메뉴 건너뛰기




Volumn 50, Issue 1, 1998, Pages 21-33

Aldose reductase in glucose toxicity: A potential target for the prevention of diabetic complications

Author keywords

[No Author keywords available]

Indexed keywords

ALDEHYDE REDUCTASE; ALDOSE REDUCTASE INHIBITOR; GLUCOSE; SORBINIL; TOLRESTAT;

EID: 0031920049     PISSN: 00316997     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Review
Times cited : (505)

References (123)
  • 2
    • 0023582040 scopus 로고
    • Glycation and mactivation of human Cu-Zn-superoxide dismutase. Identification of the in vitro glycated sites
    • Arai K, Maguchi S, Fujii S, Ishibashi H, Oikawa K, and Taniguchi N (1987) Glycation and mactivation of human Cu-Zn-superoxide dismutase. Identification of the in vitro glycated sites J Biol Chem 262:16969-16972.
    • (1987) J Biol Chem , vol.262 , pp. 16969-16972
    • Arai, K.1    Maguchi, S.2    Fujii, S.3    Ishibashi, H.4    Oikawa, K.5    Taniguchi, N.6
  • 3
    • 0041542248 scopus 로고
    • Induction of aldose reductase and sorbitol in renal inner medullary cells by elevated extracellular NaCI
    • Bagnasco SM, Uchida S, Balaban RS, Kador PF, and Burg MB (1987) Induction of aldose reductase and sorbitol in renal inner medullary cells by elevated extracellular NaCI. Proc Natl Acad Sci USA 84:1718-1720.
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 1718-1720
    • Bagnasco, S.M.1    Uchida, S.2    Balaban, R.S.3    Kador, P.F.4    Burg, M.B.5
  • 4
    • 0029103124 scopus 로고
    • Mechanism of human aldehyde reductase: Characterization of the active site pocket
    • Barski OA, Gabbay KH, Grimshaw CE, and Bohren KM (1995) Mechanism of human aldehyde reductase: characterization of the active site pocket. Biochemistry 34: 11264-11275.
    • (1995) Biochemistry , vol.34 , pp. 11264-11275
    • Barski, O.A.1    Gabbay, K.H.2    Grimshaw, C.E.3    Bohren, K.M.4
  • 5
    • 0024333867 scopus 로고
    • The aldo-keto reductase superfamily. cDNAs and deduced amino acid sequences of human aldehyde and aldose reductases
    • Bohren KM, Bullock B, Wennuth B, and Gabbay KH (1989) The aldo-keto reductase superfamily. cDNAs and deduced amino acid sequences of human aldehyde and aldose reductases J Biol Chem 264:9547-9551.
    • (1989) J Biol Chem , vol.264 , pp. 9547-9551
    • Bohren, K.M.1    Bullock, B.2    Wennuth, B.3    Gabbay, K.H.4
  • 6
    • 0026443085 scopus 로고
    • The crystal structure of the aldose reductase: NADPH binary complex
    • Borhani DW, Harter TM, and Petraah JM (1992) The crystal structure of the aldose reductase: NADPH binary complex. J Biol Chem 267:24841-24847.
    • (1992) J Biol Chem , vol.267 , pp. 24841-24847
    • Borhani, D.W.1    Harter, T.M.2    Petraah, J.M.3
  • 7
    • 0025375545 scopus 로고
    • A multicentre trial of the aldose-reductase inhibitor, tolrestat, in patients with symptomatic diabetic neuropathy
    • Boulton AJ, Levin S, and Comstock J (1990) A multicentre trial of the aldose-reductase inhibitor, tolrestat, in patients with symptomatic diabetic neuropathy. Diabetologia 33:431-437.
    • (1990) Diabetologia , vol.33 , pp. 431-437
    • Boulton, A.J.1    Levin, S.2    Comstock, J.3
  • 8
    • 0023803371 scopus 로고
    • Advanced products of nonenzymatic glycosylation and the pathogenesis of diabetic vascular diseases
    • Brownlee M, Cerami A, and Vlaasara H (1988) Advanced products of nonenzymatic glycosylation and the pathogenesis of diabetic vascular diseases. Diabetes Metab Rev 4:437-451.
    • (1988) Diabetes Metab Rev , vol.4 , pp. 437-451
    • Brownlee, M.1    Cerami, A.2    Vlaasara, H.3
  • 9
    • 0021231172 scopus 로고
    • Nonenzymatic glycooylation and the Pathogenesis of diabetic complications
    • Brownlee M, Vlasaara H, and Cerami A (1984) Nonenzymatic glycooylation and the Pathogenesis of diabetic complications Ann Interum Med 101-527-537.
    • (1984) Ann Interum Med , vol.101 , pp. 527-537
    • Brownlee, M.1    Vlasaara, H.2    Cerami, A.3
  • 10
    • 0028894492 scopus 로고
    • Molecular basis of osmotic regulation
    • Burg MB (1995) Molecular basis of osmotic regulation. Am J Physiol 268:F983-996.
    • (1995) Am J Physiol , vol.268
    • Burg, M.B.1
  • 11
    • 0026738167 scopus 로고
    • Impaired contraction and relaxation in aorta from streptozotocin-diabetic rats: Role of polyol pathway activity
    • Cameron NE and Cotter MA (1992) Impaired contraction and relaxation in aorta from streptozotocin-diabetic rats: role of polyol pathway activity Diabetologia 35:1011-1019.
    • (1992) Diabetologia , vol.35 , pp. 1011-1019
    • Cameron, N.E.1    Cotter, M.A.2
  • 12
    • 0028040725 scopus 로고
    • The relationship of vascular changes to metabolic factors in diabetes mellitus and their role in the development of peripheral nature complications
    • Cameron NE, and Cotter MA (1994) The relationship of vascular changes to metabolic factors in diabetes mellitus and their role in the development of peripheral nature complications Diabetes Metab Rev 10:189-224.
    • (1994) Diabetes Metab Rev , vol.10 , pp. 189-224
    • Cameron, N.E.1    Cotter, M.A.2
  • 13
    • 0027193749 scopus 로고
    • Pharmacological manipulation of vascular endothelium function in non-diabetic and streptozotocin-diabetic rats: Effects on nerve conduction, hypoxic resistance and endoneurial pillarization
    • Camerson NE, Cotter MA, Dines KC, and Maxfield EK (1993) Pharmacological manipulation of vascular endothelium function in non-diabetic and streptozotocin-diabetic rats: effects on nerve conduction, hypoxic resistance and endoneurial pillarization. Diabetologia 35:516-522.
