메뉴 건너뛰기




Volumn 18, Issue 5, 2012, Pages 1791-1799

Novel insights into the structural requirements for the design of selective and specific aldose reductase inhibitors

Author keywords

ALR2; Detoxification; Docking; Induced fit cavity; Selectivity; Specificity

Indexed keywords

ALDEHYDE REDUCTASE; ALDOSE REDUCTASE INHIBITOR; FIDARESTAT; GLUCOSE; GLUCOSE 6 PHOSPHATE; GLYCERALDEHYDE 3 PHOSPHATE; METHYLGLYOXAL; NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; POLYOL; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; SORBITOL; ZOPOLRESTAT;

EID: 84861230090     PISSN: 16102940     EISSN: 09485023     Source Type: Journal    
DOI: 10.1007/s00894-011-1195-0     Document Type: Article
Times cited : (37)

References (36)
  • 2
    • 0021363571 scopus 로고
    • Direct measurement of polyol pathway activity in the ocular lens
    • Gonzalez RG, Barnett P, Aguayo J, Cheng HM, Chylack LT (1984) Direct measurement of polyol pathway activity in the ocular lens. Diabetes 33:196-199 (Pubitemid 14184708)
    • (1984) Diabetes , vol.33 , Issue.2 , pp. 196-199
    • Gonzalez, R.G.1    Barnett, P.2    Aguayo, J.3
  • 3
    • 0021067173 scopus 로고
    • Polyol pathway activity and myo-inositol metabolism. A suggested relationship in the pathogenesis of diabetic neuropathy
    • Finegold D, Lattimer SA, Nolle S, Bernstein M, Greene DA (1983) Polyol pathway activity and myo-inositol metabolism. A suggested relationship in the pathogenesis of diabetic neuropathy. Diabetes 32:988-992 (Pubitemid 14225114)
    • (1983) Diabetes , vol.32 , Issue.11 , pp. 988-992
    • Finegold, D.1    Lattimer, S.A.2    Nolle, S.3
  • 4
    • 33750561283 scopus 로고    scopus 로고
    • Endotoxin-induced cardiomyopathy and systemic inflammation in mice is prevented by aldose reductase inhibition
    • DOI 10.1161/CIRCULATIONAHA.106.630830, PII 0000301720061024000010
    • Ramana KV, Willis MS, White MD, Horton JW, DiMaio JM, Srivastava D, Bhatnagar A, Srivastava SK (2006) Endotoxininduced cardiomyopathy and systemic inflammation in mice is prevented by aldose reductase inhibition. Circulation 114:1838-1846 (Pubitemid 44673359)
    • (2006) Circulation , vol.114 , Issue.17 , pp. 1838-1846
    • Ramana, K.V.1    Willis, M.S.2    White, M.D.3    Horton, J.W.4    Dimaio, J.M.5    Srivastava, D.6    Bhatnagar, A.7    Srivastava, S.K.8
  • 5
    • 0034118468 scopus 로고    scopus 로고
    • Elevated sorbitol concentration in the cerebrospinal fluid of patients with mood disorders
    • DOI 10.1016/S0306-4530(00)00012-3, PII S0306453000000123
    • Regenold WT, Kling MA, Hauser P (2000) Elevated sorbitol concentration in the cerebrospinal fluid of patients with mood disorders. Psychoneuroendocrinology 25:593-606 (Pubitemid 30407311)
    • (2000) Psychoneuroendocrinology , vol.25 , Issue.6 , pp. 593-606
    • Regenold, W.T.1    A. Kling, M.2    Hauser, P.3
  • 6
    • 0036723885 scopus 로고    scopus 로고
    • Plasma 3-deoxyglucosone elevation in chronic renal failure is associated with increased aldose reductase in erythrocytes
    • DOI 10.1053/ajkd.2002.34884
    • Hasuike Y, Nakanishi T, Otaki Y, Nanami M, Tanimoto T, Taniguchi N, Takamitsu Y (2002) Plasma 3-deoxyglucosone elevation in chronic renal failure is associated with increased aldose reductase in erythrocytes. Am J Kidney Dis 40:464-471 (Pubitemid 34971273)
    • (2002) American Journal of Kidney Diseases , vol.40 , Issue.3 , pp. 464-471
    • Hasuike, Y.1    Nakanishi, T.2    Otaki, Y.3    Nanami, M.4    Tanimoto, T.5    Taniguchi, N.6    Takamitsu, Y.7
  • 8
    • 0035097039 scopus 로고    scopus 로고
    • Overexpression of aldose reductase in liver cancers may contribute to drug resistance
