Affinage

AKR1B10

Aldo-keto reductase family 1 member B10 · UniProt O60218

Length
316 aa
Mass
36.0 kDa
Annotated
2026-06-09
100 papers in source corpus 35 papers cited in narrative 34 extracted findings
Cross-family judge vs UniProt: tie faithfulness: 10/10 claims corpus-supported (100%)

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

AKR1B10 is a cytosolic NADPH-dependent aldo-keto reductase that detoxifies and metabolizes a broad panel of carbonyl substrates, positioning it at the interface of lipid, retinoid, isoprenoid, and xenobiotic metabolism and cancer cell signaling (PMID:16381663, PMID:19013440, PMID:19464995). Biochemically, the enzyme reduces reactive lipid peroxidation aldehydes (4-HNE, 4-ONE), long-chain isoprenoid aldehydes (farnesal, geranylgeranial), retinals, and xenobiotic and anthracycline carbonyls, while also oxidizing aliphatic alcohols and certain hydroxysteroids (PMID:16381663, PMID:19013440, PMID:18788756, PMID:19464995). Cys299 is a critical active-site residue that, together with His111 and Tyr49, governs catalysis and is the covalent target of cyclopentenone prostaglandins; NADPH binding protects the enzyme from carbonyl-mediated inactivation at this residue (PMID:19013440, PMID:21507934). Crystallographic analysis shows the native Trp112 orientation defines a broad active site exploited by selective inhibitors (PMID:24100137). Through its reductase activity AKR1B10 supports protein prenylation, sustaining KRAS farnesylation and downstream Raf/MEK/ERK signaling, and its inhibition suppresses KRAS prenylation and tumorigenesis in vivo (PMID:22222635, PMID:23689354). In cancer cells it drives proliferation, migration, and metastasis by elevating lipid second messengers that activate PKC/ERK, by engaging integrin α5/δ-catenin/FAK/Rac1 and ERK/MMP axes, and by activating PI3K/AKT/NF-κB signaling (PMID:27248472, PMID:28402270, PMID:29846015, PMID:34419144). It also reprograms metabolism—promoting glycolysis and histone lactylation—and confers anthracycline and other chemoresistance by reducing drug carbonyls, an activity blocked by inhibitors such as epalrestat and dasatinib (PMID:21640744, PMID:24656094, PMID:34339712, PMID:37587486). Its reductase activity additionally restrains GAPDH nuclear translocation and autophagy, suppresses ferroptosis via the AKT/NRF2/GPX4 axis, and shapes retinoic-acid-dependent transcription and paracrine TGF-β/collagen programs (PMID:33758077, PMID:40613296, PMID:27025872). AKR1B10 is secreted non-classically through HSP90α binding to its helix 10 and lysosomal routing (PMID:24217247). Its expression is controlled by an Nrf2-responsive ARE-A/AP-1 promoter element and by upstream SMARCA4/IRAK1 and CBX7/PRC1 transcriptional regulators, post-transcriptionally stabilized by AUF1 and m6A-modified by METTL3 (PMID:28219640, PMID:34140644, PMID:34035231, PMID:35178834, PMID:36476503).

Mechanistic history

Synthesis pass · year-by-year structured walk · 25 steps
  1. 2005 High

    Establishing AKR1B10 as a genuine NADPH-dependent carbonyl reductase required isolating the native enzyme and demonstrating catalysis on defined substrates, which this work delivered for xenobiotics and a carcinogen.

    Evidence Native protein purification from human liver cytosol with HPLC kinetic assays on dolasetron, daunorubicin, oracin, and NNK

    PMID:16381663

    Open questions at the time
    • Physiological substrate hierarchy not established
    • No structural basis for substrate selectivity
  2. 2008 High

    Defining AKR1B10's role in detoxifying reactive carbonyls and identifying Cys299 as a redox-sensitive residue clarified both a protective function and a regulatory vulnerability of the enzyme.

    Evidence Recombinant kinetics on 4-HNE/4-ONE/4-methylpentanal, C299S mutagenesis, and NADPH protection assays

    PMID:19013440

    Open questions at the time
    • In vivo relevance of 4-HNE detoxification not tested
    • Mechanism of NADPH protection at Cys299 not fully resolved
  3. 2008 High

    Comparing retinal reductase versus PAH dihydrodiol oxidation activities resolved which catalytic role dominates, pointing to retinoic acid homeostasis dysregulation over carcinogen activation.

    Evidence In vitro substrate panel oxidation and catalytic efficiency comparison in A549 lysates

    PMID:18788756

    Open questions at the time
    • Cellular retinoid flux not directly quantified here
    • PAH-quinone biological consequences untested
  4. 2009 High

    Identifying farnesal and geranylgeranial as efficient substrates connected AKR1B10 to isoprenoid/prenylation metabolism, suggesting a role beyond xenobiotic detoxification.

    Evidence Comparative AKR1B10/AKR1B1 kinetics, steroid/bile-acid inhibition, and docking

    PMID:19464995

    Open questions at the time
    • Direct link to cellular prenylation not yet shown at this stage
    • Physiological inhibitor concentrations unclear
  5. 2011 High

    Mapping covalent PGA1 modification to Cys299 with loss of enzymatic activity established a chemical handle for inactivating AKR1B10 and confirmed active-site residues.

    Evidence Biotinylated-PGA1 pulldown, C299S/H111/Y49 mutagenesis, activity assays, cellular doxorubicin accumulation

    PMID:21507934

    Open questions at the time
    • Endogenous prostaglandin regulation of AKR1B10 not demonstrated
    • Therapeutic exploitation untested in vivo
  6. 2011 High

    Demonstrating reduction of anthracycline C13-ketones to inactive alcohols mechanistically explained AKR1B10-mediated drug resistance and its reversal by inhibition.

    Evidence Recombinant kinetics, cellular HPLC quantitation, drug resistance assays with epalrestat synergy

    PMID:21640744

    Open questions at the time
    • Clinical relevance in patients not addressed
    • Substrate specificity vs doxorubicin only partly explained
  7. 2013 High

    Crystal structures of the holoenzyme provided the structural basis for inhibitor selectivity by defining the native Trp112 conformation and its flip in AKR1B1-like states.

    Evidence X-ray crystallography of AKR1B10 holoenzyme with inhibitor complexes and SAR analysis

    PMID:24100137

    Open questions at the time
    • No substrate-bound complex resolved
    • Conformational dynamics in solution untested
  8. 2013 Medium

    Linking AKR1B10 to KRAS prenylation and Ras/ERK signaling, and showing inhibition suppresses pancreatic tumorigenesis in vivo, converted a biochemical activity into an oncogenic mechanism.

