific antibodies.	phthalic acid	4-13	phospholipase D1	Rattus norvegicus	195-245
23010583-5	2012	This rise in DAG formation was due to phospholipase D1 (PLD1) and PLD2 activations.	Diglycerides	13-16	phospholipase D1	Rattus norvegicus	38-54
23010583-5	2012	This rise in DAG formation was due to phospholipase D1 (PLD1) and PLD2 activations.	Diglycerides	13-16	phospholipase D1	Rattus norvegicus	56-60
23010583-8	2012	Iron-induced oxidative stress promoted an increased localization of PLD1 in membrane rafts, whereas PLD2 was excluded from these domains and appeared to be involved in glutamate transporter function.	Iron	0-4	phospholipase D1	Rattus norvegicus	68-72
22674271-8	2012	Moreover, the inhibition of dendritic branching by V14-RhoA and WT-PLD1 can be partially ameliorated by reducing the level of phosphatidic acid (PA), which is the enzymatic product of PLD1.	Phosphatidic Acids	126-143	phospholipase D1	Rattus norvegicus	67-71
22674271-8	2012	Moreover, the inhibition of dendritic branching by V14-RhoA and WT-PLD1 can be partially ameliorated by reducing the level of phosphatidic acid (PA), which is the enzymatic product of PLD1.	Phosphatidic Acids	126-143	phospholipase D1	Rattus norvegicus	184-188
22674271-8	2012	Moreover, the inhibition of dendritic branching by V14-RhoA and WT-PLD1 can be partially ameliorated by reducing the level of phosphatidic acid (PA), which is the enzymatic product of PLD1.	Phosphatidic Acids	145-147	phospholipase D1	Rattus norvegicus	67-71
22674271-8	2012	Moreover, the inhibition of dendritic branching by V14-RhoA and WT-PLD1 can be partially ameliorated by reducing the level of phosphatidic acid (PA), which is the enzymatic product of PLD1.	Phosphatidic Acids	145-147	phospholipase D1	Rattus norvegicus	184-188
21212180-9	2011	Incubation with catalytically inactive PLD1, but not catalytically inactive mutant PLD2 adenovirus, also increased Cch-stimulated protein secretion and decreased ERK activity.	Carbachol	115-118	phospholipase D1	Rattus norvegicus	39-43
21212180-10	2011	Inhibition of Rho with C3 exotoxin and a dominant negative Rho adenovirus and inhibition of ROCK with Y-27632 inhibited Cch-stimulated PLD1 activity, increased protein secretion, and decreased ERK activity.	Y 27632	102-109	phospholipase D1	Rattus norvegicus	135-139
21212180-10	2011	Inhibition of Rho with C3 exotoxin and a dominant negative Rho adenovirus and inhibition of ROCK with Y-27632 inhibited Cch-stimulated PLD1 activity, increased protein secretion, and decreased ERK activity.	Carbachol	120-123	phospholipase D1	Rattus norvegicus	135-139
21212180-11	2011	The association of PLD1 and ROCK increased with Cch stimulation, as determined by immunoprecipitation.	Carbachol	48-51	phospholipase D1	Rattus norvegicus	19-23
15980073-10	2005	Finally, using various RalA mutants selectively impaired in their ability to activate downstream effectors, we show that PLD1 activation is essential for the activation of secretion by GTP-loaded RalA.	Guanosine Triphosphate	185-188	phospholipase D1	Rattus norvegicus	121-125
18003982-7	2008	Overexpression of the phosphatidic acid-generating enzyme, phospholipase D1, completely rescued the secretory defect seen with the 5RK/A mutant.	Phosphatidic Acids	22-39	phospholipase D1	Rattus norvegicus	59-75
16439353-2	2006	Using chromaffin and PC12 cells, we have recently described that the granule-associated GTPase ARF6 plays a crucial role in exocytosis by activating phospholipase D1 at the plasma membrane and, presumably, promoting the fusion reaction between the two membrane bilayers.	chromaffin	6-16	phospholipase D1	Rattus norvegicus	149-165
16459925-8	2005	Dominant negative PLD1 and PLD2 constructs inhibited the effects of PTH on the phospholipid hydrolysis.	Phospholipids	79-91	phospholipase D1	Rattus norvegicus	18-22
17540765-0	2007	Phospholipase D1 production of phosphatidic acid at the plasma membrane promotes exocytosis of large dense-core granules at a late stage.	Phosphatidic Acids	31-48	phospholipase D1	Rattus norvegicus	0-16
17540765-4	2007	Using a short interference RNA strategy on chromaffin and PC12 cells, we demonstrate here that phospholipase D1 is activated in secretagogue-stimulated cells and that it produces PA at the plasma membrane at the secretory granule docking sites.	chromaffin	43-53	phospholipase D1	Rattus norvegicus	95-111
17540765-4	2007	Using a short interference RNA strategy on chromaffin and PC12 cells, we demonstrate here that phospholipase D1 is activated in secretagogue-stimulated cells and that it produces PA at the plasma membrane at the secretory granule docking sites.	Phosphatidic Acids	179-181	phospholipase D1	Rattus norvegicus	95-111
15980073-11	2005	Together, these results provide evidence that RalA is a positive regulator of calcium-evoked exocytosis of large dense core secretory granules and suggest that stimulation of PLD1 and consequent changes in plasma membrane phospholipid composition is the major function RalA undertakes in calcium-regulated exocytosis.	Calcium	78-85	phospholipase D1	Rattus norvegicus	175-179
15339843-5	2004	This dominant-negative PLD1 enhanced FcepsilonRI-induced tyrosine phosphorylations of early signaling molecules such as the receptor subunits, Syk and phospholipase C-gamma which resulted in faster release of Ca(2+) from intracellular sources.	Tyrosine	57-65	phospholipase D1	Rattus norvegicus	23-27
15616193-8	2005	Endogenous PLD1 was located at the level of SFLSs, and by means of an intracellularly expressed fluorescent probe, PA was shown to be accumulated along these structures in response to AVP.	Phosphatidic Acids	115-117	phospholipase D1	Rattus norvegicus	11-15