    • (1993) Diabetologia , vol.35 , pp. 516-522
    • Camerson, N.E.1    Cotter, M.A.2    Dines, K.C.3    Maxfield, E.K.4
  • 14
    • 0028286444 scopus 로고
    • Aldose reductase inhibition, nerve perfusion, oxygenation and function in streplozotocin-diabetic rata: Dose-response considerations and independence from a myo-inositol mechanism
    • Cameron NE, Cotter MA, Dines KC, Maxfield EK, Carey F, and Mirrleea DJ (1994) Aldose reductase inhibition, nerve perfusion, oxygenation and function in streplozotocin-diabetic rata: dose-response considerations and independence from a myo-inositol mechanism. Diabetologia 37:51-663.
    • (1994) Diabetologia , vol.37 , pp. 51-663
    • Cameron, N.E.1    Cotter, M.A.2    Dines, K.C.3    Maxfield, E.K.4    Carey, F.5    Mirrleea, D.J.6
  • 17
    • 0024438305 scopus 로고
    • Effect of aldose reductase inhibition and insulin treatment on retinal capillary basement membrane thickening in BB rats
    • Chakrabarti S and Sima AA (1989) Effect of aldose reductase inhibition and insulin treatment on retinal capillary basement membrane thickening in BB rats. Diabetes 38:1181-1186.
    • (1989) Diabetes , vol.38 , pp. 1181-1186
    • Chakrabarti, S.1    Sima, A.A.2
  • 18
    • 0023204429 scopus 로고
    • Aldose reductase in the BB rat: Isolation, immunological identification and localization in the retina and peripheral nerve
    • Chakrabarti S, Sima AA, Nakajima T, Yagihashi S, and Greene DA (1987) Aldose reductase in the BB rat: isolation, immunological identification and localization in the retina and peripheral nerve Diabetologia 30:244-251.
    • (1987) Diabetologia , vol.30 , pp. 244-251
    • Chakrabarti, S.1    Sima, A.A.2    Nakajima, T.3    Yagihashi, S.4    Greene, D.A.5
  • 19
    • 0024420222 scopus 로고
    • Cloning and sequence determination of human placental aldose reductase gene
    • Chung S and LaMendola J (1989) Cloning and sequence determination of human placental aldose reductase gene. J Biol. Chem 264:14770-14777.
    • (1989) J Biol. Chem , vol.264 , pp. 14770-14777
    • Chung, S.1    LaMendola, J.2
  • 21
    • 0025313272 scopus 로고
    • Increase in diacylglycerol mass in isolated glomeruli by glucose from de nouv synthesis of glycerolipids
    • Craven PA, Davidson CM, and DeRubertis FR (1990) Increase in diacylglycerol mass in isolated glomeruli by glucose from de nouv synthesis of glycerolipids Diabetes 39:667-674.
    • (1990) Diabetes , vol.39 , pp. 667-674
    • Craven, P.A.1    Davidson, C.M.2    DeRubertis, F.R.3
  • 22
    • 0031024997 scopus 로고    scopus 로고
    • Isolation of the mouse aldose reductase promoter and identification of a tonicity-responsive element
    • Daoudal S, Tournaire C, Halere A, VeyssiOere G, and Jean C (1997) Isolation of the mouse aldose reductase promoter and identification of a tonicity-responsive element. J Biol Chem 272:2615-2619.
    • (1997) J Biol Chem , vol.272 , pp. 2615-2619
    • Daoudal, S.1    Tournaire, C.2    Halere, A.3    VeyssiOere, G.4    Jean, C.5
  • 23
    • 0027370108 scopus 로고
    • The effect of intensive treatment of diabetes on the development and progression of long-term complications in insulin-dependent diabetes mellitus
    • Diabetes Control and Complications Trial Research Group (1993) The effect of intensive treatment of diabetes on the development and progression of long-term complications in insulin-dependent diabetes mellitus. N Engl J Med 329:977-986.
    • (1993) N Engl J Med , vol.329 , pp. 977-986
  • 24
    • 0028346373 scopus 로고
    • A delayed-early gene activated by fibroblast growth factor-1 encodes a protein related to aldose reductase
    • Donohue PJ, Alberts GF, Hampton BS, and Winkles JA (1994) A delayed-early gene activated by fibroblast growth factor-1 encodes a protein related to aldose reductase. J Biol Chem 269:8604-8609.
    • (1994) J Biol Chem , vol.269 , pp. 8604-8609
    • Donohue, P.J.1    Alberts, G.F.2    Hampton, B.S.3    Winkles, J.A.4
  • 25
    • 0022618827 scopus 로고
    • The spatial distribution of fiber loss in diabetic polyneuropathy suggests ischemia
    • Dyck PJ, Karnes JL, O'Brien P, Okazaki H, Lais A, and Engelstad J (1986) The spatial distribution of fiber loss in diabetic polyneuropathy suggests ischemia. Ann Neural 19:440-449.
    • (1986) Ann Neural , vol.19 , pp. 440-449
    • Dyck, P.J.1    Karnes, J.L.2    O'Brien, P.3    Okazaki, H.4    Lais, A.5    Engelstad, J.6
  • 26
    • 84914325794 scopus 로고
    • Diabetic neuropathy: A clinical and histologic study on the significance of vascular affections
    • Fagerberg SE (1959) Diabetic neuropathy: a clinical and histologic study on the significance of vascular affections. Acta Med Scand 164:1-80.
    • (1959) Acta Med Scand , vol.164 , pp. 1-80
    • Fagerberg, S.E.1
  • 27
    • 0021884170 scopus 로고
    • Limited benefit of treatment of diabetic polyneuropathy with an aldose reductase inhibitor: A 24-week controlled trial
    • Fagius J, Brattberg A, Jameson S, and Berne C (1985) Limited benefit of treatment of diabetic polyneuropathy with an aldose reductase inhibitor: a 24-week controlled trial. Diabetologia 28:323-329.
