ライフサイエンスコーパス: NADH

1 NADH and its oxidized form NAD(+) have a central role in

2 NADH ED-FRAP parameters were optimized to deliver 23.8 m

3 NADH production rate was significantly higher in every p

4 NADH-ubiquinone oxidoreductase (complex I) is the larges

5 NADH:ubiquinone-1 activities in the reconstituted membra

6 Escherichia coli lactate dehydrogenase as an NADH scavenger, thereby preventing reversible formaldehy

7 second gene of the hcp-hcr operon encodes an NADH-dependent reductase, Hcr.

8 H2 -dependent monooxygenase that requires an NADH:FMN oxidoreductase (EmoB) to provide FMNH2 as a cos

9 photocurrent of the nanostructures shows an NADH-dependent magnitude.

10 To increase methanol consumption, an "NADH Sink" was created using Escherichia coli lactate de

11 acids in cytochrome c oxidase subunit 1 and NADH dehydrogenase subunit 5.

12 ltaneous cytosolic pyruvate accumulation and NADH depletion, suggesting the involvement of mitochondr

13 HKCs correlating with an increase in ATP and NADH levels.

14 rial genes, namely, cytochrome b (CYT B) and NADH dehydrogenase subunit 2 (ND2), from 383 archived sp

15 ticle-associated heterotrophic bacteria, and NADH-oxidizing enzymes.

16 inducing factor (AIF), an FAD-containing and NADH-specific oxidoreductase critically important for en

17 identified (cytochrome oxidase 2 (COX2) and NADH:ubiquinone oxidoreductase core subunit 4 (MT-ND4))

18 e of persulfide sulfur also requires GTP and NADH, probably mediated by a GTPase and a reductase, res

19 Sensitivity of NAD(+) and NADH to cKO or cNAMPT was observed, as anticipated.

20 icotinamide adenine dinucleotide (NAD(+) and NADH) and nicotinamide adenine dinucleotide phosphate (N

21 icotinamide adenine dinucleotide (NAD(+) and NADH), oxidized and reduced forms of nicotinamide adenin

22 oxia, accompanied by increased free NADH and NADH/NAD(+) ratios.

23 affecting the pools of ferredoxin, NADPH and NADH, as well as influencing metabolic pathways and thio

24 orrecting imbalanced production of NADPH and NADH, were enabled by direct mutations to the transhydro

25 on spectral profile levels of tryptophan and NADH were higher in AD samples than normal samples.

26 Mitochondrial complex I (also known as NADH:ubiquinone oxidoreductase) contributes to cellular

27 agweed pollen allergen repertoire as well as NADH oxidases are present in SPP, highlighting an import

28 the absence of a functional malate-aspartate NADH shuttle caused by aralar/AGC1 disruption causes a b

29 the regulatory step in the malate-aspartate NADH shuttle, MAS.

30 regenerate important cofactors, such as ATP, NADH, and NADPH.

31 lism have called out three metabolites: ATP, NADH, and acetyl-CoA, as sentinel molecules whose accumu

32 analyses largely leave out how and why ATP, NADH, and acetyl-CoA (Figure 1 ) at the molecular level

33 energy released by electron transfer between NADH and ubiquinone (UQ) to pump sodium, producing a gra

34 complex I couples electron transfer between NADH and ubiquinone to proton translocation across an en

35 ASQ generated photochemically in bifurcating NADH-dependent ferredoxin-NADP(+) oxidoreductase and the

36 the short lifetime of the ASQ of bifurcating NADH-dependent ferredoxin-NADP(+) oxidoreductase I and c

37 y in live cells, we show that free and bound NADH are compartmentalized inside of the nucleus, and it

38 unding stroma, many show a higher free/bound NADH ratio consistent with their known preference for ae

39 cence (usually associated with protein-bound NADH conformations) separately from the autofluorescence

40 t shift in the contribution of protein-bound NADH towards free NADH, indicating increased glycolysis-

41 es the nuclear organization of protein-bound NADH.

42 the concomitant reduction of crotonyl-CoA by NADH, a process called electron bifurcation.

