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Synthesis of non-prenyl analogues of baccharin as selective and potent inhibitors for aldo-keto reductase 1C3.

Gifu Pharmaceutical University

Morpholylureas are a new class of potent and selective inhibitors of the type 5 17-ß-hydroxysteroid dehydrogenase (AKR1C3).

University of Auckland

Synthesis and structure-activity relationships for 1-(4-(piperidin-1-ylsulfonyl)phenyl)pyrrolidin-2-ones as novel non-carboxylate inhibitors of the aldo-keto reductase enzyme AKR1C3.

University of Auckland

2,3-diarylpropenoic acids as selective non-steroidal inhibitors of type-5 17ß-hydroxysteroid dehydrogenase (AKR1C3).

University of Ljubljana

Development of potent and selective indomethacin analogues for the inhibition of AKR1C3 (Type 5 17ß-hydroxysteroid dehydrogenase/prostaglandin F synthase) in castrate-resistant prostate cancer.

Vanderbilt University School of Medicine

Selective inhibitors of aldo-keto reductases AKR1C1 and AKR1C3 discovered by virtual screening of a fragment library.

University of Ljubljana

3-(3,4-Dihydroisoquinolin-2(1H)-ylsulfonyl)benzoic Acids: highly potent and selective inhibitors of the type 5 17-ß-hydroxysteroid dehydrogenase AKR1C3.

University of Auckland

N-Benzoyl anthranilic acid derivatives as selective inhibitors of aldo-keto reductase AKR1C3.

University of Ljubljana

Development of potent and selective inhibitors of aldo-keto reductase 1C3 (type 5 17ß-hydroxysteroid dehydrogenase) based on N-phenyl-aminobenzoates and their structure-activity relationships.

University of Pennsylvania

Selective inhibition of human type-5 17ß-hydroxysteroid dehydrogenase (AKR1C3) by baccharin, a component of Brazilian propolis.

Gifu Pharmaceutical University

Crystal 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.

Perelman School of Medicine University of Pennsylvania

Structure-based optimization and biological evaluation of human 20a-hydroxysteroid dehydrogenase (AKR1C1) salicylic acid-based inhibitors.

Monash University (Parkville Campus)

New cyclopentane derivatives as inhibitors of steroid metabolizing enzymes AKR1C1 and AKR1C3.

University of Ljubljana

Structure-guided design, synthesis, and evaluation of salicylic acid-based inhibitors targeting a selectivity pocket in the active site of human 20alpha-hydroxysteroid dehydrogenase (AKR1C1).

Monash University (Parkville Campus)

Discovery of Novel Aldo-Keto Reductase 1C3 Inhibitors as Chemotherapeutic Potentiators for Cancer Drug Resistance.

China Pharmaceutical University

Overview of AKR1C3: Inhibitor Achievements and Disease Insights.

China Pharmaceutical University

Development of Novel AKR1C3 Inhibitors as New Potential Treatment for Castration-Resistant Prostate Cancer.

Gifu Pharmaceutical University

Discovery of (R)-2-(6-Methoxynaphthalen-2-yl)butanoic Acid as a Potent and Selective Aldo-keto Reductase 1C3 Inhibitor.

University of Pennsylvania

Potent and Highly Selective Aldo-Keto Reductase 1C3 (AKR1C3) Inhibitors Act as Chemotherapeutic Potentiators in Acute Myeloid Leukemia and T-Cell Acute Lymphoblastic Leukemia.

Texas Tech University Health Sciences Center

Probing the inhibitor selectivity pocket of human 20?-hydroxysteroid dehydrogenase (AKR1C1) with X-ray crystallography and site-directed mutagenesis.

Monash University (Parkville Campus)

Screening, synthesis, crystal structure, and molecular basis of 6-amino-4-phenyl-1,4-dihydropyrano[2,3-c]pyrazole-5-carbonitriles as novel AKR1C3 inhibitors.

Guangzhou Medical University

Synthesis of Potent and Selective Inhibitors of Aldo-Keto Reductase 1B10 and Their Efficacy against Proliferation, Metastasis, and Cisplatin Resistance of Lung Cancer Cells.

Gifu Pharmaceutical University

Selectivity determinants of inhibitor binding to human 20alpha-hydroxysteroid dehydrogenase: crystal structure of the enzyme in ternary complex with coenzyme and the potent inhibitor 3,5-dichlorosalicylic acid.

Monash University