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References

  • 1
    Penning TM & Drury JE (2007) Human aldo-keto reductases: function, gene regulation, and single nucleotide polymorphisms. Arch Biochem Biophys 464, 241250.
  • 2
    Jez JM, Flynn TG & Penning TM (1997) A new nomenclature for the aldo-keto reductase superfamily. Biochem Pharmacol 54, 639647.
  • 3
    Hoog SS, Pawlowski JE, Alzari PM, Penning TM & Lewis M (1994) Three-dimensional structure of rat liver 3 alpha-hydroxysteroid/dihydrodiol dehydrogenase: a member of the aldo-keto reductase superfamily. Proc Natl Acad Sci USA 91, 25172521.
  • 4
    Kilunga KB, Inoue T, Okano Y, Kabututu Z, Martin SK, Lazarus M, Duszenko M, Sumii Y, Kusakari Y, Matsumura H et al. (2005) Structural and mutational analysis of Trypanosoma brucei prostaglandin H2 reductase provides insight into the catalytic mechanism of aldo-ketoreductases. J Biol Chem 280, 2637126382.
  • 5
    Wilson DK, Bohren KM, Gabbay KH & Quiocho FA (1992) An unlikely sugar substrate site in the 1.65 Å structure of the human aldose reductase holoenzyme implicated in diabetic complications. Science 257, 8184.
  • 6
    Wilson DK, Nakano T, Petrash JM & Quiocho FA (1995) 1.7 Å structure of FR-1, a fibroblast growth factor-induced member of the aldo-keto reductase family, complexed with coenzyme and inhibitor. Biochemistry 34, 1432314330.
  • 7
    Petrash JM (2004) All in the family: aldose reductase and closely related aldo-keto reductases. Cell Mol Life Sci 61, 737749.
  • 8
    Kubiseski TJ, Hyndman DJ, Morjana NA & Flynn TG (1992) Studies on pig muscle aldose reductase. Kinetic mechanism and evidence for a slow conformational change upon coenzyme binding. J Biol Chem 267, 65106517.
  • 9
    Kabututu Z, Manin M, Pointud JC, Maruyama T, Nagata N, Lambert S, Lefrancois-Martinez AM, Martinez A & Urade Y (2009) Prostaglandin F synthase activities of aldo-keto reductase 1B1, 1B3 and 1B7. J Biochem 145, 161168.
  • 10
    Watanabe K (2002) Prostaglandin F synthase. Prostaglandins Other Lipid Mediat 68–69, 401407.
  • 11
    Crawford K, Kaufman PL & Gabelt BT (1987) Effects of topical PGF on aqueous humor dynamics in cynomolgus monkeys. Curr Eye Res 6, 10351044.
  • 12
    Weber PC (1980) Renal prostaglandins, kidney function and essential hypertension. Contrib Nephrol 23, 8392.
  • 13
    Sasaki S, Hozumi Y & Kondo S (2005) Influence of prostaglandin F and its analogues on hair regrowth and follicular melanogenesis in a murine model. Exp Dermatol 14, 323328.
  • 14
    McCracken JA, Custer EE & Lamsa JC (1999) Luteolysis: a neuroendocrine-mediated event. Physiol Rev 79, 263323.
  • 15
    Bresson E, Boucher-Kovalik S, Chapdelaine P, Madore E, Harvey N, Laberge PY, Leboeuf M & Fortier MA (2011) The human aldose reductase AKR1B1 qualifies as the primary prostaglandin F synthase in the endometrium. J Clin Endocrinol Metab 96, 210219.
  • 16
    Fujimori K, Ueno T, Nagata N, Kashiwagi K, Aritake K, Amano F & Urade Y (2010) Suppression of adipocyte differentiation by aldo-keto reductase 1B3 acting as prostaglandin F synthase. J Biol Chem 285, 88808886.
  • 17
    Liston TE, Oates JA & Roberts LJ II (1985) Prostaglandin D2 is metabolized in humans to 9 alpha,11 beta-prostaglandin F2, a novel biologically active prostaglandin. Adv Prostaglandin Thromboxane Leukot Res 15, 365367.
  • 18
    Watanabe K, Yoshida R, Shimizu T & Hayaishi O (1985) Enzymatic formation of prostaglandin F from prostaglandin H2 and D2. Purification and properties of prostaglandin F synthetase from bovine lung. J Biol Chem 260, 70357041.
  • 19
    Hayaishi O, Watanabe K, Fujii Y, Nakayama K, Ohkubo H, Kuramitsu S, Kagamiyama H & Nakanishi S (1988) Prostaglandin F synthetase, a dual function enzyme. Prog Clin Biol Res 274, 577587.
  • 20
    Watanabe K, Fujii Y, Nakayama K, Ohkubo H, Kuramitsu S, Kagamiyama H, Nakanishi S & Hayaishi O (1988) Structural similarity of bovine lung prostaglandin F synthase to lens epsilon-crystallin of the European common frog. Proc Natl Acad Sci USA 85, 1115.
