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ATP5O — CD2

Text-mined interactions from Literome

Eren et al., Plant Physiol 2004 : HMA2 is a Zn ( 2+ ) -dependent ATPase that is also activated by Cd2+ and, to a lesser extent, by other divalent heavy metals ( Pb2+, Ni2+, Cu2+, and Co2+ )
Banerjee et al., Nucleic Acids Res 2005 : Zinc ( Zn2+ ) does not overcome the direct inhibitory effect of Cd2+ on the MSH2-MSH6 ATPase activity in vitro
Chao et al., Arch Toxicol 1990 : These findings suggest that the activation of myofibrillar ATPase by Cd2+ and Pb2+ is mediated through TnC
Yamaguchi et al., Chem Pharm Bull (Tokyo) 1989 : Regucalcin ( 2.0 microM ) did not enhance the effect of V5+ and Cd2+ on Ca2+-ATPase activity
Böhme et al., Biochim Biophys Acta 1987 : The high-affinity Ca2+-ATPase was competitively inhibited by La3+ and Cd2+ ; we suggest that this high-affinity enzyme mediates the release of Ca2+ from D. discoideum cells
Nimura et al., Ecotoxicol Environ Saf 1987 : The effects of Cd2+ on Ca2+-sensitive myosin ATPase activity were examined ... In the absence of Ca2+, the Ca2+ dependent myosin ATPase activity was enhanced by Cd2+ to the same extent as with Ca2+ at concentrations ranging from 10 ( -6 ) to 10 ( -3 ) M
King et al., Biochem Pharmacol 1983 (Hemolysis) : The effects of Al3+, Cd2+ and Mn2+ on human erythrocyte choline transport, Na-K-ATPase , Ca-Mg-ATPase and intracellular K+ levels were examined
Visser et al., Biochim Biophys Acta 1993 : In the presence as well as in the absence of calmodulin, Cd2+ inhibits the human erythrocyte plasma membrane Ca ( 2+ ) -ATPase activity non-competitively with Ki = 2 nM, whereas ATP dependent Ca ( 2+ ) -transport across the red cell membrane was found to be inhibited competitively by Cd2+ ( Verbost, P.M., Flik, G., Pang, P.K.T., Lock, R.A.C. and Wendelaar Bonga, S.E. ( 1989 ) J. Biol. Chem. 264, 5613-5615 )
Carfagna et al., Chem Biol Interact 1996 : Simultaneous exposure to Cd2+/Pb2+ antagonistically inhibited Mg2+-ATPase activity while Cd2+/Mn2+ or Pb2+/Mn2+ additively inhibited Mg2+-ATPase activity at low Mn2+ concentrations, but inhibited antagonistically at higher concentrations
Labyntseva et al., Ukr Biokhim Zh 1998 : The inhibiting effect of Pb2+, Zn2+ and Cd2+ on Mg ( 2+ ) -dependent superprecipitation and ATPase activity of myometrium actomyosin