PMID-sentid	Pub_year	Sent_text	comp_official_name	comp_offset	protein_name	organism	prot_offset
31742833-2	2020	Remarkably, NMDA receptor activation is aided by a second protein, postsynaptic density of 95 kDa (PSD95), forming the ternary protein complex NMDA/PSD95/nNOS.	N-Methylaspartate	12-16	discs large MAGUK scaffold protein 4	Homo sapiens	99-104
32551298-5	2020	In the CM-STZ rodent model of AD, we observed increase in extracellular amyloid-beta (Abeta) deposition and decrease and abnormal morphology of post-synaptic protein, PSD95 in 16 weeks STZ-injected group.	Streptozocin	10-13	discs large MAGUK scaffold protein 4	Homo sapiens	167-172
32551298-5	2020	In the CM-STZ rodent model of AD, we observed increase in extracellular amyloid-beta (Abeta) deposition and decrease and abnormal morphology of post-synaptic protein, PSD95 in 16 weeks STZ-injected group.	Streptozocin	185-188	discs large MAGUK scaffold protein 4	Homo sapiens	167-172
32045717-7	2020	Acute TMZ exposure (4 h) caused a rapid reduction in dendritic branching and loss of postsynaptic density-95 (PSD95) puncta on dendrites.	temozolomide	6-9	discs large MAGUK scaffold protein 4	Homo sapiens	85-108
32045717-7	2020	Acute TMZ exposure (4 h) caused a rapid reduction in dendritic branching and loss of postsynaptic density-95 (PSD95) puncta on dendrites.	temozolomide	6-9	discs large MAGUK scaffold protein 4	Homo sapiens	110-115
31742833-2	2020	Remarkably, NMDA receptor activation is aided by a second protein, postsynaptic density of 95 kDa (PSD95), forming the ternary protein complex NMDA/PSD95/nNOS.	N-Methylaspartate	12-16	discs large MAGUK scaffold protein 4	Homo sapiens	148-153
31742833-2	2020	Remarkably, NMDA receptor activation is aided by a second protein, postsynaptic density of 95 kDa (PSD95), forming the ternary protein complex NMDA/PSD95/nNOS.	N-Methylaspartate	143-147	discs large MAGUK scaffold protein 4	Homo sapiens	99-104
31742833-2	2020	Remarkably, NMDA receptor activation is aided by a second protein, postsynaptic density of 95 kDa (PSD95), forming the ternary protein complex NMDA/PSD95/nNOS.	N-Methylaspartate	143-147	discs large MAGUK scaffold protein 4	Homo sapiens	148-153
32256312-5	2020	Pin1 associates via its WW domain with phosphorylated threonine (T19) and serine (S25) in the N-terminus domain of PSD-95 and this association alters the local conformation of PSD-95.	Serine	74-80	discs large MAGUK scaffold protein 4	Homo sapiens	115-121
32256312-5	2020	Pin1 associates via its WW domain with phosphorylated threonine (T19) and serine (S25) in the N-terminus domain of PSD-95 and this association alters the local conformation of PSD-95.	Threonine	54-63	discs large MAGUK scaffold protein 4	Homo sapiens	115-121
32256312-6	2020	Most importantly, I show that proline-directed phosphorylation of the N-terminus domain of PSD-95 alters the local conformation of this region.	Proline	30-37	discs large MAGUK scaffold protein 4	Homo sapiens	91-97
32256312-5	2020	Pin1 associates via its WW domain with phosphorylated threonine (T19) and serine (S25) in the N-terminus domain of PSD-95 and this association alters the local conformation of PSD-95.	Threonine	54-63	discs large MAGUK scaffold protein 4	Homo sapiens	176-182
32256312-7	2020	Therefore, proline-directed phosphorylation of the N-terminus of PSD-95, Pin1 association, and peptidyl-prolyl cis-trans isomerization may all play a role in excitatory synaptic function and synapse development.	Proline	11-18	discs large MAGUK scaffold protein 4	Homo sapiens	65-71
32087818-1	2020	BACKGROUND: Nerinetide, an eicosapeptide that interferes with post-synaptic density protein 95, is a neuroprotectant that is effective in preclinical stroke models of ischaemia-reperfusion.	Tat-NR2B9c	12-22	discs large MAGUK scaffold protein 4	Homo sapiens	62-94
32087818-1	2020	BACKGROUND: Nerinetide, an eicosapeptide that interferes with post-synaptic density protein 95, is a neuroprotectant that is effective in preclinical stroke models of ischaemia-reperfusion.	eicosapeptide	27-40	discs large MAGUK scaffold protein 4	Homo sapiens	62-94
31831623-4	2020	The postsynaptic density protein PSD-95 contains a three-domain supramodule (denoted PSG), which consists of PDZ, SH3, and guanylate kinase-like domains.	2'(3')-O-(glycyl)guanosine-5'-(O-methylphosphate)	123-132	discs large MAGUK scaffold protein 4	Homo sapiens	33-39
32231520-2	2020	Phosphorylation of the N-terminus of PSD-95 at threonine 19 (T19) and serine 25 (S25) decreases PSD-95 stability at synapses; however, a molecular mechanism linking PSD-95 phosphorylation to altered synaptic stability is lacking.	Threonine	47-56	discs large MAGUK scaffold protein 4	Homo sapiens	37-43
32231520-2	2020	Phosphorylation of the N-terminus of PSD-95 at threonine 19 (T19) and serine 25 (S25) decreases PSD-95 stability at synapses; however, a molecular mechanism linking PSD-95 phosphorylation to altered synaptic stability is lacking.	Threonine	47-56	discs large MAGUK scaffold protein 4	Homo sapiens	96-102
32231520-2	2020	Phosphorylation of the N-terminus of PSD-95 at threonine 19 (T19) and serine 25 (S25) decreases PSD-95 stability at synapses; however, a molecular mechanism linking PSD-95 phosphorylation to altered synaptic stability is lacking.	Threonine	47-56	discs large MAGUK scaffold protein 4	Homo sapiens	96-102
32231520-2	2020	Phosphorylation of the N-terminus of PSD-95 at threonine 19 (T19) and serine 25 (S25) decreases PSD-95 stability at synapses; however, a molecular mechanism linking PSD-95 phosphorylation to altered synaptic stability is lacking.	Serine	70-76	discs large MAGUK scaffold protein 4	Homo sapiens	96-102
32231520-2	2020	Phosphorylation of the N-terminus of PSD-95 at threonine 19 (T19) and serine 25 (S25) decreases PSD-95 stability at synapses; however, a molecular mechanism linking PSD-95 phosphorylation to altered synaptic stability is lacking.	Serine	70-76	discs large MAGUK scaffold protein 4	Homo sapiens	96-102
32231520-3	2020	Here, we show that phosphorylation of T19/S25 recruits the phosphorylation-dependent peptidyl-prolyl cis-trans isomerase (Pin1) and reduces the palmitoylation of Cysteine 3 and Cysteine 5 in PSD-95.	Cysteine	162-170	discs large MAGUK scaffold protein 4	Homo sapiens	191-197
32231520-3	2020	Here, we show that phosphorylation of T19/S25 recruits the phosphorylation-dependent peptidyl-prolyl cis-trans isomerase (Pin1) and reduces the palmitoylation of Cysteine 3 and Cysteine 5 in PSD-95.	Cysteine	177-185	discs large MAGUK scaffold protein 4	Homo sapiens	191-197
31919735-0	2020	Correction to: Phosphomimetic Mutation of Glycine Transporter GlyT1 C-Terminal PDZ Binding Motif Inhibits its Interactions with PSD95.	Glycine	42-49	discs large MAGUK scaffold protein 4	Homo sapiens	128-133
31919735-0	2020	Correction to: Phosphomimetic Mutation of Glycine Transporter GlyT1 C-Terminal PDZ Binding Motif Inhibits its Interactions with PSD95.	Carbon	0-1	discs large MAGUK scaffold protein 4	Homo sapiens	128-133
32029829-1	2020	PSD-95, via interactions with stargazin, anchors AMPA receptors at the synapse and regulates AMPAR currents.	alpha-Amino-3-hydroxy-5-methyl-4-isoxazolepropionic Acid	49-53	discs large MAGUK scaffold protein 4	Homo sapiens	0-6
32029829-4	2020	Here, we show that NMDA-induced long-term depression of synaptic transmission (NMDA-LTD) is accompanied by downregulation of PSD-95 protein levels.	N-Methylaspartate	19-23	discs large MAGUK scaffold protein 4	Homo sapiens	125-131
32029829-4	2020	Here, we show that NMDA-induced long-term depression of synaptic transmission (NMDA-LTD) is accompanied by downregulation of PSD-95 protein levels.	N-Methylaspartate	79-83	discs large MAGUK scaffold protein 4	Homo sapiens	125-131
32029829-5	2020	Using pharmacologic and molecular manipulations, we further demonstrate that the NMDA-induced downregulation of PSD-95 depends on the activation of CaMKII and CaMKII-driven phosphorylation of PSD-95 serine 73.	N-Methylaspartate	81-85	discs large MAGUK scaffold protein 4	Homo sapiens	112-118
32029829-5	2020	Using pharmacologic and molecular manipulations, we further demonstrate that the NMDA-induced downregulation of PSD-95 depends on the activation of CaMKII and CaMKII-driven phosphorylation of PSD-95 serine 73.	cholecystokinin C-terminal flanking peptide	199-205	discs large MAGUK scaffold protein 4	Homo sapiens	112-118
31753031-6	2019	This interaction was mediated by the C-terminal tail regions of KIF5A and the third PDZ domain of PSD-95.	Carbon	37-38	discs large MAGUK scaffold protein 4	Homo sapiens	98-104
31938742-3	2020	Key findings: Prenatal alcohol exposure induced the generation of ROS, nitrite and lipid peroxide, decreased mitochondrial Complex-I and IV activities, increased Caspase-1 and 3 activities, had no effect on cholinergic neurotransmission, increased expression of PSD-95, decreased LTP and decreased performance on spatial memory tasks.	Ethanol	23-30	discs large MAGUK scaffold protein 4	Homo sapiens	262-268
31454827-9	2019	D-methadone administration also increased levels of the synaptic proteins, PSD95, GluA1, and Synapsin 1 and enhanced synaptic function in the mPFC.	D-methadone	0-11	discs large MAGUK scaffold protein 4	Homo sapiens	75-80
32039235-9	2020	Moreover, the molecular dynamic simulation for the complex of DLG1 and GKI-QSF was carried out and predicted that the GKI-QSF could bind with DLG1 with similar Kd value compared to DLG4/GKI-QSF, which was verified by using ITC assay (Kd = 1.20 +- 0.29 muM).	24-telluracholestanol	223-226	discs large MAGUK scaffold protein 4	Homo sapiens	181-185
32066698-9	2020	Furthermore, 17beta-estradiol also caused the enrichment of synaptic proteins at synapses and increased the number of dendritic spines containing PSD-95 or that overlapped with the pre-synaptic marker bassoon.	Estradiol	13-29	discs large MAGUK scaffold protein 4	Homo sapiens	146-152
31753031-7	2019	Additionally, the ADPDZ3 (the association domain of NMDA receptor and PDZ3 domain) expression significantly reduced the levels of PSD-95, glutamate receptor 1 (GluA1) in dendrites.	N-Methylaspartate	52-56	discs large MAGUK scaffold protein 4	Homo sapiens	130-136
31753031-9	2019	Taken together, our data suggest a new mechanism for dendritic transport of the AMPA receptor-PSD-95.	alpha-Amino-3-hydroxy-5-methyl-4-isoxazolepropionic Acid	80-84	discs large MAGUK scaffold protein 4	Homo sapiens	94-100
31246351-11	2019	Intriguingly, addition of the astrocyte-derived synapse maturation inducer cholesterol increased the dendritic density of PSD95-positive excitatory synapses in glia- cultures.	Cholesterol	75-86	discs large MAGUK scaffold protein 4	Homo sapiens	122-127
31827434-7	2019	Our data also suggest that STAT3 might play a role in ketamine"s antidepressant effects, mediated, at least in part, through eukaryotic elongation factor 2 (EEF2), resulting in the augmentation of brain-derived neurotropic factor (BDNF) expression and promoting the synthesis of synaptic proteins postsynaptic density protein 95 (PSD95) and synapsin I (SYN1).	Ketamine	54-62	discs large MAGUK scaffold protein 4	Homo sapiens	297-328
31827434-7	2019	Our data also suggest that STAT3 might play a role in ketamine"s antidepressant effects, mediated, at least in part, through eukaryotic elongation factor 2 (EEF2), resulting in the augmentation of brain-derived neurotropic factor (BDNF) expression and promoting the synthesis of synaptic proteins postsynaptic density protein 95 (PSD95) and synapsin I (SYN1).	Ketamine	54-62	discs large MAGUK scaffold protein 4	Homo sapiens	330-335
31344440-5	2019	Further investigation of such interaction using mutational analyses revealed that mutating the alanine residue at 175 residue of beta-arrestin2 to phenylalanine impairs interaction with PSD-95.	Alanine	95-102	discs large MAGUK scaffold protein 4	Homo sapiens	186-192
31344440-5	2019	Further investigation of such interaction using mutational analyses revealed that mutating the alanine residue at 175 residue of beta-arrestin2 to phenylalanine impairs interaction with PSD-95.	Phenylalanine	147-160	discs large MAGUK scaffold protein 4	Homo sapiens	186-192
31236807-5	2019	Furthermore, YL-0919 treatment for 5 days reversed the brain derived neurotrophic factor (BDNF)-mammalian target of rapamycin (mTOR) signaling and the key synaptic proteins, such as post-synaptic density (PSD95), GluR1 and presynaptic protein synapsin1.	1-(1-benzyl-4-hydroxypiperidin-4-ylmethyl)-2(1H)-pyridinone	13-20	discs large MAGUK scaffold protein 4	Homo sapiens	205-210
31102917-9	2019	The intracellular calcium levels were elevated in hCNs after BPA exposure through NMDARs-nNOS-PSD-95 mediating.	Calcium	18-25	discs large MAGUK scaffold protein 4	Homo sapiens	94-100
31102917-9	2019	The intracellular calcium levels were elevated in hCNs after BPA exposure through NMDARs-nNOS-PSD-95 mediating.	bisphenol A	61-64	discs large MAGUK scaffold protein 4	Homo sapiens	94-100
30988255-6	2019	In this work, crystallographic structures of the following have been solved: a truncated form of the third PDZ domain of the neuronal postsynaptic density protein 95 from which alpha3 has been removed, D332P and D332G variants of the protein, and a new crystal form of this domain showing the binding of Asp332 to the carboxylate-binding site of a symmetry-related molecule.	carboxylate	318-329	discs large MAGUK scaffold protein 4	Homo sapiens	134-165
30747034-2	2019	Despite the fact that much is known about the role of PSD-95 in NMDA-mediated toxicity, less is known about its role in mechanical injury, and more specifically, in traumatic brain injury (TBI).	N-Methylaspartate	64-68	discs large MAGUK scaffold protein 4	Homo sapiens	54-60
30953815-5	2019	Using presynaptic protein synaptophysin and postsynaptic protein PSD-95 antibodies, immunofluorescence staining and western blotting results indicated that BPA exposure altered the morphology of dendritic spines and increased synaptophysin and PSD-95 expression.	bisphenol A	156-159	discs large MAGUK scaffold protein 4	Homo sapiens	65-71
30953815-5	2019	Using presynaptic protein synaptophysin and postsynaptic protein PSD-95 antibodies, immunofluorescence staining and western blotting results indicated that BPA exposure altered the morphology of dendritic spines and increased synaptophysin and PSD-95 expression.	bisphenol A	156-159	discs large MAGUK scaffold protein 4	Homo sapiens	244-250
30709918-6	2019	Furthermore, our data indicate that tPA-induced p35-mediated Cdk5 activation does not induce cell death, but instead prevents NMDA-induced ubiquitylation of postsynaptic density protein-95 (PSD-95; also known as Dlg4) and the removal of GluR1 (also known as Gria1)-containing alpha-amino-3-hydroxy-5-methyl-4-isoxazoleproprionic acid (AMPA) receptors from the PSD.	N-Methylaspartate	126-130	discs large MAGUK scaffold protein 4	Homo sapiens	157-188
30481547-5	2019	Compared with vehicles, NAbs-alpha-syn significantly attenuated the memory and motor deficits by reducing the levels of soluble alpha-syn, total human alpha-syn and alpha-syn oligomers, decreasing the intracellular p-alpha-synser129 deposits and axonal pathology, inhibiting the microgliosis and astrogliosis, as well as the production of proinflammatory cytokines, increasing the levels of PSD95, synaptophysin and TH in the brain of A53T transgenic mice.	nabs	24-28	discs large MAGUK scaffold protein 4	Homo sapiens	391-396
31024297-5	2019	Melatonin (5 mg/kg) attenuated ischemia-induced down regulation of NMDA receptor 2 (NR2a), postsynaptic density-95 (PSD95) and increases NR2a/PSD95 complex association, which further activates the pro-survival PI3K/Akt/GSK3beta pathway with mitigated collapsin response mediator protein 2 (CRMP2) phosphorylation.	Melatonin	0-9	discs large MAGUK scaffold protein 4	Homo sapiens	91-114
31024297-5	2019	Melatonin (5 mg/kg) attenuated ischemia-induced down regulation of NMDA receptor 2 (NR2a), postsynaptic density-95 (PSD95) and increases NR2a/PSD95 complex association, which further activates the pro-survival PI3K/Akt/GSK3beta pathway with mitigated collapsin response mediator protein 2 (CRMP2) phosphorylation.	Melatonin	0-9	discs large MAGUK scaffold protein 4	Homo sapiens	116-121
31024297-5	2019	Melatonin (5 mg/kg) attenuated ischemia-induced down regulation of NMDA receptor 2 (NR2a), postsynaptic density-95 (PSD95) and increases NR2a/PSD95 complex association, which further activates the pro-survival PI3K/Akt/GSK3beta pathway with mitigated collapsin response mediator protein 2 (CRMP2) phosphorylation.	Melatonin	0-9	discs large MAGUK scaffold protein 4	Homo sapiens	142-147
30709918-6	2019	Furthermore, our data indicate that tPA-induced p35-mediated Cdk5 activation does not induce cell death, but instead prevents NMDA-induced ubiquitylation of postsynaptic density protein-95 (PSD-95; also known as Dlg4) and the removal of GluR1 (also known as Gria1)-containing alpha-amino-3-hydroxy-5-methyl-4-isoxazoleproprionic acid (AMPA) receptors from the PSD.	N-Methylaspartate	126-130	discs large MAGUK scaffold protein 4	Homo sapiens	190-196
30709918-6	2019	Furthermore, our data indicate that tPA-induced p35-mediated Cdk5 activation does not induce cell death, but instead prevents NMDA-induced ubiquitylation of postsynaptic density protein-95 (PSD-95; also known as Dlg4) and the removal of GluR1 (also known as Gria1)-containing alpha-amino-3-hydroxy-5-methyl-4-isoxazoleproprionic acid (AMPA) receptors from the PSD.	N-Methylaspartate	126-130	discs large MAGUK scaffold protein 4	Homo sapiens	212-216
30254284-5	2018	Membrane depolarization by high extracellular potassium maintained PSD-95 puncta density and partially rescued both spontaneous synaptic activity and cell death, while spike generation remained blocked.	Potassium	46-55	discs large MAGUK scaffold protein 4	Homo sapiens	67-73
30395175-2	2019	Here, we show that an excess of the blood-brain barrier permeable cholesterol metabolite 27-hydroxycholesterol (27-OH) impairs neuronal morphology and reduces hippocampal spine density and the levels of the postsynaptic protein PSD95.	Cholesterol	66-77	discs large MAGUK scaffold protein 4	Homo sapiens	228-233
30395175-2	2019	Here, we show that an excess of the blood-brain barrier permeable cholesterol metabolite 27-hydroxycholesterol (27-OH) impairs neuronal morphology and reduces hippocampal spine density and the levels of the postsynaptic protein PSD95.	27-hydroxycholesterol	89-110	discs large MAGUK scaffold protein 4	Homo sapiens	228-233
30395175-6	2019	Here, we report that high levels of 27-OH induce REST-miR124a-PTBP1 axis dysregulation in a possible RxRgamma-dependent manner, suggesting that 27-OH reduces PSD95 levels through this mechanism.	27-hydroxycholesterol	36-41	discs large MAGUK scaffold protein 4	Homo sapiens	158-163
30395175-6	2019	Here, we report that high levels of 27-OH induce REST-miR124a-PTBP1 axis dysregulation in a possible RxRgamma-dependent manner, suggesting that 27-OH reduces PSD95 levels through this mechanism.	27-hydroxycholesterol	144-149	discs large MAGUK scaffold protein 4	Homo sapiens	158-163
30524234-9	2018	Western blotting showed that YL-0919 significantly enhanced the expression levels of synaptic proteins such as synapsin I, postsynaptic density protein 95 (PSD95), phosphorylated mammalian targeting of rapamycin (pmTOR) and brain-derived neurotrophic factor (BDNF) in the hippocampus.	1-(1-benzyl-4-hydroxypiperidin-4-ylmethyl)-2(1H)-pyridinone	29-36	discs large MAGUK scaffold protein 4	Homo sapiens	123-154
30524234-9	2018	Western blotting showed that YL-0919 significantly enhanced the expression levels of synaptic proteins such as synapsin I, postsynaptic density protein 95 (PSD95), phosphorylated mammalian targeting of rapamycin (pmTOR) and brain-derived neurotrophic factor (BDNF) in the hippocampus.	1-(1-benzyl-4-hydroxypiperidin-4-ylmethyl)-2(1H)-pyridinone	29-36	discs large MAGUK scaffold protein 4	Homo sapiens	156-161
31152397-6	2019	Here, we describe a systematic method to screen the ABHD serine hydrolase genes, which unveiled ABHD17 as the depalmitoylating enzyme for PSD-95.	Serine	57-63	discs large MAGUK scaffold protein 4	Homo sapiens	138-144
30581378-4	2018	Here, we reported the characterization of a small molecule (Methyl 3,4-dihydroxybenzoate; MDHB) that selectively induces hippocampal NSCs to differentiate into cholinergic motor neurons which expressed synapsin 1 (SYN1) and postsynaptic density protein 95 (PSD-95).	methyl 3,4-dihydroxybenzoate	60-88	discs large MAGUK scaffold protein 4	Homo sapiens	224-255
30581378-4	2018	Here, we reported the characterization of a small molecule (Methyl 3,4-dihydroxybenzoate; MDHB) that selectively induces hippocampal NSCs to differentiate into cholinergic motor neurons which expressed synapsin 1 (SYN1) and postsynaptic density protein 95 (PSD-95).	methyl 3,4-dihydroxybenzoate	60-88	discs large MAGUK scaffold protein 4	Homo sapiens	257-263
30581378-4	2018	Here, we reported the characterization of a small molecule (Methyl 3,4-dihydroxybenzoate; MDHB) that selectively induces hippocampal NSCs to differentiate into cholinergic motor neurons which expressed synapsin 1 (SYN1) and postsynaptic density protein 95 (PSD-95).	methyl 3,4-dihydroxybenzoate	90-94	discs large MAGUK scaffold protein 4	Homo sapiens	224-255
30581378-4	2018	Here, we reported the characterization of a small molecule (Methyl 3,4-dihydroxybenzoate; MDHB) that selectively induces hippocampal NSCs to differentiate into cholinergic motor neurons which expressed synapsin 1 (SYN1) and postsynaptic density protein 95 (PSD-95).	methyl 3,4-dihydroxybenzoate	90-94	discs large MAGUK scaffold protein 4	Homo sapiens	257-263
30125942-4	2018	Here, we present evidence showing that Asef1 negatively regulates the synaptic localization of postsynaptic density protein 95 (PSD-95) in the excitatory synapse by inhibiting Staufen-mediated synaptic localization of PSD-95.	staufen	176-183	discs large MAGUK scaffold protein 4	Homo sapiens	95-126
30125942-4	2018	Here, we present evidence showing that Asef1 negatively regulates the synaptic localization of postsynaptic density protein 95 (PSD-95) in the excitatory synapse by inhibiting Staufen-mediated synaptic localization of PSD-95.	staufen	176-183	discs large MAGUK scaffold protein 4	Homo sapiens	128-134
30125942-4	2018	Here, we present evidence showing that Asef1 negatively regulates the synaptic localization of postsynaptic density protein 95 (PSD-95) in the excitatory synapse by inhibiting Staufen-mediated synaptic localization of PSD-95.	staufen	176-183	discs large MAGUK scaffold protein 4	Homo sapiens	218-224
29547062-3	2018	The postsynaptic density protein-95 (PSD-95) is the most abundant scaffolding protein in the postsynaptic density (PSD), where it modulates the postsynaptic response to the presynaptic release of glutamate by regulating the anchoring of glutamate receptors to the PSD.	Glutamic Acid	196-205	discs large MAGUK scaffold protein 4	Homo sapiens	4-35
