PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
30347329-5	2019	Molecular modeling suggested a mode of binding interaction at the JNK catalytic site and that the selected oxime derivatives were potentially competitive JNK inhibitors.	Oximes	107-112	mitogen-activated protein kinase 8	Homo sapiens	66-69	
30347329-5	2019	Molecular modeling suggested a mode of binding interaction at the JNK catalytic site and that the selected oxime derivatives were potentially competitive JNK inhibitors.	Oximes	107-112	mitogen-activated protein kinase 8	Homo sapiens	154-157	
30347329-7	2019	Thus, oximes with indenoquinoxaline and tryptanthrin nuclei can serve as specific small-molecule modulators for mechanistic studies of JNK, as well as potential leads for the development of anti-inflammatory drugs.	Oximes	6-12	mitogen-activated protein kinase 8	Homo sapiens	135-138	
34577159-3	2021	We synthesized 13 derivatives of our reported JNK inhibitor 11H-indeno(1,2-b)quinoxalin-11-one oxime and evaluated their binding to the three JNK isoforms and their biological effects.	Oximes	95-100	mitogen-activated protein kinase 8	Homo sapiens	46-49	
34577159-3	2021	We synthesized 13 derivatives of our reported JNK inhibitor 11H-indeno(1,2-b)quinoxalin-11-one oxime and evaluated their binding to the three JNK isoforms and their biological effects.	Oximes	95-100	mitogen-activated protein kinase 8	Homo sapiens	142-145