15339843-8	2004	Dominant-negative PLD1 reduced the basal phosphatidic acid formation in unstimulated cells, which was accompanied by an increase in FcepsilonRI within the lipid rafts.	Phosphatidic Acids	41-58	phospholipase D1	Rattus norvegicus	18-22
15339843-9	2004	These results indicate that constitutive basal PLD1 activity by regulating phosphatidic acid formation controls the early signals initiated by FcepsilonRI aggregation that lead to mast cell degranulation.	Phosphatidic Acids	75-92	phospholipase D1	Rattus norvegicus	47-51
15150437-1	2004	In the presence of vanadate, H(2)O(2) induced tyrosine phosphorylation of PLD1, protein kinase C-alpha (PKC-alpha), and other unidentified proteins in rat vascular smooth muscle cells (VSMCs).	Vanadates	19-27	phospholipase D1	Rattus norvegicus	74-78
15150437-3	2004	Stimulation of the cells by H(2)O(2) and vanadate showed a concentration-dependent tyrosine phosphorylation of the proteins in PLD1 immunoprecipitates and activation of PLD.	Vanadates	41-49	phospholipase D1	Rattus norvegicus	127-131
15150437-3	2004	Stimulation of the cells by H(2)O(2) and vanadate showed a concentration-dependent tyrosine phosphorylation of the proteins in PLD1 immunoprecipitates and activation of PLD.	Tyrosine	83-91	phospholipase D1	Rattus norvegicus	127-131
15150437-1	2004	In the presence of vanadate, H(2)O(2) induced tyrosine phosphorylation of PLD1, protein kinase C-alpha (PKC-alpha), and other unidentified proteins in rat vascular smooth muscle cells (VSMCs).	Hydrogen Peroxide	29-37	phospholipase D1	Rattus norvegicus	74-78
15150437-1	2004	In the presence of vanadate, H(2)O(2) induced tyrosine phosphorylation of PLD1, protein kinase C-alpha (PKC-alpha), and other unidentified proteins in rat vascular smooth muscle cells (VSMCs).	Tyrosine	46-54	phospholipase D1	Rattus norvegicus	74-78
15150437-2	2004	Interestingly, PLD1 was found to be constitutively associated with PKC-alpha in VSMCs.	vsmcs	80-85	phospholipase D1	Rattus norvegicus	15-19
15150437-3	2004	Stimulation of the cells by H(2)O(2) and vanadate showed a concentration-dependent tyrosine phosphorylation of the proteins in PLD1 immunoprecipitates and activation of PLD.	Hydrogen Peroxide	28-36	phospholipase D1	Rattus norvegicus	127-131
12642902-7	2003	These data indicate that both PLD1 and PLD2 play a protective role against glutamate-induced cell death in PC12 cells.	Glutamic Acid	75-84	phospholipase D1	Rattus norvegicus	30-34
15015836-2	2004	Western blot analysis showed that the level of the PLD1 isoform was significantly increased in the hearts of rats with EAM on days 14, 17 and 21 postimmunization (pi) (P < 0.01; control vs EAM at 14 pi, 17 pi and 21 pi).	molibresib	119-122	phospholipase D1	Rattus norvegicus	51-55
15015836-2	2004	Western blot analysis showed that the level of the PLD1 isoform was significantly increased in the hearts of rats with EAM on days 14, 17 and 21 postimmunization (pi) (P < 0.01; control vs EAM at 14 pi, 17 pi and 21 pi).	molibresib	192-195	phospholipase D1	Rattus norvegicus	51-55
15015836-5	2004	Some PLD1-positive cells were also positive for proliferating cell nuclear antigen in some cardiomyocytes or terminal deoxynucleotidyl transferase (TdT)-mediated dUTP nick end-labeling in some macrophages, suggesting that PLD1 positive cells have a capacity for proliferation or apoptosis depending on cell types in the target organ.	deoxyuridine triphosphate	162-166	phospholipase D1	Rattus norvegicus	5-9
15015836-6	2004	Thus, it is postulated that increased expression of PLD1 in EAM may support an early inflammatory response in proliferating inflammatory cells, and its expression in cardiomyocytes may help them to survive by activation of survival factors in hearts with EAM.	molibresib	60-63	phospholipase D1	Rattus norvegicus	52-56
12829737-6	2003	These results and previously reported effects of short-chain ceramides on phospholipase D activity prompted us to compare the effects of C2-ceramide, C2-dihydroceramide and C16-ceramide on phospholipase D1 and phospholipase D2 activities in vitro.	N-palmitoylsphingosine	173-185	phospholipase D1	Rattus norvegicus	189-205
12829737-7	2003	We find that the effects of these ceramides on phospholipase D1 activity strongly correlate with their effects on antigen-stimulated Ca2+ mobilization and with their disruption of lipid order.	Ceramides	34-43	phospholipase D1	Rattus norvegicus	47-63
12876278-3	2003	PLD1 localized to perinuclear endosomes and Golgi in COS-7 cells, but on cellular stimulation, translocated to the plasma membrane in an activity-facilitated manner and then returned to the endosomes.	carbonyl sulfide	53-56	phospholipase D1	Rattus norvegicus	0-4
12556526-1	2003	Both known isoforms of phospholipase (PL) D, PLD1 and PLD2, require phosphatidylinositol 4,5-bisphosphate for activity.	Phosphatidylinositol 4,5-Diphosphate	68-105	phospholipase D1	Rattus norvegicus	45-49
12642902-3	2003	The data presented here show that both PLD isozymes, PLD1 and PLD2 are also required in attenuating glutamate-induced cell death in PC12 cells.	Glutamic Acid	100-109	phospholipase D1	Rattus norvegicus	53-57
12642902-6	2003	When cDNAs of PLD1 and PLD2 were transfected into PC12 cells respectively, overexpression of PLD1 or PLD2 resulted in inhibition of glutamate-induced apoptotic cell death.	Glutamic Acid	132-141	phospholipase D1	Rattus norvegicus	14-18
12642902-6	2003	When cDNAs of PLD1 and PLD2 were transfected into PC12 cells respectively, overexpression of PLD1 or PLD2 resulted in inhibition of glutamate-induced apoptotic cell death.	Glutamic Acid	132-141	phospholipase D1	Rattus norvegicus	93-97
12374567-0	2003	Endogenous phospholipase D2 localizes to the plasma membrane of RBL-2H3 mast cells and can be distinguished from ADP ribosylation factor-stimulated phospholipase D1 activity by its specific sensitivity to oleic acid.	Oleic Acid	205-215	phospholipase D1	Rattus norvegicus	148-164