    • DOI 10.1097/00001813-200102000-00005
    • Lee KWY, Ko BCB, Jiang Z, Cao D, Chung SSM (2001) Overexpression of aldose reductase in liver cancers may contribute to drug resistance. Anticancer Drugs 12:129-132 (Pubitemid 32207361)
    • (2001) Anti-Cancer Drugs , vol.12 , Issue.2 , pp. 129-132
    • Lee, K.W.Y.1    Ko, B.C.B.2    Jiang, Z.3    Cao, D.4    Chung, S.S.M.5
  • 10
    • 0142188162 scopus 로고    scopus 로고
    • Choice of Normal Ovarian Control Influences Determination of Differentially Expressed Genes in Ovarian Cancer Expression Profiling Studies
    • Zorn KK, Jazaeri AA, Awtrey CS, Gardner GJ, Mok SC, Boyd J, Michael J (2003) Choice of normal ovarian control influences determination of differentially expressed genes in ovarian cancer expression profiling studies. Birrer Clin Cancer Res AACR 9:4811-4818 (Pubitemid 37323284)
    • (2003) Clinical Cancer Research , vol.9 , Issue.13 , pp. 4811-4818
    • Zorn, K.K.1    Jazaeri, A.A.2    Awtrey, C.S.3    Gardner, G.J.4    Mok, S.C.5    Boyd, J.6    Birrer, M.J.7
  • 11
    • 33646054140 scopus 로고    scopus 로고
    • Analysis of differential protein expression by cisplatin treatment in cervical carcinoma cells
    • Yim EK, Lee KH, Kim CJ, Park JS (2006) Analysis of differential protein expression by cisplatin treatment in cervical carcinoma cells. Int J Gynecol Cancer 16:690
    • (2006) Int J Gynecol Cancer , vol.16 , pp. 690
    • Yim, E.K.1    Lee, K.H.2    Kim, C.J.3    Park, J.S.4
  • 13
    • 65649103414 scopus 로고    scopus 로고
    • Aldose reductase enzyme and its implication to major health problems of the 21 (st) Century
    • Alexiou P, Pegklidou K, Chatzopoulou M, Nicolaou I, Demopoulos VJ (2009) Aldose reductase enzyme and its implication to major health problems of the 21 (st) Century. Curr Med Chem 16:734-752
    • (2009) Curr Med Chem , vol.16 , pp. 734-752
    • Alexiou, P.1    Pegklidou, K.2    Chatzopoulou, M.3    Nicolaou, I.4    Demopoulos, V.J.5
  • 14
    • 0035969891 scopus 로고    scopus 로고
    • The aldo-keto reductase (AKR) superfamily: An update
    • DOI 10.1016/S0009-2797(00)00295-7, PII S0009279700002957
    • Jez JM, Penning TM (2001) The aldo-keto reductase (AKR) superfamily: an update. Chem Biol Interact 130:499-525 (Pubitemid 32295840)
    • (2001) Chemico-Biological Interactions , vol.130-132 , pp. 499-525
    • Jez, J.M.1    Penning, T.M.2
  • 16
    • 0015830590 scopus 로고
    • Heterogeneity of NADPHdependent aldehyde reductase from human and rat brain
    • Ris MM, Wartburg JP (1973) Heterogeneity of NADPHdependent aldehyde reductase from human and rat brain. Eur J Biochem 37:69-77
    • (1973) Eur J Biochem , vol.37 , pp. 69-77
    • Ris, M.M.1    Wartburg, J.P.2
  • 17
    • 0024333867 scopus 로고
    • The aldo-keto reductase superfamily. cDNAs and deduced amino acid sequences of human aldehyde and aldose reductases
    • Bohren KM, Bullock B, Wermuth B, 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    Wermuth, B.3    Gabbay, K.H.4
  • 18
    • 23944478339 scopus 로고    scopus 로고
    • Structure of aldehyde reductase holoenzyme in complex with the potent aldose reductase inhibitor fidarestat: Implications for inhibitor binding and selectivity
    • DOI 10.1021/jm050412o
    • El-Kabbani O, Carbone V, Darmanin C, Oka M, Mitschler A, Podjarny A, Schulze-Briese C, PtC R (2005) Structure of aldehyde reductase holoenzyme in complex with the potent aldose reductase inhibitor fidarestat: implications for inhibitor binding and selectivity. J Med Chem 48:5536-5542 (Pubitemid 41209251)
    • (2005) Journal of Medicinal Chemistry , vol.48 , Issue.17 , pp. 5536-5542