    • (1985) Diabetologia , vol.28 , pp. 323-329
    • Fagius, J.1    Brattberg, A.2    Jameson, S.3    Berne, C.4
  • 28
    • 0029039747 scopus 로고
    • Catalysis of reduction of carbohydrate 2-oxoaldehydes (osones) by mammalian aldose reductase and aldehyde reductase
    • Feather MS, Flynn TG, Munro KA, Kubiseski TJ, and Walton DJ (1995) Catalysis of reduction of carbohydrate 2-oxoaldehydes (osones) by mammalian aldose reductase and aldehyde reductase. Biochim Biophys Acta 1244:10-16.
    • (1995) Biochim Biophys Acta , vol.1244 , pp. 10-16
    • Feather, M.S.1    Flynn, T.G.2    Munro, K.A.3    Kubiseski, T.J.4    Walton, D.J.5
  • 30
    • 0029770440 scopus 로고    scopus 로고
    • ORE, a eukaryotic minimal essential osmotic response element. the aldose reductase gene in hyperosmotic stress
    • Ferraris JD, Williams CK, Jung KY, Bedford JJ, Burg MB, and Garcia-Perez A (1996) ORE, a eukaryotic minimal essential osmotic response element. The aldose reductase gene in hyperosmotic stress. J Biol Chem 271:18318-18321.
    • (1996) J Biol Chem , vol.271 , pp. 18318-18321
    • Ferraris, J.D.1    Williams, C.K.2    Jung, K.Y.3    Bedford, J.J.4    Burg, M.B.5    Garcia-Perez, A.6
  • 31
    • 0021043111 scopus 로고
    • Golactoro-induced retinal capillary basement membrane thickening: Prevention by Sorbinil
    • Frank RN, Keirn RJ, Kennedy A, and Frank KW (1983) Golactoro-induced retinal capillary basement membrane thickening: prevention by Sorbinil. Invest Opthalmol & Visual Sci 24:1519-1524.
    • (1983) Invest Opthalmol & Visual Sci , vol.24 , pp. 1519-1524
    • Frank, R.N.1    Keirn, R.J.2    Kennedy, A.3    Frank, K.W.4
  • 33
    • 0028943426 scopus 로고
    • Tolrestat in the primary prevention of diabetic neuropathy
    • Giugliano D, Misso L, and Acampora R (1995) Tolrestat in the primary prevention of diabetic neuropathy. Diabetes Care 18:536-541.
    • (1995) Diabetes Care , vol.18 , pp. 536-541
    • Giugliano, D.1    Misso, L.2    Acampora, R.3
  • 35
    • 0027254362 scopus 로고
    • Effects of aldose reductase inhibitors on the progression of nerve damage
    • Greene DA and Sima AAF (1993) Effects of aldose reductase inhibitors on the progression of nerve damage. Diabetic Med 10:31S-32S
    • (1993) Diabetic Med , vol.10
    • Greene, D.A.1    Sima, A.A.F.2
  • 36
    • 0023116890 scopus 로고
    • Sorbitol, phoaphoinositides, and sodium-potassium-ATPase in the pathogenesis of diabetic complications
    • Greene DA, Lattimer SA, and Sima AA (1987) Sorbitol, phoaphoinositides, and sodium-potassium-ATPase in the pathogenesis of diabetic complications. N Engl J Med 316:599-606.
    • (1987) N Engl J Med , vol.316 , pp. 599-606
    • Greene, D.A.1    Lattimer, S.A.2    Sima, A.A.3
  • 38
    • 0028839089 scopus 로고
    • Presence of a closely related subgroup in the aldo-ketoreductaee family of the mouse
    • Gui T, Tanimoto T, Kokai Y, and Nishimura C (1995) Presence of a closely related subgroup in the aldo-ketoreductaee family of the mouse. Eur J Biochem 227:448-453.
    • (1995) Eur J Biochem , vol.227 , pp. 448-453
    • Gui, T.1    Tanimoto, T.2    Kokai, Y.3    Nishimura, C.4
  • 39
    • 0026063179 scopus 로고
    • Crucial role of aldose reductase activity and plasma glucose level in sorbitol accumulation in erythrocytes from diabetic patients
    • Hamada Y, Kitoh R, and Raskin P (1991) Crucial role of aldose reductase activity and plasma glucose level in sorbitol accumulation in erythrocytes from diabetic patients. Diabetes 40:1233-1240.
    • (1991) Diabetes , vol.40 , pp. 1233-1240
    • Hamada, Y.1    Kitoh, R.2    Raskin, P.3
  • 40
    • 0027417982 scopus 로고
    • Association of erythrocyte aldose reductase activity with diabetic complications in type 1 diabetes
    • Hamada Y, Kitoh R, and Raskin P (1993) Association of erythrocyte aldose reductase activity with diabetic complications in type 1 diabetes. Diabetic Med 10:33-38.
    • (1993) Diabetic Med , vol.10 , pp. 33-38
    • Hamada, Y.1    Kitoh, R.2    Raskin, P.3
  • 41
    • 0026323337 scopus 로고
    • Aminoguanidine treatment inhibits the development of experimental diabetic retinopathy
    • Hammes HP, Martin S, Federlin K, Geisen K, and Brownlee M (1991) Aminoguanidine treatment inhibits the development of experimental diabetic retinopathy. Proc Natl Acad Sci USA 88:11555-11558.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 11555-11558
    • Hammes, H.P.1    Martin, S.2    Federlin, K.3    Geisen, K.4    Brownlee, M.5
  • 42
    • 0000930578 scopus 로고
    • Isolation and properties of lens aldose reductase
    • Hayman S and Kinoshita JH (1965) Isolation and properties of lens aldose reductase J Biol Chem 240:877-882.
    • (1965) J Biol Chem , vol.240 , pp. 877-882
    • Hayman, S.1    Kinoshita, J.H.2
  • 43
    • 0027202755 scopus 로고
    • Altered aldose reductase gene regulation in cultured human retinal pigment epithelial cells
    • Henry DN, Del MM, Greene DA, and Killen PD (1993) Altered aldose reductase gene regulation in cultured human retinal pigment epithelial cells. J Clin Invest 92: 617-623.
    • (1993) J Clin Invest , vol.92 , pp. 617-623
    • Henry, D.N.1    Del, M.M.2    Greene, D.A.3    Killen, P.D.4
  • 44
    • 0000116568 scopus 로고
    • Le Mechanisme de la transformation de glucose en fructose par les vesicules seminales
    • Hers HG (1956) Le Mechanisme de la transformation de glucose en fructose par les vesicules seminales. Biochim Biophys Acta 22202-203.
