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1  molecule mediating contact between HCCS and apocytochrome c.
2 s heme and in complex with its cognate human apocytochrome c.
3  served as the platform for interaction with apocytochrome c.
4 cific heme-binding residues of both CcmE and apocytochrome c.
5 valent attachment of the haem to periplasmic apocytochrome c.
6  with the view that the natural substrate is apocytochrome c.
7  the iron in the haem attachment reaction to apocytochromes c.
8 sulphide bond into the haem-binding motif of apocytochromes c.
9 ion of heme with the CXXCH sequence motif in apocytochromes c.
10 asurement of the redox midpoint potential of apocytochrome c(1) indicates that neither the P nor the
11  In this study, using Rhodobacter capsulatus apocytochrome c(2) as a Ccm substrate, we demonstrate fo
12 monstrate for the first time that CcmI binds apocytochrome c(2) but not holocytochrome c(2).
13 signed to serve as a model for R. capsulatus apocytochrome c(2) have also been carried out, and an E(
14 s interaction requires a free thiol group at apocytochrome c(2) heme binding site.
15 nly the C-terminal portions of both CcmI and apocytochrome c(2) mediate this binding.
16 E(m) versus pH plots for HelX, Ccl2, and the apocytochrome c(2) model peptide were all linear over th
17 terminal domain of CcmI can also weakly bind apocytochrome c(2), but this interaction requires a free
18 ons via the conserved structural elements in apocytochrome c(2), like the heme ligating cysteines or
19 he reduction of the cysteine residues of the apocytochromes c, a prerequisite for covalent ligation t
20 can efficiently reduce the disulfide bond of apocytochrome c and also resolve a mixed disulfide bond
21  is required for the activity of CCHL toward apocytochrome c and c1 and becomes essential for the hem
22                                Mitochondrial apocytochrome c and c1 are converted to their holoforms
23 hiol-independent, direct interaction between apocytochrome c and CcmG.
24 esolve a mixed disulfide bond formed between apocytochrome c and CcmH.
25                                    We employ apocytochrome c and peptide analogs containing CXXCH as
26 hetically made, pure Drosophila melanogaster apocytochrome c and Saccharomyces cerevisiae mitochondri
27 that the heme chaperone apoCcmE binds to the apocytochrome c and the apocytochrome c chaperone CcmI t
28 tions occurring between these components and apocytochrome c and the identity of their active Cys res
29 d Cyc2p catalyse covalent haem attachment to apocytochromes c and c(1) .
30 that Cyc2p interacts with CCHL and also with apocytochromes c and c(1) .
31 Catalysis of the thioether bonds between the apocytochromes c and heme b is mediated by the heme liga
32 ck a mitochondrial targeting sequence, e.g., apocytochrome c, and possibly Cox17, a mitochondrial cop
33 t, the binding of heme, and the mechanism of apocytochrome c (apocyt c) interaction with the synthase
34                                              Apocytochrome c (apocyt c), which in aqueous solution is
35 hift that exposes the heme for reaction with apocytochrome c (apocyt c).
36 chemistry of the heme attachment reaction to apocytochrome c are known in bacteria and plastids but n
37 rther show that Cys-45 of CcmH and Cys-34 of apocytochrome c are most likely to form this mixed disul
38     Using purified wild-type CcmG, CcmH, and apocytochrome c, as well as their respective Cys mutant
39                                              Apocytochrome c associated with yeast mitochondria in tw
40 he periplasmic reduction of the cysteines of apocytochromes c before ligation.
41   In addition we show that overexpression of apocytochrome c blocks Bax-induced apoptosis in cells.
42                                         Like apocytochrome c, but in contrast to holocytochrome c, Ct
43 e reduction of heme prior to its ligation to apocytochrome c by CCHL.
44 gated protein-protein interactions among the apocytochrome c, CcmG, and the heme-ligation components
45 apoCcmE binds to the apocytochrome c and the apocytochrome c chaperone CcmI to yield stable binary an
46 ubunit of the CcmFHI complex functions as an apocytochrome c chaperone during the Ccm process used by
47 nents, including CcmI, proposed to act as an apocytochrome c chaperone, R. capsulatus does not have t
48 chrome c synthetases (CcmF and SirE) and two apocytochrome c chaperones (CcmI and SirG).