43 tion of dihydroxyacetone phosphate (DHAP) by NADH, and there is a 6.7 kcal/mol stabilization of this

44 ze the endergonic reduction of ferredoxin by NADH, which is also driven by the concomitant reduction

45 the irreversible reduction of flavodoxin by NADH to the blue semiquinone.

46 fore cannot be used to measure inhibition by NADH.

47 a, driven by the reduction of quinone (Q) by NADH.

48 eraction between QD-GNP pair was unlocked by NADH leading to QD fluorescence turn-on.

49 To assess this methodology, cardiac NADH and NAD(+) ratios/pool sizes were measured using mo

50 ycling the two other primary redox carriers, NADH and ferredoxin.

51 ing subunits of mitochondrial complex I (CI; NADH:ubiquinone oxidoreductase), the first enzyme of the

52 lting in the simple equation: crotonyl-CoA + NADH + H(+) = butyryl-CoA + NAD(+) with Km = 1.4 mum fer

53 We show that the binding of the coenzyme NADH alone or in concert with GTP results in a binary mi

54 dated by honey oxidising the enzyme cofactor NADH.

55 accharomyces cerevisiae initiates collective NADH dynamics termed glycolytic oscillations.

56 ic reticulum (ER), display elevated combined NADH and NADPH (i.e., NAD(P)H) autofluorescence.

57 p activation of particular OXPHOS complexes, NADH supply and glycolysis, and strong (third-order) gly

58 e respiratory chain dehydrogenase component, NADH:menaquinone oxidoreductase (Ndh) of Mycobacterium t

59 n AMPK activity, Akt activity, and cytosolic NADH/NAD(+) redox state were temporally linked in indivi

60 r AMPK activity, Akt activity, and cytosolic NADH/NAD(+) redox.

61 tling of reducing equivalents from cytosolic NADH to the mitochondrial respiratory chain via the D-la

62 red the transport and oxidation of cytosolic NADH in the mitochondria, resulting in altered cytosolic

63 MAS is used to oxidize cytosolic NADH in mitochondria, a process required to maintain oxi

64 mediated by GAD1, we monitored the cytosolic NADH:NAD(+) equilibrium in tumor cells.

65 al activity through effects on the cytosolic NADH:NAD(+) ratio and the NAD(H) sensitive transcription

66 y responses through effects on the cytosolic NADH:NAD+ ratio and the NAD(H)-sensitive transcription c

67 Of note, it decreased NADH-ubiquinone reductase activity but not the activity

68 est producer were reduced owing to decreased NADH oxidization by aerobic respiration.

69 Decreasing NADH pharmacologically with MTOB or genetically blocking

70 tidylyltransferase, CDP-Glc 4,6-dehydratase, NADH-dependent SAM:C-methyltransferase, and NADPH-depend

71 se conditions is related to Mg(2+)-dependent NADH generation by malic enzyme.

72 The sodium-dependent NADH dehydrogenase (Na(+)-NQR) is a key component of the

73 ed form of nicotinamide adenine dinucleotid (NADH) ratio and the NAD(+)-dependent deacetylase activit

74 ies (beta-nicotinamide adenine dinucleotide (NADH) and H2O2) acting as coreactants for the ECL emissi

75 g reduced nicotinamide adenine dinucleotide (NADH) as the cofactor.

76 Reduced nicotinamide adenine dinucleotide (NADH) can generate a ruthenium-hydride intermediate that

77 cofactor nicotinamide adenine dinucleotide (NADH) is a possible hydride source inside the cell based

78 Nicotinamide Adenine Dinucleotide (NADH) is an important coenzyme in the human body that pa

79 , reduced nicotinamide adenine dinucleotide (NADH), and flavin denine dinucleotide (FAD) in fresh bra

80 ibuted to nicotinamide adenine dinucleotide (NADH), was induced by two-photon laser excitation and it

81 opment of nicotinamide adenine dinucleotide (NADH)-based biosensors.

82 d form of nicotinamide adenine dinucleotide (NADH).