    Evidence siRNA knockdown with prenylation/signaling Western blots; sulindac inhibition in a KrasG12D-Trp53 transgenic mouse model

    PMID:22222635 PMID:23689354

    Open questions at the time
    • Direct reduction of a prenylation precursor in cells not biochemically isolated
    • Sulindac off-target effects not excluded
  9. 2013 High

    Identifying HSP90α binding to helix 10 and lysosomal routing explained how a cytosolic enzyme is secreted, expanding its potential extracellular and biomarker roles.

    Evidence Reciprocal Co-IP, geldanamycin dissociation, GFP-fusion secretion assay, helix-10 point mutagenesis

    PMID:24217247

    Open questions at the time
    • Function of secreted AKR1B10 not defined here
    • Trigger for secretion in physiological contexts unknown
  10. 2013 Medium

    shRNA silencing showing increased apoptosis and chemosensitivity in hepatocellular carcinoma established AKR1B10 as a functional survival factor, not merely a marker.

    Evidence shRNA knockdown with colony formation, apoptosis, and doxorubicin cytotoxicity assays

    PMID:24656094

    Open questions at the time
    • Molecular mediator of survival not identified
    • Single cell-type context
  11. 2016 High

    Defining the integrin α5/δ-catenin/FAK/Rac1 pathway gave AKR1B10 a concrete pro-metastatic signaling mechanism validated by epistasis.

    Evidence Ectopic expression, double siRNA of integrin α5/δ-catenin, migration assays, lung metastasis model

    PMID:27248472

    Open questions at the time
    • How reductase activity links to integrin upregulation unresolved
    • Direct molecular intermediates absent
  12. 2017 Medium

    Mapping the ARE-A/AP-1 promoter element placed AKR1B10 under Nrf2-driven antioxidant transcriptional control, explaining its induction by oxidative/xenobiotic stress.

    Evidence Luciferase reporter deletion/mutation analysis with Nrf2 activation

    PMID:28219640

    Open questions at the time
    • Endogenous Nrf2 occupancy not shown by ChIP here
    • Cooperativity with AP-1 mechanistically incomplete
  13. 2017 Medium

    Connecting AKR1B10 to ERK/MMP2 signaling and to keratinocyte retinoic-acid/TGF-β programs extended its functional reach into migration and paracrine fibrosis.

    Evidence Gain/loss of function with MEK inhibitor epistasis; RARE reporter and conditioned-medium transfer assays

    PMID:27025872 PMID:28402270

    Open questions at the time
    • Direct ERK activation mechanism not defined
    • Retinoid depletion measured indirectly
  14. 2018 High

    Demonstrating AKR1B10-driven lipogenesis and DAG production activating PKC/ERK established a lipid-signaling mechanism for proliferation.

    Evidence LC-MS DAG lipidomics, PKC/ERK Western blots, Go6983/U0126/PD98059 epistasis, 3D culture and xenograft

    PMID:29846015

    Open questions at the time
    • Reductase substrate driving lipogenesis not pinpointed
    • Which DAG species are causal not resolved
  15. 2018 Medium

    Identifying IRAK4/IRAK1/AP-1 as a transcriptional driver of AKR1B10 linked it to cancer stemness and provided a regulatory axis upstream of the enzyme.

    Evidence Transcriptome sequencing, IRAK1/AKR1B10 manipulation, AP-1 reporter, sphere/TIC assays, xenograft with IRAK inhibitor

    PMID:29483095

    Open questions at the time
    • Direct AP-1 binding to AKR1B10 promoter not mapped here
    • Single cancer type
  16. 2019 Medium

    Showing AKR1B10 silencing reduces MMP-2/9 via MEK/ERK and blood-brain-barrier extravasation extended its metastatic role to brain colonization.

    Evidence siRNA in Transwell BBB, microfluidic chip, and in vivo brain metastasis models with MEK/ERK and MMP readouts

    PMID:31034948

    Open questions at the time
    • Mechanistic link to ERK activation unresolved
    • Single lab/model panel
  17. 2021 Medium

    Demonstrating that AKR1B10 reductase activity restrains GAPDH nuclear translocation and autophagy under glucose starvation revealed a redox-dependent regulatory interaction.

    Evidence Co-IP, nuclear fractionation, activity-dead mutant, autophagy markers under glucose starvation

    PMID:33758077

    Open questions at the time
    • Direct enzymatic modification of GAPDH not isolated
    • Reciprocal validation limited
  18. 2021 Medium

    Placing AKR1B10 upstream of PI3K/AKT/NF-κB and showing NF-κB-dependent cytokine induction connected its activity to proliferation, EMT, and inflammation.

    Evidence Overexpression/knockdown with LY294002 epistasis (breast cancer) and reductase-dead mutant cytokine assays (colon cancer)

    PMID:34419144 PMID:35920984

    Open questions at the time
    • Direct activator of PI3K not identified
    • Reductase-to-signaling coupling mechanism incomplete
  19. 2021 Medium

    Identifying CBX7/PRC1, SMARCA4/IRAK1 enhancer control, and E2F1/AUF1 mRNA stabilization built a multilayered regulatory network governing AKR1B10 abundance.

    Evidence ChIP assays, luciferase/enhancer reporters, RNA-binding pulldown, mRNA stability and rescue epistasis; Ras-transgenic mouse

    PMID:34035231 PMID:34140644 PMID:35178834

    Open questions at the time
    • Integration among these regulators not tested together
    • Cell-type specificity of each axis unclear
  20. 2021 Medium

    Identifying dasatinib as a direct AKR1B10 inhibitor that reverses daunorubicin resistance added a repurposable pharmacological tool against the enzyme.

    Evidence Recombinant enzyme inhibition (Ki=0.6 µM), cellular IC50, drug resistance assays

    PMID:34339712

    Open questions at the time
    • Selectivity over other AKRs limited
    • In vivo efficacy untested
  21. 2022 Medium

    Demonstrating METTL3-mediated m6A modification stabilizing/enhancing AKR1B10 added an epitranscriptomic layer driving glycolysis and tumor growth.

    Evidence MeRIP-qPCR, METTL3 manipulation, AKR1B10 siRNA rescue, xenograft in cholangiocarcinoma

    PMID:36476503

    Open questions at the time
    • m6A reader mediating the effect unidentified
    • Single tumor context
  22. 2022 Medium

    Showing AKR1B10 induces pro-inflammatory cytokines and transfers via extracellular vesicles broadened its non-cell-autonomous and inflammatory roles.

    Evidence Overexpression in macrophages/lung cells, LPS stimulation, cytokine ELISA, zopolrestat inhibition, EV transfer experiments

    PMID:35163833

    Open questions at the time
    • EV cargo function in recipient cells not defined
    • Reductase dependence of cytokine induction not fully isolated here
  23. 2023 Medium

    Linking AKR1B10 to LDHA-driven glycolysis, histone lactylation, and CCNB1 transcription defined a metabolic-epigenetic route to chemoresistance.

