PMID-sentid	Pub_year	Sent_text	comp_official_name	comp_offset	protein_name	organism	prot_offset
27296115-0	2016	BDNF modulates glycine uptake in hippocampal synaptosomes by decreasing membrane insertion of glycine transporter 2.	Glycine	15-22	solute carrier family 6 member 5	Rattus norvegicus	94-115
27296115-1	2016	Glycine transporter 2 (GlyT2) is localized in the nerve terminals of glycinergic neurons, promoting glycine uptake and ensuring the refilling of glycinergic vesicles.	Glycine	69-76	solute carrier family 6 member 5	Rattus norvegicus	0-21
27296115-1	2016	Glycine transporter 2 (GlyT2) is localized in the nerve terminals of glycinergic neurons, promoting glycine uptake and ensuring the refilling of glycinergic vesicles.	Glycine	69-76	solute carrier family 6 member 5	Rattus norvegicus	23-28
27296115-4	2016	We herein show that BDNF decreases [(3)H]glycine uptake mediated by GlyT2 in isolated nerve endings (synaptosomes) obtained from rat hippocampus, by reducing the maximum velocity (Vmax) of transport while not influencing the transporter affinity constant (Km) for glycine.	[(3)h]glycine	35-48	solute carrier family 6 member 5	Rattus norvegicus	68-73
27296115-4	2016	We herein show that BDNF decreases [(3)H]glycine uptake mediated by GlyT2 in isolated nerve endings (synaptosomes) obtained from rat hippocampus, by reducing the maximum velocity (Vmax) of transport while not influencing the transporter affinity constant (Km) for glycine.	Glycine	41-48	solute carrier family 6 member 5	Rattus norvegicus	68-73
27296115-6	2016	Monensin, a transporter recycling inhibitor, prevented the BDNF action upon glycine uptake, suggesting that BDNF reduces GlyT2 insertion in the plasma membrane.	Glycine	76-83	solute carrier family 6 member 5	Rattus norvegicus	121-126
23529192-1	2014	GlyT1 and GlyT2 are the transporters responsible for glycine uptake from the synaptic cleft.	Glycine	53-60	solute carrier family 6 member 5	Rattus norvegicus	10-15
26200505-4	2015	We report that BDNF decreases GlyT1- and GlyT2- mediated [(3) H]glycine transport in primary cultures of astrocytes from rat cerebral cortex.	[(3) h]glycine	57-71	solute carrier family 6 member 5	Rattus norvegicus	41-46
26200505-1	2015	Glycine transporters (GlyT), GlyT1 and GlyT2, are responsible for the termination of glycine-mediated synaptic activity through removal of neurotransmitter from synaptic cleft.	Glycine	85-92	solute carrier family 6 member 5	Rattus norvegicus	39-44
26101830-2	2015	The glycine concentration in the synaptic cleft is controlled by the glycine transporters GlyT1 and GlyT2.	Glycine	4-11	solute carrier family 6 member 5	Rattus norvegicus	100-105
25579325-0	2015	Antinociceptive effect of intracerebroventricular administration of glycine transporter-2 inhibitor ALX1393 in rat models of inflammatory and neuropathic pain.	ALX 1393	100-107	solute carrier family 6 member 5	Rattus norvegicus	68-89
25579325-2	2015	The glycine transporter-2 (GlyT2) is localized at presynaptic terminals of glycinergic neurons and eliminates glycine from the synaptic cleft to terminate glycinergic transmission.	Glycine	4-11	solute carrier family 6 member 5	Rattus norvegicus	27-32
25579325-6	2015	administration of the selective GlyT2 inhibitor ALX1393 on inflammatory and neuropathic pain in experimental models.	ALX 1393	48-55	solute carrier family 6 member 5	Rattus norvegicus	32-37
24797328-6	2014	Hippocampal levels of glycine were decreased in sarcosine-treated animals, which was associated with a reduction of [(3)H] glycine uptake and a decrease in glycine transporter expression (GlyT-1 and GlyT-2).	Glycine	22-29	solute carrier family 6 member 5	Rattus norvegicus	199-205