    • El-Kabbani, O.1    Carbone, V.2    Darmanin, C.3    Oka, M.4    Mitschler, A.5    Podjarny, A.6    Schulze-Briese, C.7    Chung, R.P.-T.8
  • 20
    • 0037184495 scopus 로고    scopus 로고
    • Molecular understanding of hyperglycemia's adverse effects for diabetic complications
    • DOI 10.1001/jama.288.20.2579
    • Sheetz MJ, King GL (2002) Molecular understanding of hyperglycemia's adverse effects for diabetic complications. Am Med Assoc 288:2579-2588 (Pubitemid 35386893)
    • (2002) Journal of the American Medical Association , vol.288 , Issue.20 , pp. 2579-2588
    • Sheetz, M.J.1    King, G.L.2
  • 21
    • 0026719692 scopus 로고
    • An unlikely sugar substrate site in the 1.65 A structure of the human aldose reductase holoenzyme implicated in diabetic complications
    • Wilson DK, Bohren KM, Gabbay KH, Quiocho FA (1992) An unlikely sugar substrate site in the 1.65 A 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
  • 24
    • 0027431819 scopus 로고
    • Probing the active site of human aldose reductase. Site-directed mutagenesis of Asp-43, Tyr-48, Lys-77, and His-110
    • 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 268:25687-25693 (Pubitemid 23358181)
    • (1993) Journal of Biological Chemistry , vol.268 , Issue.34 , pp. 25687-25693
    • Tarle, I.1    Borhani, B.W.2    Wilson, D.K.3    Quiocho, F.A.4    Petrash, J.M.5
  • 26
    • 0033982936 scopus 로고    scopus 로고
    • KEGG: Kyoto encyclopedia of genes and genomes
    • Kanehisa M, Goto S (2000) KEGG: Kyoto encyclopedia of genes and genomes. Nucleic Acids Res 28:27
    • (2000) Nucleic Acids Res , vol.28 , pp. 27
    • Kanehisa, M.1    Goto, S.2
  • 29
    • 0022594196 scopus 로고
    • An introduction to hidden Markov models
    • Rabiner L, Juang B (1986) An introduction to hidden Markov models. IEEE ASSP Mag 3:4-16
    • (1986) IEEE ASSP Mag , vol.3 , pp. 4-16
    • Rabiner, L.1    Juang, B.2
  • 30
    • 0031743421 scopus 로고    scopus 로고
    • Profile hidden Markov models
    • Eddy SR (1998) Profile hidden Markov models. Bioinformatics 14:755-763 (Pubitemid 28552108)
    • (1998) Bioinformatics , vol.14 , Issue.9 , pp. 755-763
    • Eddy, S.R.1
  • 33
    • 18744394070 scopus 로고    scopus 로고
    • Q-SiteFinder: An energy-based method for the prediction of protein-ligand binding sites
    • DOI 10.1093/bioinformatics/bti315
    • Laurie ATR, Jackson RM (2005) Q-SiteFinder: an energy-based method for the prediction of protein-ligand binding sites. Bioinformatics 21:1908-1916 (Pubitemid 40668026)
    • (2005) Bioinformatics , vol.21 , Issue.9 , pp. 1908-1916
    • Laurie, A.T.R.1    Jackson, R.M.2
  • 34
    • 84878884224 scopus 로고    scopus 로고
    • Schrödinger Inc, San Diego, CA, USA
    • GLIDE, version 5.0, Schrödinger Inc, San Diego, CA, USA
    • GLIDE, Version 5.0
  • 35
    • 84861227776 scopus 로고    scopus 로고
    • Schrödinger Inc, San Diego, CA, USA
    • QikProp, version 3.1,Schrödinger Inc, San Diego, CA, USA
    • QikProp, Version 3.1
  • 36
    • 33845868822 scopus 로고    scopus 로고
    • PHASE: A new engine for pharmacophore perception, 3D QSAR model development, and 3D database screening: 1. Methodology and preliminary results
    • DOI 10.1007/s10822-006-9087-6
    • Dixon SL, Smondyrev AM, Knoll EH, Rao SN, Shaw DE, Friesner RA (2006) PHASE: a new engine for pharmacophore perception, 3D QSAR model development, and 3D database screening: 1. Methodology and preliminary results. J Comput Aided Mol Des 20:647-671 (Pubitemid 46023928)
    • (2006) Journal of Computer-Aided Molecular Design , vol.20 , Issue.10-11 , pp. 647-671
    • Dixon, S.L.1    Smondyrev, A.M.2    Knoll, E.H.3    Rao, S.N.4    Shaw, D.E.5    Friesner, R.A.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.