    Evidence GC-MS metabolomics, RNA-seq, H4K12la/CCNB1 Western blots, siRNA, in vivo drug sensitivity

    PMID:37587486

    Open questions at the time
    • Direct enzymatic step controlling LDHA not isolated
    • Generality beyond brain metastasis cells unclear
  24. 2023 Medium

    Identifying RNF152-mediated IRAK1 ubiquitination as an upstream regulator of AKR1B10 added a degradation-based control point over its expression and fatty acid oxidation.

    Evidence Co-IP, ubiquitination assay, IRAK1/AKR1B10 rescue, xenograft, FAO assay

    PMID:37717980

    Open questions at the time
    • Direct RNF152-AKR1B10 link absent (acts via IRAK1)
    • Single cancer type
  25. 2024 High

    Direct target engagement by berberine and the AKT/NRF2/GPX4-dependent ferroptosis suppression established AKR1B10 as a druggable node in metabolic disease and cell-death regulation.

    Evidence Five orthogonal target-engagement methods (DARTS/CETSA/SPR/click/co-localization) with NAFLD genetic rescue; ferroptosis pathway epistasis in TNBC

    PMID:38762210 PMID:40613296

    Open questions at the time
    • Direct substrate driving ferroptosis suppression unknown
    • In vivo ferroptosis modulation not shown

Open questions

Synthesis pass · forward-looking unresolved questions
  • How AKR1B10's catalytic reduction of specific carbonyl substrates is mechanistically coupled to the diverse downstream signaling cascades (ERK, PI3K/AKT/NF-κB, integrin, ferroptosis) remains unresolved.
  • The causal metabolite connecting reductase activity to each pathway is unidentified
  • Whether secreted vs intracellular AKR1B10 mediates distinct effects is unknown

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0016491 oxidoreductase activity 5 GO:0016209 antioxidant activity 2
Localization
GO:0005576 extracellular region 2 GO:0005829 cytosol 2 GO:0005764 lysosome 1
Pathway
R-HSA-1430728 Metabolism 4 R-HSA-162582 Signal Transduction 4 R-HSA-1643685 Disease 3 R-HSA-9748784 Drug ADME 2
Partners
GAPDHHSP90AA1