    • (1956) Biochim Biophys Acta , vol.22 , pp. 202-203
    • Hers, H.G.1
  • 45
    • 0024557533 scopus 로고
    • Aldose reductase and polyol in cultured pericytes of human retinal capillaries
    • Hohman TC, Nishimura C, and Robison WG, Jr (1989) Aldose reductase and polyol in cultured pericytes of human retinal capillaries. Exp Eye Res 48:55-60.
    • (1989) Exp Eye Res , vol.48 , pp. 55-60
    • Hohman, T.C.1    Nishimura, C.2    Robison Jr., W.G.3
  • 46
    • 0027255884 scopus 로고
    • Oxidative alterations in the experimental glycation model of diabetes mellitus are due to protein-glucose adduct oxidation. Some fundamental differences in proposed mechanisms of glucose oxidation and oxidant production
    • Hunt JV, Bottoms MA, and Mitchinson MJ (1993) Oxidative alterations in the experimental glycation model of diabetes mellitus are due to protein-glucose adduct oxidation. Some fundamental differences in proposed mechanisms of glucose oxidation and oxidant production. Biochem J 291:529-535.
    • (1993) Biochem J , vol.291 , pp. 529-535
    • Hunt, J.V.1    Bottoms, M.A.2    Mitchinson, M.J.3
  • 49
    • 0030871930 scopus 로고    scopus 로고
    • The level of erythrocyte aldose reductage: A risk factor for diabetic neuropathy?
    • Ito T, Nishimura C, Takahashi Y, Saito T, and Omori Y (1997) The level of erythrocyte aldose reductage: a risk factor for diabetic neuropathy? Diabetes Res Clin Pract 36:161-167.
    • (1997) Diabetes Res Clin Pract , vol.36 , pp. 161-167
    • Ito, T.1    Nishimura, C.2    Takahashi, Y.3    Saito, T.4    Omori, Y.5
  • 51
    • 0025117987 scopus 로고
    • The purification and properties of aldose reductase from rat ovary
    • Iwata N, Inazu N, and Satoh T (1990) The purification and properties of aldose reductase from rat ovary. Arch Biochem Biophys 282:70-77.
    • (1990) Arch Biochem Biophys , vol.282 , pp. 70-77
    • Iwata, N.1    Inazu, N.2    Satoh, T.3
  • 52
    • 0030973817 scopus 로고    scopus 로고
    • A nomenclature system for the aldo-keto reductase superfamily
    • (Weiner H, Lindahl R, Crabb DW, and Flynn TG, eds) Plenum Press, New York
    • Jez JM, Flynn GF, and Penning TM (1996) A nomenclature system for the aldo-keto reductase superfamily, in Enzymology and Molecular Biology of Carbonyl Metabolism 6 (Weiner H, Lindahl R, Crabb DW, and Flynn TG, eds) pp 579-589, Plenum Press, New York.
    • (1996) Enzymology and Molecular Biology of Carbonyl Metabolism , vol.6 , pp. 579-589
    • Jez, J.M.1    Flynn, G.F.2    Penning, T.M.3
  • 54
    • 0025218060 scopus 로고
    • Induction of aldose reductase expression in rat kidney mesangial cells and Chinese hamster ovary cells under hypertonic conditions
    • Kaneko M, Carper D, Nishimura C, Millen J, Bock M, and Hohman TC (1990) Induction of aldose reductase expression in rat kidney mesangial cells and Chinese hamster ovary cells under hypertonic conditions. Exp Cell Res 188:135-140.
    • (1990) Exp Cell Res , vol.188 , pp. 135-140
    • Kaneko, M.1    Carper, D.2    Nishimura, C.3    Millen, J.4    Bock, M.5    Hohman, T.C.6
  • 56
    • 0020564549 scopus 로고
    • Aldose reductase activity in retinal and cerebral microvessels and cultured vascular cells
    • Kennedy A, Frank RN, and Varma SD (1983) Aldose reductase activity in retinal and cerebral microvessels and cultured vascular cells. Invest Opthalmol & Visual Sci 24:1250-1258.
    • (1983) Invest Opthalmol & Visual Sci , vol.24 , pp. 1250-1258
    • Kennedy, A.1    Frank, R.N.2    Varma, S.D.3
  • 57
    • 0029091370 scopus 로고
    • Substrate specificity, gene structure, and tissue-specific distribution of multiple human 3α-hydroxysteroid dehydrogenase
    • Khanna M, Qin K-N, Wang RW, and Cheng K-C (1995) Substrate specificity, gene structure, and tissue-specific distribution of multiple human 3α-hydroxysteroid dehydrogenase. J Biol Chem 270:20162-20168.
    • (1995) J Biol Chem , vol.270 , pp. 20162-20168
    • Khanna, M.1    Qin, K.-N.2    Wang, R.W.3    Cheng, K.-C.4
  • 58
    • 0023913225 scopus 로고
    • The involvement of aldose reductase in diabetic complications
    • Kinoshita JH and Nishimura C (1988) The involvement of aldose reductase in diabetic complications Diabetes Metab Rev 4:323-337.
    • (1988) Diabetes Metab Rev , vol.4 , pp. 323-337
    • Kinoshita, J.H.1    Nishimura, C.2
  • 59
    • 0030908643 scopus 로고    scopus 로고
    • Identification and characterization of multiple osmotic response sequences in the human aldose reductase gene
    • Ko BCB, Ruepp B, Bohren KM, and Gabbay KH (1997) Identification and characterization of multiple osmotic response sequences in the human aldose reductase gene. J Biol Chem 272:16431-16437.
    • (1997) J Biol Chem , vol.272 , pp. 16431-16437
    • Ko, B.C.B.1    Ruepp, B.2    Bohren, K.M.3    Gabbay, K.H.4
  • 60
    • 0028213845 scopus 로고
    • Aldose reductase-catalyzed reduction of acrolein: Implications in cyclophosphamide toxicity
    • Kolb NS, Hunsaker LA, and Vander Jagt DL (1994) Aldose reductase-catalyzed reduction of acrolein: implications in cyclophosphamide toxicity. Mol Pharmacol 45:797-801.
