ReviewHuman genomics2009
Aldo-keto reductase (AKR) superfamily: genomics and annotation.
Review in Human genomics, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 76 papers, 1 of them a synthesis that pooled it.
What it found
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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
76 citing papers in PubMed, 1 synthesis or guideline pooled it, 150 citations in OpenAlex.
- The effect of disease associated point mutations on 5β-reductase (AKR1D1) enzyme function.Chemico-biological interactions · 2011Pooled it
- Prostaglandin and myokine involvement in the cyclooxygenase-inhibiting drug enhancement of skeletal muscle adaptations to resistance exercise in older adults.American journal of physiology. Regulatory, integrative and comparative physiology · 2013Trial
- A new branch of mammalian vitamin BThe FEBS journal · 2026Article
- Target-driven machine learning-enabled virtual screening (TAME-VS) enables prioritization of AKR1C3 inhibitors.Communications chemistry · 2026Article
- Rootstock selection shapes melon taste by divergent regulation of sugar and amino acid metabolism.Frontiers in plant science · 2026Article
- Advances in Sources, Content Determination, and Bioactivity of 20α-Hydroxyprogesterone.Endocrine, metabolic & immune disorders drug targets · 2026Review
- A dirigent protein redirects extracellular terpenoid metabolism for defense against biotic challenges.Nature communications · 2025Article
- Genome-wide identification analysis of aldo-keto reductase gene family in cotton and GhAKR40 role in salt stress tolerance.Functional & integrative genomics · 2025Article
- Discovery and Optimization of a Covalent AKR1C3 Inhibitor.Journal of medicinal chemistry · 2025Article
- Crystal Structure of an Aldo-keto Reductase MGG_00097 from Magnaporthe grisea.The plant pathology journal · 2025Article
- Do microglia metabolize fructose in Alzheimer's disease?Journal of neuroinflammation · 2025Review
- Human AKR1C3 binds agonists of GPR84 and participates in an expanded polyamine pathway.Cell chemical biology · 2025Article
- Redox Regulation of KAntioxidants & redox signaling · 2024Review
- AKR7A5 knockout promote acute liver injury by inducing inflammatory response, oxidative stress and apoptosis in mice.Journal of cellular and molecular medicine · 2024Article
- Promoter of COR2-like gene is a stress inducible regulatory region in banana.Transgenic research · 2024Article
- Overexpression of carbonyl reductase 1 in ovarian cancer cells suppresses proliferation and activates the eIF2 signaling pathway.Oncology letters · 2024Article
- Cancer to Cataracts: The Mechanistic Impact of Aldo-Keto Reductases in Chronic Diseases.The Yale journal of biology and medicine · 2024Review
- Review
- An NADH/NADApplied and environmental microbiology · 2024Article
- Review
16 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
2 authors at 1 institution in 1 country.
Funding
Abstract
Aldo-keto reductases (AKRs) are phase I metabolising enzymes that catalyse the reduced nicotinamide adenine dinucleotide (phosphate) (NAD(P)H)-dependent reduction of carbonyl groups to yield primary and secondary alcohols on a wide range of substrates, including aliphatic and aromatic aldehydes and ketones, ketoprostaglandins, ketosteroids and xenobiotics. In so doing they functionalise the carbonyl group for conjugation (phase II enzyme reactions). Although functionally diverse, AKRs form a protein superfamily based on their high sequence identity and common protein fold, the (alpha/beta) 8 -barrel structure. Well over 150 AKR enzymes, from diverse organisms, have been annotated so far and given systematic names according to a nomenclature that is based on multiple protein sequence alignment and degree of identity. Annotation of non-vertebrate AKRs at the National Center for Biotechnology Information or Vertebrate Genome Annotation (vega) database does not often include the systematic nomenclature name, so the most comprehensive overview of all annotated AKRs is found on the AKR website (http://www.med.upenn.edu/akr/). This site also hosts links to more detailed and specialised information (eg on crystal structures, gene expression and single nucleotide polymorphisms [SNPs]). The protein-based AKR nomenclature allows unambiguous identification of a given enzyme but does not reflect the wealth of genomic and transcriptomic variation that exists in the various databases. In this context, identification of putative new AKRs and their distinction from pseudogenes are challenging. This review provides a short summary of the characteristic features of AKR biochemistry and structure that have been reviewed in great detail elsewhere, and focuses mainly on nomenclature and database entries of human AKRs that so far have not been subject to systematic annotation. Recent developments in the annotation of SNP and transcript variance in AKRs are also summarised.
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What OpenQuestion holds
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.