Human aldo-keto reductases: Function, gene regulation, and single nucleotide polymorphisms.
about
The isolation and characterization of β-glucogallin as a novel aldose reductase inhibitor from Emblica officinalisAldo-keto Reductase 1B15 (AKR1B15): a mitochondrial human aldo-keto reductase with activity toward steroids and 3-keto-acyl-CoA conjugatesRetinaldehyde is a substrate for human aldo-keto reductases of the 1C subfamilyEnzymes of the cyclooxygenase pathways of prostanoid biosynthesisCopy number variation in the horse genomeConversion of Human Steroid 5 -Reductase (AKR1D1) into 3 -Hydroxysteroid Dehydrogenase by Single Point Mutation E120H: EXAMPLE OF PERFECT ENZYME ENGINEERINGA structural characterization of the isoniazidMycobacterium tuberculosisdrug target, Rv2971, in its unliganded formInhibitor selectivity between aldo-keto reductase superfamily members AKR1B10 and AKR1B1: role of Trp112 (Trp111)NF-E2-related factor 2 regulates the stress response to UVA-1-oxidized phospholipids in skin cells.Modulation of cell metabolic pathways and oxidative stress signaling contribute to acquired melphalan resistance in multiple myeloma cellsMethyl jasmonate: putative mechanisms of action on cancer cells cycle, metabolism, and apoptosisBiogenesis and functions of lipid droplets in plants: Thematic Review Series: Lipid Droplet Synthesis and Metabolism: from Yeast to ManTemporal-spatial analysis of U.S.-Mexico border environmental fine and coarse PM air sample extract activity in human bronchial epithelial cellsMatrix rigidity regulates cancer cell growth by modulating cellular metabolism and protein synthesis.Contributions of human enzymes in carcinogen metabolismLack of functional and expression homology between human and mouse aldo-keto reductase 1C enzymes: implications for modelling human cancersEnvironmental sensing and response genes in cnidaria: the chemical defensome in the sea anemone Nematostella vectensis.Modulated expression of genes encoding estrogen metabolizing enzymes by G1-phase cyclin-dependent kinases 6 and 4 in human breast cancer cells.Effects of cigarette smoke on the human oral mucosal transcriptomeInterindividual variability in the cardiac expression of anthracycline reductases in donors with and without Down syndrome.Partners in crime: deregulation of AR activity and androgen synthesis in prostate cancerAldo-keto reductase family 1 member B8 is secreted via non-classical pathway.Selective inhibitors of aldo-keto reductases AKR1C1 and AKR1C3 discovered by virtual screening of a fragment librarySmoking-induced upregulation of AKR1B10 expression in the airway epithelium of healthy individuals.Role of aldo-keto reductases and other doxorubicin pharmacokinetic genes in doxorubicin resistance, DNA binding, and subcellular localization.AKR1C3 is a biomarker of sensitivity to PR-104 in preclinical models of T-cell acute lymphoblastic leukemiaMutations of protocadherin 19 in female epilepsy (PCDH19-FE) lead to allopregnanolone deficiency.Substrate specificity and inhibitor analyses of human steroid 5β-reductase (AKR1D1)Functional expression of novel human and murine AKR1B genesStructural importance of the C-terminal region in pig aldo-keto reductase family 1 member C1 and their effects on enzymatic activity.The curcuminoid CLEFMA selectively induces cell death in H441 lung adenocarcinoma cells via oxidative stress.Label-free protein profiling of adipose-derived human stem cells under hyperosmotic treatment.Quantitative evaluation of aldo-keto reductase expression in hepatocellular carcinoma (HCC) cell lines.Polycyclic aromatic hydrocarbons: from metabolism to lung cancer.Global transcriptomic analysis of model human cell lines exposed to surface-modified gold nanoparticles: the effect of surface chemistry.Crystallization and preliminary X-ray diffraction analysis of mouse prostaglandin F2α synthase, AKR1B3.Genetic variability in the metabolism of the tobacco-specific nitrosamine 4-(methylnitrosamino)-1-(3-pyridyl)-1-butanone (NNK) to 4-(methylnitrosamino)-1-(3-pyridyl)-1-butanol (NNAL).Promiscuity and diversity in 3-ketosteroid reductases.Enzymes of the AKR1B and AKR1C Subfamilies and Uterine Diseases.Biological role of aldo-keto reductases in retinoic Acid biosynthesis and signaling.