83 ratio of nicotinamide adenine dinucleotide (NADH/NAD(+) ratio) and protein acetylation in the failin

84 onooxygenase activity; however, it displayed NADH:quinone reductase and a small NADH:oxidase activity

85 NDUFAF6 encodes NADH:ubiquinone oxidoreductase complex assembly factor 6

86 he Streptococcus sanguinis nox gene encoding NADH oxidase is involved in both competition with Strept

87 mutation in the mitochondrial gene encoding NADH:ubiquinone oxidoreductase subunit 4 (ND4).

88 uter membrane protein X), and nuoN (encoding NADH:ubiquinone oxidoreductase); 2) by investigating co-

89 All require oxygen [8] and energy (NADH or NADPH) for bioluminescence and are reported to e

90 cidated recently for the flavin-based enzyme NADH-dependent ferredoxin NADP(+) oxidoreductase I (NfnI

91 Replenishment of epicardial NADH fluorescence was then imaged using low intensity UV

92 ntensity UV pulses to photobleach epicardial NADH.

93 drug isoniazid, which inhibits the essential NADH-dependent enoyl-acyl-carrier protein (ACP) reductas

94 ng on gene transcription, enzyme expression, NADH/NAD(+) ratio, and metabolite concentration was also

95 s fluorescence from the metabolic co-factors NADH and FAD with quantitation from Fluorescence Lifetim

96 ry cortex was assessed by measuring the FAD+/NADH ratio using fluorescence imaging.

97 In the presence of FMN, NADH, and flavin reductase, which reduces FMN to FMNH2 u

98 nt of InhA results in increased affinity for NADH and DD-CoA turnover but with a reduction in Vmax fo

99 ) and compared these plants with ndufs4 (for NADH:ubiquinone oxidoreductase Fe-S protein4) mutants po

100 absence of the catalytic subunit NDUFV1 (for NADH:ubiquinone oxidoreductase flavoprotein1) and compar

101 The extrinsic arm contains binding sites for NADH, the primary electron acceptor FMN, and seven iron-

102 Firstly, NiO-FET was tested for NADH detection showing a linear concentration range 1aM

103 n of NAD(+) by dehydrogenase enzymes to form NADH is a key component of cellular metabolism.

104 eotide (NAD(+)) to that of its reduced form (NADH) is less clear.

105 We used a water-forming NADH oxidase from Lactobacillus brevis (LbNOX) as a gene

106 er lifetime shift occurs towards higher free NADH suggesting a possible synergism between metabolic d

107 nder normoxia, accompanied by increased free NADH and NADH/NAD(+) ratios.

108 d a significant shift towards increased free NADH, indicating an increased glycolytic state for cells

109 is is coupled with an increased pool of free NADH, increased mitochondrial biogenesis, triggering of

110 tribution of protein-bound NADH towards free NADH, indicating increased glycolysis-mediated metabolic

111 To uncouple biosynthesis from NADH generation cancer cells can synthesize lipids from

112 glycolysis and uncoupling biosynthesis from NADH generation.

113 It funnels electrons coming from NADH and ubiquinol to cytochrome c, but it is also capab

114 aleic anhydride using electrons derived from NADH and transferred through a ferredoxin and ferredoxin

115 ratory chain and diversion of electrons from NADH oxidoreductases to oxygen.

116 gy production by transferring electrons from NADH to ubiquinone coupled to proton translocation acros

117 ratory enzyme that conserves the energy from NADH oxidation by ubiquinone-10 (Q10) in proton transpor

118 nters by accepting reducing equivalents from NADH.

119 using the energy from electron transfer from NADH to ubiquinone-10 to drive protons across the energy

120 le in reverse electron transport to generate NADH.