    • (1994) Mol Pharmacol , vol.45 , pp. 797-801
    • Kolb, N.S.1    Hunsaker, L.A.2    Vander Jagt, D.L.3
  • 61
    • 0027979898 scopus 로고
    • Cloning and expression of cDNA of human delta 4-3-oxosteroid 5 beta-reductase and substrate specificity of the expressed enzyme
    • Kondo KH, Kai MH, Setoguchi Y, Eggertsen G, Sjoblom P, Sctoguchi T, Okuda KI, and Bjorkhem (1994) Cloning and expression of cDNA of human delta 4-3-oxosteroid 5 beta-reductase and substrate specificity of the expressed enzyme Eur J Biochem 219:357-363.
    • (1994) Eur J Biochem , vol.219 , pp. 357-363
    • Kondo, K.H.1    Kai, M.H.2    Setoguchi, Y.3    Eggertsen, G.4    Sjoblom, P.5    Sctoguchi, T.6    Okuda, K.I.7    Bjorkhem8
  • 62
    • 0026631063 scopus 로고
    • A 12-month randomized controlled study of the aldose reductase inhibitor ponalrestat in patients with chronic symptomatic diabetic neuropathy
    • Krentz AJ, Honigsberger L, Ellis SH, Hardman M, and Nattrass M (1992) A 12-month randomized controlled study of the aldose reductase inhibitor ponalrestat in patients with chronic symptomatic diabetic neuropathy, Diabetic Med 9:463-468.
    • (1992) Diabetic Med , vol.9 , pp. 463-468
    • Krentz, A.J.1    Honigsberger, L.2    Ellis, S.H.3    Hardman, M.4    Nattrass, M.5
  • 63
    • 0000358508 scopus 로고
    • Activation of protein kinase C by elevation of glucose concentration: Proposal for a mechanism in the development of diabetic vascular complications
    • Lee T-S, Saltsman KA, Ohashi H, and King GL (1989) Activation of protein kinase C by elevation of glucose concentration: proposal for a mechanism in the development of diabetic vascular complications. Proc Natl Acad Sci USA 86:5141-5145.
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 5141-5145
    • Lee, T.-S.1    Saltsman, K.A.2    Ohashi, H.3    King, G.L.4
  • 64
    • 0029992934 scopus 로고    scopus 로고
    • Aldose reductase is a major reductase for isocaproaldehyde, a product of side-chain cleavage of cholesterol, in human and animal adrenal glands
    • Matsuura K, Deyashiki Y, Bunai Y, Ohya I, and Kara A (1996) Aldose reductase is a major reductase for isocaproaldehyde, a product of side-chain cleavage of cholesterol, in human and animal adrenal glands. Arch Biochem Biophys 328:265-271.
    • (1996) Arch Biochem Biophys , vol.328 , pp. 265-271
    • Matsuura, K.1    Deyashiki, Y.2    Bunai, Y.3    Ohya, I.4    Kara, A.5
  • 65
    • 0021984681 scopus 로고
    • Oxygen-derived free radicals in postischemic tissue injury
    • McCord JM (1985) Oxygen-derived free radicals in postischemic tissue injury. N Engl J Med 312:159-163.
    • (1985) N Engl J Med , vol.312 , pp. 159-163
    • McCord, J.M.1
  • 69
    • 10144251743 scopus 로고    scopus 로고
    • The efficacy of tolrestat in the treatment of diabetic peripheral neuropathy. A metaanalysis of individual patient data
    • Nicolucci A, Carinci F, Graepel JG, Hohman TC, Ferris F, and Lachm JM (1996) The efficacy of tolrestat in the treatment of diabetic peripheral neuropathy. A metaanalysis of individual patient data. Diabetes Care 19:1091-1096.
    • (1996) Diabetes Care , vol.19 , pp. 1091-1096
    • Nicolucci, A.1    Carinci, F.2    Graepel, J.G.3    Hohman, T.C.4    Ferris, F.5    Lachm, J.M.6
  • 70
    • 0027182340 scopus 로고
    • Quantitative determination of human aldose reductase by enzyme-linked immunosorbent assay. Immunoassay of human aldose reductase
    • Nishimura C, Furue M, Ito T, Omori Y, and Tanimoto T (1993) Quantitative determination of human aldose reductase by enzyme-linked immunosorbent assay. Immunoassay of human aldose reductase. Biochem Pnarmacol 46:21-28.
    • (1993) Biochem Pnarmacol , vol.46 , pp. 21-28
    • Nishimura, C.1    Furue, M.2    Ito, T.3    Omori, Y.4    Tanimoto, T.5
  • 74
    • 0023240968 scopus 로고
    • Depletion of myo-inositol and amino acids in galactosemic neuropathy
    • Nishimura C, Lou MF, and Kinoshita JH (1987) Depletion of myo-inositol and amino acids in galactosemic neuropathy. J Neurochem 49:290-295.
    • (1987) J Neurochem , vol.49 , pp. 290-295
    • Nishimura, C.1    Lou, M.F.2    Kinoshita, J.H.3
  • 76
    • 0028280426 scopus 로고
    • High levels of erythrocyte aldose reductase and diabetic retinopathy in NIDDM patients
    • Nishimura C, Saito T, Ito T, Otmori Y, and Tanimoto T (1994b) High levels of erythrocyte aldose reductase and diabetic retinopathy in NIDDM patients. Diabetologia 37:328-330.
    • (1994) Diabetologia , vol.37 , pp. 328-330
    • Nishimura, C.1    Saito, T.2    Ito, T.3    Otmori, Y.4    Tanimoto, T.5
  • 77
    • 0025829982 scopus 로고
    • Purification and characterization of the recombinant human aldose reductase expressed in baculovirus system
    • Nishimura C, Yamaoka T, Mizutani M, Yamashita K, Akera T, and Taaimoto T (1991) Purification and characterization of the recombinant human aldose reductase expressed in baculovirus system Biochim Biophys Acta 1078:171-178.
    • (1991) Biochim Biophys Acta , vol.1078 , pp. 171-178
    • Nishimura, C.1    Yamaoka, T.2    Mizutani, M.3    Yamashita, K.4    Akera, T.5    Taaimoto, T.6
  • 78
    • 0023774175 scopus 로고
    • Aldose reductase inhibition in diabetic neuropathy: Clinical and neurophysiological studies of one year's treatment with sorbinil
    • O'Hare JP, Morgan MH, Alden P, Chissel S, OBrien LA, and Corrall RJ (1988) Aldose reductase inhibition in diabetic neuropathy: clinical and neurophysiological studies of one year's treatment with sorbinil. Diabetic Med 5:537-542.
