PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
11425486-3	2001	Depending on their concentrations, GO and MGO promoted phosphorylations of ERK1 and ERK2, which were blocked by the protein-tyrosine kinase (PTK) inhibitors herbimycin A and staurosporine, thereby being PTK-dependent.	Glyoxal	35-37	mitogen-activated protein kinase 3	Homo sapiens	75-79	
20397192-0	2010	Carbonyl compounds methylglyoxal and glyoxal affect interleukin-8 secretion in intestinal cells by superoxide anion generation and activation of MAPK p38.	Glyoxal	25-32	mitogen-activated protein kinase 3	Homo sapiens	145-149	
11425486-9	2001	These results demonstrated that GO and MGO triggered two distinct signal cascades, one for PTK-dependent control of ERK and another for PTK-independent redox-linked activation of JNK/p38 MAPK and caspases in HUVECs, depending on the structure of the carbon skeleton of the chemicals.	Glyoxal	32-34	mitogen-activated protein kinase 3	Homo sapiens	187-191	
11425486-4	2001	GO and MGO also induced phosphorylations of JNK, p38 MAPK, and c-Jun, either PTK-dependently (GO) or -independently (MGO).	Glyoxal	0-2	mitogen-activated protein kinase 3	Homo sapiens	53-57	
32746708-11	2021	CONCLUSIONS: GO and MGO induced pro-inflammatory cytokines and MUC5AC/5B expression via ERK1/2, p38 MAPK, and NF-kappaB in human nasal epithelial cells.	Glyoxal	13-15	mitogen-activated protein kinase 3	Homo sapiens	88-94