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Volumn 48, Issue 22, 2005, Pages 6897-6907

Naphtho[1,2-d]isothiazole acetic acid derivatives as a novel class of selective aldose reductase inhibitors

Author keywords

[No Author keywords available]

Indexed keywords

(1,3,3 TRIOXO 1,2 DIHYDRONAPHTHO[1,2 D]ISOTHIAZOL 2 YL)ACETIC ACID; 2 BENZYL 1,3,3 TRIOXO 1,2 DIHYDRONAPHTHO[1,2 D]ISOTHIAZOLE 4 CARBOXYLIC ACID; 2 CARBOXYMETHYL 1,3,3 TRIOXO 1,2 DIHYDRONAPHTHO[1,2 D]ISOTHIAZOLE 4 CARBOXYLIC ACID; 2 CARBOXYMETHYL 1,3,3 TRIOXO 1,2 DIHYDRONAPHTHO[1,2 D]ISOTHIAZOLE 4 CARBOXYLIC ACID CARBOXYMETHYL ESTER; 2 ISOPROPOXYCARBONYLMETHYL 1,3,3 TRIOXO 1,2 DIHYDRONAPHTHO[1,2 D]ISOTHIAZOLE 4 CARBOXYLIC ACID ISOPROPYL ESTER; 2 METHYL 1,3,3 TRIOXO 1,2 DIHYDRONAPHTHO[1,2 D]ISOTHIAZOLE 4 CARBOXYLIC ACID; ACETIC ACID DERIVATIVE; ALDEHYDE REDUCTASE; ALDOSE REDUCTASE INHIBITOR; EPALRESTAT; GLUTATHIONE REDUCTASE; IDITOL DEHYDROGENASE; NAPHTHO[1,2 D]ISOTHIAZOLE ACETIC ACID DERIVATIVE; PRODRUG; QUERCETIN; SORBINIL; TOLRESTAT; UNCLASSIFIED DRUG; ZOPOLRESTAT;

EID: 27444440949     PISSN: 00222623     EISSN: None     Source Type: Journal    
DOI: 10.1021/jm050382p     Document Type: Article
Times cited : (55)

References (56)
  • 1
    • 0031752685 scopus 로고    scopus 로고
    • Global burden of diabetes, 1995-2025. Prevalence, numeric estimates, and projections
    • King, H.; Aubert, R. E.; Herman, W. H. Global Burden of Diabetes, 1995-2025. Prevalence, Numeric Estimates, and Projections. Diabetes Care 1998, 21, 1414-1431.
    • (1998) Diabetes Care , vol.21 , pp. 1414-1431
    • King, H.1    Aubert, R.E.2    Herman, W.H.3
  • 2
    • 0026633018 scopus 로고
    • New pharmacological approaches to therapy of NIDDM
    • Bressler, R.; Johnson, D. New Pharmacological Approaches to Therapy of NIDDM. Diabetes Care 1992, 15, 792-805.
    • (1992) Diabetes Care , vol.15 , pp. 792-805
    • Bressler, R.1    Johnson, D.2
  • 3
    • 0027730267 scopus 로고
    • Lessons learned from use of cyclosporine for insulin-dependent diabetes mellitus. The case of immunotherapy for insulin-dependent diabetics having residual insulin secretion
    • Mahon, J. L.; Dupre, J.; Stiller, C. R. Lessons Learned from Use of Cyclosporine for Insulin-Dependent Diabetes Mellitus. The Case of Immunotherapy for Insulin-Dependent Diabetics Having Residual Insulin Secretion. Ann. N.Y. Acad. Sci. 1993, 696, 3651-3663.
    • (1993) Ann. N.Y. Acad. Sci. , vol.696 , pp. 3651-3663
    • Mahon, J.L.1    Dupre, J.2    Stiller, C.R.3
  • 4
    • 0035856980 scopus 로고    scopus 로고
    • Biochemistry and molecular cell biology of diabetic complications
    • Brownlee, M. Biochemistry and Molecular Cell Biology of Diabetic Complications. Nature 2001, 414, 813-820.