121 ith synthetic pathways converting glycolytic NADH into the lipid biosynthetic precursors NADPH or ace

122 Both the [4-(2)H]NADH (NADD) kinetic isotope effect and the D2O solvent i

123 hypoglycemia through an increase in hepatic NADH, which inhibits hepatic gluconeogenesis by reducing

124 A homologous NADH:quinone oxidoreductase complex IA likely operates i

125 Mitochondrial complex I (NADH dehydrogenase) is a major contributor to neuronal e

126 Complex I (NADH ubiquinone oxidoreductase) in mammalian mitochondri

127 Complex I (NADH ubiquinone oxidoreductase) is a large multisubunit

128 Energy-transducing respiratory complex I (NADH:ubiquinone oxidoreductase) is one of the largest an

129 Respiratory complex I (NADH:ubiquinone oxidoreductase), one of the largest memb

130 Complex I (NADH:ubiquinone oxidoreductase), one of the largest memb

131 d intact cell respiration, reduced complex I/NADH oxidase activity and electron leak occurring at com

132 Furthermore, we also identified NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subun

133 Type II NADH:quinone oxidoreductase (NDH-2) is central to the re

134 necessary and sufficient to drive changes in NADH.

135 of NADH oxidation, as further increases in [NADH] elevate ubiquinol-related complex III reduction be

136 Increased NADH/NAD(+) and protein hyperacetylation, previously obs

137 urther inactivate Sirt3 because of increased NADH (nicotinamide adenine dinucleotide, reduced form) a

138 tylase of the same class, does not influence NADH nuclear localization.

139 re, inactive P5CDH and PRODH mutants inhibit NADH production and increase trapping of the P5C interme

140 on of ADH and ethanol transforms NAD(+) into NADH, which causes a decrease in the OECT source drain c

141 e FAD(HI) and demonstrated a glycolytic-like NADH-FLIM signature that was readily separated from the

142 Elevated matrix NADH, in turn, diminished the cytosolic NAD(+)/NADH rati

143 I-supported respiration by leakage of matrix NADH.

144 restingly, despite failing to restore matrix NADH/NAD balance, pyruvate does increase aspartate, like

145 veal a connection between NAD(+) metabolism, NADH distribution, and SIRT1 activity in the nucleus of

146 cription factor Nrf2 increased mitochondrial NADH levels and restored mitochondrial membrane potentia

147 ial for the translation of the mitochondrial NADH dehydrogenase subunit7 (nad7) mRNA.

148 Moreover, NADH binding significantly affected EcAhpF flexibility a

149 ng mitochondrial genes encoded in the mtDNA [NADH dehydrogenase 6 (ND6) and cytochrome c oxidase subu

150 Multiple NADH dehydrogenases, transcription factors of unknown fu

151 verall, our results indicate that myocardial NADH ED-FRAP is a useful optical non-destructive approac

152 plex I dysfunction, as well as lower NAD(+) /NADH ratio and ATP content.

153 Consistently, lower NAD(+) /NADH ratio was observed during hyperammonaemia with redu

154 ts between the intramitochondrial [NAD(+) ]/[NADH] pool to molecular oxygen, with irreversible reduct

155 by the PO2 and intramitochondrial [NAD(+) ]/[NADH].

156 t that it helps readjust the cellular NAD(+)/NADH balance when perturbed by different stimuli.

157 mononucleotide restored the cellular NAD(+)/NADH ratio and normalized the CypD-deficient phenotype.

158 indicators and metabolites: cytosolic NAD(+)/NADH ratio (inferred from the dihydroxyacetone phosphate

159 DH, in turn, diminished the cytosolic NAD(+)/NADH ratio and triggered a subsequent downregulation of

160 lock due to the inability to maintain NAD(+)/NADH homeostasis.

161 ing on the cytosolic or mitochondrial NAD(+)/NADH ratios.

162 an overall decrease in mitochondrial NAD(+)/NADH.

163 etailed protocol to image and monitor NAD(+)/NADH redox state in living cells and in vivo using a hig

164 ysical behavior to that of the native NAD(+)/NADH.

165 and a role for a more oxidized state (NAD(+)/NADH) in the cytosol during GIIS that favors high glycol

166 compartment-specific increase of the NAD(+)/NADH ratio in human cells.

167 cribed the sirtuins as sensors of the NAD(+)/NADH ratio, but it has not been formally tested for all

168 tate of lipoamide moieties set by the NAD(+)/NADH ratio.