Evidence

Reading pass · 34 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2005 AKR1B10 was purified in its native form from human liver cytosol and shown to catalyze NADPH-dependent carbonyl reduction of xenobiotics including dolasetron, daunorubicin, oracin, and NNK (carcinogen), as well as NADP+-dependent oxidation of (S)-1-indanol; kinetic parameters were determined for each substrate. Protein purification from human liver cytosol; HPLC-based kinetic assays with recombinant and native enzyme Drug metabolism and disposition High 16381663
2008 AKR1B10 efficiently catalyzes NADPH-dependent reduction of toxic lipid peroxidation aldehydes 4-HNE (Km=0.3 mM, kcat=43 min⁻¹), 4-ONE (Km=0.3 mM, kcat=40 min⁻¹), and 4-methylpentanal (Km=0.05 mM, kcat=25 min⁻¹). 4-ONE inactivates AKR1B10 in the absence of NADPH, and NADPH pre-incubation protects the enzyme. The C299S mutant retains activity but is still inactivated by 4-ONE in the absence of NADPH, implicating Cys299 in NADPH-dependent protection. Recombinant enzyme kinetic assays; site-directed mutagenesis (C299S); NADPH protection experiment Chemico-biological interactions High 19013440
2008 AKR1B10 oxidizes a wide range of polycyclic aromatic hydrocarbon (PAH) trans-dihydrodiols to PAH o-quinones in vitro, though with stereospecificity for minor diastereomers. Retinal reductase activity of AKR1B10 is 5- to 150-fold greater than PAH trans-dihydrodiol oxidation, suggesting its predominant role in lung carcinogenesis is through dysregulation of retinoic acid homeostasis rather than PAH activation. In vitro enzymatic assay with recombinant AKR1B10; substrate panel oxidation measured; retinal reductase activity compared in A549 cell lysates Chemical research in toxicology High 18788756
2008 AKR1B10 catalyzes NADPH-dependent reduction of daunorubicin carbonyl groups (Km=1.1 mM, kcat=1.4 min⁻¹). The C299S mutation reduces substrate affinity for dl-glyceraldehyde (Km increases from 2.2 to 15.8 mM) but increases kcat, resulting in reduced overall catalytic efficiency; this mutation also alters inhibitor kinetics (sorbinil and EBPC no longer inhibit C299S mutant). In vitro kinetic assay with wild-type and C299S mutant recombinant AKR1B10; inhibitor kinetic analyses Chemico-biological interactions High 18325492 19028477
2009 AKR1B10 efficiently reduces long-chain aliphatic aldehydes including farnesal and geranylgeranial (from the mevalonate/prenylation pathway), oxidizes 20α-hydroxysteroids, and is inhibited by steroid hormones and bile acids (IC50 0.03–25 µM). Kinetic analyses and docking suggest inhibitory steroids and tolrestat bind overlapping sites within the active site of the enzyme-coenzyme complex, proposing a novel role for AKR1B10 in isoprenoid homeostasis. Recombinant AKR1B10 and AKR1B1 comparative kinetic assays; inhibition studies; molecular docking Archives of biochemistry and biophysics High 19464995
2010 Cigarette smoke extract upregulates AKR1B10 expression in airway epithelial cells in vitro, and transfection of AKR1B10 into airway epithelial cells enhances conversion of retinal to retinol, directly demonstrating AKR1B10's role in retinol/retinoic acid metabolism in airway cells. In vitro cigarette smoke extract treatment; AKR1B10 transfection with functional retinal-to-retinol conversion assay Chest Medium 20705797
2011 AKR1B10 reduces the C13-ketonic group on the side chain of daunorubicin and idarubicin to hydroxyl forms (daunorubicinol, idarubicinol), conferring cellular resistance. Kinetic parameters: daunorubicin Vmax=837 nmol/mg/min, Km=9.3 mM; idarubicin Vmax=460 nmol/mg/min, Km=0.46 mM (higher efficiency). AKR1B10 was less active toward doxorubicin and epirubicin (which have a C14-hydroxyl group). The AKR1B10 inhibitor epalrestat synergized with these drugs in cells. In vitro enzymatic assay with recombinant AKR1B10; HPLC quantitation in living cells; ectopic AKR1B10 expression with drug resistance assay; pharmacological inhibition with epalrestat Toxicology and applied pharmacology High 21640744
2011 Prostaglandin A1 (PGA1) covalently modifies AKR1B10 at Cys299, selectively among AKR family members. Mutation of Cys299 abolishes PGA1-biotin incorporation; mutation of His111 or Tyr49 reduces the interaction. Modification by PGA1 correlates with loss of AKR1B10 enzymatic activity. In lung cancer cells, PGA1 reduced tumorigenic potential and increased accumulation of the AKR1B10 substrate doxorubicin. Biotinylated PGA1 pulldown; site-directed mutagenesis (C299S, H111, Y49); enzymatic activity assay; molecular modeling; cell-based doxorubicin accumulation assay Cancer research High 21507934
2012 siRNA-mediated silencing of AKR1B10 in pancreatic cancer cells increased non-farnesylated HDJ2 protein, decreased membrane-bound prenylated KRAS protein, and downregulated phosphorylated ERK, MEK, and membrane-bound E-cadherin, demonstrating that AKR1B10 promotes protein prenylation (farnesylation of KRAS) and downstream Ras/ERK signaling. siRNA knockdown; Western blot for prenylated KRAS, HDJ2, p-ERK, p-MEK; immunohistochemistry in pancreatic cancer specimens Modern pathology Medium 22222635
2013 Crystal structures of AKR1B10 holoenzyme revealed that Trp112 adopts a native conformation stabilized by a Gln114-centered hydrogen bond network; AKR1B1 inhibitors can induce a Trp112 flip to create an 'AKR1B1-like' active site in AKR1B10, while selective AKR1B10 inhibitors exploit the broader active site provided by the native Trp112 orientation. X-ray crystallography of AKR1B10 holoenzyme with inhibitor complexes; structure-activity analysis FEBS letters High 24100137
2013 HSP90α (heat shock protein 90α) physically associates with AKR1B10, translocates it to secretory lysosomes, and mediates its non-classical secretion. Ectopic HSP90α increased AKR1B10 secretion; the HSP90 inhibitor geldanamycin dissociated AKR1B10-HSP90α complexes and reduced secretion. Helix 10 (amino acids 233–240) of AKR1B10 mediates HSP90α binding, with Lys233, Glu236, and Lys240 identified as key residues by targeted point mutations. Co-immunoprecipitation; ectopic overexpression; geldanamycin inhibition; GFP-fusion protein secretion assay; site-directed mutagenesis of helix 10 residues Journal of Biological Chemistry High 24217247