    • (2001) Nature , vol.414 , pp. 813-820
    • Brownlee, M.1
  • 5
    • 14944340746 scopus 로고    scopus 로고
    • Oxidative stress and antioxidant treatment in diabetes
    • Scott, J. A.; King, G. L. Oxidative Stress and Antioxidant Treatment in Diabetes. Ann. N.Y. Acad. Sci. 2004, 1031, 204-213.
    • (2004) Ann. N.Y. Acad. Sci. , vol.1031 , pp. 204-213
    • Scott, J.A.1    King, G.L.2
  • 6
    • 20444380690 scopus 로고    scopus 로고
    • Cellular mechanisms and treatment of diabetes vascular complications converge on reactive oxygen species
    • Whiteside, C. I. Cellular Mechanisms and Treatment of Diabetes Vascular Complications Converge on Reactive Oxygen Species. Curr. Hypertens. Rep. 2005, 7, 148-154.
    • (2005) Curr. Hypertens. Rep. , vol.7 , pp. 148-154
    • Whiteside, C.I.1
  • 7
    • 0029560077 scopus 로고
    • The pathological implications of protein glycation
    • Brownlee, M. The Pathological Implications of Protein Glycation. Clin. Invest. Med. 1995, 18, 275-281.
    • (1995) Clin. Invest. Med. , vol.18 , pp. 275-281
    • Brownlee, M.1
  • 8
    • 0027934146 scopus 로고
    • Aldose reductase inhibitors and their potential for the treatment of diabetic complications
    • Tomlinson, D. R.; Stevens, E. J.; Diemel, L. T. Aldose Reductase Inhibitors and Their Potential for the Treatment of Diabetic Complications. Trends Pharmacol. Sci. 1994, 15, 293-297.
    • (1994) Trends Pharmacol. Sci. , vol.15 , pp. 293-297
    • Tomlinson, D.R.1    Stevens, E.J.2    Diemel, L.T.3
  • 9
    • 0023899991 scopus 로고
    • The role of aldose reductase in the development of diabetic complications
    • Kador, P. F. The Role of Aldose Reductase in the Development of Diabetic Complications. Med. Res. Rev. 1988, 8, 325-352.
    • (1988) Med. Res. Rev. , vol.8 , pp. 325-352
    • Kador, P.F.1
  • 11
    • 0022650672 scopus 로고
    • The effect of high glucose and oxidative stress on lens metabolism, aldose reductase, and senile cataractogenesis
    • Cheng, H. M.; Gonzales, R. G. The Effect of High Glucose and Oxidative Stress on Lens Metabolism, Aldose Reductase, and Senile Cataractogenesis. Metabolism 1986, 35, 10-14.
    • (1986) Metabolism , vol.35 , pp. 10-14
    • Cheng, H.M.1    Gonzales, R.G.2
  • 12
    • 0042867413 scopus 로고    scopus 로고
    • Contribution of polyol pathway to diabetes-induced oxidative stress
    • Chung, S. S. M.; Ho, E. C. M.; Lam, K. S. L.; Chung, S. K. Contribution of Polyol Pathway to Diabetes-Induced Oxidative Stress. J. Am. Soc. Nephrol. 2003, 14, S234-S236.
    • (2003) J. Am. Soc. Nephrol. , vol.14
    • Chung, S.S.M.1    Ho, E.C.M.2    Lam, K.S.L.3    Chung, S.K.4
  • 13
    • 0034122558 scopus 로고    scopus 로고
    • Surface oxidase and oxidative stress propagation in aging
    • Morre, D. M.; Lenaz, G.; Morre, D. J. Surface Oxidase and Oxidative Stress Propagation in Aging. J. Exp. Biol. 2000, 203, 1513-1521.
    • (2000) J. Exp. Biol. , vol.203 , pp. 1513-1521
    • Morre, D.M.1    Lenaz, G.2    Morre, D.J.3
  • 14
    • 0027326529 scopus 로고
    • Aldose reductase inhibitors: Recent developments
    • Sarges, R.; Oates, P. J. Aldose Reductase Inhibitors: Recent Developments. Prog. Drug Res. 1993, 40, 99-161.
    • (1993) Prog. Drug Res. , vol.40 , pp. 99-161
    • Sarges, R.1    Oates, P.J.2
  • 15
    • 0027378377 scopus 로고
    • Refined 1.8 Å structure of human aldose reductase complexed with the potent inhibitor zopolrestat
    • Wilson, D. K.; Tarle, I.; Petrash, J. M.; Quiocho, F. A. Refined 1.8 Å Structure of Human Aldose Reductase Complexed with the Potent Inhibitor Zopolrestat. Proc. Natl. Acad. Sci. U.S.A. 1993, 90, 9847-9851.
