5.6.1.7	Ca2+	is found to protect against proteolysis of a form of GroEL, ox-GroEL, prepared by exposing GroEL to hydroxide peroxide, induces a conformational change	684903	
5.6.1.7	Ca2+	the enzyme is less active, when Ca2+, Cu2+, Co2+, and Ni2+ are used ar the same concentration instead of Mn2+	668673	
5.6.1.7	Co2+	2 mM, 41% of activity with Mg2+	654945	
5.6.1.7	Co2+	divalent cation required for ATP hydrolysis, mediate nucleoside triphosphate-dependent refolding of malate dehydrogenase	698649	
5.6.1.7	Co2+	Pf Cpn shows increased ATPase activity in the presence of either Co2+ or Mn2+	711001	
5.6.1.7	Co2+	relatively low ATPase activity in presence of Co2+ or Mn2+	711541	
5.6.1.7	Co2+	Ta-cpn beta1 shows ATPase activity in the presence of Co2+. A weak ATPase activity is observed in the presence of Mn2+ or Mg2+	711214	
5.6.1.7	Co2+	Ta-cpn R1 hydrolyzes ATP in the presence of Co2+, Mn2+, or Mg2+. ATPase activity of the monomeric enzyme is the highest in the presence of Co2+	711214	
5.6.1.7	Co2+	the enzyme is less active, when Ca2+, Cu2+, Co2+, and Ni2+ are used ar the same concentration instead of Mn2+	668673	
5.6.1.7	Cs+	1 mM, 81% of K+ activation	289233