169 the sirtuins as direct sensors of the NAD(+)/NADH ratio.

170 ondrial energy production through the NAD(+)/NADH redox state and modulating cellular signaling proce

171 vate] ratio but not the whole-cell [NAD(+)]/[NADH] ratio.

172 porter or a redox shuttle by mediating a NAD/NADH exchange, but instead catalyzed the import of NAD i

173 sites are open to solvent, which allows NAD/NADH exchange to support multiple turnover.

174 catalyze pyridine-nucleotide-dependent (NAD/NADH) reduction of thiol residues in other proteins.

175 The up-regulation of NAD/NADH phosphorylation and dephosphorylation pathway, and

176 he import of NAD or CoA, the exchange of NAD/NADH, and the export of CoA.

177 muscle NAD in vivo does not perturb the NAD/NADH redox ratio.

178 on-bifurcating flavoproteins nitroreductase, NADH oxidase, and flavodoxin.

179 a demonstrate a clear benefit of normalizing NADH/NAD(+) imbalance in the failing hearts.

180 racterized occludin biochemically as a novel NADH oxidase that controls the expression and activation

181 We then tested the ability of NADH, ADP-ribose, and nicotinamide to inhibit these NAD(

182 tamine, leading to cytosolic accumulation of NADH and increased oxidative status.

183 e reductase activity but not the activity of NADH-ferricyanide reductase.

184 The activity of NADH:ubiquinone oxidoreductase (complex I) was inhibited

185 for the purpose of industrial application of NADH co-factor regeneration.

186 otifs of PA1024, which define a new class of NADH:quinone reductases and are present in more than 490

187 greater than the predicted concentrations of NADH in cells; therefore, our data indicate that NADH is

188 However, the inhibitory concentrations of NADH in these assays are far greater than the predicted

189 The impact of abnormal concentrations of NADH significantly causes different diseases in human bo

190 The amperometric detection of NADH at 0.200V showed a sensitivity of (217+/-3)microAmM

191 Electrochemical detection of NADH using bare electrode is a challenging task especial

192 -triggered photoelectrochemical detection of NADH.

193 This signal results from a drop of NADH levels and induction of mitochondrial ROS productio

194 esidues have allowed the electrooxidation of NADH at low potentials due to the catalytic activity of

195 effects are inhibited by forced elevation of NADH, reduced expression of CtBP, or transfection with a

196 nase (NNT) reduces NADP(+) at the expense of NADH oxidation and H(+) movement down the electrochemica

197 t on mtRNA expression and that expression of NADH dehydrogenase 1, 3, and 6 (ND-1, ND-3, ND-6) and AT

198 A new family of NADH dehydrogenases, the flavin oxidoreductase (FlxABCD,

199 changes between free and bound fractions of NADH as a indirect measure of metabolic alteration in li

200 e recovery after photobleaching (ED-FRAP) of NADH has been shown to be an effective approach for meas

201 termined by fluorescence lifetime imaging of NADH and kidney fibrosis determined by second harmonic i

202 piericidin, demonstrating the importance of NADH-related ubiquinone reduction for ROS production und

203 tered respiratory function, as inhibition of NADH dehydrogenase brought ROS levels back to wild-type

204 The kinetics of NADH synthesis and respiration, feedback from ATP hydrol

205 x I mitochondrial respiration due to lack of NADH for the electron transport chain.

206 ent investigations showed that the levels of NADH and NADPH diminish by up to approximately 50% withi

207 rameters provided repeatable measurements of NADH production rate during multiple metabolic perturbat

208 vated NOX4 activity accelerates oxidation of NADH and supports increased glycolysis by generating NAD

209 ate of ATP synthesis, driven by oxidation of NADH or succinate with different sections of the respira

210 a redox enzyme that may promote oxidation of NADH to facilitate enhanced glycolysis in the cytosol an

211 and oxidize NADH to NAD(+) The oxidation of NADH to NAD(+) was diminished in the nox mutant.

