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1 nicotinamide adenine dinucleotide), and FAD (flavin adenine dinucleotide).
2 e and has stoichiometric amounts of heme and flavin adenine dinucleotide.
3 active oxygen species (ROS) formation at the flavin adenine dinucleotide.
4 adenylate cofactors NAD(P), coenzyme A, and flavin adenine dinucleotide.
5 with potential binding sites for NAD(P)H and flavin adenine dinucleotide.
6 d a molecular weight of 22,000 and contained flavin adenine dinucleotide.
7 ion of nicotinamide adenine dinucleotide and flavin adenine dinucleotide.
8 e dehydrogenase with a bicovalently attached flavin adenine dinucleotide.
9 e flavin coenzymes flavin mononucleotide and flavin adenine dinucleotide.
10 spectra of ALR bound to oxidized and reduced flavin adenine dinucleotide.
11 rescent metabolic coenzymes reduced NADH and flavin adenine dinucleotide.
12 to coenzyme forms flavin mononucleotide and flavin adenine dinucleotide.
13 th stoichiometric amounts of the chromophore flavin-adenine dinucleotide.
15 ineages, whereas redox and light sensing via flavin adenine dinucleotide and flavin mononucleotide co
17 ers also formed in mutants that did not bind flavin adenine dinucleotide and in truncated peptides wi
18 ructure harbors typical FMO aspects with the flavin adenine dinucleotide and NAD(P)H binding domains
19 nent, was found to contain approximately one flavin adenine dinucleotide and one ferredoxin-type [2Fe
20 ites across the two molecules, involving the flavin adenine dinucleotide and substrate-binding pocket
21 revealed that the two well-known cofactors, flavin adenine dinucleotide and the photoantenna 6,7-dim
22 li, was shown to possess noncovalently bound flavin adenine dinucleotide and to exhibit L-2-hydroxygl
23 n glucose oxidase, electron transfer between flavin-adenine-dinucleotide and tryptophan(s)/tyrosine(s
24 llular NADPH, across a chain comprising FAD (flavin adenine dinucleotide) and two haems, to reduce ex
26 factor in addition to a molybdenum cofactor, flavin adenine dinucleotide, and FeS centers, were purif
27 educed nicotinamide adenine dinucleotide and flavin adenine dinucleotide, and the absorption of cytoc
28 BLUF domains (sensors of blue light using flavin adenine dinucleotide) are a group of flavin-conta
29 ores (riboflavin, flavin mononucleotide, and flavin adenine dinucleotide) are notoriously similar eve
30 ated WC-1 and WC-2 confirmed that WC-1, with flavin adenine dinucleotide as a cofactor, is the blue l
31 the oxidation of d-lactate to pyruvate using flavin adenine dinucleotide as a cofactor; knowledge of
32 lation, it depends on magnesium and utilizes flavin adenine dinucleotide as substrate to attach the f
34 teine-to-serine substitution remote from the flavin adenine dinucleotide binding site decouples confo
35 ce of DWF1 shows significant similarity to a flavin adenine dinucleotide-binding domain conserved in
36 this family is that the sequence of the key flavin adenine dinucleotide-binding domain is split into
38 se-methanol-choline oxidoreductase family of flavin adenine dinucleotide-binding enzymes catalyzing h
40 mical studies reveal that M6766 binds to the flavin adenine dinucleotide-binding pocket in ERO1alpha
41 This gene is predicted to encode a conserved flavin adenine dinucleotide-binding protein involved in
42 hey had open reading frames that predicted a flavin adenine dinucleotide-binding site, multiple N-gly
44 utative redox active site CAVC as well as an flavin-adenine dinucleotide-binding domain are highly co
45 that the amino terminus domain of IrtA is a flavin-adenine dinucleotide-binding domain essential for
48 s a flavoprotein containing covalently bound flavin adenine dinucleotide, but no detectable heavy met
49 th the flavoprotein SdhA, directly bound the flavin adenine dinucleotide co-factor, and was required
50 hotoinduced electron transfer from a reduced flavin adenine dinucleotide cofactor (FADH(-)) to the bo
51 rified NDH-2 contains a non-covalently bound flavin adenine dinucleotide cofactor and oxidizes NADH w
52 clic electron transfer between the catalytic flavin adenine dinucleotide cofactor and the damaged DNA
53 ht activation, electron transfer between the flavin adenine dinucleotide cofactor and tryptophan resi
54 tate of the electron transport system via an flavin adenine dinucleotide cofactor bound to a PAS doma
56 the entire pH range under investigation, the flavin adenine dinucleotide cofactor of GOx changed dire
57 unohistochemistry, disrupts the light-driven flavin adenine dinucleotide cofactor photoreduction, pro
59 hat the compound interacts directly with the flavin adenine dinucleotide cofactor, blocking the menaq
