ライフサイエンスコーパス: metallochaperone

1 aperone complex and UreE serving as a nickel metallochaperone.

2 and structurally distinct attributes of this metallochaperone.

3 imer being critical for UreE's function as a metallochaperone.

4 Sco behaves more like a redox protein than a metallochaperone.

5 abundant protein postulated to function as a metallochaperone.

6 ch is thought to function as a mitochondrial metallochaperone.

7 cludes the ZnuACB uptake system and the YciC metallochaperone.

8 FKBP52 domain I and Atox1, a copper-binding metallochaperone.

9 scoring the specificity of the corresponding metallochaperones.

10 discovering a completely novel function for metallochaperones.

11 without requiring auxiliary factors such as metallochaperones.

12 pper is escorted to specific compartments by metallochaperones.

13 ilability is carefully regulated by cellular metallochaperones.

14 pecific intracellular targets is mediated by metallochaperones.

15 The exploratory cancer drug zinc metallochaperone-1 (ZMC1) was previously demonstrated to

16 gs provide a physical mechanism linking zinc metallochaperone-1 in both in vitro and in vivo activiti

17 no-terminal Domain I homologous to the Atx1p metallochaperone, a central portion (Domain II) homologo

18 consistent with a role for this protein as a metallochaperone, a class of metal ion transporters invo

19 These experiments establish a metallochaperone activity for CusF in the periplasm of g

20 ate that in addition to trafficking Cu ions, metallochaperones also function as buffers to modulate t

21 ails known for examples of uptake permeases, metallochaperones and proteins involved in metallocenter

22 quivalent repulsion between bacterial copper metallochaperones and the amino-terminal regions of P(1)

23 belongs to the recently discovered family of metallochaperones and to copper-transporting P-type ATPa

24 enesis, include two rubredoxins, a potential metallochaperone, and a new DnaJ-like protein.

25 Metallochaperones are a diverse family of trafficking mo

26 nd the emerging field of metal transport via metallochaperones are outlined.

27 Here we report the structure of the arsenic metallochaperone ArsD at 1.4 A and a model for its bindi

28 Copper metallochaperones assist copper in reaching vital destin

29 functions include exchanging copper with the metallochaperone Atox1 and mediating copper-responsive c

30 The metallochaperone Atox1 directly interacts with the coppe

31 in-protein interactions between WNDP and the metallochaperone Atox1, suggesting that these interactio

32 To elucidate the role of the metallochaperone Atox1, we analyzed mice with a disrupti

33 o the WND metal-binding domains and to their metallochaperone Atox1.

34 that detected interaction between the Cu(+)-metallochaperone Atx1 and the amino-terminal domain of C

35 ising stability of the drug complex with the metallochaperone Atx1 arises from formation of a sulfur-

36 opper homeostasis, even for the well-studied metallochaperone Atx1, remain unresolved.

37 pport of this latter role for cyanobacterial metallochaperone, Atx1.

38 C flexible loop in zinc acquisition from the metallochaperone AztD, yielding critical insights into m

39 yet is essential for zinc transfer from the metallochaperone AztD.

40 only the binding of multiple cuprous ions by metallochaperones but also protein-associated tetranucle

41 lic Cu(+), restricted contact with the Cu(+)-metallochaperone can impose a barrier impairing the form

42 This mutation did not inhibit the metallochaperone capacity of CCS, and in fact, D200H CCS

43 mplished in vivo by the action of the copper metallochaperone CCS (copper chaperone for SOD1).

44 ar copper availability and indicate that the metallochaperone CCS is a critical determinant of SOD1 a

45 Co-localization of human Sod1 and the metallochaperone CCS within the mitochondrial matrix res

46 The Cu(B) metallochaperone Cox11 transiently interacts with Shy1 b

47 The copper metallochaperone Cox17 is proposed to shuttle Cu(I) ions

48 An NMR titration of apoWLN5-6 with the metallochaperone Cu(I)HAH1 reveals no complex formation

49 vitro, and metal is transferred between the metallochaperone CusF and CusB-NT in vitro.

50 The tripartite efflux pump CusCBA and its metallochaperone CusF are vital to the detoxification of

51 The ArsD metallochaperone delivers trivalent metalloids, As(III)

52 G-protein metallochaperones ensure fidelity during cofactor assemb

53 Cox17 is the candidate copper metallochaperone for delivery of copper ions to the mito

54 affinity argues against a specific role as a metallochaperone for the delivery of ferrous ion to othe

55 parameter necessary for developing synthetic metallochaperones for clinical use.

56 pper and/or sulfur delivery and possibly for metallochaperone function.

57 The copper metallochaperone HAH1 (human Atx1) binds Cu(I) via a CXX

58 Metallochaperones help to achieve metal ion homeostasis

59 he maturation of both enzymes depends on the metallochaperone, HypA.

60 -loop GTPases, which contains other putative metallochaperones HypB, CooC, and UreG.