212 yruvate to lactate coupled with oxidation of NADH to NAD(+), plays a crucial role in the promotion of

213 ectron donor, mitoNEET mediates oxidation of NADH with a concomitant reduction of oxygen.

214 The oxidation of NADH, studied in most detail, is much faster at the lowe

215 ochondria by using the reducing potential of NADH to drive protons across the inner mitochondrial mem

216 tetrazolium to diformazan in the presence of NADH, indicating the formation of superoxide anion radic

217 target-induced consumption or production of NADH through cascade enzymatic reactions.

218 For maximal ROS production, the rate of NADH generation has to be equal or below that of NADH ox

219 effective approach for measuring the rate of NADH production to assess dehydrogenase enzyme activity.

220 based modified electrodes for the sensing of NADH.

221 hus, proteins and even molecules the size of NADH (663 Da) will be retained during these tPTP.

222 the slo3 mutant was defective in splicing of NADH dehydrogenase subunit7 (nad7) intron 2.

223 Whereas the structure of NADH in the active site is similar between the open and

224 orly characterized supernumerary subunits of NADH:ubiquinone oxidoreductase, known as complex I (cI),

225 peroxide, which required increased supply of NADH for respiratory chain oxidoreductases from central

226 generation has to be equal or below that of NADH oxidation, as further increases in [NADH] elevate u

227 asured in the forward direction, whereby one NADH is recycled, resulting in the simple equation: crot

228 and STD-NMR experiments did not show NAD or NADH exchange on the NMR timescale.

229 It functions by binding to either NAD(+) or NADH, thus inducing protein conformational changes that

230 nis could reduce oxygen to water and oxidize NADH to NAD(+) The oxidation of NADH to NAD(+) was dimin

231 perates in the opposite direction to oxidize NADH.

232 intracellular redox homeostasis by oxidizing NADH, our work suggests that phenazines may substitute f

233 ells are grown on oleate medium, peroxisomal NADH is reoxidised to NAD(+) by malate dehydrogenase (Md

234 The enzyme preferred NADH to NADPH as a reducing substrate.

235 pids from carbon sources that do not produce NADH in their catabolism, including acetate and the amin

236 esses small molecules as inputs and produces NADH as an output.

237 Mitochondrial proton-pumping NADH:ubiquinone oxidoreductase (respiratory complex I) c

238 e and oxidised (NAD+ and NADP+) and reduced (NADH) nicotinamide dinucleotides, which therapy decrease

239 nd provide a good reusability for repetitive NADH detection.

240 Mutations of respiratory NADH dehydrogenases prevent nitrotyrosine formation and

241 rescued by addition of products that restore NADH production.

242 ed recombinant ADHE catalyzed the reversible NADH-mediated interconversions of acetyl-CoA, acetaldehy

243 itrate synthase activity, rotenone-sensitive NADH oxidase activity, and proximal tubular mitochondria

244 displayed NADH:quinone reductase and a small NADH:oxidase activity.

245 at under these conditions calcium stimulates NADH synthesis in skeletal muscle mitochondria but not i

246 application of the phasor approach to study NADH fluorescence lifetime and emission allowed us to id

247 bioenergetic function could be supplemental NADH oxidation in cells.

248 ors, genes required for glutamine synthesis, NADH/NAD(P)H metabolism, as well as general DNA/RNA and

249 erted movement involving the NTD, C-terminal NADH, and FAD domains, and the flexible linker between t

250 ing equivalents 1000-fold more abundant than NADH, which would enable significantly greater H2O2 prod

251 We also found that NADH production rate remained significantly impaired aft

252 in cells; therefore, our data indicate that NADH is unlikely to inhibit sirtuinsin vivo These data s

253 und that the model accurately predicted that NADH depletion would delay clearance at low H2O2 concent

254 These data suggest that NADH binds to aggregated aS.

255 This suggests that NADH-binding geometry of InhA likely permits long-range

256 se conditions PntAB functions to balance the NADH: NADPH equilibrium specifically in the direction of

257 S transiently escapes from repression by the NADH-sensitive transcription factor Rex and binds to the

258 e show that human fibroblasts mutant for the NADH dehydrogenase (ubiquinone) Fe-S protein 1 (NDUFS1)

259 g-range interactions between residues in the NADH-binding pocket to facilitate substrate turnover in

260 roteins that was sensitive to changes in the NADH/NAD(+) ratio.