60 tors but unique in having a PAS domain and a flavin-adenine dinucleotide cofactor that is postulated
61 cotinamide adenine dinucleotide and oxidized flavin adenine dinucleotide cofactors we use optical ima
63 The acyl-CoA dehydrogenases are a family of flavin adenine dinucleotide-containing enzymes that cata
67 ned to flavin absorption and conjugated with flavin adenine dinucleotide, creating a nanoagonist capa
69 Here we report the identification of a novel flavin adenine dinucleotide-dependent amine oxidase (ren
71 ression of whiE ORFVIII, encoding a putative flavin adenine dinucleotide-dependent hydroxylase that c
72 e cytochrome P450 monooxygenase (TamI) and a flavin adenine dinucleotide-dependent oxidase (TamL), wh
73 midine/spermine N1-acetyltransferase and the flavin adenine dinucleotide-dependent polyamine oxidase
74 talyses removal of H3K4me2/H3K4me1 through a flavin-adenine-dinucleotide-dependent oxidation reaction
75 , such as LOV and BLUF (blue-light-utilizing flavin adenine dinucleotide) domains, cryptochromes, and
76 a DSOR-like charge transfer interaction with flavin adenine dinucleotide, eliminating the need for cy
78 .1 atom/mol), Fe (21 +/- 1.6 atoms/mol), and flavin adenine dinucleotide (FAD) (0.83 +/- 0.1 mol/mol)
79 ltage sensing (LOV) and Blue-Light-Utilizing flavin adenine dinucleotide (FAD) (BLUF) domains represe
80 is required for formation of C4a-hydroperoxy flavin adenine dinucleotide (FAD) (FAD(C4aOOH)), a key f
81 ced nicotine adenine dinucleotide (NADH) and flavin adenine dinucleotide (FAD) - is demonstrated.
82 ively reported based on enzyme sensors using flavin adenine dinucleotide (FAD) -dependent d-amino aci
83 tion of the histone tail lysine (H3K4), with flavin adenine dinucleotide (FAD) acting as cofactor.
84 nzyme activity by forming a compact N-formyl flavin adenine dinucleotide (FAD) adduct that spares the
85 at contain noncovalently or covalently bound flavin adenine dinucleotide (FAD) analogues were studied
86 ophilum at 1.6 A resolution, in complex with flavin adenine dinucleotide (FAD) and a bacterial lipid.
87 activated electron-transfer reaction between flavin adenine dinucleotide (FAD) and a chain of tryptop
88 se is a homodimeric flavoenzyme containing a flavin adenine dinucleotide (FAD) and a redox-active dis
89 etrahydrofolate (CH(2)THF), while MnmG binds flavin adenine dinucleotide (FAD) and a reduced nicotina
90 ve a common structural fold, a dependence on flavin adenine dinucleotide (FAD) and an internal photoa
91 nt HlmI was purified from E. coli with bound flavin adenine dinucleotide (FAD) and converts reduced h
92 also contain other metabolite caps including flavin adenine dinucleotide (FAD) and dephosphoCoA (dpCo
94 s soluble and contains an equimolar ratio of flavin adenine dinucleotide (FAD) and flavin mononucleot
96 vin as the direct precursor of the cofactors flavin adenine dinucleotide (FAD) and flavin mononucleot
98 ia a light-driven hydrogen-bond switch among flavin adenine dinucleotide (FAD) and glutamine and tyro
100 de ring opening reactions in the presence of flavin adenine dinucleotide (FAD) and nicotinamide adeni
101 the formation of the essential flavocoenzyme flavin adenine dinucleotide (FAD) and plays an important
102 interactions on the stabilization of reduced flavin adenine dinucleotide (FAD) and substrate/product
103 ns in the dihedral and librational angles of flavin adenine dinucleotide (FAD) and tryptophan (Trp) r
104 flux between flavin mononucleotide (FMN) and flavin adenine dinucleotide (FAD) and/or the electron ac
107 yglutamate (MTHF) and the catalytic cofactor flavin adenine dinucleotide (FAD) are noncovalently boun
111 al to the molecular clock using a pterin and flavin adenine dinucleotide (FAD) as chromophore/cofacto
113 nstead methylenetetrahydrofolate and reduced flavin adenine dinucleotide (FAD) as essential cofactors
114 heir interactions and the functional role of flavin adenine dinucleotide (FAD) binding in CRYs remain
115 t DntB contains the highly conserved ADP and flavin adenine dinucleotide (FAD) binding motifs charact
116 rs of electrons requiring photoactivation of flavin adenine dinucleotide (FAD) bound near a triad of
117 oS contains a flavin cofactor, identified as flavin adenine dinucleotide (FAD) by fluorescence spectr
118 purified PrnF protein catalyzes reduction of flavin adenine dinucleotide (FAD) by NADH with a k(cat)
119 s sheds light on the early events around the Flavin Adenine Dinucleotide (FAD) chromophore in the lig
121 produce type II symptoms occur close to the flavin adenine dinucleotide (FAD) cofactor binding site.