    • (1988) Diabetic Med , vol.5 , pp. 537-542
    • O'Hare, J.P.1    Morgan, M.H.2    Alden, P.3    Chissel, S.4    Obrien, L.A.5    Corrall, R.J.6
  • 79
    • 0025258521 scopus 로고
    • Androgen-dependent protein from mouse vas deferens. cDNA cloning and protein homology with the aldo-keto reductase superfamily
    • Pailhoux EA, Martinez A, Veyssiere GM, and Jean CG (1990) Androgen-dependent protein from mouse vas deferens. cDNA cloning and protein homology with the aldo-keto reductase superfamily. J Biol Chem 268:19932-19936.
    • (1990) J Biol Chem , vol.268 , pp. 19932-19936
    • Pailhoux, E.A.1    Martinez, A.2    Veyssiere, G.M.3    Jean, C.G.4
  • 80
    • 0030973816 scopus 로고    scopus 로고
    • A potential role for aldose reductase in steroid metabolism
    • (Weiner H, Lindahl R, Crabb DW, and Flynn TG, eds) Plenum Press, New York
    • Petrash JM, Harter TM, and Murdock GL (1996) A potential role for aldose reductase in steroid metabolism, in Enzymology and Molecular Biology of Carbonyl Metabolism 6 (Weiner H, Lindahl R, Crabb DW, and Flynn TG, eds) pp 465-473, Plenum Press, New York.
    • (1996) Enzymology and Molecular Biology of Carbonyl Metabolism , vol.6 , pp. 465-473
    • Petrash, J.M.1    Harter, T.M.2    Murdock, G.L.3
  • 81
    • 0030931810 scopus 로고    scopus 로고
    • Aldose reductase inhibitors: The end of an erea or the need for different trial designs?
    • Pfeifer MA, Schumer MP, and Gelber DA (1996) Aldose reductase inhibitors: the end of an erea or the need for different trial designs? Diabetes 46:S82-S89.
    • (1996) Diabetes , vol.46
    • Pfeifer, M.A.1    Schumer, M.P.2    Gelber, D.A.3
  • 82
    • 0025767877 scopus 로고
    • Glucose-induced metabolic imbalances in the pathogenesis of diabetic vascular disease
    • Pugliese G, Tilton GT, and Williamson JR (1991) Glucose-induced metabolic imbalances in the pathogenesis of diabetic vascular disease. Diabetes Metab Rev 7:35-59.
    • (1991) Diabetes Metab Rev , vol.7 , pp. 35-59
    • Pugliese, G.1    Tilton, G.T.2    Williamson, J.R.3
  • 83
    • 0030041937 scopus 로고    scopus 로고
    • Increased levels of methylglyoxal-metabolizing enzymes in mononuclear and polymorphonuclear cells from insulin-dependent diabetic patients with diabetic complications: Aldose reductase, glyoxalase I, and glyoxalase II - A clinical research center study
    • Ratliff DM, Vander Jagt DJ, Eaton RP, and Vander Jagt DL (1996) Increased levels of methylglyoxal-metabolizing enzymes in mononuclear and polymorphonuclear cells from insulin-dependent diabetic patients with diabetic complications: aldose reductase, glyoxalase I, and glyoxalase II - a clinical research center study. J Clin Endocrinol & Metab 81:488-492.
    • (1996) J Clin Endocrinol & Metab , vol.81 , pp. 488-492
    • Ratliff, D.M.1    Vander Jagt, D.J.2    Eaton, R.P.3    Vander Jagt, D.L.4
  • 85
    • 0020604667 scopus 로고
    • Retinal capillaries: Basement membrane thickening by galactosemia prevented with aldose reductase inhibitor
    • Robison WG, Jr, Kador PF and Kinoshita JH (1983) Retinal capillaries: basement membrane thickening by galactosemia prevented with aldose reductase inhibitor Science 221:1177-1179.
    • (1983) Science , vol.221 , pp. 1177-1179
    • Robison Jr., W.G.1    Kador, P.F.2    Kinoshita, J.H.3
  • 88
    • 0025171028 scopus 로고
    • Inhibition of aldehyde reductase by aldose reductase inhibitors
    • Sato S and Kador PF (1990) Inhibition of aldehyde reductase by aldose reductase inhibitors Biochem Pharmacol 40:1033-1042.
    • (1990) Biochem Pharmacol , vol.40 , pp. 1033-1042
    • Sato, S.1    Kador, P.F.2
  • 90
    • 0023748415 scopus 로고
    • Regeneration and repair of myelinated fibers in sural-nerve biopsy specimens from patients with diabetic neuropathy treated with sorbinil
    • Sima AA, Bril V, Nathaniel V, McEwen TA, Brown MB, Lattimer SA, and Greene DA (1988) Regeneration and repair of myelinated fibers in sural-nerve biopsy specimens from patients with diabetic neuropathy treated with sorbinil. N Engl J Med 319:548-555.
    • (1988) N Engl J Med , vol.319 , pp. 548-555
    • Sima, A.A.1    Bril, V.2    Nathaniel, V.3    McEwen, T.A.4    Brown, M.B.5    Lattimer, S.A.6    Greene, D.A.7
  • 93
    • 0027158606 scopus 로고
    • cDNA Cloning and expression of the human hepatic bile acid-binding protein
    • Stolz A, Hammond L, Lou H, Takikawa H, Ronk M, and Shively JE (1993) cDNA Cloning and expression of the human hepatic bile acid-binding protein. J Biol Chem 268:10448-10457.
    • (1993) J Biol Chem , vol.268 , pp. 10448-10457
    • Stolz, A.1    Hammond, L.2    Lou, H.3    Takikawa, H.4    Ronk, M.5    Shively, J.E.6
  • 94
    • 0015831493 scopus 로고
    • Enzymatic reduction of "biogenic" aldehydes in brain
    • Tabakoff B, Anderson R, and Alivisatos SGA (1973) Enzymatic reduction of "biogenic" aldehydes in brain. Mol Pharmacol 9:428-437.
