PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
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	
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	
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	
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	
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	
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	
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	
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	
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	
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