2013 Sulindac competitively inhibits AKR1B10 activity in pancreatic cancer cells in a dose-dependent manner. siRNA silencing or sulindac treatment reduced KRAS and HDJ2 prenylation and downregulated phospho-c-Raf, ERK1/2, and MEK1/2. In LSL-KrasG12D-Trp53R172H-Pdx1-Cre mice, sulindac reduced pancreatic cancer incidence (90% to 56%) and increased survival, establishing AKR1B10 inhibition as sufficient to suppress KRAS prenylation and downstream Ras signaling in vivo. In vitro AKR1B10 activity assay with dose-response; siRNA knockdown; Western blot; transgenic mouse pancreatic cancer model with sulindac treatment Carcinogenesis High 23689354
2013 shRNA-mediated silencing of AKR1B10 in hepatocellular carcinoma cells increased cell apoptosis, decreased colony formation, and enhanced cytoreductive response to doxorubicin chemotherapy, establishing AKR1B10 as a functional contributor to HCC cell survival and chemoresistance. shRNA knockdown; colony formation assay; apoptosis assay; doxorubicin cytotoxicity assay Human pathology Medium 24656094
2016 AKR1B10 overexpression in breast cancer cells MCF-7 and MDA-MB-231 upregulated integrin α5 and δ-catenin, activated FAK signaling, and stimulated Rac1-mediated cell migration. siRNA silencing of integrin α5 or δ-catenin eradicated AKR1B10-enhanced adhesion and migration, establishing that AKR1B10 promotes metastasis through the integrin α5/δ-catenin/FAK/Src/Rac1 pathway. Ectopic AKR1B10 expression; siRNA silencing of integrin α5 and δ-catenin; migration/invasion assays; Western blot for FAK/Src/Rac1 signaling; in vivo lung metastasis model in nude mice Oncotarget High 27248472
2017 AKR1B10 overexpression in breast cancer cells MCF-7 activated ERK1/2 signaling and upregulated MMP2 and vimentin expression, promoting cell migration and invasion. The MEK inhibitor PD98059 blocked AKR1B10-induced migration and MMP2/vimentin expression, placing AKR1B10 upstream of the ERK/MMP2 axis. Ectopic AKR1B10 expression and siRNA silencing; wound healing, transwell migration, and matrigel invasion assays; Western blot for p-ERK, MMP2, vimentin; MEK inhibitor epistasis Oncotarget Medium 28402270
2017 AKR1B10 transfection into normal human keratinocytes reproduced an abnormal retinoic acid pathway expression pattern found in keloid epidermis. Co-transfection with a luciferase reporter showed reduced retinoic acid response element (RARE) activity, indicating that AKR1B10 overexpression causes retinoic acid synthesis deficiency. Conditioned medium from AKR1B10-overexpressing keratinocytes upregulated TGF-β1, TGF-β2, and collagens I and III in fibroblasts. Transfection-based RARE luciferase reporter assay; conditioned medium transfer experiment; Western blot/qPCR for TGF-β and collagen Journal of Investigative Dermatology Medium 27025872
2018 IRAK1 transcriptionally upregulates AKR1B10 expression in hepatocellular carcinoma via the AP-1 complex. Knockdown of AKR1B10 negated IRAK1-induced tumor-initiating cell functions. IRAK4/IRAK1/AP-1/AKR1B10 constitutes an epistatic signaling cascade regulating cancer stemness and drug resistance. Transcriptome sequencing; knockdown/overexpression of IRAK1 and AKR1B10; AP-1 reporter assay; sphere and TIC assays; xenograft model with IRAK1/4 inhibitor Cancer research Medium 29483095
2018 AKR1B10 ectopic expression in breast cancer cells MCF-7 promoted lipogenesis and elevated lipid second messengers PIP2, DAG, and IP3. AKR1B10 regulated total DAG and most DAG subspecies levels (confirmed by LC-MS), leading to activation of PKC isoforms (PKCδ, PKCµ, PKCα/βII) and the PKC/c-Raf/MEK/ERK cascade. A pan-PKC inhibitor (Go6983) blocked AKR1B10-induced ERK1/2 activation, establishing the DAG→PKC→ERK pathway as AKR1B10's mechanism for promoting proliferation. Ectopic AKR1B10 expression and siRNA silencing; LC-MS lipidomics for DAG species; Western blot for PKC phosphorylation and ERK signaling; pharmacological inhibition (Go6983, U0126, PD98059); 3D culture and xenograft Molecular carcinogenesis High 29846015
2019 AKR1B10 silencing in brain-metastatic lung cancer cells suppressed MMP-2 and MMP-9 expression via the MEK/ERK signaling pathway, reducing extravasation through the blood-brain barrier in Transwell, microfluidic chip, and in vivo models. siRNA silencing; Transwell BBB model; multi-organ microfluidic chip; in vivo brain metastasis nude mouse model; Western blot for MMP-2/9 and MEK/ERK Acta biomaterialia Medium 31034948
2021 AKR1B10 interacts with and inhibits the nuclear translocation of GAPDH in colon cancer cells. This interaction is associated with an NADPH-dependent reduction reaction between AKR1B10 and GAPDH. AKR1B10 reductase activity is required for repression of autophagy under glucose starvation. Co-immunoprecipitation; knockdown and overexpression; nuclear fractionation; enzymatic activity-dead mutant studies; autophagy markers Journal of cell science Medium 33758077
2021 AKR1B10 overexpression in breast cancer cells activates PI3K, AKT, and NF-κB p65, induces nuclear translocation of NF-κB p65, and increases proliferation-related (c-myc, cyclinD1, Survivin) and EMT-related (ZEB1, SLUG, Twist) proteins. The PI3K inhibitor LY294002 attenuated these effects, placing AKR1B10 upstream of the PI3K/AKT/NF-κB cascade. AKR1B10 overexpression and shRNA knockdown; Western blot for PI3K/AKT/NF-κB pathway; LY294002 pharmacological epistasis; nuclear fractionation; xenograft model Cell & bioscience Medium 34419144
2021 CBX7 directly represses AKR1B10 transcription in a PRC1-dependent manner in urinary bladder cancer cells, as determined by ChIP assay. AKR1B10 overexpression reversed CBX7-suppressed ERK signaling, and AKR1B10 siRNA or oleanolic acid inhibitor reversed CBX7 deficiency-induced aggressiveness, establishing CBX7→AKR1B10→ERK as an epigenetic regulatory axis. RNA-seq; ChIP assay; siRNA and overexpression; ERK signaling Western blot; pharmacological AKR1B10 inhibition; xenograft Cell death & disease Medium 34035231
