PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
216760-2	1978	In some preparations vanadium was found to be the most potent inhibitor of Na+  + K+ATPase activity so far reported.	Vanadium	21-29	ATPase Na+/K+ transporting subunit beta 1	Homo sapiens	84-90	
216760-3	1978	Concentrations of vanadium causing 50 percent inhibition of Na+ + K+ATPase activity ranged from 6 x 10(-8) to 5 x 10(-7) M in microsomal fractions and from 2 x 10(-7) to 1 x 10(-6) M in tissue homogenates.	Vanadium	18-26	ATPase Na+/K+ transporting subunit beta 1	Homo sapiens	68-74	
216760-6	1978	Mg2+ ATPase, which contaminated the enzyme preparations to a variable degree, was 1,000-10,000 times more resistant to vanadium than was Na+ + K+ATPase.	Vanadium	119-127	ATPase Na+/K+ transporting subunit beta 1	Homo sapiens	5-11	
216760-11	1978	This could mean that vanadium inhibits the Na+ + K+ATPase at the site activated by Na+, and that ATP protects the enzyme either by binding vanadium or by competing for a mutual receptor on the enzyme.	Vanadium	21-29	ATPase Na+/K+ transporting subunit beta 1	Homo sapiens	51-57