PMID-sentid	Pub_year	Sent_text	comp_official_name	comp_offset	protein_name	organism	prot_offset
17467927-1	2007	Calmodulin-dependent cyclic nucleotide phopshodiesterase (PDE1) has been extensively characterized and is a key enzyme involved in the complex interaction between cyclic nucleotide and Ca(2+) second-messenger systems.	Nucleotides, Cyclic	21-38	phosphodiesterase 1A	Bos taurus	58-62
17467927-1	2007	Calmodulin-dependent cyclic nucleotide phopshodiesterase (PDE1) has been extensively characterized and is a key enzyme involved in the complex interaction between cyclic nucleotide and Ca(2+) second-messenger systems.	Nucleotides, Cyclic	163-180	phosphodiesterase 1A	Bos taurus	58-62
17400261-3	2007	The most active natural inhibitors of the system CaM-PDE1 were benzyl benzoates 3-5, which inhibited the activity of PDE1 in a concentration-dependent manner.	benzyl benzoate	63-79	phosphodiesterase 1A	Bos taurus	53-57
17400261-3	2007	The most active natural inhibitors of the system CaM-PDE1 were benzyl benzoates 3-5, which inhibited the activity of PDE1 in a concentration-dependent manner.	benzyl benzoate	63-79	phosphodiesterase 1A	Bos taurus	117-121
16780358-15	2006	The results show YTX affinity by cyclic nucleotide PDE 1, PDE 3, PDE 4, and exonuclease PDE I.	yessotoxin	17-20	phosphodiesterase 1A	Bos taurus	51-56
16780358-15	2006	The results show YTX affinity by cyclic nucleotide PDE 1, PDE 3, PDE 4, and exonuclease PDE I.	Nucleotides, Cyclic	33-50	phosphodiesterase 1A	Bos taurus	51-56
15599707-8	2004	Hesperetin preferentially inhibited calmodulin (CaM)-activated PDE1 and PDE4 isolated from bovine aorta with IC(50) values of about 74 microM and 70 microM respectively.	hesperetin	0-10	phosphodiesterase 1A	Bos taurus	63-67
15599707-10	2004	These results suggest that the vasorelaxant effects of hesperetin are basically due to the inhibition of PDE1 and PDE4 activities.	hesperetin	55-65	phosphodiesterase 1A	Bos taurus	105-109
15302227-6	2004	The cAMP degradation by purified bovine brain PDE was partially suppressed by PDE1 inhibitor vinpocetin, PDE2 inhibitor erythro-9-(2-hydroxy-3-nonyl)adenine hydrochloride and PDE4 inhibitor rolipram but not by PDE3 inhibitor cilostamide, and completely inhibited by 3-isobutyl-1-methylxanthine, suggesting that is attributed almost exclusively to PDE1, PDE2 and PDE4.	Cyclic AMP	4-8	phosphodiesterase 1A	Bos taurus	78-82
15302227-6	2004	The cAMP degradation by purified bovine brain PDE was partially suppressed by PDE1 inhibitor vinpocetin, PDE2 inhibitor erythro-9-(2-hydroxy-3-nonyl)adenine hydrochloride and PDE4 inhibitor rolipram but not by PDE3 inhibitor cilostamide, and completely inhibited by 3-isobutyl-1-methylxanthine, suggesting that is attributed almost exclusively to PDE1, PDE2 and PDE4.	Cyclic AMP	4-8	phosphodiesterase 1A	Bos taurus	347-351
15302227-6	2004	The cAMP degradation by purified bovine brain PDE was partially suppressed by PDE1 inhibitor vinpocetin, PDE2 inhibitor erythro-9-(2-hydroxy-3-nonyl)adenine hydrochloride and PDE4 inhibitor rolipram but not by PDE3 inhibitor cilostamide, and completely inhibited by 3-isobutyl-1-methylxanthine, suggesting that is attributed almost exclusively to PDE1, PDE2 and PDE4.	vinpocetine	93-103	phosphodiesterase 1A	Bos taurus	78-82
15302227-6	2004	The cAMP degradation by purified bovine brain PDE was partially suppressed by PDE1 inhibitor vinpocetin, PDE2 inhibitor erythro-9-(2-hydroxy-3-nonyl)adenine hydrochloride and PDE4 inhibitor rolipram but not by PDE3 inhibitor cilostamide, and completely inhibited by 3-isobutyl-1-methylxanthine, suggesting that is attributed almost exclusively to PDE1, PDE2 and PDE4.	Rolipram	190-198	phosphodiesterase 1A	Bos taurus	78-82
