PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
10920267-5	2000	(4) Vanadate at the concentrations that did not inhibit the GTPase activities of EF-Tu and EF-G, depressed the poly(U)-dependent polyphe synthesis, suggesting that ribosomal ATPase (GTPase) participates in peptide elongation by inducing positive conformational changes of ribosomes required for the attachment of elongational components.	Vanadates	4-12	ATPase	Escherichia coli	174-180	
15781971-6	2005	ATPase activity of wild-type and mutant torsinA proteins was influenced by factors that varied with cell stress, such as temperature, pH, and ionic strength, and was inhibited by sodium vanadate.	Vanadates	179-194	ATPase	Escherichia coli	0-6	
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.	Vanadates	50-58	ATPase	Escherichia coli	4-10	
12734587-7	1998	ATPase activity and the formation of phosphointermediates verify the full function of the enzyme: the ATPase is inhibited by vanadate (IC(50)= 119 &mgr;M) and the formation of phosphorylated enzyme intermediates shown by acidic PAGE depends on calcium, indicating that the Synechocystis P-ATPase functions as a calcium pump.	Vanadates	125-133	ATPase	Escherichia coli	0-6	
12734587-7	1998	ATPase activity and the formation of phosphointermediates verify the full function of the enzyme: the ATPase is inhibited by vanadate (IC(50)= 119 &mgr;M) and the formation of phosphorylated enzyme intermediates shown by acidic PAGE depends on calcium, indicating that the Synechocystis P-ATPase functions as a calcium pump.	Vanadates	125-133	ATPase	Escherichia coli	102-108	
12734587-7	1998	ATPase activity and the formation of phosphointermediates verify the full function of the enzyme: the ATPase is inhibited by vanadate (IC(50)= 119 &mgr;M) and the formation of phosphorylated enzyme intermediates shown by acidic PAGE depends on calcium, indicating that the Synechocystis P-ATPase functions as a calcium pump.	Vanadates	125-133	ATPase	Escherichia coli	102-108	
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.	Vanadates	104-112	ATPase	Escherichia coli	5-11	
1400242-2	1992	A vanadate-sensitive, K(+)-stimulated and Mg(2+)-stimulated ATPase was purified from membranes of these cells by solubilization with decyl-beta-D-maltoside in the presence of Escherichia coli phospholipids followed by triazine-dye affinity chromatography.	Vanadates	2-10	ATPase	Escherichia coli	60-66	
2527329-2	1989	A vanadate-sensitive, K+- and Mg2+-stimulated ATPase was partially purified from membranes of these cells by solubilization with a non-ionic detergent followed by ion-exchange chromatography of the extract.	Vanadates	2-10	ATPase	Escherichia coli	46-52	
2527329-4	1989	The affinity of the partially purified ATPase from B. acidocaldarius for its substrates K+ (Km 2-3 microM) and ATP (Km 80 microM), its stimulation by various divalent cations, and its inhibition by vanadate (Ki 1-2 microM), bafilomycin A1 (Ki 20 microM), DCCD (Ki 200 microM) or Ca2+ were also similar to those of the E. coli enzyme, indicating that the two K+-translocating ATPases have almost identical properties.	Vanadates	198-206	ATPase	Escherichia coli	39-45	
18344567-4	2008	The protein ATPase activity was inhibited by vanadate and showed variable patterns of stimulation and inhibition by lipid A and other compounds.	Vanadates	45-53	ATPase	Escherichia coli	12-18