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1 The ATP7A gene encodes a copper-transporting ATPase.
2 s disease gene (MNK), which encodes a copper-transporting ATPase.
3 related members of the P-type family of ion transporting ATPases.
4 se disorders encode highly homologous copper transporting ATPases.
5 al pipeline, we identified aminophospholipid transporting ATPase 2 (ALA2) and the related ALA1 in the
6 key catalytic properties of the ATP7B copper-transporting ATPase and provide a foundation for quantit
7 one Atox1 directly interacts with the copper-transporting ATPases and plays a critical role in perina
8 These results suggest that PepO, a cation-transporting ATPase, and an ABC transporter are required
21 y sequence analysis suggests that the copper-transporting ATPase ATP7B or the Wilson's disease protei
24 erevisiae deficient in the homologous copper-transporting ATPase CCC2, suggesting that this protein m
25 Collectively, these data suggest that copper-transporting ATPases, CopA and ATP7A, in both bacteria a
26 g heavy metal-associated (HMA) domains of Cu-transporting ATPases (Cu-ATPases), and the genes for cop
29 Wilson's disease protein (WNDP) is a copper-transporting ATPase essential for normal distribution of
31 omain of WNDP and is conserved in all copper-transporting ATPases from bacteria to mammals; however,
32 erichia coli, a Pb(II)-, Zn(II)-, and Cd(II)-transporting ATPase, has an approximately 120 residue am
33 The WD protein functions as a P-type copper transporting ATPase in the Golgi but any action in mitoc
34 ide biochemical evidence that PMR1 is a Ca2+-transporting ATPase in the Golgi, a hitherto unusual loc
35 it assembly, it is only functional as an ion-transporting ATPase in the presence of the beta-subunit.
36 the function and localization of the copper-transporting ATPases in mammalian cells and provide comp
37 ns of intracellular and plasma membrane Ca2+-transporting ATPases in the control of cytosolic and org
39 minal domain (ZiaA(N)) of the P(1)-type zinc-transporting ATPase is especially similar to the copper
40 which belongs to the P-type family of cation-transporting ATPases, is activated up to 10-fold by grow
41 , which belongs to the P2 subgroup of cation-transporting ATPases, is encoded by the PMA1 gene and fu
42 hows higher similarity to the bacterial K(+)-transporting ATPase KdpB than to the mammalian Ca(2+)-AT
44 Within the large family of P-type cation-transporting ATPases, members differ in the number of C-
48 Wilson's disease protein (WNDP) is a copper-transporting ATPase regulating distribution of copper in
50 , alpha-catenin, tubulin alpha-chain, copper-transporting ATPase, salivary gland protein SGS-3 precur
51 hibition of sarco-endoplasmic reticulum Ca2+-transporting ATPase (SERCA; 10 microM cyclopiazonic acid
53 ssesses signatures of a P1B-type heavy metal-transporting ATPase that is widely distributed from bact
54 by knockdown of ATP7A, a trans-Golgi, copper-transporting ATPase that traffics to the plasma membrane
55 (-7) at rs6564903) and that encoding calcium-transporting ATPase, type2C, member2 (ATP2C2, minP = 2.0
58 of Escherichia coli lacking the CopA copper-transporting ATPase was hypersensitive to killing by RAW
60 sed by mutations in a gene encoding a copper-transporting ATPase (Wilson's disease protein, WNDP).
61 for copper-dependent movement of the copper-transporting ATPases within the secretory compartment an
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