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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 cludes the ZnuACB uptake system and the YciC metallochaperone.
5 Sco behaves more like a redox protein than a metallochaperone.
6 abundant protein postulated to function as a metallochaperone.
7 ch is thought to function as a mitochondrial metallochaperone.
8  FKBP52 domain I and Atox1, a copper-binding metallochaperone.
9 pecific intracellular targets is mediated by metallochaperones.
10 scoring the specificity of the corresponding metallochaperones.
11 ction that are assembled by subunit-specific metallochaperones.
12 nsport proteins (ZIP, TroA-like) and COG0523 metallochaperones.
13  discovering a completely novel function for metallochaperones.
14  without requiring auxiliary factors such as metallochaperones.
15 pper is escorted to specific compartments by metallochaperones.
16 ilability is carefully regulated by cellular metallochaperones.
17             The exploratory cancer drug zinc metallochaperone-1 (ZMC1) was previously demonstrated to
18 gs provide a physical mechanism linking zinc metallochaperone-1 in both in vitro and in vivo activiti
19 no-terminal Domain I homologous to the Atx1p metallochaperone, a central portion (Domain II) homologo
20 consistent with a role for this protein as a metallochaperone, a class of metal ion transporters invo
21                These experiments establish a metallochaperone activity for CusF in the periplasm of g
22 doxin-1 (hGrx1) has been shown to possess Cu metallochaperone activity.
23 ate that in addition to trafficking Cu ions, metallochaperones also function as buffers to modulate t
24 ting with the capture of As(III) by the ArsD metallochaperone and culminating in its removal from the
25  data reveal the existence of a family of Zn metallochaperones and assign ZNG1 an important role for
26 ails known for examples of uptake permeases, metallochaperones and proteins involved in metallocenter
27 quivalent repulsion between bacterial copper metallochaperones and the amino-terminal regions of P(1)
28 belongs to the recently discovered family of metallochaperones and to copper-transporting P-type ATPa
29 enesis, include two rubredoxins, a potential metallochaperone, and a new DnaJ-like protein.
30                                              Metallochaperones are a diverse family of trafficking mo
31                                    G-protein metallochaperones are essential for the proper maturatio
32 nd the emerging field of metal transport via metallochaperones are outlined.
33 ng Zn limitation, specialized enzymes called metallochaperones are predicted to allocate Zn to specif
34  Here we report the structure of the arsenic metallochaperone ArsD at 1.4 A and a model for its bindi
35                                       Copper metallochaperones assist copper in reaching vital destin
36 functions include exchanging copper with the metallochaperone Atox1 and mediating copper-responsive c
37                 hGrx1 can transfer Cu to the metallochaperone Atox1 and to the MBDs 5-6 of ATP7B (WLN
38                                          The metallochaperone Atox1 directly interacts with the coppe
39 in-protein interactions between WNDP and the metallochaperone Atox1, suggesting that these interactio
40                 To elucidate the role of the metallochaperone Atox1, we analyzed mice with a disrupti
41 o the WND metal-binding domains and to their metallochaperone Atox1.
42  that detected interaction between the Cu(+)-metallochaperone Atx1 and the amino-terminal domain of C
43 ising stability of the drug complex with the metallochaperone Atx1 arises from formation of a sulfur-
44 opper homeostasis, even for the well-studied metallochaperone Atx1, remain unresolved.
45 pport of this latter role for cyanobacterial metallochaperone, Atx1.
46 C flexible loop in zinc acquisition from the metallochaperone AztD, yielding critical insights into m
47  yet is essential for zinc transfer from the metallochaperone AztD.
48 ion includes the expression of putative zinc metallochaperones belonging to subfamily 1 of the COG052
49 only the binding of multiple cuprous ions by metallochaperones but also protein-associated tetranucle
50 lic Cu(+), restricted contact with the Cu(+)-metallochaperone can impose a barrier impairing the form
51            This mutation did not inhibit the metallochaperone capacity of CCS, and in fact, D200H CCS
52 mplished in vivo by the action of the copper metallochaperone CCS (copper chaperone for SOD1).
