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Volumn 385, Issue 2, 2009, Pages 606-617

Structural Base for Enzymatic Cyclodextrin Hydrolysis

Author keywords

cyclodextrin deformation; cyclomaltodextrinases; glycosyl hydrolase family no. 13; oligomerization; X ray diffraction

Indexed keywords

ALPHA CYCLODEXTRIN; ARGININE; BETA CYCLODEXTRIN; DIMER; GAMMA CYCLODEXTRIN; MUTANT PROTEIN; PHENYLALANINE;

EID: 58149083826     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2008.10.085     Document Type: Article
Times cited : (32)

References (47)
  • 1
    • 84985609923 scopus 로고
    • Cyclodextrin inclusion compounds in research and industry
    • Saenger W. Cyclodextrin inclusion compounds in research and industry. Angew. Chem. Int. Ed. 19 (1980) 344-362
    • (1980) Angew. Chem. Int. Ed. , vol.19 , pp. 344-362
    • Saenger, W.1
  • 2
    • 0028343242 scopus 로고
    • Molecular nanotube aggregates of β-and γ-cyclodextrins linked by diphenylhexatrienes
    • Li G., and McGown L.B. Molecular nanotube aggregates of β-and γ-cyclodextrins linked by diphenylhexatrienes. Science 264 (1994) 249-251
    • (1994) Science , vol.264 , pp. 249-251
    • Li, G.1    McGown, L.B.2
  • 3
    • 0029819323 scopus 로고    scopus 로고
    • Pharmaceutical applications of cyclodextrins. 1. Drug solubilisation and stabilization
    • Loftsson T., and Brewster M.E. Pharmaceutical applications of cyclodextrins. 1. Drug solubilisation and stabilization. J. Pharm. Sci. 85 (1996) 1017-1025
    • (1996) J. Pharm. Sci. , vol.85 , pp. 1017-1025
    • Loftsson, T.1    Brewster, M.E.2
  • 4
    • 0032119526 scopus 로고    scopus 로고
    • Cyclodextrin drug carrier systems
    • Uekama K., Hirayama F., and Irie T. Cyclodextrin drug carrier systems. Chem. Rev. 98 (1998) 2045-2076
    • (1998) Chem. Rev. , vol.98 , pp. 2045-2076
    • Uekama, K.1    Hirayama, F.2    Irie, T.3
  • 5
    • 0030757173 scopus 로고    scopus 로고
    • Enantioselective determination of chiral organochlorine compounds in biota by gas chromatography on modified cyclodextrins
    • Vetter W., and Schurig V. Enantioselective determination of chiral organochlorine compounds in biota by gas chromatography on modified cyclodextrins. J. Chromatogr. A 774 (1997) 143-175
    • (1997) J. Chromatogr. A , vol.774 , pp. 143-175
    • Vetter, W.1    Schurig, V.2
  • 6
    • 0029166485 scopus 로고
    • Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases
    • Henrissat B., Callebaut I., Fabrega S., Lehn P., Mornon J.P., and Davies G. Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases. Proc. Natl Acad. Sci. USA 92 (1995) 7090-7094
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 7090-7094
    • Henrissat, B.1    Callebaut, I.2    Fabrega, S.3    Lehn, P.4    Mornon, J.P.5    Davies, G.6
  • 7
  • 8
    • 0024307344 scopus 로고
    • Three-dimensional structure of cyclodextrin glycosyltransferase from Bacillus circulans at 3.4 Å resolution
    • Hofmann B.E., Bender H., and Schulz G.E. Three-dimensional structure of cyclodextrin glycosyltransferase from Bacillus circulans at 3.4 Å resolution. J. Mol. Biol. 209 (1989) 793-800
    • (1989) J. Mol. Biol. , vol.209 , pp. 793-800
    • Hofmann, B.E.1    Bender, H.2    Schulz, G.E.3
  • 9
    • 0014228472 scopus 로고
    • Purification and properties of the cyclodextrinase of Bacillus macerans
    • DePinto J.A., and Campbell L.L. Purification and properties of the cyclodextrinase of Bacillus macerans. Biochemistry 7 (1968) 121-125
    • (1968) Biochemistry , vol.7 , pp. 121-125
    • DePinto, J.A.1    Campbell, L.L.2
  • 10
    • 0033574502 scopus 로고    scopus 로고
    • Crystal structure of Thermoactinomyces vulgaris R-47 α-amylase II (TVA II) hydrolyzing cyclodextrins and pullulan at 2.6 Å resolution
    • Kamitori S., Kondo S., Okuyama K., Yokota T., Shimura Y., Tonozuka T., and Sakano Y. Crystal structure of Thermoactinomyces vulgaris R-47 α-amylase II (TVA II) hydrolyzing cyclodextrins and pullulan at 2.6 Å resolution. J. Mol. Biol. 287 (1999) 907-921