15302227-6	2004	The cAMP degradation by purified bovine brain PDE was partially suppressed by PDE1 inhibitor vinpocetin, PDE2 inhibitor erythro-9-(2-hydroxy-3-nonyl)adenine hydrochloride and PDE4 inhibitor rolipram but not by PDE3 inhibitor cilostamide, and completely inhibited by 3-isobutyl-1-methylxanthine, suggesting that is attributed almost exclusively to PDE1, PDE2 and PDE4.	cilostamide	225-236	phosphodiesterase 1A	Bos taurus	78-82
15302227-6	2004	The cAMP degradation by purified bovine brain PDE was partially suppressed by PDE1 inhibitor vinpocetin, PDE2 inhibitor erythro-9-(2-hydroxy-3-nonyl)adenine hydrochloride and PDE4 inhibitor rolipram but not by PDE3 inhibitor cilostamide, and completely inhibited by 3-isobutyl-1-methylxanthine, suggesting that is attributed almost exclusively to PDE1, PDE2 and PDE4.	1-Methyl-3-isobutylxanthine	266-293	phosphodiesterase 1A	Bos taurus	78-82
15302227-9	2004	The cAMP degradation by bovine heart PDE was almost completely inhibited by the combination with vinpocetine and cilostamide, indicating that is mediated almost exclusively by PDE1 and PDE3.	Cyclic AMP	4-8	phosphodiesterase 1A	Bos taurus	176-180
15302227-9	2004	The cAMP degradation by bovine heart PDE was almost completely inhibited by the combination with vinpocetine and cilostamide, indicating that is mediated almost exclusively by PDE1 and PDE3.	vinpocetine	97-108	phosphodiesterase 1A	Bos taurus	176-180
15302227-9	2004	The cAMP degradation by bovine heart PDE was almost completely inhibited by the combination with vinpocetine and cilostamide, indicating that is mediated almost exclusively by PDE1 and PDE3.	cilostamide	113-124	phosphodiesterase 1A	Bos taurus	176-180
22900295-1	2003	Calmodulin(CaM)-dependent cyclic nucleotide phosphodiesterase (PDE1) plays a critical role in the complex interactions between the cyclic nucleotide and Ca(2+) second messenger systems.	Nucleotides, Cyclic	26-43	phosphodiesterase 1A	Bos taurus	63-67
22900295-6	2003	Another main difference is that 60 kDa PDE1 isozyme is a substrate of cAMP-dependent protein kinase, whereas, 63 kDa PDE1 isozyme is phosphorylated by CaM-dependent protein kinase.	Cyclic AMP	70-74	phosphodiesterase 1A	Bos taurus	39-43
22900295-6	2003	Another main difference is that 60 kDa PDE1 isozyme is a substrate of cAMP-dependent protein kinase, whereas, 63 kDa PDE1 isozyme is phosphorylated by CaM-dependent protein kinase.	Cyclic AMP	70-74	phosphodiesterase 1A	Bos taurus	117-121
22900295-8	2003	The complex regulatory properties of PDE1 isozymes are precisely regulated by cross-talk between the Ca(2+) and cAMP signaling pathways.	Cyclic AMP	112-116	phosphodiesterase 1A	Bos taurus	37-41
12514091-14	2003	Although cAMP regulation by PDE 1 may occur early during capacitation, downstream events appear to prevent full capacitation from occurring prematurely.	Cyclic AMP	9-13	phosphodiesterase 1A	Bos taurus	28-33
10965223-3	2000	These increases were due to: (1) increased number of spindle PDE isozymes in the cytosolic fraction (for cAMP: PDE1, PDE2, PDE3 and PDE4 compared to PDE2 and PDE4 in cobblestone; for cGMP: PDE2 and PDE5 compared to PDE2 in cobblestone); (2) increased spindle-specific activities of cytosolic and particulate PDE2, cytosolic PDE3 and particulate PDE4.	Cyclic AMP	105-109	phosphodiesterase 1A	Bos taurus	111-115
9419816-4	1997	In addition, the enzymatic activity of HSPDE1B1 was inhibited by phosphodiesterase inhibitors with potencies similar to that displayed toward the bovine PDE1 enzymes: IBMX approximately equal to 8-methoxymethyl-IBMX > vinpocetine approximately equal to zaprinast > cilostamide > rolipram.	MMPX	195-215	phosphodiesterase 1A	Bos taurus	41-45