24797328-6	2014	Hippocampal levels of glycine were decreased in sarcosine-treated animals, which was associated with a reduction of [(3)H] glycine uptake and a decrease in glycine transporter expression (GlyT-1 and GlyT-2).	Sarcosine	48-57	solute carrier family 6 member 5	Rattus norvegicus	199-205
23529192-6	2014	The functional characterization of GlyT1 and GlyT2 in cultured astrocytes performed by [(3)H]glycine uptake experiments revealed that both transporters take up glycine in a concentration-dependent way, but with a very distinct affinity.	Glycine	93-100	solute carrier family 6 member 5	Rattus norvegicus	45-50
23529192-6	2014	The functional characterization of GlyT1 and GlyT2 in cultured astrocytes performed by [(3)H]glycine uptake experiments revealed that both transporters take up glycine in a concentration-dependent way, but with a very distinct affinity.	Glycine	160-167	solute carrier family 6 member 5	Rattus norvegicus	45-50
21348870-4	2011	The NMDA/glycine-induced release in 1.2 mM Mg(2+) strictly depended on glycine uptake through the glycine transporter type 1 (GlyT1), because the GlyT1 blocker N-[3-(4"-fluorophenyl)-3-(4"-phenylphenoxy)propyl])sarcosine hydrochloride, but not the GlyT2 blocker Org 25534, prevented it.	n-[3-(4"-fluorophenyl)-3-(4"-phenylphenoxy)propyl])sarcosine hydrochloride	160-234	solute carrier family 6 member 5	Rattus norvegicus	248-253
22542656-4	2012	ASP2535 potently inhibited rat GlyT1 (IC(50)=92 nM) with 50-fold selectivity over rat glycine transporter-2 (GlyT2).	4-(3-isopropyl-5-(6-phenyl-3-pyridyl)-4H-1,2,4-triazol-4-yl)-2,1,3-benzoxadiazole	0-7	solute carrier family 6 member 5	Rattus norvegicus	86-107
21348870-4	2011	The NMDA/glycine-induced release in 1.2 mM Mg(2+) strictly depended on glycine uptake through the glycine transporter type 1 (GlyT1), because the GlyT1 blocker N-[3-(4"-fluorophenyl)-3-(4"-phenylphenoxy)propyl])sarcosine hydrochloride, but not the GlyT2 blocker Org 25534, prevented it.	N-Methylaspartate	4-8	solute carrier family 6 member 5	Rattus norvegicus	248-253
22341128-1	2012	BACKGROUND: Glycine is a major inhibitory neurotransmitter in the spinal cord, the concentration of which is regulated by two types of glycine transporters (GlyTs): GlyT1 and GlyT2.	Glycine	12-19	solute carrier family 6 member 5	Rattus norvegicus	175-180
22341128-8	2012	RESULTS AND LIMITATIONS: During cystometry in CYP-treated rats, significant increases in intercontraction interval and micturition pressure threshold were elicited by ALX-1393, a selective GlyT2 inhibitor, but not by sarcosine, a GlyT1 inhibitor.	ALX 1393	167-175	solute carrier family 6 member 5	Rattus norvegicus	189-194
22341128-13	2012	CONCLUSIONS: These results indicate that GlyT2 plays a major role in the clearance of extracellular glycine in the spinal cord and that GlyT2 inhibition leads to amelioration of CYP-induced bladder overactivity and pain behavior.	Glycine	100-107	solute carrier family 6 member 5	Rattus norvegicus	41-46
20860669-5	2010	NAGly and ALX-1393 (inhibitor of the glycine transporter, GLYT2), but not the GLYT1 inhibitor, ALX-5407, produced a strychnine-sensitive inward current.	N-arachidonylglycine	0-5	solute carrier family 6 member 5	Rattus norvegicus	58-63
21348870-4	2011	The NMDA/glycine-induced release in 1.2 mM Mg(2+) strictly depended on glycine uptake through the glycine transporter type 1 (GlyT1), because the GlyT1 blocker N-[3-(4"-fluorophenyl)-3-(4"-phenylphenoxy)propyl])sarcosine hydrochloride, but not the GlyT2 blocker Org 25534, prevented it.	Glycine	9-16	solute carrier family 6 member 5	Rattus norvegicus	248-253
21348870-4	2011	The NMDA/glycine-induced release in 1.2 mM Mg(2+) strictly depended on glycine uptake through the glycine transporter type 1 (GlyT1), because the GlyT1 blocker N-[3-(4"-fluorophenyl)-3-(4"-phenylphenoxy)propyl])sarcosine hydrochloride, but not the GlyT2 blocker Org 25534, prevented it.	Glycine	71-78	solute carrier family 6 member 5	Rattus norvegicus	248-253