2021 AKR1B10 promotes NF-κB-dependent expression of pro-inflammatory cytokines IL-1α and IL-6 in colon cancer cells stimulated by LPS; this effect depends on AKR1B10's reductase activity, as a reductase-dead mutant fails to activate NF-κB signaling. siRNA knockdown; AKR1B10 overexpression; reductase-dead mutant; Western blot and ELISA for IL-1α, IL-6, NF-κB pathway components; LPS stimulation model Journal of molecular histology Medium 35920984
2021 SMARCA4 activates AKR1B10 expression in liver cancer cells through an IRAK1 enhancer, as demonstrated by ChIP-qPCR and luciferase assays showing SMARCA4 binding to the IRAK1 active enhancer. IRAK1 transcriptional activation then induces AKR1B10 expression, establishing the SMARCA4→IRAK1 enhancer→IRAK1→AKR1B10 axis in hepatocarcinogenesis. ChIP-qPCR; luciferase reporter assay; siRNA and overexpression; in vivo Ras-transgenic mouse model Oncogene Medium 34140644
2022 AUF1 binds the 3'UTR of AKR1B10 mRNA and stabilizes it, increasing AKR1B10 protein expression. This post-transcriptional mechanism mediates AUF1-induced HCC cell proliferation and doxorubicin resistance; AKR1B10 knockdown negated AUF1's pro-tumor effects. E2F1 transcriptionally drives AUF1 expression, establishing an E2F1/AUF1/AKR1B10 regulatory axis. RNA-binding pulldown; 3'UTR binding assay; siRNA rescue experiments; mRNA stability assay; E2F1 transcription factor reporter and ChIP Cancer science Medium 35178834
2022 METTL3 methyltransferase directly binds and adds m6A modification to AKR1B10 mRNA, enhancing AKR1B10 expression in cholangiocarcinoma. MeRIP-qPCR confirmed AKR1B10 m6A modification. AKR1B10 knockdown rescued the tumor-promoting effects of METTL3 overexpression, including proliferation, migration, invasion, glycolysis, and lactate production. RNA-seq; MeRIP-qPCR; METTL3 overexpression/knockdown; siRNA rescue (AKR1B10); xenograft; tissue microarray Cancer cell international Medium 36476503
2022 AKR1B10 overexpression in macrophages and lung cells induces pro-inflammatory cytokines IL-6, IL-1β, and TNFα. The AKR1B10 inhibitor zopolrestat significantly reduces LPS-induced production of these cytokines. AKR1B10 can be secreted and transferred via extracellular vesicles between different cell types. AKR1B10 overexpression in macrophages/lung cells; LPS stimulation; cytokine ELISA; pharmacological inhibition with zopolrestat; extracellular vesicle isolation and transfer experiments International journal of molecular sciences Medium 35163833
2021 In dasatinib inhibition studies, AKR1B10 was identified as a direct target with Ki=0.6 µM (recombinant enzyme) and IC50=0.5 µM (cellular). Dasatinib selectively inhibited AKR1B10-mediated daunorubicin reduction, attenuating daunorubicin resistance in AKR1B10-overexpressing cancer cells. Recombinant enzyme inhibition assay; IC50 determination in AKR1B10-overexpressing cells; drug resistance assay with daunorubicin Biochemical pharmacology Medium 34339712
2023 AKR1B10 promotes glycolysis by regulating LDHA expression and increasing lactate production in lung cancer brain metastasis cells. Elevated lactate acts as a precursor for histone lactylation (H4K12la), which activates CCNB1 transcription and accelerates DNA replication and cell cycle progression, establishing the AKR1B10/glycolysis/H4K12la/CCNB1 axis as a mechanism of pemetrexed resistance. GC-MS metabolomics; RNA-seq; Western blot for LDHA, H4K12la, CCNB1; siRNA knockdown; in vitro and in vivo drug sensitivity assays Journal of translational medicine Medium 37587486
2024 Berberine directly binds AKR1B10 protein (validated by click chemistry proteomics, DARTS, CETSA, SPR, and fluorescence co-localization). Berberine decreased AKR1B10 expression and activity. AKR1B10 knockdown recapitulated berberine's effects on lipid/glucose metabolism (ACC1, CPT-1, GLUT2) and PPAR signaling in NAFLD models; these effects were abolished when AKR1B10 was knocked down, confirming AKR1B10 as the direct target. Click chemistry proteomics; DARTS; CETSA; SPR; fluorescence co-localization; shRNA/siRNA knockdown; RNA-seq; NAFLD mouse model Journal of ethnopharmacology High 38762210
2024 AKR1B10 suppresses ferroptosis in triple-negative breast cancer MDA-MB-231 cells by activating the AKT(Ser473)/GSK3β(Ser9)/NRF2/GPX4 pathway. AKR1B10 overexpression increased GPX4, FTH1, HO-1, and NQO-1 expression; the AKT inhibitor OSU-T315 reversed AKR1B10-suppressed ferroptosis. The ferroptosis inhibitor ferrostatin-1 rescued cell death, confirming the ferroptosis mechanism. Stable lentiviral overexpression and knockdown; RSL3-induced ferroptosis model; C11-BODIPY lipid ROS flow cytometry; Western blot for AKT/GSK3β/NRF2/GPX4; pharmacological inhibition (OSU-T315, ferrostatin-1); RNA-seq; KEGG/GSEA pathway analysis Frontiers in bioscience Medium 40613296
2017 The functional antioxidant response element (ARE) for AKR1B10 transcription was mapped to the region between -530 and -520 bp (ARE-A) from the translation start site using luciferase reporter deletion and mutation analyses. ARE-A functions cooperatively with an adjacent AP-1 site for augmented Nrf2-mediated gene regulation. Luciferase reporter assays with ARE deletion and point mutants; Nrf2 activation studies Chemico-biological interactions Medium 28219640
2012 Site-directed mutagenesis of AKR1B10 active site residues Phe123, Trp220, Val301, and Gln303 reduced tight binding of γ-mangostin (competitive inhibitor, Ki=5.6 nM), establishing these residues as important for inhibitor binding in the substrate-binding site. Site-directed mutagenesis; recombinant enzyme inhibition kinetics; molecular docking Biological & pharmaceutical bulletin Medium 23123477
2023 RNF152 ubiquitinates IRAK1 (demonstrated by co-IP and ubiquitination assay), reducing IRAK1 stability in lung adenocarcinoma cells. This decreases IRAK1-mediated AKR1B10 expression, suppressing fatty acid oxidation and the malignant phenotype. Ectopic IRAK1 restored AKR1B10 expression in RNF152-overexpressing cells, establishing RNF152/IRAK1 ubiquitination as an upstream regulator of AKR1B10. Co-IP; ubiquitination assay; IRAK1 and AKR1B10 overexpression rescue; xenograft model; fatty acid oxidation assay American journal of pathology Medium 37717980