53 ar copper availability and indicate that the metallochaperone CCS is a critical determinant of SOD1 a
54        Co-localization of human Sod1 and the metallochaperone CCS within the mitochondrial matrix res
55 ights into the molecular basis by which this metallochaperone contributes to AdoCbl delivery without
56                                    The Cu(B) metallochaperone Cox11 transiently interacts with Shy1 b
57                                   The copper metallochaperone Cox17 is proposed to shuttle Cu(I) ions
58                            The mitochondrial metallochaperone COX19 influences iron and copper respon
59       An NMR titration of apoWLN5-6 with the metallochaperone Cu(I)HAH1 reveals no complex formation
60 es and transfer it to the periplasmic copper metallochaperone CueP.
61  vitro, and metal is transferred between the metallochaperone CusF and CusB-NT in vitro.
62    The tripartite efflux pump CusCBA and its metallochaperone CusF are vital to the detoxification of
63                                     The ArsD metallochaperone delivers trivalent metalloids, As(III)
64                                    G-protein metallochaperones ensure fidelity during cofactor assemb
65                Cox17 is the candidate copper metallochaperone for delivery of copper ions to the mito
66 affinity argues against a specific role as a metallochaperone for the delivery of ferrous ion to othe
67 parameter necessary for developing synthetic metallochaperones for clinical use.
68 pper and/or sulfur delivery and possibly for metallochaperone function.
69                                   The copper metallochaperone HAH1 (human Atx1) binds Cu(I) via a CXX
70 ed to G3E GTPase COG0523 proteins, yet no Zn metallochaperone has been experimentally identified in a
71                The results suggest that zinc metallochaperones have the capability to treat 120,500 p
72                                              Metallochaperones help to achieve metal ion homeostasis
73 nstrate that the Bacillus subtilis YciC zinc metallochaperone (here renamed ZagA for ZTP activated GT
74 he maturation of both enzymes depends on the metallochaperone, HypA.
75 -loop GTPases, which contains other putative metallochaperones HypB, CooC, and UreG.
76 al the molecular architecture of a G-protein metallochaperone in complex with its target protein.
77 esis of cytochrome C oxidase 2 (SCO2), a key metallochaperone in the electron transport chain, is cri
78 we have investigated the mechanistic role of metallochaperones in regulating Cu efflux.
79                                       Unlike metallochaperone-independent copper-supply to superoxide
80 ally, mechanistic studies show that the drug-metallochaperone inhibits metal transfer functions betwe
81                                     Although metallochaperones insert the correct metal into some pro
82 t3, we determined that ES can bypass Atx1, a metallochaperone involved in Cu delivery to the Golgi me
83 are generally present in at least one of the metallochaperones involved in nickel delivery.
84  protection against oxidative stress, and as metallochaperones involved in the homeostasis of both es
85                  To explore the role of this metallochaperone, its structure was solved in the nucleo
86 that although defects in these mitochondrial metallochaperones lead to a global copper deficiency at
87 particles, resulting in the up-regulation of metallochaperone-like genes or the down-regulation of aq
88                   Many MerA proteins possess metallochaperone-like N-terminal domains (NmerA) that ca
89 ) M(-1) s(-1)), establishing transfer to the metallochaperone-like NmerA domain as the kinetically fa
90 ch protomer, the cytoplasmic domain adopts a metallochaperone-like protein fold; the transmembrane do
91  we describe a novel conserved mitochondrial metallochaperone-like protein, Cmc1p, whose function aff
92  we describe another conserved mitochondrial metallochaperone-like protein, Cmc2, a close homologue o
93 tions of copper deficiency and mitochondrial metallochaperone malfunction, illustrating the importanc
94                                    G-protein metallochaperone MeaB in bacteria [methylmalonic aciduri
95 tx1p does not suppress oxidative damage by a metallochaperone mechanism but may directly consume supe
96 te and protein-protein interactions enabling metallochaperone-mediated assembly of the copper site.
97 e Atx1p represents a member of the family of metallochaperone molecules that escort copper to distinc
98 istic explanation for previously observed Cu metallochaperone mutation phenotypes.
99 lthough intracellular copper is regulated by metallochaperones, no chaperones involved in conferring
100 t for understanding how heavy metals bind to metallochaperones or metalloregulatory proteins.
