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                             44 gevonden resultaten
nr titel auteur tijdschrift jaar jaarg. afl. pagina('s) type
1 Alcohol dehydrogenase, SDR and MDR structural stages, present update and altered era Jörnvall, Hans
2015
234 C p. 75-79
5 p.
artikel
2 Aldehyde dehydrogenase homologous folate enzymes: Evolutionary switch between cytoplasmic and mitochondrial localization Krupenko, Natalia I.
2015
234 C p. 12-17
6 p.
artikel
3 Aldose reductase expression as a risk factor for cataract Snow, Anson
2015
234 C p. 247-253
7 p.
artikel
4 Aldose reductase inhibition alleviates hyperglycemic effects on human retinal pigment epithelial cells Chang, Kun-Che
2015
234 C p. 254-260
7 p.
artikel
5 Amino acid residues that affect the basicity of the catalytic glutamate of the hydrolytic aldehyde dehydrogenases Muñoz-Clares, Rosario A.
2015
234 C p. 45-58
14 p.
artikel
6 Carbonyl-reducing enzymes as targets of a drug-immobilised affinity carrier Andrýs, Rudolf
2015
234 C p. 169-177
9 p.
artikel
7 Characterization of 3,17β-hydroxysteroid dehydrogenase in Comamonas testosteroni Yu, Yuanhua
2015
234 C p. 221-228
8 p.
artikel
8 Cloning and characterization of a novel β-ketoacyl-ACP reductase from Comamonas testosteroni Zhang, Hao
2015
234 C p. 213-220
8 p.
artikel
9 Cloning, expression and characterization of a putative 2,5-diketo-d-gluconic acid reductase in Comamonas testosteroni Chen, Yuanan
2015
234 C p. 229-235
7 p.
artikel
10 Comparative and evolutionary studies of vertebrate ALDH1A-like genes and proteins Holmes, Roger S.
2015
234 C p. 4-11
8 p.
artikel
11 Construction of a biosensor mutant of Comamonas testosteroni for testosterone determination by cloning the EGFP gene downstream to the regulatory region of the 3,17β-HSD gene Xiong, Guangming
2015
234 C p. 188-196
9 p.
artikel
12 Contribution of liver alcohol dehydrogenase to metabolism of alcohols in rats Plapp, Bryce V.
2015
234 C p. 85-95
11 p.
artikel
13 Curcumin is a tight-binding inhibitor of the most efficient human daunorubicin reductase – Carbonyl reductase 1 Hintzpeter, Jan
2015
234 C p. 162-168
7 p.
artikel
14 Development of a high-throughput in vitro assay to identify selective inhibitors for human ALDH1A1 Morgan, Cynthia A.
2015
234 C p. 29-37
9 p.
artikel
15 Discovery of a series of aromatic lactones as ALDH1/2-directed inhibitors Buchman, Cameron D.
2015
234 C p. 38-44
7 p.
artikel
16 Down-regulation of aldo–keto reductase AKR1B10 gene expression by a phorbol ester via the ERK/c-Jun signaling pathway Nishinaka, Toru
2015
234 C p. 274-281
8 p.
artikel
17 Editorial Penning, Trevor M.
2015
234 C p. 1-3
3 p.
artikel
18 Editorial Board 2015
234 C p. ii-
1 p.
artikel
19 Evolutionary origins of retinoid active short-chain dehydrogenases/reductases of SDR16C family Belyaeva, Olga V.
2015
234 C p. 135-143
9 p.
artikel
20 Expression of AKR1B1, AKR1C3 and other genes of prostaglandin F2α biosynthesis and action in ovarian endometriosis tissue and in model cell lines Sinreih, Maša
2015
234 C p. 320-331
12 p.
artikel
21 HSD17B1 expression enhances estrogen signaling stimulated by the low active estrone, evidenced by an estrogen responsive element-driven reporter gene in vivo Järvensivu, Päivi
2015
234 C p. 126-134
9 p.
artikel
22 Human prostaglandin reductase 1 (PGR1): Substrate specificity, inhibitor analysis and site-directed mutagenesis Mesa, Julio
2015
234 C p. 105-113
9 p.
artikel
23 Identification and isolation of a regulator protein for 3,17β-HSD expressional regulation in Comamonas testosteroni Wu, Yin
2015
234 C p. 197-204
8 p.