12401204-1	2002	Phospholipase D1 and D2 (PLD1, PLD2) both have PX and PH domains in their N-terminal regions with these inositol lipid binding domains playing key roles in regulating PLD activity and localisation.	inositol lipid	104-118	phospholipase D1	Rattus norvegicus	0-23
12401204-1	2002	Phospholipase D1 and D2 (PLD1, PLD2) both have PX and PH domains in their N-terminal regions with these inositol lipid binding domains playing key roles in regulating PLD activity and localisation.	inositol lipid	104-118	phospholipase D1	Rattus norvegicus	25-29
12379803-7	2002	Together, these results provide the first direct evidence that ARF6 plays a role in calcium-regulated exocytosis in neuroendocrine cells, and suggest that ARF6-stimulated PLD1 activation at the plasma membrane and consequent changes in membrane phospholipid composition are critical for formation of the exocytotic fusion pore.	Calcium	84-91	phospholipase D1	Rattus norvegicus	171-175
12379803-7	2002	Together, these results provide the first direct evidence that ARF6 plays a role in calcium-regulated exocytosis in neuroendocrine cells, and suggest that ARF6-stimulated PLD1 activation at the plasma membrane and consequent changes in membrane phospholipid composition are critical for formation of the exocytotic fusion pore.	Phospholipids	245-257	phospholipase D1	Rattus norvegicus	171-175
11812783-2	2002	Recently, we showed that rPLD1 is modified by Ser/Thr phosphorylation and palmitoylation.	Serine	46-49	phospholipase D1	Rattus norvegicus	25-30
12388770-9	2002	Antigen or phorbol 12-myristate 13-acetate stimulation increased both PLD1 and PLD2 activity when expressed individually in RBL-2H3 cells.	Tetradecanoylphorbol Acetate	11-42	phospholipase D1	Rattus norvegicus	70-74
12023367-4	2002	These processes and secretion of granules are suppressed by expression of a catalytically inactive mutant of PLD1 or by the presence of 50 mM 1-butanol but not tert-butanol, an indication that these events are dependent on the catalytic activity of PLD1.	1-Butanol	142-151	phospholipase D1	Rattus norvegicus	109-113
12023367-4	2002	These processes and secretion of granules are suppressed by expression of a catalytically inactive mutant of PLD1 or by the presence of 50 mM 1-butanol but not tert-butanol, an indication that these events are dependent on the catalytic activity of PLD1.	1-Butanol	142-151	phospholipase D1	Rattus norvegicus	249-253
12023367-6	2002	Subsequent stimulation of calcium influx with Ag or thapsigargin leads to rapid redistribution of PLD1 to the plasma membrane and accelerated secretion.	Calcium	26-33	phospholipase D1	Rattus norvegicus	98-102
12023367-6	2002	Subsequent stimulation of calcium influx with Ag or thapsigargin leads to rapid redistribution of PLD1 to the plasma membrane and accelerated secretion.	Thapsigargin	52-64	phospholipase D1	Rattus norvegicus	98-102
12023367-9	2002	These data indicate a two-step process: translocation of granules to the cell periphery, regulated by granule-associated PLD1, and a calcium-dependent fusion of granules with the plasma membrane, regulated by plasma membrane-associated PLD2 and possibly PLD1.	Calcium	133-140	phospholipase D1	Rattus norvegicus	254-258
11812783-2	2002	Recently, we showed that rPLD1 is modified by Ser/Thr phosphorylation and palmitoylation.	Threonine	50-53	phospholipase D1	Rattus norvegicus	25-30
11812783-4	2002	Mutations of Cys(240) and Cys(241) of rPLD1, which abolish both post-translational modifications, did not affect the ability of either Galpha(13)Q226L or Galpha(q)Q209L to activate rPLD1.	Cysteine	13-16	phospholipase D1	Rattus norvegicus	38-43
11812783-4	2002	Mutations of Cys(240) and Cys(241) of rPLD1, which abolish both post-translational modifications, did not affect the ability of either Galpha(13)Q226L or Galpha(q)Q209L to activate rPLD1.	Cysteine	26-29	phospholipase D1	Rattus norvegicus	38-43
11812783-6	2002	On the contrary, the PKC-insensitive mutant rPLD1(DeltaN168), which lacks the first 168 amino acids of rPLD1, responded to Galpha(13)Q226L but not to Galpha(q)Q209L.	galpha	123-129	phospholipase D1	Rattus norvegicus	44-49
11812783-11	2002	In summary, Galpha(13) activation of rPLD1 in COS-7 cells is mediated by Rho, while Galpha(q) activation requires PKC.	galpha	12-18	phospholipase D1	Rattus norvegicus	37-42
11522330-1	2001	To assess a possible role for phospholipase D (PLD) in PC12 cell signal transduction and differentiation, we have investigated the expression of PLD in PC12 cells and found that the differentiation factor, nerve growth factor (NGF) increased PLD1 protein expression and phorbol 12-myristate 13 acetate (PMA)-induced PLD activity.	Tetradecanoylphorbol Acetate	270-301	phospholipase D1	Rattus norvegicus	242-246
11918661-11	2002	The expression pattern of the PLD1 during development of the retina suggests that PLD1 plays important roles in glutamate-associated differentiation of both specific neurons and radial glial cells, and in glutamate-mediated cellular signalling in Muller cells.	Glutamic Acid	112-121	phospholipase D1	Rattus norvegicus	30-34
11918661-11	2002	The expression pattern of the PLD1 during development of the retina suggests that PLD1 plays important roles in glutamate-associated differentiation of both specific neurons and radial glial cells, and in glutamate-mediated cellular signalling in Muller cells.	Glutamic Acid	112-121	phospholipase D1	Rattus norvegicus	82-86
11918661-11	2002	The expression pattern of the PLD1 during development of the retina suggests that PLD1 plays important roles in glutamate-associated differentiation of both specific neurons and radial glial cells, and in glutamate-mediated cellular signalling in Muller cells.	Glutamic Acid	205-214	phospholipase D1	Rattus norvegicus	30-34