29547062-3	2018	The postsynaptic density protein-95 (PSD-95) is the most abundant scaffolding protein in the postsynaptic density (PSD), where it modulates the postsynaptic response to the presynaptic release of glutamate by regulating the anchoring of glutamate receptors to the PSD.	Glutamic Acid	196-205	discs large MAGUK scaffold protein 4	Homo sapiens	37-43
29547062-5	2018	Our data show that PSD-95 is removed from the PSD during the early stages of cerebral ischemia, and that this effect is abrogated by either the release of neuronal tPA, or intravenous administration of recombinant tPA (rtPA).	rtpa	219-223	discs large MAGUK scaffold protein 4	Homo sapiens	19-25
30510585-16	2018	Conclusion: Edaravone can dose-dependently induce hUMSCs to differentiate into neuron-like cells that expressed the neuronal markers including NSE, nestin, and GFAP and synaptic makers such as SYN, PSD95, and GAP43.	Edaravone	12-21	discs large MAGUK scaffold protein 4	Homo sapiens	198-203
29751053-4	2018	Consistent with our previous findings, we found that treatment with l-Cysteine after HI reduced early brain injury, improved behavioral deficits and synaptic damage, effects which were associated with an up-regulation of synaptophysin and postsynaptic density protein 95 expression in the lesioned cortex.	Cysteine	68-78	discs large MAGUK scaffold protein 4	Homo sapiens	239-270
29384407-7	2018	Protein amounts of neurofilament proteins, NF-H, NF-M, PSD-95 in post-synaptic density, GAP-43 in growing neurites and NeuN in differentiated neurons were upregulated by addition of ACB, indicating that cell survival increased in differentiated neurons, shown by immunoblot analysis.	aucubin	182-185	discs large MAGUK scaffold protein 4	Homo sapiens	55-61
30143658-2	2018	However, postsynaptic density-95 (PSD-95) and neuronal nitric oxide synthase (nNOS) coupling, the downstream signaling of NMDARs activation, obstructs the BDNF signaling transduction.	nmdars	122-128	discs large MAGUK scaffold protein 4	Homo sapiens	9-32
30143658-2	2018	However, postsynaptic density-95 (PSD-95) and neuronal nitric oxide synthase (nNOS) coupling, the downstream signaling of NMDARs activation, obstructs the BDNF signaling transduction.	nmdars	122-128	discs large MAGUK scaffold protein 4	Homo sapiens	34-40
30143658-9	2018	Because inhibitors of PSD-95-nNOS interaction produce antidepressant and anxiolytic effect without NMDAR-induced side effects, PSD-95-nNOS could be a valuable target for PTSD treatment.	nmdar	99-104	discs large MAGUK scaffold protein 4	Homo sapiens	22-28
30126976-5	2018	We incorporated these oligonucleotides into a phage library and screened the PDZ (PSD-95/Dlg/ZO-1) domains of Scribble and DLG1 for interactions potentially enabled or disabled by ligand phosphorylation.	Oligonucleotides	22-38	discs large MAGUK scaffold protein 4	Homo sapiens	82-88
30108200-2	2018	Following NMDAR activation, efficient production of NO requires linking the 95 kDa postsynaptic density protein (PSD95), a scaffolding protein to neuronal nitric oxide synthase (nNOS).	nmdar	10-15	discs large MAGUK scaffold protein 4	Homo sapiens	113-118
30108200-5	2018	Our results show that systemic treatment with ZL006, a compound that disrupts PSD95/nNOS binding, attenuates fear memory compared to its inactive isomer ZL007.	4-((3,5-dichloro-2-hydroxybenzyl)amino)-2-hydroxybenzoic acid	46-51	discs large MAGUK scaffold protein 4	Homo sapiens	78-83
30108200-6	2018	Co-immunoprecipitation after fear conditioning showed a robust increase in the amygdala PSD95/nNOS binding, which was blocked by systemic pre-administration of ZL006.	4-((3,5-dichloro-2-hydroxybenzyl)amino)-2-hydroxybenzoic acid	160-165	discs large MAGUK scaffold protein 4	Homo sapiens	88-93
30108200-10	2018	These findings support the hypothesis that disrupting the PSD95/nNOS interaction downstream of NMDARs selectively reduces fear memory, and highlights PSD95/nNOS interaction as a novel target for fear-related disorders, such as posttraumatic stress disorder.	nmdars	95-101	discs large MAGUK scaffold protein 4	Homo sapiens	58-63
29565039-3	2018	Recent findings have provided insights into the pathophysiology and mechanisms of ischemic stroke, complementing the traditional glutamate hypothesis: the molecular interaction between PSD95 and GluN2B has been identified as a culprit in stroke-mediated excitotoxicity, leading to the discovery of NA-1, a peptide that disrupts that interaction, as a potent neuroprotective agent for the treatment of acute stroke.	Glutamic Acid	129-138	discs large MAGUK scaffold protein 4	Homo sapiens	185-190
29618004-7	2018	Importantly, we find that tianeptine, a cognitive enhancer and antidepressant drug, known to recruit and stabilise AMPA-Rs at the synaptic sites, can normalise the expression of membrane inserted AMPA-Rs as well as the number of PSD-95 clusters, suggesting its therapeutic potential for patients with mutations in CDKL5.	tianeptine	26-36	discs large MAGUK scaffold protein 4	Homo sapiens	229-235
29910712-6	2018	Indeed, palmitate cycling on postsynaptic density-95 (PSD-95), the major postsynaptic density protein at excitatory synapses, regulates the number of synaptic alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptors (AMPARs) and thus affects synaptic transmission.	Palmitates	8-17	discs large MAGUK scaffold protein 4	Homo sapiens	29-52
29910712-6	2018	Indeed, palmitate cycling on postsynaptic density-95 (PSD-95), the major postsynaptic density protein at excitatory synapses, regulates the number of synaptic alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptors (AMPARs) and thus affects synaptic transmission.	Palmitates	8-17	discs large MAGUK scaffold protein 4	Homo sapiens	54-60
29225110-6	2018	Prenatal nicotine and alcohol exposure induced oxidative stress, did not affect the mitochondrial functions, increased the monoamine oxidase activity, increased caspase expression and decreased ILK, PSD-95 and GLUR1 expression without affecting the GSK-3beta.	Nicotine	9-17	discs large MAGUK scaffold protein 4	Homo sapiens	199-205
28343296-8	2018	Cypermethrin induced Parkinsonian traits and attenuated the dendritic length, spine number and expression of synaptophysin and PSD-95.	cypermethrin	0-12	discs large MAGUK scaffold protein 4	Homo sapiens	127-133
28343296-10	2018	Ibuprofen normalized the changes in dendritic morphology, length, spine number and expression of synaptophysin, PSD-95, and pro-inflammatory and apoptotic proteins.	Ibuprofen	0-9	discs large MAGUK scaffold protein 4	Homo sapiens	112-118
29429936-4	2018	Mutating lysine at position 10 or lysine at position 11 of PSD-95 to glutamate, or glutamate at position 53 or glutamate and aspartate at positions 213 and 217 of alpha-actinin, respectively, to lysine impairs, in parallel, PSD-95 binding to alpha-actinin and postsynaptic localization of PSD-95 and AMPARs.	Lysine	9-15	discs large MAGUK scaffold protein 4	Homo sapiens	59-65
29429936-4	2018	Mutating lysine at position 10 or lysine at position 11 of PSD-95 to glutamate, or glutamate at position 53 or glutamate and aspartate at positions 213 and 217 of alpha-actinin, respectively, to lysine impairs, in parallel, PSD-95 binding to alpha-actinin and postsynaptic localization of PSD-95 and AMPARs.	Lysine	34-40	discs large MAGUK scaffold protein 4	Homo sapiens	59-65
29429936-4	2018	Mutating lysine at position 10 or lysine at position 11 of PSD-95 to glutamate, or glutamate at position 53 or glutamate and aspartate at positions 213 and 217 of alpha-actinin, respectively, to lysine impairs, in parallel, PSD-95 binding to alpha-actinin and postsynaptic localization of PSD-95 and AMPARs.	Glutamic Acid	69-78	discs large MAGUK scaffold protein 4	Homo sapiens	59-65
29429936-4	2018	Mutating lysine at position 10 or lysine at position 11 of PSD-95 to glutamate, or glutamate at position 53 or glutamate and aspartate at positions 213 and 217 of alpha-actinin, respectively, to lysine impairs, in parallel, PSD-95 binding to alpha-actinin and postsynaptic localization of PSD-95 and AMPARs.	Lysine	34-40	discs large MAGUK scaffold protein 4	Homo sapiens	59-65
29267967-6	2018	In-depth functional studies showed that a frame-shift mutation, FRMPD4p.Cys618ValfsX8, results in a disruption of FRMPD4 binding with PSD-95 and HOMER1, and a failure to increase spine density in transfected hippocampal neurons.	cys618valfsx8	72-85	discs large MAGUK scaffold protein 4	Homo sapiens	134-140
29225110-6	2018	Prenatal nicotine and alcohol exposure induced oxidative stress, did not affect the mitochondrial functions, increased the monoamine oxidase activity, increased caspase expression and decreased ILK, PSD-95 and GLUR1 expression without affecting the GSK-3beta.	Alcohols	22-29	discs large MAGUK scaffold protein 4	Homo sapiens	199-205
29484270-12	2018	DLGAP1 was associated with cognitive flexibility and plan, and the role of DLGAP1 might be implemented through the complex of DLGAP1-DLG4-NMDA.	N-Methylaspartate	138-142	discs large MAGUK scaffold protein 4	Homo sapiens	133-137
28158955-4	2017	Further investigation demonstrated that this effect of H2S was mediated by reversing the CUMS-induced decrease in dendritic spine density and required the activation of mammalian target of rapamycin (mTOR)C1 and neurotrophic TrkB receptors, which proceeded to increase synaptic protein expression, including postsynaptic density protein 95, synaptophysin, and alpha-amino-3-hydroxy-5-methyl-4-isoxazole-propionic acid receptor GluR1/2 subunit.	cums	89-93	discs large MAGUK scaffold protein 4	Homo sapiens	308-339
29118000-4	2018	Our NMR structural analysis identified E17 within the PSD-95 N-terminus as important for binding to Ca2+/CaM by interacting with R126 on CaM.	cafestol palmitate	105-108	discs large MAGUK scaffold protein 4	Homo sapiens	54-60
29118000-4	2018	Our NMR structural analysis identified E17 within the PSD-95 N-terminus as important for binding to Ca2+/CaM by interacting with R126 on CaM.	cafestol palmitate	137-140	discs large MAGUK scaffold protein 4	Homo sapiens	54-60
29118000-6	2018	Accordingly, increased binding of Ca2+/CaM to PSD-95 induced by a chronic increase in Ca2+ influx is a critical molecular event in homeostatic downscaling of glutamatergic synaptic transmission.	cafestol palmitate	39-42	discs large MAGUK scaffold protein 4	Homo sapiens	46-52
29281827-0	2017	Synaptic Targeting and Function of SAPAPs Mediated by Phosphorylation-Dependent Binding to PSD-95 MAGUKs.	sapaps	35-41	discs large MAGUK scaffold protein 4	Homo sapiens	91-97
29281827-3	2017	Here, we show that the PSD-95/SAPAP interaction, SAPAP synaptic targeting, and SAPAP-mediated synaptogenesis require phosphorylation of the N-terminal repeat sequences of SAPAPs.	sapap	30-35	discs large MAGUK scaffold protein 4	Homo sapiens	23-29
29281827-3	2017	Here, we show that the PSD-95/SAPAP interaction, SAPAP synaptic targeting, and SAPAP-mediated synaptogenesis require phosphorylation of the N-terminal repeat sequences of SAPAPs.	sapaps	171-177	discs large MAGUK scaffold protein 4	Homo sapiens	23-29
29281827-4	2017	The atomic structure of the PSD-95 guanylate kinase (GK) in complex with a phosphor-SAPAP repeat peptide, together with biochemical studies, reveals the molecular mechanism underlying the phosphorylation-dependent PSD-95/SAPAP interaction, and it also provides an explanation of a PSD-95 mutation found in patients with intellectual disabilities.	sapap	84-89	discs large MAGUK scaffold protein 4	Homo sapiens	28-34
29281827-4	2017	The atomic structure of the PSD-95 guanylate kinase (GK) in complex with a phosphor-SAPAP repeat peptide, together with biochemical studies, reveals the molecular mechanism underlying the phosphorylation-dependent PSD-95/SAPAP interaction, and it also provides an explanation of a PSD-95 mutation found in patients with intellectual disabilities.	sapap	84-89	discs large MAGUK scaffold protein 4	Homo sapiens	214-220
29281827-4	2017	The atomic structure of the PSD-95 guanylate kinase (GK) in complex with a phosphor-SAPAP repeat peptide, together with biochemical studies, reveals the molecular mechanism underlying the phosphorylation-dependent PSD-95/SAPAP interaction, and it also provides an explanation of a PSD-95 mutation found in patients with intellectual disabilities.	sapap	84-89	discs large MAGUK scaffold protein 4	Homo sapiens	214-220
29281827-4	2017	The atomic structure of the PSD-95 guanylate kinase (GK) in complex with a phosphor-SAPAP repeat peptide, together with biochemical studies, reveals the molecular mechanism underlying the phosphorylation-dependent PSD-95/SAPAP interaction, and it also provides an explanation of a PSD-95 mutation found in patients with intellectual disabilities.	sapap	221-226	discs large MAGUK scaffold protein 4	Homo sapiens	28-34
29281827-4	2017	The atomic structure of the PSD-95 guanylate kinase (GK) in complex with a phosphor-SAPAP repeat peptide, together with biochemical studies, reveals the molecular mechanism underlying the phosphorylation-dependent PSD-95/SAPAP interaction, and it also provides an explanation of a PSD-95 mutation found in patients with intellectual disabilities.	sapap	221-226	discs large MAGUK scaffold protein 4	Homo sapiens	214-220
29281827-4	2017	The atomic structure of the PSD-95 guanylate kinase (GK) in complex with a phosphor-SAPAP repeat peptide, together with biochemical studies, reveals the molecular mechanism underlying the phosphorylation-dependent PSD-95/SAPAP interaction, and it also provides an explanation of a PSD-95 mutation found in patients with intellectual disabilities.	sapap	221-226	discs large MAGUK scaffold protein 4	Homo sapiens	214-220
29281827-5	2017	Guided by the structural data, we developed potent non-phosphorylated GK inhibitory peptides capable of blocking the PSD-95/SAPAP interaction and interfering with PSD-95/SAPAP-mediated synaptic maturation and strength.	sapap	124-129	discs large MAGUK scaffold protein 4	Homo sapiens	117-123
28965935-7	2017	Data showed that carbamazepine individually, venlafaxine individually and mixture treatment at environmental concentrations significantly altered the expression of key synaptic proteins (NMDAR1, PSD95, SV2A, HTR1B, HTR2C and OXTR).	Carbamazepine	17-30	discs large MAGUK scaffold protein 4	Homo sapiens	195-200
28965935-7	2017	Data showed that carbamazepine individually, venlafaxine individually and mixture treatment at environmental concentrations significantly altered the expression of key synaptic proteins (NMDAR1, PSD95, SV2A, HTR1B, HTR2C and OXTR).	Venlafaxine Hydrochloride	45-56	discs large MAGUK scaffold protein 4	Homo sapiens	195-200
28238085-5	2017	In addition, eliminating the O-GlcNAcylation of nNOS protects neurons from apoptosis during glutamate stimulation by decreasing the formation of nNOS-postsynaptic density protein 95 complexes.	Glutamic Acid	92-101	discs large MAGUK scaffold protein 4	Homo sapiens	150-181
28790172-0	2017	Postsynaptic density 95 (PSD-95) serine 561 phosphorylation regulates a conformational switch and bidirectional dendritic spine structural plasticity.	Serine	33-39	discs large MAGUK scaffold protein 4	Homo sapiens	0-23
28790172-0	2017	Postsynaptic density 95 (PSD-95) serine 561 phosphorylation regulates a conformational switch and bidirectional dendritic spine structural plasticity.	Serine	33-39	discs large MAGUK scaffold protein 4	Homo sapiens	25-31
28790172-4	2017	Here we show that phosphorylation of PSD-95 at Ser-561 in its guanylate kinase (GK) domain, which is mediated by the partitioning-defective 1 (Par1) kinases, regulates a conformational switch and is important for bidirectional plasticity.	Serine	47-50	discs large MAGUK scaffold protein 4	Homo sapiens	37-43
28790172-5	2017	Using a fluorescence resonance energy transfer (FRET) biosensor, we show that a phosphomimetic mutation of Ser-561 promotes an intramolecular interaction between GK and the nearby Src homology 3 (SH3) domain, leading to a closed conformation, whereas a non-phosphorylatable S561A mutation or inhibition of Par1 kinase activity decreases SH3-GK interaction, causing PSD-95 to adopt an open conformation.	Serine	107-110	discs large MAGUK scaffold protein 4	Homo sapiens	365-371
28158955-4	2017	Further investigation demonstrated that this effect of H2S was mediated by reversing the CUMS-induced decrease in dendritic spine density and required the activation of mammalian target of rapamycin (mTOR)C1 and neurotrophic TrkB receptors, which proceeded to increase synaptic protein expression, including postsynaptic density protein 95, synaptophysin, and alpha-amino-3-hydroxy-5-methyl-4-isoxazole-propionic acid receptor GluR1/2 subunit.	Hydrogen Sulfide	55-58	discs large MAGUK scaffold protein 4	Homo sapiens	308-339
28411102-4	2017	The goal of the study was to investigate the potential protective effects of ZL006, a small-molecule inhibitor of the PSD-95/nNOS interaction, in an in vitro SCI model induced by oxygen and glucose deprivation (OGD) in cultured spinal cord neurons.	4-((3,5-dichloro-2-hydroxybenzyl)amino)-2-hydroxybenzoic acid	77-82	discs large MAGUK scaffold protein 4	Homo sapiens	118-124
28346830-7	2017	A combination of DHA and ASA efficiently enhanced heterodimer formations of PPARalpha and RXRalpha and increased the expression of neurotrophic factors PSD-95, brain-derived neurotrophic factor (BDNF), and glial cell-derived neurotrophic factor (GDNF), while inhibiting NFkappaB and COX2.	Docosahexaenoic Acids	17-20	discs large MAGUK scaffold protein 4	Homo sapiens	152-158
28235555-3	2017	METHODS: Molecular imaging of gene expression was used to investigate whether chronic treatment with first and second generation antipsychotics (haloperidol, asenapine and olanzapine) may induce changes in the expression levels of PSD transcripts involved in schizophrenia pathophysiology, i.e. Homers, Shank1, PSD-95 and Arc.	Haloperidol	145-156	discs large MAGUK scaffold protein 4	Homo sapiens	311-317
28235555-3	2017	METHODS: Molecular imaging of gene expression was used to investigate whether chronic treatment with first and second generation antipsychotics (haloperidol, asenapine and olanzapine) may induce changes in the expression levels of PSD transcripts involved in schizophrenia pathophysiology, i.e. Homers, Shank1, PSD-95 and Arc.	asenapine	158-167	discs large MAGUK scaffold protein 4	Homo sapiens	311-317
28235555-3	2017	METHODS: Molecular imaging of gene expression was used to investigate whether chronic treatment with first and second generation antipsychotics (haloperidol, asenapine and olanzapine) may induce changes in the expression levels of PSD transcripts involved in schizophrenia pathophysiology, i.e. Homers, Shank1, PSD-95 and Arc.	Olanzapine	172-182	discs large MAGUK scaffold protein 4	Homo sapiens	311-317
28769761-8	2017	Inhibition of miR-142-5p rescued the Abeta42-mediated synaptic dysfunctions, as indicated by the expression of postsynaptic density protein 95 (PSD-95).	mir-142-5p	14-24	discs large MAGUK scaffold protein 4	Homo sapiens	111-142
28769761-8	2017	Inhibition of miR-142-5p rescued the Abeta42-mediated synaptic dysfunctions, as indicated by the expression of postsynaptic density protein 95 (PSD-95).	mir-142-5p	14-24	discs large MAGUK scaffold protein 4	Homo sapiens	144-150
28522733-8	2017	Treatment with either GSK2656157 or overexpression of a kinase-dead mutant of PERK (PERK-K618A) rescues BDNF and PSD95 levels in the pericontusional cortex by reducing phosphorylation of CREB and PSD95 proteins after TBI.	GSK2656157	22-32	discs large MAGUK scaffold protein 4	Homo sapiens	113-118
28522733-8	2017	Treatment with either GSK2656157 or overexpression of a kinase-dead mutant of PERK (PERK-K618A) rescues BDNF and PSD95 levels in the pericontusional cortex by reducing phosphorylation of CREB and PSD95 proteins after TBI.	GSK2656157	22-32	discs large MAGUK scaffold protein 4	Homo sapiens	196-201
28522733-15	2017	Therefore, our study suggests that CREB and PSD95 are novel substrates of PERK, so inhibition of PERK phosphorylation using GSK2656157 would be beneficial against memory impairment after TBI.	GSK2656157	124-134	discs large MAGUK scaffold protein 4	Homo sapiens	44-49
28346830-7	2017	A combination of DHA and ASA efficiently enhanced heterodimer formations of PPARalpha and RXRalpha and increased the expression of neurotrophic factors PSD-95, brain-derived neurotrophic factor (BDNF), and glial cell-derived neurotrophic factor (GDNF), while inhibiting NFkappaB and COX2.	Aspirin	25-28	discs large MAGUK scaffold protein 4	Homo sapiens	152-158
28346830-8	2017	These findings suggest that a combination of DHA and ASA could significantly improve the expression of PSD-95, BDNF, and GDNF by promoting heterodimerization of PPARalpha and RXRalpha, thus supplying a new therapeutic method for PD.	Docosahexaenoic Acids	45-48	discs large MAGUK scaffold protein 4	Homo sapiens	103-109
28346830-8	2017	These findings suggest that a combination of DHA and ASA could significantly improve the expression of PSD-95, BDNF, and GDNF by promoting heterodimerization of PPARalpha and RXRalpha, thus supplying a new therapeutic method for PD.	Aspirin	53-56	discs large MAGUK scaffold protein 4	Homo sapiens	103-109
28377693-8	2017	Rapamycin reduced mechanical allodynia and downregulated the expression of postsynaptic density protein 95 (PSD95), decreased neural excitability in the IC, thereby inhibiting neuropathic pain-induced synaptic plasticity.	Sirolimus	0-9	discs large MAGUK scaffold protein 4	Homo sapiens	75-106
28212538-6	2017	The newborn neurons in the sevoflurane preconditioning group showed miniature excitatory postsynaptic currents (mEPSCs), increased synaptophysin and PSD95 staining density, indicating normal neuronal function.	Sevoflurane	27-38	discs large MAGUK scaffold protein 4	Homo sapiens	149-154
28377693-8	2017	Rapamycin reduced mechanical allodynia and downregulated the expression of postsynaptic density protein 95 (PSD95), decreased neural excitability in the IC, thereby inhibiting neuropathic pain-induced synaptic plasticity.	Sirolimus	0-9	discs large MAGUK scaffold protein 4	Homo sapiens	108-113
27640997-0	2016	ATP from synaptic terminals and astrocytes regulates NMDA receptors and synaptic plasticity through PSD-95 multi-protein complex.	Adenosine Triphosphate	0-3	discs large MAGUK scaffold protein 4	Homo sapiens	100-106
28957809-8	2017	Moreover, geniposide"s protection was due to the enhancement of GluN2A-dependent survival signals, including pAKT, pERK and PSD-95.	geniposide	10-20	discs large MAGUK scaffold protein 4	Homo sapiens	124-130
26968265-5	2016	We further show that AS-NMD is a conserved mechanism among mammals to induce developmental expression of the synaptic scaffold protein PSD-95.	as-nmd	21-27	discs large MAGUK scaffold protein 4	Homo sapiens	135-141
27472651-4	2016	Here, we examined the importance of a conserved Lys/Arg residue in the ligand-binding site of the second PDZ domain of PSD-95, by employing a semisynthetic approach.	Lysine	48-51	discs large MAGUK scaffold protein 4	Homo sapiens	119-125