122 , cycles of reduction and reoxidation of the flavin adenine dinucleotide (FAD) cofactor depend on rat
123 ichia coli photolyase, photoreduction of the flavin adenine dinucleotide (FAD) cofactor in its neutra
124 en a spin label and an enzymatically reduced flavin adenine dinucleotide (FAD) cofactor in P. denitri
125 DHA(R451) so that covalent attachment of the flavin adenine dinucleotide (FAD) cofactor is supported.
128 , which lacks the covalent attachment to the flavin adenine dinucleotide (FAD) cofactor present in th
129 r, has a HAMP domain and a PAS domain with a flavin adenine dinucleotide (FAD) cofactor that senses t
130 homology region (PHR) carrying the oxidized flavin adenine dinucleotide (FAD) cofactor, and a crypto
135 formation of flavin mononucleotide (FMN) and flavin adenine dinucleotide (FAD) cofactors, is internal
136 are important redox enzymes that contain two flavin adenine dinucleotide (FAD) cofactors, with contra
138 hF) of p-cresol methylhydroxylase (PCMH) has flavin adenine dinucleotide (FAD) covalently tethered to
140 tone demethylase LSDl (KDMlA) belongs to the flavin adenine dinucleotide (FAD) dependent family of mo
141 adaic enzyme EIS sensor, which used DET-type flavin adenine dinucleotide (FAD) dependent glucose dehy
142 the cytoplasm, where the PAS (Per-ARNT-Sim)-flavin adenine dinucleotide (FAD) domain senses redox ch
143 on of the NAD(P)H domain with respect to the flavin adenine dinucleotide (FAD) domain that precludes
144 responses were matched by inverted biphasic flavin adenine dinucleotide (FAD) fluorescence transient
145 5'-nucleotidase, resulted in accumulation of flavin adenine dinucleotide (FAD) in culture supernatant
146 d ultrafast photoreduction of oxidized state flavin adenine dinucleotide (FAD) in subpicosecond and o
147 es a reaction in two parts: reduction of the flavin adenine dinucleotide (FAD) in the enzyme by reduc
148 reduction of FMN by electrons from NADPH and flavin adenine dinucleotide (FAD) in the reductase domai
153 we demonstrate that the cellular metabolite flavin adenine dinucleotide (FAD) is used as a non-canon
154 tive folding was shown to depend on cellular flavin adenine dinucleotide (FAD) levels but not on ubiq
155 nd that removal of the electron-transferring flavin adenine dinucleotide (FAD) moiety from both prote
157 t in addition to having a tightly associated flavin adenine dinucleotide (FAD) moiety, yeast Ero1p is
158 PA) capture probes prebound to electroactive flavin adenine dinucleotide (FAD) molecules, and a signa
160 studies of Aer suggested that it might use a flavin adenine dinucleotide (FAD) prosthetic group to mo
161 eductase (MMOR), which contains [2Fe-2S] and flavin adenine dinucleotide (FAD) prosthetic groups.