artikel
24 Important roles of the AKR1C2 and SRD5A1 enzymes in progesterone metabolism in endometrial cancer model cell lines Sinreih, Maša
2015
234 C p. 297-308
12 p.
artikel
25 Inside front cover Editorial board 2015
234 C p. IFC-
1 p.
artikel
26 Isolation and identification of a repressor TetR for 3,17β-HSD expressional regulation in Comamonas testosteroni Pan, Tianyuan
2015
234 C p. 205-212
8 p.
artikel
27 Metabolism of doxorubicin to the cardiotoxic metabolite doxorubicinol is increased in a mouse model of chronic glutathione deficiency: A potential role for carbonyl reductase 3 Schaupp, Christopher M.
2015
234 C p. 154-161
8 p.
artikel
28 Molecular and biochemical characterisation of human short-chain dehydrogenase/reductase member 3 (DHRS3) Lundová, Tereza
2015
234 C p. 178-187
10 p.
artikel
29 N,N-diethylaminobenzaldehyde (DEAB) as a substrate and mechanism-based inhibitor for human ALDH isoenzymes Morgan, Cynthia A.
2015
234 C p. 18-28
11 p.
artikel
30 Nrf2-mediated adaptive response to methyl glyoxal in HepG2 cells involves the induction of AKR7A2 Li, Dan
2015
234 C p. 366-371
6 p.
artikel
31 Oxidative and reductive metabolism of lipid-peroxidation derived carbonyls Singh, Mahavir
2015
234 C p. 261-273
13 p.
artikel
32 15-Oxoeicosatetraenoic acid is a 15-hydroxyprostaglandin dehydrogenase-derived electrophilic mediator of inflammatory signaling pathways Snyder, Nathaniel W.
2015
234 C p. 144-153
10 p.
artikel
33 Protective effects of ferulic acid and related polyphenols against glyoxal- or methylglyoxal-induced cytotoxicity and oxidative stress in isolated rat hepatocytes Maruf, Abdullah Al
2015
234 C p. 96-104
9 p.
artikel
34 Protective roles of aldo-keto reductase 1B10 and autophagy against toxicity induced by p-quinone metabolites of tert-butylhydroquinone in lung cancer A549 cells Endo, Satoshi
2015
234 C p. 282-289
8 p.
artikel
35 Residues that influence coenzyme preference in the aldehyde dehydrogenases González-Segura, Lilian
2015
234 C p. 59-74
16 p.
artikel
36 Ruthenium complexes as inhibitors of the aldo–keto reductases AKR1C1–1C3 Traven, Katja
2015
234 C p. 349-359
11 p.
artikel
37 Screening baccharin analogs as selective inhibitors against type 5 17β-hydroxysteroid dehydrogenase (AKR1C3) Zang, Tianzhu
2015
234 C p. 339-348
10 p.
artikel
38 Structural analysis of sulindac as an inhibitor of aldose reductase and AKR1B10 Cousido-Siah, Alexandra
2015
234 C p. 290-296
7 p.
artikel
39 The aldo-keto reductases (AKRs): Overview Penning, Trevor M.
2015
234 C p. 236-246
11 p.
artikel
40 The DHEA-sulfate depot following P450c17 inhibition supports the case for AKR1C3 inhibition in high risk localized and advanced castration resistant prostate cancer Tamae, Daniel
2015
234 C p. 332-338
7 p.
artikel
41 The endometrial cancer cell lines Ishikawa and HEC-1A, and the control cell line HIEEC, differ in expression of estrogen biosynthetic and metabolic genes, and in androstenedione and estrone-sulfate metabolism Hevir-Kene, Neli
2015
234 C p. 309-319
11 p.
artikel
42 The mammalian alcohol dehydrogenase genome shows several gene duplications and gene losses resulting in a large set of different enzymes including pseudoenzymes Östberg, Linus J.
2015
234 C p. 80-84
5 p.
artikel
43 The rate-determining steps of aldo–keto reductases (AKRs), a study on human steroid 5β-reductase (AKR1D1) Chen, Mo
2015
234 C p. 360-365
6 p.
artikel
44 Towards a systematic analysis of human short-chain dehydrogenases/reductases (SDR): Ligand identification and structure–activity relationships Bhatia, Chitra
2015
234 C p. 114-125
12 p.
artikel
                             44 gevonden resultaten
 
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