PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 8123667-7 1994 Ca2+, Mg2+, Mn2+, and Ni2+ stimulated calmodulin N-methyltransferase activity but Zn2+ did not. Nickel(2+) 22-26 calmodulin 1 Homo sapiens 38-48 11437384-0 2001 Ni(2+), a double-acting inhibitor of neuronal nitric oxide synthase interfering with L-arginine binding and Ca(2+)/calmodulin-dependent enzyme activation. Nickel(2+) 0-6 calmodulin 1 Homo sapiens 115-125 11437384-3 2001 Ni(2+) also inhibited CaM-dependent cytochrome c reduction, NADPH oxidation, and H(2)O(2) production by nNOS. Nickel(2+) 0-6 calmodulin 1 Homo sapiens 22-25 11437384-4 2001 Overall, the action profile of Ni(2+) was suggestive of an unusual, double-acting inhibitor of nNOS affecting l-arginine-binding and Ca(2+)/CaM-dependent enzyme activation. Nickel(2+) 31-37 calmodulin 1 Homo sapiens 140-143 1663111-0 1991 Calmodulin antagonists differentiate between Ni(2+)- and Mn(2+)-stimulated phosphatase activity of calcineurin. Nickel(2+) 45-51 calmodulin 1 Homo sapiens 0-10 1663111-3 1991 Other calmodulin antagonists, such as trifluoperazine, thioridazine, and W-7, also inhibited the Ni(2+)-stimulated phosphatase activity. Nickel(2+) 97-103 calmodulin 1 Homo sapiens 6-16 1663111-6 1991 When the amount of additional B subunit was increased, the phosphatase activity recovered to 94% of the control level, thereby implying that calmidazolium inhibits the Ni(2+)-stimulated phosphatase activity by interacting with the B subunit, in the absence of calmodulin. Nickel(2+) 168-174 calmodulin 1 Homo sapiens 260-270 1663111-8 1991 These results indicate that the Ni(2+)- and Mn(2+)-stimulated activities of calcineurin are differentially affected by calmodulin antagonists and that the B subunit plays a crucial role in the expression of the Ni(2+)-stimulated phosphatase activity. Nickel(2+) 32-38 calmodulin 1 Homo sapiens 119-129 1663111-2 1991 Calmidazolium, a potent calmodulin antagonist, inhibited the Ni(2+)-stimulated calmodulin-independent phosphatase activity to much the same extent as it did the Ca2+/calmodulin-stimulated activity. Nickel(2+) 61-67 calmodulin 1 Homo sapiens 24-34 1663111-2 1991 Calmidazolium, a potent calmodulin antagonist, inhibited the Ni(2+)-stimulated calmodulin-independent phosphatase activity to much the same extent as it did the Ca2+/calmodulin-stimulated activity. Nickel(2+) 61-67 calmodulin 1 Homo sapiens 79-89 1663111-2 1991 Calmidazolium, a potent calmodulin antagonist, inhibited the Ni(2+)-stimulated calmodulin-independent phosphatase activity to much the same extent as it did the Ca2+/calmodulin-stimulated activity. Nickel(2+) 61-67 calmodulin 1 Homo sapiens 79-89 2620798-3 1989 In the presence of Ca(II), the CAM molecule has two binding sites for Ni(II) (K1 = 7.25 x 10(5) M-1; K2 = 3.79 x 10(5) M-1) (Hill coefficient = 1.20 +/- 0.03 SE). Nickel(2+) 70-76 calmodulin 1 Homo sapiens 31-34 2620798-5 1989 Binding of Ni(II) to CAM in the presence of Ca(II) is inhibited slightly by added MnCl2 (50 microM) and very strongly by CuCl2 and ZnCl2 (10 microM). Nickel(2+) 11-17 calmodulin 1 Homo sapiens 21-24 2620798-8 1989 Thus, the observed inhibition by Zn(II) of the Ni(II) binding to Ca(II)/CAM does not involve competition for the same binding sites but is rather caused by a conformational arrangement of CAM in its Ca(II)/Zn(II) complex that is different than the Ca(II) complex. Nickel(2+) 47-53 calmodulin 1 Homo sapiens 72-75 2620798-8 1989 Thus, the observed inhibition by Zn(II) of the Ni(II) binding to Ca(II)/CAM does not involve competition for the same binding sites but is rather caused by a conformational arrangement of CAM in its Ca(II)/Zn(II) complex that is different than the Ca(II) complex. Nickel(2+) 47-53 calmodulin 1 Homo sapiens 188-191 2620798-1 1989 The binding of Ni(II) to calmodulin (CAM) in the presence and in the absence of Ca(II) was investigated by equilibrium dialysis in order to test the physicochemistry of direct Ni(II)-CAM interactions that might be responsible for the effects of this metal on CAM observed in vivo. Nickel(2+) 15-21 calmodulin 1 Homo sapiens 25-35 2620798-1 1989 The binding of Ni(II) to calmodulin (CAM) in the presence and in the absence of Ca(II) was investigated by equilibrium dialysis in order to test the physicochemistry of direct Ni(II)-CAM interactions that might be responsible for the effects of this metal on CAM observed in vivo. Nickel(2+) 15-21 calmodulin 1 Homo sapiens 37-40 2620798-1 1989 The binding of Ni(II) to calmodulin (CAM) in the presence and in the absence of Ca(II) was investigated by equilibrium dialysis in order to test the physicochemistry of direct Ni(II)-CAM interactions that might be responsible for the effects of this metal on CAM observed in vivo. Nickel(2+) 176-182 calmodulin 1 Homo sapiens 183-186 2620798-1 1989 The binding of Ni(II) to calmodulin (CAM) in the presence and in the absence of Ca(II) was investigated by equilibrium dialysis in order to test the physicochemistry of direct Ni(II)-CAM interactions that might be responsible for the effects of this metal on CAM observed in vivo. Nickel(2+) 176-182 calmodulin 1 Homo sapiens 183-186 6327669-8 1984 We have utilized the nonprotein chromogenic substrate p-nitrophenyl phosphate to investigate the effects of several divalent metal ions on calcineurin activity and have found that Ni2+ is the best activator of calcineurin both in the presence and absence of calmodulin. Nickel(2+) 180-184 calmodulin 1 Homo sapiens 258-268 6314931-11 1983 In contrast Mg2+, Hg2+, Sn2+, Fe2+, Ni2+, Co2+, and Cu2+ triggered, if at all, a non-saturable binding of calmodulin. Nickel(2+) 36-40 calmodulin 1 Homo sapiens 106-116 6311199-1 1983 Calcineurin, a Ca2+- and calmodulin-dependent phosphoprotein phosphatase, was dramatically activated by Ni2+ ions. Nickel(2+) 104-108 calmodulin 1 Homo sapiens 25-35 6311199-2 1983 Activation by Ni2+ was independent of calmodulin and was not reversed by high concentrations of chelators. Nickel(2+) 14-18 calmodulin 1 Homo sapiens 38-48 6311199-4 1983 Similar to the Ca2+- and Mn2+-supported reactions, the presence of calmodulin caused a 20-fold activation of the Ni2+-activated calcineurin over the basal rate. Nickel(2+) 113-117 calmodulin 1 Homo sapiens 67-77