data_final.csv

"oligomers","p2ry12","The extracellular Tau oligomers were found to interact with microglial purinergic receptor P2Y12 which then led to microglial migration, activation and phagocytosis via various remodeled actin structure.","microglia","40973402","oligomers-p2ry12-40973402"
"oligomers","p2ry12","The extracellular Tau oligomers were found to interact with microglial purinergic receptor P2Y12 which then led to microglial migration, activation and phagocytosis via various remodeled actin structure.","prime_immune_cells","40973402","oligomers-p2ry12-40973402"
"oligomers","p2ry12","The extracellular Tau oligomers were found to interact with microglial purinergic receptor P2Y12 which then led to microglial migration, activation and phagocytosis via various remodeled actin structure.","senescent_microglia","40973402","oligomers-p2ry12-40973402"
"mapt","protein","In its physiological state, Tau interacts with various molecules and proteins.","neurons","40973401","mapt-protein-40973401"
"gas","ctnnb1","Autodock Vina simulation demonstrated that GAS binds to β-catenin with a binding energy of less than -5 kcal/mol.","aβ25-35-treated_ht22_cells","40915373","gas-ctnnb1-40915373"
"gas","ctnnb1","Autodock Vina simulation demonstrated that GAS binds to β-catenin with a binding energy of less than -5 kcal/mol.","aβ25-35-challenged_ht22_cells","40915373","gas-ctnnb1-40915373"
"gas","ctnnb1","Autodock Vina simulation demonstrated that GAS binds to β-catenin with a binding energy of less than -5 kcal/mol.","ht22_cells","40915373","gas-ctnnb1-40915373"
"gnb5","bace1","Mechanistically, we demonstrated that Gnb5 interacts with BACE1, modulating its expression and potentially influencing Aβ generation.","excitatory_neurons","40587559","gnb5-bace1-40587559"
"clec7a","microglial-cells","This review highlights how Dectin-1 interacts with microglial cells, as well as the implications of these interactions in inflammatory, neurodegenerative, and psychiatric processes.","microglial_cells","40758965","clec7a-microglial-cells-40758965"
"ara","mek","Mechanistic investigations reveal that ARA directly binds to Raf, MEK, and ERK proteins and activates autophagy in a Raf/MEK/ERK-dependent manner.","aralia_elata","40742404","ara-mek-40742404"
"app","extracellular","We show that APP binds to the extracellular domain of NCAM2.","transfected_cho_cells","40721030","app-extracellular-40721030"
"app","extracellular","We show that APP binds to the extracellular domain of NCAM2.","neurons","40721030","app-extracellular-40721030"
"dpysl2","adenine-nucleotide-translocase","We found that CRMP2 binds to the adenine nucleotide translocase (ANT) in a phosphorylation-dependent manner.","crmp2","40358171","dpysl2-adenine-nucleotide-translocase-40358171"
"dpysl2","adenine-nucleotide-translocase","We found that CRMP2 binds to the adenine nucleotide translocase (ANT) in a phosphorylation-dependent manner.","cultured_cortical_neurons","40358171","dpysl2-adenine-nucleotide-translocase-40358171"
"dpysl2","adenine-nucleotide-translocase","We found that CRMP2 binds to the adenine nucleotide translocase (ANT) in a phosphorylation-dependent manner.","cultured_neurons","40358171","dpysl2-adenine-nucleotide-translocase-40358171"
"dpysl2","adenine-nucleotide-translocase","We found that CRMP2 binds to the adenine nucleotide translocase (ANT) in a phosphorylation-dependent manner.","neurons","40358171","dpysl2-adenine-nucleotide-translocase-40358171"
"gprin1","htr6","Notably, the G protein-regulated inducer of neurite outgrowth 1 (GPRIN1) interacts with 5-HT6Rs independently of agonists, enhancing receptor activity.","serotonergic_neurons","40347153","gprin1-htr6-40347153"
"acetylcholine","receptors","Acetylcholine interacts with cortical muscarinic and nicotinic receptors, each with varied regional distribution, to produce its effects.","ch3-dbh","40340056","acetylcholine-receptors-40340056"
"acetylcholine","receptors","Acetylcholine interacts with cortical muscarinic and nicotinic receptors, each with varied regional distribution, to produce its effects.","ch4","40340056","acetylcholine-receptors-40340056"
"acetylcholine","receptors","Acetylcholine interacts with cortical muscarinic and nicotinic receptors, each with varied regional distribution, to produce its effects.","ch4-nbm","40340056","acetylcholine-receptors-40340056"
