Every reference with a DOI in the deposited reference list resolved to a known
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withdrawal, or removal notice.
The 127 checked references that resolve
resolves10.1074/jbc.M006655200The Reactive Oxygen Species- and Michael Acceptor-inducible Human Aldo-Keto Reductase AKR1C1 Reduces the α,β-Unsaturated Aldehyde 4-Hydroxy-2-nonenal to 1,4-Dihydroxy-2-nonene
resolves10.1124/mol.105.019794Induction of AKR1C2 by Phase II Inducers: Identification of a Distal Consensus Antioxidant Response Element Regulated by NRF2
resolves10.1074/jbc.272.26.16431Identification and Characterization of Multiple Osmotic Response Sequences in the Human Aldose Reductase Gene
resolves10.1016/S0021-9258(18)42844-XReduction of trioses by NADPH-dependent aldo-keto reductases. Aldose reductase, methylglyoxal, and diabetic complications.
resolves10.1021/bi000796eSelective Recognition of Glutathiolated Aldehydes by Aldose Reductase
resolves10.1042/bj3430487Major differences exist in the function and tissue-specific expression of human aflatoxin B1 aldehyde reductase and the principal human aldo-keto reductase AKR1 family members
resolves10.1074/jbc.M112424200Activation of Polycyclic Aromatic Hydrocarbontrans-Dihydrodiol Proximate Carcinogens by Human Aldo-keto Reductase (AKR1C) Enzymes and Their Functional Overexpression in Human Lung Carcinoma (A549) Cells
resolves10.1021/bi010872tThe Ubiquitous Aldehyde Reductase (AKR1A1) Oxidizes Proximate Carcinogen <i>trans</i>-Dihydrodiols to <i>o</i>-Quinones: Potential Role in Polycyclic Aromatic Hydrocarbon Activation
resolves10.1080/00498250050119826Purification and characterization of oxidoreductases-catalyzing carbonyl reduction of the tobacco-specific nitrosamine 4-methylnitrosamino-1-(3-pyridyl)-1-butanone (NNK) in human liver cytosol
resolves10.1016/S0009-2797(00)00304-5Characterization of enzymes participating in carbonyl reduction of 4-methylnitrosamino-1-(3-pyridyl)-1-butanone (NNK) in human placenta
resolves10.1007/s00280-007-0554-0Dihydrodiol dehydrogenases regulate the generation of reactive oxygen species and the development of cisplatin resistance in human ovarian carcinoma cells
resolves10.1074/jbc.M112028200Increased Expression of Dihydrodiol Dehydrogenase Induces Resistance to Cisplatin in Human Ovarian Carcinoma Cells
resolves10.1016/j.taap.2014.04.027Anthracycline resistance mediated by reductive metabolism in cancer cells: The role of aldo-keto reductase 1C3
resolves10.1016/j.jsbmb.2009.12.009Aldo-keto reductase 1C3 expression in MCF-7 cells reveals roles in steroid hormone and prostaglandin metabolism that may explain its over-expression in breast cancer
resolves10.1093/molehr/gau023Generation of human endometrial knockout cell lines with the CRISPR/Cas9 system confirms the prostaglandin F2 synthase activity of aldo-ketoreductase 1B1
resolves10.1093/oxfordjournals.jbchem.a022211Identification of a Principal mRNA Species for Human 3 -Hydroxysteroid Dehydrogenase Isoform (AKR1C3) That Exhibits High Prostaglandin D2 11-Ketoreductase Activity
resolves10.1016/j.jsbmb.2011.12.002Metabolism of the synthetic progestogen norethynodrel by human ketosteroid reductases of the aldo–keto reductase superfamily
resolves10.1210/mend.11.13.0026Expression and Characterization of Recombinant Type 2 3α-Hydroxysteroid Dehydrogenase (HSD) from Human Prostate: Demonstration of Bifunctional 3α/17β-HSD Activity and Cellular Distribution
