PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
18024134-4	2008	A hypothesis for the reduced hPNMT inhibitory potency of these compounds has been formed on the basis of molecular modeling and docking studies using the X-ray crystal structures of hPNMT co-crystallized with THIQ-type inhibitors and S-adenosyl-L-homocysteine as a template.	1,2,3,4-tetrahydroisoquinoline	209-213	phenylethanolamine N-methyltransferase	Homo sapiens	29-34	
18024134-4	2008	A hypothesis for the reduced hPNMT inhibitory potency of these compounds has been formed on the basis of molecular modeling and docking studies using the X-ray crystal structures of hPNMT co-crystallized with THIQ-type inhibitors and S-adenosyl-L-homocysteine as a template.	1,2,3,4-tetrahydroisoquinoline	209-213	phenylethanolamine N-methyltransferase	Homo sapiens	182-187	
17126018-2	2007	Docking studies indicated that the enhanced PNMT inhibitory potency of 11 (hPNMT K(i)=0.49microM) versus 1,2,3,4-tetrahydroisoquinoline (5, hPNMT K(i)=5.8microM) was likely due to hydrophobic interactions with Val53, Met258, Val272, and Val269 in the PNMT active site.	1,2,3,4-tetrahydroisoquinoline	105-135	phenylethanolamine N-methyltransferase	Homo sapiens	44-48	
17126018-2	2007	Docking studies indicated that the enhanced PNMT inhibitory potency of 11 (hPNMT K(i)=0.49microM) versus 1,2,3,4-tetrahydroisoquinoline (5, hPNMT K(i)=5.8microM) was likely due to hydrophobic interactions with Val53, Met258, Val272, and Val269 in the PNMT active site.	1,2,3,4-tetrahydroisoquinoline	105-135	phenylethanolamine N-methyltransferase	Homo sapiens	140-145	
17126018-2	2007	Docking studies indicated that the enhanced PNMT inhibitory potency of 11 (hPNMT K(i)=0.49microM) versus 1,2,3,4-tetrahydroisoquinoline (5, hPNMT K(i)=5.8microM) was likely due to hydrophobic interactions with Val53, Met258, Val272, and Val269 in the PNMT active site.	1,2,3,4-tetrahydroisoquinoline	105-135	phenylethanolamine N-methyltransferase	Homo sapiens	76-80	
10464018-2	1999	These compounds were found to be selective inhibitors of PNMT due to their decreased affinity for the alpha(2)-adrenoceptor, which was attributed to steric bulk intolerance around the 3-position of 1,2,3,4-tetrahydroisoquinoline (THIQ) at the alpha(2)-adrenoceptor and to the decreased pK(a) of the THIQ amine due to the 3-trifluoromethyl moiety.	1,2,3,4-tetrahydroisoquinoline	230-234	phenylethanolamine N-methyltransferase	Homo sapiens	57-61	
11504632-2	2001	Since the PNMT inhibitory activity and selectivity of THIQ were enhanced by the introduction of a hydrophilic electron-withdrawing 7-substituent and a 3-alkyl-substituent, a similar study was conducted on THBA.	1,2,3,4-tetrahydroisoquinoline	54-58	phenylethanolamine N-methyltransferase	Homo sapiens	10-14	
10400340-0	1999	1,3-Dimethyl-7-substituted-1,2,3,4-tetrahydroisoquinolines as probes for the binding orientation of tetrahydroisoquinoline at the active site of phenylethanolamine N-methyltransferase.	1,2,3,4-tetrahydroisoquinoline	35-57	phenylethanolamine N-methyltransferase	Homo sapiens	145-183	
10354406-6	1999	A synergistic effect in increasing the PNMT-inhibitory potency of the THIQ nucleus and reducing the affinity toward the alpha2-adrenoceptor was observed with this 3, 7-disubstitution.	1,2,3,4-tetrahydroisoquinoline	70-74	phenylethanolamine N-methyltransferase	Homo sapiens	39-43	
10400340-3	1999	To gain further understanding about how THIQs bind at the PNMT active site and in an attempt to further increase the selectivity of THIQ-type inhibitors versus the alpha2-adrenoceptor, a series of cis- and trans-1,3-dimethyl-7-substituted-THIQs were synthesized.	1,2,3,4-tetrahydroisoquinoline	40-44	phenylethanolamine N-methyltransferase	Homo sapiens	58-62	
3681890-1	1987	In a continuation of studies directed toward characterizing the hydrophilic pocket within the aromatic ring binding region of the active site of phenylethanolamine N-methyltransferase (PNMT), 5-, 6-, 7-, and 8-hydroxy-1,2,3,4-tetrahydroisoquinoline were prepared and evaluated as substrates and inhibitors of PNMT.	1,2,3,4-tetrahydroisoquinoline	217-248	phenylethanolamine N-methyltransferase	Homo sapiens	145-183	
8784452-2	1996	Based on semiempirical calculations (MNDO) and molecular modeling studies, PNMT-inhibitory activity of these compounds seemed to be dependent on (a) the torsion angle between the plane of the aromatic ring and the endo N atom lone pair ( tau 2 angle), with the optimal value of tau 2 being about - 75 degrees, and (b) the amount of steric bulk about the 3-position of 1,2,3,4-tetrahydroisoquinoline (5, THIQ).	1,2,3,4-tetrahydroisoquinoline	368-398	phenylethanolamine N-methyltransferase	Homo sapiens	75-79	
