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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*
- K. Bohren, Varsha Nadkarni, Jian H. Song, K. Gabbay, D. Owerbach
- Biology, Medicine
- Journal of Biological Chemistry
- 25 June 2004
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.
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
Glycosylated hemoglobins and long-term blood glucose control in diabetes mellitus.
- K. Gabbay, K. Hasty, J. Breslow, R. C. Ellison, H. Bunn, P. Gallop
- The Journal of clinical endocrinology and…
- 1 May 1977
Hb A1a+b+c levels correlated with plasma cholesterol levels, suggesting that long-term hyperglycemia is associated with hypercholesterolemia, and it is suggested that glycosylated hemoglobin measurement is a good index of long- term blood glucose levels in diabetic patients. Expand
The biosynthesis of human hemoglobin A1c. Slow glycosylation of hemoglobin in vivo.
- H. Bunn, D. N. Haney, S. Kamin, K. Gabbay, P. Gallop
- Chemistry, Medicine
- The Journal of clinical investigation
- 1 June 1976
Results indicate that Hb A1c is slowly formed during the 120-day life-span of the erythrocyte, probably by a nonenzymatic process. Expand
Sequence of cDNA encoding human insulin-like growth factor I precursor
The nucleotide sequence of a human liver cDNA encoding the complete amino acid sequence of IGF-I is reported, providing evidence that IGF-i is synthesized as a precursor protein and that formation of IGFs from this precursor requires proteolytic processing at both ends. Expand
The aldo-keto reductase superfamily. cDNAs and deduced amino acid sequences of human aldehyde and aldose reductases.
- K. Bohren, B. Bullock, B. Wermuth, K. Gabbay
- Biology, Medicine
- The Journal of biological chemistry
- 5 June 1989
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
The glycosylation of hemoglobin: relevance to diabetes mellitus.
By providing an integrated measurement of blood glucose, hemoglobin AIc is useful in assessing the degree of diabetic control and is a useful model of nonenzymatic glycosylation of other proteins that may be involved in the long-term complications of the disease. Expand
The sorbitol pathway and the complications of diabetes.
- K. Gabbay
- The New England journal of medicine
- 19 April 1973
The main problems in the care of diabetic patients are ketoacidosis and infections, but since the introduction of insulin therapy, these problems are no longer the main problems. Expand
Pancreatic Beta-Cell Web: Its Possible Role in Insulin Secretion
A cortical band of fine microfilaments is consistently observed in the beta cells of the rat pancreas. Alteration of this cell web by cytochalasin B is associated with an enhancement of… Expand
Identification and Characterization of Multiple Osmotic Response Sequences in the Human Aldose Reductase Gene*
- B. Ko, B. Ruepp, K. Bohren, K. Gabbay, S. Chung
- Biology, Medicine
- The Journal of Biological Chemistry
- 27 June 1997
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