11918661-11	2002	The expression pattern of the PLD1 during development of the retina suggests that PLD1 plays important roles in glutamate-associated differentiation of both specific neurons and radial glial cells, and in glutamate-mediated cellular signalling in Muller cells.	Glutamic Acid	205-214	phospholipase D1	Rattus norvegicus	82-86
11923096-1	2002	Our previous studies showed that truncation of the N-terminal 168 amino acids of rat brain phospholipase D1 (rPLD1) abolishes its response to protein kinase C (PKC) and greatly diminishes its palmitoylation and Ser/Thr phosphorylation.	Serine	211-214	phospholipase D1	Rattus norvegicus	91-107
11923096-1	2002	Our previous studies showed that truncation of the N-terminal 168 amino acids of rat brain phospholipase D1 (rPLD1) abolishes its response to protein kinase C (PKC) and greatly diminishes its palmitoylation and Ser/Thr phosphorylation.	Serine	211-214	phospholipase D1	Rattus norvegicus	109-114
11923096-1	2002	Our previous studies showed that truncation of the N-terminal 168 amino acids of rat brain phospholipase D1 (rPLD1) abolishes its response to protein kinase C (PKC) and greatly diminishes its palmitoylation and Ser/Thr phosphorylation.	Threonine	215-218	phospholipase D1	Rattus norvegicus	91-107
11923096-1	2002	Our previous studies showed that truncation of the N-terminal 168 amino acids of rat brain phospholipase D1 (rPLD1) abolishes its response to protein kinase C (PKC) and greatly diminishes its palmitoylation and Ser/Thr phosphorylation.	Threonine	215-218	phospholipase D1	Rattus norvegicus	109-114
11923096-2	2002	In this study, we show that the response to PKC as well as the palmitoylation and Ser/Thr phosphorylation were restored when the truncated rPLD1 mutant (rPLD1(DeltaN168)) was coexpressed with a fragment containing the N-terminal 168 amino acids.	Serine	82-85	phospholipase D1	Rattus norvegicus	139-144
11923096-2	2002	In this study, we show that the response to PKC as well as the palmitoylation and Ser/Thr phosphorylation were restored when the truncated rPLD1 mutant (rPLD1(DeltaN168)) was coexpressed with a fragment containing the N-terminal 168 amino acids.	Serine	82-85	phospholipase D1	Rattus norvegicus	153-158
11923096-2	2002	In this study, we show that the response to PKC as well as the palmitoylation and Ser/Thr phosphorylation were restored when the truncated rPLD1 mutant (rPLD1(DeltaN168)) was coexpressed with a fragment containing the N-terminal 168 amino acids.	Threonine	86-89	phospholipase D1	Rattus norvegicus	139-144
11923096-2	2002	In this study, we show that the response to PKC as well as the palmitoylation and Ser/Thr phosphorylation were restored when the truncated rPLD1 mutant (rPLD1(DeltaN168)) was coexpressed with a fragment containing the N-terminal 168 amino acids.	Threonine	86-89	phospholipase D1	Rattus norvegicus	153-158
11923096-3	2002	Immunoprecipitation experiments showed that the N-terminal fragment associated with rPLD1(DeltaN168) when coexpressed in COS 7 cells and that palmitoylation of Cys(240) and Cys(241) was not necessary for the association.	carbonyl sulfide	121-124	phospholipase D1	Rattus norvegicus	84-89
11923096-7	2002	In summary, the N-terminal 168-amino-acid fragment of rPLD1 can associate with truncated rPLD1(DeltaN168) to restore its palmitoylation, Ser/Thr phosphorylation and PKC response.	Serine	137-140	phospholipase D1	Rattus norvegicus	54-59
11923096-7	2002	In summary, the N-terminal 168-amino-acid fragment of rPLD1 can associate with truncated rPLD1(DeltaN168) to restore its palmitoylation, Ser/Thr phosphorylation and PKC response.	Serine	137-140	phospholipase D1	Rattus norvegicus	89-94
11923096-7	2002	In summary, the N-terminal 168-amino-acid fragment of rPLD1 can associate with truncated rPLD1(DeltaN168) to restore its palmitoylation, Ser/Thr phosphorylation and PKC response.	Threonine	141-144	phospholipase D1	Rattus norvegicus	54-59
11923096-7	2002	In summary, the N-terminal 168-amino-acid fragment of rPLD1 can associate with truncated rPLD1(DeltaN168) to restore its palmitoylation, Ser/Thr phosphorylation and PKC response.	Threonine	141-144	phospholipase D1	Rattus norvegicus	89-94
11752468-7	2001	PLD1(K898R) produced a fast and potent dose-dependent inhibition of ACh release.	Acetylcholine	68-71	phospholipase D1	Rattus norvegicus	0-4
11752468-9	2001	Analysis of the fluctuations in amplitude of the postsynaptic responses revealed that the PLD1(K898R) blocked ACh release by reducing the number of active presynaptic-releasing sites.	Acetylcholine	110-113	phospholipase D1	Rattus norvegicus	90-94
11950936-2	2002	In vitro PLD1b activity is phosphatidylinositol 4,5-bisphosphate dependent via an N-terminal PH domain and is stimulated by Rho, ARF, and PKC family proteins, combinations of which cooperatively increase this activity.	Phosphatidylinositol 4,5-Diphosphate	27-64	phospholipase D1	Rattus norvegicus	9-14
11680625-7	2001	Pretreatment of intact acini with a phorbol ester (4beta-phorbol 12-myristate 13-acetate, PMA) to activate PLD1 protein kinase C (PKC) dependently did not change the subcellular distribution of PLD1.	Phorbol Esters	36-49	phospholipase D1	Rattus norvegicus	107-111
11680625-7	2001	Pretreatment of intact acini with a phorbol ester (4beta-phorbol 12-myristate 13-acetate, PMA) to activate PLD1 protein kinase C (PKC) dependently did not change the subcellular distribution of PLD1.	Tetradecanoylphorbol Acetate	51-88	phospholipase D1	Rattus norvegicus	107-111
11680625-7	2001	Pretreatment of intact acini with a phorbol ester (4beta-phorbol 12-myristate 13-acetate, PMA) to activate PLD1 protein kinase C (PKC) dependently did not change the subcellular distribution of PLD1.	Tetradecanoylphorbol Acetate	90-93	phospholipase D1	Rattus norvegicus	107-111