21245148-3	2011	In this study, we report that stimulation of P2Y purinergic receptors with 2-methylthioadenosine 5"-diphosphate in rat brainstem/spinal cord primary neuronal cultures and adult rat synaptosomes leads to the inhibition of GLYT2 and the stimulation of GLYT1 by a paracrine regulation.	methylthio-ADP	75-111	solute carrier family 6 member 5	Rattus norvegicus	221-226
21245148-8	2011	GLYT1 and GLYT2 are differentially sensitive to NO/cGMP/PKG-I both in brain-derived preparations and in heterologous systems expressing the recombinant transporters and P2Y(1) receptor.	Cyclic GMP	51-55	solute carrier family 6 member 5	Rattus norvegicus	10-15
21245148-9	2011	Sensitivity to 2-methylthioadenosine 5"-diphosphate by GLYT1 and GLYT2 was abolished by small interfering RNA (siRNA)-mediated knockdown of nitric-oxide synthase.	methylthio-ADP	15-51	solute carrier family 6 member 5	Rattus norvegicus	65-70
21731704-7	2011	In contrast, the GlyT-2 inhibitor ALX1393 exhibited very weak for [3H]CHIBA-3007 binding.	ALX 1393	34-41	solute carrier family 6 member 5	Rattus norvegicus	17-23
21731704-7	2011	In contrast, the GlyT-2 inhibitor ALX1393 exhibited very weak for [3H]CHIBA-3007 binding.	Tritium	67-69	solute carrier family 6 member 5	Rattus norvegicus	17-23
21731704-7	2011	In contrast, the GlyT-2 inhibitor ALX1393 exhibited very weak for [3H]CHIBA-3007 binding.	chiba-	70-76	solute carrier family 6 member 5	Rattus norvegicus	17-23
20860669-10	2010	CONCLUSIONS AND IMPLICATIONS: Our results suggest that NAGly enhanced inhibitory glycinergic synaptic transmission within the superficial dorsal horn by blocking glycine uptake via GLYT2.	N-arachidonylglycine	55-60	solute carrier family 6 member 5	Rattus norvegicus	181-186
20860669-10	2010	CONCLUSIONS AND IMPLICATIONS: Our results suggest that NAGly enhanced inhibitory glycinergic synaptic transmission within the superficial dorsal horn by blocking glycine uptake via GLYT2.	Glycine	81-88	solute carrier family 6 member 5	Rattus norvegicus	181-186
20860669-5	2010	NAGly and ALX-1393 (inhibitor of the glycine transporter, GLYT2), but not the GLYT1 inhibitor, ALX-5407, produced a strychnine-sensitive inward current.	ALX 1393	10-18	solute carrier family 6 member 5	Rattus norvegicus	58-63
20335821-1	2010	In this study, we have examined the possible roles of a glycine transporter type 2 (GlyT-2) in the forskolin-induced increase of the amplitude of glycinergic miniature inhibitory postsynaptic currents (mIPSCs) in acutely isolated rat substantia gelatinosa neurons.	Colforsin	99-108	solute carrier family 6 member 5	Rattus norvegicus	84-90
20335821-3	2010	This effect disappeared by the addition of ALX1393 (a GlyT-2 antagonist).	ALX 1393	43-50	solute carrier family 6 member 5	Rattus norvegicus	54-60
20335821-4	2010	These results suggest that both extracellular glycine and GlyT-2 are essential for the forskolin-induced increase in the amplitude of glycinergic mIPSCs.	Colforsin	87-96	solute carrier family 6 member 5	Rattus norvegicus	58-64
20081141-0	2010	The antinociceptive effect of intrathecal administration of glycine transporter-2 inhibitor ALX1393 in a rat acute pain model.	ALX 1393	92-99	solute carrier family 6 member 5	Rattus norvegicus	60-81
20335821-0	2010	GlyT-2 mediates the forskolin-induced increase of glycinergic transmission.	Colforsin	20-29	solute carrier family 6 member 5	Rattus norvegicus	0-6
20335821-1	2010	In this study, we have examined the possible roles of a glycine transporter type 2 (GlyT-2) in the forskolin-induced increase of the amplitude of glycinergic miniature inhibitory postsynaptic currents (mIPSCs) in acutely isolated rat substantia gelatinosa neurons.	Colforsin	99-108	solute carrier family 6 member 5	Rattus norvegicus	56-82