    • (1973) Mol Pharmacol , vol.9 , pp. 428-437
    • Tabakoff, B.1    Anderson, R.2    Alivisatos, S.G.A.3
  • 95
    • 0021760428 scopus 로고
    • A novel type of crystallin in the frog eye lens. 35-kDa polypeptide is not homologous to any of the major classes of lens crystallins
    • Tamarev AS, Zinovieva RD, Dolgilevich SM, Luchin SD, Krayev AS, Skryabin KG, and Gause GGJ (1984) A novel type of crystallin in the frog eye lens. 35-kDa polypeptide is not homologous to any of the major classes of lens crystallins. FEBS Lett 171:297-302.
    • (1984) FEBS Lett , vol.171 , pp. 297-302
    • Tamarev, A.S.1    Zinovieva, R.D.2    Dolgilevich, S.M.3    Luchin, S.D.4    Krayev, A.S.5    Skryabin, K.G.6    Gause, G.G.J.7
  • 97
    • 0021279144 scopus 로고
    • Prevention and reversal of defective axonal transport and motor nerve conduction velocity in rats with experimental diabetes by treatment with the aldose reductase inhibitor Sorbinil
    • Tomlinson DR, Moriarty RJ, and Mayer JH (1984) Prevention and reversal of defective axonal transport and motor nerve conduction velocity in rats with experimental diabetes by treatment with the aldose reductase inhibitor Sorbinil. Diabetes 33:470-476.
    • (1984) Diabetes , vol.33 , pp. 470-476
    • Tomlinson, D.R.1    Moriarty, R.J.2    Mayer, J.H.3
  • 98
    • 0021145258 scopus 로고
    • Endoneurial blood flow and oxygen tension in the sciatic nerve of rats with experimental diabetic neuropathy
    • Tuck RR, Schmelzer JD, and Low PA (1984) Endoneurial blood flow and oxygen tension in the sciatic nerve of rats with experimental diabetic neuropathy. Brain 107:935-950.
    • (1984) Brain , vol.107 , pp. 935-950
    • Tuck, R.R.1    Schmelzer, J.D.2    Low, P.A.3
  • 99
    • 0015445926 scopus 로고
    • The characterization of two reduced nicotinamideadenine dinucleotide phosphate-linked aldehyde reductases from pig brain
    • Turner AJ and Tipton KF (1972) The characterization of two reduced nicotinamideadenine dinucleotide phosphate-linked aldehyde reductases from pig brain. Biochem J 130:765-772.
    • (1972) Biochem J , vol.130 , pp. 765-772
    • Turner, A.J.1    Tipton, K.F.2
  • 100
    • 0031570301 scopus 로고    scopus 로고
    • A 'specificity' pocket inferred from the crystal structures of the complexes of aldose reductase with the pharmaceutically important inhibitors tolrestat and sorbinil
    • Urzhumtsev A, Téte-Favier F, Mitschler A, Barbanton J, Barth P, Urzhumtseva L, Biellmann J-F, Podjarny AD, and Moras D (1997) A 'specificity' pocket inferred from the crystal structures of the complexes of aldose reductase with the pharmaceutically important inhibitors tolrestat and sorbinil Structure 5:601-612.
    • (1997) Structure , vol.5 , pp. 601-612
    • Urzhumtsev, A.1    Téte-Favier, F.2    Mitschler, A.3    Barbanton, J.4    Barth, P.5    Urzhumtseva, L.6    Biellmann, J.-F.7    Podjarny, A.D.8    Moras, D.9
  • 101
    • 0000841548 scopus 로고
    • Formation of polyols by the lens of the rat with 'sugar' cataract
    • van Heyningen R (1959) Formation of polyols by the lens of the rat with 'sugar' cataract Nature 468:194-195.
    • (1959) Nature , vol.468 , pp. 194-195
    • Van Heyningen, R.1
  • 102
    • 0025193840 scopus 로고
    • Aldehyde and aldose reductases from human placenta Heterogeneous expression of multiple enzyme forms
    • Vander Jagt DL, Hunsaker LA, Robinson B, Stangebye LA, and Deck LM (1990) Aldehyde and aldose reductases from human placenta Heterogeneous expression of multiple enzyme forms. J Biol Chem 266:10912-10918.
    • (1990) J Biol Chem , vol.266 , pp. 10912-10918
    • Vander Jagt, D.L.1    Hunsaker, L.A.2    Robinson, B.3    Stangebye, L.A.4    Deck, L.M.5
  • 104
    • 0026646131 scopus 로고
    • Reduction of trioscs by NADPH-dependent aldo-keto reductases Aldose reductase, methylglyoxal, and diabetic complications
    • Vander Jagt DL, Robinson B, Taylor KK, and Hunsaker LA (1992) Reduction of trioscs by NADPH-dependent aldo-keto reductases Aldose reductase, methylglyoxal, and diabetic complications. J Biol Chem 267:4364-4369.
    • (1992) J Biol Chem , vol.267 , pp. 4364-4369
    • Vander Jagt, D.L.1    Robinson, B.2    Taylor, K.K.3    Hunsaker, L.A.4
  • 106
    • 0016354878 scopus 로고
    • The absence of cataracts in mice with congenital hyperglycemia
    • Varma SD and Kinoshita JH (1974) The absence of cataracts in mice with congenital hyperglycemia Exp Eye Res 19:577-582.
    • (1974) Exp Eye Res , vol.19 , pp. 577-582
    • Varma, S.D.1    Kinoshita, J.H.2
  • 107
    • 0027275780 scopus 로고
    • Characterization of the human aldose reductase gene promoter
    • Wang K, Bohren KM, and Gabbay KH (1993) Characterization of the human aldose reductase gene promoter J Biol Chem 268:16052-16058.
    • (1993) J Biol Chem , vol.268 , pp. 16052-16058
    • Wang, K.1    Bohren, K.M.2    Gabbay, K.H.3
  • 108
    • 0027461303 scopus 로고
    • Molecular cloning of testicular 20 alpha-hydroxysteroid dehydrogenase: Identity with aldose reductase
    • Warren JC, Murdock GL, Ma Y, Goodman SR, and Zimmer WE (1993) Molecular cloning of testicular 20 alpha-hydroxysteroid dehydrogenase: identity with aldose reductase. Biochemtstry 32:1401-1406.