11522330-1	2001	To assess a possible role for phospholipase D (PLD) in PC12 cell signal transduction and differentiation, we have investigated the expression of PLD in PC12 cells and found that the differentiation factor, nerve growth factor (NGF) increased PLD1 protein expression and phorbol 12-myristate 13 acetate (PMA)-induced PLD activity.	Tetradecanoylphorbol Acetate	303-306	phospholipase D1	Rattus norvegicus	242-246
10327185-0	1999	Increased expression of phospholipase D1 mRNA during cAMP- or NGF-induced differentiation in PC12 cells.	Cyclic AMP	53-57	phospholipase D1	Rattus norvegicus	24-40
11359912-6	2001	In the three clones expressing rPLD1-V5, PLD activity stimulated by phorbol myristate acetate (PMA) or lysophosphatidic acid (LPA) was reduced by ~50%, while the PLD activity of Rat2V20 cells was normal.	Tetradecanoylphorbol Acetate	68-93	phospholipase D1	Rattus norvegicus	31-36
11359912-6	2001	In the three clones expressing rPLD1-V5, PLD activity stimulated by phorbol myristate acetate (PMA) or lysophosphatidic acid (LPA) was reduced by ~50%, while the PLD activity of Rat2V20 cells was normal.	Tetradecanoylphorbol Acetate	95-98	phospholipase D1	Rattus norvegicus	31-36
11359912-6	2001	In the three clones expressing rPLD1-V5, PLD activity stimulated by phorbol myristate acetate (PMA) or lysophosphatidic acid (LPA) was reduced by ~50%, while the PLD activity of Rat2V20 cells was normal.	lysophosphatidic acid	103-124	phospholipase D1	Rattus norvegicus	31-36
11359912-6	2001	In the three clones expressing rPLD1-V5, PLD activity stimulated by phorbol myristate acetate (PMA) or lysophosphatidic acid (LPA) was reduced by ~50%, while the PLD activity of Rat2V20 cells was normal.	lysophosphatidic acid	126-129	phospholipase D1	Rattus norvegicus	31-36
11311142-4	2001	Selection with phage display of different peptides of rPLD(1) confirmed that GTP-bound RhoA interacted with a site in the amino acid sequence 873-1024 at the C-terminus of rPLD(1).	Guanosine Triphosphate	77-80	phospholipase D1	Rattus norvegicus	54-61
11311142-4	2001	Selection with phage display of different peptides of rPLD(1) confirmed that GTP-bound RhoA interacted with a site in the amino acid sequence 873-1024 at the C-terminus of rPLD(1).	Guanosine Triphosphate	77-80	phospholipase D1	Rattus norvegicus	172-179
11311142-5	2001	RhoA also associated with this peptide in a GTP-dependent manner in COS-7 cell lysates and the peptide inhibited RhoA stimulation of PLD activity in membranes from COS-7 cells expressing rPLD(1).	Guanosine Triphosphate	44-47	phospholipase D1	Rattus norvegicus	187-194
11311142-5	2001	RhoA also associated with this peptide in a GTP-dependent manner in COS-7 cell lysates and the peptide inhibited RhoA stimulation of PLD activity in membranes from COS-7 cells expressing rPLD(1).	carbonyl sulfide	68-71	phospholipase D1	Rattus norvegicus	187-194
11311142-5	2001	RhoA also associated with this peptide in a GTP-dependent manner in COS-7 cell lysates and the peptide inhibited RhoA stimulation of PLD activity in membranes from COS-7 cells expressing rPLD(1).	carbonyl sulfide	164-167	phospholipase D1	Rattus norvegicus	187-194
11311142-9	2001	It is concluded that basic amino acids in a restricted C-terminal region of rPLD(1) are important for binding of RhoA and its activation of PLD activity.	Amino Acids, Basic	21-38	phospholipase D1	Rattus norvegicus	76-83
11121416-2	2001	The two halves of rPLD1 can associate in vivo, and the association is essential for catalytic activity and Ser/Thr phosphorylation of the enzyme.	Serine	107-110	phospholipase D1	Rattus norvegicus	18-23
11121416-2	2001	The two halves of rPLD1 can associate in vivo, and the association is essential for catalytic activity and Ser/Thr phosphorylation of the enzyme.	Threonine	111-114	phospholipase D1	Rattus norvegicus	18-23
11121416-3	2001	In this study, we found that this association is also required for palmitoylation of rPLD1, which occurs on cysteines 240 and 241.	Cysteine	108-117	phospholipase D1	Rattus norvegicus	85-90
11121416-8	2001	Wild type rPLD1 remains membrane-associated when extracted with 1 m NaCl or Na(2)CO(3) (pH 11), while rPLD1 mutants that lack palmitoylation are partially released.	Sodium Chloride	68-72	phospholipase D1	Rattus norvegicus	10-15
11121416-8	2001	Wild type rPLD1 remains membrane-associated when extracted with 1 m NaCl or Na(2)CO(3) (pH 11), while rPLD1 mutants that lack palmitoylation are partially released.	sodium sulfide	76-81	phospholipase D1	Rattus norvegicus	10-15
11121416-8	2001	Wild type rPLD1 remains membrane-associated when extracted with 1 m NaCl or Na(2)CO(3) (pH 11), while rPLD1 mutants that lack palmitoylation are partially released.	co(3)	81-86	phospholipase D1	Rattus norvegicus	10-15
11121416-10	2001	Characterization of the other cysteine mutations of rPLD1 showed that mutation of cysteine 310 or 612 to alanine increased basal phospholipase D activity 2- and 4-fold, respectively.	Cysteine	30-38	phospholipase D1	Rattus norvegicus	52-57
11121416-10	2001	Characterization of the other cysteine mutations of rPLD1 showed that mutation of cysteine 310 or 612 to alanine increased basal phospholipase D activity 2- and 4-fold, respectively.	Cysteine	82-90	phospholipase D1	Rattus norvegicus	52-57
11121416-10	2001	Characterization of the other cysteine mutations of rPLD1 showed that mutation of cysteine 310 or 612 to alanine increased basal phospholipase D activity 2- and 4-fold, respectively.	Alanine	105-112	phospholipase D1	Rattus norvegicus	52-57
11106425-4	2000	Serial deletion of the last four amino acids, EVWT, which are conserved in all mammalian PLD isoforms, abolished the catalytic activity of rPLD1.	evwt	46-50	phospholipase D1	Rattus norvegicus	139-144