9419816-4	1997	In addition, the enzymatic activity of HSPDE1B1 was inhibited by phosphodiesterase inhibitors with potencies similar to that displayed toward the bovine PDE1 enzymes: IBMX approximately equal to 8-methoxymethyl-IBMX > vinpocetine approximately equal to zaprinast > cilostamide > rolipram.	vinpocetine	221-232	phosphodiesterase 1A	Bos taurus	41-45
9419816-4	1997	In addition, the enzymatic activity of HSPDE1B1 was inhibited by phosphodiesterase inhibitors with potencies similar to that displayed toward the bovine PDE1 enzymes: IBMX approximately equal to 8-methoxymethyl-IBMX > vinpocetine approximately equal to zaprinast > cilostamide > rolipram.	zaprinast	256-265	phosphodiesterase 1A	Bos taurus	41-45
9419816-4	1997	In addition, the enzymatic activity of HSPDE1B1 was inhibited by phosphodiesterase inhibitors with potencies similar to that displayed toward the bovine PDE1 enzymes: IBMX approximately equal to 8-methoxymethyl-IBMX > vinpocetine approximately equal to zaprinast > cilostamide > rolipram.	cilostamide	271-282	phosphodiesterase 1A	Bos taurus	41-45
9419816-4	1997	In addition, the enzymatic activity of HSPDE1B1 was inhibited by phosphodiesterase inhibitors with potencies similar to that displayed toward the bovine PDE1 enzymes: IBMX approximately equal to 8-methoxymethyl-IBMX > vinpocetine approximately equal to zaprinast > cilostamide > rolipram.	Rolipram	288-296	phosphodiesterase 1A	Bos taurus	41-45
8043581-6	1994	In the present study, purified 61-kDa CaM-PDE was phosphorylated in the presence of [gamma-32P]ATP and cleaved with a Lys-C endoproteinase.	[gamma-32p]atp	84-98	phosphodiesterase 1A	Bos taurus	31-45
8043581-17	1994	We conclude that phosphorylation of serine 120 by PKA is responsible for the reduction in affinity of the 61-kDa CaM-PDE for CaM.	Serine	36-42	phosphodiesterase 1A	Bos taurus	106-120
27548062-4	2016	The PDE superfamily is subdivided into 11 families (PDE1 to 11), which act on either cAMP or cGMP, or on both cAMP and cGMP although with different enzymatic properties.	Cyclic AMP	85-89	phosphodiesterase 1A	Bos taurus	52-56
27548062-4	2016	The PDE superfamily is subdivided into 11 families (PDE1 to 11), which act on either cAMP or cGMP, or on both cAMP and cGMP although with different enzymatic properties.	Cyclic GMP	93-97	phosphodiesterase 1A	Bos taurus	52-56
27548062-4	2016	The PDE superfamily is subdivided into 11 families (PDE1 to 11), which act on either cAMP or cGMP, or on both cAMP and cGMP although with different enzymatic properties.	Cyclic AMP	110-114	phosphodiesterase 1A	Bos taurus	52-56
27548062-4	2016	The PDE superfamily is subdivided into 11 families (PDE1 to 11), which act on either cAMP or cGMP, or on both cAMP and cGMP although with different enzymatic properties.	Cyclic GMP	119-123	phosphodiesterase 1A	Bos taurus	52-56
26513204-2	2016	The presence of PDE1 hydrolyzing both cyclic nucleotides in BTSM strips was revealed.	Nucleotides, Cyclic	38-56	phosphodiesterase 1A	Bos taurus	16-20
26513204-3	2016	Moreover, a vinpocetine and muscarinic antagonists inhibited PDE1 located at plasma membranes (PM) fractions from BTSM showing such inhibition, an M(2)AChR pharmacological profile.	vinpocetine	12-23	phosphodiesterase 1A	Bos taurus	61-65
26513204-4	2016	Therefore, a novel Ca(2+)/CaM dependent and vinpocetine inhibited PDE1 was purified and characterized at PM fractions from BTSM.	vinpocetine	44-55	phosphodiesterase 1A	Bos taurus	66-70
26513204-5	2016	This PDE1 activity was removed from PM fractions using a hypotonic buffer and purified some 38 fold using two columns (Q-Sepharose and CaM-agarose).	q-sepharose	119-130	phosphodiesterase 1A	Bos taurus	5-9
26513204-5	2016	This PDE1 activity was removed from PM fractions using a hypotonic buffer and purified some 38 fold using two columns (Q-Sepharose and CaM-agarose).	cam-agarose	135-146	phosphodiesterase 1A	Bos taurus	5-9