resolves10.1042/bj3510067Human 3α-hydroxysteroid dehydrogenase isoforms (AKR1C1–AKR1C4) of the aldo-keto reductase superfamily: functional plasticity and tissue distribution reveals roles in the inactivation and formation of male and female sex hormones
resolves10.1210/en.2002-0032Human Type 3 3α-Hydroxysteroid Dehydrogenase (Aldo-Keto Reductase 1C2) and Androgen Metabolism in Prostate Cells
resolves10.1124/mol.104.004515Tibolone Is Metabolized by the 3α/3β-Hydroxysteroid Dehydrogenase Activities of the Four Human Isozymes of the Aldo-Keto Reductase 1C Subfamily: Inversion of Stereospecificity with a Δ5(10)-3-Ketosteroid
resolves10.1006/bbrc.1997.6943An Nrf2/Small Maf Heterodimer Mediates the Induction of Phase II Detoxifying Enzyme Genes through Antioxidant Response Elements
resolves10.1101/gad.13.1.76Keap1 represses nuclear activation of antioxidant responsive elements by Nrf2 through binding to the amino-terminal Neh2 domain
resolves10.1016/S0076-6879(04)82019-6Role of Nicotinamide Quinone Oxidoreductase 1 (NQO1) in Protection against Toxicity of Electrophiles and Reactive Oxygen Intermediates
resolves10.1073/pnas.172398899Direct evidence that sulfhydryl groups of Keap1 are the sensors regulating induction of phase 2 enzymes that protect against carcinogens and oxidants
resolves10.1073/pnas.1305687110Regulatory flexibility in the Nrf2-mediated stress response is conferred by conformational cycling of the Keap1-Nrf2 protein complex
resolves10.1128/MCB.01204-10SCF/β-TrCP Promotes Glycogen Synthase Kinase 3-Dependent Degradation of the Nrf2 Transcription Factor in a Keap1-Independent Manner
resolves10.1038/onc.2012.388Nrf2 is controlled by two distinct β-TrCP recognition motifs in its Neh6 domain, one of which can be modulated by GSK-3 activity
resolves10.1016/S0021-9258(18)99004-6The antioxidant responsive element. Activation by oxidative stress and identification of the DNA consensus sequence required for functional activity
resolves10.1016/S0021-9258(18)77351-1Transcriptional regulation of the rat glutathione S-transferase Ya subunit gene. Characterization of a xenobiotic-responsive element controlling inducible expression by phenolic antioxidants.
resolves10.1016/j.freeradbiomed.2015.06.021Mechanisms of activation of the transcription factor Nrf2 by redox stressors, nutrient cues, and energy status and the pathways through which it attenuates degenerative disease
resolves10.1002/hep.24493Aldo-keto reductase-7A protects liver cells and tissues from acetaminophen-induced oxidative stress and hepatotoxicity
resolves10.1371/journal.pone.0150219Sulforaphane Preconditioning Sensitizes Human Colon Cancer Cells towards the Bioreductive Anticancer Prodrug PR-104A
resolves10.1016/j.cbi.2011.09.007Human aldo–keto reductase AKR7A2 protects against the cytotoxicity and mutagenicity of reactive aldehydes and lowers intracellular reactive oxygen species in hamster V79-4 cells
resolves10.1016/j.cbi.2014.10.019Nrf2-mediated adaptive response to methyl glyoxal in HepG2 cells involves the induction of AKR7A2
resolves10.1093/carcin/bgp176Characterization of the cancer chemopreventive NRF2-dependent gene battery in human keratinocytes: demonstration that the KEAP1–NRF2 pathway, and not the BACH1–NRF2 pathway, controls cytoprotection against electrophiles as well as redox-cycling compounds
resolves10.1007/s10549-011-1536-9Transcriptomic and proteomic profiling of KEAP1 disrupted and sulforaphane-treated human breast epithelial cells reveals common expression profiles
resolves10.1016/S0026-895X(25)13665-1Overproduction of a 37.5-kDa cytosolic protein structurally related to prostaglandin F synthase in ethacrynic acid-resistant human colon cells.