10825182-8	2000	Furthermore, we found that rPLD1 could be modified by Ser/Thr phosphorylation.	Serine	54-57	phospholipase D1	Rattus norvegicus	27-32
10825182-8	2000	Furthermore, we found that rPLD1 could be modified by Ser/Thr phosphorylation.	Threonine	58-61	phospholipase D1	Rattus norvegicus	27-32
10441128-4	1999	For the first time, we have now identified multiple basal phophopeptides and multiple phorbol myristate acetate (PMA) induced phosphopeptides of endogenous PLD1 in 3Y1 cells as well as of transiently expressed PLD1 in COS-7 cells.	Tetradecanoylphorbol Acetate	86-111	phospholipase D1	Rattus norvegicus	156-160
10441128-4	1999	For the first time, we have now identified multiple basal phophopeptides and multiple phorbol myristate acetate (PMA) induced phosphopeptides of endogenous PLD1 in 3Y1 cells as well as of transiently expressed PLD1 in COS-7 cells.	Tetradecanoylphorbol Acetate	113-116	phospholipase D1	Rattus norvegicus	156-160
10441128-4	1999	For the first time, we have now identified multiple basal phophopeptides and multiple phorbol myristate acetate (PMA) induced phosphopeptides of endogenous PLD1 in 3Y1 cells as well as of transiently expressed PLD1 in COS-7 cells.	Tetradecanoylphorbol Acetate	113-116	phospholipase D1	Rattus norvegicus	210-214
10441128-9	1999	Interestingly, threonine 147 is located in the PX domain and serine 561 is in the negative regulatory "loop" region of PLD1.	Threonine	15-24	phospholipase D1	Rattus norvegicus	119-123
10441128-9	1999	Interestingly, threonine 147 is located in the PX domain and serine 561 is in the negative regulatory "loop" region of PLD1.	Serine	61-67	phospholipase D1	Rattus norvegicus	119-123
10441128-10	1999	Mutation of serine 2, threonine 147, or serine 561 significantly reduced PMA-induced PLD1 activity.	Serine	12-18	phospholipase D1	Rattus norvegicus	85-89
10441128-10	1999	Mutation of serine 2, threonine 147, or serine 561 significantly reduced PMA-induced PLD1 activity.	Threonine	22-31	phospholipase D1	Rattus norvegicus	85-89
10441128-10	1999	Mutation of serine 2, threonine 147, or serine 561 significantly reduced PMA-induced PLD1 activity.	Serine	40-46	phospholipase D1	Rattus norvegicus	85-89
10085097-1	1999	In the course of delineating the regulatory mechanism underlying phosphatidylinositol 3,4,5-trisphosphate (PI(3,4,5)P3) metabolism, we have discovered three distinct phosphoinositide-specific phospholipase D (PI-PLD) isozymes from rat brain, tentatively designated as PI-PLDa, PI-PLDb, and PI-PLDc.	phosphatidylinositol 3,4,5-triphosphate	65-105	phospholipase D1	Rattus norvegicus	271-275
10085097-1	1999	In the course of delineating the regulatory mechanism underlying phosphatidylinositol 3,4,5-trisphosphate (PI(3,4,5)P3) metabolism, we have discovered three distinct phosphoinositide-specific phospholipase D (PI-PLD) isozymes from rat brain, tentatively designated as PI-PLDa, PI-PLDb, and PI-PLDc.	phosphatidylinositol 3,4,5-triphosphate	65-105	phospholipase D1	Rattus norvegicus	280-284
10085097-1	1999	In the course of delineating the regulatory mechanism underlying phosphatidylinositol 3,4,5-trisphosphate (PI(3,4,5)P3) metabolism, we have discovered three distinct phosphoinositide-specific phospholipase D (PI-PLD) isozymes from rat brain, tentatively designated as PI-PLDa, PI-PLDb, and PI-PLDc.	phosphoinositide-3,4,5-triphosphate	107-118	phospholipase D1	Rattus norvegicus	271-275
10085097-1	1999	In the course of delineating the regulatory mechanism underlying phosphatidylinositol 3,4,5-trisphosphate (PI(3,4,5)P3) metabolism, we have discovered three distinct phosphoinositide-specific phospholipase D (PI-PLD) isozymes from rat brain, tentatively designated as PI-PLDa, PI-PLDb, and PI-PLDc.	phosphoinositide-3,4,5-triphosphate	107-118	phospholipase D1	Rattus norvegicus	280-284
10090765-2	1999	Previously we have demonstrated that protein kinase Calpha (PKCalpha) directly interacts with phospholipase D1 (PLD1), activating the enzymatic activity of PLD1 in the presence of phorbol 12-myristate 13-acetate (PMA) [Lee, T. G., et al.	Tetradecanoylphorbol Acetate	180-211	phospholipase D1	Rattus norvegicus	94-110
10090765-2	1999	Previously we have demonstrated that protein kinase Calpha (PKCalpha) directly interacts with phospholipase D1 (PLD1), activating the enzymatic activity of PLD1 in the presence of phorbol 12-myristate 13-acetate (PMA) [Lee, T. G., et al.	Tetradecanoylphorbol Acetate	180-211	phospholipase D1	Rattus norvegicus	112-116
10090765-2	1999	Previously we have demonstrated that protein kinase Calpha (PKCalpha) directly interacts with phospholipase D1 (PLD1), activating the enzymatic activity of PLD1 in the presence of phorbol 12-myristate 13-acetate (PMA) [Lee, T. G., et al.	Tetradecanoylphorbol Acetate	180-211	phospholipase D1	Rattus norvegicus	156-160
10090765-2	1999	Previously we have demonstrated that protein kinase Calpha (PKCalpha) directly interacts with phospholipase D1 (PLD1), activating the enzymatic activity of PLD1 in the presence of phorbol 12-myristate 13-acetate (PMA) [Lee, T. G., et al.	Tetradecanoylphorbol Acetate	213-216	phospholipase D1	Rattus norvegicus	94-110
10090765-2	1999	Previously we have demonstrated that protein kinase Calpha (PKCalpha) directly interacts with phospholipase D1 (PLD1), activating the enzymatic activity of PLD1 in the presence of phorbol 12-myristate 13-acetate (PMA) [Lee, T. G., et al.	Tetradecanoylphorbol Acetate	213-216	phospholipase D1	Rattus norvegicus	112-116
10090765-2	1999	Previously we have demonstrated that protein kinase Calpha (PKCalpha) directly interacts with phospholipase D1 (PLD1), activating the enzymatic activity of PLD1 in the presence of phorbol 12-myristate 13-acetate (PMA) [Lee, T. G., et al.	Tetradecanoylphorbol Acetate	213-216	phospholipase D1	Rattus norvegicus	156-160