    • (1993) Proc. Natl. Acad. Sci. U.S.A. , vol.90 , pp. 9847-9851
    • Wilson, D.K.1    Tarle, I.2    Petrash, J.M.3    Quiocho, F.A.4
  • 16
    • 0031570301 scopus 로고    scopus 로고
    • "Specificity" pocket inferred from the crystal structures of the complexes of aldose reductase with the pharmaceutically important inhibitors tolrestat and sorbinil
    • Urzhumtsev, A.; Tête-Favier, F.; Mitschler, A.; Barbanton, J.; Barth, P.; Urzhumtseva, L.; Biellmann, J.-F.; Podjarny, A. D.; Moras, D. A "Specificity" Pocket Inferred from the Crystal Structures of the Complexes of Aldose Reductase with the Pharmaceutically Important Inhibitors Tolrestat and Sorbinil. Structure 1997, 5, 601-612.
    • (1997) Structure , vol.5 , pp. 601-612
    • Urzhumtsev, A.1    Tête-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.A.9
  • 17
    • 0031424157 scopus 로고    scopus 로고
    • The alrestatin double-decker: Binding of two inhibitor molecules to human aldose reductase reveals a new specificity determinant
    • Harrison, D. H. T.; Bohren, K. M.; Petsko, G. A.; Ringe, D.; Gabbay, K. H. The Alrestatin Double-Decker: Binding of Two Inhibitor Molecules to Human Aldose Reductase Reveals a New Specificity Determinant. Biochemistry 1997, 36, 16134-16140.
    • (1997) Biochemistry , vol.36 , pp. 16134-16140
    • Harrison, D.H.T.1    Bohren, K.M.2    Petsko, G.A.3    Ringe, D.4    Gabbay, K.H.5
  • 18
    • 0028331867 scopus 로고
    • An anionic binding site in human aldose reductase: Mechanistic implications for the binding of citrate, cacodylate, and glucose-6-phosphate
    • Harrison, D. H.; Bohren, K. M.; Ringe, D.; Petsko, G. A.; Gabbay, K. H. An Anionic Binding Site in Human Aldose Reductase: Mechanistic Implications for the Binding of Citrate, Cacodylate, and Glucose-6-phosphate. Biochemistry 1994, 33, 2011-2020.
    • (1994) Biochemistry , vol.33 , pp. 2011-2020
    • Harrison, D.H.1    Bohren, K.M.2    Ringe, D.3    Petsko, G.A.4    Gabbay, K.H.5
  • 22
    • 0023192764 scopus 로고
    • Peroxide-induced effects on lens cation transport following inhibition of glutathione reductase activity in vitro
    • Giblin, F. J.; McCready, J. P.; Schrimscher, L.; Reddy, V. N. Peroxide-Induced Effects on Lens Cation Transport Following Inhibition of Glutathione Reductase Activity in Vitro. Exp. Eye Res. 1987, 45, 77-91.
    • (1987) Exp. Eye Res. , vol.45 , pp. 77-91
    • Giblin, F.J.1    McCready, J.P.2    Schrimscher, L.3    Reddy, V.N.4
  • 23
    • 0023895652 scopus 로고    scopus 로고
    • Influence of the activity of glutathione reductase on the response of cultured lens epithelial cells from young and old rabbits to hydrogen peroxide
    • Reddan, J. R.; Giblin, F. J.; Dziedzic, D. C.; McCready, J. P.; Schrimscher, L.; Reddy, V. N. Influence of the Activity of Glutathione Reductase on the Response of Cultured Lens Epithelial Cells from Young and Old Rabbits to Hydrogen Peroxide. Exp. Eye Res. 1998, 46, 209-221.