27472651-4	2016	Here, we examined the importance of a conserved Lys/Arg residue in the ligand-binding site of the second PDZ domain of PSD-95, by employing a semisynthetic approach.	Arginine	52-55	discs large MAGUK scaffold protein 4	Homo sapiens	119-125
27640997-7	2016	Genetic deletion of the PSD-95 or P2X4 receptors obliterated ATP-mediated down-regulation of NMDA receptors.	Adenosine Triphosphate	61-64	discs large MAGUK scaffold protein 4	Homo sapiens	24-30
27300007-2	2016	Our previous study demonstrated that APPL1 (adaptor protein containing pleckstrin homology domain, phosphotyrosine-binding domain, and leucine zipper motif) mediates the synaptic activity-dependent activation of PI3K-Akt signaling via coupling this pathway with NMDAR-PSD95 (postsynaptic density protein 95) complexes.	Phosphotyrosine	99-114	discs large MAGUK scaffold protein 4	Homo sapiens	268-273
27300007-2	2016	Our previous study demonstrated that APPL1 (adaptor protein containing pleckstrin homology domain, phosphotyrosine-binding domain, and leucine zipper motif) mediates the synaptic activity-dependent activation of PI3K-Akt signaling via coupling this pathway with NMDAR-PSD95 (postsynaptic density protein 95) complexes.	Phosphotyrosine	99-114	discs large MAGUK scaffold protein 4	Homo sapiens	275-306
27300007-6	2016	Furthermore, we identified serine 707 of APPL1, a predicted phosphorylation site within the PDZ-binding motif at the C-terminus, as critical for the binding of APPL1 to PSD95, as well as for activation of the Akt signaling pathway during synaptic activity.	Serine	27-33	discs large MAGUK scaffold protein 4	Homo sapiens	169-174
27211904-7	2016	These findings suggest that the activation of BDNF-dependent mTOR signaling, which produces a rapid increase in the postsynaptic protein PSD-95 and GluA1 and further triggers the long-term enhancement of synaptic neurotransmission, may be the mechanism underlying the rapid antidepressant and anxiolytic effects induced by YY-21.	yy-21	323-328	discs large MAGUK scaffold protein 4	Homo sapiens	137-143
26013316-8	2016	CONCLUSION: These data suggest that differences in cortical NMDAR expression and post-synaptic density protein 95 are present in psychiatric disorders and suicide completion and may contribute to different responses to ketamine.	Ketamine	219-227	discs large MAGUK scaffold protein 4	Homo sapiens	81-113
26991362-5	2016	We also noted the striking ability of PSD95 to enhance glutamate-stimulated potentiation effects of NETO2 on GluK1 without the need for Con A and with a robust signal that could be utilized for high-throughput FLIPR assays.	Glutamic Acid	55-64	discs large MAGUK scaffold protein 4	Homo sapiens	38-43
26701913-5	2015	We used activity profiling to identify novel serine hydrolase targets of the APT1/2 inhibitor Palmostatin B, and discovered that a family of uncharacterized ABHD17 proteins can accelerate palmitate turnover on PSD95 and N-Ras.	palmostatin B	94-107	discs large MAGUK scaffold protein 4	Homo sapiens	210-215
26969072-0	2016	Lambda-cyhalothrin disrupts the up-regulation effect of 17beta-estradiol on post-synaptic density 95 protein expression via estrogen receptor alpha-dependent Akt pathway.	cyhalothrin	7-18	discs large MAGUK scaffold protein 4	Homo sapiens	76-100
26969072-0	2016	Lambda-cyhalothrin disrupts the up-regulation effect of 17beta-estradiol on post-synaptic density 95 protein expression via estrogen receptor alpha-dependent Akt pathway.	Estradiol	56-72	discs large MAGUK scaffold protein 4	Homo sapiens	76-100
26941605-0	2016	D-Serine and Serine Racemase Are Associated with PSD-95 and Glutamatergic Synapse Stability.	D-serine	0-8	discs large MAGUK scaffold protein 4	Homo sapiens	49-55
26941605-5	2016	Using morphological and molecular studies in cortical neuronal cultures, we demonstrate that D-serine/SR are associated with PSD-95 and NMDARs in postsynaptic neurons and with glutamatergic synapse stability during synaptic development.	D-serine	93-101	discs large MAGUK scaffold protein 4	Homo sapiens	125-131
26941605-6	2016	Endogenous D-serine and SR colocalize with PSD-95, but not presynaptic vesicular glutamate transporter 1 (VGLUT1), in glutamatergic synapses of cultured cortical neurons.	D-serine	11-19	discs large MAGUK scaffold protein 4	Homo sapiens	43-49
26941605-8	2016	More interestingly, endogenous D-serine and SR colocalize with PSD-95 in the postsynaptic terminals of glutamatergic synapses during early and late synaptic development, implicating involvement of D-serine/SR in glutamatergic synaptic development.	D-serine	31-39	discs large MAGUK scaffold protein 4	Homo sapiens	63-69
26941605-9	2016	Exogenous application of D-serine enhances the interactions of SR with PSD-95 and NR1, and increases the number of VGLUT1- and PSD-95-positive glutamatergic synapses, suggesting that exogenous D-serine enhances postsynaptic SR/PSD-95 signaling and stabilizes glutamatergic synapses during cortical synaptic development.	D-serine	25-33	discs large MAGUK scaffold protein 4	Homo sapiens	71-77
26941605-9	2016	Exogenous application of D-serine enhances the interactions of SR with PSD-95 and NR1, and increases the number of VGLUT1- and PSD-95-positive glutamatergic synapses, suggesting that exogenous D-serine enhances postsynaptic SR/PSD-95 signaling and stabilizes glutamatergic synapses during cortical synaptic development.	D-serine	25-33	discs large MAGUK scaffold protein 4	Homo sapiens	127-133
26941605-9	2016	Exogenous application of D-serine enhances the interactions of SR with PSD-95 and NR1, and increases the number of VGLUT1- and PSD-95-positive glutamatergic synapses, suggesting that exogenous D-serine enhances postsynaptic SR/PSD-95 signaling and stabilizes glutamatergic synapses during cortical synaptic development.	D-serine	25-33	discs large MAGUK scaffold protein 4	Homo sapiens	127-133
26941605-9	2016	Exogenous application of D-serine enhances the interactions of SR with PSD-95 and NR1, and increases the number of VGLUT1- and PSD-95-positive glutamatergic synapses, suggesting that exogenous D-serine enhances postsynaptic SR/PSD-95 signaling and stabilizes glutamatergic synapses during cortical synaptic development.	D-serine	193-201	discs large MAGUK scaffold protein 4	Homo sapiens	127-133
26941605-9	2016	Exogenous application of D-serine enhances the interactions of SR with PSD-95 and NR1, and increases the number of VGLUT1- and PSD-95-positive glutamatergic synapses, suggesting that exogenous D-serine enhances postsynaptic SR/PSD-95 signaling and stabilizes glutamatergic synapses during cortical synaptic development.	D-serine	193-201	discs large MAGUK scaffold protein 4	Homo sapiens	127-133
26941605-12	2016	Taken together, our findings demonstrate that D-serine/SR are associated with PSD-95 and NMDARs in postsynaptic neurons and with glutamatergic synapse stability during synaptic development, implicating D-serine/SR as regulators of cortical synaptic and circuit development.	D-serine	46-54	discs large MAGUK scaffold protein 4	Homo sapiens	78-84
27669335-8	2016	DFO treatment decreased mRNA levels for genes indexing dendritic and synaptic development (i.e. BdnfVI,Camk2a,Vamp1,Psd95,Cfl1, Pfn1,Pfn2, and Gda) and mitochondrial function (i.e. Ucp2,Pink1, and Cox6a1).	Deferoxamine	0-3	discs large MAGUK scaffold protein 4	Homo sapiens	116-121
26648848-5	2015	PSD-95 is now known to negatively regulate not only N-methyl-D-aspartate glutamate signaling, but also dopamine D1 signals at sites of postsynaptic transmission.	n-methyl-d-aspartate glutamate	52-82	discs large MAGUK scaffold protein 4	Homo sapiens	0-6
26648848-5	2015	PSD-95 is now known to negatively regulate not only N-methyl-D-aspartate glutamate signaling, but also dopamine D1 signals at sites of postsynaptic transmission.	Dopamine	103-111	discs large MAGUK scaffold protein 4	Homo sapiens	0-6
26648848-9	2015	In addition to the possible involvement of PSD-95-mediated synaptic function in compartment-specific dopamine signals, we suggest that the striosomes might be more susceptible to D1R-mediated neurotoxicity than the matrix compartment.	Dopamine	101-109	discs large MAGUK scaffold protein 4	Homo sapiens	43-49
26071957-0	2015	Small-molecule inhibitors at the PSD-95/nNOS interface protect against glutamate-induced neuronal atrophy in primary cortical neurons.	Glutamic Acid	71-80	discs large MAGUK scaffold protein 4	Homo sapiens	33-39
26100636-7	2015	Although neuroprotection was partially dependent upon CN2097 binding to the PDZ domain of PSD-95, our results show that the polyarginine-rich transport moiety C-R(7), linked to the PDZ-PSD-95-binding cyclic peptide, was sufficient to mediate short and long term protection via a mitochondrial targeting mechanism.	polyarginine	124-136	discs large MAGUK scaffold protein 4	Homo sapiens	185-191
26071957-9	2015	These data support the hypothesis that targeting the NMDA-R/PSD-95/nNOS interaction downstream of NMDA-R promotes neurotrophic effects by preventing neurite shrinkage in response to excess glutamatergic stimulation.	N-Methylaspartate	53-57	discs large MAGUK scaffold protein 4	Homo sapiens	60-66
26071957-9	2015	These data support the hypothesis that targeting the NMDA-R/PSD-95/nNOS interaction downstream of NMDA-R promotes neurotrophic effects by preventing neurite shrinkage in response to excess glutamatergic stimulation.	N-Methylaspartate	98-102	discs large MAGUK scaffold protein 4	Homo sapiens	60-66
25669908-2	2015	Tat-NR2B9c is designed to prevent nitric oxide (NO) production by preventing postsynaptic density protein 95 (PSD-95) binding to N-methyl-D-aspartate (NMDA) receptors and neuronal nitric oxide synthase; however, PSD-95 is a scaffolding protein that also couples NMDA receptors to other downstream effects.	Nitric Oxide	34-46	discs large MAGUK scaffold protein 4	Homo sapiens	77-108
25307211-9	2015	Li, VPA, and CBZ prevented B27 deprivation-induced decreases in BDNF, PSD-95, NLG1, beta-neurexin, and SYP levels, whereas LTG did not.	Valproic Acid	4-7	discs large MAGUK scaffold protein 4	Homo sapiens	70-76
25307211-9	2015	Li, VPA, and CBZ prevented B27 deprivation-induced decreases in BDNF, PSD-95, NLG1, beta-neurexin, and SYP levels, whereas LTG did not.	Carbamazepine	13-16	discs large MAGUK scaffold protein 4	Homo sapiens	70-76
25669908-2	2015	Tat-NR2B9c is designed to prevent nitric oxide (NO) production by preventing postsynaptic density protein 95 (PSD-95) binding to N-methyl-D-aspartate (NMDA) receptors and neuronal nitric oxide synthase; however, PSD-95 is a scaffolding protein that also couples NMDA receptors to other downstream effects.	Nitric Oxide	34-46	discs large MAGUK scaffold protein 4	Homo sapiens	110-116
25071552-5	2014	Our results indicate that copper also enhances neurotransmission through the accumulation of PSD95 protein, which increase the levels of alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA) receptors located at the plasma membrane of the post-synaptic density.	Copper	26-32	discs large MAGUK scaffold protein 4	Homo sapiens	93-98
25662731-10	2015	In addition, chronic administration of 2"-FL increased the expression of different molecules involved in the storage of newly acquired memories, such as the postsynaptic density protein 95, phosphorylated calcium/calmodulin-dependent kinase II and brain-derived neurotrophic factor in cortical and subcortical structures.	2'-fucosyllactose	39-44	discs large MAGUK scaffold protein 4	Homo sapiens	157-188
24981431-5	2015	We found that either NMDA or chemical LTP induction leads to rapid phosphorylation of PSD-95 by Src in cultured cortical neurons.	N-Methylaspartate	21-25	discs large MAGUK scaffold protein 4	Homo sapiens	86-92
24981431-7	2015	Comparing to wild-type PSD-95, overexpression of nonphosphorylatable mutant PSD-95Y523F attenuated the NMDA-stimulated NR2A tyrosine phosphorylation that enhances electrophysiological responses of NMDA receptor channels, while did not affect the membrane localization of NR2A subunits.	N-Methylaspartate	103-107	discs large MAGUK scaffold protein 4	Homo sapiens	23-29
24981431-7	2015	Comparing to wild-type PSD-95, overexpression of nonphosphorylatable mutant PSD-95Y523F attenuated the NMDA-stimulated NR2A tyrosine phosphorylation that enhances electrophysiological responses of NMDA receptor channels, while did not affect the membrane localization of NR2A subunits.	Tyrosine	124-132	discs large MAGUK scaffold protein 4	Homo sapiens	23-29
24981431-8	2015	PSD-95Y523D, a phosphomimetic mutant of PSD-95, induced NR2A tyrosine phosphorylation even if there was no NMDA treatment.	Tyrosine	61-69	discs large MAGUK scaffold protein 4	Homo sapiens	0-6
24981431-8	2015	PSD-95Y523D, a phosphomimetic mutant of PSD-95, induced NR2A tyrosine phosphorylation even if there was no NMDA treatment.	N-Methylaspartate	107-111	discs large MAGUK scaffold protein 4	Homo sapiens	0-6
24981431-10	2015	These results indicate that PSD-95 phosphorylation by Src facilitates the integration of Pyk2 to PSD-95 signal complex, the activation of Pyk2/Src, as well as the subsequent tyrosine phosphorylation of NR2A, which ultimately results in the upregulation of NMDA receptor function and synaptic transmission.	Tyrosine	174-182	discs large MAGUK scaffold protein 4	Homo sapiens	28-34
24981431-10	2015	These results indicate that PSD-95 phosphorylation by Src facilitates the integration of Pyk2 to PSD-95 signal complex, the activation of Pyk2/Src, as well as the subsequent tyrosine phosphorylation of NR2A, which ultimately results in the upregulation of NMDA receptor function and synaptic transmission.	Tyrosine	174-182	discs large MAGUK scaffold protein 4	Homo sapiens	97-103
24047601-7	2015	U0126 abolished ODP consolidation and reduced both phosphorylation of eukaryotic initiation factor 4E (eIF4E) and levels of the synaptic marker PSD-95.	U 0126	0-5	discs large MAGUK scaffold protein 4	Homo sapiens	144-150
25540577-8	2014	The PSD-95 protein was observed at fiber cell membranes overlapping with N-methyl-D-aspartate (NMDA) and alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA) glutamate and GABA receptor proteins, tyrosine phosphatase STEP, CaMKIIalpha, the Ca(V)1.3 calcium channel, and clathrin, which were previously identified at lens fiber cell membranes.	N-Methylaspartate	73-93	discs large MAGUK scaffold protein 4	Homo sapiens	4-10
25540577-8	2014	The PSD-95 protein was observed at fiber cell membranes overlapping with N-methyl-D-aspartate (NMDA) and alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA) glutamate and GABA receptor proteins, tyrosine phosphatase STEP, CaMKIIalpha, the Ca(V)1.3 calcium channel, and clathrin, which were previously identified at lens fiber cell membranes.	N-Methylaspartate	95-99	discs large MAGUK scaffold protein 4	Homo sapiens	4-10
25540577-8	2014	The PSD-95 protein was observed at fiber cell membranes overlapping with N-methyl-D-aspartate (NMDA) and alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA) glutamate and GABA receptor proteins, tyrosine phosphatase STEP, CaMKIIalpha, the Ca(V)1.3 calcium channel, and clathrin, which were previously identified at lens fiber cell membranes.	3-(1,2-oxazol-3-yl)propanoic acid	138-161	discs large MAGUK scaffold protein 4	Homo sapiens	4-10
25452082-0	2014	Small-molecule inhibitors at the PSD-95/nNOS interface attenuate MPP+-induced neuronal injury through Sirt3 mediated inhibition of mitochondrial dysfunction.	mangion-purified polysaccharide (Candida albicans)	65-69	discs large MAGUK scaffold protein 4	Homo sapiens	33-39
25221472-3	2014	Recruitment by NMDARs of calcium-dependent enzyme nNOS via PSD95 is seen as a key contributor to neuronal dysfunction.	Calcium	25-32	discs large MAGUK scaffold protein 4	Homo sapiens	59-64
24981431-0	2015	The upregulation of NR2A-containing N-methyl-D-aspartate receptor function by tyrosine phosphorylation of postsynaptic density 95 via facilitating Src/proline-rich tyrosine kinase 2 activation.	Tyrosine	78-86	discs large MAGUK scaffold protein 4	Homo sapiens	106-129
25040426-6	2014	Exposure of cultured neurons to conditioned media from ammonia-treated astrocytes showed a decrease in synaptophysin, PSD95, and synaptotagmin levels.	Ammonia	55-62	discs large MAGUK scaffold protein 4	Homo sapiens	118-123
25164819-0	2014	Serine racemase regulated by binding to stargazin and PSD-95: potential N-methyl-D-aspartate-alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (NMDA-AMPA) glutamate neurotransmission cross-talk.	nmda-ampa	151-160	discs large MAGUK scaffold protein 4	Homo sapiens	54-60
25164819-0	2014	Serine racemase regulated by binding to stargazin and PSD-95: potential N-methyl-D-aspartate-alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (NMDA-AMPA) glutamate neurotransmission cross-talk.	Glutamic Acid	162-171	discs large MAGUK scaffold protein 4	Homo sapiens	54-60
25071552-8	2014	Our results suggest that copper increases GluA1 subunit levels of the AMPA receptor through the anchorage of AMPA receptors to the plasma membrane as a result of PSD-95 accumulation.	Copper	25-31	discs large MAGUK scaffold protein 4	Homo sapiens	162-168
24659082-8	2014	Administration of low dose ZD7288 (0.25 mug) at 30 min and 3 h after the onset of ischemia attenuated the impairment of LTP induction and alleviated the NR2B and PSD-95 mRNA and protein down-regulation commonly induced by cerebral ischemia/reperfusion injury.	ICI D2788	27-33	discs large MAGUK scaffold protein 4	Homo sapiens	162-168
24586041-5	2014	Cultured hippocampal neurons expressing a fusion protein of PSD-95 coupled to 3MT (PDS-95-3MT) were incubated with CdCl2 to result in the formation of Cd-bound PSD-95-3MT.	Palladium	83-86	discs large MAGUK scaffold protein 4	Homo sapiens	60-66
24586041-5	2014	Cultured hippocampal neurons expressing a fusion protein of PSD-95 coupled to 3MT (PDS-95-3MT) were incubated with CdCl2 to result in the formation of Cd-bound PSD-95-3MT.	Palladium	83-86	discs large MAGUK scaffold protein 4	Homo sapiens	160-166
24586041-5	2014	Cultured hippocampal neurons expressing a fusion protein of PSD-95 coupled to 3MT (PDS-95-3MT) were incubated with CdCl2 to result in the formation of Cd-bound PSD-95-3MT.	Cadmium Chloride	115-120	discs large MAGUK scaffold protein 4	Homo sapiens	60-66
24586041-5	2014	Cultured hippocampal neurons expressing a fusion protein of PSD-95 coupled to 3MT (PDS-95-3MT) were incubated with CdCl2 to result in the formation of Cd-bound PSD-95-3MT.	Cadmium Chloride	115-120	discs large MAGUK scaffold protein 4	Homo sapiens	160-166
24586041-5	2014	Cultured hippocampal neurons expressing a fusion protein of PSD-95 coupled to 3MT (PDS-95-3MT) were incubated with CdCl2 to result in the formation of Cd-bound PSD-95-3MT.	Cadmium	115-117	discs large MAGUK scaffold protein 4	Homo sapiens	60-66
24586041-5	2014	Cultured hippocampal neurons expressing a fusion protein of PSD-95 coupled to 3MT (PDS-95-3MT) were incubated with CdCl2 to result in the formation of Cd-bound PSD-95-3MT.	Cadmium	115-117	discs large MAGUK scaffold protein 4	Homo sapiens	160-166
24586041-6	2014	Two types of electron-dense deposits composed of Cd-bound PSD-95-3MT were observed in these cells by TEM, as reported previously.	Cadmium	49-51	discs large MAGUK scaffold protein 4	Homo sapiens	58-64
24845085-2	2014	It is achieved through an intra-domain electrostatic network involving some charged residues in the beta2-beta3 loop (were a succinimide modification occurs), the alpha3 helix (an extra-structural element that links the PDZ3 domain with the following SH3 domain in PSD-95, and contains the phosphorylation target Tyr397), and the ligand peptide.	succinimide	125-136	discs large MAGUK scaffold protein 4	Homo sapiens	265-271
24744726-12	2014	While both chelerythrine and ZIP suppressed the postsynaptic localization of PSD-95, RNA interference for PKMpi did not have a significant effect.	chelerythrine	11-24	discs large MAGUK scaffold protein 4	Homo sapiens	77-83
23959764-0	2013	Ovarian steroids increase PSD-95 expression and dendritic spines in the dorsal raphe of ovariectomized macaques.	Steroids	8-16	discs large MAGUK scaffold protein 4	Homo sapiens	26-32
24477114-4	2014	We observe substantial and differential effects upon amide-to-ester mutation in PDZ2 of postsynaptic density protein 95 and other PDZ domains, suggesting that hydrogen bonding at the carboxylate-binding site contributes to both affinity and selectivity.	Amides	53-58	discs large MAGUK scaffold protein 4	Homo sapiens	88-119
24477114-4	2014	We observe substantial and differential effects upon amide-to-ester mutation in PDZ2 of postsynaptic density protein 95 and other PDZ domains, suggesting that hydrogen bonding at the carboxylate-binding site contributes to both affinity and selectivity.	Esters	62-67	discs large MAGUK scaffold protein 4	Homo sapiens	88-119
24477114-4	2014	We observe substantial and differential effects upon amide-to-ester mutation in PDZ2 of postsynaptic density protein 95 and other PDZ domains, suggesting that hydrogen bonding at the carboxylate-binding site contributes to both affinity and selectivity.	Hydrogen	159-167	discs large MAGUK scaffold protein 4	Homo sapiens	88-119
24477114-4	2014	We observe substantial and differential effects upon amide-to-ester mutation in PDZ2 of postsynaptic density protein 95 and other PDZ domains, suggesting that hydrogen bonding at the carboxylate-binding site contributes to both affinity and selectivity.	carboxylate	183-194	discs large MAGUK scaffold protein 4	Homo sapiens	88-119
23800465-6	2013	We focused on Homer1a/Homer1b/PSD-95 signaling network, which may be implicated in glutamate-dependent synaptic plasticity, as well as in psychosis pathophysiology and treatment.	Glutamic Acid	83-92	discs large MAGUK scaffold protein 4	Homo sapiens	30-36
24012668-5	2013	In addition, we found that Valsartan increases the puncta number of PSD-95 and trends toward an increase in the puncta number of synaptophysin.	Valsartan	27-36	discs large MAGUK scaffold protein 4	Homo sapiens	68-74
23800465-7	2013	Ketamine (25 and 50mg/kg) and MK-801 (0.8mg/kg) significantly induced the transcripts of immediate-early genes (Arc, c-fos, and Homer1a) in cortical regions compared to vehicle, whereas they reduced Homer1b and PSD-95 expression in cortical and striatal regions.	Ketamine	0-8	discs large MAGUK scaffold protein 4	Homo sapiens	211-217
23800465-7	2013	Ketamine (25 and 50mg/kg) and MK-801 (0.8mg/kg) significantly induced the transcripts of immediate-early genes (Arc, c-fos, and Homer1a) in cortical regions compared to vehicle, whereas they reduced Homer1b and PSD-95 expression in cortical and striatal regions.	Dizocilpine Maleate	30-36	discs large MAGUK scaffold protein 4	Homo sapiens	211-217
23800465-10	2013	When compared to ketamine and MK-801, memantine significantly increased the expression of c-fos, Homer1b and PSD-95.	Memantine	38-47	discs large MAGUK scaffold protein 4	Homo sapiens	109-115