101 ion of Coa6 and Sco2, a mitochondrial copper metallochaperone, or Coa6 and Cox12/COX6B, a structural
102 etalation is facilitated by metal exporters, metallochaperones, or partner proteins that enhance meta
103  1 (CTR1) uptake protein to all known copper metallochaperone pathways, while simultaneously making i
104 of mammalian cells and demonstrate that this metallochaperone plays a critical role in perinatal copp
105                        Holo hGRX5 works as a metallochaperone preventing the [2Fe-2S] cluster to be r
106                                         This metallochaperone protein activates the target enzyme thr
107  efflux systems involving a CopZ-like copper metallochaperone protein and a CopA P(1)-type ATPase.
108                                     The Atx1 metallochaperone protein is a cytoplasmic Cu(I) receptor
109 c superoxide dismutase (SOD1) by its partner metallochaperone protein is not well understood.
110 gulatory sensors, and diffusible cytoplasmic metallochaperone proteins that protect and guide metal i
111 oration into these enzymes is facilitated by metallochaperone proteins which probably use copper from
112 icity can be achieved through metal-specific metallochaperone proteins.
113 d stepwise and involves molecular scaffolds, metallochaperones, radical chemistry, and novel and uniq
114 peroxide dismutase (CCS) is an intracellular metallochaperone required for incorporation of copper in
115 xperiments demonstrate that a synthetic zinc metallochaperone rescues not only mutations that decreas
116   COA7 interacts transiently with the copper metallochaperones SCO1 and SCO2 and catalyzes the reduct
117 ll Metabolism, report that the mitochondrial metallochaperones Sco1 and Sco2, essential for cytochrom
118 ies on a tripartite efflux complex SilCBA, a metallochaperone SilF and an intrinsically disordered pr
119                                This chemical metallochaperone strategy may be an effective means for
120                                       Copper metallochaperones supply copper to cupro-proteins throug
121 The current state of knowledge on how copper metallochaperones support the maturation of cuproprotein
122                                    ArsD is a metallochaperone that delivers As(III) to ArsA, increasi
123 nction of WNDP depends on Atox1, a cytosolic metallochaperone that delivers copper to WNDP.
124                 Klebsiella aerogenes UreE, a metallochaperone that delivers nickel ions during urease
125                                    ArsD is a metallochaperone that delivers trivalent metalloids [As(
126                                    Sco1 is a metallochaperone that is required for copper delivery to
127  biochemical study that shows that Sco1 is a metallochaperone that selectively transfers Cu(I) ions b
128                                    CusF is a metallochaperone that transfers Cu(I) and Ag(I) to the C
129 icant superoxide scavenging activity to this metallochaperone that was readily detected with CCS expr
130 ems, which rely on the activities of soluble metallochaperones that participate in Cu exchange throug
131 teractions and it has been hypothesized that metallochaperones thereby inhibit copper from causing da
132 oproteome remodeling and metal allocation by metallochaperones to both client proteins and compartmen
133 ved, again consistent with a role for copper metallochaperones to withhold copper from binding sites
134 ells have evolved metal carrier proteins, or metallochaperones, to deliver the toxic ions to specific
135                                              Metallochaperones traffic copper (Cu(+)) from its point
136                   This buffering function of metallochaperones ultimately sets the upper limit for in
137 a cell biological model for the role of this metallochaperone under the physiological conditions of c
138 r ions are specifically released from copper metallochaperones upon contact with their cognate cuprop
139                                          The metallochaperone UreE is suggested to transfer its bound
140  the urease active site are delivered by the metallochaperone UreE, whose metal binding properties ar
141 in eukaryotes involves small proteins termed metallochaperones, which mediate copper delivery to spec
142                            SCO1 and SCO2 are metallochaperones whose principal function is to add two
143                               In this sense, metallochaperones work like enzymes, carefully tailoring
144 o Zn starvation, we identified a putative Zn metallochaperone, ZigA, which binds Zn and is required f
145 at small-molecule zinc chelators called zinc metallochaperones (ZMCs) reactivate mutant p53 by restor
146 nt p53 mutants using a mechanism called zinc metallochaperones (ZMCs) that restore zinc binding by sh

 
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