PMID-sentid	Pub_year	Sent_text	compound_name	comp_offset	prot_official_name	organism	prot_offset
9681926-7	1998	Inhibitor constants (Ki) obtained for L-HCSA, L-CSA, L-CA and L-SOS in [3H]glutamate receptor binding studies with mGluR1alpha cells indicated that L-HCSA, L-CSA, L-CA and L-SOS can bind specifically to mGluR1 with L-HCSA showing the highest affinity.	L-Cysteinesulfinic acid	46-51	glutamate metabotropic receptor 1	Homo sapiens	115-121
18656538-6	2008	Consistent with the cell culture model results, we observed that the degree and rate of drug transfer into human blood was more pronounced for CsA-PG than for L-CsA with the area under the curve (AUC) of CsA-PG being about 1.6 times higher than for the L-CsA formulation.	L-Cysteinesulfinic acid	159-164	ERCC excision repair 8, CSA ubiquitin ligase complex subunit	Homo sapiens	204-210
18656538-6	2008	Consistent with the cell culture model results, we observed that the degree and rate of drug transfer into human blood was more pronounced for CsA-PG than for L-CsA with the area under the curve (AUC) of CsA-PG being about 1.6 times higher than for the L-CsA formulation.	L-Cysteinesulfinic acid	253-258	ERCC excision repair 8, CSA ubiquitin ligase complex subunit	Homo sapiens	143-149
18656538-6	2008	Consistent with the cell culture model results, we observed that the degree and rate of drug transfer into human blood was more pronounced for CsA-PG than for L-CsA with the area under the curve (AUC) of CsA-PG being about 1.6 times higher than for the L-CsA formulation.	L-Cysteinesulfinic acid	253-258	ERCC excision repair 8, CSA ubiquitin ligase complex subunit	Homo sapiens	204-210
12649361-3	2003	We discovered that L-homocysteine sulfinic acid (L-HCSA), L-homocysteic acid, L-cysteine sulfinic acid, and L-cysteic acid are potent and effective agonists at several rat metabotropic glutamate receptors (mGluRs).	L-Cysteinesulfinic acid	78-102	glutamyl-tRNA synthetase 2, mitochondrial	Mus musculus	206-212
10561426-11	1999	Taken together, these results support the glutamate hypothesis of DSI and argue that L-Glu or L-CSA are potential retrograde messengers in CA1.	L-Cysteinesulfinic acid	94-99	carbonic anhydrase 1	Homo sapiens	139-142
9681926-7	1998	Inhibitor constants (Ki) obtained for L-HCSA, L-CSA, L-CA and L-SOS in [3H]glutamate receptor binding studies with mGluR1alpha cells indicated that L-HCSA, L-CSA, L-CA and L-SOS can bind specifically to mGluR1 with L-HCSA showing the highest affinity.	L-Cysteinesulfinic acid	156-161	protein tyrosine phosphatase receptor type C	Homo sapiens	53-57
9681926-7	1998	Inhibitor constants (Ki) obtained for L-HCSA, L-CSA, L-CA and L-SOS in [3H]glutamate receptor binding studies with mGluR1alpha cells indicated that L-HCSA, L-CSA, L-CA and L-SOS can bind specifically to mGluR1 with L-HCSA showing the highest affinity.	L-Cysteinesulfinic acid	156-161	glutamate metabotropic receptor 1	Homo sapiens	115-121
34068845-6	2021	We determined the kinetic constants using L-cysteine sulfinic acid as substrate, and also showed that human cysteine sulfinic acid decarboxylase is capable to catalyze the decarboxylation-besides its natural substrates L-cysteine sulfinic acid and L-cysteic acid-of L-aspartate and L-glutamate, although with much lower efficiency.	L-Cysteinesulfinic acid	42-66	cysteine sulfinic acid decarboxylase	Homo sapiens	108-144
7739795-3	1995	Like 1S,3R-ACPD, L-CSA induced a cAMP response that was inhibited by the adenosine receptor antagonist, 8-para-sulfyltheophylline, and by adenosine deaminase.	L-Cysteinesulfinic acid	17-22	adenosine deaminase	Rattus norvegicus	138-157
34068845-6	2021	We determined the kinetic constants using L-cysteine sulfinic acid as substrate, and also showed that human cysteine sulfinic acid decarboxylase is capable to catalyze the decarboxylation-besides its natural substrates L-cysteine sulfinic acid and L-cysteic acid-of L-aspartate and L-glutamate, although with much lower efficiency.	L-Cysteinesulfinic acid	219-243	cysteine sulfinic acid decarboxylase	Homo sapiens	108-144
25444857-1	2015	Cysteine dioxygenase (CDO) is a non-heme mononuclear iron enzyme that catalyzes the oxygen-dependent oxidation of L-cysteine (Cys) to produce L-cysteine sulfinic acid (CSA).	L-Cysteinesulfinic acid	142-166	cysteine dioxygenase 1, cytosolic	Mus musculus	0-20
25444857-1	2015	Cysteine dioxygenase (CDO) is a non-heme mononuclear iron enzyme that catalyzes the oxygen-dependent oxidation of L-cysteine (Cys) to produce L-cysteine sulfinic acid (CSA).	L-Cysteinesulfinic acid	142-166	cysteine dioxygenase 1, cytosolic	Mus musculus	22-25