49 rA requires the combined function of the two apocytochrome c chaperones CcmI and SirG.
50  interact with each other, forming a CcmFGHI-apocytochrome c complex.
51                                 In fact, all apocytochromes c containing deletions located to the car
52 th respect to heme transfer from CcmE to the apocytochromes c during heme ligation assisted by the co
53 duction of a disulphide at the CXXCH site of apocytochrome c (E(m) = -265 mV) is a thermodynamically
54  to an acceptor protein (apoCcmE for CcmC or apocytochrome c for CcmF and CcsBA) such that the heme v
55 ine, suggesting that in the absence of CccA, apocytochrome c haem binding motifs become oxidised, pre
56  removed) is substantially more ordered than apocytochrome c, having characteristics consistent with
57 sulfide bond between the Cys residues at the apocytochrome c heme-binding site (CXXCH).
58 vors the presence of a disulfide bond at the apocytochrome c heme-binding site.
59                     A conserved histidine in apocytochrome c (His19 of CXXCH) supplied the second axi
60 gation to a coexpressed Bordetella pertussis apocytochrome c in an Escherichia coli mutant lacking it
61 he protein responsible for reducing oxidized apocytochrome c in Bacillus subtilis, ResA, is specific
62  an integral role in the transfer of heme to apocytochrome c in many prokaryotes and some mitochondri
63                 Mutants containing wild type apocytochrome c in mitochondria lack COX, suggesting tha
64 me c, resulting from stalling of the altered apocytochrome c in partially imported states.
65  binding, transport, and coupling of heme to apocytochrome c in the periplasm of these Gram-negative
66 e, determined by the overall conformation of apocytochrome c in the vicinity of lysine 72, appears to
67                      Purified CcmG* can bind apocytochrome c in vitro, revealing for the first time a
68 ave indicated that specific heme delivery to apocytochrome c is a critical feature of the cytochrome
69                                              Apocytochrome c is synthesized in the cytoplasm, transpo
70 obligatory components of a minimalistic heme-apocytochrome c ligation complex in R. capsulatus.
71 tent with the stereo-specificity of the heme-apocytochrome c ligation reaction.
72 cmI interact with each other to perform heme-apocytochrome c ligation.
73 or thioreduction reactions that lead to heme-apocytochrome c ligation.
74                    A site-directed mutant of apocytochrome c (lysines 5, 7, and 8 replaced by glutami
75 avourable reaction, Cyc2p does not act as an apocytochrome c or c(1) CXXCH disulphide reductase in vi
76 he Ccl2 cysteine residues are oxidized by an apocytochrome c peptide containing the CXXCH domain.
77 s27, lead to reduced mitochondrial import of apocytochrome c, resulting from stalling of the altered
78                                        Thus, apocytochrome c secretion is normal in each of the four
79 fide cascade that reduces a disulfide on the apocytochromes c so that two cysteine thiols are availab
80                            Here we show that apocytochrome c still binds Apaf-1 and that it can block
81 ocytochrome c synthase (HCCS) binds heme and apocytochrome c substrate to catalyze this attachment, s
82        How the CcmFHI complex recognizes its apocytochrome c substrates remained unknown.
83 ut the requirements for delivery of haem and apocytochrome c substrates to produce c holocytochromes.
84 ted haem for processes besides attachment to apocytochrome c, the export of a non-haem compound throu
85           Thus, the high affinity binding of apocytochrome c to mitochondria is not directly related
86             It occurs after translocation of apocytochromes c to the p side of energy transducing mem
87 l process that occurs after translocation of apocytochromes c to the positive (p) side of energy-tran
88                        Import of the altered apocytochromes c was assayed in yeast strains that overe
89  form a thioreduction pathway (HelX-->Ccl2-->apocytochrome c) whereby Ccl2 function may be highly spe
90 cient mitochondrial accumulation of forms of apocytochrome c which are incapable of having heme coval
91 eby Ccl2 function may be highly specific for apocytochromes c while HelX may act as a more general re