23818519-3	2013	These changes induce rapid cytoskeletal rearrangements (increased PSD-95 co-clustering) within the post-synaptic density; these events are accompanied by increased surface NMDA receptor expression, reflecting corticosterone-induced inhibition of NMDA receptor endocytosis.	Corticosterone	209-223	discs large MAGUK scaffold protein 4	Homo sapiens	66-72
23436724-2	2013	Indeed, this PSD-95/DlgA/ZO-1 (PDZ) domain-containing protein has been shown to interact with a wide variety of neurotransmitter receptors, transporters, and enzymes, including glutamate and nicotinic acetylcholine receptors, dopamine and glutamate transporters, and the enzyme serine racemase.	Glutamic Acid	177-186	discs large MAGUK scaffold protein 4	Homo sapiens	13-19
23701246-6	2013	Mas degradation was robustly inhibited by the proteasome inhibitor MG132 in time- and dose-dependent manners, and the expression of PSD95 impaired Mas ubiquitination, indicating that the PSD95-Mas association inhibits Mas receptor degradation via the ubiquitin-proteasome proteolytic pathway.	benzyloxycarbonylleucyl-leucyl-leucine aldehyde	67-72	discs large MAGUK scaffold protein 4	Homo sapiens	187-192
23864670-4	2013	In the dorsomedial, but not ventral, striatum, cocaine decreases PSD95 expression and phosphorylation of cortactin, a cytoskeletal regulator that interacts with, and is phophorylated by, the Abl2 (Arg) kinase.	Cocaine	47-54	discs large MAGUK scaffold protein 4	Homo sapiens	65-70
23178182-0	2013	UCCB01-125, a dimeric inhibitor of PSD-95, reduces inflammatory pain without disrupting cognitive or motor performance: comparison with the NMDA receptor antagonist MK-801.	UCCB01-125	0-10	discs large MAGUK scaffold protein 4	Homo sapiens	35-41
23770246-0	2013	Neurexin-1beta binding to neuroligin-1 triggers the preferential recruitment of PSD-95 versus gephyrin through tyrosine phosphorylation of neuroligin-1.	Tyrosine	111-119	discs large MAGUK scaffold protein 4	Homo sapiens	80-86
23606502-4	2013	Previously we found that glutamate stimulation induced other postsynaptic proteins, such as postsynaptic density-95 (PSD95), a biphasic change with an initially diffuse distribution after 30 min to 1 hr, followed by reassembly to more than the original level after 4-8 hr, suggesting that glutamate stimulation induces a global biphasic alteration in synaptic structures.	Glutamic Acid	25-34	discs large MAGUK scaffold protein 4	Homo sapiens	92-115
23606502-4	2013	Previously we found that glutamate stimulation induced other postsynaptic proteins, such as postsynaptic density-95 (PSD95), a biphasic change with an initially diffuse distribution after 30 min to 1 hr, followed by reassembly to more than the original level after 4-8 hr, suggesting that glutamate stimulation induces a global biphasic alteration in synaptic structures.	Glutamic Acid	25-34	discs large MAGUK scaffold protein 4	Homo sapiens	117-122
23606502-4	2013	Previously we found that glutamate stimulation induced other postsynaptic proteins, such as postsynaptic density-95 (PSD95), a biphasic change with an initially diffuse distribution after 30 min to 1 hr, followed by reassembly to more than the original level after 4-8 hr, suggesting that glutamate stimulation induces a global biphasic alteration in synaptic structures.	Glutamic Acid	289-298	discs large MAGUK scaffold protein 4	Homo sapiens	92-115
23606502-4	2013	Previously we found that glutamate stimulation induced other postsynaptic proteins, such as postsynaptic density-95 (PSD95), a biphasic change with an initially diffuse distribution after 30 min to 1 hr, followed by reassembly to more than the original level after 4-8 hr, suggesting that glutamate stimulation induces a global biphasic alteration in synaptic structures.	Glutamic Acid	289-298	discs large MAGUK scaffold protein 4	Homo sapiens	117-122
23355722-5	2013	Immunoprecipitation analyses revealed that, in response to inductive signals such as dibutyryl cyclic AMP and epidermal growth factor, NADRIN formed a complex with ezrin-radixin-moesin (ERM) protein by interacting with ERM-binding phosphoprotein 50 via its carboxy-terminal PSD95/DlgA/ZO-1-binding motif.	Bucladesine	85-105	discs large MAGUK scaffold protein 4	Homo sapiens	274-279
23178182-1	2013	Excessive N-Methyl-d-aspartate receptor (NMDAR)-dependent production of nitric oxide (NO) is involved in the development and maintenance of chronic pain states, and is mediated by postsynaptic density protein-95 (PSD-95).	Nitric Oxide	72-84	discs large MAGUK scaffold protein 4	Homo sapiens	180-211
23178182-1	2013	Excessive N-Methyl-d-aspartate receptor (NMDAR)-dependent production of nitric oxide (NO) is involved in the development and maintenance of chronic pain states, and is mediated by postsynaptic density protein-95 (PSD-95).	Nitric Oxide	72-84	discs large MAGUK scaffold protein 4	Homo sapiens	213-219
23201339-5	2013	Conversely, high intensity magnetic stimulation (HIMS, 1.55Tesla, 1Hz) appeared to be detrimental, reducing dendritic and axonal arborization and causing apparent structural damage, including thinning of PSD, less synapses and disordered synaptic structure, as well as upregulation of GAP43 and PSD95, possibly for their ability to mitigate dysfunction.	hims	49-53	discs large MAGUK scaffold protein 4	Homo sapiens	295-300
22940546-3	2013	Postsynaptic synapse-associated protein 90/postsynaptic density 95-associated proteins (SAPAPs) constitute a part of the N-methyl-d-aspartate receptor-associated postsynaptic density proteins, and are involved in synapse formation.	sapaps	88-94	discs large MAGUK scaffold protein 4	Homo sapiens	13-42
23775690-1	2013	The discovery that PSD-95/Discs large/ZO-1 (PDZ) domains can function as lipid-binding modules, in particular interacting with phosphoinositides (PIs), was made more than 10 years ago (Mol Cell 9(6): 1215-1225, 2002).	Phosphatidylinositols	127-144	discs large MAGUK scaffold protein 4	Homo sapiens	19-25
23775690-1	2013	The discovery that PSD-95/Discs large/ZO-1 (PDZ) domains can function as lipid-binding modules, in particular interacting with phosphoinositides (PIs), was made more than 10 years ago (Mol Cell 9(6): 1215-1225, 2002).	Phosphatidylinositols	146-149	discs large MAGUK scaffold protein 4	Homo sapiens	19-25
23000395-0	2012	ATPA induced GluR5-containing kainite receptor S-nitrosylation via activation of GluR5-Gq-PLC-IP(3)R pathway and signalling module GluR5 PSD-95 nNOS.	ATPA	0-4	discs large MAGUK scaffold protein 4	Homo sapiens	137-143
23179966-4	2013	Moving from receptors to postsynaptic density (PSD) scenario, the scaffolding protein PSD-95 is known to interact with N-methyl-D-aspartate (NMDA), D(2) and 5-HT(2) receptors, regulating their activation state.	N-Methylaspartate	119-139	discs large MAGUK scaffold protein 4	Homo sapiens	86-92
23179966-4	2013	Moving from receptors to postsynaptic density (PSD) scenario, the scaffolding protein PSD-95 is known to interact with N-methyl-D-aspartate (NMDA), D(2) and 5-HT(2) receptors, regulating their activation state.	N-Methylaspartate	141-145	discs large MAGUK scaffold protein 4	Homo sapiens	86-92
22807451-6	2012	Phosphorylation at a conserved serine residue in the KXGS motif in PSD-95 regulates spine morphogenesis, and a phosphomimetic mutant of this site can rescue the defects of kinase-dead PAR-1.	Serine	31-37	discs large MAGUK scaffold protein 4	Homo sapiens	67-73
23041629-0	2012	PSD-95 expression controls L-DOPA dyskinesia through dopamine D1 receptor trafficking.	Levodopa	27-33	discs large MAGUK scaffold protein 4	Homo sapiens	0-6
22703994-4	2012	Chronic ethanol exposure has been shown to increase the synaptic clustering of NMDA receptors and PSD-95.	Ethanol	8-15	discs large MAGUK scaffold protein 4	Homo sapiens	98-104
22763587-4	2012	Stimulation of dopamine and glutamate receptors modulates the gene expression and the function of specific PSD proteins, the "scaffolding" proteins (Homer, Shank, and PSD95), belonging to a complex Ca(2+)-regulated network that integrates and converges dopamine and glutamate signaling to appropriate nuclear targets.	Dopamine	15-23	discs large MAGUK scaffold protein 4	Homo sapiens	167-172
22763587-4	2012	Stimulation of dopamine and glutamate receptors modulates the gene expression and the function of specific PSD proteins, the "scaffolding" proteins (Homer, Shank, and PSD95), belonging to a complex Ca(2+)-regulated network that integrates and converges dopamine and glutamate signaling to appropriate nuclear targets.	Dopamine	253-261	discs large MAGUK scaffold protein 4	Homo sapiens	167-172
22763587-4	2012	Stimulation of dopamine and glutamate receptors modulates the gene expression and the function of specific PSD proteins, the "scaffolding" proteins (Homer, Shank, and PSD95), belonging to a complex Ca(2+)-regulated network that integrates and converges dopamine and glutamate signaling to appropriate nuclear targets.	Glutamic Acid	28-37	discs large MAGUK scaffold protein 4	Homo sapiens	167-172
22709448-5	2012	Previously, we reported that brain ischemia promotes the phosphorylation of postsynaptic density protein 95 (PSD-95) at tyrosine 523 (Y523), which is associated with postsynaptic mechanisms of excitotoxicity.	Tyrosine	120-128	discs large MAGUK scaffold protein 4	Homo sapiens	76-107
22709448-5	2012	Previously, we reported that brain ischemia promotes the phosphorylation of postsynaptic density protein 95 (PSD-95) at tyrosine 523 (Y523), which is associated with postsynaptic mechanisms of excitotoxicity.	Tyrosine	120-128	discs large MAGUK scaffold protein 4	Homo sapiens	109-115
22375001-1	2012	N-methyl-D-aspartate (NMDA) neurotransmitter receptors and the postsynaptic density-95 (PSD-95) membrane-associated guanylate kinase (MAGUK) family of scaffolding proteins are integral components of post-synaptic macromolecular signaling complexes that serve to propagate glutamate responses intracellularly.	Glutamic Acid	272-281	discs large MAGUK scaffold protein 4	Homo sapiens	63-86
22378468-4	2012	In primary cultures of hippocampal neurons, PKMzeta activity was critical for increasing the size of PSD-95 clusters during chemical LTP (cLTP).	cltp	138-142	discs large MAGUK scaffold protein 4	Homo sapiens	101-107
22378468-6	2012	Overexpression of an inactive mutant of PKMzeta did not increase PSD-95 clustering, and applications of the zeta-pseudosubstrate inhibitor ZIP reversed the PKMzeta-mediated increases in PSD-95 clustering, indicating that the activity of PKMzeta is necessary to induce and maintain the increased size of PSD-95 clusters.	pkmzeta	156-163	discs large MAGUK scaffold protein 4	Homo sapiens	186-192
22378468-6	2012	Overexpression of an inactive mutant of PKMzeta did not increase PSD-95 clustering, and applications of the zeta-pseudosubstrate inhibitor ZIP reversed the PKMzeta-mediated increases in PSD-95 clustering, indicating that the activity of PKMzeta is necessary to induce and maintain the increased size of PSD-95 clusters.	pkmzeta	156-163	discs large MAGUK scaffold protein 4	Homo sapiens	186-192
22114864-4	2012	LY 341495 administration rapidly (1 h) activates the mTOR pathway (mTOR, p70S6K, 4E-BP1) and subsequently (24 h later) increases levels of synaptic proteins (PSD-95, GluR1 and Synapsin I), similar to the effects of ketamine.	LY 341495	0-9	discs large MAGUK scaffold protein 4	Homo sapiens	158-164
21069783-4	2012	DGKzeta, one of many mammalian DGKs, is localized to synapses through direct interaction with the postsynaptic scaffolding protein PSD-95, and regulates dendritic spine maintenance by promoting DAG-to-PA conversion.	Diglycerides	194-197	discs large MAGUK scaffold protein 4	Homo sapiens	131-137
21069783-4	2012	DGKzeta, one of many mammalian DGKs, is localized to synapses through direct interaction with the postsynaptic scaffolding protein PSD-95, and regulates dendritic spine maintenance by promoting DAG-to-PA conversion.	Phosphatidic Acids	201-203	discs large MAGUK scaffold protein 4	Homo sapiens	131-137
22375001-1	2012	N-methyl-D-aspartate (NMDA) neurotransmitter receptors and the postsynaptic density-95 (PSD-95) membrane-associated guanylate kinase (MAGUK) family of scaffolding proteins are integral components of post-synaptic macromolecular signaling complexes that serve to propagate glutamate responses intracellularly.	Glutamic Acid	272-281	discs large MAGUK scaffold protein 4	Homo sapiens	88-94
22378880-6	2012	We also found that exogenous ATP protected Abeta42-mediated reduction in synaptic molecules, such as NMDA receptor 2A and PSD-95, through P2 purinergic receptors and prevented Abeta42-induced spine reduction in cultured primary hippocampal neurons.	Adenosine Triphosphate	29-32	discs large MAGUK scaffold protein 4	Homo sapiens	122-128
22342969-12	2012	PSD-95, a postsynaptic scaffold protein, was examined with immunogold silver staining (n=2/group), and the total number of PSD-95-positive puncta was determined with stereology across four levels of the dorsal raphe.	Silver	70-76	discs large MAGUK scaffold protein 4	Homo sapiens	0-6
21530246-0	2011	NMR evaluation of interactions between substituted-indole and PDZ1 domain of PSD-95.	substituted-indole	39-57	discs large MAGUK scaffold protein 4	Homo sapiens	77-83
22098454-5	2011	Characterization of ID-PRIME in living mammalian cells shows that multiple protein-protein interactions can be imaged (FRB-FKBP, Fos-Jun, and neuroligin-PSD-95), with as little as 10 min of coumarin treatment.	coumarin	190-198	discs large MAGUK scaffold protein 4	Homo sapiens	153-159
21741804-8	2011	Steroid-treated stressed animals displayed significantly increased dendritic growth and spine density, with increased levels of brain-derived neurotrophic factor (BDNF) and obtunded postsynaptic density-95 (PSD-95) levels.	Steroids	0-7	discs large MAGUK scaffold protein 4	Homo sapiens	182-205
21741804-8	2011	Steroid-treated stressed animals displayed significantly increased dendritic growth and spine density, with increased levels of brain-derived neurotrophic factor (BDNF) and obtunded postsynaptic density-95 (PSD-95) levels.	Steroids	0-7	discs large MAGUK scaffold protein 4	Homo sapiens	207-213
21626699-11	2011	Finally, binding to PDZ domains of PSD-95, syntrophin, and DVL3 was studied using 1H,15N HSQC NMR spectroscopy.	Hydrogen	82-84	discs large MAGUK scaffold protein 4	Homo sapiens	35-41
21626699-11	2011	Finally, binding to PDZ domains of PSD-95, syntrophin, and DVL3 was studied using 1H,15N HSQC NMR spectroscopy.	15n	85-88	discs large MAGUK scaffold protein 4	Homo sapiens	35-41
22343531-2	2012	Here we report the design and synthesis of a novel dimeric inhibitor, Tat-NPEG4(IETDV)(2) (Tat-N-dimer), which binds the tandem PDZ1-2 domain of PSD-95 with an unprecedented high affinity of 4.6 nM, and displays extensive protease-resistance as evaluated in vitro by stability-measurements in human blood plasma.	tat-npeg4	70-79	discs large MAGUK scaffold protein 4	Homo sapiens	145-151
22343531-2	2012	Here we report the design and synthesis of a novel dimeric inhibitor, Tat-NPEG4(IETDV)(2) (Tat-N-dimer), which binds the tandem PDZ1-2 domain of PSD-95 with an unprecedented high affinity of 4.6 nM, and displays extensive protease-resistance as evaluated in vitro by stability-measurements in human blood plasma.	ietdv	80-85	discs large MAGUK scaffold protein 4	Homo sapiens	145-151
23251670-3	2012	We demonstrate the biocompatibility and stability of a red-emitting squaraine-rotaxane (SeTau-647) by imaging dye-filled neurons in vivo over 5 days, and utility for sensitive subcellular imaging by synthesizing a specific peptide-conjugate label for the synaptic protein PSD-95.	squaraine-rotaxane	68-86	discs large MAGUK scaffold protein 4	Homo sapiens	272-278
21427709-4	2011	Here, we show that spinal delivery of the mimetic peptide Tat-NR2B9c disrupts the interaction between PSD-95 and NR2B subunits in the dorsal horn and selectively reduces NMDA receptor-dependent events including wind-up of spinal sensory neurons, and both persistent formalin-induced neuronal activity and pain-related behaviors, attributed to central sensitization.	Formaldehyde	266-274	discs large MAGUK scaffold protein 4	Homo sapiens	102-108
21530246-2	2011	These indole-based compounds were evaluated for their interaction with the PDZ1 domain of the post-synaptic density 95 (PSD-95) protein.	indole	6-12	discs large MAGUK scaffold protein 4	Homo sapiens	94-118
21530246-2	2011	These indole-based compounds were evaluated for their interaction with the PDZ1 domain of the post-synaptic density 95 (PSD-95) protein.	indole	6-12	discs large MAGUK scaffold protein 4	Homo sapiens	120-126
20972425-6	2010	Specificity of nitric oxide signalling is often achieved by the binding of nitric oxide synthase (NOS) to target proteins, either directly or through scaffolding proteins such as PSD-95 (ref.	Nitric Oxide	15-27	discs large MAGUK scaffold protein 4	Homo sapiens	179-185
21217644-5	2011	Furthermore, depletion of synaptic Zn(2+) along with the knockdown of zinc-insensitive Shank1 causes the rapid disintegration of PSDs and the loss of several postsynaptic molecules including Homer1, PSD-95 and NMDA receptors.	Zinc	35-37	discs large MAGUK scaffold protein 4	Homo sapiens	199-205
21126734-7	2011	In line with the GluA1-PSD-95 implications of enhanced synaptic plasticity, Homer 1b/c protein expression was increased in both heroin and cocaine users as was its binding partner, dynamin-3.	Cocaine	139-146	discs large MAGUK scaffold protein 4	Homo sapiens	23-29
21270901-8	2011	The interaction of PSD95 with nNOS controls synapse formation and is implicated in N-methyl-D-aspartic acid-induced neuronal death.	Aspartic Acid	94-107	discs large MAGUK scaffold protein 4	Homo sapiens	19-24
21055435-10	2011	PSD95 showed a significant upregulation by acute citalopram and by haloperidol plus valproate in both cortical and subcortical regions.	Citalopram	49-59	discs large MAGUK scaffold protein 4	Homo sapiens	0-5
21055435-10	2011	PSD95 showed a significant upregulation by acute citalopram and by haloperidol plus valproate in both cortical and subcortical regions.	Haloperidol	67-78	discs large MAGUK scaffold protein 4	Homo sapiens	0-5
21055435-10	2011	PSD95 showed a significant upregulation by acute citalopram and by haloperidol plus valproate in both cortical and subcortical regions.	Valproic Acid	84-93	discs large MAGUK scaffold protein 4	Homo sapiens	0-5
20831617-6	2010	We found that the concentration of Tat-NR2B9c required to dissociate 50% of PSD-95 was fourfold lower for NR2B than NR2A in cultured hippocampal and striatal neurons, and that this concentration correlated tightly with protection against NMDA-induced toxicity in hippocampal neurons without altering NMDAR current.	N-Methylaspartate	238-242	discs large MAGUK scaffold protein 4	Homo sapiens	76-82
20401643-3	2010	In cocaine-treated animals, latrunculin-reduced dendritic spine density and decreased the levels of F-actin and PSD-95 in postsynaptic density subfractions.	Cocaine	3-10	discs large MAGUK scaffold protein 4	Homo sapiens	112-118
21322614-5	2011	Subsequent optimization of the N-alkyl groups and evaluation of cell permeability led to identification of N-cyclohexylethyl-ETA(S)V (54) as the most potent, plasma-stable and cell-permeable inhibitor, which is a promising tool in unraveling the therapeutic potential of the PSD-95/NMDA receptor interaction.	n-cyclohexylethyl-eta	107-128	discs large MAGUK scaffold protein 4	Homo sapiens	275-281
20888327-0	2010	Calcium/calmodulin-dependent kinase II facilitated GluR6 subunit serine phosphorylation through GluR6-PSD95-CaMKII signaling module assembly in cerebral ischemia injury.	Serine	65-71	discs large MAGUK scaffold protein 4	Homo sapiens	102-107
20888327-2	2010	Our present study shows that the assembly of the GluR6-PSD95-CaMKII signaling module induced by brain ischemia facilitates the serine phosphorylation of GluR6 and further induces the activation of c-Jun NH2-terminal kinase JNK.	Serine	127-133	discs large MAGUK scaffold protein 4	Homo sapiens	55-60
20888327-3	2010	More important, a selective CaMKII inhibitor KN-93 suppressed the increase of the GluR6-PSD95-CaMKII signaling module assembly and GluR6 serine phosphorylation as well as JNK activation.	KN 93	45-50	discs large MAGUK scaffold protein 4	Homo sapiens	88-93
20926668-3	2010	Morphine treatment for ~20 h increased the colocalization of GIRK2 with PSD95, a dendritic spine marker.	Morphine	0-8	discs large MAGUK scaffold protein 4	Homo sapiens	72-77
20852624-4	2010	Our results suggest that the molecular mechanism involves a dynamic interaction between the neuronal calcium sensor protein hippocalcin, the clathrin adaptor molecule AP2, the postsynaptic density enriched protein PSD-95 and NMDARs.	Calcium	101-108	discs large MAGUK scaffold protein 4	Homo sapiens	214-220
20219637-8	2010	The released GABA activates postsynaptic GABA(A) receptors, which suppress the ischemic depolarization and decrease the association of signaling module Gluk2-PSD-95-MLK3 induced by the activation of postsynaptic Gluk2-KA receptors.	gamma-Aminobutyric Acid	13-17	discs large MAGUK scaffold protein 4	Homo sapiens	158-164
20652539-12	2010	A modulation by haloperidol was also seen for PSD-95 and alphaCaMKII.	Haloperidol	16-27	discs large MAGUK scaffold protein 4	Homo sapiens	46-52
20036314-8	2010	However, the block of PI-3K signaling by Wortmannin partially suppressed estrogen (48 h)-induced PSD-95 and SYP expression, suggesting a crosstalk mechanism between genomic and non-genomic actions of estrogen on synaptic plasticity.	Wortmannin	41-51	discs large MAGUK scaffold protein 4	Homo sapiens	97-103
20219637-5	2010	Moreover, our data show that ethanol can inhibit the increased assembly of the Gluk2-PSD-95-MLK3 (postsynaptic density protein-95, PSD-95 and mixed-lineage kinase 3, MLK3) module induced by cerebral ischemia and the activation of the MLK3-MKK4/7-JNK (mitogen-activated protein kinase kinase 4/7, MKK4/7) cascade.	Ethanol	29-36	discs large MAGUK scaffold protein 4	Homo sapiens	85-91
20219637-5	2010	Moreover, our data show that ethanol can inhibit the increased assembly of the Gluk2-PSD-95-MLK3 (postsynaptic density protein-95, PSD-95 and mixed-lineage kinase 3, MLK3) module induced by cerebral ischemia and the activation of the MLK3-MKK4/7-JNK (mitogen-activated protein kinase kinase 4/7, MKK4/7) cascade.	Ethanol	29-36	discs large MAGUK scaffold protein 4	Homo sapiens	98-129
20219637-5	2010	Moreover, our data show that ethanol can inhibit the increased assembly of the Gluk2-PSD-95-MLK3 (postsynaptic density protein-95, PSD-95 and mixed-lineage kinase 3, MLK3) module induced by cerebral ischemia and the activation of the MLK3-MKK4/7-JNK (mitogen-activated protein kinase kinase 4/7, MKK4/7) cascade.	Ethanol	29-36	discs large MAGUK scaffold protein 4	Homo sapiens	131-137
20008487-3	2010	After chronic ethanol exposure, there was a significant increase in the clustering of NR1 and NR2B subunits and their colocalization with the synaptic proteins synaptophysin and postsynaptic density protein 95, respectively.	Ethanol	14-21	discs large MAGUK scaffold protein 4	Homo sapiens	178-209
