Human aldose reductase

Kramer O, Hazemann I, Podjarny AD, Klebe G. Virtual screening for inhibitors of human aldose reductase. Proteins Struct Funct Genet 2004 55 814-23. 

Yamaoka T, Nishimura C, Yamashita K, Itakura M, Yamada T, Fujimoto J, Kokai Y. Acute onset of diabetic pathological changes in transgenic mice with human aldose reductase cDNA. Diabetologia 1995 38 255-261. 

Wilson DK, Tarle I, Petrash JM, Quiocho FA. Refined 1.8 A structure of human aldose reductase complexed with the potent inhibitor zopolrestat. Proc Natl Acad Sci USA 1993 90 9847-9851. 

Glu51 (human aldose reductase numbering) Yprlp, Gcylp, Aralp, Gre3p, Yjr096wp 80... 

The locations of sequence insertions and deletions present in the yeast sequences are congruent with the three-dimensional structure of human aldose reductase. Most occur between secondary structure elements, as would be expected for proteins with the same overall fold but differences in surface-exposed loops... 

DH Harrison, KM Bohren, D Ringe, GA Petsko, KH Gabbay. An anion binding site in human aldose reductase mechanistic implications for the binding of citrate, cacodylate, and glucose-6-phosphate. Biochemistry 33 2011-2020, 1994. 

Varnai P, A Warshel (2000) Computer simulation studies of the catalytic mechanism of human aldose reductase. J. Am. Chem. Soc. 122 (16) 3849-3860... 

Ko, B.C., Ruepp, B., Bohren, K.M., Gabbay, K.H., and Chung, S.S., 1997, Identification and characterization of multiple osmotic response sequences in the human aldose reductase gene. J. Biol. Chem. 272(26) 16431-16437. 

Howard, E. 1., Sanishvili, R., Cachau, R. E., Mitschler, A., Chevrier, B., Barth, R, Lamour, V., Van Zandt, M., Sibley, E., Bon, C., Moras, D., Schneider, T. R., Joachimiak, A., Podjarny, A. Ultrahigh resolution drug design 1 details of interactions in human aldose reductase-inhibitor complex at 0.66 A. Proteins Struct. Fund. Bioinf. 2004,55, 792-804. 

Significant differences in susceptibility of AR enzymes to inhibition have been observed. No trends can be predicted other than that in general HPAR is less susceptible to inhibition than other AR enzymes. From a drug discovery viewpoint fluctuation in inhibitor potency to aldose reductase from various sources complicates the discovery of a clinically effective AR and may require the use of human aldose reductase from the appropriate target tissue. ... 

Saito, R., Tokita, M., Uda, K., Ishikawa, C., and Satoh, M. (2009) Synthesis and in vitro evaluation of botryllazine B analogues as a new class of inhibitor against human aldose reductase. Tetrahedron, 65, 3019-3026. 

Boukouvalas, J. and McCann, LC. (2010) Synthesis of the human aldose reductase inhibitor rubrolide L. Tetrahedron Lett., 51,4636—4639. 

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