Proteins > Aldo-keto reductase family 1 member B10
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Aldo-keto reductase family 1 member B10
An aldo-keto reductase family 1 member B10 that is encoded in the genome of human. [PRO:DNx, UniProtKB:O60218]
Synonyms
EC 1.1.1.300;
EC 1.1.1.54;
ARL-1;
Aldose reductase-like;
Aldose reductase-related protein;
ARP;
hARP;
Small intestine reductase;
SI reductase
Research
Bioassay Publications (12)
| Timeframe | Studies on this Protein(%) | All Drugs % |
|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 0 (0.00) | 18.2507 |
| 2000's | 1 (8.33) | 29.6817 |
| 2010's | 9 (75.00) | 24.3611 |
| 2020's | 2 (16.67) | 2.80 |
Compounds (37)
Drugs with Inhibition Measurements
Drugs with Other Measurements
[no title available]ACS chemical biology, , 10-21, Volume: 11, Issue:10, 2016
Development of potent and selective inhibitors of aldo-keto reductase 1C3 (type 5 17β-hydroxysteroid dehydrogenase) based on N-phenyl-aminobenzoates and their structure-activity relationships.Journal of medicinal chemistry, , Mar-08, Volume: 55, Issue:5, 2012
Chromene-3-carboxamide derivatives discovered from virtual screening as potent inhibitors of the tumour maker, AKR1B10.Bioorganic & medicinal chemistry, , Apr-01, Volume: 18, Issue:7, 2010
Targeting aldose reductase for the treatment of diabetes complications and inflammatory diseases: new insights and future directions.Journal of medicinal chemistry, , Mar-12, Volume: 58, Issue:5, 2015
Flavones Inhibit the Activity of AKR1B10, a Promising Therapeutic Target for Cancer Treatment.Journal of natural products, , Nov-25, Volume: 78, Issue:11, 2015
Synthesis of Potent and Selective Inhibitors of Aldo-Keto Reductase 1B10 and Their Efficacy against Proliferation, Metastasis, and Cisplatin Resistance of Lung Cancer Cells.Journal of medicinal chemistry, , 10-26, Volume: 60, Issue:20, 2017
[no title available]ACS chemical biology, , 10-21, Volume: 11, Issue:10, 2016
Selective inhibition of the tumor marker aldo-keto reductase family member 1B10 by oleanolic acid.Journal of natural products, , May-27, Volume: 74, Issue:5, 2011
Chromene-3-carboxamide derivatives discovered from virtual screening as potent inhibitors of the tumour maker, AKR1B10.Bioorganic & medicinal chemistry, , Apr-01, Volume: 18, Issue:7, 2010
Structural basis for the high all-trans-retinaldehyde reductase activity of the tumor marker AKR1B10.Proceedings of the National Academy of Sciences of the United States of America, , Dec-26, Volume: 104, Issue:52, 2007
[no title available]ACS chemical biology, , 10-21, Volume: 11, Issue:10, 2016
Chromene-3-carboxamide derivatives discovered from virtual screening as potent inhibitors of the tumour maker, AKR1B10.Bioorganic & medicinal chemistry, , Apr-01, Volume: 18, Issue:7, 2010
Early identification of promiscuous attributes of aldose reductase inhibitors using a DMSO-perturbation assay.Bioorganic & medicinal chemistry letters, , 01-15, Volume: 30, Issue:2, 2020
Design, synthesis, and biological evaluation of novel (1-thioxo-1,2,3,4-tetrahydro-β-carbolin-9-yl)acetic acids as selective inhibitors for AKR1B1.Bioorganic & medicinal chemistry, , Jan-01, Volume: 20, Issue:1, 2012
Chromene-3-carboxamide derivatives discovered from virtual screening as potent inhibitors of the tumour maker, AKR1B10.Bioorganic & medicinal chemistry, , Apr-01, Volume: 18, Issue:7, 2010
Overview of AKR1C3: Inhibitor Achievements and Disease Insights.Journal of medicinal chemistry, , 10-22, Volume: 63, Issue:20, 2020
[no title available]ACS chemical biology, , 10-21, Volume: 11, Issue:10, 2016
Design, synthesis and evaluation of caffeic acid phenethyl ester-based inhibitors targeting a selectivity pocket in the active site of human aldo-keto reductase 1B10.European journal of medicinal chemistry, , Volume: 48, 2012
Enables
This protein enables 9 target(s):
| Target | Category | Definition |
|---|
| retinal dehydrogenase activity | molecular function | Catalysis of the reaction: retinal + NAD+ + H2O = retinoate + NADH. Acts on both 11-trans and 13-cis forms of retinal. [EC:1.2.1.36] |
| aldo-keto reductase (NADPH) activity | molecular function | Catalysis of the reaction: an alcohol + NADP+ = an aldehyde or a ketone + NADPH + H+. [GOC:ai] |