10090765-10	1999	PMA elicits translocation of PKCalpha to the CEMs, inducing PLD activation through the interaction of PKCalpha with PLD1 in the CEMs.	Tetradecanoylphorbol Acetate	0-3	phospholipase D1	Rattus norvegicus	116-120
9989263-3	1999	Upon treatment with phorbol myristate acetate (PMA), PKC alpha translocated from the cytosolic fraction to the membrane fraction to which PLD1 also localized.	Tetradecanoylphorbol Acetate	20-45	phospholipase D1	Rattus norvegicus	138-142
9989263-3	1999	Upon treatment with phorbol myristate acetate (PMA), PKC alpha translocated from the cytosolic fraction to the membrane fraction to which PLD1 also localized.	Tetradecanoylphorbol Acetate	47-50	phospholipase D1	Rattus norvegicus	138-142
10919268-4	2000	PLD1 can induce phosphatidic acid formation and subsequent activation of protein kinase C, a process which stimulates insulin release.	Phosphatidic Acids	16-33	phospholipase D1	Rattus norvegicus	0-4
10919268-8	2000	NG-methyl-L-arginine (LMA), a blocker of the inducible form of nitric oxide synthase (iNOS), prevented this late inhibitory effect of IL-1beta, suggesting that IL-1beta-induced decrease in PLD1a expression is NO-mediated.	ng-methyl-l-arginine	0-20	phospholipase D1	Rattus norvegicus	189-194
10919268-8	2000	NG-methyl-L-arginine (LMA), a blocker of the inducible form of nitric oxide synthase (iNOS), prevented this late inhibitory effect of IL-1beta, suggesting that IL-1beta-induced decrease in PLD1a expression is NO-mediated.	dodecyl methacrylate	22-25	phospholipase D1	Rattus norvegicus	189-194
10832096-6	2000	We conclude that, in astrocytes, the PLD isoform which is activated by phorbol ester requires PKC, ARF and Rho proteins for full activity and probably represents PLD1.	Phorbol Esters	71-84	phospholipase D1	Rattus norvegicus	162-166
9856987-3	1998	Deletion mutants of rPLD1 that contained only an N- or C-terminal HKD domain exhibited no catalytic activity when expressed in COS 7 cells.	carbonyl sulfide	127-130	phospholipase D1	Rattus norvegicus	20-25
9856987-6	1998	In addition, deletion of 168 amino acids from the N terminus of rPLD1 significantly enhanced basal PLD activity while inhibiting the response to phorbol ester.	Phorbol Esters	145-158	phospholipase D1	Rattus norvegicus	64-69
9792719-2	1998	In the presence of vanadate, H2O2 induced tyrosine phosphorylation of PLD as well as the platelet-derived growth (PDGF) factor receptor, protein kinase Calpha (PKCalpha), and a 62-kDa protein in rat brain PLD1 (rPLD1) immune complexes.	Vanadates	19-27	phospholipase D1	Rattus norvegicus	205-209
9792719-2	1998	In the presence of vanadate, H2O2 induced tyrosine phosphorylation of PLD as well as the platelet-derived growth (PDGF) factor receptor, protein kinase Calpha (PKCalpha), and a 62-kDa protein in rat brain PLD1 (rPLD1) immune complexes.	Vanadates	19-27	phospholipase D1	Rattus norvegicus	211-216
9792719-2	1998	In the presence of vanadate, H2O2 induced tyrosine phosphorylation of PLD as well as the platelet-derived growth (PDGF) factor receptor, protein kinase Calpha (PKCalpha), and a 62-kDa protein in rat brain PLD1 (rPLD1) immune complexes.	Hydrogen Peroxide	29-33	phospholipase D1	Rattus norvegicus	205-209
9792719-2	1998	In the presence of vanadate, H2O2 induced tyrosine phosphorylation of PLD as well as the platelet-derived growth (PDGF) factor receptor, protein kinase Calpha (PKCalpha), and a 62-kDa protein in rat brain PLD1 (rPLD1) immune complexes.	Hydrogen Peroxide	29-33	phospholipase D1	Rattus norvegicus	211-216
9792719-5	1998	Stimulation by H2O2 showed a concentration- and time-dependent tyrosine phosphorylation of the proteins in rPLD1 immunoprecipitates and activation of PLD in the cells.	Hydrogen Peroxide	15-19	phospholipase D1	Rattus norvegicus	107-112
9792719-5	1998	Stimulation by H2O2 showed a concentration- and time-dependent tyrosine phosphorylation of the proteins in rPLD1 immunoprecipitates and activation of PLD in the cells.	Tyrosine	63-71	phospholipase D1	Rattus norvegicus	107-112
9792719-10	1998	Reduction of intracellular H2O2 levels by pretreatment of the cells with catalase dramatically abrogated tyrosine phosphorylation of proteins in the rPLD1 immune complex and PLD activation, suggesting the potential role of intracellular H2O2 in H2O2-mediated PLD signaling.	Hydrogen Peroxide	27-31	phospholipase D1	Rattus norvegicus	149-154
9792719-10	1998	Reduction of intracellular H2O2 levels by pretreatment of the cells with catalase dramatically abrogated tyrosine phosphorylation of proteins in the rPLD1 immune complex and PLD activation, suggesting the potential role of intracellular H2O2 in H2O2-mediated PLD signaling.	Tyrosine	105-113	phospholipase D1	Rattus norvegicus	149-154
9792719-10	1998	Reduction of intracellular H2O2 levels by pretreatment of the cells with catalase dramatically abrogated tyrosine phosphorylation of proteins in the rPLD1 immune complex and PLD activation, suggesting the potential role of intracellular H2O2 in H2O2-mediated PLD signaling.	Hydrogen Peroxide	237-241	phospholipase D1	Rattus norvegicus	149-154
9792719-10	1998	Reduction of intracellular H2O2 levels by pretreatment of the cells with catalase dramatically abrogated tyrosine phosphorylation of proteins in the rPLD1 immune complex and PLD activation, suggesting the potential role of intracellular H2O2 in H2O2-mediated PLD signaling.	Hydrogen Peroxide	237-241	phospholipase D1	Rattus norvegicus	149-154
9703960-2	1998	In this study, a PLD isoform (rPLD1) was shown to bind to PKC-alpha in Rat1 fibroblasts treated with phorbol ester.	Phorbol Esters	101-114	phospholipase D1	Rattus norvegicus	30-35
