PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
34906039-4	2021	This component with characteristic time tau   40 micros and relative amplitude of ~10% of the total Deltapsi was attributed to the vectorial electron transfer from QA- to cyt c3+ serving as an external acceptor.	Quinolinic Acid	164-167	microtubule associated protein tau	Homo sapiens	40-43	
31779690-9	2019	The tryptophan catabolites, kynurenic acid and quinolinic acid, showed significantly higher concentrations in CSF of AD patients, which, together with other tryptophan pathway intermediates, were correlated with either CSF Amyloidbeta1-42, or tau and phosphorylated Tau-181.	Quinolinic Acid	47-62	microtubule associated protein tau	Homo sapiens	243-246	
31678113-0	2020	Pyridine-2,3-dicarboxylate, quinolinic acid, induces 1N4R Tau amyloid aggregation in vitro: Another evidence for the detrimental effect of the inescapable endogenous neurotoxin.	Quinolinic Acid	0-26	microtubule associated protein tau	Homo sapiens	58-61	
31678113-0	2020	Pyridine-2,3-dicarboxylate, quinolinic acid, induces 1N4R Tau amyloid aggregation in vitro: Another evidence for the detrimental effect of the inescapable endogenous neurotoxin.	Quinolinic Acid	28-43	microtubule associated protein tau	Homo sapiens	58-61	
31678113-5	2020	Herein we report accelerated amyloid oligomerization of 1N4R Tau under the effect of QA, in vitro, then the molecular structure, morphology and toxicity of the protein aggregate were documented by using various theoretical/experimental approaches.	Quinolinic Acid	85-87	microtubule associated protein tau	Homo sapiens	61-64	
31678113-6	2020	The possible mechanism of action of QA-induced Tau oligomerization has also been explored.	Quinolinic Acid	36-38	microtubule associated protein tau	Homo sapiens	47-50	
31779690-9	2019	The tryptophan catabolites, kynurenic acid and quinolinic acid, showed significantly higher concentrations in CSF of AD patients, which, together with other tryptophan pathway intermediates, were correlated with either CSF Amyloidbeta1-42, or tau and phosphorylated Tau-181.	Quinolinic Acid	47-62	microtubule associated protein tau	Homo sapiens	266-269	
19623258-0	2009	The excitotoxin quinolinic acid induces tau phosphorylation in human neurons.	Quinolinic Acid	16-31	microtubule associated protein tau	Homo sapiens	40-43	
19623258-15	2009	Altogether these results indicate a likely role of QA in the AD pathology through promotion of tau phosphorylation.	Quinolinic Acid	51-53	microtubule associated protein tau	Homo sapiens	95-98	
19623258-3	2009	We hypothesized that QA in pathophysiological concentrations affects tau phosphorylation.	Quinolinic Acid	21-23	microtubule associated protein tau	Homo sapiens	69-72	
19623258-5	2009	We then investigated in vitro the effects of QA at various pathophysiological concentrations on tau phosphorylation in primary cultures of human neurons.	Quinolinic Acid	45-47	microtubule associated protein tau	Homo sapiens	96-99	
19623258-6	2009	Using western blot, we found that QA treatment increased the phosphorylation of tau at serine 199/202, threonine 231 and serine 396/404 in a dose dependent manner.	Quinolinic Acid	34-36	microtubule associated protein tau	Homo sapiens	80-83