PMID-sentid	Pub_year	Sent_text	compound_name	comp_offset	prot_official_name	organism	prot_offset
2522991-0	1989	Resolved N,N-dialkylated 2-amino-8-hydroxytetralins: stereoselective interactions with 5-HT1A receptors in the brain.	n,n	9-12	5-hydroxytryptamine receptor 1A	Rattus norvegicus	87-93
16078841-6	2005	Although the K(i) value of the inhibitor is in the micromolar range, it is more potent than N,N-bis(2-chloroethyl)-N-nitrosourea, which is currently the most commonly employed irreversible GR inhibitor with a reported IC(50) value of 646 microM.	n,n	92-95	glutathione-disulfide reductase	Homo sapiens	189-191
12773035-2	2003	Novel 2,4-diaminopyrimidines bearing N,N-disubstituted aminomethyl residues at the 5-position were designed as dihydrofolate reductase (DHFR) inhibitors.	n,n	37-40	dihydrofolate reductase	Homo sapiens	111-134
12773035-2	2003	Novel 2,4-diaminopyrimidines bearing N,N-disubstituted aminomethyl residues at the 5-position were designed as dihydrofolate reductase (DHFR) inhibitors.	n,n	37-40	dihydrofolate reductase	Homo sapiens	136-140
2139186-8	1990	The size of the N,N-dialkyl substituent was a secondary determinant of affinity, with groups larger than N,N-diisopropyl resulting in a marked reduction in affinity at both the 5-HT2A and 5-HT1A recognition sites.	n,n	16-19	5-hydroxytryptamine receptor 2A	Rattus norvegicus	177-183
2139186-8	1990	The size of the N,N-dialkyl substituent was a secondary determinant of affinity, with groups larger than N,N-diisopropyl resulting in a marked reduction in affinity at both the 5-HT2A and 5-HT1A recognition sites.	n,n	16-19	5-hydroxytryptamine receptor 1A	Rattus norvegicus	188-194
27934012-4	2016	Additionally the N,N-dimethylamino PMO-DNA chimeras were found to stimulate RNaseH1 activity.	n,n	17-20	ribonuclease H1	Homo sapiens	76-83
7844046-5	1994	The compound possessing an N,N-dimethylcarbamoyloxy moiety at the C-3 position showed good oral absorption and well-balanced antibacterial activity.	n,n	27-30	complement C3	Homo sapiens	66-69
6962833-2	1982	It was found that the binding ability with the ACM antisera was markedly decreased by the following structural changes in ACM: N,N-didemethylation of the rhodosamine moiety; 6-O- or 4-O-methylation; removal of the methoxycarbonyl group at C-10; hydroxylation at C-1, C-2 or C-11.	n,n	127-130	complement C2	Oryctolagus cuniculus	267-270