PMID-sentid	Pub_year	Sent_text	compound_name	comp_offset	prot_official_name	organism	prot_offset
28041833-0	2017	X-ray structure based evaluation of analogs of citalopram: Compounds with increased affinity and selectivity compared with R-citalopram for the allosteric site (S2) on hSERT.	(R)-citalopram	123-135	solute carrier family 6 member 4	Homo sapiens	168-173
19616061-7	2009	This suggests that the allosteric binding site mediates both the low affinity and higher affinity interactions between R-citalopram, escitalopram, and hSERT.	(R)-citalopram	119-131	solute carrier family 6 member 4	Homo sapiens	151-156
27665061-2	2016	It consists of two enantiomers, S-citalopram (escitalopram) and R-citalopram, of which escitalopram exerts the antidepressant therapeutic effect and has been shown to be one of the most efficient antidepressants, while R-citalopram antagonizes escitalopram via an unknown molecular mechanism that may depend on binding to a low-affinity allosteric binding site of the serotonin transporter.	(R)-citalopram	64-76	solute carrier family 6 member 4	Homo sapiens	368-389
27171685-1	2016	AIM: Studies using S- and R-enantiomers of the SSRI citalopram have shown that R-citalopram exerts an antagonistic effect on the efficacy of the antidepressant S-citalopram (escitalopram) through an interaction at an allosteric modulator site on the serotonin transporter (SERT).	(R)-citalopram	79-91	solute carrier family 6 member 4	Rattus norvegicus	250-271
27171685-1	2016	AIM: Studies using S- and R-enantiomers of the SSRI citalopram have shown that R-citalopram exerts an antagonistic effect on the efficacy of the antidepressant S-citalopram (escitalopram) through an interaction at an allosteric modulator site on the serotonin transporter (SERT).	(R)-citalopram	79-91	solute carrier family 6 member 4	Rattus norvegicus	273-277
27171685-7	2016	Finally, in vitro, quantification of the amount of cell surface-expressed SERT molecules revealed that R-citalopram prevented escitalopram-induced SERT internalization that was completely altered by staurosporine.	(R)-citalopram	103-115	solute carrier family 6 member 4	Rattus norvegicus	74-78
27171685-7	2016	Finally, in vitro, quantification of the amount of cell surface-expressed SERT molecules revealed that R-citalopram prevented escitalopram-induced SERT internalization that was completely altered by staurosporine.	(R)-citalopram	103-115	solute carrier family 6 member 4	Rattus norvegicus	147-151
21901317-10	2012	R-citalopram, the nontherapeutic enantiomer in citalopram, is also an allosteric modulator of SERT but can inhibit the actions of escitalopram by interfering negatively with its binding.	(R)-citalopram	0-12	solute carrier family 6 member 4	Homo sapiens	94-98
24810106-0	2014	The interaction of escitalopram and R-citalopram at the human serotonin transporter investigated in the mouse.	(R)-citalopram	36-48	solute carrier family 6 member 4	Homo sapiens	62-83
24810106-2	2014	It has been hypothesized that binding of R-citalopram to the serotonin transporter (SERT) antagonizes escitalopram binding to and inhibition of the SERT, there by curtailing the elevation of extracellular 5-hydroxytryptamine (5-HTExt), and hence anti-depressant efficacy.	(R)-citalopram	41-53	solute carrier family 6 (neurotransmitter transporter, serotonin), member 4	Mus musculus	61-82
24810106-2	2014	It has been hypothesized that binding of R-citalopram to the serotonin transporter (SERT) antagonizes escitalopram binding to and inhibition of the SERT, there by curtailing the elevation of extracellular 5-hydroxytryptamine (5-HTExt), and hence anti-depressant efficacy.	(R)-citalopram	41-53	solute carrier family 6 (neurotransmitter transporter, serotonin), member 4	Mus musculus	84-88
