PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
9459604-8	1998	The ATPase activity of the enzyme is inhibited by vanadate (IC50 = 119 microM), N-ethylmaleimide, N,N-dicyclohexylcarbodiimide, and inhibitors of eukaryotic sarco(endo)plasmic reticulum Ca2+-ATPases; however, it is stimulated by thapsigargin.	Ethylmaleimide	80-96	ATPase	Escherichia coli	4-10	
1386722-5	1992	N-Ethylmaleimide (NEM) inactivated alpha C373 F1 steady-state ATPase potently but had no effect on unisite ATPase.	Ethylmaleimide	0-16	ATPase	Escherichia coli	62-68	
8515869-6	1993	This ATPase activity is not affected by known inhibitors of the vesicular V- and P-type ATPases such as vanadate and N-ethylmaleimide.	Ethylmaleimide	117-133	ATPase	Escherichia coli	5-11	
8428942-4	1993	The ATPase activity of NSF is sensitive to N-ethylmaleimide and influenced by monoclonal antibodies against recombinant NSF.	Ethylmaleimide	43-59	ATPase	Escherichia coli	4-10	
1386722-5	1992	N-Ethylmaleimide (NEM) inactivated alpha C373 F1 steady-state ATPase potently but had no effect on unisite ATPase.	Ethylmaleimide	18-21	ATPase	Escherichia coli	62-68	
2644253-8	1989	N-Ethylmaleimide, which inactivates the ATPase, did not inhibit peptide hydrolysis.	Ethylmaleimide	0-16	ATPase	Escherichia coli	40-46	
2884218-9	1987	The finding that N-ethylmaleimide inhibition of ATPase activity was protectable by nucleotides is consistent with the idea of sulfhydryl groups in the ATP-binding site.	Ethylmaleimide	17-33	ATPase	Escherichia coli	48-54