    • (1998) Exp. Eye Res. , vol.46 , pp. 209-221
    • Reddan, J.R.1    Giblin, F.J.2    Dziedzic, D.C.3    McCready, J.P.4    Schrimscher, L.5    Reddy, V.N.6
  • 27
    • 0031416721 scopus 로고    scopus 로고
    • Benzisothiazole-1,1-dioxide alkanoic acid derivatives as inhibitors of rat lens aldose reductase
    • Primofiore, G.; Da Settimo, F.; La Motta, C.; Simorini, F.; Minutolo, A.; Boldrini, E. Benzisothiazole-1,1-dioxide Alkanoic Acid Derivatives as Inhibitors of Rat Lens Aldose Reductase. Farmaco 1997, 52, 583-588.
    • (1997) Farmaco , vol.52 , pp. 583-588
    • Primofiore, G.1    Da Settimo, F.2    La Motta, C.3    Simorini, F.4    Minutolo, A.5    Boldrini, E.6
  • 28
    • 0025148456 scopus 로고
    • Conformationally rigid analogues of aldose reductase inhibitors, tolrestat. Novel syntheses of naphthalene-fused γ-, δ-, and ε-lactams
    • Wrobel, J.; Dietrich, A.; Gorham, B. J.; Sestanj, K. Conformationally Rigid Analogues of Aldose Reductase Inhibitors, Tolrestat. Novel Syntheses of Naphthalene-Fused γ-, δ-, and ε-Lactams. J. Org. Chem. 1990, 55, 2694-2702.
    • (1990) J. Org. Chem. , vol.55 , pp. 2694-2702
    • Wrobel, J.1    Dietrich, A.2    Gorham, B.J.3    Sestanj, K.4
  • 29
    • 0032578366 scopus 로고    scopus 로고
    • Structural features of the aldose reductase and aldehyde reductase inhibitor-binding sites
    • El-Kabbani, O.; Wilson, D. K.; Petrash, J. M.; Quiocho, F. A. Structural Features of the Aldose Reductase and Aldehyde Reductase Inhibitor-Binding Sites. Mol. Vision 1998, 4, 19-25.
    • (1998) Mol. Vision , vol.4 , pp. 19-25
    • El-Kabbani, O.1    Wilson, D.K.2    Petrash, J.M.3    Quiocho, F.A.4
  • 30
    • 33947290164 scopus 로고
    • Preparation of substituted 1,2-benzoisothiazolin-3-one-1,1-dioxides (o-Benzoic Sulfimides)
    • Lombardino, J. G. Preparation of Substituted 1,2-Benzoisothiazolin-3-one- 1,1-dioxides (o-Benzoic Sulfimides). J. Org. Chem. 1971, 36, 1843-1845.
    • (1971) J. Org. Chem. , vol.36 , pp. 1843-1845
    • Lombardino, J.G.1
  • 31
    • 0037472690 scopus 로고    scopus 로고
    • Substituted pyrrol-1-ylacetic acids that combine aldose reductase enzyme inhibitory activity and ability to prevent the nonenzymatic irreversible modification of proteins from monosaccharides
    • Nicolaou, I.; Demopoulos, V. J. Substituted Pyrrol-1-ylacetic Acids That Combine Aldose Reductase Enzyme Inhibitory Activity and Ability To Prevent the Nonenzymatic Irreversible Modification of Proteins from Monosaccharides. J. Med. Chem. 2003, 46, 417-426.
    • (2003) J. Med. Chem. , vol.46 , pp. 417-426
    • Nicolaou, I.1    Demopoulos, V.J.2
  • 32
    • 84981834386 scopus 로고
    • Synthèse d'analogues structuraux de L'oxytocine
    • Boissonnas, R. A.; Guttmann, St.; Jaquenoud, P.-A.; Waller, J.-P. Synthèse d'Analogues Structuraux de L'oxytocine (Synthesis of Structural Analogues of Oxytocin). Helv. Chim. Acta 1956, 39, 1421-1427.
    • (1956) Helv. Chim. Acta , vol.39 , pp. 1421-1427
    • Boissonnas, R.A.1    Guttmann, S.2    Jaquenoud, P.-A.3    Waller, J.-P.4
  • 33
    • 0027980979 scopus 로고
    • Synthesis of pyridazine acetic acid derivatives possessing aldose reductase inhibitory activity and antioxidant properties
    • Coudert, P.; Albuisson, E.; Boire, J. Y.; Durox, E.; Bastide, P.; Couquelet, J. Synthesis of Pyridazine Acetic Acid Derivatives Possessing Aldose Reductase Inhibitory Activity and Antioxidant Properties. Eur. J. Med. Chem. 1994, 29, 471-477.