24810106-2	2014	It has been hypothesized that binding of R-citalopram to the serotonin transporter (SERT) antagonizes escitalopram binding to and inhibition of the SERT, there by curtailing the elevation of extracellular 5-hydroxytryptamine (5-HTExt), and hence anti-depressant efficacy.	(R)-citalopram	41-53	solute carrier family 6 (neurotransmitter transporter, serotonin), member 4	Mus musculus	148-152
18789789-15	2007	The exact mechanism by which R-citalopram exerts its action is not yet fully defined; however, an allosteric interaction between the enantiomers and the 5-HT transporter (SERT) has been proposed.	(R)-citalopram	29-41	solute carrier family 6 member 4	Rattus norvegicus	153-169
19616061-0	2009	An allosteric binding site at the human serotonin transporter mediates the inhibition of escitalopram by R-citalopram: kinetic binding studies with the ALI/VFL-SI/TT mutant.	(R)-citalopram	105-117	solute carrier family 6 member 4	Homo sapiens	40-61
19616061-1	2009	The human serotonin transporter (hSERT) has primary and allosteric binding sites for escitalopram and R-citalopram.	(R)-citalopram	102-114	solute carrier family 6 member 4	Homo sapiens	10-31
19616061-1	2009	The human serotonin transporter (hSERT) has primary and allosteric binding sites for escitalopram and R-citalopram.	(R)-citalopram	102-114	solute carrier family 6 member 4	Homo sapiens	33-38
19616061-4	2009	The low affinity allosteric activities of escitalopram and R-citalopram are essentially eliminated in a mutant hSERT with changes in some of these residues, namely A505V, L506F, I507L, S574T, I575T, as measured in dissociation binding studies.	(R)-citalopram	59-71	solute carrier family 6 member 4	Homo sapiens	111-116
19616061-5	2009	We confirm that in association binding experiments, R-citalopram at clinically relevant concentrations reduces the association rate of [(3)H]escitalopram as a ligand to wild type hSERT.	(R)-citalopram	52-64	solute carrier family 6 member 4	Homo sapiens	179-184
19616061-6	2009	We demonstrate that the ability of R-citalopram to reduce the association rate of escitalopram is also abolished in the mutant hSERT (A505V, L506F, I507L, S574T, I575T), along with the expected disruption the low affinity allosteric function on dissociation binding.	(R)-citalopram	35-47	solute carrier family 6 member 4	Homo sapiens	127-132
18289523-5	2008	As the binding and action of escitalopram is limited by the inactive enantiomer R-citalopram present in racemic citalopram, we propose that the regulation of 5-HT1A receptor function in the dorsal raphe nucleus at the level of receptor-G protein interaction may be a result of greater inhibition of the serotonin transporter by escitalopram.	(R)-citalopram	80-92	5-hydroxytryptamine receptor 1A	Homo sapiens	158-173
18789789-19	2007	On the other hand, in the presence of the two enantiomers, R-citalopram binds to the allosteric site and decreases the escitalopram action on SERT.	(R)-citalopram	59-71	solute carrier family 6 member 4	Rattus norvegicus	142-146
17201996-10	2007	The small but significant difference in occupancy and K(i),(app) found between R,S-citalopram and S-citalopram suggests that not only S-citalopram but also R-citalopram to some degree occupies the 5-HTT in the human brain in vivo.	(R)-citalopram	156-168	solute carrier family 6 member 4	Homo sapiens	197-202
18789789-15	2007	The exact mechanism by which R-citalopram exerts its action is not yet fully defined; however, an allosteric interaction between the enantiomers and the 5-HT transporter (SERT) has been proposed.	(R)-citalopram	29-41	solute carrier family 6 member 4	Rattus norvegicus	171-175
17499240-3	2007	The objectives of this study were 1) to identify hSERT mutations that inactivate the high-affinity site without affecting the allosteric site and 2) to observe allosteric effects in which hSERT binds R-citalopram with higher affinity than S-citalopram.	(R)-citalopram	200-212	solute carrier family 6 member 4	Homo sapiens	188-193
