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1 ycin A catalyzed by Aln4, an NADPH-dependent aldo-keto reductase.
2 a dimeric aldo-keto reductase or a family 2 aldo-keto reductase.
3 ing pocket that is more polar than a typical aldo-keto reductase.
4 ient binding of glutathione conjugates to an aldo-keto reductase.
6 nt from bacteria to mammals, and we identify aldo-keto reductase 1A1 as the mammalian functional anal
8 show that FXR induces expression of Akr1b7 (aldo-keto reductase 1b7) in murine small intestine, colo
10 Type 5 17beta-hydroxysteroid dehydrogenase, aldo-keto reductase 1C3 (AKR1C3) converts Delta(4)-andro
16 template for the homology modeling of other aldo/keto-reductase 4 family members, including the redu
17 d (2) it expresses alcohol dehydrogenase and aldo-keto reductase activity native to AdhD from Pyrococ
18 pe 3 3alpha-hydroxysteroid dehydrogenase, or aldo-keto reductase (AKR) 1C2, eliminates the androgen s
21 It is the only HSD of known structure in the aldo-keto reductase (AKR) superfamily and may provide a
23 , E.C. 1.1.1.213, AKR1C9) is a member of the aldo-keto reductase (AKR) superfamily which inactivates
24 ase isoforms (AKR1C1-AKR1C4), members of the aldo-keto reductase (AKR) superfamily, activate trans-di
25 ydrogenase (3 alpha-HSD/DD), a member of the aldo-keto reductase (AKR) superfamily, oxidizes PAH tran
28 d with recombinant rat liver 3 alpha-HSD, an aldo-keto reductase (AKR) that plays critical roles in s
29 servation indicates that Kvbeta resembles an aldo-keto reductase (AKR), an enzyme that catalyzes a re
30 Aldose reductase (ALR2), a NADPH-dependent aldo-keto reductase (AKR), is widely distributed in mamm
35 g carcinoma, differential display shows that aldo-keto reductase (AKR1C) transcripts are dramatically
38 show that four homogeneous human recombinant aldo-keto reductases (AKR1C1-AKR1C4) are regioselective
39 for monitoring the activity of the inducible aldo-keto reductases AKR1C2 and AKR1C3 in living human c
40 d isoform-selective (1500-fold) inhibitor of aldo-keto reductase AKR1C3: a target of interest in both
41 Dihydrodiol dehydrogenases are a family of aldo-keto reductases (AKR1Cs) involved in the metabolism
45 on of intermediate PAH trans-dihydrodiols by aldo-keto reductases (AKRs) leads to the formation of el
46 PAH-diols can be converted to o-quinones by aldo-keto reductases (AKRs) or to diol-epoxides by cytoc
48 dihydrodiol dehydrogenase (DD) isoforms are aldo-keto reductases (AKRs) that activate polycyclic aro
49 rodiol proximate carcinogens are oxidized by aldo-keto reductases (AKRs) to their corresponding react
50 zo[a]pyrene (B[a]P-7,8-trans-dihydrodiol) by aldo-keto reductases (AKRs) to yield benzo[a]pyrene-7,8-
52 hydroxy-7,8-dihydroB[a]P by the mediation of aldo-keto reductases and its role in the genotoxicity an
53 ining substrate and inhibitor specificity of aldo-keto reductases and specifically identifies Arg311
54 rgeted for deletion: three genes that encode aldo-keto reductases and three genes that encode alcohol
55 tic hydrocarbon (PAH) o-quinones produced by aldo-keto reductases are ligands for the aryl hydrocarbo
56 d role for the metabolic enzymes enolase and aldo-keto reductase as positive and negative regulators
57 ydroxysteroid dehydrogenase (3alpha-HSD), an aldo-keto reductase, binds NADP(+) in an extended anti-c
65 hesis of androgens (5alpha-reductase/SRD5A1, aldo-keto reductase family 1 member C3/AKR1C3), b) estab
66 ce of marker proteins for renin cells (e.g., aldo-keto reductase family 1, member 7 and connexin 40)
68 sponding gene revealed that a protein of the aldo-keto reductase family carries out this reaction in
69 s high sequence identity with the genes from aldo-keto reductase family of proteins including the mou
75 xylose-pathway gene, a novel homolog of the aldo-keto reductase gene GRE3, while a second locus cont
76 sine residue found in the active site of all aldo-keto reductases have wild-type trafficking characte
78 molecular rationale to explore the status of aldo-keto reductases in dysregulations of adipose tissue
79 revealed surprising structural homology with aldo-keto reductases, including a triosephosphate isomer
82 determined for a xylose reductase, a dimeric aldo-keto reductase or a family 2 aldo-keto reductase.
83 t throughout the remainder of the oligomeric aldo-keto reductases, predicting alternate modes of olig
84 ein has highest sequence similarity to other aldo-keto reductases, such as chalcone reductase, an enz
85 a mammalian HSD using rat 3alpha-HSD of the aldo-keto reductase superfamily (AKR1C9) with the substr
86 o all other characterized human genes of the aldo-keto reductase superfamily (aldose reductase, bile
87 n 3alpha-HSDs and 20alpha-HSDs belong to the aldo-keto reductase superfamily and share 67% amino acid
90 esidues as are found in other members of the aldo-keto reductase superfamily that are naturally able
93 ensitive K(+) (K(v)) channels belongs to the aldo-keto reductase superfamily, and the crystal structu
94 id reductase A (2,5-DKGR A), a member of the aldo-keto reductase superfamily, has been determined by
97 hydrogenase (3alpha-HSD/DD), a member of the aldo-keto reductase superfamily, inactivates circulating
98 e analyses showed M6PR to be a member of the aldo-keto reductase superfamily, which includes both ani
109 reated a fusion consisting of a thermostable aldo-keto reductase, two alpha-helical leucine zipper do
110 these reactions (fatty acid synthase, Fasp; aldo-keto reductase, Ypr1p; alpha-acetoxy ketone reducta
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