P2860
Q21134782-AB2747C4-2AF8-4980-9EF6-1ACF60143D75Q24313499-E8BEAC58-9ECC-4CDA-8C21-F4DE7542A107Q24323295-3822726C-7DA3-4270-A9FA-6BDFC0BA9137Q24630614-22FF483F-BBE9-4541-BFFD-1AD842E08AC7Q27312309-A26D7AFF-4EE7-470A-AD34-74AEF7CAFA54Q27678144-4F754542-F746-4910-A81D-E584BC918BC0Q27683735-67571377-8C5B-42A2-89D0-390B16126D25Q27686951-0C4201B1-9682-4C9A-BA54-49C9ED78CDB5Q28392832-9B6D679D-B26A-4E69-90DC-9CE353C0F802Q28544009-4FBD2A0C-3680-4B6F-81B1-6C411A536B4AQ28658683-24C824E2-D866-4F30-A82E-3AEED48CF612Q28732336-8F99C1CA-E84C-4374-B19B-9145C41BFF4CQ28752124-18E78BDF-CF8F-4BC8-93E5-53ABD0E39491Q30426836-BB712852-6813-4EAC-B7C3-B1130A3D9670Q30520640-10654516-F9F1-4CD4-AF47-540362CE25F4Q33587153-7DF4E3D8-9F62-4497-BD3B-5A953DBA6290Q33609122-41475EEC-D77D-4DFE-A445-B558D7C7CDAEQ33645120-D27BCC2B-2B0A-431F-88B9-755E249ACDC8Q33707973-60F6B201-8210-4D52-B1F8-56F4F144CB7DQ33784640-AF47BA76-B7CF-48E8-B9D1-72F314AB7B8BQ33823702-572580AF-2763-45D1-89D8-CDF63BD5BCBBQ34028973-E1198F64-CFA6-42D6-9079-4ED8984A5CD7Q34375275-D7289899-8D73-4F85-A1BA-11AB95B0C531Q34386382-5B2B6805-A2F1-4D7F-9AE8-42466EB54B8FQ34400600-A6B7E34B-68CC-4A6B-AF90-102F26F88280Q34482552-B8AB8DFF-E023-40FE-B4C0-37760AF01A89Q34482877-A9EE3A9D-2EBE-4368-A455-1F3DA9814DF8Q34669224-36ADE8E8-DCC5-4E15-B005-C4EB2479442EQ35012115-EA632371-2E8B-4804-BED2-C7AA698EF3A7Q35025567-240257E3-08C5-41B5-80DC-9B651B557F9DQ35032472-3C533327-8653-4625-BC92-A88167C16852Q35156459-345EC095-D52E-4BD2-99D0-B8165A0C5D85Q35171770-2CE39220-2E99-4896-80D4-BEEFBAF72A27Q35535447-9B504EA7-B749-433D-AECC-5FD6B64BBDEBQ35545338-4CBD0177-FCBE-403F-9D0B-16D235959EA6Q35596643-DC686172-18BD-4168-8FE0-E65D9AB7CF23Q35638655-3A6DEA0E-C9B6-4A6D-AA6D-E5C72F54EFDFQ35691232-EBE90773-0AC3-4763-974D-4A72F69458E3Q35825211-C9519431-CDFD-4502-A9AC-3D86C2C608C6Q35893754-CBCEB590-819E-452C-845E-E817ECE22521
P2860
Human aldo-keto reductases: Function, gene regulation, and single nucleotide polymorphisms.
description
2007 nî lūn-bûn
@nan
2007 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
2007 թվականի մայիսին հրատարակված գիտական հոդված
@hy
2007年の論文
@ja
2007年論文
@yue
2007年論文
@zh-hant
2007年論文
@zh-hk
2007年論文
@zh-mo
2007年論文
@zh-tw
2007年论文
@wuu
name
Human aldo-keto reductases: Fu ...... ngle nucleotide polymorphisms.
@ast
Human aldo-keto reductases: Fu ...... ngle nucleotide polymorphisms.
@en
Human aldo-keto reductases: Fu ...... ngle nucleotide polymorphisms.
@nl
type
label
Human aldo-keto reductases: Fu ...... ngle nucleotide polymorphisms.
@ast
Human aldo-keto reductases: Fu ...... ngle nucleotide polymorphisms.
@en
Human aldo-keto reductases: Fu ...... ngle nucleotide polymorphisms.
@nl
prefLabel
Human aldo-keto reductases: Fu ...... ngle nucleotide polymorphisms.
@ast
Human aldo-keto reductases: Fu ...... ngle nucleotide polymorphisms.
@en
Human aldo-keto reductases: Fu ...... ngle nucleotide polymorphisms.
@nl
P2860
P1476
Human aldo-keto reductases: Fu ...... ngle nucleotide polymorphisms.
@en
P2093
Jason E Drury
Trevor M Penning
P2860
P304
P356
10.1016/J.ABB.2007.04.024
P407
P577
2007-05-11T00:00:00Z