17499240-7	2007	Further, R-citalopram previously thought of as an inactive enantiomer strongly attenuated dissociation of the wild-type [(3)H]-imipramine:hSERT complex, whereas S-citalopram had almost no effect on this complex.	(R)-citalopram	9-21	solute carrier family 6 member 4	Homo sapiens	138-143
17499240-9	2007	2: The allosteric effects of R-citalopram on the dissociation of [(3)H]-imipramine from hSERT indicate that R-citalopram introduces a conformational change in hSERT.	(R)-citalopram	29-41	solute carrier family 6 member 4	Homo sapiens	88-93
17499240-9	2007	2: The allosteric effects of R-citalopram on the dissociation of [(3)H]-imipramine from hSERT indicate that R-citalopram introduces a conformational change in hSERT.	(R)-citalopram	29-41	solute carrier family 6 member 4	Homo sapiens	159-164
17499240-9	2007	2: The allosteric effects of R-citalopram on the dissociation of [(3)H]-imipramine from hSERT indicate that R-citalopram introduces a conformational change in hSERT.	(R)-citalopram	108-120	solute carrier family 6 member 4	Homo sapiens	88-93
17499240-9	2007	2: The allosteric effects of R-citalopram on the dissociation of [(3)H]-imipramine from hSERT indicate that R-citalopram introduces a conformational change in hSERT.	(R)-citalopram	108-120	solute carrier family 6 member 4	Homo sapiens	159-164
15695064-2	2005	The interaction of the S- and R-enantiomers (escitalopram and R-citalopram) of citalopram, with high- and low-affinity binding sites in COS-1 cell membranes expressing human SERT (hSERT) were investigated.	(R)-citalopram	62-74	solute carrier family 6 member 4	Homo sapiens	180-185
17675913-3	2007	Citalopram"s pharmacologic activity is centered on the S enantiomer"s high affinity for the serotonin transporter which is twice as high as citalopram"s and 30 to 40 times higher than R-citalopram.	(R)-citalopram	184-196	solute carrier family 6 member 4	Homo sapiens	92-113
17675913-19	2007	The antagonism of escitalopram by R-citalopram was not expected and one hypothesis is that a direct interaction between the 2 enantiomers may occur on a particular site of the serotonin transporter.	(R)-citalopram	34-46	solute carrier family 6 member 4	Homo sapiens	176-197
16448580-5	2007	In-vitro binding studies showed that R-citalopram attenuated the association rates of escitalopram and paroxetine to the 5-HT transporter, but had no effect on the association rates of fluoxetine, venlafaxine or sertraline.	(R)-citalopram	37-49	solute carrier family 6 member 4	Rattus norvegicus	121-137
16448580-12	2007	In conclusion, the present in-vitro and in-vivo studies show that R-citalopram counteracts the activity of escitalopram and paroxetine, but not fluoxetine, by acting at the allosteric binding site of the 5-HT transporter, either located in the dorsal raphe nucleus or post-synaptically in the ventral hippocampus.	(R)-citalopram	66-78	solute carrier family 6 member 4	Rattus norvegicus	204-220
17235610-10	2007	The results can also be explained by an attenuating effect of R-citalopram on the occupancy of S-citalopram at the SERT.	(R)-citalopram	62-74	solute carrier family 6 member 4	Homo sapiens	115-119
16918708-2	2006	The exact molecular mechanism by which R-citalopram inhibits the effect of S-citalopram on the serotonin transporter remains to be elucidated.	(R)-citalopram	39-51	solute carrier family 6 member 4	Homo sapiens	95-116
16918708-3	2006	Preliminary evidence indicates an effect of R-citalopram on the association of escitalopram with the high affinity primary site, and on its dissociation from the serotonin transporter, via an allosteric mechanism.	(R)-citalopram	44-56	solute carrier family 6 member 4	Homo sapiens	162-183
15695064-2	2005	The interaction of the S- and R-enantiomers (escitalopram and R-citalopram) of citalopram, with high- and low-affinity binding sites in COS-1 cell membranes expressing human SERT (hSERT) were investigated.	(R)-citalopram	62-74	solute carrier family 6 member 4	Homo sapiens	174-178