resolves10.1073/pnas.0501475102Utility of siRNA against Keap1 as a strategy to stimulate a cancer chemopreventive phenotype
resolves10.1093/carcin/bgg016Characterization of the rat aflatoxin B1 aldehyde reductase gene, AKR7A1. Structure and chromosomal localization of AKR7A1 as well as identification of antioxidant response elements in the gene promoter
resolves10.1073/pnas.90.21.10350An ethoxyquin-inducible aldehyde reductase from rat liver that metabolizes aflatoxin B1 defines a subfamily of aldo-keto reductases.
resolves10.1021/tx7004458Protection Against Aflatoxin B<sub>1</sub>-Induced Cytotoxicity by Expression of the Cloned Aflatoxin B<sub>1</sub>-Aldehyde Reductases Rat AKR7A1 and Human AKR7A3
resolves10.1158/1078-0432.CCR-04-1238Overexpression of the Aldo-Keto Reductase Family Protein AKR1B10 Is Highly Correlated with Smokers' Non–Small Cell Lung Carcinomas
resolves10.1002/path.2039Smoking and cancer‐related gene expression in bronchial epithelium and non‐small‐cell lung cancers
resolves10.4161/epi.6.6.15773Frequent epigenetics inactivation of KEAP1 gene in non-small cell lung cancer
resolves10.1042/BJ20051988Comparative functional analysis of human medium-chain dehydrogenases, short-chain dehydrogenases/reductases and aldo-keto reductases with retinoids
resolves10.1378/chest.09-2634Smoking-Induced Upregulation of AKR1B10 Expression in the Airway Epithelium of Healthy Individuals
resolves10.1016/S0090-9556(24)02973-8ENANTIOSELECTIVITY OF CARBONYL REDUCTION OF 4-METHYLNITROSAMINO-1-(3-PYRIDYL)-1-BUTANONE BY TISSUE FRACTIONS FROM HUMAN AND RAT AND BY ENZYMES ISOLATED FROM HUMAN LIVER
resolves10.1021/tx0600503Translesion DNA Synthesis across the Heptanone−Etheno-2‘-Deoxycytidine Adduct in Cells
resolves10.1074/jbc.M109.022897Aldo-keto Reductase Family 1 Member B10 Promotes Cell Survival by Regulating Lipid Synthesis and Eliminating Carbonyls
resolves10.1016/j.bbrc.2009.06.123Aldo–keto reductase family 1 B10 protein detoxifies dietary and lipid-derived alpha, beta-unsaturated carbonyls at physiological levels
resolves10.1016/j.neuint.2012.10.007Aldo–keto reductases mediate constitutive and inducible protection against aldehyde toxicity in human neuroblastoma SH-SY5Y cells
resolves10.1097/CAD.0b013e3283448df0Involvement of the aldo–keto reductase, AKR1B10, in mitomycin-c resistance through reactive oxygen species-dependent mechanisms
resolves10.1593/neo.10526Long-term In Vitro Treatment of Human Glioblastoma Cells with Temozolomide Increases Resistance In Vivo through Up-regulation of GLUT Transporter and Aldo-Keto Reductase Enzyme AKR1C Expression
resolves10.2174/156800908784293631The Gene Expression Profiles of Medulloblastoma Cell Lines Resistant to Preactivated Cyclophosphamide
resolves10.3389/fphar.2012.00005Aldo–Keto Reductase 1B10 and Its Role in Proliferation Capacity of Drug-Resistant Cancers
resolves10.1124/dmd.108.020388Aldo-Keto Reductase 1C2 Fails to Metabolize Doxorubicin and Daunorubicin in Vitro
resolves10.1097/FPC.0b013e32832c484bInduction of 1C aldoketoreductases and other drug dose-dependent genes upon acquisition of anthracycline resistance
resolves10.1016/j.tox.2007.05.021Aldo-keto reductases (AKR) from the AKR1C subfamily catalyze the carbonyl reduction of the novel anticancer drug oracin in man
resolves10.1093/toxsci/kfp003Transgenic Expression of Aflatoxin Aldehyde Reductase (AKR7A1) Modulates Aflatoxin B1 Metabolism but not Hepatic Carcinogenesis in the Rat
resolves10.1021/tx8002005Oxidation of PAH <i>trans</i>-Dihydrodiols by Human Aldo-Keto Reductase AKR1B10
resolves10.1021/tx950055sGeneration of Reactive Oxygen Species during the Enzymatic Oxidation of Polycyclic Aromatic Hydrocarbon <i>trans</i>-Dihydrodiols Catalyzed by Dihydrodiol Dehydrogenase
resolves10.1016/S0021-9258(19)84546-5Regio- and stereospecificity of homogeneous 3 alpha-hydroxysteroid-dihydrodiol dehydrogenase for trans-dihydrodiol metabolites of polycyclic aromatic hydrocarbons.
