Aldose reductase: model for a new paradigm of enzymic perfection in detoxification catalysts
about
Molecular cloning, expression and catalytic activity of a human AKR7 member of the aldo-keto reductase superfamily: evidence that the major 2-carboxybenzaldehyde reductase from human liver is a homologue of rat aflatoxin B1-aldehyde reductaseHuman aldose reductase and human small intestine aldose reductase are efficient retinal reductases: consequences for retinoid metabolismNAD(P)H-dependent aldose reductase from the xylose-assimilating yeast Candida tenuis. Isolation, characterization and biochemical properties of the enzymeCloning and characterization of the xyl1 gene, encoding an NADH-preferring xylose reductase from Candida parapsilosis, and its functional expression in Candida tropicalisThree-dimensional structures of the three human class I alcohol dehydrogenasesA structural characterization of the isoniazidMycobacterium tuberculosisdrug target, Rv2971, in its unliganded formAFAP-120. A variant form of the Src SH2/SH3-binding partner AFAP-110 is detected in brain and contains a novel internal sequence which binds to a 67-kDa protein.A vertebrate aldo-keto reductase active with retinoids and ethanol.A new approach to control the enigmatic activity of aldose reductase.Using a Label Free Quantitative Proteomics Approach to Identify Changes in Protein Abundance in Multidrug-Resistant Mycobacterium tuberculosis.Metabolism of the lipid peroxidation product, 4-hydroxy-trans-2-nonenal, in isolated perfused rat heart.Aldose reductase and cardiovascular diseases, creating human-like diabetic complications in an experimental model.Binding of pyridine nucleotide coenzymes to the beta-subunit of the voltage-sensitive K+ channel.Product of side-chain cleavage of cholesterol, isocaproaldehyde, is an endogenous specific substrate of mouse vas deferens protein, an aldose reductase-like protein in adrenocortical cells.Further characterization of a rat hepatoma-derived aldose-reductase-like protein--organ distribution and modulation in vitro.Binding energy and specificity in the catalytic mechanism of yeast aldose reductases.Catalytic reaction profile for NADH-dependent reduction of aromatic aldehydes by xylose reductase from Candida tenuis.Aldehyde reductase activity in the antennae of Helicoverpa armigera.Substrate specificity of sheep liver sorbitol dehydrogenase.Probing the substrate binding site of Candida tenuis xylose reductase (AKR2B5) with site-directed mutagenesis.Antidiabetic potential of polyoxotungstates: in vitro and in vivo studies.Tyr-51 is the proton donor-acceptor for NAD(H)-dependent interconversion of xylose and xylitol by Candida tenuis xylose reductase (AKR2B5).AKR1B1 reduces Glc to D-sorbitolThe aldo-keto reductase superfamily and its role in drug metabolism and detoxification
P2860
Q24313464-A75C5237-4110-43B6-9C7A-6ABB191CC5E8Q24530114-60AAE68D-F141-4B47-BC55-C2DCA0968D3FQ24530335-9466FFC5-940D-4922-974F-EF50AAE43B1DQ24564945-C227616D-AAE2-43EA-8629-2D8B69F4E667Q24644663-423330F1-B1BF-4C9E-80B1-DE16DFA29885Q27683735-6FCC7566-AFDA-433E-B983-C9C469C19812Q30193637-F08B64AF-32C1-45B8-A497-E1F9A8D437B1Q30661574-01AB3792-DFEA-46F2-8953-E886CD4F3B07Q34982833-953BD003-EDA8-4907-897D-B805A52D3095Q35186976-422EF7E4-69AF-4FFF-A186-0D14729D4835Q36466156-E49514FC-A9C5-4C66-A362-88DD6C3AF458Q37751655-0C23A965-952B-47FB-AA99-39841A4A54EEQ38302714-D683D24D-9D26-45C3-A138-3AB7E5500916Q40919255-3AADF88F-3134-4BC3-A64B-A7E57B652884Q41096240-D651F9F1-1791-4EAE-A1BA-CFF03AB9C6F3Q41969694-F434F1CA-3E6A-4136-A4B8-8791D207DAADQ42000244-855C22F0-E332-4758-84A3-A372C82D9862Q42004611-19CE703B-7F79-4273-A8CE-6E7DB391CC12Q42989502-1916E21C-AB91-4E7E-818A-B89D6179E99BQ43226721-E1698865-2A30-48A9-9221-F7CE3DD320F3Q46191421-D6B9C073-8AEC-49AB-9F19-02F6CDB0A7BCQ46233178-4F814251-A8D0-41B8-921E-C7F365DCBFD0Q50293182-B2B3F57F-1AFA-4EFB-A8DD-D9FB5E8833E9Q56760512-A9048542-7BC2-42AE-A249-35D0340A56D0
P2860
Aldose reductase: model for a new paradigm of enzymic perfection in detoxification catalysts
description
1992 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1992 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
artículu científicu espublizáu en 1992
@ast
im Oktober 1992 veröffentlicher wissenschaftlicher Artikel
@de
scientific journal article
@en
vedecký článok (publikovaný 1992/10/27)
@sk
vědecký článek publikovaný v roce 1992
@cs
wetenschappelijk artikel (gepubliceerd op 1992/10/27)
@nl
наукова стаття, опублікована в жовтні 1992
@uk
مقالة علمية (نشرت في 27-10-1992)
@ar
name
Aldose reductase: model for a ...... on in detoxification catalysts
@ast
Aldose reductase: model for a ...... on in detoxification catalysts
@en
Aldose reductase: model for a ...... on in detoxification catalysts
@nl
type
label
Aldose reductase: model for a ...... on in detoxification catalysts
@ast
Aldose reductase: model for a ...... on in detoxification catalysts
@en
Aldose reductase: model for a ...... on in detoxification catalysts
@nl
prefLabel
Aldose reductase: model for a ...... on in detoxification catalysts
@ast
Aldose reductase: model for a ...... on in detoxification catalysts
@en
Aldose reductase: model for a ...... on in detoxification catalysts
@nl
P356
P1433
P1476
Aldose reductase: model for a ...... on in detoxification catalysts
@en
P2093
C. E. Grimshaw
P304
10139–10145
P356
10.1021/BI00157A001
P407
P577
1992-10-27T00:00:00Z