Source papers

Stage 0 corpus · 100 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2005 Overexpression of the aldo-keto reductase family protein AKR1B10 is highly correlated with smokers' non-small cell lung carcinomas. Clinical cancer research : an official journal of the American Association for Cancer Research 246 15755999
2019 AKR1B10 (Aldo-keto reductase family 1 B10) promotes brain metastasis of lung cancer cells in a multi-organ microfluidic chip model. Acta biomaterialia 130 31034948
2019 Long non-coding RNA linc00665 promotes lung adenocarcinoma progression and functions as ceRNA to regulate AKR1B10-ERK signaling by sponging miR-98. Cell death & disease 111 30692511
2012 Overexpression and oncogenic function of aldo-keto reductase family 1B10 (AKR1B10) in pancreatic carcinoma. Modern pathology : an official journal of the United States and Canadian Academy of Pathology, Inc 109 22222635
2012 AKR1B10 overexpression in breast cancer: association with tumor size, lymph node metastasis and patient survival and its potential as a novel serum marker. International journal of cancer 99 22539036
2009 Kinetic studies of AKR1B10, human aldose reductase-like protein: endogenous substrates and inhibition by steroids. Archives of biochemistry and biophysics 98 19464995
2008 Role of human aldo-keto-reductase AKR1B10 in the protection against toxic aldehydes. Chemico-biological interactions 97 19013440
2005 Purification and characterization of akr1b10 from human liver: role in carbonyl reduction of xenobiotics. Drug metabolism and disposition: the biological fate of chemicals 93 16381663
2018 IRAK1 Augments Cancer Stemness and Drug Resistance via the AP-1/AKR1B10 Signaling Cascade in Hepatocellular Carcinoma. Cancer research 92 29483095
2013 Inhibitor selectivity between aldo-keto reductase superfamily members AKR1B10 and AKR1B1: role of Trp112 (Trp111). FEBS letters 88 24100137
2023 Warburg effect enhanced by AKR1B10 promotes acquired resistance to pemetrexed in lung cancer-derived brain metastasis. Journal of translational medicine 87 37587486
2017 AKR1B10 promotes breast cancer cell migration and invasion via activation of ERK signaling. Oncotarget 86 28402270
2012 Expression of the Aldo-Ketoreductases AKR1B1 and AKR1B10 in Human Cancers. Frontiers in pharmacology 84 22685431
2021 AKR1B10 promotes breast cancer cell proliferation and migration via the PI3K/AKT/NF-κB signaling pathway. Cell & bioscience 72 34419144
2011 AKR1B10 induces cell resistance to daunorubicin and idarubicin by reducing C13 ketonic group. Toxicology and applied pharmacology 72 21640744
2008 Oxidation of PAH trans-dihydrodiols by human aldo-keto reductase AKR1B10. Chemical research in toxicology 72 18788756
2021 The Role of AKR1B10 in Physiology and Pathophysiology. Metabolites 65 34063865
2013 Aldoketoreductase family 1B10 (AKR1B10) as a biomarker to distinguish hepatocellular carcinoma from benign liver lesions. Human pathology 52 24656094
2011 AKR1B10 expression is associated with less aggressive hepatocellular carcinoma: a clinicopathological study of 168 cases. Liver international : official journal of the International Association for the Study of the Liver 50 21645211
2022 E2F1-mediated AUF1 upregulation promotes HCC development and enhances drug resistance via stabilization of AKR1B10. Cancer science 49 35178834
2017 Opposing roles of the aldo-keto reductases AKR1B1 and AKR1B10 in colorectal cancer. Cellular oncology (Dordrecht, Netherlands) 48 28929377
2010 Chromene-3-carboxamide derivatives discovered from virtual screening as potent inhibitors of the tumour maker, AKR1B10. Bioorganic & medicinal chemistry 47 20304656
2021 CBX7 suppresses urinary bladder cancer progression via modulating AKR1B10-ERK signaling. Cell death & disease 45 34035231
2010 Smoking-induced upregulation of AKR1B10 expression in the airway epithelium of healthy individuals. Chest 44 20705797
2008 Cancer biomarker AKR1B10 and carbonyl metabolism. Chemico-biological interactions 44 19028477
2011 Proteasome inhibitors MG-132 and bortezomib induce AKR1C1, AKR1C3, AKR1B1, and AKR1B10 in human colon cancer cell lines SW-480 and HT-29. Chemico-biological interactions 43 21215737
2011 Identification of aldo-keto reductase AKR1B10 as a selective target for modification and inhibition by prostaglandin A(1): implications for antitumoral activity. Cancer research 43 21507934
2018 Biostatistics mining associated method identifies AKR1B10 enhancing hepatocellular carcinoma cell growth and degenerated by miR-383-5p. Scientific reports 42 30038373
2017 AKR1B10-inhibitory Selaginella tamariscina extract and amentoflavone decrease the growth of A549 human lung cancer cells in vitro and in vivo. Journal of ethnopharmacology 37 28286104
2014 Metabolomics reveals that aldose reductase activity due to AKR1B10 is upregulated in hepatitis C virus infection. Journal of viral hepatitis 37 25487531
2018 AKR1B10 activates diacylglycerol (DAG) second messenger in breast cancer cells. Molecular carcinogenesis 35 29846015
2016 Overexpression and enhanced specific activity of aldoketo reductases (AKR1B1 & AKR1B10) in human breast cancers. Breast (Edinburgh, Scotland) 35 27855345
2011 AKR1B10 is associated with smoking and smoking-related non-small-cell lung cancer. The Journal of international medical research 34 21672310
2017 Combined Transcriptomic Analysis Revealed AKR1B10 Played an Important Role in Psoriasis through the Dysregulated Lipid Pathway and Overproliferation of Keratinocyte. BioMed research international 33 29204449
2013 Sulindac inhibits pancreatic carcinogenesis in LSL-KrasG12D-LSL-Trp53R172H-Pdx-1-Cre mice via suppressing aldo-keto reductase family 1B10 (AKR1B10). Carcinogenesis 33 23689354
2022 METTL3 promotes glycolysis and cholangiocarcinoma progression by mediating the m6A modification of AKR1B10. Cancer cell international 31 36476503
2016 AKR1B10 promotes breast cancer metastasis through integrin α5/δ-catenin mediated FAK/Src/Rac1 signaling pathway. Oncotarget 30 27248472
2008 The leishmania ARL-1 and Golgi traffic. PloS one 30 18286177
2008 Inhibiting wild-type and C299S mutant AKR1B10; a homologue of aldose reductase upregulated in cancers. European journal of pharmacology 30 18325492
2021 Aldo Keto Reductases AKR1B1 and AKR1B10 in Cancer: Molecular Mechanisms and Signaling Networks. Advances in experimental medicine and biology 29 33945128
2021 SMARCA4 oncogenic potential via IRAK1 enhancer to activate Gankyrin and AKR1B10 in liver cancer. Oncogene 29 34140644
2008 AKR1B10 in usual interstitial pneumonia: expression in squamous metaplasia in association with smoking and lung cancer. Pathology, research and practice 29 18358633
2020 AKR1B10 Inhibitor Epalrestat Facilitates Sorafenib-Induced Apoptosis and Autophagy Via Targeting the mTOR Pathway in Hepatocellular Carcinoma. International journal of medical sciences 28 32547320
2020 Loss of AKR1B10 promotes colorectal cancer cells proliferation and migration via regulating FGF1-dependent pathway. Aging 28 32615540
2024 Berberine directly targets AKR1B10 protein to modulate lipid and glucose metabolism disorders in NAFLD. Journal of ethnopharmacology 26 38762210
2021 Role of AKR1B10 and AKR1B8 in the pathogenesis of non-alcoholic steatohepatitis (NASH) in mouse. Biochimica et biophysica acta. Molecular basis of disease 26 34954342
2017 High expression of AKR1B10 predicts low risk of early tumor recurrence in patients with hepatitis B virus-related hepatocellular carcinoma. Scientific reports 26 28181486
2015 Flavones Inhibit the Activity of AKR1B10, a Promising Therapeutic Target for Cancer Treatment. Journal of natural products 26 26529431
2013 Heat shock protein 90-α mediates aldo-keto reductase 1B10 (AKR1B10) protein secretion through secretory lysosomes. The Journal of biological chemistry 26 24217247
2023 AKR1B10 Is a New Sensitive and Specific Marker for Fumarate Hydratase-Deficient Renal Cell Carcinoma. Modern pathology : an official journal of the United States and Canadian Academy of Pathology, Inc 25 37580017
2016 The Aldo-Keto Reductase AKR1B10 Is Up-Regulated in Keloid Epidermis, Implicating Retinoic Acid Pathway Dysregulation in the Pathogenesis of Keloid Disease. The Journal of investigative dermatology 25 27025872