20081141-2	2010	Neuronal isoform glycine transporter-2 (GlyT2) reuptakes presynaptically released glycine and regulates the glycinergic neurotransmission.	Glycine	17-24	solute carrier family 6 member 5	Rattus norvegicus	40-45
20081141-3	2010	In this study, we examined whether a selective GlyT2 inhibitor, ALX1393, elicits an antinociceptive effect in a rat acute pain model.	ALX 1393	64-71	solute carrier family 6 member 5	Rattus norvegicus	47-52
18695510-2	2008	The effective synaptic concentrations of glycine are regulated by at least two transporters: glycine transporter 1 and glycine transporter 2.	Glycine	41-48	solute carrier family 6 member 5	Rattus norvegicus	119-140
19374720-1	2009	The neuronal glycine transporter GLYT2 belongs to the neurotransmitter:sodium:symporter (NSS) family and removes glycine from the synaptic cleft, thereby aiding the termination of the glycinergic signal and achieving the reloading of the presynaptic terminal.	Glycine	13-20	solute carrier family 6 member 5	Rattus norvegicus	33-38
19374720-7	2009	Coexpression of a Rab11 dominant negative mutant with recombinant GLYT2 impaired transporter trafficking and glycine transport.	Glycine	109-116	solute carrier family 6 member 5	Rattus norvegicus	66-71
19875446-0	2009	Extracellular loops 2 and 4 of GLYT2 are required for N-arachidonylglycine inhibition of glycine transport.	N-arachidonylglycine	54-74	solute carrier family 6 member 5	Rattus norvegicus	31-36
19875446-0	2009	Extracellular loops 2 and 4 of GLYT2 are required for N-arachidonylglycine inhibition of glycine transport.	Glycine	67-74	solute carrier family 6 member 5	Rattus norvegicus	31-36
19875446-1	2009	Concentrations of extracellular glycine in the central nervous system are regulated by Na(+)/Cl(-)-dependent glycine transporters, GLYT1 and GLYT2.	Glycine	32-39	solute carrier family 6 member 5	Rattus norvegicus	141-146
19875446-2	2009	N-Arachidonylglycine (NAGly) is an endogenous inhibitor of GLYT2 with little or no effect on GLYT1 and is analgesic in rat models of neuropathic and inflammatory pain.	N-arachidonylglycine	0-20	solute carrier family 6 member 5	Rattus norvegicus	59-64
19875446-2	2009	N-Arachidonylglycine (NAGly) is an endogenous inhibitor of GLYT2 with little or no effect on GLYT1 and is analgesic in rat models of neuropathic and inflammatory pain.	N-arachidonylglycine	22-27	solute carrier family 6 member 5	Rattus norvegicus	59-64
19875446-3	2009	Understanding the molecular basis of NAGly interactions with GLYT2 may allow for the development of novel therapeutics.	N-arachidonylglycine	37-42	solute carrier family 6 member 5	Rattus norvegicus	61-66
19875446-4	2009	In this study, chimeric transporters were used to determine the structural basis for differences in NAGly sensitivity between GLYT1 and GLYT2 and also the actions of a series of related N-arachidonyl amino acids.	N-arachidonylglycine	100-105	solute carrier family 6 member 5	Rattus norvegicus	136-141
19875446-5	2009	Extracellular loops 2 and 4 of GLYT2 are important in the selective inhibition of GLYT2 by NAGly and by the related compounds N-arachidonyl-gamma-aminobutyric acid and N-arachidonyl-d-alanine, whereas only the extracellular loop 4 of GLYT2 is required for N-arachidonyl-l-alanine inhibition of transport.	N-arachidonylglycine	91-96	solute carrier family 6 member 5	Rattus norvegicus	31-36
19875446-5	2009	Extracellular loops 2 and 4 of GLYT2 are important in the selective inhibition of GLYT2 by NAGly and by the related compounds N-arachidonyl-gamma-aminobutyric acid and N-arachidonyl-d-alanine, whereas only the extracellular loop 4 of GLYT2 is required for N-arachidonyl-l-alanine inhibition of transport.	N-arachidonylglycine	91-96	solute carrier family 6 member 5	Rattus norvegicus	82-87