    • (1994) Eur. J. Med. Chem. , vol.29 , pp. 471-477
    • Coudert, P.1    Albuisson, E.2    Boire, J.Y.3    Durox, E.4    Bastide, P.5    Couquelet, J.6
  • 35
    • 0023197411 scopus 로고
    • 2α and its isopropyl ester in vitro
    • 2α and Its Isopropyl Ester in Vitro. Int. J. Pharm. 1987, 37, 27-32.
    • (1987) Int. J. Pharm. , vol.37 , pp. 27-32
    • Camber, O.1    Edman, P.2
  • 36
    • 0025787163 scopus 로고
    • Permeability of pilocarpic acid diesters across albino rabbit cornea in vitro
    • Suhonen, P.; Järvinen, T.; Peura, P.; Urtti, A. Permeability of Pilocarpic Acid Diesters across Albino Rabbit Cornea in Vitro. Int. J. Pharm. 1991, 74, 221-228.
    • (1991) Int. J. Pharm. , vol.74 , pp. 221-228
    • Suhonen, P.1    Järvinen, T.2    Peura, P.3    Urtti, A.4
  • 38
    • 11644261806 scopus 로고    scopus 로고
    • Automated docking using a lamarckian genetic algorithm and an empirical binding free energy function
    • Morris, G. M.; Goodsell, D. S.; Halliday, R. S.; Huey, R.; Hart, W. E.; Belew, R. K.; Olson, A. J. Automated Docking Using a Lamarckian Genetic Algorithm and an Empirical Binding Free Energy Function. J. Comput. Chem. 1998, 19, 1639-1662.
    • (1998) J. Comput. Chem. , vol.19 , pp. 1639-1662
    • Morris, G.M.1    Goodsell, D.S.2    Halliday, R.S.3    Huey, R.4    Hart, W.E.5    Belew, R.K.6    Olson, A.J.7
  • 39
    • 0023989064 scopus 로고
    • Database searching (SWISS-PROT), sequence alignment, and analysis of rat and pig ALR2 sequences were carried out using FASTA (Pearson, W. R. Proc. Natl. Acad. Sci. U.S.A. 1988, 85, 2444-2448)
    • (1988) Proc. Natl. Acad. Sci. U.S.A. , vol.85 , pp. 2444-2448
    • Pearson, W.R.1
  • 40
    • 0000302276 scopus 로고    scopus 로고
    • and BLAST programs (Wang, S.; Pak, Y. J. Phys. Chem. B 2000, 104, 354-359). The SWISS-PROT accession numbers for rat and pig ALR2 types are P07943 and P80276, respectively.
    • (2000) J. Phys. Chem. B , vol.104 , pp. 354-359
    • Wang, S.1    Pak, Y.2
  • 41
    • 0031424157 scopus 로고    scopus 로고
    • The alrestatin double-decker: Binding of two inhibitor molecules to human aldose reductase reveals a new specificity determinant
    • Harrison, D. H. T.; Bohren, K. M.; Petsko, G. A.; Ringe, D.; Gabbay, K. H. The Alrestatin Double-Decker: Binding of Two Inhibitor Molecules to Human Aldose Reductase Reveals a New Specificity Determinant. Biochemistry 1997, 36, 16134-16140.
    • (1997) Biochemistry , vol.36 , pp. 16134-16140
    • Harrison, D.H.T.1    Bohren, K.M.2    Petsko, G.A.3    Ringe, D.4    Gabbay, K.H.5
  • 43
    • 0028222097 scopus 로고
    • 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
    • Bohren, K. M.; Grimshaw, C. E.; Lai, C. J.; Harrison, D. H.; Ringe, D.; Petsko, G. A.; Gabbay, K. H. 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 1994, 33, 2021-2032.