  • 21
    Kubata BK, Duszenko M, Kabututu Z, Rawer M, Szallies A, Fujimori K, Inui T, Nozaki T, Yamashita K, Horii T et al. (2000) Identification of a novel prostaglandin F synthase in Trypanosoma brucei. J Exp Med 192, 13271338.
  • 22
    Kubata BK, Kabututu Z, Nozaki T, Munday CJ, Fukuzumi S, Ohkubo K, Lazarus M, Maruyama T, Martin SK, Duszenko M et al. (2002) A key role for old yellow enzyme in the metabolism of drugs by Trypanosoma cruzi. J Exp Med 196, 12411251.
  • 23
    Moriuchi H, Koda N, Okuda-Ashitaka E, Daiyasu H, Ogasawara K, Toh H, Ito S, Woodward DF & Watanabe K (2008) Molecular characterization of a novel type of prostamide/prostaglandin F synthase, belonging to the thioredoxin-like superfamily. J Biol Chem 283, 792801.
  • 24
    Urade Y, Fujimoto N & Hayaishi O (1985) Purification and characterization of rat brain prostaglandin D synthetase. J Biol Chem 260, 1241012415.
  • 25
    Bohren KM, Grimshaw CE, Lai CJ, Harrison DH, Ringe D, Petsko GA & Gabbay KH (1994) 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 mutant enzyme. Biochemistry 33, 20212032.
  • 26
    Tarle I, Borhani DW, Wilson DK, Quiocho FA & Petrash JM (1993) Probing the active site of human aldose reductase. Site-directed mutagenesis of Asp-43, Tyr-48, Lys-77, and His-110. J Biol Chem 268, 2568725693.
  • 27
    Fukunishi Y, Mikami Y & Nakamura H (2005) Similarities among receptor pockets and among compounds: analysis and application to in silico ligand screening. J Mol Graph Model 24, 3445.
  • 28
    Klimacek M, Szekely M, Griessler R & Nidetzky B (2001) Exploring the active site of yeast xylose reductase by site-directed mutagenesis of sequence motifs characteristic of two dehydrogenase/reductase family types. FEBS Lett 500, 149152.
  • 29
    Schlegel BP, Jez JM & Penning TM (1998) Mutagenesis of 3 alpha-hydroxysteroid dehydrogenase reveals a ‘push-pull’ mechanism for proton transfer in aldo-keto reductases. Biochemistry 37, 35383548.
  • 30
    Lefrancois-Martinez AM, Bertherat J, Val P, Tournaire C, Gallo-Payet N, Hyndman D, Veyssiere G, Bertagna X, Jean C & Martinez A (2004) Decreased expression of cyclic adenosine monophosphate-regulated aldose reductase (AKR1B1) is associated with malignancy in human sporadic adrenocortical tumors. J Clin Endocrinol Metab 89, 30103019.
  • 31
    Lefrancois-Martinez AM, Tournaire C, Martinez A, Berger M, Daoudal S, Tritsch D, Veyssiere G & Jean C (1999) 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. J Biol Chem 274, 3287532880.
  • 32
    Irikura D, Aritake K, Nagata N, Maruyama T, Shimamoto S & Urade Y (2009) Biochemical, functional, and pharmacological characterization of AT-56, an orally active and selective inhibitor of lipocalin-type prostaglandin D synthase. J Biol Chem 284, 76237630.
  • 33
    Jez JM, Schlegel BP & Penning TM (1996) Characterization of the substrate binding site in rat liver 3alpha-hydroxysteroid/dihydrodiol dehydrogenase. The roles of tryptophans in ligand binding and protein fluorescence. J Biol Chem 271, 3019030198.
  • 34
    Wang J, Wolf RM, Caldwell JW, Kollman PA & Case DA (2004) Development and testing of a general amber force field. J Comput Chem 25, 11571174.
  • 35
    Fukunishi Y, Mikami Y & Nakamura H (2003) The filling potential method: a method for estimating the free energy surface for protein–ligand docking. J Phys Chem B 107, 1320113210.
  • 36
    Gasteiger J & Marsili M (1980) Iterative partial equalization of orbital electronegativity – a rapid access to atomic charges. Tetrahedron 36, 32193228.
  • 37
    Gasteiger J & Marsili M (1978) A new model for calculating atomic charges in molecules. Tetrahedron Lett 34, 31813184.
  • 38
    Case DA, Darden TA, Cheatham TEI, Simmerling CL, Wang J, Duke RE, Luo R, Merz KM, Wang B, Pearlman DA et al. (2004) AMBER 8. University of California, San Francisco, CA.
  • 39
    DeLano WL (2005) The case for open-source software in drug discovery. Drug Discov Today 10, 213217.