261 Changes in the NADH:NAD(+) ratio regulate CtBP binding to the acetyltra

262 yellow fluorescent protein (cpYFP) into the NADH-binding domain of Rex protein from Thermus aquaticu

263 glycolytic reprogramming and to measure the NADH/NAD(+) ratio in bovine and human adventitial fibrob

264 micking DNAzymes ("peroxidymes") mediate the NADH-driven oxidation of a colorless, nonfluorescent phe

265 Expression of the NADH sensor CtBP1 was increased in vivo and in vitro in

266 echanism involving increased activity of the NADH-sensitive transcriptional corepressor C-terminal bi

267 Ndufc2, a subunit of the NADH: ubiquinone oxidoreductase, plays a key role in the

268 Reduced glucose availability reduces the NADH:NAD(+) ratio, NF-kappaB transcriptional activity, a

269 PH/NADP(+) ratio severalfold higher than the NADH/NAD(+) ratio in the matrix.

270 rected mutagenesis was used to show that the NADH:quinone oxidoreductase complex IE was essential for

271 protein a series of mutants, targeted to the NADH co-factor binding pocket were created.

272 he relationship to O2(-) generated using the NADH/PMS method (R(2)=0.859).

273 celles") and is accelerated by light through NADH photochemistry.

274 Thus, NADH oxidase contributes to multiple phenotypes related

275 CP3 Tg mice, suggestive of a shift in tissue NADH/NAD(+) ratio.

276 5 A), bound to NAD(+) (1.45 A), and bound to NADH (1.79 A).

277 During this process, NAD(+) is reduced to NADH.

278 n deacylase activities showed sensitivity to NADH in this assay.

279 The intensity ratio of tryptophan to NADH and the change rate of fluorescence intensity with

280 ited a significant decrease in the NAD(+)-to-NADH ratio, which reflects the oxidative phosphorylation

281 ocatalytic activity of SWCNT-Polytyr towards NADH oxidation has also made possible the development of

282 lycolysis for energy generation and uncouple NADH generation from biosynthesis.

283 and major Amb a 1 allergens, and as unique, NADH dehydrogenases.

284 on reduce alpha-ketoglutarate to D-2HG using NADH and represent major intracellular sources of D-2HG

285 Isolated mitochondria were energised using NADH- or FADH2-linked substrates.

286 reductase, which reduces FMN to FMNH2 using NADH as the electron donor, mitoNEET mediates oxidation

287 thin the myocardium of perfused hearts using NADH ED-FRAP.

288 ng metabolic heterogeneity when imaged using NADH Fluorescent Lifetime Imaging Microscopy and, compar

289 respiration was higher in L rats when using NADH-linked substrates and these rats had lower serum gl

290 ially available enzymatic assay kits utilize NADH in their detection, this discovery will allow the t

291 n, the reduction of CO2 to formate utilizing NADH as electron donor, has been investigated.

292 d as compared with the wild-type enzyme when NADH is the substrate.

293 he analyte or biosensors by combination with NADH producing enzymes.

294 ophore has significant spectral overlap with NADH and therefore cannot be used to measure inhibition

295 The reductive half-reaction with NADH showed a kred value of 24 s(-1) and an apparent Kd

296 ts as an intermediate in this reaction, with NADH and NADPH (the reduced forms of nicotinamide adenin

297 reen for chelated Fe(III)-NTA reduction with NADH as electron donor, we have identified proteins from

298 itochondrial DNA: the matR gene found within NADH dehydrogenase 1 (nad1) intron 4.

299 restored by ectopic expression of the yeast NADH dehydrogenase Ndi1.

300 s rescued by bypassing complex I using yeast NADH dehydrogenase Ndi1.