8784452-2	1996	Based on semiempirical calculations (MNDO) and molecular modeling studies, PNMT-inhibitory activity of these compounds seemed to be dependent on (a) the torsion angle between the plane of the aromatic ring and the endo N atom lone pair ( tau 2 angle), with the optimal value of tau 2 being about - 75 degrees, and (b) the amount of steric bulk about the 3-position of 1,2,3,4-tetrahydroisoquinoline (5, THIQ).	1,2,3,4-tetrahydroisoquinoline	403-407	phenylethanolamine N-methyltransferase	Homo sapiens	75-79	
8784452-3	1996	2,3,4,5-Tetrahydro-1H-2-benzazepine (6) was found to have the highest selectivity (PNMT Ki = 3.34 microM, alpha 2 Ki = 11 microM, selectivity = 3.2) as compared to other homologues of THIQ (PNMT Ki = 9.67 microM, alpha 2 Ki = 0.35 microM, selectivity = 0.036).	1,2,3,4-tetrahydroisoquinoline	184-188	phenylethanolamine N-methyltransferase	Homo sapiens	83-87	
8784452-3	1996	2,3,4,5-Tetrahydro-1H-2-benzazepine (6) was found to have the highest selectivity (PNMT Ki = 3.34 microM, alpha 2 Ki = 11 microM, selectivity = 3.2) as compared to other homologues of THIQ (PNMT Ki = 9.67 microM, alpha 2 Ki = 0.35 microM, selectivity = 0.036).	1,2,3,4-tetrahydroisoquinoline	184-188	phenylethanolamine N-methyltransferase	Homo sapiens	190-194	
3351861-0	1988	Synthesis and evaluation of 3-substituted analogues of 1,2,3,4-tetrahydroisoquinoline as inhibitors of phenylethanolamine N-methyltransferase.	1,2,3,4-tetrahydroisoquinoline	55-85	phenylethanolamine N-methyltransferase	Homo sapiens	103-141	
3351861-1	1988	1,2,3,4-Tetrahydroisoquinoline (THIQ) and aryl-substituted derivatives of THIQ are potent inhibitors of the enzyme that catalyzes the formation of epinephrine--phenylethanolamine N-methyltransferase (PNMT, E.C.	1,2,3,4-tetrahydroisoquinoline	0-30	phenylethanolamine N-methyltransferase	Homo sapiens	147-198	
3351861-1	1988	1,2,3,4-Tetrahydroisoquinoline (THIQ) and aryl-substituted derivatives of THIQ are potent inhibitors of the enzyme that catalyzes the formation of epinephrine--phenylethanolamine N-methyltransferase (PNMT, E.C.	1,2,3,4-tetrahydroisoquinoline	0-30	phenylethanolamine N-methyltransferase	Homo sapiens	200-204	
3351861-1	1988	1,2,3,4-Tetrahydroisoquinoline (THIQ) and aryl-substituted derivatives of THIQ are potent inhibitors of the enzyme that catalyzes the formation of epinephrine--phenylethanolamine N-methyltransferase (PNMT, E.C.	1,2,3,4-tetrahydroisoquinoline	32-36	phenylethanolamine N-methyltransferase	Homo sapiens	147-198	
3351861-1	1988	1,2,3,4-Tetrahydroisoquinoline (THIQ) and aryl-substituted derivatives of THIQ are potent inhibitors of the enzyme that catalyzes the formation of epinephrine--phenylethanolamine N-methyltransferase (PNMT, E.C.	1,2,3,4-tetrahydroisoquinoline	32-36	phenylethanolamine N-methyltransferase	Homo sapiens	200-204	
3351861-1	1988	1,2,3,4-Tetrahydroisoquinoline (THIQ) and aryl-substituted derivatives of THIQ are potent inhibitors of the enzyme that catalyzes the formation of epinephrine--phenylethanolamine N-methyltransferase (PNMT, E.C.	1,2,3,4-tetrahydroisoquinoline	74-78	phenylethanolamine N-methyltransferase	Homo sapiens	147-198	
3351861-1	1988	1,2,3,4-Tetrahydroisoquinoline (THIQ) and aryl-substituted derivatives of THIQ are potent inhibitors of the enzyme that catalyzes the formation of epinephrine--phenylethanolamine N-methyltransferase (PNMT, E.C.	1,2,3,4-tetrahydroisoquinoline	74-78	phenylethanolamine N-methyltransferase	Homo sapiens	200-204	
3351861-4	1988	To more fully delineate this region of the PNMT active site, we have synthesized and evaluated other 3-substituted THIQ analogues that vary in both steric and electronic character.	1,2,3,4-tetrahydroisoquinoline	115-119	phenylethanolamine N-methyltransferase	Homo sapiens	43-47	
3339613-5	1988	Substitution by a methyl group on either benzylic position of THIQ results in diminished activity as a PNMT inhibitor; however, 3-methyl-THIQ shows enhanced activity as an inhibitor vs THIQ itself.	1,2,3,4-tetrahydroisoquinoline	62-66	phenylethanolamine N-methyltransferase	Homo sapiens	103-107	
3681890-1	1987	In a continuation of studies directed toward characterizing the hydrophilic pocket within the aromatic ring binding region of the active site of phenylethanolamine N-methyltransferase (PNMT), 5-, 6-, 7-, and 8-hydroxy-1,2,3,4-tetrahydroisoquinoline were prepared and evaluated as substrates and inhibitors of PNMT.	1,2,3,4-tetrahydroisoquinoline	217-248	phenylethanolamine N-methyltransferase	Homo sapiens	185-189	
6674125-0	1983	Quantitative structure-activity relationship studies of 1,2,3,4-tetrahydroisoquinoline derivatives as inhibitors of phenylethanolamine N-methyltransferase.	1,2,3,4-tetrahydroisoquinoline	56-86	phenylethanolamine N-methyltransferase	Homo sapiens	116-154