19875446-5	2009	Extracellular loops 2 and 4 of GLYT2 are important in the selective inhibition of GLYT2 by NAGly and by the related compounds N-arachidonyl-gamma-aminobutyric acid and N-arachidonyl-d-alanine, whereas only the extracellular loop 4 of GLYT2 is required for N-arachidonyl-l-alanine inhibition of transport.	N-arachidonylglycine	91-96	solute carrier family 6 member 5	Rattus norvegicus	82-87
19875446-5	2009	Extracellular loops 2 and 4 of GLYT2 are important in the selective inhibition of GLYT2 by NAGly and by the related compounds N-arachidonyl-gamma-aminobutyric acid and N-arachidonyl-d-alanine, whereas only the extracellular loop 4 of GLYT2 is required for N-arachidonyl-l-alanine inhibition of transport.	NAGABA	126-163	solute carrier family 6 member 5	Rattus norvegicus	31-36
19875446-5	2009	Extracellular loops 2 and 4 of GLYT2 are important in the selective inhibition of GLYT2 by NAGly and by the related compounds N-arachidonyl-gamma-aminobutyric acid and N-arachidonyl-d-alanine, whereas only the extracellular loop 4 of GLYT2 is required for N-arachidonyl-l-alanine inhibition of transport.	NAGABA	126-163	solute carrier family 6 member 5	Rattus norvegicus	82-87
19875446-5	2009	Extracellular loops 2 and 4 of GLYT2 are important in the selective inhibition of GLYT2 by NAGly and by the related compounds N-arachidonyl-gamma-aminobutyric acid and N-arachidonyl-d-alanine, whereas only the extracellular loop 4 of GLYT2 is required for N-arachidonyl-l-alanine inhibition of transport.	NAGABA	126-163	solute carrier family 6 member 5	Rattus norvegicus	82-87
19875446-5	2009	Extracellular loops 2 and 4 of GLYT2 are important in the selective inhibition of GLYT2 by NAGly and by the related compounds N-arachidonyl-gamma-aminobutyric acid and N-arachidonyl-d-alanine, whereas only the extracellular loop 4 of GLYT2 is required for N-arachidonyl-l-alanine inhibition of transport.	N-arachidonyl-D-alanine	168-191	solute carrier family 6 member 5	Rattus norvegicus	31-36
19875446-5	2009	Extracellular loops 2 and 4 of GLYT2 are important in the selective inhibition of GLYT2 by NAGly and by the related compounds N-arachidonyl-gamma-aminobutyric acid and N-arachidonyl-d-alanine, whereas only the extracellular loop 4 of GLYT2 is required for N-arachidonyl-l-alanine inhibition of transport.	N-arachidonyl-D-alanine	168-191	solute carrier family 6 member 5	Rattus norvegicus	82-87
19875446-5	2009	Extracellular loops 2 and 4 of GLYT2 are important in the selective inhibition of GLYT2 by NAGly and by the related compounds N-arachidonyl-gamma-aminobutyric acid and N-arachidonyl-d-alanine, whereas only the extracellular loop 4 of GLYT2 is required for N-arachidonyl-l-alanine inhibition of transport.	N-arachidonyl-D-alanine	168-191	solute carrier family 6 member 5	Rattus norvegicus	82-87
19875446-5	2009	Extracellular loops 2 and 4 of GLYT2 are important in the selective inhibition of GLYT2 by NAGly and by the related compounds N-arachidonyl-gamma-aminobutyric acid and N-arachidonyl-d-alanine, whereas only the extracellular loop 4 of GLYT2 is required for N-arachidonyl-l-alanine inhibition of transport.	C23H37NO3	256-279	solute carrier family 6 member 5	Rattus norvegicus	31-36
19875446-5	2009	Extracellular loops 2 and 4 of GLYT2 are important in the selective inhibition of GLYT2 by NAGly and by the related compounds N-arachidonyl-gamma-aminobutyric acid and N-arachidonyl-d-alanine, whereas only the extracellular loop 4 of GLYT2 is required for N-arachidonyl-l-alanine inhibition of transport.	C23H37NO3	256-279	solute carrier family 6 member 5	Rattus norvegicus	82-87