19610093-3	2009	Here, we first report that overexpression of the PDZ1 domain of PSD-95 protein exerts a protective role against neuronal death induced by cerebral ischemia-reperfusion in vivo and can prevent neuronal cell death induced by oxygen-glucose deprivation.	oxygen-glucose	223-237	discs large MAGUK scaffold protein 4	Homo sapiens	64-70
19883643-0	2010	Sigma receptor ligand 4-phenyl-1-(4-phenylbutyl)-piperidine modulates neuronal nitric oxide synthase/postsynaptic density-95 coupling mechanisms and protects against neonatal ischemic degeneration of striatal neurons.	4-phenyl-1-(4-phenylbutyl)piperidine	22-59	discs large MAGUK scaffold protein 4	Homo sapiens	101-124
20847396-2	2010	In this report, we show that soluble Abeta downregulates the levels of two synaptic proteins, PSD-95 and synaptophysin, and that this effect can be blocked by MK-801 (NMDAR antagonist) and ifenprodil (NR2B antagonist).	Dizocilpine Maleate	159-165	discs large MAGUK scaffold protein 4	Homo sapiens	94-100
20847396-2	2010	In this report, we show that soluble Abeta downregulates the levels of two synaptic proteins, PSD-95 and synaptophysin, and that this effect can be blocked by MK-801 (NMDAR antagonist) and ifenprodil (NR2B antagonist).	ifenprodil	189-199	discs large MAGUK scaffold protein 4	Homo sapiens	94-100
19098102-3	2008	Using glutamate iontophoresis and patch-clamp recordings, we identified functional AMPA receptors (AMPARs) and NMDA receptors at postsynaptic density protein 95 clusters induced by neurexin-1beta coated microspheres on primary hippocampal neurons.	Glutamic Acid	6-15	discs large MAGUK scaffold protein 4	Homo sapiens	129-160
19470753-5	2009	Intracellular HtrA1 is localized to microtubules in a PDZ (PSD95, Dlg, ZO1) domain-dependent, nocodazole-sensitive manner.	Nocodazole	94-104	discs large MAGUK scaffold protein 4	Homo sapiens	59-64
19411609-3	2009	In amygdala slices, NMDA at a concentration that normally does not have a long-term effect was found to reduce the cellular levels of postsynaptic density protein 95 and synapse-associated protein 97, in addition to the surface expression of GluR1/2, in the presence of a glycine transporter blocker, N[3-(4-fluorophenil)-3-(4"-phenilphenoxy)] propylsarcosine (NFPS).	N-Methylaspartate	20-24	discs large MAGUK scaffold protein 4	Homo sapiens	134-165
19596852-5	2009	We found that blocking synaptic activity rapidly induces PSD-95 palmitoylation and mediates synaptic clustering of PSD-95 and associated AMPA (alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid)-type glutamate receptors.	3-ISOXAZOL-4-YL-PROPIONIC ACID	174-200	discs large MAGUK scaffold protein 4	Homo sapiens	57-63
19596852-5	2009	We found that blocking synaptic activity rapidly induces PSD-95 palmitoylation and mediates synaptic clustering of PSD-95 and associated AMPA (alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid)-type glutamate receptors.	3-ISOXAZOL-4-YL-PROPIONIC ACID	174-200	discs large MAGUK scaffold protein 4	Homo sapiens	115-121
19261890-0	2009	PSD-95 uncouples dopamine-glutamate interaction in the D1/PSD-95/NMDA receptor complex.	Dopamine	17-25	discs large MAGUK scaffold protein 4	Homo sapiens	0-6
19261890-0	2009	PSD-95 uncouples dopamine-glutamate interaction in the D1/PSD-95/NMDA receptor complex.	Dopamine	17-25	discs large MAGUK scaffold protein 4	Homo sapiens	58-64
19261890-0	2009	PSD-95 uncouples dopamine-glutamate interaction in the D1/PSD-95/NMDA receptor complex.	Glutamic Acid	26-35	discs large MAGUK scaffold protein 4	Homo sapiens	0-6
19261890-0	2009	PSD-95 uncouples dopamine-glutamate interaction in the D1/PSD-95/NMDA receptor complex.	Glutamic Acid	26-35	discs large MAGUK scaffold protein 4	Homo sapiens	58-64
19261890-6	2009	Knockdown of PSD-95 immobilizes D(1) receptors on the cell surface and escalates NMDA receptor-dependent D(1) cAMP signaling in neurons.	Cyclic AMP	110-114	discs large MAGUK scaffold protein 4	Homo sapiens	13-19
18570704-10	2009	Increased levels of NR2A and PSD-95 suggest that glutamate signalling at the NMDA receptor in the amygdala is disrupted in depression.	Glutamic Acid	49-58	discs large MAGUK scaffold protein 4	Homo sapiens	29-35
19072119-1	2009	The two N-terminal PDZ domains of postsynaptic density protein-95 (PDS-95 PDZ1 and PDZ2) are closely connected in tandem by a conserved peptide linker of five amino acids.	Palladium	67-70	discs large MAGUK scaffold protein 4	Homo sapiens	34-65
19400698-3	2009	Animals given three of these compounds, all nutrients-uridine, the omega-3 polyunsaturated fatty acid docosahexaenoic acid, and choline-develop increased levels of brain phosphatides and of proteins that are concentrated within synaptic membranes (e.g., PSD-95, synapsin-1), improved cognition, and enhanced neurotransmitter release.	omega-3 polyunsaturated fatty acid	67-101	discs large MAGUK scaffold protein 4	Homo sapiens	254-260
19400698-3	2009	Animals given three of these compounds, all nutrients-uridine, the omega-3 polyunsaturated fatty acid docosahexaenoic acid, and choline-develop increased levels of brain phosphatides and of proteins that are concentrated within synaptic membranes (e.g., PSD-95, synapsin-1), improved cognition, and enhanced neurotransmitter release.	Choline	128-135	discs large MAGUK scaffold protein 4	Homo sapiens	254-260
19400698-3	2009	Animals given three of these compounds, all nutrients-uridine, the omega-3 polyunsaturated fatty acid docosahexaenoic acid, and choline-develop increased levels of brain phosphatides and of proteins that are concentrated within synaptic membranes (e.g., PSD-95, synapsin-1), improved cognition, and enhanced neurotransmitter release.	Phospholipids	170-182	discs large MAGUK scaffold protein 4	Homo sapiens	254-260
19388649-2	2009	A series of peptides derived from the C-terminal sequence of Stargazin was first used with PDZ domains of PSD-95 and Shank3 to identify the optimal position and linker length for the 4-DMAP chromophore.	4-dimethylaminopyridine	183-189	discs large MAGUK scaffold protein 4	Homo sapiens	106-112
19041927-5	2009	In this study, we determined whether prenatal morphine exposure altered the synaptic complex association between PSD-95 and three major NMDAR subunits (NR1, NR2A, and NR2B), at the mRNA and protein levels, within the hippocampal CA1 subregion (an important integration area for mammalian learning and memory) of rat offspring along with the performance of long-term cognitive functions.	Morphine	46-54	discs large MAGUK scaffold protein 4	Homo sapiens	113-119
19075115-0	2008	PSD-95 promotes synaptogenesis and multiinnervated spine formation through nitric oxide signaling.	Nitric Oxide	75-87	discs large MAGUK scaffold protein 4	Homo sapiens	0-6
19091974-7	2008	In agreement, brief treatment with NMDA (a chemical LTD paradigm) caused the degradation of PSD-95 and the redistribution of AKAP79/150 and alpha-actinin from dendritic spines into the shaft, without a concurrent loss or redistribution of Ca(V)1.2-HA clusters.	N-Methylaspartate	35-39	discs large MAGUK scaffold protein 4	Homo sapiens	92-98
18424056-0	2008	Postsynaptic density protein PSD-95 expression in Alzheimer"s disease and okadaic acid induced neuritic retraction.	Okadaic Acid	74-86	discs large MAGUK scaffold protein 4	Homo sapiens	29-35
19081375-0	2008	Destabilization of the postsynaptic density by PSD-95 serine 73 phosphorylation inhibits spine growth and synaptic plasticity.	Serine	54-60	discs large MAGUK scaffold protein 4	Homo sapiens	47-53
19081375-5	2008	Activity-dependent trafficking of PSD-95 is triggered by phosphorylation at serine 73, a conserved calcium/calmodulin-dependent protein kinase II (CaMKII) consensus phosphorylation site, which negatively regulates spine growth and potentiation of synaptic currents.	Serine	76-82	discs large MAGUK scaffold protein 4	Homo sapiens	34-40
18512761-5	2008	Coapplication of muscimol with baclofen not only enhanced nNOS (Ser847) phosphorylation but also increased the interaction of nNOS with PSD95 at 6 hr and 1 day of reperfusion.	Muscimol	17-25	discs large MAGUK scaffold protein 4	Homo sapiens	136-141
18512761-5	2008	Coapplication of muscimol with baclofen not only enhanced nNOS (Ser847) phosphorylation but also increased the interaction of nNOS with PSD95 at 6 hr and 1 day of reperfusion.	Baclofen	31-39	discs large MAGUK scaffold protein 4	Homo sapiens	136-141
18579798-3	2008	PSD-95 has been implicated in recruiting proteins to lipid rafts, which are membrane microdomains rich in cholesterol and sphingolipids that organize receptor/signaling complexes.	Cholesterol	106-117	discs large MAGUK scaffold protein 4	Homo sapiens	0-6
18579798-3	2008	PSD-95 has been implicated in recruiting proteins to lipid rafts, which are membrane microdomains rich in cholesterol and sphingolipids that organize receptor/signaling complexes.	Sphingolipids	122-135	discs large MAGUK scaffold protein 4	Homo sapiens	0-6
18579798-5	2008	When cells were exposed to methyl-beta-cyclodextrin to deplete membrane cholesterol and disrupt lipid rafts, PSD-95 localization to lipid raft fractions was abolished and no longer inhibited ASIC3 current.	methyl-beta-cyclodextrin	27-51	discs large MAGUK scaffold protein 4	Homo sapiens	109-115
18579798-5	2008	When cells were exposed to methyl-beta-cyclodextrin to deplete membrane cholesterol and disrupt lipid rafts, PSD-95 localization to lipid raft fractions was abolished and no longer inhibited ASIC3 current.	Cholesterol	72-83	discs large MAGUK scaffold protein 4	Homo sapiens	109-115
18579798-6	2008	Likewise, mutation of two cysteine residues in PSD-95 that undergo palmitoylation (a lipid modification that targets PSD-95 to lipid rafts) prevented its inhibition of ASIC3 current and cell surface expression.	Cysteine	26-34	discs large MAGUK scaffold protein 4	Homo sapiens	47-53
18579798-6	2008	Likewise, mutation of two cysteine residues in PSD-95 that undergo palmitoylation (a lipid modification that targets PSD-95 to lipid rafts) prevented its inhibition of ASIC3 current and cell surface expression.	Cysteine	26-34	discs large MAGUK scaffold protein 4	Homo sapiens	117-123
18400955-2	2008	We previously reported that glycine-independent desensitization decreases during hippocampal neuronal development, correlating with NMDAR synaptic localization and association with postsynaptic density 95 (PSD-95).	Glycine	28-35	discs large MAGUK scaffold protein 4	Homo sapiens	181-204
18400955-2	2008	We previously reported that glycine-independent desensitization decreases during hippocampal neuronal development, correlating with NMDAR synaptic localization and association with postsynaptic density 95 (PSD-95).	Glycine	28-35	discs large MAGUK scaffold protein 4	Homo sapiens	206-212
18809680-8	2008	Interestingly, DHPG dissociated PSD-95 and N-cadherin from the delta-catenin complex, increased the association of delta-catenin with Cortactin, and induced the phosphorylation of delta-catenin within the sites that bind to these protein partners.	3,5-dihydroxyphenylglycine	15-19	discs large MAGUK scaffold protein 4	Homo sapiens	32-38
18678878-8	2008	GABA(A) receptor agonist muscimol could attenuate Src activation and interactions among NR2A, PSD-95 and Src, resulting the suppression of NMDA receptor tyrosine phosphorylation.	Muscimol	25-33	discs large MAGUK scaffold protein 4	Homo sapiens	94-100
18678878-8	2008	GABA(A) receptor agonist muscimol could attenuate Src activation and interactions among NR2A, PSD-95 and Src, resulting the suppression of NMDA receptor tyrosine phosphorylation.	Tyrosine	153-161	discs large MAGUK scaffold protein 4	Homo sapiens	94-100
18811137-2	2008	An undecapeptide corresponding to the C-terminal of the NMDA was used as a template for finding lead candidates for the inhibition of the PSD-95/NMDA receptor interaction.	N-Methylaspartate	56-60	discs large MAGUK scaffold protein 4	Homo sapiens	138-144
18811137-6	2008	The best compound, N-cyclohexylethyl-ETAV (56), demonstrated up to 19-fold lower K i value ( K i = 0.94 and 0.45 microM against PDZ1 and PDZ2 of PSD-95, respectively) compared to wild-type values, providing the most potent inhibitors of this interaction reported so far.	N-Cyclohexylethyl-ETAV	19-41	discs large MAGUK scaffold protein 4	Homo sapiens	145-151
18676085-8	2008	Moreover, treatment with sodium nitroprusside (SNP), an exogenous NO donor, increases the S-nitrosylation and phosphorylation of nNOS, leading to the attenuation of the increased S-nitrosylation of GluR6 and the assembling of GluR6* postsynaptic density protein 95 (PSD95)* mixed lineage kinase 3 (MLK3) signaling module induced by cerebral ischemia-reperfusion.	Nitroprusside	25-45	discs large MAGUK scaffold protein 4	Homo sapiens	233-264
18676085-8	2008	Moreover, treatment with sodium nitroprusside (SNP), an exogenous NO donor, increases the S-nitrosylation and phosphorylation of nNOS, leading to the attenuation of the increased S-nitrosylation of GluR6 and the assembling of GluR6* postsynaptic density protein 95 (PSD95)* mixed lineage kinase 3 (MLK3) signaling module induced by cerebral ischemia-reperfusion.	Nitroprusside	25-45	discs large MAGUK scaffold protein 4	Homo sapiens	266-271
17955054-5	2008	Whereas LH animals treated 21 days with saline (LH-S group) displayed diminished SYN and PSD-95 immunostainings in the CA3 but not in the DG, chronic treatment with FLX not only reversed the despaired behavior induced by exposure to LH paradigm, but also fully recovered SYN and PSD-95 labeling to control values.	Sodium Chloride	40-46	discs large MAGUK scaffold protein 4	Homo sapiens	89-95
17955054-5	2008	Whereas LH animals treated 21 days with saline (LH-S group) displayed diminished SYN and PSD-95 immunostainings in the CA3 but not in the DG, chronic treatment with FLX not only reversed the despaired behavior induced by exposure to LH paradigm, but also fully recovered SYN and PSD-95 labeling to control values.	Sodium Chloride	40-46	discs large MAGUK scaffold protein 4	Homo sapiens	279-285
17955054-5	2008	Whereas LH animals treated 21 days with saline (LH-S group) displayed diminished SYN and PSD-95 immunostainings in the CA3 but not in the DG, chronic treatment with FLX not only reversed the despaired behavior induced by exposure to LH paradigm, but also fully recovered SYN and PSD-95 labeling to control values.	Fluoxetine	165-168	discs large MAGUK scaffold protein 4	Homo sapiens	89-95
17955054-5	2008	Whereas LH animals treated 21 days with saline (LH-S group) displayed diminished SYN and PSD-95 immunostainings in the CA3 but not in the DG, chronic treatment with FLX not only reversed the despaired behavior induced by exposure to LH paradigm, but also fully recovered SYN and PSD-95 labeling to control values.	Fluoxetine	165-168	discs large MAGUK scaffold protein 4	Homo sapiens	279-285
17955054-8	2008	When FLX treatment was withdrawn for 90 days in those LH-FLX animals in which reversion of despair had been observed at day 25, recurrence of despaired behavior was found accompanied by decreased SYN, PSD-95, and NFL labelings.	Fluoxetine	5-8	discs large MAGUK scaffold protein 4	Homo sapiens	201-207
18600508-2	2008	In addition, the identification of PDZ (PSD-95, DglA, and ZO-1) domain protein PDZK1 as a binding partner of URAT1, and the emerging role of PDZ scaffold for renal apical transporters have led to a new concept of renal urate transport: urate-transporting multimolecular complex, or "urate transportsome," that may form an ultimate functional unit at the apical membrane of renal proximal tubules.	Uric Acid	219-224	discs large MAGUK scaffold protein 4	Homo sapiens	40-46
17486105-7	2008	Processing of the C terminus of NR2A is irreversibly induced by brief agonist exposure of NR2B-containing receptors, and requires calcium influx and the activity of calpain, also responsible for PSD-95 cleavage.	Calcium	130-137	discs large MAGUK scaffold protein 4	Homo sapiens	195-201
18600508-2	2008	In addition, the identification of PDZ (PSD-95, DglA, and ZO-1) domain protein PDZK1 as a binding partner of URAT1, and the emerging role of PDZ scaffold for renal apical transporters have led to a new concept of renal urate transport: urate-transporting multimolecular complex, or "urate transportsome," that may form an ultimate functional unit at the apical membrane of renal proximal tubules.	Uric Acid	236-241	discs large MAGUK scaffold protein 4	Homo sapiens	40-46
18600508-2	2008	In addition, the identification of PDZ (PSD-95, DglA, and ZO-1) domain protein PDZK1 as a binding partner of URAT1, and the emerging role of PDZ scaffold for renal apical transporters have led to a new concept of renal urate transport: urate-transporting multimolecular complex, or "urate transportsome," that may form an ultimate functional unit at the apical membrane of renal proximal tubules.	Uric Acid	236-241	discs large MAGUK scaffold protein 4	Homo sapiens	40-46
17765978-7	2007	Time-lapse imaging showed clustering of GFP/PSD-95 in postsynaptic neurons within 1-3h, indicating the rapid formation of new synaptic sites.	Tritium	84-86	discs large MAGUK scaffold protein 4	Homo sapiens	44-50
17988632-0	2007	Synaptic accumulation of PSD-95 and synaptic function regulated by phosphorylation of serine-295 of PSD-95.	Serine	86-92	discs large MAGUK scaffold protein 4	Homo sapiens	25-31
17988632-0	2007	Synaptic accumulation of PSD-95 and synaptic function regulated by phosphorylation of serine-295 of PSD-95.	Serine	86-92	discs large MAGUK scaffold protein 4	Homo sapiens	100-106
17988632-2	2007	Here we report that phosphorylation of ser-295 enhances the synaptic accumulation of PSD-95 and the ability of PSD-95 to recruit surface AMPA receptors and potentiate excitatory postsynaptic currents.	Serine	39-42	discs large MAGUK scaffold protein 4	Homo sapiens	85-91
17988632-2	2007	Here we report that phosphorylation of ser-295 enhances the synaptic accumulation of PSD-95 and the ability of PSD-95 to recruit surface AMPA receptors and potentiate excitatory postsynaptic currents.	Serine	39-42	discs large MAGUK scaffold protein 4	Homo sapiens	111-117
17988632-3	2007	We present evidence that a Rac1-JNK1 signaling pathway mediates ser-295 phosphorylation and regulates synaptic content of PSD-95.	Serine	64-67	discs large MAGUK scaffold protein 4	Homo sapiens	122-128
17988632-6	2007	Overexpression of a phosphomimicking mutant (S295D) of PSD-95 inhibited NMDA-induced AMPA receptor internalization and blocked the induction of LTD.	N-Methylaspartate	72-76	discs large MAGUK scaffold protein 4	Homo sapiens	55-61
17988632-7	2007	The data suggest that synaptic strength can be regulated by phosphorylation-dephosphorylation of ser-295 of PSD-95 and that synaptic depression requires the dephosphorylation of ser-295.	Serine	97-100	discs large MAGUK scaffold protein 4	Homo sapiens	108-114
17982573-7	2007	These observations led us to propose a molecular model for ethanol-induced plasticity at excitatory synapses in which increases in NR2B-containing NMDA receptors and PSD-95 at the PSD provide an expanded scaffolding platform for the recruitment and activation of signaling molecules that regulate spine actin dynamics, protein translation, and synaptic plasticity.	Ethanol	59-66	discs large MAGUK scaffold protein 4	Homo sapiens	166-172
17646177-0	2007	Tyrosine phosphorylation of ErbB4 is enhanced by PSD95 and repressed by protein tyrosine phosphatase receptor type Z.	Tyrosine	0-8	discs large MAGUK scaffold protein 4	Homo sapiens	49-54
17854350-5	2007	Through patch-clamp electrophysiology, immunochemistry, and co-immunoprecipitation, we found that while Kv1.3 and PSD-95 alone interact via the canonical C-terminal PDZ recognition motif of the channel, this molecular site of interaction acts to cluster the channels but the PSD-95 SH(3)-guanylate kinase domain functionally modulates Kv1.3 activity via two proline-rich domains in its N- and C-terminal.	Proline	358-365	discs large MAGUK scaffold protein 4	Homo sapiens	114-120
17906398-4	2007	NaPi- II a is part of the heteromeric protein complexes organized by PDZ ( [PSD-95/Disc-large/ZO-1] -binding proteins) proteins.	napi- ii a	0-10	discs large MAGUK scaffold protein 4	Homo sapiens	76-82
17898222-6	2007	The same nicotine treatment increased the levels of the AMPA glutamate receptor subunit GluR1, the NMDA receptor subunit NR2A, the metabotropic receptor mGluR1alpha, the plasticity factor Homer-1A, and the scaffolding postsynaptic density protein PSD-95, whereas the levels of another scaffolding protein, Shank, were reduced.	Nicotine	9-17	discs large MAGUK scaffold protein 4	Homo sapiens	247-253
17369255-7	2007	Co-expression of PSD-95 with D1 in mammalian cells inhibits the D1-mediated cAMP accumulation without altering the total expression level or the agonist binding properties of the receptor.	Cyclic AMP	76-80	discs large MAGUK scaffold protein 4	Homo sapiens	17-23
16573685-4	2006	Protein interaction is mediated by the carboxy-terminal Thr-Arg-Leu (TRL) motif of Map and the PSD-95/Disk-large/ZO-1 domain 1 (PDZ1) of EBP50/NHERF1.	Threonine	56-59	discs large MAGUK scaffold protein 4	Homo sapiens	95-101
17507558-5	2007	Double immunostaining for the postsynaptic density protein PSD95 revealed that spines with high pPAK or pCofilin levels had larger synapses (+60-70%) with a more normal size frequency distribution than did neighboring spines.	pcofilin	104-112	discs large MAGUK scaffold protein 4	Homo sapiens	59-64
17270176-3	2007	Herein we investigated the long-term effects of perinatal hypoxia upon the complex of PSD-95 with NMDAR subunits by means of downstream signalling cAMP response element binding protein (CREB) phosphorylation at the Serine-133 locus (CREB(Ser-133) phosphorylation) within the hippocampal CA1 area (an essential integration area for mammalian learning and memory) within test-rat brains, as well as the effects upon afflicted-individual long-term learning and memory performance.	Serine	215-221	discs large MAGUK scaffold protein 4	Homo sapiens	86-92
17270176-3	2007	Herein we investigated the long-term effects of perinatal hypoxia upon the complex of PSD-95 with NMDAR subunits by means of downstream signalling cAMP response element binding protein (CREB) phosphorylation at the Serine-133 locus (CREB(Ser-133) phosphorylation) within the hippocampal CA1 area (an essential integration area for mammalian learning and memory) within test-rat brains, as well as the effects upon afflicted-individual long-term learning and memory performance.	Serine	215-218	discs large MAGUK scaffold protein 4	Homo sapiens	86-92
17187494-12	2007	In agreement, the ErbB4-PSD-95-NMDA complex was more tightly coupled in schizophrenic brains and NRG1-mediated stimulation of ErbB4 was markedly enhanced.	N-Methylaspartate	31-35	discs large MAGUK scaffold protein 4	Homo sapiens	24-30
17156196-5	2006	CaMKII-dependent phosphorylation of PSD-95 occurs both in vitro, in GST-PSD-95 fusion proteins phosphorylated by purified active CaMKII, and in vivo, in transfected COS-7 as well as in cultured hippocampal neurons.	cos-7	165-170	discs large MAGUK scaffold protein 4	Homo sapiens	36-42