9703960-6	1998	p220 was phosphorylated on serine/threonine in PMA-stimulated Rat1 cells, and rPLD1 expressed in Sf9 cells was also serine/threonine phosphorylated in response to PMA treatment.	Serine	116-122	phospholipase D1	Rattus norvegicus	78-83
9703960-6	1998	p220 was phosphorylated on serine/threonine in PMA-stimulated Rat1 cells, and rPLD1 expressed in Sf9 cells was also serine/threonine phosphorylated in response to PMA treatment.	Threonine	123-132	phospholipase D1	Rattus norvegicus	78-83
9703960-7	1998	These data suggest the PMA induces the formation of a RPLD1/PKC alpha/P220 complex in cells, some components of which undergo serine/threonine phosphorylation.	Serine	126-132	phospholipase D1	Rattus norvegicus	54-59
9703960-7	1998	These data suggest the PMA induces the formation of a RPLD1/PKC alpha/P220 complex in cells, some components of which undergo serine/threonine phosphorylation.	Threonine	133-142	phospholipase D1	Rattus norvegicus	54-59
9295164-0	1997	Phorbol myristate acetate-dependent association of protein kinase C alpha with phospholipase D1 in intact cells.	Tetradecanoylphorbol Acetate	0-25	phospholipase D1	Rattus norvegicus	79-95
9507013-3	1998	We have expressed rPLD1 as a histidine-tagged fusion protein in insect (Sf9) cells using the expression vector pBlueBacHis and purified the recombinant protein to homogeneity by Ni2+-agarose affinity chromatography.	Histidine	29-38	phospholipase D1	Rattus norvegicus	18-23
9507013-3	1998	We have expressed rPLD1 as a histidine-tagged fusion protein in insect (Sf9) cells using the expression vector pBlueBacHis and purified the recombinant protein to homogeneity by Ni2+-agarose affinity chromatography.	ni2+-agarose	178-190	phospholipase D1	Rattus norvegicus	18-23
9507013-5	1998	The activity of rPLD1 was dependent on both Mg2+ and Ca2+.	magnesium ion	44-48	phospholipase D1	Rattus norvegicus	16-21
9507013-8	1998	Protein kinase C (PKC)-alpha and -betaII, but not PKC-gamma, -delta, -epsilon, or -zeta, activated rPLD1 in a manner that was stimulated by phorbol ester but did not require ATP.	Phorbol Esters	140-153	phospholipase D1	Rattus norvegicus	99-104
9507013-12	1998	rPLD1 bound to concanavalin A-Sepharose beads, and its electrophoretic mobility was altered by treatment with endoglycosidase F. The amount of PLD bound to the beads was decreased in a concentration-dependent manner when tunicamycin was added to the Sf9 expression system.	Sepharose	30-39	phospholipase D1	Rattus norvegicus	0-5
9507013-12	1998	rPLD1 bound to concanavalin A-Sepharose beads, and its electrophoretic mobility was altered by treatment with endoglycosidase F. The amount of PLD bound to the beads was decreased in a concentration-dependent manner when tunicamycin was added to the Sf9 expression system.	Tunicamycin	221-232	phospholipase D1	Rattus norvegicus	0-5
9507013-13	1998	Tunicamycin also decreased membrane localization of rPLD1.	Tunicamycin	0-11	phospholipase D1	Rattus norvegicus	52-57
9478920-3	1998	Expression of the constitutively active Q226L mutant of the alpha-subunit of G13 in COS-7 cells stimulated the activity of a rat brain phospholipase D isozyme (rPLD1) co-expressed in the cells.	carbonyl sulfide	84-87	phospholipase D1	Rattus norvegicus	160-165
9445394-12	1998	Both of the rat PLD1 isoforms expressed in the fission yeast Schizosaccharomyces pombe were dependent on ADP-ribosylation factor 1 and phosphatidylinositol 4,5-bisphosphate.	Phosphatidylinositol 4,5-Diphosphate	135-172	phospholipase D1	Rattus norvegicus	16-20
9514932-0	1998	Definition of the protein kinase C interaction site of phospholipase D. Serial deletions of the N-terminal 319 amino acids of rPLD1 expressed in COS-7 cells resulted in increased basal PLD activity.	carbonyl sulfide	145-148	phospholipase D1	Rattus norvegicus	126-131
9514932-0	1998	Definition of the protein kinase C interaction site of phospholipase D. Serial deletions of the N-terminal 319 amino acids of rPLD1 expressed in COS-7 cells resulted in increased basal PLD activity.	carbonyl sulfide	145-148	phospholipase D1	Rattus norvegicus	127-130
9514932-1	1998	Incubation of the cells with phorbol myristate acetate increased the activity of endogenous and wild-type rPLD1.	Tetradecanoylphorbol Acetate	29-54	phospholipase D1	Rattus norvegicus	106-111
9514932-2	1998	The mutant rPLD1 with deletion of the first 50 amino acids responded to the phorbol ester, however, rPLD1 with deletions of 115 amino acids or more did not.	Phorbol Esters	76-89	phospholipase D1	Rattus norvegicus	11-16
9514932-5	1998	When myristoylated ADP-ribosylation factor 3 (mARF3) was added together with guanosine 5"-3-O-(thio)triphosphate, all mutants showed stimulation of PLD activity.	Guanosine 5'-O-(3-Thiotriphosphate)	77-112	phospholipase D1	Rattus norvegicus	148-151
9295164-1	1997	A phospholipase D1 (PLD1) was purified from rat brain by the use of antibody-coupled protein A Sepharose.	Sepharose	95-104	phospholipase D1	Rattus norvegicus	2-18
9295164-1	1997	A phospholipase D1 (PLD1) was purified from rat brain by the use of antibody-coupled protein A Sepharose.	Sepharose	95-104	phospholipase D1	Rattus norvegicus	20-24
9295164-2	1997	We found that protein kinase C alp (PKCalpha) stimulated PLD1 activity in the presence of phorbol myristate acetate (PMA).	Tetradecanoylphorbol Acetate	90-115	phospholipase D1	Rattus norvegicus	57-61
9295164-2	1997	We found that protein kinase C alp (PKCalpha) stimulated PLD1 activity in the presence of phorbol myristate acetate (PMA).	Tetradecanoylphorbol Acetate	117-120	phospholipase D1	Rattus norvegicus	57-61
8753790-4	1996	RT-PCR using non-degenerate primers showed that rPLDa mRNA increased within 12h following treatment with dbcAMP, reaching a broad plateau and then returned to the initial level at 48h.	Bucladesine	105-111	phospholipase D1	Rattus norvegicus	48-53