PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
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	
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.	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	
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	
9756850-4	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	
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	
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	
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	
29281827-4	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