16473877-7	2006	The interaction of Ggamma13 with the PDZ domain of PSD95 was via the C-terminal CAAX tail of Ggamma13 (where AA indicates the aliphatic amino acid); alanine substitution of the CTAL sequence at the C terminus of Ggamma13 abolished its interactions with PSD95 in two-hybrid and pull-down assays.	Alanine	149-156	discs large MAGUK scaffold protein 4	Homo sapiens	51-56
17267564-6	2007	Virus-mediated expression of PSD-95:CFP (postsynaptic density-95 tagged with cyan fluorescent protein) revealed that spontaneous local calcium transients occurred frequently at postsynaptic sites along the dendrite.	Calcium	135-142	discs large MAGUK scaffold protein 4	Homo sapiens	29-35
17164261-0	2007	Fine mapping of a linkage region on chromosome 17p13 reveals that GABARAP and DLG4 are associated with vulnerability to nicotine dependence in European-Americans.	Nicotine	120-128	discs large MAGUK scaffold protein 4	Homo sapiens	78-82
17093888-1	2007	The postsynaptic density protein 95 (PSD-95) - the prototype of this family - is a modular protein that enables anchoring of NMDA receptors, modulates NMDA receptor sensitivity to glutamate and coordinates NMDA receptor-related intracellular processes.	Glutamic Acid	180-189	discs large MAGUK scaffold protein 4	Homo sapiens	4-35
17093888-1	2007	The postsynaptic density protein 95 (PSD-95) - the prototype of this family - is a modular protein that enables anchoring of NMDA receptors, modulates NMDA receptor sensitivity to glutamate and coordinates NMDA receptor-related intracellular processes.	Glutamic Acid	180-189	discs large MAGUK scaffold protein 4	Homo sapiens	37-43
17093888-7	2007	Further genetic studies in schizophrenia with other PSD-95-like molecules that interact with the glutamate system are suggested.	Glutamic Acid	97-106	discs large MAGUK scaffold protein 4	Homo sapiens	52-58
17018532-3	2006	We investigated the binding reaction between PSD-95 PDZ3 and a peptide corresponding to a native ligand with protein engineering in conjunction with stopped-flow and equilibrium fluorimetry and found that the two conserved residues Arg-318 and His-372 were responsible for the salt and pH dependencies, respectively.	Arginine	232-235	discs large MAGUK scaffold protein 4	Homo sapiens	45-51
17018532-3	2006	We investigated the binding reaction between PSD-95 PDZ3 and a peptide corresponding to a native ligand with protein engineering in conjunction with stopped-flow and equilibrium fluorimetry and found that the two conserved residues Arg-318 and His-372 were responsible for the salt and pH dependencies, respectively.	Histidine	244-247	discs large MAGUK scaffold protein 4	Homo sapiens	45-51
17018532-3	2006	We investigated the binding reaction between PSD-95 PDZ3 and a peptide corresponding to a native ligand with protein engineering in conjunction with stopped-flow and equilibrium fluorimetry and found that the two conserved residues Arg-318 and His-372 were responsible for the salt and pH dependencies, respectively.	Salts	277-281	discs large MAGUK scaffold protein 4	Homo sapiens	45-51
17018532-8	2006	Both chloride concentration and pH (during ischemia) vary in the postsynaptic density, where PSD-95 is present, and the physiological buffer conditions may thus modulate the interaction between PSD-95 and its ligands through binding of chloride and protons to the "molecular switches" Arg-318 and His-372, respectively.	Chlorides	5-13	discs large MAGUK scaffold protein 4	Homo sapiens	93-99
17018532-8	2006	Both chloride concentration and pH (during ischemia) vary in the postsynaptic density, where PSD-95 is present, and the physiological buffer conditions may thus modulate the interaction between PSD-95 and its ligands through binding of chloride and protons to the "molecular switches" Arg-318 and His-372, respectively.	Chlorides	5-13	discs large MAGUK scaffold protein 4	Homo sapiens	194-200
17018532-8	2006	Both chloride concentration and pH (during ischemia) vary in the postsynaptic density, where PSD-95 is present, and the physiological buffer conditions may thus modulate the interaction between PSD-95 and its ligands through binding of chloride and protons to the "molecular switches" Arg-318 and His-372, respectively.	Chlorides	236-244	discs large MAGUK scaffold protein 4	Homo sapiens	194-200
17018532-8	2006	Both chloride concentration and pH (during ischemia) vary in the postsynaptic density, where PSD-95 is present, and the physiological buffer conditions may thus modulate the interaction between PSD-95 and its ligands through binding of chloride and protons to the "molecular switches" Arg-318 and His-372, respectively.	Arginine	285-288	discs large MAGUK scaffold protein 4	Homo sapiens	93-99
17018532-8	2006	Both chloride concentration and pH (during ischemia) vary in the postsynaptic density, where PSD-95 is present, and the physiological buffer conditions may thus modulate the interaction between PSD-95 and its ligands through binding of chloride and protons to the "molecular switches" Arg-318 and His-372, respectively.	Arginine	285-288	discs large MAGUK scaffold protein 4	Homo sapiens	194-200
17018532-8	2006	Both chloride concentration and pH (during ischemia) vary in the postsynaptic density, where PSD-95 is present, and the physiological buffer conditions may thus modulate the interaction between PSD-95 and its ligands through binding of chloride and protons to the "molecular switches" Arg-318 and His-372, respectively.	Histidine	297-300	discs large MAGUK scaffold protein 4	Homo sapiens	93-99
17018532-8	2006	Both chloride concentration and pH (during ischemia) vary in the postsynaptic density, where PSD-95 is present, and the physiological buffer conditions may thus modulate the interaction between PSD-95 and its ligands through binding of chloride and protons to the "molecular switches" Arg-318 and His-372, respectively.	Histidine	297-300	discs large MAGUK scaffold protein 4	Homo sapiens	194-200
16990796-6	2006	Contrary to typical SH2 domain binding, the PSD-95-Src SH2 domain interaction is phosphotyrosine-independent.	Phosphotyrosine	81-96	discs large MAGUK scaffold protein 4	Homo sapiens	44-50
16573685-4	2006	Protein interaction is mediated by the carboxy-terminal Thr-Arg-Leu (TRL) motif of Map and the PSD-95/Disk-large/ZO-1 domain 1 (PDZ1) of EBP50/NHERF1.	Arginine	60-63	discs large MAGUK scaffold protein 4	Homo sapiens	95-101
16573685-4	2006	Protein interaction is mediated by the carboxy-terminal Thr-Arg-Leu (TRL) motif of Map and the PSD-95/Disk-large/ZO-1 domain 1 (PDZ1) of EBP50/NHERF1.	Leucine	64-67	discs large MAGUK scaffold protein 4	Homo sapiens	95-101
16719811-5	2006	Therefore, PSD-95 PDZ domains become attractive targets for treatment of glutamate-induced overproduction of nitric oxide.	Glutamic Acid	73-82	discs large MAGUK scaffold protein 4	Homo sapiens	11-17
16421296-2	2006	Although the synaptic localization of PSD-95 requires palmitoylation of two cysteines at the N terminus and the presence of at least one PDZ domain, how the clustering of PSD-95 is initiated and regulated remains essentially unknown.	Cysteine	76-85	discs large MAGUK scaffold protein 4	Homo sapiens	38-44
16421296-6	2006	The sensitivity to 2-bromo-palmitate and latrunculin A, reagents known to affect PSD-95 turnover, was also augmented.	2-bromopalmitate	19-36	discs large MAGUK scaffold protein 4	Homo sapiens	81-87
16421296-6	2006	The sensitivity to 2-bromo-palmitate and latrunculin A, reagents known to affect PSD-95 turnover, was also augmented.	latrunculin A	41-54	discs large MAGUK scaffold protein 4	Homo sapiens	81-87
16332460-4	2006	The "micro PSD fraction" obtained following two consecutive extractions of a synaptosomal fraction with Triton X-100 shows a significant enrichment in the marker protein PSD-95.	Octoxynol	104-116	discs large MAGUK scaffold protein 4	Homo sapiens	170-176
16719811-5	2006	Therefore, PSD-95 PDZ domains become attractive targets for treatment of glutamate-induced overproduction of nitric oxide.	Nitric Oxide	109-121	discs large MAGUK scaffold protein 4	Homo sapiens	11-17
16049001-5	2005	Both PDZ3 from postsynaptic density protein 95 and PDZ2 from protein tyrosine phosphatase L1 bind their respective target peptides through an apparent A + B --> A.B mechanism without rate-limiting conformational changes.	Peptides	122-130	discs large MAGUK scaffold protein 4	Homo sapiens	15-46
16140506-8	2005	A reduction in PSD-95 at glutamate synapses of the molecular layer may have a deleterious impact on information flow to other hippocampal regions via granule cells and their projecting mossy fibres.	Glutamic Acid	25-34	discs large MAGUK scaffold protein 4	Homo sapiens	15-21
16299499-2	2005	We show that mPins (mammalian homologue of Drosophila melanogaster partner of inscuteable) interacts with SAP102 and PSD-95 (two PDZ proteins present in neurons), and functions in the formation of the NMDAR-MAGUK (N-methyl-D-aspartate receptor-membrane-associated guanylate kinase) complex.	-maguk	206-212	discs large MAGUK scaffold protein 4	Homo sapiens	117-123
15748165-5	2005	Only CDs that lowered cholesterol levels redistributed the NMDA receptor NR2B subunit, PSD-95 (postsynaptic density protein 95 kDa) and neuronal nitric oxide synthase (nNOS) from Triton X-100 insoluble membrane domains to soluble fractions.	Cyclodextrins	5-8	discs large MAGUK scaffold protein 4	Homo sapiens	87-93
15748165-5	2005	Only CDs that lowered cholesterol levels redistributed the NMDA receptor NR2B subunit, PSD-95 (postsynaptic density protein 95 kDa) and neuronal nitric oxide synthase (nNOS) from Triton X-100 insoluble membrane domains to soluble fractions.	Octoxynol	179-191	discs large MAGUK scaffold protein 4	Homo sapiens	87-93
15748165-5	2005	Only CDs that lowered cholesterol levels redistributed the NMDA receptor NR2B subunit, PSD-95 (postsynaptic density protein 95 kDa) and neuronal nitric oxide synthase (nNOS) from Triton X-100 insoluble membrane domains to soluble fractions.	Octoxynol	179-191	discs large MAGUK scaffold protein 4	Homo sapiens	95-130
15748165-6	2005	Cholesterol repletion counteracted the ability of methylated beta-CD to protect against NMDA toxicity, and reversed NR2B, PSD-95 and nNOS localization to Triton X-100 insoluble membrane fraction.	Cholesterol	0-11	discs large MAGUK scaffold protein 4	Homo sapiens	122-128
15663949-1	2005	The folding pathway of the third domain of PDZ from the synaptic protein PSD-95 was characterized using kinetic and equilibrium methods by monitoring the fluorescence signal from a Trp residue that is incorporated at a near-surface position.	Tryptophan	181-184	discs large MAGUK scaffold protein 4	Homo sapiens	73-79
15631993-2	2005	Although the postsynaptic density protein PSD95 can recruit the calcium-dependent neuronal NO synthase (nNOS) to the mouth of the calcium-permeable NMDA receptor, and depletion of PSD95 inhibits excitotoxicity, the possibility that selective uncoupling of nNOS from PSD95 might be neuroprotective is unexplored.	Calcium	64-71	discs large MAGUK scaffold protein 4	Homo sapiens	42-47
15631993-2	2005	Although the postsynaptic density protein PSD95 can recruit the calcium-dependent neuronal NO synthase (nNOS) to the mouth of the calcium-permeable NMDA receptor, and depletion of PSD95 inhibits excitotoxicity, the possibility that selective uncoupling of nNOS from PSD95 might be neuroprotective is unexplored.	Calcium	64-71	discs large MAGUK scaffold protein 4	Homo sapiens	180-185
15631993-2	2005	Although the postsynaptic density protein PSD95 can recruit the calcium-dependent neuronal NO synthase (nNOS) to the mouth of the calcium-permeable NMDA receptor, and depletion of PSD95 inhibits excitotoxicity, the possibility that selective uncoupling of nNOS from PSD95 might be neuroprotective is unexplored.	Calcium	64-71	discs large MAGUK scaffold protein 4	Homo sapiens	180-185
15631993-5	2005	Experiments using a panel of decoy constructs targeting the PSD95-nNOS interaction suggest that this interaction and subsequent NO production are critical for glutamate-induced p38 activation and the ensuing cell death, and demonstrate that the PSD95-nNOS interface provides a genuine possibility for design of neuroprotective drugs with increased selectivity.	Glutamic Acid	159-168	discs large MAGUK scaffold protein 4	Homo sapiens	60-65
15631993-5	2005	Experiments using a panel of decoy constructs targeting the PSD95-nNOS interaction suggest that this interaction and subsequent NO production are critical for glutamate-induced p38 activation and the ensuing cell death, and demonstrate that the PSD95-nNOS interface provides a genuine possibility for design of neuroprotective drugs with increased selectivity.	Glutamic Acid	159-168	discs large MAGUK scaffold protein 4	Homo sapiens	245-250
15748165-5	2005	Only CDs that lowered cholesterol levels redistributed the NMDA receptor NR2B subunit, PSD-95 (postsynaptic density protein 95 kDa) and neuronal nitric oxide synthase (nNOS) from Triton X-100 insoluble membrane domains to soluble fractions.	Cyclodextrins	5-8	discs large MAGUK scaffold protein 4	Homo sapiens	95-130
15748165-5	2005	Only CDs that lowered cholesterol levels redistributed the NMDA receptor NR2B subunit, PSD-95 (postsynaptic density protein 95 kDa) and neuronal nitric oxide synthase (nNOS) from Triton X-100 insoluble membrane domains to soluble fractions.	Cholesterol	22-33	discs large MAGUK scaffold protein 4	Homo sapiens	87-93
15748165-5	2005	Only CDs that lowered cholesterol levels redistributed the NMDA receptor NR2B subunit, PSD-95 (postsynaptic density protein 95 kDa) and neuronal nitric oxide synthase (nNOS) from Triton X-100 insoluble membrane domains to soluble fractions.	Cholesterol	22-33	discs large MAGUK scaffold protein 4	Homo sapiens	95-130
15387515-2	2004	By substituting standard and nonproteinogenic aliphatic amino acids for the C-terminal valine of the hexapeptide KKETEV, binding to the third PDZ domain (PDZ3) of the PSD-95 protein is characterized by distinct changes in the Gibbs free energy (DeltaG), enthalpy (DeltaH), and entropy (TDeltaS) parameters.	Valine	87-93	discs large MAGUK scaffold protein 4	Homo sapiens	167-173
15458848-0	2004	Modulation of dopamine mediated phosphorylation of AMPA receptors by PSD-95 and AKAP79/150.	Dopamine	14-22	discs large MAGUK scaffold protein 4	Homo sapiens	69-75
15458848-7	2004	These results suggest in vivo stimulation of dopamine release directly influences AMPA receptor phosphorylation and together with in vitro data indicate that coupling of the AMPA receptor to AKAP79/150 and PSD-95 modulate this process.	Dopamine	45-53	discs large MAGUK scaffold protein 4	Homo sapiens	206-212
14969737-8	2004	In this study, we investigated dopamine-glutamate interactions by measuring the expression of transcripts encoding the subunits for the ionotropic glutamate receptors (NMDA, AMPA and kainate) and five NMDAR-associated intracellular proteins, PSD-93, PSD-95, SAP102, NF-L and yotiao in the dopaminergic neurons in the substantia nigra pars compacta (SNc) of subjects with schizophrenia and a comparison group.	Dopamine	31-39	discs large MAGUK scaffold protein 4	Homo sapiens	250-256
14741046-8	2004	SAP90 also becomes phosphorylated in response to mitogens, and this phosphorylation is prevented by pretreatment of the cells with PD 184352, but not with SB 203580.	2-(2-chloro-4-iodophenylamino)-N-cyclopropylmethoxy-3,4-difluorobenzamide	131-140	discs large MAGUK scaffold protein 4	Homo sapiens	0-5
15123241-1	2004	A cyclic peptide, Tyr-Lys-c[-Lys-Thr-Glu(betaAla)-]-Val, incorporating a beta-Ala lactam side chain linker and designed to target the PDZ domains of the postsynaptic density protein 95 (PSD-95), has been synthesized and structurally characterized by NMR while free and bound to the PDZ1 domain of PSD-95.	Peptides, Cyclic	2-16	discs large MAGUK scaffold protein 4	Homo sapiens	153-184
15123241-1	2004	A cyclic peptide, Tyr-Lys-c[-Lys-Thr-Glu(betaAla)-]-Val, incorporating a beta-Ala lactam side chain linker and designed to target the PDZ domains of the postsynaptic density protein 95 (PSD-95), has been synthesized and structurally characterized by NMR while free and bound to the PDZ1 domain of PSD-95.	Peptides, Cyclic	2-16	discs large MAGUK scaffold protein 4	Homo sapiens	186-192
15123241-1	2004	A cyclic peptide, Tyr-Lys-c[-Lys-Thr-Glu(betaAla)-]-Val, incorporating a beta-Ala lactam side chain linker and designed to target the PDZ domains of the postsynaptic density protein 95 (PSD-95), has been synthesized and structurally characterized by NMR while free and bound to the PDZ1 domain of PSD-95.	Peptides, Cyclic	2-16	discs large MAGUK scaffold protein 4	Homo sapiens	297-303
15123241-1	2004	A cyclic peptide, Tyr-Lys-c[-Lys-Thr-Glu(betaAla)-]-Val, incorporating a beta-Ala lactam side chain linker and designed to target the PDZ domains of the postsynaptic density protein 95 (PSD-95), has been synthesized and structurally characterized by NMR while free and bound to the PDZ1 domain of PSD-95.	tyr-lys-c	18-27	discs large MAGUK scaffold protein 4	Homo sapiens	153-184
15123241-1	2004	A cyclic peptide, Tyr-Lys-c[-Lys-Thr-Glu(betaAla)-]-Val, incorporating a beta-Ala lactam side chain linker and designed to target the PDZ domains of the postsynaptic density protein 95 (PSD-95), has been synthesized and structurally characterized by NMR while free and bound to the PDZ1 domain of PSD-95.	tyr-lys-c	18-27	discs large MAGUK scaffold protein 4	Homo sapiens	186-192
15123241-1	2004	A cyclic peptide, Tyr-Lys-c[-Lys-Thr-Glu(betaAla)-]-Val, incorporating a beta-Ala lactam side chain linker and designed to target the PDZ domains of the postsynaptic density protein 95 (PSD-95), has been synthesized and structurally characterized by NMR while free and bound to the PDZ1 domain of PSD-95.	tyr-lys-c	18-27	discs large MAGUK scaffold protein 4	Homo sapiens	297-303
15123241-1	2004	A cyclic peptide, Tyr-Lys-c[-Lys-Thr-Glu(betaAla)-]-Val, incorporating a beta-Ala lactam side chain linker and designed to target the PDZ domains of the postsynaptic density protein 95 (PSD-95), has been synthesized and structurally characterized by NMR while free and bound to the PDZ1 domain of PSD-95.	[-lys-thr-glu(betaala)-]-val	27-55	discs large MAGUK scaffold protein 4	Homo sapiens	153-184
15123241-1	2004	A cyclic peptide, Tyr-Lys-c[-Lys-Thr-Glu(betaAla)-]-Val, incorporating a beta-Ala lactam side chain linker and designed to target the PDZ domains of the postsynaptic density protein 95 (PSD-95), has been synthesized and structurally characterized by NMR while free and bound to the PDZ1 domain of PSD-95.	[-lys-thr-glu(betaala)-]-val	27-55	discs large MAGUK scaffold protein 4	Homo sapiens	186-192
15123241-1	2004	A cyclic peptide, Tyr-Lys-c[-Lys-Thr-Glu(betaAla)-]-Val, incorporating a beta-Ala lactam side chain linker and designed to target the PDZ domains of the postsynaptic density protein 95 (PSD-95), has been synthesized and structurally characterized by NMR while free and bound to the PDZ1 domain of PSD-95.	beta-ala lactam	73-88	discs large MAGUK scaffold protein 4	Homo sapiens	153-184
15190099-2	2004	Here we show that NMDA receptor 1 (NR1) subunit and postsynaptic density (PSD)-95 protein levels are selectively reduced in the PSD of dopamine (DA)-denervated striata.	Dopamine	135-143	discs large MAGUK scaffold protein 4	Homo sapiens	52-81
12435606-6	2002	Co-expression of PSD95 with Kv1.5 N- and C-terminal deletions in HEK cells had contrasting effects on the magnitudes of the potassium currents across the membranes of these cells.	Potassium	124-133	discs large MAGUK scaffold protein 4	Homo sapiens	17-22
14642282-5	2003	Mutations that block PSD-95 ubiquitination prevent NMDA-induced AMPA receptor endocytosis.	N-Methylaspartate	51-55	discs large MAGUK scaffold protein 4	Homo sapiens	21-27
12810713-5	2003	Expression of polyglutamine-expanded huntingtin induced elevation of phosphorylated or activated Src and increased targeting of PSD-95 (post-synaptic density 95) and activated Src to cell surface membrane.	polyglutamine	14-27	discs large MAGUK scaffold protein 4	Homo sapiens	128-134
12810713-5	2003	Expression of polyglutamine-expanded huntingtin induced elevation of phosphorylated or activated Src and increased targeting of PSD-95 (post-synaptic density 95) and activated Src to cell surface membrane.	polyglutamine	14-27	discs large MAGUK scaffold protein 4	Homo sapiens	136-160
12592016-6	2003	In the original work, the PDZ3 of PSD-95 was used, which preferentially recognizes the consensus sequence Ser-X-Val-COOH.	ser-x-val	106-115	discs large MAGUK scaffold protein 4	Homo sapiens	34-40
12592016-6	2003	In the original work, the PDZ3 of PSD-95 was used, which preferentially recognizes the consensus sequence Ser-X-Val-COOH.	Carbonic Acid	116-120	discs large MAGUK scaffold protein 4	Homo sapiens	34-40
12581858-1	2003	PDZ-GEF1 (RA-GEF/nRapGEP/CNrasGEF) is a guanine nucleotide exchange factor (GEF) characterised by the presence of a PSD-95/DlgA/ZO-1 (PDZ) domain, a Ras-association (RA) domain and a region related to a cyclic nucleotide binding domain (RCBD).	Nucleotides, Cyclic	203-220	discs large MAGUK scaffold protein 4	Homo sapiens	116-122
12438413-4	2002	Here, we show that PSD-95 colocalizes precisely with Kv1 potassium channels and Caspr2 at juxtaparanodes, and that a macromolecular complex of Kv1 channels and PSD-95 can be immunopurified from mammalian brain and spinal cord.	juxtaparanodes	90-104	discs large MAGUK scaffold protein 4	Homo sapiens	19-25
12438413-6	2002	These data suggest that the primary function of PSD-95 at juxtaparanodes lies outside of its accepted role in mediating the high density clustering of Kv1 potassium channels at these sites.	juxtaparanodes	58-72	discs large MAGUK scaffold protein 4	Homo sapiens	48-54
14622105-3	2003	Thin-section and rotary shadow immuno-electron microscopy of the Triton X-100-derived PSD fraction shows many PSD-95-positive structures that resemble in situ PSDs in shape and size.	Octoxynol	65-77	discs large MAGUK scaffold protein 4	Homo sapiens	110-116
14622105-7	2003	This preparation was used to assess the association of alpha-amino-3-hydroxy-5-methylisoxazole-4-propionate (AMPA)-type glutamate receptors with the PSD-95-containing complex.	-3-hydroxy-5-methylisoxazole-4-propionate	66-107	discs large MAGUK scaffold protein 4	Homo sapiens	149-155
12810713-9	2003	Taken together, our studies show that polyglutamine-expanded huntingtin increases tyrosine phosphorylation of NMDA receptors via PSD-95 and Src, and increased tyrosine phosphorylation may contribute to the sensitization of the receptors mediated by polyglutamine-expanded huntingtin.	polyglutamine	38-51	discs large MAGUK scaffold protein 4	Homo sapiens	129-135
12810713-9	2003	Taken together, our studies show that polyglutamine-expanded huntingtin increases tyrosine phosphorylation of NMDA receptors via PSD-95 and Src, and increased tyrosine phosphorylation may contribute to the sensitization of the receptors mediated by polyglutamine-expanded huntingtin.	Tyrosine	82-90	discs large MAGUK scaffold protein 4	Homo sapiens	129-135