2009 Proteomic identification of aldo-keto reductase AKR1B10 induction after treatment of colorectal cancer cells with the proteasome inhibitor bortezomib. Molecular cancer therapeutics 25 19567817
2022 Comparison of 2SC, AKR1B10, and FH Antibodies as Potential Biomarkers for FH-deficient Uterine Leiomyomas. The American journal of surgical pathology 24 34678832
2021 AKR1B10 negatively regulates autophagy through reducing GAPDH upon glucose starvation in colon cancer. Journal of cell science 24 33758077
2010 Properties and tissue distribution of a novel aldo-keto reductase encoding in a rat gene (Akr1b10). Archives of biochemistry and biophysics 23 20709016
2022 In-silico Investigations of quinine and quinidine as potential Inhibitors of AKR1B1 and AKR1B10: Functional and structural characterization. PloS one 22 36301939
2019 Overexpression of AKR1B10 predicts tumor recurrence and short survival in oral squamous cell carcinoma patients. Journal of oral pathology & medicine : official publication of the International Association of Oral Pathologists and the American Academy of Oral Pathology 22 31237374
2013 AKR1B10 is induced by hyperglycaemia and lipopolysaccharide in patients with diabetic nephropathy. Cell stress & chaperones 22 23975544
2021 AKR1B10 confers resistance to radiotherapy via FFA/TLR4/NF-κB axis in nasopharyngeal carcinoma. International journal of biological sciences 20 33767586
2017 STAR and AKR1B10 are down-regulated in high-grade endometrial cancer. The Journal of steroid biochemistry and molecular biology 20 28232277
2016 IDD388 Polyhalogenated Derivatives as Probes for an Improved Structure-Based Selectivity of AKR1B10 Inhibitors. ACS chemical biology 20 27359042
2021 AKR1B10 inhibits the proliferation and migration of gastric cancer via regulating epithelial-mesenchymal transition. Aging 19 34552036
2020 Glycyrrhetinic acid attenuates disturbed vitamin a metabolism in non-alcoholic fatty liver disease through AKR1B10. European journal of pharmacology 19 32485245
2021 Fidarestat induces glycolysis of NK cells through decreasing AKR1B10 expression to inhibit hepatocellular carcinoma. Molecular therapy oncolytics 18 34853813
2018 Immunohistochemistry Detects Increased Expression of Aldo-Keto Reductase Family 1 Member B10 (AKR1B10) in Early-Stage Hepatocellular Carcinoma. Medical science monitor : international medical journal of experimental and clinical research 18 30328412
2016 Overexpression of AKR1B10 in nasopharyngeal carcinoma as a potential biomarker. Cancer biomarkers : section A of Disease markers 18 26835713
2015 Structural Determinants of the Selectivity of 3-Benzyluracil-1-acetic Acids toward Human Enzymes Aldose Reductase and AKR1B10. ChemMedChem 18 26549844
2024 Targeting AKR1B10 by Drug Repurposing with Epalrestat Overcomes Chemoresistance in Non-Small Cell Lung Cancer Patient-Derived Tumor Organoids. Clinical cancer research : an official journal of the American Association for Cancer Research 17 39017606
2020 HSI-II Gene Cluster of Pseudomonas syringae pv. tomato DC3000 Encodes a Functional Type VI Secretion System Required for Interbacterial Competition. Frontiers in microbiology 17 32582082
2018 AKR1B10 expression predicts response of gastric cancer to neoadjuvant chemotherapy. Oncology letters 17 30655829
2005 Comparison of resistance to protein adsorption and stability of thin films derived from alpha-hepta-(ethylene glycol) methyl omega-undecenyl ether on HSi(111) and HSi(100) surfaces. Journal of colloid and interface science 17 15837490
2012 Decreased levels of AKR1B1 and AKR1B10 in cancerous endometrium compared to adjacent non-cancerous tissue. Chemico-biological interactions 16 23146748
2021 The expression and significance of AKR1B10 in laryngeal squamous cell carcinoma. Scientific reports 15 34521883
2017 Identification and characterization of functional antioxidant response elements in the promoter of the aldo-keto reductase AKR1B10 gene. Chemico-biological interactions 15 28219640
2016 Pretreatment AKR1B10 expression predicts the risk of hepatocellular carcinoma development after hepatitis C virus eradication. World journal of gastroenterology 15 27672277
2012 Inhibition of human aldose reductase-like protein (AKR1B10) by α- and γ-mangostins, major components of pericarps of mangosteen. Biological & pharmaceutical bulletin 15 23123477
2022 AKR1B10 accelerates the production of proinflammatory cytokines via the NF-κB signaling pathway in colon cancer. Journal of molecular histology 14 35920984
2022 AKR1B10, One of the Triggers of Cytokine Storm in SARS-CoV2 Severe Acute Respiratory Syndrome. International journal of molecular sciences 13 35163833
2022 AKR1B10 as a Potential Novel Serum Biomarker for Breast Cancer: A Pilot Study. Frontiers in oncology 12 35280770
2019 Silanized NaCa2HSi3O9 nanorods with a reduced pH increase on Ti for improving osteogenesis and angiogenesis in vitro. Journal of materials chemistry. B 12 31867581
2006 [Transcription TIMP3, DAPk1 and AKR1B10 genes in squamous cell lung cancer]. Molekuliarnaia biologiia 12 17209433
2024 Role of AKR1B10 in inflammatory diseases. Scandinavian journal of immunology 11 38769661
2023 AKR1B10 inhibits the proliferation and metastasis of hepatocellular carcinoma cells by regulating the PI3K/AKT pathway. Oncology letters 11 38034486
2023 AKR1B10 regulates M2 macrophage polarization to promote the malignant phenotype of gastric cancer. Bioscience reports 10 37039038
2022 Clinical value of AKR1B10 in hepatocellular carcinoma: A systematic review and meta-analysis. PloS one 10 36584078
2018 Potential of AKR1B10 as a Biomarker and Therapeutic Target in Type 2 Leprosy Reaction. Frontiers in medicine 10 30320113
2015 Detection of AKR1B10 in Peripheral Blood by Anti-AKR1B10-Conjugated CdTe/CdS Quantum Dots. Clinical laboratory 10 26554246
2024 Nicotinate-curcumin improves NASH by inhibiting the AKR1B10/ACCα-mediated triglyceride synthesis. Lipids in health and disease 9 38937844
2022 LncRNA 1700020I14Rik promotes AKR1B10 expression and activates Erk pathway to induce hepatocyte damage in alcoholic hepatitis. Cell death discovery 9 36028503
2024 CHES1 modulated tumorigenesis and senescence of pancreas cancer cells through repressing AKR1B10. Biochimica et biophysica acta. Molecular basis of disease 8 38718846
2022 Amentoflavone-loaded nanoparticles enhanced chemotherapy efficacy by inhibition of AKR1B10. Nanotechnology 8 35697009
2021 Inhibition of AKR1B10-mediated metabolism of daunorubicin as a novel off-target effect for the Bcr-Abl tyrosine kinase inhibitor dasatinib. Biochemical pharmacology 8 34339712
2011 Carboplatin-gemcitabine combination chemotherapy upregulates AKR1B10 expression in bladder cancer. International journal of clinical oncology 8 22198799
2025 In Search for Inhibitors of Human Aldo-Keto Reductase 1B10 (AKR1B10) as Novel Agents to Fight Cancer and Chemoresistance: Current State-of-the-Art and Prospects. Journal of medicinal chemistry 7 39757466
2015 Genetic variants in AKR1B10 associate with human eating behavior. BMC genetics 7 25887478
2025 Aldo-keto Reductase 1B10 (AKR1B10) Suppresses Sensitivity of Ferroptosis in TNBC by Activating the AKT/GSK3β/Nrf2/GPX4 Axis. Frontiers in bioscience (Landmark edition) 6 40613296
2024 A Composite Blood Biomarker Including AKR1B10 and Cytokeratin 18 for Progressive Types of Nonalcoholic Fatty Liver Disease. Diabetes & metabolism journal 6 38311058
2024 AKR1B10 expression characteristics in hepatocellular carcinoma and its correlation with clinicopathological features and immune microenvironment. Scientific reports 6 38802416
2023 RNF152 Suppresses Fatty Acid Oxidation and Metastasis of Lung Adenocarcinoma by Inhibiting IRAK1-Mediated AKR1B10 Expression. The American journal of pathology 6 37717980
2019 [AKR1B10 inhibitor enhances the inhibitory effect of sorafenib on liver cancer xenograft]. Zhonghua gan zang bing za zhi = Zhonghua ganzangbing zazhi = Chinese journal of hepatology 6 30685922

Missed literature

Know a paper Affinage missed for AKR1B10? Flag it for the maintainers and the community.

No submissions yet.