61 al the molecular architecture of a G-protein metallochaperone in complex with its target protein.

62 we have investigated the mechanistic role of metallochaperones in regulating Cu efflux.

63 Unlike metallochaperone-independent copper-supply to superoxide

64 ally, mechanistic studies show that the drug-metallochaperone inhibits metal transfer functions betwe

65 Although metallochaperones insert the correct metal into some pro

66 protection against oxidative stress, and as metallochaperones involved in the homeostasis of both es

67 To explore the role of this metallochaperone, its structure was solved in the nucleo

68 that although defects in these mitochondrial metallochaperones lead to a global copper deficiency at

69 particles, resulting in the up-regulation of metallochaperone-like genes or the down-regulation of aq

70 Many MerA proteins possess metallochaperone-like N-terminal domains (NmerA) that ca

71 ) M(-1) s(-1)), establishing transfer to the metallochaperone-like NmerA domain as the kinetically fa

72 ch protomer, the cytoplasmic domain adopts a metallochaperone-like protein fold; the transmembrane do

73 we describe a novel conserved mitochondrial metallochaperone-like protein, Cmc1p, whose function aff

74 we describe another conserved mitochondrial metallochaperone-like protein, Cmc2, a close homologue o

75 tions of copper deficiency and mitochondrial metallochaperone malfunction, illustrating the importanc

76 tx1p does not suppress oxidative damage by a metallochaperone mechanism but may directly consume supe

77 te and protein-protein interactions enabling metallochaperone-mediated assembly of the copper site.

78 e Atx1p represents a member of the family of metallochaperone molecules that escort copper to distinc

79 istic explanation for previously observed Cu metallochaperone mutation phenotypes.

80 lthough intracellular copper is regulated by metallochaperones, no chaperones involved in conferring

81 t for understanding how heavy metals bind to metallochaperones or metalloregulatory proteins.

82 ion of Coa6 and Sco2, a mitochondrial copper metallochaperone, or Coa6 and Cox12/COX6B, a structural

83 of mammalian cells and demonstrate that this metallochaperone plays a critical role in perinatal copp

84 Holo hGRX5 works as a metallochaperone preventing the [2Fe-2S] cluster to be r

85 This metallochaperone protein activates the target enzyme thr

86 efflux systems involving a CopZ-like copper metallochaperone protein and a CopA P(1)-type ATPase.

87 The Atx1 metallochaperone protein is a cytoplasmic Cu(I) receptor

88 c superoxide dismutase (SOD1) by its partner metallochaperone protein is not well understood.

89 gulatory sensors, and diffusible cytoplasmic metallochaperone proteins that protect and guide metal i

90 oration into these enzymes is facilitated by metallochaperone proteins which probably use copper from

91 icity can be achieved through metal-specific metallochaperone proteins.

92 peroxide dismutase (CCS) is an intracellular metallochaperone required for incorporation of copper in

93 ll Metabolism, report that the mitochondrial metallochaperones Sco1 and Sco2, essential for cytochrom

94 This chemical metallochaperone strategy may be an effective means for

95 Copper metallochaperones supply copper to cupro-proteins throug

96 The current state of knowledge on how copper metallochaperones support the maturation of cuproprotein

97 ArsD is a metallochaperone that delivers As(III) to ArsA, increasi

98 nction of WNDP depends on Atox1, a cytosolic metallochaperone that delivers copper to WNDP.

99 Klebsiella aerogenes UreE, a metallochaperone that delivers nickel ions during urease

100 ArsD is a metallochaperone that delivers trivalent metalloids [As(

101 Sco1 is a metallochaperone that is required for copper delivery to

102 biochemical study that shows that Sco1 is a metallochaperone that selectively transfers Cu(I) ions b

103 CusF is a metallochaperone that transfers Cu(I) and Ag(I) to the C

104 icant superoxide scavenging activity to this metallochaperone that was readily detected with CCS expr

105 teractions and it has been hypothesized that metallochaperones thereby inhibit copper from causing da

106 ved, again consistent with a role for copper metallochaperones to withhold copper from binding sites

107 Metallochaperones traffic copper (Cu(+)) from its point

108 This buffering function of metallochaperones ultimately sets the upper limit for in

109 a cell biological model for the role of this metallochaperone under the physiological conditions of c

110 r ions are specifically released from copper metallochaperones upon contact with their cognate cuprop

111 The metallochaperone UreE is suggested to transfer its bound

112 the urease active site are delivered by the metallochaperone UreE, whose metal binding properties ar

113 in eukaryotes involves small proteins termed metallochaperones, which mediate copper delivery to spec

114 SCO1 and SCO2 are metallochaperones whose principal function is to add two

115 In this sense, metallochaperones work like enzymes, carefully tailoring

116 o Zn starvation, we identified a putative Zn metallochaperone, ZigA, which binds Zn and is required f

117 at small-molecule zinc chelators called zinc metallochaperones (ZMCs) reactivate mutant p53 by restor