12630910-7	2003	The results showed that PSD-95 directly promotes the nNOS phosphorylation at Ser(847) induced by endogenous CaM-K II.	Serine	77-80	discs large MAGUK scaffold protein 4	Homo sapiens	24-30
12630910-10	2003	Thus PSD-95 mediates cellular trafficking of nNOS, and may be required for the efficient phosphorylation of nNOS at Ser(847) by CaM-K II in neuronal cells.	Serine	116-119	discs large MAGUK scaffold protein 4	Homo sapiens	5-11
12576483-6	2003	The proline-rich regions in the C-terminal half of Pyk2 bind to the SH3 domain of PSD-95 and SAP102.	Proline	4-11	discs large MAGUK scaffold protein 4	Homo sapiens	82-88
11988170-2	2002	We show that HEK293T cells cotransfected with Kir5.1 and PSD-95 exhibit a Ba(2+)-sensitive inward-rectifying K+ current.	N-methyl-valyl-amiclenomycin	74-80	discs large MAGUK scaffold protein 4	Homo sapiens	57-63
12369822-3	2002	cAMP-mediated inhibition of NHE3 requires the transporter to bind to the second PDZ (PSD95, disk large, ZO1) domain of the adapter protein NHE3 kinase A regulatory protein (E3KARP).	Cyclic AMP	0-4	discs large MAGUK scaffold protein 4	Homo sapiens	85-90
11964389-2	2002	It is known that dCrumbs interacts with Discs lost (Dlt), a protein with four PDZ (PSD95/Discs Large/ZO-1) domains (2), and Stardust (Sdt), a protein of the MAGUK (membrane-associated guanylate kinase) family (3, 4).	dcrumbs	17-24	discs large MAGUK scaffold protein 4	Homo sapiens	83-88
11923279-4	2002	We therefore investigated whether the C-terminal valine-serine-alanine-leucine (VSAL) of Kv4.2 is a novel binding motif for PSD-95.	Valine	49-55	discs large MAGUK scaffold protein 4	Homo sapiens	124-130
11923279-4	2002	We therefore investigated whether the C-terminal valine-serine-alanine-leucine (VSAL) of Kv4.2 is a novel binding motif for PSD-95.	vsal	80-84	discs large MAGUK scaffold protein 4	Homo sapiens	124-130
12068077-2	2002	The inhibition constants (K (I) s) for the binding of l-glutamate and glycine to NR1-1a/NR2A determined by [3 H]CGP 39653 and [3 H]MDL 105 519 displacement assays, respectively, were not significantly different between NR1-1a/NR2A receptors coexpressed +/- PSD-95(c-Myc).	Glutamic Acid	54-65	discs large MAGUK scaffold protein 4	Homo sapiens	257-263
12068077-2	2002	The inhibition constants (K (I) s) for the binding of l-glutamate and glycine to NR1-1a/NR2A determined by [3 H]CGP 39653 and [3 H]MDL 105 519 displacement assays, respectively, were not significantly different between NR1-1a/NR2A receptors coexpressed +/- PSD-95(c-Myc).	Glycine	70-77	discs large MAGUK scaffold protein 4	Homo sapiens	257-263
12065635-5	2002	Here we demonstrate that PSD-95 eliminates the Src-induced potentiation of NR1/NR2A channels expressed in oocytes and reduces the sensitivity of the channels to Zn(2+).	Zinc	161-163	discs large MAGUK scaffold protein 4	Homo sapiens	25-31
12417658-7	2002	The models (1) reveal that alternative splicing of the beta4 N terminus results in dramatic differences in surface charge distribution and (2) localize the proline-rich motif of beta4b to an extended arm structure that flanks what would be the equivalent of a highly modified PSD-95 carboxylate binding loop.	Proline	156-163	discs large MAGUK scaffold protein 4	Homo sapiens	276-282
12417658-7	2002	The models (1) reveal that alternative splicing of the beta4 N terminus results in dramatic differences in surface charge distribution and (2) localize the proline-rich motif of beta4b to an extended arm structure that flanks what would be the equivalent of a highly modified PSD-95 carboxylate binding loop.	carboxylate	283-294	discs large MAGUK scaffold protein 4	Homo sapiens	276-282
12068077-1	2002	Coexpression of PSD-95(c-Myc) with NR1-1a/NR2A NMDA receptors in human embryonic kidney (HEK) 293 cells resulted in a decrease in efficacy for the glycine stimulation of [3 H]MK801 binding similar to that previously described for l-glutamate.	Glycine	147-154	discs large MAGUK scaffold protein 4	Homo sapiens	16-22
12068077-1	2002	Coexpression of PSD-95(c-Myc) with NR1-1a/NR2A NMDA receptors in human embryonic kidney (HEK) 293 cells resulted in a decrease in efficacy for the glycine stimulation of [3 H]MK801 binding similar to that previously described for l-glutamate.	Dizocilpine Maleate	175-180	discs large MAGUK scaffold protein 4	Homo sapiens	16-22
12068077-1	2002	Coexpression of PSD-95(c-Myc) with NR1-1a/NR2A NMDA receptors in human embryonic kidney (HEK) 293 cells resulted in a decrease in efficacy for the glycine stimulation of [3 H]MK801 binding similar to that previously described for l-glutamate.	Glutamic Acid	230-241	discs large MAGUK scaffold protein 4	Homo sapiens	16-22
10488080-3	1999	Formation of this complex is mediated by the PDZ domains of PSD-95, which bind to the COOH termini of specific NMDA receptor subunits.	Carbonic Acid	86-90	discs large MAGUK scaffold protein 4	Homo sapiens	60-66
11955437-5	2002	We also find that rapid glutamate-mediated AMPA receptor internalization requires depalmitoylation of PSD-95.	Glutamic Acid	24-33	discs large MAGUK scaffold protein 4	Homo sapiens	102-108
11779506-3	2001	We have determined the crystal structures of the apo and GMP-bound forms to 2.3 and 2.0 A resolutions, respectively, of a fragment containing the SH3, HOOK, and guanylate kinase (GK) domains of PSD-95.	guanosine 5'-monophosphorothioate	57-60	discs large MAGUK scaffold protein 4	Homo sapiens	194-200
11546762-4	2001	Systematic mutagenesis of the GAP-43 and PSD-95 palmitoylation motifs indicates that the spacing of the palmitoylated cysteines and the presence of nearby basic amino acids determine polarized targeting by these two motifs.	Amino Acids, Basic	155-172	discs large MAGUK scaffold protein 4	Homo sapiens	41-47
11687275-6	2001	SE resulted in a decrease in the solubility of NMDA receptor subunits and of PSD-95 in 1% deoxycholate.	Deoxycholic Acid	90-102	discs large MAGUK scaffold protein 4	Homo sapiens	77-83
11677266-0	2001	Tyrosine phosphorylation of ionotropic glutamate receptors by Fyn or Src differentially modulates their susceptibility to calpain and enhances their binding to spectrin and PSD-95.	Tyrosine	0-8	discs large MAGUK scaffold protein 4	Homo sapiens	173-179
11080203-3	2000	Characterisation of the radioligand binding properties of [(3)H]MK-801 to NR1-1a/NR2A receptors with or without PSD-95 showed that PSD-95 induced a threefold increase in B:(max) values and an apparent approximately fivefold decrease in affinity in the presence of 10 microM: L-glutamate.	Glutamic Acid	275-286	discs large MAGUK scaffold protein 4	Homo sapiens	131-137
11080203-4	2000	In the presence of 1 mM: L-glutamate, the K:(i) for MK-801 binding to NR1-1a/NR2A with PSD-95 was not significantly different from that for NR1-1a/NR2A without PSD-95.	Glutamic Acid	25-36	discs large MAGUK scaffold protein 4	Homo sapiens	87-93
11080203-4	2000	In the presence of 1 mM: L-glutamate, the K:(i) for MK-801 binding to NR1-1a/NR2A with PSD-95 was not significantly different from that for NR1-1a/NR2A without PSD-95.	Glutamic Acid	25-36	discs large MAGUK scaffold protein 4	Homo sapiens	160-166
11080203-4	2000	In the presence of 1 mM: L-glutamate, the K:(i) for MK-801 binding to NR1-1a/NR2A with PSD-95 was not significantly different from that for NR1-1a/NR2A without PSD-95.	Dizocilpine Maleate	52-58	discs large MAGUK scaffold protein 4	Homo sapiens	87-93
11029657-5	2000	PSD-95-NMDA-R-APC association was found to require two cysteine residues conserved in the amino-terminus of PSD-95 that are known to be critical for its multimerization.	Cysteine	55-63	discs large MAGUK scaffold protein 4	Homo sapiens	0-6
11029657-5	2000	PSD-95-NMDA-R-APC association was found to require two cysteine residues conserved in the amino-terminus of PSD-95 that are known to be critical for its multimerization.	Cysteine	55-63	discs large MAGUK scaffold protein 4	Homo sapiens	108-114
11029657-6	2000	CONCLUSION: Our findings suggest that the PSD-95-NMDA-R-APC complex forms due to the multimerization of PSD-95 monomers, each of which can associate with either NMDA-R or APC.	r	54-55	discs large MAGUK scaffold protein 4	Homo sapiens	42-48
11029657-6	2000	CONCLUSION: Our findings suggest that the PSD-95-NMDA-R-APC complex forms due to the multimerization of PSD-95 monomers, each of which can associate with either NMDA-R or APC.	r	54-55	discs large MAGUK scaffold protein 4	Homo sapiens	104-110
12903335-5	2000	Excess passing of calcium ions through the loss of the signal pathway without PSD-95 proteins caused by antisense compound.	Calcium	18-25	discs large MAGUK scaffold protein 4	Homo sapiens	78-84
11826098-6	2002	Another difference between large GABAergic and small non-GABAergic GABA(A)R clusters was that a significant proportion of the latter was juxtaposed to postsynaptic markers of glutamatergic synapses such as PSD-95 and AMPA receptor GluR1 subunit.	gamma-Aminobutyric Acid	33-37	discs large MAGUK scaffold protein 4	Homo sapiens	206-212
11319238-5	2001	In this study we provide evidence that (i) normal huntingtin is associated with N-methyl-d-aspartate (NMDA) and kainate receptors via postsynaptic density 95 (PSD-95), (ii) the SH3 domain of PSD-95 mediates its binding to huntingtin, and (iii) polyglutamine expansion interferes with the ability of huntingtin to interact with PSD-95.	N-Methylaspartate	80-100	discs large MAGUK scaffold protein 4	Homo sapiens	134-157
11319238-5	2001	In this study we provide evidence that (i) normal huntingtin is associated with N-methyl-d-aspartate (NMDA) and kainate receptors via postsynaptic density 95 (PSD-95), (ii) the SH3 domain of PSD-95 mediates its binding to huntingtin, and (iii) polyglutamine expansion interferes with the ability of huntingtin to interact with PSD-95.	N-Methylaspartate	80-100	discs large MAGUK scaffold protein 4	Homo sapiens	159-165
11319238-5	2001	In this study we provide evidence that (i) normal huntingtin is associated with N-methyl-d-aspartate (NMDA) and kainate receptors via postsynaptic density 95 (PSD-95), (ii) the SH3 domain of PSD-95 mediates its binding to huntingtin, and (iii) polyglutamine expansion interferes with the ability of huntingtin to interact with PSD-95.	N-Methylaspartate	80-100	discs large MAGUK scaffold protein 4	Homo sapiens	191-197
11319238-5	2001	In this study we provide evidence that (i) normal huntingtin is associated with N-methyl-d-aspartate (NMDA) and kainate receptors via postsynaptic density 95 (PSD-95), (ii) the SH3 domain of PSD-95 mediates its binding to huntingtin, and (iii) polyglutamine expansion interferes with the ability of huntingtin to interact with PSD-95.	N-Methylaspartate	80-100	discs large MAGUK scaffold protein 4	Homo sapiens	191-197
11319238-5	2001	In this study we provide evidence that (i) normal huntingtin is associated with N-methyl-d-aspartate (NMDA) and kainate receptors via postsynaptic density 95 (PSD-95), (ii) the SH3 domain of PSD-95 mediates its binding to huntingtin, and (iii) polyglutamine expansion interferes with the ability of huntingtin to interact with PSD-95.	N-Methylaspartate	102-106	discs large MAGUK scaffold protein 4	Homo sapiens	134-157
11319238-5	2001	In this study we provide evidence that (i) normal huntingtin is associated with N-methyl-d-aspartate (NMDA) and kainate receptors via postsynaptic density 95 (PSD-95), (ii) the SH3 domain of PSD-95 mediates its binding to huntingtin, and (iii) polyglutamine expansion interferes with the ability of huntingtin to interact with PSD-95.	N-Methylaspartate	102-106	discs large MAGUK scaffold protein 4	Homo sapiens	159-165
11319238-5	2001	In this study we provide evidence that (i) normal huntingtin is associated with N-methyl-d-aspartate (NMDA) and kainate receptors via postsynaptic density 95 (PSD-95), (ii) the SH3 domain of PSD-95 mediates its binding to huntingtin, and (iii) polyglutamine expansion interferes with the ability of huntingtin to interact with PSD-95.	N-Methylaspartate	102-106	discs large MAGUK scaffold protein 4	Homo sapiens	191-197
11319238-5	2001	In this study we provide evidence that (i) normal huntingtin is associated with N-methyl-d-aspartate (NMDA) and kainate receptors via postsynaptic density 95 (PSD-95), (ii) the SH3 domain of PSD-95 mediates its binding to huntingtin, and (iii) polyglutamine expansion interferes with the ability of huntingtin to interact with PSD-95.	N-Methylaspartate	102-106	discs large MAGUK scaffold protein 4	Homo sapiens	191-197
11319238-5	2001	In this study we provide evidence that (i) normal huntingtin is associated with N-methyl-d-aspartate (NMDA) and kainate receptors via postsynaptic density 95 (PSD-95), (ii) the SH3 domain of PSD-95 mediates its binding to huntingtin, and (iii) polyglutamine expansion interferes with the ability of huntingtin to interact with PSD-95.	polyglutamine	244-257	discs large MAGUK scaffold protein 4	Homo sapiens	134-157
11319238-5	2001	In this study we provide evidence that (i) normal huntingtin is associated with N-methyl-d-aspartate (NMDA) and kainate receptors via postsynaptic density 95 (PSD-95), (ii) the SH3 domain of PSD-95 mediates its binding to huntingtin, and (iii) polyglutamine expansion interferes with the ability of huntingtin to interact with PSD-95.	polyglutamine	244-257	discs large MAGUK scaffold protein 4	Homo sapiens	159-165
11319238-5	2001	In this study we provide evidence that (i) normal huntingtin is associated with N-methyl-d-aspartate (NMDA) and kainate receptors via postsynaptic density 95 (PSD-95), (ii) the SH3 domain of PSD-95 mediates its binding to huntingtin, and (iii) polyglutamine expansion interferes with the ability of huntingtin to interact with PSD-95.	polyglutamine	244-257	discs large MAGUK scaffold protein 4	Homo sapiens	191-197
11319238-5	2001	In this study we provide evidence that (i) normal huntingtin is associated with N-methyl-d-aspartate (NMDA) and kainate receptors via postsynaptic density 95 (PSD-95), (ii) the SH3 domain of PSD-95 mediates its binding to huntingtin, and (iii) polyglutamine expansion interferes with the ability of huntingtin to interact with PSD-95.	polyglutamine	244-257	discs large MAGUK scaffold protein 4	Homo sapiens	191-197
11319238-9	2001	Our results demonstrate that polyglutamine expansion impairs the ability of huntingtin to bind PSD-95 and inhibits glutamate-mediated excitotoxicity.	polyglutamine	29-42	discs large MAGUK scaffold protein 4	Homo sapiens	95-101
11368788-8	2001	Overexpression of cDNAs encoding neuroligin 4 and the PDZ-domain protein, PSD-95, in COS-7 cells resulted in the formation of detergent-resistant complexes.	carbonyl sulfide	85-88	discs large MAGUK scaffold protein 4	Homo sapiens	74-80
11080203-4	2000	In the presence of 1 mM: L-glutamate, the K:(i) for MK-801 binding to NR1-1a/NR2A with PSD-95 was not significantly different from that for NR1-1a/NR2A without PSD-95.	Dizocilpine Maleate	52-58	discs large MAGUK scaffold protein 4	Homo sapiens	160-166
11080203-5	2000	The EC(50) value for the enhancement of [(3)H]MK-801 binding by L-glutamate to NR1-1a/NR2A was 1.8 +/- 0.4 (n = 4) and 8.9 (mean of n = 2) microM: in the absence and presence of PSD-95, respectively.	[(3)h]mk-801	40-52	discs large MAGUK scaffold protein 4	Homo sapiens	178-184
11080203-5	2000	The EC(50) value for the enhancement of [(3)H]MK-801 binding by L-glutamate to NR1-1a/NR2A was 1.8 +/- 0.4 (n = 4) and 8.9 (mean of n = 2) microM: in the absence and presence of PSD-95, respectively.	Glutamic Acid	64-75	discs large MAGUK scaffold protein 4	Homo sapiens	178-184
11080203-6	2000	Thus, coexpression of PSD-95 with NR1-1a/NR2A results in a decreased sensitivity to L-glutamate and an enhanced expression of NR2A and NR2B subunits.	Glutamic Acid	84-95	discs large MAGUK scaffold protein 4	Homo sapiens	22-28
10748194-0	2000	Synaptic targeting of the postsynaptic density protein PSD-95 mediated by a tyrosine-based trafficking signal.	Tyrosine	76-84	discs large MAGUK scaffold protein 4	Homo sapiens	55-61
10748194-3	2000	We now show that this C-terminal targeting domain of PSD-95 mediates postsynaptic localization through a short tyrosine-based motif followed by a pair of hydrophobic amino acids.	Tyrosine	111-119	discs large MAGUK scaffold protein 4	Homo sapiens	53-59
10748194-7	2000	Thus, postsynaptic targeting of PSD-95 requires a tyrosine-based signal that can mediate clathrin-coated vesicle formation.	Tyrosine	50-58	discs large MAGUK scaffold protein 4	Homo sapiens	32-38
10629226-6	2000	Replacing the palmitoylated NH(2) terminus of PSD-95 with alternative palmitoylation motifs at either the NH(2) or COOH termini restores ion channel clustering also induces postsynaptic targeting, respectively.	Carbonic Acid	115-119	discs large MAGUK scaffold protein 4	Homo sapiens	46-52
10364559-0	1999	Specific coupling of NMDA receptor activation to nitric oxide neurotoxicity by PSD-95 protein.	Nitric Oxide	49-61	discs large MAGUK scaffold protein 4	Homo sapiens	79-85
10443587-5	1999	N-methyl-D-aspartate (NMDA) subunits NR2A and NR2B, bind to the PSD protein called PSD-95, which in turn binds neuroligins, providing a handle for interacting with neurexin, located in the plasma membrane at the presynaptic active zone.	N-Methylaspartate	0-20	discs large MAGUK scaffold protein 4	Homo sapiens	83-89
10443587-5	1999	N-methyl-D-aspartate (NMDA) subunits NR2A and NR2B, bind to the PSD protein called PSD-95, which in turn binds neuroligins, providing a handle for interacting with neurexin, located in the plasma membrane at the presynaptic active zone.	N-Methylaspartate	22-26	discs large MAGUK scaffold protein 4	Homo sapiens	83-89
10364559-2	1999	In cultured cortical neurons, suppressing the expression of the NMDAR scaffolding protein PSD-95 (postsynaptic density-95) selectively attenuated excitotoxicity triggered via NMDARs, but not by other glutamate or calcium ion (Ca2+) channels.	Glutamic Acid	200-209	discs large MAGUK scaffold protein 4	Homo sapiens	90-96
10364559-2	1999	In cultured cortical neurons, suppressing the expression of the NMDAR scaffolding protein PSD-95 (postsynaptic density-95) selectively attenuated excitotoxicity triggered via NMDARs, but not by other glutamate or calcium ion (Ca2+) channels.	Glutamic Acid	200-209	discs large MAGUK scaffold protein 4	Homo sapiens	98-121
10364559-4	1999	Suppressing PSD-95 blocked Ca2+-activated nitric oxide production by NMDARs selectively, without affecting neuronal nitric oxide synthase expression or function.	Nitric Oxide	42-54	discs large MAGUK scaffold protein 4	Homo sapiens	12-18
10364559-5	1999	Thus, PSD-95 is required for efficient coupling of NMDAR activity to nitric oxide toxicity, and imparts specificity to excitotoxic Ca2+ signaling.	Nitric Oxide	69-81	discs large MAGUK scaffold protein 4	Homo sapiens	6-12
9892651-0	1999	PSD-95 promotes Fyn-mediated tyrosine phosphorylation of the N-methyl-D-aspartate receptor subunit NR2A.	Tyrosine	29-37	discs large MAGUK scaffold protein 4	Homo sapiens	0-6
9892651-6	1999	Results also showed that PSD-95, which directly binds to and coclusters with NMDA receptors, promotes Fyn-mediated tyrosine phosphorylation of NR2A.	Tyrosine	115-123	discs large MAGUK scaffold protein 4	Homo sapiens	25-31
9756850-3	1998	PSD-95/SAP90 also interacts with the postsynaptic density (PSD) fraction-enriched protein, named SAPAP (also called GKAP and DAP), through the GK domain.	sapap	97-102	discs large MAGUK scaffold protein 4	Homo sapiens	0-6
9875542-3	1998	In transfected COS cells, a subpopulation of PSD-95 is buoyant in sucrose gradients, and co-migrates with caveolin, a marker for caveolar domains.	Sucrose	66-73	discs large MAGUK scaffold protein 4	Homo sapiens	45-51
9875542-4	1998	Sucrose gradient separation of brain extracts showed that some neuronal PSD-95 protein is present in buoyant fractions as well.	Sucrose	0-7	discs large MAGUK scaffold protein 4	Homo sapiens	72-78
9867876-0	1999	Requirement of N-terminal cysteines of PSD-95 for PSD-95 multimerization and ternary complex formation, but not for binding to potassium channel Kv1.4.	Cysteine	26-35	discs large MAGUK scaffold protein 4	Homo sapiens	39-45
9867876-0	1999	Requirement of N-terminal cysteines of PSD-95 for PSD-95 multimerization and ternary complex formation, but not for binding to potassium channel Kv1.4.	Cysteine	26-35	discs large MAGUK scaffold protein 4	Homo sapiens	50-56
9867876-4	1999	A pair of N-terminal cysteines, Cys3 and Cys5, is essential for the ability of PSD-95 to self-associate and to form cell surface clusters with Kv1.4.	Cysteine	21-30	discs large MAGUK scaffold protein 4	Homo sapiens	79-85
9867876-5	1999	However, PSD-95 mutants lacking these cysteine residues retain their ability to associate with membranes and to bind to Kv1.4.	Cysteine	38-46	discs large MAGUK scaffold protein 4	Homo sapiens	9-15
9867876-6	1999	Unlike wild type PSD-95, the cysteine mutant of PSD-95 cannot form a ternary complex with Kv1.4 and the cell adhesion molecule Fasciclin II.	Cysteine	29-37	discs large MAGUK scaffold protein 4	Homo sapiens	48-54
9867876-7	1999	These results suggest that the N-terminal cysteines are essential for PSD-95 multimerization and that multimerization is required for simultaneous binding of multiple membrane protein ligands by PSD-95.	Cysteine	42-51	discs large MAGUK scaffold protein 4	Homo sapiens	70-76
9756850-4	1998	SAPAP is Triton X-100-insoluble and recruits PSD-95/SAP90 into the Triton X-100-insoluble fraction in the transfected cells, suggesting that SAPAP may fix PSD-95/SAP90 to the PSD.	sapap	0-5	discs large MAGUK scaffold protein 4	Homo sapiens	52-57
9756850-4	1998	SAPAP is Triton X-100-insoluble and recruits PSD-95/SAP90 into the Triton X-100-insoluble fraction in the transfected cells, suggesting that SAPAP may fix PSD-95/SAP90 to the PSD.	sapap	0-5	discs large MAGUK scaffold protein 4	Homo sapiens	155-161
9756850-4	1998	SAPAP is Triton X-100-insoluble and recruits PSD-95/SAP90 into the Triton X-100-insoluble fraction in the transfected cells, suggesting that SAPAP may fix PSD-95/SAP90 to the PSD.	sapap	0-5	discs large MAGUK scaffold protein 4	Homo sapiens	162-167
9756850-4	1998	SAPAP is Triton X-100-insoluble and recruits PSD-95/SAP90 into the Triton X-100-insoluble fraction in the transfected cells, suggesting that SAPAP may fix PSD-95/SAP90 to the PSD.	Octoxynol	9-21	discs large MAGUK scaffold protein 4	Homo sapiens	45-51
9756850-4	1998	SAPAP is Triton X-100-insoluble and recruits PSD-95/SAP90 into the Triton X-100-insoluble fraction in the transfected cells, suggesting that SAPAP may fix PSD-95/SAP90 to the PSD.	Octoxynol	9-21	discs large MAGUK scaffold protein 4	Homo sapiens	52-57
9756850-4	1998	SAPAP is Triton X-100-insoluble and recruits PSD-95/SAP90 into the Triton X-100-insoluble fraction in the transfected cells, suggesting that SAPAP may fix PSD-95/SAP90 to the PSD.	Octoxynol	9-21	discs large MAGUK scaffold protein 4	Homo sapiens	155-161