19875446-5	2009	Extracellular loops 2 and 4 of GLYT2 are important in the selective inhibition of GLYT2 by NAGly and by the related compounds N-arachidonyl-gamma-aminobutyric acid and N-arachidonyl-d-alanine, whereas only the extracellular loop 4 of GLYT2 is required for N-arachidonyl-l-alanine inhibition of transport.	C23H37NO3	256-279	solute carrier family 6 member 5	Rattus norvegicus	82-87
19875446-7	2009	Site-directed mutagenesis of GLYT2 EL4 residues was used to identify the key residues Arg(531), Lys(532), and Ile(545) that contribute to the differences in NAGly sensitivity.	Arginine	86-89	solute carrier family 6 member 5	Rattus norvegicus	29-34
19875446-7	2009	Site-directed mutagenesis of GLYT2 EL4 residues was used to identify the key residues Arg(531), Lys(532), and Ile(545) that contribute to the differences in NAGly sensitivity.	Lysine	96-99	solute carrier family 6 member 5	Rattus norvegicus	29-34
19875446-7	2009	Site-directed mutagenesis of GLYT2 EL4 residues was used to identify the key residues Arg(531), Lys(532), and Ile(545) that contribute to the differences in NAGly sensitivity.	Isoleucine	110-113	solute carrier family 6 member 5	Rattus norvegicus	29-34
19875446-7	2009	Site-directed mutagenesis of GLYT2 EL4 residues was used to identify the key residues Arg(531), Lys(532), and Ile(545) that contribute to the differences in NAGly sensitivity.	N-arachidonylglycine	157-162	solute carrier family 6 member 5	Rattus norvegicus	29-34
18793697-2	2008	Since the concentration of glycine in the synaptic cleft is controlled by specialized proteins, the glycine transporters GlyT1 and GlyT2, manipulation of this system might have significant effects on nociception.	Glycine	27-34	solute carrier family 6 member 5	Rattus norvegicus	131-136
17962467-16	2007	Although GLYT1 and -2 are likely to mediate glycine uptake in cortical fiber cells, GLYT2 alone appears responsible for the accumulation of glycine in the center of the lens.	Glycine	140-147	solute carrier family 6 member 5	Rattus norvegicus	84-89
12941372-1	2003	In the central nervous system, re-uptake of the neurotransmitter glycine is mediated by two different glycine transporters, GlyT1 and GlyT2.	Glycine	65-72	solute carrier family 6 member 5	Rattus norvegicus	134-139
17962467-0	2007	Mapping of glutathione and its precursor amino acids reveals a role for GLYT2 in glycine uptake in the lens core.	Glutathione	11-22	solute carrier family 6 member 5	Rattus norvegicus	72-77
17962467-0	2007	Mapping of glutathione and its precursor amino acids reveals a role for GLYT2 in glycine uptake in the lens core.	Glycine	81-88	solute carrier family 6 member 5	Rattus norvegicus	72-77
17336274-3	2007	The results showed that in all segments the majority of the GlyT2 mRNA labeled (glycinergic) neuronal somata was present in the deep dorsal horn and the intermediate zone (laminae III-VIII), with around 50% (range 43.7-70.9%) in laminae VII&VIII.	Adenosine Monophosphate	241-244	solute carrier family 6 member 5	Rattus norvegicus	60-65
15276154-1	2004	The glycine transporter subtype 2 (GlyT2) is localized at glycinergic axon terminals where it mediates the re-uptake of glycine from the extracellular space.	Glycine	4-11	solute carrier family 6 member 5	Rattus norvegicus	35-40
9509996-5	1998	However, whereas GLYT2a is able to actively accumulate glycine into transfected COS cells, GLYT2b seems only to exchange (or release) glycine.	Glycine	55-62	solute carrier family 6 member 5	Rattus norvegicus	17-22
12091465-3	2002	Functional analysis of the GFP-GLYT1 and GFP-GLYT2 stable cell lines demonstrated that they exhibited high affinity for glycine and the characteristic properties of both glycine transporter subtypes.	Glycine	120-127	solute carrier family 6 member 5	Rattus norvegicus	45-50
