PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
30282042-0	2018	Removal of hERG potassium channel affinity through introduction of an oxygen atom: Molecular insights from structure-activity relationships of strychnine and its analogs.	Oxygen	70-76	ETS transcription factor ERG	Homo sapiens	11-15	
30282042-8	2018	Compared to their parent compounds, only an oxygen atom was introduced in the nitrogen oxidative isoforms to compensate for the N+ - charge, suggesting that the protonated nitrogen is the key group for strychnine and brucine binding to hERG channel.	Oxygen	44-50	ETS transcription factor ERG	Homo sapiens	236-240	
30282042-12	2018	This study suggests that introduction of an oxygen to compensate for the N+ - charge could be a useful strategy for reducing hERG potency and increasing the safety margin of alkaloid-type compounds in drug development.	Oxygen	44-50	ETS transcription factor ERG	Homo sapiens	125-129