162 he active site, where a non-covalently bound flavin adenine dinucleotide (FAD) sits at the base of an
163 which covalently attach to the LSD1 cofactor flavin adenine dinucleotide (FAD) to inhibit demethylase
164 5 is required for the covalent attachment of flavin adenine dinucleotide (FAD) to protein Sdh1, a sub
165 ic dehydrogenase domain (DH(CDH)) containing flavin adenine dinucleotide (FAD), a cytochrome domain (
166 ia, with a decrease in the cellular level of flavin adenine dinucleotide (FAD), a metabolic cofactor
167 , shown to possess stoichiometric amounts of flavin adenine dinucleotide (FAD), and confirmed to have
168 asured the 2P-excitation spectra of NAD(P)H, flavin adenine dinucleotide (FAD), and lipoamide dehydro
169 P450-type heme, flavin mononucleotide (FMN), flavin adenine dinucleotide (FAD), and tetrahydrobiopter
170 but not by the addition of L-arginine, heme, flavin adenine dinucleotide (FAD), flavin mononucleotide
171 ps the excited state of the active cofactor, flavin adenine dinucleotide (FAD), in a highly bent geom
172 contains an N-terminal PAS domain that binds flavin adenine dinucleotide (FAD), senses aerotactic sti
173 enine dinucleotide (phosphate) (NAD(P)H) and flavin adenine dinucleotide (FAD), to assess the metabol
175 ith isotopically labeled riboflavin (Rf) and flavin adenine dinucleotide (FAD), which permit the firs
176 aks were due to the redox of enzyme cofactor flavin adenine dinucleotide (FAD), which was not the par
177 e atomic crystal structures of the catalytic flavin adenine dinucleotide (FAD)- and heme-binding doma
178 previously characterized BdlA homolog is the flavin adenine dinucleotide (FAD)-binding Aer, the redox
179 rochemical analysis of this and the isolated flavin adenine dinucleotide (FAD)-binding domain in the
180 oach yielded a polypeptide that included the flavin adenine dinucleotide (FAD)-binding domain of nNOS
181 esolution of the three domains of d-LDH: the flavin adenine dinucleotide (FAD)-binding domain, the ca
184 cytes deficient in flavin mononucleotide and flavin adenine dinucleotide (FAD)-collectively known as
187 ient composite for electron transfer between flavin adenine dinucleotide (FAD)-dependent glucose dehy
189 SgcC3 unveiled the following: (i) SgcC3 is a flavin adenine dinucleotide (FAD)-dependent halogenase;
191 w revealed that (i) SgcC is a two-component, flavin adenine dinucleotide (FAD)-dependent monooxygenas
192 line dehydrogenase domain that catalyzes the flavin adenine dinucleotide (FAD)-dependent oxidation of
193 ve evolved from an ancestor functioning as a flavin adenine dinucleotide (FAD)-dependent oxidocyclase
207 ced flavins (flavin mononucleotide [FMN] and flavin adenine dinucleotide [FAD]) and cob(III)alamin to
208 between VVD residue Cys108 and its cofactor flavin adenine dinucleotide(FAD), and prompts VVD switch
210 steady-state kinetic mechanism of the active flavin adenine dinucleotide-(FAD-) containing form of th
212 e (4HPA) 3-monooxygenase (HpaB) is a reduced flavin adenine dinucleotide (FADH(2)) utilizing monooxyg
214 ation of the enzyme indicated that a reduced flavin adenine dinucleotide (FADH2)-utilizing monooxygen
215 apparent molecular mass of 47 kDa, requires flavin adenine dinucleotide for activity, has NADH-speci
216 The dynamics of electron transfer to excited flavin adenine dinucleotide from a neighboring tyrosine
217 ERO1alpha followed by displacement of bound flavin adenine dinucleotide from the active site of the
218 explains why premixing of FDHs with reduced flavin adenine dinucleotide generally results in abolish
219 me composed of an Aspergillus flavus-derived flavin adenine dinucleotide glucose dehydrogenase (AfGDH
221 icotinamide adenine dinucleotide phosphate , flavin adenine dinucleotide , glutathione disulfide/glut
222 tes bind in close proximity to the catalytic flavin adenine dinucleotide group, substantial flexibili
223 he distance and orientation between MTHF and flavin adenine dinucleotide in At-Cry3 is similar to tha
224 s between the flavin and adenine moieties of flavin adenine dinucleotide in four redox forms of the o
227 to FMN (K(D) approximately 4 microM) than to flavin adenine dinucleotide (K(D) approximately 12 micro
229 a molecular mass of 45 kDa and contains one flavin adenine dinucleotide molecule per mole but lacks
230 icotinamide adenine dinucleotide (phosphate)/flavin adenine dinucleotide (NAD[P]H/FAD) autofluorescen
231 a protein complex composed of oxidoreductase flavin adenine dinucleotide/NAD(P)-binding subunit (Dred
232 degradation, likely due to the imbalance of flavin adenine dinucleotide/nicotinamide adenine dinucle
235 recognition coincided with the loss of FAD (flavin-adenine dinucleotide) recognition in all isolates
236 ne, which encodes a 399-amino-acid NAD+- and flavin adenine dinucleotide-requiring enzyme responsible
237 le recognition and segmentation based on the flavin adenine dinucleotide signal revealed that quantif
238 anaerobic levels, and binding of NADH to the flavin-adenine dinucleotide site seemed to prevent oxyge
242 ), also known as acetolactate synthase, is a flavin adenine dinucleotide-, thiamine diphosphate- and
243 ur subunits that contain a covalently linked flavin adenine dinucleotide, three different iron-sulfur
244 at m5U54 is added by the enzyme TrmFO using flavin adenine dinucleotide together with N5,N10-methyle
245 ed in the literature for flavodoxin and free flavin adenine dinucleotide were simulated based on sele
246 precursor of flavin mononucleotide (FMN) and flavin adenine dinucleotide, which are essential coenzym
247 ates in the Krebs cycle to generate NADH and flavin adenine dinucleotide, which are further oxidized