9756850-4	1998	SAPAP is Triton X-100-insoluble and recruits PSD-95/SAP90 into the Triton X-100-insoluble fraction in the transfected cells, suggesting that SAPAP may fix PSD-95/SAP90 to the PSD.	Octoxynol	9-21	discs large MAGUK scaffold protein 4	Homo sapiens	162-167
9756850-4	1998	SAPAP is Triton X-100-insoluble and recruits PSD-95/SAP90 into the Triton X-100-insoluble fraction in the transfected cells, suggesting that SAPAP may fix PSD-95/SAP90 to the PSD.	Octoxynol	67-79	discs large MAGUK scaffold protein 4	Homo sapiens	45-51
9756850-4	1998	SAPAP is Triton X-100-insoluble and recruits PSD-95/SAP90 into the Triton X-100-insoluble fraction in the transfected cells, suggesting that SAPAP may fix PSD-95/SAP90 to the PSD.	Octoxynol	67-79	discs large MAGUK scaffold protein 4	Homo sapiens	52-57
9756850-4	1998	SAPAP is Triton X-100-insoluble and recruits PSD-95/SAP90 into the Triton X-100-insoluble fraction in the transfected cells, suggesting that SAPAP may fix PSD-95/SAP90 to the PSD.	Octoxynol	67-79	discs large MAGUK scaffold protein 4	Homo sapiens	155-161
9756850-4	1998	SAPAP is Triton X-100-insoluble and recruits PSD-95/SAP90 into the Triton X-100-insoluble fraction in the transfected cells, suggesting that SAPAP may fix PSD-95/SAP90 to the PSD.	Octoxynol	67-79	discs large MAGUK scaffold protein 4	Homo sapiens	162-167
9756850-4	1998	SAPAP is Triton X-100-insoluble and recruits PSD-95/SAP90 into the Triton X-100-insoluble fraction in the transfected cells, suggesting that SAPAP may fix PSD-95/SAP90 to the PSD.	sapap	141-146	discs large MAGUK scaffold protein 4	Homo sapiens	45-51
9756850-4	1998	SAPAP is Triton X-100-insoluble and recruits PSD-95/SAP90 into the Triton X-100-insoluble fraction in the transfected cells, suggesting that SAPAP may fix PSD-95/SAP90 to the PSD.	sapap	141-146	discs large MAGUK scaffold protein 4	Homo sapiens	155-161
9756850-4	1998	SAPAP is Triton X-100-insoluble and recruits PSD-95/SAP90 into the Triton X-100-insoluble fraction in the transfected cells, suggesting that SAPAP may fix PSD-95/SAP90 to the PSD.	sapap	141-146	discs large MAGUK scaffold protein 4	Homo sapiens	162-167
9808460-4	1998	Similar to NMDA receptors, GluR6 clustering is mediated by the interaction of its C-terminal amino acid sequence, ETMA, with the PDZ1 domain of SAP90.	N'-ethylamidinothiocholine	114-118	discs large MAGUK scaffold protein 4	Homo sapiens	144-149
9694864-5	1998	PSD-95/SAP90 belongs to a family of membrane-associated guanylate kinases and binds N-methyl-D-aspartate receptors, potassium channels, and neuroligins through the PDZ domains and GKAP/SAPAP/DAP through the guanylate kinase (GK) domain.	sapap	185-190	discs large MAGUK scaffold protein 4	Homo sapiens	0-6
9694864-5	1998	PSD-95/SAP90 belongs to a family of membrane-associated guanylate kinases and binds N-methyl-D-aspartate receptors, potassium channels, and neuroligins through the PDZ domains and GKAP/SAPAP/DAP through the guanylate kinase (GK) domain.	sapap	185-190	discs large MAGUK scaffold protein 4	Homo sapiens	7-12
9756850-3	1998	PSD-95/SAP90 also interacts with the postsynaptic density (PSD) fraction-enriched protein, named SAPAP (also called GKAP and DAP), through the GK domain.	sapap	97-102	discs large MAGUK scaffold protein 4	Homo sapiens	7-12
9756850-3	1998	PSD-95/SAP90 also interacts with the postsynaptic density (PSD) fraction-enriched protein, named SAPAP (also called GKAP and DAP), through the GK domain.	alpha,beta-diacryloxypropionic acid	125-128	discs large MAGUK scaffold protein 4	Homo sapiens	0-6
9756850-3	1998	PSD-95/SAP90 also interacts with the postsynaptic density (PSD) fraction-enriched protein, named SAPAP (also called GKAP and DAP), through the GK domain.	alpha,beta-diacryloxypropionic acid	125-128	discs large MAGUK scaffold protein 4	Homo sapiens	7-12
9756850-4	1998	SAPAP is Triton X-100-insoluble and recruits PSD-95/SAP90 into the Triton X-100-insoluble fraction in the transfected cells, suggesting that SAPAP may fix PSD-95/SAP90 to the PSD.	sapap	0-5	discs large MAGUK scaffold protein 4	Homo sapiens	45-51
9094134-6	1997	This differs from the only known (Thr/Ser)-X-Val consensus that interacts with PDZ domains from PSD-95.	Threonine	34-37	discs large MAGUK scaffold protein 4	Homo sapiens	96-102
9430700-4	1998	Pump 4b and PSD-95 could be co-immunoprecipitated from COS-7 cells overexpressing these proteins.	carbonyl sulfide	55-58	discs large MAGUK scaffold protein 4	Homo sapiens	12-18
9459447-2	1998	The coupling of NMDA receptor-mediated calcium influx and nNOS activation is postulated to be due to a physical coupling of the receptor and the enzyme by an intermediary adaptor protein, PSD95, through a unique PDZ-PDZ domain interaction between PSD95 and nNOS.	Calcium	39-46	discs large MAGUK scaffold protein 4	Homo sapiens	188-193
9459447-2	1998	The coupling of NMDA receptor-mediated calcium influx and nNOS activation is postulated to be due to a physical coupling of the receptor and the enzyme by an intermediary adaptor protein, PSD95, through a unique PDZ-PDZ domain interaction between PSD95 and nNOS.	Calcium	39-46	discs large MAGUK scaffold protein 4	Homo sapiens	247-252
9459448-4	1998	Metabolic labeling of brain slices or cultured cells demonstrates that PSD-95 is modified by thioester-linked palmitate, a long chain fatty acid that targets proteins to cell membranes.	thioester-linked palmitate	93-119	discs large MAGUK scaffold protein 4	Homo sapiens	71-77
9459448-4	1998	Metabolic labeling of brain slices or cultured cells demonstrates that PSD-95 is modified by thioester-linked palmitate, a long chain fatty acid that targets proteins to cell membranes.	long chain fatty acid	123-144	discs large MAGUK scaffold protein 4	Homo sapiens	71-77
9459448-6	1998	Mutagenesis indicates that palmitoylation of PSD-95 occurs on conserved N-terminal cysteines 3 and 5.	Cysteine	83-92	discs large MAGUK scaffold protein 4	Homo sapiens	45-51
9148889-1	1997	An inwardly rectifying potassium channel predominantly expressed in glial cells, Kir4.1/KAB-2, has a sequence of Ser-Asn-Val in its carboxyl-terminal end, suggesting a possible interaction with an anchoring protein of the PSD-95 family.	Ser-Asn-Val	113-124	discs large MAGUK scaffold protein 4	Homo sapiens	222-228
9115257-8	1997	SAPAPs induce the enrichment of PSD-95/SAP90 to the plasma membrane in transfected cells.	sapaps	0-6	discs large MAGUK scaffold protein 4	Homo sapiens	32-38
9115257-8	1997	SAPAPs induce the enrichment of PSD-95/SAP90 to the plasma membrane in transfected cells.	sapaps	0-6	discs large MAGUK scaffold protein 4	Homo sapiens	39-44
9094134-6	1997	This differs from the only known (Thr/Ser)-X-Val consensus that interacts with PDZ domains from PSD-95.	Serine	38-41	discs large MAGUK scaffold protein 4	Homo sapiens	96-102
9094134-6	1997	This differs from the only known (Thr/Ser)-X-Val consensus that interacts with PDZ domains from PSD-95.	Valine	45-48	discs large MAGUK scaffold protein 4	Homo sapiens	96-102
7867790-3	1995	Here we show that SAP90 specifically binds GMP in the micromolar range while binding to ATP, GDP and ADP is at a much lower affinity (10-25 mM), whether or not binding is detected for other guanine and adenine nucleotides.	guanosine 5'-monophosphorothioate	43-46	discs large MAGUK scaffold protein 4	Homo sapiens	18-23
8893032-4	1996	Within the C-terminal tail of Kir 2.3, a serine residue critical for interaction with PSD-95, is also a substrate for phosphorylation by protein kinase A (PKA).	Serine	41-47	discs large MAGUK scaffold protein 4	Homo sapiens	86-92
9042661-2	1996	This results in codon 85, in exon 3 in the PDZ (PSD-95, discs-large, Z0-1) domain, being either ACG or ACT.	acceleratory factor from growth hormone	96-99	discs large MAGUK scaffold protein 4	Homo sapiens	48-54
7867790-3	1995	Here we show that SAP90 specifically binds GMP in the micromolar range while binding to ATP, GDP and ADP is at a much lower affinity (10-25 mM), whether or not binding is detected for other guanine and adenine nucleotides.	Adenosine Triphosphate	88-91	discs large MAGUK scaffold protein 4	Homo sapiens	18-23
7867790-3	1995	Here we show that SAP90 specifically binds GMP in the micromolar range while binding to ATP, GDP and ADP is at a much lower affinity (10-25 mM), whether or not binding is detected for other guanine and adenine nucleotides.	Guanosine Diphosphate	93-96	discs large MAGUK scaffold protein 4	Homo sapiens	18-23
7867790-3	1995	Here we show that SAP90 specifically binds GMP in the micromolar range while binding to ATP, GDP and ADP is at a much lower affinity (10-25 mM), whether or not binding is detected for other guanine and adenine nucleotides.	Adenosine Diphosphate	101-104	discs large MAGUK scaffold protein 4	Homo sapiens	18-23
7867790-3	1995	Here we show that SAP90 specifically binds GMP in the micromolar range while binding to ATP, GDP and ADP is at a much lower affinity (10-25 mM), whether or not binding is detected for other guanine and adenine nucleotides.	Guanine	190-197	discs large MAGUK scaffold protein 4	Homo sapiens	18-23
7867790-3	1995	Here we show that SAP90 specifically binds GMP in the micromolar range while binding to ATP, GDP and ADP is at a much lower affinity (10-25 mM), whether or not binding is detected for other guanine and adenine nucleotides.	Adenine Nucleotides	202-221	discs large MAGUK scaffold protein 4	Homo sapiens	18-23
16815335-4	2006	We find that both PSD-95 and SAP97 contain alternative N termini expressing either double cysteines that normally are palmitoylated (alpha-isoforms) or an L27 domain (beta-isoforms).	Cysteine	90-99	discs large MAGUK scaffold protein 4	Homo sapiens	18-24
33794133-0	2021	Interaction between the guanylate kinase domain of PSD-95 and the proline-rich region and microtubule binding repeats 2 and 3 of tau.	Proline	66-73	discs large MAGUK scaffold protein 4	Homo sapiens	51-57
34637756-5	2022	The theory is applied to the neuronal proteins SynGAP and PSD-95, whose complex coacervate serves as a rudimentary model for neuronal postsynaptic densities (PSDs).	coacervate	80-90	discs large MAGUK scaffold protein 4	Homo sapiens	58-64
35158223-8	2022	In addition, the levels of PSD-95, Nrxn1 and Nlgn were significantly decreased in the hippocampus of 6-OHDA-treated animals.	Oxidopamine	101-107	discs large MAGUK scaffold protein 4	Homo sapiens	27-33
34538002-6	2021	Unlike other structural domains in PSD-95, the N-terminal region (PSD-95NT) is flexible and interacts with various targets, which modulates its palmitoylation of two cysteines (C3/C5) and glutamate receptor distributions in postsynaptic densities.	Cysteine	166-175	discs large MAGUK scaffold protein 4	Homo sapiens	35-41
34538002-6	2021	Unlike other structural domains in PSD-95, the N-terminal region (PSD-95NT) is flexible and interacts with various targets, which modulates its palmitoylation of two cysteines (C3/C5) and glutamate receptor distributions in postsynaptic densities.	Glutamic Acid	188-197	discs large MAGUK scaffold protein 4	Homo sapiens	35-41
34761188-6	2021	Thus, by genetically introducing phosphoserine site-specifically and exploring the impact on phase separation, we have provided new insights into the regulation of PSD-95 by phosphorylation and the dynamics of the PSD.	Phosphoserine	33-46	discs large MAGUK scaffold protein 4	Homo sapiens	164-170
34593014-8	2021	Soluble Abeta oligomers caused reduced METTL3 expression and METTL3 knockdown exacerbated while METTL3 overexpression rescued Abeta-induced synaptic PSD95 loss in vitro.	UNII-042A8N37WH	126-131	discs large MAGUK scaffold protein 4	Homo sapiens	149-154
34790098-7	2021	Additionally, these cells in cocultures restored calcium homeostasis in neurons, redistributing calcium from somas to dendrites, accompanied by dendrite branching, higher dendritic spines and synapsin-PSD95 clustering.	Calcium	96-103	discs large MAGUK scaffold protein 4	Homo sapiens	201-206
34601865-11	2021	We found that inhibiting the activation of mTOR blocked the rapid antidepressant-like effects of MH, which also inhibited the upregulation of expressions of BDNF and PSD95.	mh	97-99	discs large MAGUK scaffold protein 4	Homo sapiens	166-171
34492814-4	2021	Pb in PM2.5 caused neurotoxicity: 1) by increasing ROS levels and thus causing apoptosis in neuronal cells and 2) by decreasing the expression of PSD95 via interfering with the calcium signaling pathway through cAMP/CREB/pCREB/BDNF/PSD95 pathway and reducing the synapse length by 50%.	Lead	0-2	discs large MAGUK scaffold protein 4	Homo sapiens	146-151
34492814-4	2021	Pb in PM2.5 caused neurotoxicity: 1) by increasing ROS levels and thus causing apoptosis in neuronal cells and 2) by decreasing the expression of PSD95 via interfering with the calcium signaling pathway through cAMP/CREB/pCREB/BDNF/PSD95 pathway and reducing the synapse length by 50%.	Lead	0-2	discs large MAGUK scaffold protein 4	Homo sapiens	232-237
34492814-4	2021	Pb in PM2.5 caused neurotoxicity: 1) by increasing ROS levels and thus causing apoptosis in neuronal cells and 2) by decreasing the expression of PSD95 via interfering with the calcium signaling pathway through cAMP/CREB/pCREB/BDNF/PSD95 pathway and reducing the synapse length by 50%.	Calcium	177-184	discs large MAGUK scaffold protein 4	Homo sapiens	146-151
34492814-4	2021	Pb in PM2.5 caused neurotoxicity: 1) by increasing ROS levels and thus causing apoptosis in neuronal cells and 2) by decreasing the expression of PSD95 via interfering with the calcium signaling pathway through cAMP/CREB/pCREB/BDNF/PSD95 pathway and reducing the synapse length by 50%.	Calcium	177-184	discs large MAGUK scaffold protein 4	Homo sapiens	232-237
34492814-4	2021	Pb in PM2.5 caused neurotoxicity: 1) by increasing ROS levels and thus causing apoptosis in neuronal cells and 2) by decreasing the expression of PSD95 via interfering with the calcium signaling pathway through cAMP/CREB/pCREB/BDNF/PSD95 pathway and reducing the synapse length by 50%.	Cyclic AMP	211-215	discs large MAGUK scaffold protein 4	Homo sapiens	146-151
34492814-4	2021	Pb in PM2.5 caused neurotoxicity: 1) by increasing ROS levels and thus causing apoptosis in neuronal cells and 2) by decreasing the expression of PSD95 via interfering with the calcium signaling pathway through cAMP/CREB/pCREB/BDNF/PSD95 pathway and reducing the synapse length by 50%.	Cyclic AMP	211-215	discs large MAGUK scaffold protein 4	Homo sapiens	232-237
35566161-1	2022	PSD95-PDZ3, the third PDZ domain of the post-synaptic density-95 protein (MW 11 kDa), undergoes a peculiar three-state thermal denaturation (N   In   D) and is amyloidogenic.	Adenosine Monophosphate	148-151	discs large MAGUK scaffold protein 4	Homo sapiens	0-5
35433833-4	2022	First, the interactions between PSD95 GK and their reported phosphorylated and unphosphorylated peptides were explored by molecular dynamics simulations.	Peptides	96-104	discs large MAGUK scaffold protein 4	Homo sapiens	32-37
35433833-5	2022	Besides the hydrogen bonding interactions mediated by the phospho-serine (p-Ser) or corresponding phosphomimic residue Asp/Glu, the hydrophobic interactions from the other amino acids also contribute to the PSD95 GK/SAPAP interaction.	Serine	66-72	discs large MAGUK scaffold protein 4	Homo sapiens	207-212
35433833-5	2022	Besides the hydrogen bonding interactions mediated by the phospho-serine (p-Ser) or corresponding phosphomimic residue Asp/Glu, the hydrophobic interactions from the other amino acids also contribute to the PSD95 GK/SAPAP interaction.	Phosphoserine	74-79	discs large MAGUK scaffold protein 4	Homo sapiens	207-212
35433833-5	2022	Besides the hydrogen bonding interactions mediated by the phospho-serine (p-Ser) or corresponding phosphomimic residue Asp/Glu, the hydrophobic interactions from the other amino acids also contribute to the PSD95 GK/SAPAP interaction.	sapap	216-221	discs large MAGUK scaffold protein 4	Homo sapiens	207-212
35433833-11	2022	Among them, F10W was the most potent inhibitor (K i = 0.75 +- 0.25 muM), suggesting that enhancement of the hydrophobic interactions is an important strategy for the design of new inhibitory peptides targeting PSD95 GK.	f10w	12-16	discs large MAGUK scaffold protein 4	Homo sapiens	210-215
35171623-5	2022	We demonstrate here that the compatible osmolyte trimethylamine-N-oxide (TMAO) as well as macromolecular crowding agents at moderate concentrations can mitigate the deleterious effect of pressure on SynGAP/PSD-95 droplet stability, extending stable LLPS up to almost a kbar level.	trimethyloxamine	49-71	discs large MAGUK scaffold protein 4	Homo sapiens	206-212
35171623-5	2022	We demonstrate here that the compatible osmolyte trimethylamine-N-oxide (TMAO) as well as macromolecular crowding agents at moderate concentrations can mitigate the deleterious effect of pressure on SynGAP/PSD-95 droplet stability, extending stable LLPS up to almost a kbar level.	trimethyloxamine	73-77	discs large MAGUK scaffold protein 4	Homo sapiens	206-212
34776441-8	2022	RESULTS: Activation of astrocytic NMDARs can significantly mitigate Abeta142-induced loss of PSD-95 and synaptophysin through increasing NGF release.	abeta142	68-76	discs large MAGUK scaffold protein 4	Homo sapiens	93-99
35197857-5	2022	Emodin ameliorated zinc-induced altered expression of levels of phosphorylated ERK1/2 (not total ETK1/2) and synaptic proteins (presynaptic SNAP 25, synaptophysin and postsynaptic PSD95) in SH-SY5Y cells.	Emodin	0-6	discs large MAGUK scaffold protein 4	Homo sapiens	180-185
35013841-3	2022	Although recent studies indicate that the PDZ-containing proteins comprising PSD-95 family co-localize with nicotinic acetylcholine receptors and mediate downstream signaling in the neurons, the mechanisms by which alpha7nAChRs are regulated remain unclear.	Acetylcholine	118-131	discs large MAGUK scaffold protein 4	Homo sapiens	77-83
33688611-2	2021	While it is known that removal of postsynaptic density protein-95 (PSD-95) from the postsynaptic density decreases synaptic N-methyl-D-aspartate (NMDA) receptors and that cypin overexpression protects neurons from NMDA-induced toxicity, little is known about cypin"s role in AMPA receptor clustering and function.	N-Methylaspartate	124-144	discs large MAGUK scaffold protein 4	Homo sapiens	67-73
33897893-9	2021	Results: (+)-Borneol selectively potentiated alpha2- and alpha3-containing GABAARs and prevented the disinhibition of laminae I excitatory neurons in the SDH and analgesic tolerance caused by chronic use of ZL006, a nNOS-PSD-95 blocker.	isoborneol	13-20	discs large MAGUK scaffold protein 4	Homo sapiens	221-227
33897893-10	2021	A dual-target compound ZL006-05 produced by linking ZL006 and (+)-borneol through an ester bond blocked nNOS-PSD-95 interaction and potentiated alpha2-containing GABAAR selectively.	4-((3,5-dichloro-2-hydroxybenzyl)amino)-2-hydroxybenzoic acid	23-28	discs large MAGUK scaffold protein 4	Homo sapiens	109-115
33897893-10	2021	A dual-target compound ZL006-05 produced by linking ZL006 and (+)-borneol through an ester bond blocked nNOS-PSD-95 interaction and potentiated alpha2-containing GABAAR selectively.	4-((3,5-dichloro-2-hydroxybenzyl)amino)-2-hydroxybenzoic acid	52-57	discs large MAGUK scaffold protein 4	Homo sapiens	109-115
33897893-10	2021	A dual-target compound ZL006-05 produced by linking ZL006 and (+)-borneol through an ester bond blocked nNOS-PSD-95 interaction and potentiated alpha2-containing GABAAR selectively.	Esters	85-90	discs large MAGUK scaffold protein 4	Homo sapiens	109-115
32683713-6	2021	In particular, modulation of glutamate receptors differentially impacted SYP and PSD-95, and antagonists of a single receptor subtype had distinct effects when either isolated or combined.	Glutamic Acid	29-38	discs large MAGUK scaffold protein 4	Homo sapiens	81-87
33688611-2	2021	While it is known that removal of postsynaptic density protein-95 (PSD-95) from the postsynaptic density decreases synaptic N-methyl-D-aspartate (NMDA) receptors and that cypin overexpression protects neurons from NMDA-induced toxicity, little is known about cypin"s role in AMPA receptor clustering and function.	N-Methylaspartate	146-150	discs large MAGUK scaffold protein 4	Homo sapiens	34-65
33688611-2	2021	While it is known that removal of postsynaptic density protein-95 (PSD-95) from the postsynaptic density decreases synaptic N-methyl-D-aspartate (NMDA) receptors and that cypin overexpression protects neurons from NMDA-induced toxicity, little is known about cypin"s role in AMPA receptor clustering and function.	N-Methylaspartate	146-150	discs large MAGUK scaffold protein 4	Homo sapiens	67-73
33688611-2	2021	While it is known that removal of postsynaptic density protein-95 (PSD-95) from the postsynaptic density decreases synaptic N-methyl-D-aspartate (NMDA) receptors and that cypin overexpression protects neurons from NMDA-induced toxicity, little is known about cypin"s role in AMPA receptor clustering and function.	N-Methylaspartate	214-218	discs large MAGUK scaffold protein 4	Homo sapiens	67-73
33165687-8	2022	Among the 17 identified hub-bottlenecks in the ACN, PSD-95 was recognized as an important protein through analyzing the module and motif interactions.	acn	47-50	discs large MAGUK scaffold protein 4	Homo sapiens	52-58
33325958-5	2021	The superiority of DHA-PL also correlates with the specific elevation of synapse-associated proteins, including BDNF, DCX, GAP-43, Syn, and PSD95, except to higher brain DHA accretion.	dha-pl	19-25	discs large MAGUK scaffold protein 4	Homo sapiens	140-145
32841551-13	2020	And we also found that DCA treatment caused a differential modulation of proteins (BDNF, cAMP-response element-binding protein1 (CREB1), p-CREB1, postsynaptic density-95 (PSD-95), synapsin I, p-synapsin I), and mRNA (BDNF, PSD-95).	Dichloroacetic Acid	23-26	discs large MAGUK scaffold protein 4	Homo sapiens	146-169
32841551-13	2020	And we also found that DCA treatment caused a differential modulation of proteins (BDNF, cAMP-response element-binding protein1 (CREB1), p-CREB1, postsynaptic density-95 (PSD-95), synapsin I, p-synapsin I), and mRNA (BDNF, PSD-95).	Dichloroacetic Acid	23-26	discs large MAGUK scaffold protein 4	Homo sapiens	171-177
32841551-13	2020	And we also found that DCA treatment caused a differential modulation of proteins (BDNF, cAMP-response element-binding protein1 (CREB1), p-CREB1, postsynaptic density-95 (PSD-95), synapsin I, p-synapsin I), and mRNA (BDNF, PSD-95).	Dichloroacetic Acid	23-26	discs large MAGUK scaffold protein 4	Homo sapiens	223-229
32416136-8	2020	Besides, DCMQA down-regulated GluN2B-containing NMDA receptors (NMDARs) and up-regulated GluN2A-containing NMDARs, promoted the disruption of nNOS and PSD95 as well as activation of CaMK II-alpha.	dcmqa	9-14	discs large MAGUK scaffold protein 4	Homo sapiens	151-156
32416136-11	2020	In addition, the underlying mechanisms of DCMQA-mediated neuroprotection are associated with modulating NMDARs and disruption of nNOS-PSD95 as well as the activation of CaMK II-alpha.	dcmqa	42-47	discs large MAGUK scaffold protein 4	Homo sapiens	134-139