    • (1993) Biochemtstry , vol.32 , pp. 1401-1406
    • Warren, J.C.1    Murdock, G.L.2    Ma, Y.3    Goodman, S.R.4    Zimmer, W.E.5
  • 109
    • 0020620332 scopus 로고
    • Aldose and aldehyde reductase exhibit isocortico-steroid reductase activity
    • Wermuth B and Monder C (1983) Aldose and aldehyde reductase exhibit isocortico-steroid reductase activity Eur J Biochem 131:423-426.
    • (1983) Eur J Biochem , vol.131 , pp. 423-426
    • Wermuth, B.1    Monder, C.2
  • 110
    • 0020461029 scopus 로고
    • Purification and characterization of human brain aldose reductase
    • Wermuth B, Burgisser H, Bohren K, and von Wartburg J-P (1982) Purification and characterization of human brain aldose reductase. Eur J Biochem 127:279-284.
    • (1982) Eur J Biochem , vol.127 , pp. 279-284
    • Wermuth, B.1    Burgisser, H.2    Bohren, K.3    Von Wartburg, J.-P.4
  • 112
    • 0028988922 scopus 로고
    • Glucose-induced vascular smooth muscle dysfunction: The role of protein kinase C
    • Williams B (1995) Glucose-induced vascular smooth muscle dysfunction: the role of protein kinase C J Hypertens 13:477-486.
    • (1995) J Hypertens , vol.13 , pp. 477-486
    • Williams, B.1
  • 113
    • 0026719692 scopus 로고
    • An unlikely sugar substrate site in the 1.65 Á structure of the human aldose reductase holoenzyme implicated in diabetic complications
    • Wilson DK, Bohren KM, Gabbay KH, and Quiocho FA (1992) An unlikely sugar substrate site in the 1.65 Á structure of the human aldose reductase holoenzyme implicated in diabetic complications. Science 257:81-84.
    • (1992) Science , vol.257 , pp. 81-84
    • Wilson, D.K.1    Bohren, K.M.2    Gabbay, K.H.3    Quiocho, F.A.4
  • 114
    • 0028970887 scopus 로고
    • 1.7 A structure of FR-1. a fibroblast growth factor-induced member of the aldo-keto reductase family. complexed with coenzyme and inhibitor
    • Wilson DK, Nakano T, Petrash JM, and Quiocho FA (1995) 1.7 A structure of FR-1. a fibroblast growth factor-induced member of the aldo-keto reductase family. complexed with coenzyme and inhibitor. Biochemistry 34:14323-14330.
    • (1995) Biochemistry , vol.34 , pp. 14323-14330
    • Wilson, D.K.1    Nakano, T.2    Petrash, J.M.3    Quiocho, F.A.4
  • 115
    • 0030943362 scopus 로고    scopus 로고
    • Structure studies of aldo-keto reductase inhibition
    • (Weiner H. Lindah) R. Crabb DW, and Flynn TG, eds Plenum Press, New York
    • Wilson DK, Nakano T, Petrash JM, and Quiocho FA (1996) Structure studies of aldo-keto reductase inhibition, in Enzymology and Molecular Biology of Carbonyl Metabolism 6 (Weiner H. Lindah) R. Crabb DW, and Flynn TG, eds) pp 435-442. Plenum Press, New York.
    • (1996) Enzymology and Molecular Biology of Carbonyl Metabolism , vol.6 , pp. 435-442
    • Wilson, D.K.1    Nakano, T.2    Petrash, J.M.3    Quiocho, F.A.4
  • 116
    • 0027378377 scopus 로고
    • Refined 1.8 Á structure of human aldose reductase completed with the potent inhibitor zopolrestat
    • Wilson DK, Tarle I, Petrash JM, and Quiocho FA (1993) Refined 1.8 Á structure of human aldose reductase completed with the potent inhibitor zopolrestat. Proc Natl Acad Sci USA 90:9847-9851.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 9847-9851
    • Wilson, D.K.1    Tarle, I.2    Petrash, J.M.3    Quiocho, F.A.4
  • 117
    • 0025177344 scopus 로고
    • Isolation and characterization of cloned cDNAs encoding human liver chlordecone reductase
    • Winters CJ, Molowa DT, and Guzelian PS (1990) Isolation and characterization of cloned cDNAs encoding human liver chlordecone reductase. Biochemistry 29: 1080-1087.
    • (1990) Biochemistry , vol.29 , pp. 1080-1087
    • Winters, C.J.1    Molowa, D.T.2    Guzelian, P.S.3
  • 118
    • 0029128239 scopus 로고
    • Pathology and pathogenetic mechanisms of diabetic neuropathy
    • Yagihashi S (1995) Pathology and pathogenetic mechanisms of diabetic neuropathy Diabetes Metab Rev 11:193-225.
    • (1995) Diabetes Metab Rev , vol.11 , pp. 193-225
    • Yagihashi, S.1
  • 119
    • 0026571089 scopus 로고
    • Effect of aminoguanidine on functional and structural abnormalities in peripheral nerve of STZ-induced diabetic rats
    • Yagihashi S, Kamijo M, Baba M, Yagihashi N, and Nagai K (1992) Effect of aminoguanidine on functional and structural abnormalities in peripheral nerve of STZ-induced diabetic rats. Diabetes 41:47-52.
    • (1992) Diabetes , vol.41 , pp. 47-52
    • Yagihashi, S.1    Kamijo, M.2    Baba, M.3    Yagihashi, N.4    Nagai, K.5
  • 122
    • 0028335907 scopus 로고
    • Identification of tumor-associated protein variants during rat hepatocarcinogenesis. Aldose reductasr
    • Zeindl-Eberhart E, Jungblut PK, Otto A, and Rabes HM (1994) Identification of tumor-associated protein variants during rat hepatocarcinogenesis. Aldose reductasr. J Biol Chem 269:14589-14594.
    • (1994) J Biol Chem , vol.269 , pp. 14589-14594
    • Zeindl-Eberhart, E.1    Jungblut, P.K.2    Otto, A.3    Rabes, H.M.4
  • 123
    • 0027318237 scopus 로고
    • Molecular species composition of glycerophospholipids in rat sciatic nerve and its alteration in streptozotocin-induced diabetes
    • Zhu X and Eichberg J (1993) Molecular species composition of glycerophospholipids in rat sciatic nerve and its alteration in streptozotocin-induced diabetes. Biochim Biophys Acta 1168:1-12.
    • (1993) Biochim Biophys Acta , vol.1168 , pp. 1-12
    • Zhu, X.1    Eichberg, J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.