PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
10899948-1	2000	Aromatic L-amino acid decarboxylase (AAAD), an enzyme required for the synthesis of catecholamines, indoleamines, and trace amines, is rapidly activated by cyclic AMP-dependent pathways in striatum and midbrain in vivo, suggesting enzyme phosphorylation.	Cyclic AMP	156-166	dopa decarboxylase	Mus musculus	0-35	
10899948-1	2000	Aromatic L-amino acid decarboxylase (AAAD), an enzyme required for the synthesis of catecholamines, indoleamines, and trace amines, is rapidly activated by cyclic AMP-dependent pathways in striatum and midbrain in vivo, suggesting enzyme phosphorylation.	Cyclic AMP	156-166	dopa decarboxylase	Mus musculus	37-41	
10899948-7	2000	A direct phosphorylation of AAAD protein by PKA might underlie the cyclic AMP-induced rapid and transient activation of AAAD in vivo.	Cyclic AMP	67-77	dopa decarboxylase	Mus musculus	28-32	
10899948-7	2000	A direct phosphorylation of AAAD protein by PKA might underlie the cyclic AMP-induced rapid and transient activation of AAAD in vivo.	Cyclic AMP	67-77	dopa decarboxylase	Mus musculus	120-124	
8388038-0	1993	Evidence for cyclic AMP-mediated increase of aromatic L-amino acid decarboxylase activity in the striatum and midbrain.	Cyclic AMP	13-23	dopa decarboxylase	Mus musculus	45-80	
8388038-5	1993	We conclude that AAAD activity of striatum and midbrain can be modulated by a cyclic AMP-dependent process.	Cyclic AMP	78-88	dopa decarboxylase	Mus musculus	17-21