11709067-4	2001	We found that GLYT2 is rapidly trafficked first towards the plasma membrane and then internalized under conditions that stimulate vesicular glycine release.	Glycine	140-147	solute carrier family 6 member 5	Rattus norvegicus	14-19
11445189-8	2001	Rat cortex and cerebellum synaptosomes also showed a high-affinity Na(+)-dependent component of glycine uptake, with affinities similar to those observed for uptake in GlyT-1c or GlyT-2 cells.	Glycine	96-103	solute carrier family 6 member 5	Rattus norvegicus	179-185
10722844-3	2000	Co-transfection of syntaxin 1A with GLYT1 or GLYT2 in COS cells resulted in approximately 40% inhibition in glycine transport.	Glycine	108-115	solute carrier family 6 member 5	Rattus norvegicus	45-50
12770560-3	2003	The present study was carried out to determine the pattern of coexistence of the two GAD isoforms in axonal boutons in different laminae of the cord, and also to examine the relation of the GADs to the glycine transporter GLYT2 (a marker for glycinergic axons), since many spinal neurons are thought to use GABA and glycine as co-transmitters.	Glycine	202-209	solute carrier family 6 member 5	Rattus norvegicus	222-227
10545158-7	1999	Acoustic stimulation at either 10 kHz or 40 kHz was used to provide controlled increases in primary afferent activity, evoking localized increases in Glyt2 mRNA in clusters of neurons in the DCN.	dcn	191-194	solute carrier family 6 member 5	Rattus norvegicus	150-155
9798949-3	1998	GLYT2 transports glycine with higher apparent affinity than GLYT1b and is not inhibited by any assayed compound, as deduced by glycine transport assays and electrophysiological recordings.	Glycine	17-24	solute carrier family 6 member 5	Rattus norvegicus	0-5
9798949-3	1998	GLYT2 transports glycine with higher apparent affinity than GLYT1b and is not inhibited by any assayed compound, as deduced by glycine transport assays and electrophysiological recordings.	Glycine	127-134	solute carrier family 6 member 5	Rattus norvegicus	0-5
9798949-8	1998	GLYT2 exhibits more voltage dependence in both its glycine-evoked current and its capacitive currents recorded in the absence of substrate.	Glycine	51-58	solute carrier family 6 member 5	Rattus norvegicus	0-5
9509996-5	1998	However, whereas GLYT2a is able to actively accumulate glycine into transfected COS cells, GLYT2b seems only to exchange (or release) glycine.	Glycine	134-141	solute carrier family 6 member 5	Rattus norvegicus	91-96
33794243-0	2021	Rescue of two trafficking-defective variants of the neuronal glycine transporter GlyT2 associated to hyperekplexia.	Glycine	61-68	solute carrier family 6 member 5	Rattus norvegicus	81-86
9472410-0	1997	An ultrastructural study of the glycine transporter GLYT2 and its association with glycine in the superficial laminae of the rat spinal dorsal horn.	Glycine	32-39	solute carrier family 6 member 5	Rattus norvegicus	52-57
9472410-1	1997	The glycine transporter GLYT2 is present in axonal boutons throughout the spinal cord, and its laminar distribution matches that of glycine-enriched axons, which are presumed to be glycinergic.	Glycine	4-11	solute carrier family 6 member 5	Rattus norvegicus	24-29
9472410-6	1997	These results confirm that GLYT2 is associated with glycine-enriched axonal boutons in the superficial dorsal horn.	Glycine	52-59	solute carrier family 6 member 5	Rattus norvegicus	27-32
7700536-3	1995	In this study we examined, by means of in situ hybridization with 35S-labelled oligodeoxynucleotide probes, the distribution of messenger RNAs encoding glycine transporter 2 in the rat CNS.	Sulfur-35	66-69	solute carrier family 6 member 5	Rattus norvegicus	152-173