| protein binding | molecular function | Binding to a protein. [GOC:go_curators] |
| alcohol dehydrogenase (NADP+) activity | molecular function | Catalysis of the reaction: an alcohol + NADP+ = an aldehyde + NADPH + H+. [EC:1.1.1.2] |
| geranylgeranyl reductase activity | molecular function | Catalysis of the formation of phytyl group from the stepwise reduction of a geranylgeranyl group. [PMID:9492312] |
| allyl-alcohol dehydrogenase activity | molecular function | Catalysis of the reaction: allyl alcohol + NADP+ = acrolein + H+ + NADPH. [EC:1.1.1.54, RHEA:12168] |
| indanol dehydrogenase activity | molecular function | Catalysis of the reaction: indan-1-ol + NAD(P)+ = indanone + NAD(P)H + H+. [EC:1.1.1.112, MetaCyc:INDANOL-DEHYDROGENASE-RXN] |
| all-trans-retinol dehydrogenase (NADP+) activity | molecular function | Catalysis of the reaction: all-trans-retinol + NADP+ = all-trans-retinal + NADPH + H+. [RHEA:25033] |
| aldose reductase (NADPH) activity | molecular function | Catalysis of the reaction: an alditol + NADP+ = an aldose + NADPH + H+. [EC:1.1.1.21] |
Located In
This protein is located in 3 target(s):
| Target | Category | Definition |
|---|
| extracellular region | cellular component | The space external to the outermost structure of a cell. For cells without external protective or external encapsulating structures this refers to space outside of the plasma membrane. This term covers the host cell environment outside an intracellular parasite. [GOC:go_curators] |
| lysosome | cellular component | A small lytic vacuole that has cell cycle-independent morphology found in most animal cells and that contains a variety of hydrolases, most of which have their maximal activities in the pH range 5-6. The contained enzymes display latency if properly isolated. About 40 different lysosomal hydrolases are known and lysosomes have a great variety of morphologies and functions. [GOC:mah, ISBN:0198506732] |
| cytosol | cellular component | The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. [GOC:hjd, GOC:jl] |
Active In
This protein is active in 2 target(s):
| Target | Category | Definition |
|---|
| cytosol | cellular component | The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. [GOC:hjd, GOC:jl] |
| mitochondrion | cellular component | A semiautonomous, self replicating organelle that occurs in varying numbers, shapes, and sizes in the cytoplasm of virtually all eukaryotic cells. It is notably the site of tissue respiration. [GOC:giardia, ISBN:0198506732] |
Involved In
This protein is involved in 6 target(s):
| Target | Category | Definition |
|---|
| retinoid metabolic process | biological process | The chemical reactions and pathways involving retinoids, any member of a class of isoprenoids that contain or are derived from four prenyl groups linked head-to-tail. Retinoids include retinol and retinal and structurally similar natural derivatives or synthetic compounds, but need not have vitamin A activity. [ISBN:0198506732] |
| farnesol catabolic process | biological process | The chemical reactions and pathways resulting in the breakdown of the sesquiterpenoid alcohol farnesol, 3,7,11-trimethyl-2,6,10,dodecatrien-1-ol. [GOC:go_curators] |
| retinol metabolic process | biological process | The chemical reactions and pathways involving retinol, one of the three compounds that makes up vitamin A. [GOC:jl, http://www.indstate.edu/thcme/mwking/vitamins.html, PMID:1924551] |
| daunorubicin metabolic process | biological process | The chemical reactions and pathways involving daunorubicin, a chemotherapeutic of the anthracycline family that is given as a treatment for some types of cancer. [PMID:20837989] |
| doxorubicin metabolic process | biological process | The chemical reactions and pathways involving doxorubicin, an anthracycline antibiotic, used in cancer chemotherapy. [PMID:10200167] |
| cellular detoxification of aldehyde | biological process | Any process carried out at the cellular level that reduces or removes the toxicity of an aldehyde. These may include transport of aldehydes away from sensitive areas and to compartments or complexes whose purpose is sequestration of the toxic substance. [GOC:vw, PMID:25656103] |