ライフサイエンスコーパス: transporting ATPase

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 This putative cation-transporting ATPase 13A5 (Atp13a5) marker was identified

6 al pipeline, we identified aminophospholipid transporting ATPase 2 (ALA2) and the related ALA1 in the

7 isorder caused by inactivation of the copper-transporting ATPase 2 (ATP7B) and copper (Cu) overload i

8 Ca(2+) pump PMCA4b (plasma membrane calcium-transporting ATPase 4b) interact tightly with each other

9 key catalytic properties of the ATP7B copper-transporting ATPase and provide a foundation for quantit

10 one Atox1 directly interacts with the copper-transporting ATPases and plays a critical role in perina

11 These results suggest that PepO, a cation-transporting ATPase, and an ABC transporter are required

12 in homologous to the mouse aminophospholipid-transporting ATPase Atp10c.

13 The calcium-transporting ATPase ATP2A2, also known as SERCA2a, is a

14 The copper-transporting ATPase ATP7A has an essential role in human

15 Copper-transporting ATPase ATP7A is essential for mammalian cop

16 Malfunctions of the Cu(+) -transporting ATPases ATP7A and ATP7B cause Menkes diseas

17 The copper-transporting ATPases ATP7A and ATP7B play a central role

18 he phenotype has been identified as a copper transporting ATPase ( ATP7A ).

19 tion mutations in the gene encoding a copper-transporting ATPase (Atp7a) on the X chromosome.

20 orders caused by mutations in the copper ion transporting ATPase, ATP7A.

21 The copper-transporting ATPase ATP7B has a dual intracellular local

22 Copper-transporting ATPase ATP7B is essential for human copper

23 The copper-transporting ATPase ATP7B is essential for normal distri

24 Copper-transporting ATPase ATP7B is essential for normal distri

25 y sequence analysis suggests that the copper-transporting ATPase ATP7B or the Wilson's disease protei

26 used by mutations in a liver-specific copper-transporting ATPase, ATP7B.

27 ity to activate the human erythrocyte Ca(2+)-transporting ATPase (Ca(2+)-ATPase) was evaluated.

28 erevisiae deficient in the homologous copper-transporting ATPase CCC2, suggesting that this protein m

29 Collectively, these data suggest that copper-transporting ATPases, CopA and ATP7A, in both bacteria a

30 g heavy metal-associated (HMA) domains of Cu-transporting ATPases (Cu-ATPases), and the genes for cop

31 Copper-transporting ATPases differ from other P-type ATPases in

32 Two membrane-bound Cu-transporting ATPase enzymes, ATP7A and ATP7B, the produc

33 Wilson's disease protein (WNDP) is a copper-transporting ATPase essential for normal distribution of

34 The Atp7b protein is a copper-transporting ATPase expressed predominantly in the liver

35 omain of WNDP and is conserved in all copper-transporting ATPases from bacteria to mammals; however,

36 erichia coli, a Pb(II)-, Zn(II)-, and Cd(II)-transporting ATPase, has an approximately 120 residue am

37 The WD protein functions as a P-type copper transporting ATPase in the Golgi but any action in mitoc

38 ide biochemical evidence that PMR1 is a Ca2+-transporting ATPase in the Golgi, a hitherto unusual loc

39 it assembly, it is only functional as an ion-transporting ATPase in the presence of the beta-subunit.

40 the function and localization of the copper-transporting ATPases in mammalian cells and provide comp

41 ns of intracellular and plasma membrane Ca2+-transporting ATPases in the control of cytosolic and org

42 e physiological functions of individual Ca2+-transporting ATPases in vivo.

43 minal domain (ZiaA(N)) of the P(1)-type zinc-transporting ATPase is especially similar to the copper

44 which belongs to the P-type family of cation-transporting ATPases, is activated up to 10-fold by grow

45 , which belongs to the P2 subgroup of cation-transporting ATPases, is encoded by the PMA1 gene and fu

46 hows higher similarity to the bacterial K(+)-transporting ATPase KdpB than to the mammalian Ca(2+)-AT

47 Human Wilson protein is a copper-transporting ATPase located in the secretory pathway pos

48 Within the large family of P-type cation-transporting ATPases, members differ in the number of C-

49 distant similarity to a subunit of the Na(+)-transporting ATPase of Enterococcus hirae.

50 omologous to a human plasma membrane calcium-transporting ATPase (PMCA).

51 The Golgi-localized Ca2+- and Mn2+-transporting ATPase Pmr1 is important for secretory path

52 TPase but encodes a single FixI/CcoI-type Cu-transporting ATPase, previously implicated in Cu deliver

53 Wilson's disease protein (WNDP) is a copper-transporting ATPase regulating distribution of copper in

54 ATP4 is thought to be a cation-transporting ATPase responsible for maintaining low intr

55 , alpha-catenin, tubulin alpha-chain, copper-transporting ATPase, salivary gland protein SGS-3 precur

56 hibition of sarco-endoplasmic reticulum Ca2+-transporting ATPase (SERCA; 10 microM cyclopiazonic acid

57 The Wilson disease protein is a copper transporting ATPase shown to play a critical role in bil

58 R 0.90 [95% CI 0.88-0.92]), sodium/potassium-transporting ATPase subunit beta2 (MR OR 1.10 [95% CI 1.

59 ssesses signatures of a P1B-type heavy metal-transporting ATPase that is widely distributed from bact

60 by knockdown of ATP7A, a trans-Golgi, copper-transporting ATPase that traffics to the plasma membrane

61 (-7) at rs6564903) and that encoding calcium-transporting ATPase, type2C, member2 (ATP2C2, minP = 2.0

62 The vacuolar-type H+-transporting ATPase (V-ATPase), rather than other Ca2+ t

63 ) (size 18), rRNA splicing (size 24) and H+- transporting ATPase, vacular (size 15).

64 of Escherichia coli lacking the CopA copper-transporting ATPase was hypersensitive to killing by RAW

65 ding cassette (ABC) transporter and a cation-transporting ATPase were upregulated in GECs.

66 sed by mutations in a gene encoding a copper-transporting ATPase (Wilson's disease protein, WNDP).

67 for copper-dependent movement of the copper-transporting ATPases within the secretory compartment an

68 We have identified the P-type metal-transporting ATPase ZosA (formerly YkvW) as an additiona