8226790-9	1993	The experimental data suggests GLYT2 might play a major role in the termination of the inhibitory effect of glycine in the brain stem and spinal cord of vertebrates.	Glycine	108-115	solute carrier family 6 member 5	Rattus norvegicus	31-36
32172509-0	2020	Phosphorylation of Serine 157 Protects the Rat Glycine Transporter GlyT2 from Calpain Cleavage.	Serine	19-25	solute carrier family 6 member 5	Rattus norvegicus	67-72
29608917-0	2018	Time-dependent, bidirectional, anti- and pro-spinal hyper-reflexia and muscle spasticity effect after chronic spinal glycine transporter 2 (GlyT2) oligonucleotide-induced downregulation.	Oligonucleotides	147-162	solute carrier family 6 member 5	Rattus norvegicus	117-138
30714733-0	2019	Development of an N-Acyl Amino Acid That Selectively Inhibits the Glycine Transporter 2 To Produce Analgesia in a Rat Model of Chronic Pain.	n-acyl amino acid	18-35	solute carrier family 6 member 5	Rattus norvegicus	66-87
30714733-2	2019	Acyl-glycine inhibitors, however, are selective for GlyT2 and have been shown to provide analgesia in animal models of pain with minimal side effects, but are comparatively weak GlyT2 inhibitors.	acyl-glycine	0-12	solute carrier family 6 member 5	Rattus norvegicus	52-57
30714733-2	2019	Acyl-glycine inhibitors, however, are selective for GlyT2 and have been shown to provide analgesia in animal models of pain with minimal side effects, but are comparatively weak GlyT2 inhibitors.	acyl-glycine	0-12	solute carrier family 6 member 5	Rattus norvegicus	178-183
30714733-3	2019	Here, we modify the simple acyl-glycine by synthesizing lipid analogues with a range of amino acid head groups in both l- and d-configurations, to produce nanomolar affinity, selective GlyT2 inhibitors.	acyl-glycine	27-39	solute carrier family 6 member 5	Rattus norvegicus	185-190
29608917-0	2018	Time-dependent, bidirectional, anti- and pro-spinal hyper-reflexia and muscle spasticity effect after chronic spinal glycine transporter 2 (GlyT2) oligonucleotide-induced downregulation.	Oligonucleotides	147-162	solute carrier family 6 member 5	Rattus norvegicus	140-145
29608917-8	2018	Chronic hyper-reflexia induced by GlyT2-ASO treatment was effectively blocked by intrathecal glycine.	Glycine	93-100	solute carrier family 6 member 5	Rattus norvegicus	34-39
29608917-10	2018	These data demonstrate that spinal GlyT2 downregulation provides only a time-limited therapeutic benefit and that subsequent loss of glycine vesicular synthesis resulting from chronic GlyT2 downregulation near completely eliminates the tonic glycine-ergic activity and is functionally expressed as profound spinal hyper-reflexia.	Glycine	133-140	solute carrier family 6 member 5	Rattus norvegicus	184-189
29608917-10	2018	These data demonstrate that spinal GlyT2 downregulation provides only a time-limited therapeutic benefit and that subsequent loss of glycine vesicular synthesis resulting from chronic GlyT2 downregulation near completely eliminates the tonic glycine-ergic activity and is functionally expressed as profound spinal hyper-reflexia.	Glycine	242-249	solute carrier family 6 member 5	Rattus norvegicus	184-189
29500820-4	2018	One approach to increase synaptic glycine is to inhibit the activity of the glycine transporter 2 (GlyT2) on inhibitory nerve terminals.	Glycine	34-41	solute carrier family 6 member 5	Rattus norvegicus	76-97
29500820-4	2018	One approach to increase synaptic glycine is to inhibit the activity of the glycine transporter 2 (GlyT2) on inhibitory nerve terminals.	Glycine	34-41	solute carrier family 6 member 5	Rattus norvegicus	99-104
29500820-6	2018	Inhibiting activity of GlyT2 increases synaptic glycine, which decreases excitability in nociceptive circuits and provides analgesia in neuropathic and inflammatory pain models.	Glycine	48-55	solute carrier family 6 member 5	Rattus norvegicus	23-28