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1  are activated by strain such as lipoic acid/lipoamide.
2 doxin-like active site that is responsive to lipoamide.
3 enotrisulfide derivatives of lipoic acid and lipoamide.
4                          Here, we identified lipoamide, a small molecule that specifically prevents c
5 ch are stress granule proteins necessary for lipoamide activity.
6                                  In animals, lipoamide ameliorates aging-associated aggregation of a
7 were noncompetitive versus NADH, NAD(+), and lipoamide and >100-fold selective compared to human Lpd.
8                                   Since free lipoamide and lipoic acid levels were shown to be undete
9 rare family of marine cyanobacterial-derived lipoamides and a new structural class of compounds exhib
10  intermediates on the E1p component, and the lipoamide-bound covalent intermediate on the E2p compone
11 mine that SIRT4 enzymatically hydrolyzes the lipoamide cofactors from the E2 component dihydrolipoyll
12 a lower K(I) for NADH, and a higher K(I) for lipoamide compared with the other two enzymes.
13 ihydrolipoamide succinyltransferase (E2) and lipoamide dehydrogenase (E3) components of alpha-ketoglu
14 rotein microscopy as a simultaneous assay of lipoamide dehydrogenase (LipDH) autofluorescence.
15 (P)H, flavin adenine dinucleotide (FAD), and lipoamide dehydrogenase (LipDH) over the wavelength rang
16 ssibility of species-selective inhibition of lipoamide dehydrogenase (Lpd), an enzyme central to Mtb'
17 hibitors of Mycobacterium tuberculosis (Mtb) lipoamide dehydrogenase (Lpd), which selectively inhibit
18                                              Lipoamide dehydrogenase also catalyzes NADH oxidation by
19 zed Ohr by NADH was shown to be catalyzed by lipoamide dehydrogenase and either lipoamide or DlaT (Su
20 oredoxin reductase is like the mechanisms of lipoamide dehydrogenase and glutathione reductase and di
21             The mechanisms and structures of lipoamide dehydrogenase and glutathione reductase are al
22 o other well-studied members of this family, lipoamide dehydrogenase and glutathione reductase, cycle
23       For each of two target enzymes tested, lipoamide dehydrogenase and mycobacterial proteasome ATP
24 nd EH(4) forms of Mycobacterium tuberculosis lipoamide dehydrogenase and rapidly mixed these enzyme f
25 mide dehydrogenase that is distinct from the lipoamide dehydrogenase associated with the pyruvate deh
26  reduction of the Mycobacterium tuberculosis lipoamide dehydrogenase by NADH and [4S-(2)H]-NADH was s
27                                              Lipoamide dehydrogenase can also catalyze the NADH-depen
28                                              Lipoamide dehydrogenase catalyses the NAD(+)-dependent o
29                                              Lipoamide dehydrogenase catalyzes the reversible NAD(+)-
30    We report the 2.4 A crystal structure for lipoamide dehydrogenase encoded by lpdC from Mycobacteri
31             Although annotated as a probable lipoamide dehydrogenase in M. tuberculosis, LpdA cannot
32 to peas (Pisum sativum), where mitochondrial lipoamide dehydrogenase is encoded by a single gene and
33 wed by reduction of the flavin, just as with lipoamide dehydrogenase or glutathione reductase.
34 te similar to that observed in titrations of lipoamide dehydrogenase or glutathione reductase.
35                                          The lipoamide dehydrogenase reaction catalyzed by the purifi
36 pdA gene, which encodes the oxidative enzyme lipoamide dehydrogenase required for tricarboxylic acid
37 oded by bkdD indicate that E. faecalis has a lipoamide dehydrogenase that is distinct from the lipoam
38  targets major enzymes of energy production (lipoamide dehydrogenase) and antioxidant defense (thiore
39 ro properties of recombinant GDC l-proteins (lipoamide dehydrogenase) from plants and the cyanobacter
40                                              Lipoamide dehydrogenase, a component of the alpha-ketogl
41                       Thioredoxin reductase, lipoamide dehydrogenase, and glutathione reductase are m
42 e, in contrast to the closely related enzyme lipoamide dehydrogenase, for which only EH2 is active.
43 l members of the enzyme family that includes lipoamide dehydrogenase, glutathione reductase and mercu
44 c uptake regulatory repressor, and possibly, lipoamide dehydrogenase, the L protein component of the
45  never been observed before in any wild-type lipoamide dehydrogenase.
46 efficiently reduced by NADH-dependent bovine lipoamide dehydrogenase.
47 d, including xanthine oxidase (XO)/xanthine, lipoamide dehydrogenase/ NADH, isolated mitochondria, mi
48 has two genes encoding for two mitochondrial lipoamide dehydrogenases.
49 f NADH and thio-NAD(+) in the absence of D,L-lipoamide, demonstrated that the enzyme uses a ping-pong
50  aureus cells experiencing a high demand for lipoamide-dependent enzymes.
51                                Likewise, the lipoamide derivative was efficiently reduced by NADH-dep
52 ass spectral analysis of the lipoic acid and lipoamide derivatives confirmed both the expected molecu
53 ions of enzyme redox states as a function of lipoamide/dihydrolipoamide, NAD(+)/NADH, and pH.
54 vior, which is modulated by the redox-active lipoamide dithiolane ring.
55  revealed that Zn(2+) competes with oxidized lipoamide for the two-electron-reduced enzyme.
56 ion and acetylation of the L1 domain or free lipoamide increased kinase activity, those modifications
57                                        Thus, lipoamide is a well-tolerated small-molecule modulator o
58 /- 0.15, (D)V(app) = 1.05 +/- 0.07] when D,L-lipoamide is the oxidant but large and equivalent [(D)(V
59 ative half-reactions, respectively, when D,L-lipoamide is the oxidant.
60 ew vinylchlorine-containing metabolites, the lipoamides janthielamide A and kimbeamides A-C and the k
61 d by the recombinant enzyme as assessed by a lipoamide-lipoamide dehydrogenase-coupled assay.
62 hanges in reduction and acetylation state of lipoamide moieties set by the NAD(+)/NADH ratio.
63  the lipoylated peptide, suggesting that the lipoamide moiety plays a marginal role within the autore
64 a proton donor in the reductive acylation of lipoamide on the lipoyl-bearing domain.
65 alyzed by lipoamide dehydrogenase and either lipoamide or DlaT (SucB).
66 lting proteins for their ability to catalyze lipoamide reduction/oxidation alone and in complex with
67                                        These lipoamides represent the newest additions to a relativel
68 ed LA production and decreased activities of lipoamide-requiring enzymes.
69 alloxan, dehydroascorbate, DTNB, lipoic acid/lipoamide, S-nitrosoglutathione, selenodiglutathione, se
70       Thermal proteome profiling showed that lipoamide stabilizes intrinsically disordered domain-con
71 uorothioamidyl lysine adducts identified the lipoamide succinyltransferase and dihydrolipoamide dehyd
72 . aureus when growth is heavily reliant upon lipoamide-utilizing enzymes, but dispensable when this r
73 s and the R,S-(+/-) racemic mixture of LA or lipoamide, we identified the biologically active form of