"acetylcholine","receptors","Acetylcholine interacts with cortical muscarinic and nicotinic receptors, each with varied regional distribution, to produce its effects.","ch2-dbv_neurons","40340056","acetylcholine-receptors-40340056"
"acetylcholine","receptors","Acetylcholine interacts with cortical muscarinic and nicotinic receptors, each with varied regional distribution, to produce its effects.","ch3-dbh_neurons","40340056","acetylcholine-receptors-40340056"
"acetylcholine","receptors","Acetylcholine interacts with cortical muscarinic and nicotinic receptors, each with varied regional distribution, to produce its effects.","olfactory_bulb","40340056","acetylcholine-receptors-40340056"
"acetylcholine","receptors","Acetylcholine interacts with cortical muscarinic and nicotinic receptors, each with varied regional distribution, to produce its effects.","ch4-nbm_neurons","40340056","acetylcholine-receptors-40340056"
"cd2ap","csf1r","Moreover, we reveal that CD2AP interacts with colony stimulating factor 1 receptor (CSF1R) and regulates CSF1R cell surface levels, which may further affect C1q expression.","peripheral_immune_cells","39695808","cd2ap-csf1r-39695808"
"cd2ap","csf1r","Moreover, we reveal that CD2AP interacts with colony stimulating factor 1 receptor (CSF1R) and regulates CSF1R cell surface levels, which may further affect C1q expression.","microglia","39695808","cd2ap-csf1r-39695808"
"cd2ap","csf1r","Moreover, we reveal that CD2AP interacts with colony stimulating factor 1 receptor (CSF1R) and regulates CSF1R cell surface levels, which may further affect C1q expression.","cultured_primary_cells","39695808","cd2ap-csf1r-39695808"
"cd2ap","csf1r","Moreover, we reveal that CD2AP interacts with colony stimulating factor 1 receptor (CSF1R) and regulates CSF1R cell surface levels, which may further affect C1q expression.","disease-associated_microglia","39695808","cd2ap-csf1r-39695808"
"cd2ap","csf1r","Moreover, we reveal that CD2AP interacts with colony stimulating factor 1 receptor (CSF1R) and regulates CSF1R cell surface levels, which may further affect C1q expression.","cd2ap-deficient_microglia","39695808","cd2ap-csf1r-39695808"
"cd2ap","csf1r","Moreover, we reveal that CD2AP interacts with colony stimulating factor 1 receptor (CSF1R) and regulates CSF1R cell surface levels, which may further affect C1q expression.","brain_cells","39695808","cd2ap-csf1r-39695808"
"elavl4","msi2","In the current study, we found that HuD interacts with Msi2 transcript and positively regulates it in the mouse neuroblastoma (N2a) cells.","human_neuroblastoma_cell_line","39680531","elavl4-msi2-39680531"
"elavl4","msi2","In the current study, we found that HuD interacts with Msi2 transcript and positively regulates it in the mouse neuroblastoma (N2a) cells.","myenteric_neurons","39680531","elavl4-msi2-39680531"
"elavl4","msi2","In the current study, we found that HuD interacts with Msi2 transcript and positively regulates it in the mouse neuroblastoma (N2a) cells.","mouse_neuroblastoma","39680531","elavl4-msi2-39680531"
"elavl4","msi2","In the current study, we found that HuD interacts with Msi2 transcript and positively regulates it in the mouse neuroblastoma (N2a) cells.","n2a_cells","39680531","elavl4-msi2-39680531"
"none, dimers","dimers","Mechanistically, ADRA1 interacts with CXCR4 to form heterodimers, triggering cytoplasmic Ca2⁺ overload and subsequent STING/NF-κB/NLRP3 pathway activation.","aβ42_oligomer-stimulated_sh-sy5y_cells","40676669","none, dimers-dimers-40676669"
"none, dimers","dimers","Mechanistically, ADRA1 interacts with CXCR4 to form heterodimers, triggering cytoplasmic Ca2⁺ overload and subsequent STING/NF-κB/NLRP3 pathway activation.","primary_murine_neurons","40676669","none, dimers-dimers-40676669"
"none, dimers","dimers","Mechanistically, ADRA1 interacts with CXCR4 to form heterodimers, triggering cytoplasmic Ca2⁺ overload and subsequent STING/NF-κB/NLRP3 pathway activation.","sh-sy5y_cells","40676669","none, dimers-dimers-40676669"
"trimer","dimer","sTRAIL monomer binds dimeric S100P strictly in the presence of Ca2+, while sTRAIL trimer interacts with S100P dimer regardless of Ca2+.","human_fibrosarcoma_ht-1080_cells","40318722","trimer-dimer-40318722"
"yod1","myh9","Mechanistically, YOD1 binds to MYH9 and maintains its stability by removing the K48 ubiquitin chain from MYH9, thereby mediating the microglia polarization signaling pathway to mediate microglia homeostasis.","microglia","40041897","yod1-myh9-40041897"