PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
1701013-3	1990	When assayed in the presence of calmodulin, many divalent metals (Ni2+, Zn2+, Pb2+, Cd2+), besides Mn2+, increased modestly the phosphatase activity at low concentrations (10-100 microM) and inhibited it markedly at high concentrations.	Nickel(2+)	66-70	calmodulin	Bos taurus	32-42	
1701013-4	1990	Ca2(+)-calmodulin stimulated phosphatase activity was antagonized by Ni2+, Zn2+, Fe2+, Cu2+, Pb2+, at low concentrations (50 microM), and by Ba2+, Cd2+ at slightly higher concentrations (greater than 100 microM); Mn2+ and Co2+ (50 microM to 1 mM) in fact augmented it.	Nickel(2+)	69-73	calmodulin	Bos taurus	7-17	
2986124-8	1985	Fourth, the phosphodiesterase isozyme could be dephosphorylated by the calmodulin-dependent phosphatase (calcineurin) in the presence of Ni2+ or Mn2+, the dephosphorylation being associated with an increase in the enzyme affinity for calmodulin.	Nickel(2+)	137-141	calmodulin	Bos taurus	71-81	
2986124-8	1985	Fourth, the phosphodiesterase isozyme could be dephosphorylated by the calmodulin-dependent phosphatase (calcineurin) in the presence of Ni2+ or Mn2+, the dephosphorylation being associated with an increase in the enzyme affinity for calmodulin.	Nickel(2+)	137-141	calmodulin	Bos taurus	234-244	
3365386-6	1988	Phosphotyrosylfodrin could be dephosphorylated by the calmodulin-stimulated phosphatase (calcineurin) in the presence of activating metal ions; Ni2+ was a much more effective activator than Mn2+ for this reaction.	Nickel(2+)	144-148	calmodulin	Bos taurus	54-64	
2426255-2	1986	The phosphatase was activated by Ni2+ and Mn2+, and stimulated further by calmodulin.	Nickel(2+)	33-37	calmodulin	Bos taurus	74-84