    • (1994) Biochemistry , vol.33 , pp. 2021-2032
    • Bohren, K.M.1    Grimshaw, C.E.2    Lai, C.J.3    Harrison, D.H.4    Ringe, D.5    Petsko, G.A.6    Gabbay, K.H.7
  • 44
    • 0028810466 scopus 로고
    • Human aldose reductase: PK of tyrosine 48 reveals the preferred ionization state for catalysis and inhibition
    • Grimshaw, C. E.; Bohren, K. M.; Lai, C. J.; Gabbay, K. H. Human Aldose Reductase: pK of Tyrosine 48 Reveals the Preferred Ionization State for Catalysis and Inhibition. Biochemistry 1995, 34, 14374-14384
    • (1995) Biochemistry , vol.34 , pp. 14374-14384
    • Grimshaw, C.E.1    Bohren, K.M.2    Lai, C.J.3    Gabbay, K.H.4
  • 45
    • 0030982582 scopus 로고    scopus 로고
    • Studies on the inhibitor-binding site of porcine aldehyde reductase: Crystal structure of the holoenzyme-inhibitor ternary complex
    • El-Kabbani, O.; Carper, D. A.; McGowan, M. H.; Devedjiev, Y.; Milton, K. J.; Flynn, T. G. Studies on the Inhibitor-Binding Site of Porcine Aldehyde Reductase: Crystal Structure of the Holoenzyme-Inhibitor Ternary Complex. Proteins 1997, 28, 186-192.
    • (1997) Proteins , vol.28 , pp. 186-192
    • El-Kabbani, O.1    Carper, D.A.2    McGowan, M.H.3    Devedjiev, Y.4    Milton, K.J.5    Flynn, T.G.6
  • 46
    • 0000930578 scopus 로고
    • Isolation and properties of lens aldose reductase
    • Hayman, S.; Kinoshita, J. H. Isolation and Properties of Lens Aldose Reductase. J. Biol. Chem. 1965, 240, 877-882.
    • (1965) J. Biol. Chem. , vol.240 , pp. 877-882
    • Hayman, S.1    Kinoshita, J.H.2
  • 48
    • 0028316619 scopus 로고
    • Inhibition and activation studies on sheep liver sorbitol dehydrogenase
    • Lindstad, R. I.; Hermansen, L. F.; McKinley-McKee, J. S. Inhibition and activation studies on sheep liver sorbitol dehydrogenase. Eur. J. Biochem. 1994, 221, 847-854.
    • (1994) Eur. J. Biochem. , vol.221 , pp. 847-854
    • Lindstad, R.I.1    Hermansen, L.F.2    McKinley-McKee, J.S.3
  • 51
    • 0023325062 scopus 로고
    • Strategic approaches to drug design. 1. An integrated software framework for molecular modelling
    • Vinter, J. G.; Davis, A.; Saunders, M. R. Strategic Approaches to Drug Design. 1. An Integrated Software Framework for Molecular Modelling. J. Comput.-Aided Mol. Des. 1987, 1, 31-55.
    • (1987) J. Comput.-Aided Mol. Des. , vol.1 , pp. 31-55
    • Vinter, J.G.1    Davis, A.2    Saunders, M.R.3
  • 53
    • 6344256147 scopus 로고
    • Consistent force field studies of intermolecular forces in hydrogen-bonded crystals
    • Hagler, A. F.; Lifson, S.; Dauber, P. Consistent Force Field Studies of Intermolecular Forces in Hydrogen-Bonded Crystals. J. Am. Chem. Soc. 1979, 101, 5122-5130.
    • (1979) J. Am. Chem. Soc. , vol.101 , pp. 5122-5130
    • Hagler, A.F.1    Lifson, S.2    Dauber, P.3
  • 54
    • 3343012886 scopus 로고
    • A broyden-fletcher-goldfarb-shannon optimization procedure for molecular geometries
    • Head, J.; Zerner, M. C. A Broyden-Fletcher-Goldfarb-Shannon Optimization Procedure for Molecular Geometries. Chem. Phys. Lett. 1985, 122, 264-274.
    • (1985) Chem. Phys. Lett. , vol.122 , pp. 264-274
    • Head, J.1    Zerner, M.C.2
  • 55
    • 49149147973 scopus 로고
    • Iterative partial equalization of orbital electronegativity. A rapid access to atomic charges
    • Gasteiger, J.; Marsili, M. Iterative Partial Equalization of Orbital Electronegativity. A Rapid Access to Atomic Charges. Tetrahedron 1980, 36, 3219-3228.
    • (1980) Tetrahedron , vol.36 , pp. 3219-3228
    • Gasteiger, J.1    Marsili, M.2


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