 Aldo-Keto Reductases
"Aldo-Keto Reductases" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus,
MeSH (Medical Subject Headings). Descriptors are arranged in a hierarchical structure,
which enables searching at various levels of specificity.
A family of NADPH-dependent oxidoreductases that reduce carbonyl substrates including sugar-aldehydes, KETOSTEROIDS; keto-prostaglandins, and QUINONES. They are monomers of approximately 37 KDa and are characterized by a parallel beta-8 (BETA SHEET)-alpha 8 (ALPHA HELICES)-barrel structure that contains the NADP binding site. This conformation favors aromatic and apolar substrates.
| Descriptor ID |
D000074408
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| MeSH Number(s) |
D08.811.682.047.150.700.156 D08.811.682.047.820.284
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| Concept/Terms |
Aldo-Keto Reductases- Aldo-Keto Reductases
- Aldo Keto Reductases
- Reductases, Aldo-Keto
- Aldo-Keto Reductase Superfamily
- Aldo Keto Reductase Superfamily
- Aldo-Keto Reductase Family
- Aldo Keto Reductase Family
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Below are MeSH descriptors whose meaning is more general than "Aldo-Keto Reductases".
Below are MeSH descriptors whose meaning is more specific than "Aldo-Keto Reductases".
This graph shows the total number of publications written about "Aldo-Keto Reductases" by people in this website by year, and whether "Aldo-Keto Reductases" was a major or minor topic of these publications.
To see the data from this visualization as text, click here.
| Year | Major Topic | Minor Topic | Total |
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| 1995 | 0 | 1 | 1 | | 2001 | 0 | 1 | 1 | | 2003 | 0 | 1 | 1 | | 2004 | 0 | 1 | 1 | | 2006 | 0 | 1 | 1 | | 2007 | 0 | 1 | 1 | | 2009 | 0 | 1 | 1 | | 2011 | 0 | 1 | 1 | | 2016 | 0 | 1 | 1 |
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Below are the most recent publications written about "Aldo-Keto Reductases" by people in Profiles.
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Chang KC, Li L, Sanborn TM, Shieh B, Lenhart P, Ammar D, LaBarbera DV, Petrash JM. Characterization of Emodin as a Therapeutic Agent for Diabetic Cataract. J Nat Prod. 2016 05 27; 79(5):1439-44.
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Salabei JK, Li XP, Petrash JM, Bhatnagar A, Barski OA. Functional expression of novel human and murine AKR1B genes. Chem Biol Interact. 2011 May 30; 191(1-3):177-84.
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Muthenna P, Suryanarayana P, Gunda SK, Petrash JM, Reddy GB. Inhibition of aldose reductase by dietary antioxidant curcumin: mechanism of inhibition, specificity and significance. FEBS Lett. 2009 Nov 19; 583(22):3637-42.
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Chang Q, Petrash JM. Disruption of aldo-keto reductase genes leads to elevated markers of oxidative stress and inositol auxotrophy in Saccharomyces cerevisiae. Biochim Biophys Acta. 2008 Feb; 1783(2):237-45.
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Chang Q, Griest TA, Harter TM, Petrash JM. Functional studies of aldo-keto reductases in Saccharomyces cerevisiae. Biochim Biophys Acta. 2007 Mar; 1773(3):321-9.
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Petrash JM. All in the family: aldose reductase and closely related aldo-keto reductases. Cell Mol Life Sci. 2004 Apr; 61(7-8):737-49.
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Chang Q, Harter TM, Rikimaru LT, Petrash JM. Aldo-keto reductases as modulators of stress response. Chem Biol Interact. 2003 Feb 01; 143-144:325-32.
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Petrash JM, Murthy BS, Young M, Morris K, Rikimaru L, Griest TA, Harter T. Functional genomic studies of aldo-keto reductases. Chem Biol Interact. 2001 Jan 30; 130-132(1-3):673-83.
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Wilson DK, Nakano T, Petrash JM, Quiocho FA. 1.7 A structure of FR-1, a fibroblast growth factor-induced member of the aldo-keto reductase family, complexed with coenzyme and inhibitor. Biochemistry. 1995 Nov 07; 34(44):14323-30.
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