26513204-6	2016	This PDE1 was stimulated by CaM and inhibited by vinpocetine showing two bands in PAGE-SDS (56, 58 kDa) being the 58 kDa identified as PDE1A by Western blotts.	cafestol palmitate	28-31	phosphodiesterase 1A	Bos taurus	5-9
26513204-6	2016	This PDE1 was stimulated by CaM and inhibited by vinpocetine showing two bands in PAGE-SDS (56, 58 kDa) being the 58 kDa identified as PDE1A by Western blotts.	cafestol palmitate	28-31	phosphodiesterase 1A	Bos taurus	135-140
26513204-6	2016	This PDE1 was stimulated by CaM and inhibited by vinpocetine showing two bands in PAGE-SDS (56, 58 kDa) being the 58 kDa identified as PDE1A by Western blotts.	vinpocetine	49-60	phosphodiesterase 1A	Bos taurus	5-9
26513204-6	2016	This PDE1 was stimulated by CaM and inhibited by vinpocetine showing two bands in PAGE-SDS (56, 58 kDa) being the 58 kDa identified as PDE1A by Western blotts.	vinpocetine	49-60	phosphodiesterase 1A	Bos taurus	135-140
26513204-6	2016	This PDE1 was stimulated by CaM and inhibited by vinpocetine showing two bands in PAGE-SDS (56, 58 kDa) being the 58 kDa identified as PDE1A by Western blotts.	Sodium Dodecyl Sulfate	87-90	phosphodiesterase 1A	Bos taurus	5-9
26513204-6	2016	This PDE1 was stimulated by CaM and inhibited by vinpocetine showing two bands in PAGE-SDS (56, 58 kDa) being the 58 kDa identified as PDE1A by Western blotts.	Sodium Dodecyl Sulfate	87-90	phosphodiesterase 1A	Bos taurus	135-140
26513204-7	2016	This PDE1A activity was assayed with [(3)H]cGMP and [(3)H]cAMP exhibiting a higher affinity as Km (muM) for cGMP than cAMP but being close values with V(max) cAMP/cGMP ratio of 1.5.	Cyclic GMP	43-47	phosphodiesterase 1A	Bos taurus	5-10
26513204-7	2016	This PDE1A activity was assayed with [(3)H]cGMP and [(3)H]cAMP exhibiting a higher affinity as Km (muM) for cGMP than cAMP but being close values with V(max) cAMP/cGMP ratio of 1.5.	Cyclic AMP	58-62	phosphodiesterase 1A	Bos taurus	5-10
26513204-7	2016	This PDE1A activity was assayed with [(3)H]cGMP and [(3)H]cAMP exhibiting a higher affinity as Km (muM) for cGMP than cAMP but being close values with V(max) cAMP/cGMP ratio of 1.5.	Cyclic GMP	108-112	phosphodiesterase 1A	Bos taurus	5-10
26513204-7	2016	This PDE1A activity was assayed with [(3)H]cGMP and [(3)H]cAMP exhibiting a higher affinity as Km (muM) for cGMP than cAMP but being close values with V(max) cAMP/cGMP ratio of 1.5.	Cyclic AMP	118-122	phosphodiesterase 1A	Bos taurus	5-10
26513204-7	2016	This PDE1A activity was assayed with [(3)H]cGMP and [(3)H]cAMP exhibiting a higher affinity as Km (muM) for cGMP than cAMP but being close values with V(max) cAMP/cGMP ratio of 1.5.	Cyclic AMP	118-122	phosphodiesterase 1A	Bos taurus	5-10
26513204-7	2016	This PDE1A activity was assayed with [(3)H]cGMP and [(3)H]cAMP exhibiting a higher affinity as Km (muM) for cGMP than cAMP but being close values with V(max) cAMP/cGMP ratio of 1.5.	Cyclic GMP	108-112	phosphodiesterase 1A	Bos taurus	5-10
26513204-10	2016	CaM stimulated the cyclic nucleotides hydrolysis by PDE1A exhibiting similar activation constant as K(CaM), in nM range.	cafestol palmitate	0-3	phosphodiesterase 1A	Bos taurus	52-57
26513204-10	2016	CaM stimulated the cyclic nucleotides hydrolysis by PDE1A exhibiting similar activation constant as K(CaM), in nM range.	Nucleotides, Cyclic	19-37	phosphodiesterase 1A	Bos taurus	52-57
26513204-10	2016	CaM stimulated the cyclic nucleotides hydrolysis by PDE1A exhibiting similar activation constant as K(CaM), in nM range.	cafestol palmitate	102-105	phosphodiesterase 1A	Bos taurus	52-57
26513204-11	2016	The original finding was the identification and purification of a vinpocetine and muscarinic antagonist-inhibited and CaM-activated PM-bound PDE1A, linked to M(2)AChR.	vinpocetine	66-77	phosphodiesterase 1A	Bos taurus	141-146