resolves10.1016/S0021-9258(19)77949-6Spectroscopic identification of ortho-quinones as the products of polycyclic aromatic trans-dihydrodiol oxidation catalyzed by dihydrodiol dehydrogenase. A potential route of proximate carcinogen metabolism.
resolves10.1073/pnas.0802776105Evidence for the aldo-keto reductase pathway of polycyclic aromatic
<i>trans</i>
-dihydrodiol activation in human lung A549 cells
resolves10.1074/jbc.M112.386052Detoxication of Benzo[a]pyrene-7,8-dione by Sulfotransferases (SULTs) in Human Lung Cells
resolves10.1021/tx400268qInterception of Benzo[<i>a</i>]pyrene-7,8-dione by UDP Glucuronosyltransferases (UGTs) in Human Lung Cells
resolves10.1074/jbc.M111.240739Detoxication of Structurally Diverse Polycyclic Aromatic Hydrocarbon (PAH) o-Quinones by Human Recombinant Catechol-O-methyltransferase (COMT) via O-Methylation of PAH Catechols
resolves10.1021/tx200294cSpecificity of Human Aldo-Keto Reductases, NAD(P)H:Quinone Oxidoreductase, and Carbonyl Reductases to Redox-Cycle Polycyclic Aromatic Hydrocarbon Diones and 4-Hydroxyequilenin-<i>o-</i>quinone
resolves10.1124/jpet.107.127068CYP2A13: Variable Expression and Role in Human Lung Microsomal Metabolic Activation of the Tobacco-Specific Carcinogen 4-(Methylnitrosamino)-1-(3-pyridyl)-1-butanone
resolves10.1093/carcin/12.11.2069<i>In vivo</i> and <i>in vitro</i> persistence of pyridyloxobutyl DNA adducts from 4-(methylnitrosamino)-1-(3-pyridyl)-1-butanone
resolves10.1021/tx700189cDevelopment of Liquid Chromatography Electrospray Ionization Tandem Mass Spectrometry Methods for Analysis of DNA Adducts of Formaldehyde and Their Application to Rats Treated with <i>N</i>-Nitrosodimethylamine or 4-(Methylnitrosamino)-1-(3-pyridyl)-1-butanone
resolves10.1021/tx060207rFormation and Accumulation of Pyridyloxobutyl DNA Adducts in F344 Rats Chronically Treated with 4-(Methylnitrosamino)-1-(3-pyridyl)-1-butanone and Enantiomers of Its Metabolite, 4-(Methylnitrosamino)-1-(3-pyridyl)-1-butanol
resolves10.1093/carcin/bgh120Stereoselective metabolism and tissue retention in rats of the individual enantiomers of 4-(methylnitrosamino)-1-(3-pyridyl)-1-butanol (NNAL), metabolites of the tobacco-specific nitrosamine, 4-(methylnitrosamino)-1-(3-pyridyl)-1-butanone (NNK)
resolves10.1016/S0006-291X(02)02789-4DNA adduct formation by the ubiquitous environmental pollutant 3-nitrobenzanthrone and its metabolites in rats
resolves10.1158/0008-5472.CAN-04-3544Environmental Pollutant and Potent Mutagen 3-Nitrobenzanthrone Forms DNA Adducts after Reduction by NAD(P)H:Quinone Oxidoreductase and Conjugation by Acetyltransferases and Sulfotransferases in Human Hepatic Cytosols
resolves10.1021/tx0500474Synthesis, Characterization, and <sup>32</sup>P-Postlabeling Analysis of DNA Adducts Derived from the Environmental Contaminant 3-Nitrobenzanthrone
resolves10.1016/j.tox.2008.01.018The environmental pollutant and carcinogen 3-nitrobenzanthrone induces cytochrome P450 1A1 and NAD(P)H:quinone oxidoreductase in rat lung and kidney, thereby enhancing its own genotoxicity
