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A M55V Polymorphism in a Novel SUMO Gene (SUMO-4) Differentially Activates Heat Shock Transcription Factors and Is Associated with Susceptibility to Type I Diabetes Mellitus*
TLDR
The identification of a novel intronless SUMO gene, SUMO-4, that encodes a 95-amino acid protein having an 86% amino acid homology withsumO-2, which is associated with type I diabetes mellitus susceptibility in families and suggests that it may be involved in the pathogenesis of type Iabetes. Expand
An unlikely sugar substrate site in the 1.65 A structure of the human aldose reductase holoenzyme implicated in diabetic complications.
TLDR
The structure of a recombinant human placenta aldose reductase is refined and it is revealed that the enzyme contains a parallel beta 8/alpha 8-barrel motif and establishes a new motif for NADP-binding oxidoreductases. Expand
The aldo-keto reductase superfamily. cDNAs and deduced amino acid sequences of human aldehyde and aldose reductases.
TLDR
Southern hybridization analysis of human genomic DNA indicates a multigene system for aldose reductase, suggesting the existence of additional proteins, and the aldo-keto reductases superfamily of proteins may have a more significant and hitherto not fully appreciated role in general cellular metabolism. Expand
Identification and Characterization of Multiple Osmotic Response Sequences in the Human Aldose Reductase Gene*
TLDR
The data indicate that cooperative interaction among the three TonE-like sequences in the human AR may be necessary for their enhancer function, suggesting that the mechanism of osmotic regulation of gene expression in these animals is similar. Expand
Tyrosine-48 is the proton donor and histidine-110 directs substrate stereochemical selectivity in the reduction reaction of human aldose reductase: enzyme kinetics and crystal structure of the Y48H
TLDR
The kinetic and mutagenesis data, together with structural data, indicate that His 110 plays an important role in the orientation of substrates in the active site pocket, while Tyr48 is the proton donor during aldehyde reduction by aldose reductase. Expand
A proline-90 residue unique to SUMO-4 prevents maturation and sumoylation.
TLDR
The maturation process of SUMO-4 to active form containing C-terminal di-glycine residues is inhibited by a unique proline residue located at position 90 (Pro-90), which appears to be unable to form covalent isopeptide bonds with substrates. Expand
Mechanism of human aldehyde reductase: characterization of the active site pocket.
TLDR
Dissociation constants and spectroscopic and fluorimetric properties of nucleotide complexes with various mutants suggest that, in addition to Tyr49 and His112, Lys79 plays a hitherto unappreciated role in nucleotide binding. Expand
Ascorbate Synthesis Pathway
TLDR
In vivo demonstration of two independent roles for ASC as an antioxidant suppressing osteoclast activity and number as well as a cofactor promoting osteoblast differentiation is demonstrated, which has important implications for human osteoporosis. Expand
Human aldose reductase: rate constants for a mechanism including interconversion of ternary complexes by recombinant wild-type enzyme.
TLDR
The proposed kinetic model provides a basic set of rate constants for interpretation of kinetic results obtained with aldose reductase mutants generated for the purpose of examining structure-function relationships of different components of the native enzyme. Expand
Mechanism of aldose reductase inhibition: binding of NADP+/NADPH and alrestatin-like inhibitors.
TLDR
Alrestatin binds preferentially to the enzyme/NADP+ complex, consistent with the steady-state inhibition pattern, and is detected by fluorescence assays, and by an ultrafiltration assay which measures the fraction of unbound alrestatin. Expand
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