15695064-5	2005	The stereoselectivity between escitalopram and R-citalopram was approximately 3:1 for the [3H]-escitalopram/hSERT complex.	(R)-citalopram	47-59	solute carrier family 6 member 4	Homo sapiens	108-113
15037515-6	2004	In both behavioural (potentiation of 5-hydroxytryptophan (5-HTP)-induced behaviour) and electrophysiological studies (inhibition of 5-HT-elicited ion currents in Xenopus oocytes expressing the human SERT (hSERT) R-citalopram inhibited the effects of S-citalopram in a dose-dependent manner.	(R)-citalopram	212-224	solute carrier family 6 member 4	Homo sapiens	199-203
15606893-3	2005	Dissociation of [3H]S-citalopram from SERT is most potently inhibited by S-citalopram followed by R-citalopram, sertraline, serotonin and paroxetine.	(R)-citalopram	98-110	solute carrier family 6 member 4	Homo sapiens	38-42
15037515-0	2004	R-citalopram functionally antagonises escitalopram in vivo and in vitro: evidence for kinetic interaction at the serotonin transporter.	(R)-citalopram	0-12	solute carrier family 6 member 4	Homo sapiens	113-134
15037515-11	2004	In oocytes, inhibition of hSERT-mediated currents by R-citalopram was almost completely reversible and characterised by fast on- and off-sets of action.	(R)-citalopram	53-65	solute carrier family 6 member 4	Homo sapiens	26-31
15037515-3	2004	Since R-citalopram is at least 20-fold weaker than S-citalopram as inhibitor of the 5-HT transporter (SERT) in preclinical studies, the clinical data suggest an unexpected antagonistic interaction between the two enantiomers.	(R)-citalopram	6-18	solute carrier family 6 member 4	Homo sapiens	102-106
15037515-14	2004	Kinetic analysis of the oocyte experiments suggests that S-citalopram binding to SERT induces a long-lasting, inhibited state of the transporter and that coapplication of R-citalopram partially relieves SERT of this persistent inhibition.	(R)-citalopram	171-183	solute carrier family 6 member 4	Homo sapiens	203-207
15037515-16	2004	We propose that the kinetic interaction of R- and S-citalopram with SERT is a critical factor contributing to the antagonistic effects of R-citalopram on S-citalopram in vitro and in vivo.	(R)-citalopram	138-150	solute carrier family 6 member 4	Homo sapiens	68-72
35303575-3	2022	Under the optimized conditions, the resolution was Rs=8.04, the enrichment factor as up to 2163 folds, the LOD values were: 3.6 ng mL-1 for R-citalopram, 4.1 ng mL-1 for S-citalopram, and 3 ng mL-1 for both enantiomers in plasma samples.	(R)-citalopram	140-152	L1 cell adhesion molecule	Mus musculus	131-135
34280395-4	2021	In this study, we investigated whether citalopram, escitalopram and R-citalopram had an electrophysiological effect on Nav1.5 voltage-gated sodium channel (VGSC) current and how their electrophysiological properties affected Nav1.5 VGSC.	(R)-citalopram	68-80	sodium voltage-gated channel alpha subunit 5	Homo sapiens	119-125
34280395-7	2021	However, 100 muM R-citalopram decreased Nav1.5 VGSC current by only 36.2 +- 8.7%.	(R)-citalopram	17-29	sodium voltage-gated channel alpha subunit 5	Homo sapiens	40-46
34280395-10	2021	These results suggest that the adverse cardiac effect produced by citalopram might result from modification of the electrophysiological properties of Nav1.5 VGSCs, and escitalopram might contribute more to this adverse effect than R-citalopram.	(R)-citalopram	231-243	sodium voltage-gated channel alpha subunit 5	Homo sapiens	150-156
35303575-3	2022	Under the optimized conditions, the resolution was Rs=8.04, the enrichment factor as up to 2163 folds, the LOD values were: 3.6 ng mL-1 for R-citalopram, 4.1 ng mL-1 for S-citalopram, and 3 ng mL-1 for both enantiomers in plasma samples.	(R)-citalopram	140-152	L1 cell adhesion molecule	Mus musculus	193-197