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1 -1-phosphate to ethanolamine phosphate and a fatty aldehyde.
2 at this neutral lipid product was a 2-chloro-fatty aldehyde.
3 to phosphoethanolamine and the corresponding fatty aldehydes.
4 s, resulting in the production of brominated fatty aldehydes.
5 ulting in the production of novel brominated fatty aldehydes.
6 lting in the production of novel chlorinated fatty aldehydes.
7 rate specificity of FALDH towards long-chain fatty aldehydes.
8 cells to the cytotoxic effects of long chain fatty aldehydes.
9  to identify and quantitate the alpha-chloro fatty aldehyde, 2-chlorohexadecanal, in atherosclerotic
10 he 16- and 18-carbon-containing alpha-chloro fatty aldehydes, 2-chlorohexadecanal and 2-chlorooctadec
11 he desired physicochemical properties (e.g., fatty aldehydes, alkanes, and alcohols), further convers
12 vinyl ether bond of lysoplasmalogen, forming fatty aldehyde and glycerophosphoethanolamine or glycero
13 e utilisation BMC with different short-chain fatty aldehydes and show that it has activity against su
14 age of plasmalogens, liberating alpha-chloro fatty aldehydes and unsaturated lysophosphatidylcholine
15   The resultant species formed, alpha-chloro fatty aldehydes and unsaturated lysophospholipids, posse
16 ents were designed to show that alpha-chloro fatty aldehydes are produced by activated neutrophils an
17  wild-type cells was most obvious when using fatty aldehydes between 14 and 20 carbons, with the grea
18                                              Fatty aldehydes can undergo biotransformation to fatty a
19         Plasmalopsychosine, a characteristic fatty aldehyde conjugate of beta-galactosylsphingosine (
20 onsistent with the production of a 16-carbon fatty aldehyde containing one chlorine atom.
21 ction of a fatty alcohol oxidase (FAO) and a fatty aldehyde dehydrogenase (FADH) before they can be b
22   SLS patients have a profound deficiency in fatty aldehyde dehydrogenase (FALDH) activity.
23                             Mutations in the fatty aldehyde dehydrogenase (FALDH) gene cause Sjogren-
24 ations in the gene coding for membrane-bound fatty aldehyde dehydrogenase (FALDH) lead to toxic accum
25 ation, spasticity, and deficient activity of fatty aldehyde dehydrogenase (FALDH).
26  to (2E)-hexadecenoic acid by the long-chain fatty aldehyde dehydrogenase ALDH3A2 (also known as FALD
27                     Specifically, it was the fatty aldehyde dehydrogenase component that was affected
28                             Mutations in the fatty aldehyde dehydrogenase gene (ALDH10) are responsib
29     To test the possible role of AasS in the fatty aldehyde-dependent bioluminescence pathway of V. h
30 ic metabolites is produced from alpha-chloro fatty aldehydes derived from reactive chlorinating speci
31 s aldehydes, alcohols, lactones, terpenoids, fatty aldehydes, fatty acids and hydrocarbons.
32  of hydrocarbon biosynthesis from long-chain fatty aldehydes has remained mysterious.
33                        Recently alpha-chloro fatty aldehydes have been shown to be products of reacti
34 nyl ether) in the substrate because the free fatty aldehyde, hexadecanal, was not converted to 2-chlo
35 membrane plasmalogens releasing alpha-chloro fatty aldehydes including 2-chlorohexadecanal (2-ClHDA),
36 d plasmalogens to generate alpha-chlorinated fatty aldehydes, including 2-chlorohexadecanal.
37 e reduction of acyl-CoA to the corresponding fatty aldehyde, indicating that the gene encodes a novel
38 ntadecane production pathway that contains a fatty aldehyde intermediate, as well as three and four e
39 ) lyase to produce phosphoethanolamine and a fatty aldehyde is the final degradative step in the sphi
40 otaxis in vitro suggesting that alpha-chloro fatty aldehydes may have a role in neutrophil recruitmen
41 he phosphatidylethanolamine was found in the fatty aldehyde-modified form in FAA.K1A, although this w
42               We propose a possible role for fatty aldehydes, or other aldehydic species, in mediatin
43 aking them elusive and rendering the task of fatty aldehyde quantitation challenging.
44 e decarbonylase (AD) catalyzes conversion of fatty aldehydes (R-CHO) to alka(e)nes (R-H) and formate.
45  active on very-long-chain fatty alcohol and fatty aldehyde substrates, respectively, and have bioche
46 calactone), fatty acids (hexadecanoic acid), fatty aldehydes (tetracosanal and octacosanal), hydrocar
47 hanism of C1-C2 bond cleavage by cAD using a fatty aldehyde that incorporates a cyclopropyl group, wh
48 r and other tissues to prevent toxicity from fatty aldehydes that are generated from oxidation of uns
49  resulting in the production of alpha-chloro fatty aldehydes that may enhance the recruitment of neut
50                ADO catalyzes conversion of a fatty aldehyde to the corresponding alk(a/e)ne and forma
51 n oxygenase that catalyzes the conversion of fatty aldehydes to alkanes and formate.
52 ylating oxygenase (cADO) converts long-chain fatty aldehydes to alkanes via a proposed diferric-perox
53 ylases (ADs) catalyze the conversion of C(n) fatty aldehydes to formate (HCO(2)(-)) and the correspon
54 version of saturated or monounsaturated C(n) fatty aldehydes to formate and the corresponding C(n-1)
55 .K1A cells were unable to convert long chain fatty aldehydes to the corresponding fatty acids.
56 n FAldDH- cell lines, addition of long chain fatty aldehydes to the medium caused a dramatic increase
57 ect pentafluorobenzyl oximes of alpha-chloro fatty aldehydes utilizing negative ion chemical ionizati
58 etected in FAldDH- cells even when exogenous fatty aldehydes were not added to the medium.
59                    In contrast, alpha-chloro fatty aldehydes were not produced in phorbol myristate a

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