resolves10.1073/pnas.0705659105Structural basis for the high
<i>all-trans</i>
-retinaldehyde reductase activity of the tumor marker AKR1B10
resolves10.1074/jbc.273.4.1855Prostaglandins Promote and Block Adipogenesis through Opposing Effects on Peroxisome Proliferator-activated Receptor γ
resolves10.1371/journal.pone.0008147Combined Bezafibrate and Medroxyprogesterone Acetate: Potential Novel Therapy for Acute Myeloid Leukaemia
resolves10.18632/oncotarget.7004Mechanism of progestin resistance in endometrial precancer/cancer through Nrf2-AKR1C1 pathway
resolves10.1021/acs.jmedchem.6b00160Discovery of (<i>R</i>)-2-(6-Methoxynaphthalen-2-yl)butanoic Acid as a Potent and Selective Aldo-keto Reductase 1C3 Inhibitor
resolves10.1021/jm201547vDevelopment of Potent and Selective Inhibitors of Aldo–Keto Reductase 1C3 (Type 5 17β-Hydroxysteroid Dehydrogenase) Based on<i>N</i>-Phenyl-Aminobenzoates and Their Structure–Activity Relationships
resolves10.1016/j.bmcl.2012.03.085Crystal structures of AKR1C3 containing an N-(aryl)amino-benzoate inhibitor and a bifunctional AKR1C3 inhibitor and androgen receptor antagonist. Therapeutic leads for castrate resistant prostate cancer
resolves10.1007/s10637-014-0130-5In vitro and in vivo characterisation of ASP9521: a novel, selective, orally bioavailable inhibitor of 17β-hydroxysteroid dehydrogenase type 5 (17βHSD5; AKR1C3)
resolves10.1021/jm3017656Development of Potent and Selective Indomethacin Analogues for the Inhibition of AKR1C3 (Type 5 17β-Hydroxysteroid Dehydrogenase/Prostaglandin F Synthase) in Castrate-Resistant Prostate Cancer
resolves10.1007/s10637-014-0101-xSafety, tolerability and anti-tumour activity of the androgen biosynthesis inhibitor ASP9521 in patients with metastatic castration-resistant prostate cancer: multi-centre phase I/II study
resolves10.1158/1078-0432.CCR-13-1151Steroidogenic Enzyme AKR1C3 Is a Novel Androgen Receptor-Selective Coactivator that Promotes Prostate Cancer Growth
resolves10.3389/fonc.2014.00159The Activity of SN33638, an Inhibitor of AKR1C3, on Testosterone and 17β-Estradiol Production and Function in Castration-Resistant Prostate Cancer and ER-Positive Breast Cancer
resolves10.1093/carcin/21.12.2287Chemoprevention of colonic aberrant crypt foci in Fischer rats by sulforaphane and phenethyl isothiocyanate
resolves10.1073/pnas.051618798Sensitivity to carcinogenesis is increased and chemoprotective efficacy of enzyme inducers is lost in
<i>nrf2</i>
transcription factor-deficient mice
resolves10.1093/carcin/7.8.1379Inhibitory effects of 5-(2-pyrazinyl)-4-methyl-1,2-dithioI-3-thione (Oltipraz) on carcinogenesis induced by benzo[a]pyrene, diethylnitrosamine and uracil mustard
resolves10.1038/nrc3278NRF2 and cancer: the good, the bad and the importance of context
resolves10.1002/jcb.240590814Effects of oltipraz and related chemoprevention compounds on gene expression in rat liver
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