ReviewEndocrine reviews2019
Structural and Functional Biology of Aldo-Keto Reductase Steroid-Transforming Enzymes.
Review in Endocrine reviews, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 73 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
73 citing papers in PubMed, 154 citations in OpenAlex.
- Synthesis and Activity-Based Protein Profiling Identifies Aldo-Keto Reductase 1C3 as Target Protein of Myxoglucamides.Angewandte Chemie (International ed. in English) · 2026Article
- Liver cirrhosis is associated with altered glucocorticoid metabolism related to disease severity.Journal of internal medicine · 2026Article
- Discovery and characterization of a nickel enzyme family that catalyses intermolecular hydride shuttling.Nature chemistry · 2026Article
- A new branch of mammalian vitamin BThe FEBS journal · 2026Article
- Review
- Adrenal AKR1C3-mediated androgen activation contributes to hyperandrogenism in prepubertal ovariectomized rats.Translational pediatrics · 2026Article
- Article
- Dissecting Polypharmacology in Phenotypic Screening to Resolve Ferroptotic and Necrotic Cell-Death Mechanisms.ACS medicinal chemistry letters · 2026Article
- Age-related downregulation of dihydrotestosterone-inactivating enzymes in human scalp sebaceous glands.Inflammation and regeneration · 2026Article
- Comprehensive analysis of the deleterious nonsynonymous, non-coding SNPs and cancer variants of human aldo-keto reductase type 1 (AKR1C1) protein and their probable association with disease risk and progression: a computational study.Biochemistry and biophysics reports · 2026Article
- Article
- RNA-Seq of Gingival Fibroblasts Grown on Collagen Membranes and Hyaluronic Acid.Journal of functional biomaterials · 2026Article
- Role of Aldo-Keto reductase family 1 member C in cancer progression: a special focus on the role of AKR1C1 in pancreatic cancer.Medical oncology (Northwood, London, England) · 2025Article
- The Role of Prostaglandins as Major Inflammatory Mediators in Colorectal Cancer.International journal of molecular sciences · 2025Review
- The structural basis of aldo-keto reductase 1C3 inhibition by 17α-picolyl and 17(Journal of enzyme inhibition and medicinal chemistry · 2025Article
- A dirigent protein redirects extracellular terpenoid metabolism for defense against biotic challenges.Nature communications · 2025Article
- Human xenobiotic metabolism proteins have full-length and split homologs in the gut microbiome.G3 (Bethesda, Md.) · 2025Article
- Brain Metabolism of Allopregnanolone and Isoallopregnanolone in Male Rat Brain.International journal of molecular sciences · 2025Article
- AKR1B10 as a novel prognostic biomarker linking methylation and immune escape in hepatocellular carcinoma.Discover oncology · 2025Article
- Crystal Structure of an Aldo-keto Reductase MGG_00097 from Magnaporthe grisea.The plant pathology journal · 2025Article
13 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
Aldo-keto reductases (AKRs) are monomeric NAD(P)(H)-dependent oxidoreductases that play pivotal roles in the biosynthesis and metabolism of steroids in humans. AKR1C enzymes acting as 3-ketosteroid, 17-ketosteroid, and 20-ketosteroid reductases are involved in the prereceptor regulation of ligands for the androgen, estrogen, and progesterone receptors and are considered drug targets to treat steroid hormone-dependent malignancies and endocrine disorders. In contrast, AKR1D1 is the only known steroid 5β-reductase and is essential for bile-acid biosynthesis, the generation of ligands for the farnesoid X receptor, and the 5β-dihydrosteroids that have their own biological activity. In this review we discuss the crystal structures of these AKRs, their kinetic and catalytic mechanisms, AKR genomics (gene expression, splice variants, polymorphic variants, and inherited genetic deficiencies), distribution in steroid target tissues, roles in steroid hormone action and disease, and inhibitor design.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.