    • (1999) J. Mol. Biol. , vol.287 , pp. 907-921
    • Kamitori, S.1    Kondo, S.2    Okuyama, K.3    Yokota, T.4    Shimura, Y.5    Tonozuka, T.6    Sakano, Y.7
  • 11
    • 0033543556 scopus 로고    scopus 로고
    • Crystal structure of a maltogenic amylase provides insights into a catalytic versatility
    • Kim J.S., Cha S.S., Kim H.J., Kim T.J., Ha N.C., Oh S.T., et al. Crystal structure of a maltogenic amylase provides insights into a catalytic versatility. J. Biol. Chem. 274 (1999) 26279-26286
    • (1999) J. Biol. Chem. , vol.274 , pp. 26279-26286
    • Kim, J.S.1    Cha, S.S.2    Kim, H.J.3    Kim, T.J.4    Ha, N.C.5    Oh, S.T.6
  • 12
    • 0037077228 scopus 로고    scopus 로고
    • Cyclomaltodextrinase, neopullulanase and maltogenic amylase are nearly indistinguishable from each other
    • Lee H.S., Kim M.S., Cho H.S., Kim J.I., Kim T.J., Choi J.H., et al. Cyclomaltodextrinase, neopullulanase and maltogenic amylase are nearly indistinguishable from each other. J. Biol. Chem. 277 (2002) 21891-21897
    • (2002) J. Biol. Chem. , vol.277 , pp. 21891-21897
    • Lee, H.S.1    Kim, M.S.2    Cho, H.S.3    Kim, J.I.4    Kim, T.J.5    Choi, J.H.6
  • 13
    • 0038192408 scopus 로고    scopus 로고
    • Covalent and three-dimensional structure of the cyclodextrinase from Flavobacterium sp. no. 92
    • Fritzsche H.B., Schwede T., and Schulz G.E. Covalent and three-dimensional structure of the cyclodextrinase from Flavobacterium sp. no. 92. Eur. J. Biochem. 270 (2003) 2332-2341
    • (2003) Eur. J. Biochem. , vol.270 , pp. 2332-2341
    • Fritzsche, H.B.1    Schwede, T.2    Schulz, G.E.3
  • 14
    • 0037423706 scopus 로고    scopus 로고
    • Three-dimensional structure and substrate binding of Bacillus stearothermophilus neopullulanase
    • Hondoh H., Kuriki T., and Matsuura Y. Three-dimensional structure and substrate binding of Bacillus stearothermophilus neopullulanase. J. Mol. Biol. 326 (2003) 177-188
    • (2003) J. Mol. Biol. , vol.326 , pp. 177-188
    • Hondoh, H.1    Kuriki, T.2    Matsuura, Y.3
  • 15
    • 0028229326 scopus 로고
    • Crystal and molecular structure of barley α-amylase
    • Kadziola A., Abe J., Svensson B., and Haser R. Crystal and molecular structure of barley α-amylase. J. Mol. Biol. 239 (1994) 104-121
    • (1994) J. Mol. Biol. , vol.239 , pp. 104-121
    • Kadziola, A.1    Abe, J.2    Svensson, B.3    Haser, R.4
  • 16
    • 0028933531 scopus 로고
    • Crystal structure of calcium-depleted Bacillus licheniformis α-amylase at 2.2 Å resolution
    • Machius M., Wiegand G., and Huber R. Crystal structure of calcium-depleted Bacillus licheniformis α-amylase at 2.2 Å resolution. J. Mol. Biol. 246 (1995) 545-559
    • (1995) J. Mol. Biol. , vol.246 , pp. 545-559
    • Machius, M.1    Wiegand, G.2    Huber, R.3
  • 17
    • 0026027728 scopus 로고
    • Structure of cyclodextrin glycosyltransferase refined at 2.0 Å resolution
    • Klein C., and Schulz G.E. Structure of cyclodextrin glycosyltransferase refined at 2.0 Å resolution. J. Mol. Biol. 217 (1991) 737-750
    • (1991) J. Mol. Biol. , vol.217 , pp. 737-750
    • Klein, C.1    Schulz, G.E.2
  • 18
    • 0033520936 scopus 로고    scopus 로고
    • The cyclization mechanism of cyclodextrin glycosyltransferase (CGTase) as revealed by a γ-cyclodextrin-CGTase complex at 1.8 Å resolution
    • Uitdehaag J.C.M., Kalk K.H., van der Veen B.A., Dijkhuizen L., and Dijkstra B.W. The cyclization mechanism of cyclodextrin glycosyltransferase (CGTase) as revealed by a γ-cyclodextrin-CGTase complex at 1.8 Å resolution. J. Biol. Chem. 274 (1999) 34868-34876
    • (1999) J. Biol. Chem. , vol.274 , pp. 34868-34876
    • Uitdehaag, J.C.M.1    Kalk, K.H.2    van der Veen, B.A.3    Dijkhuizen, L.4    Dijkstra, B.W.5
  • 19
    • 0030513264 scopus 로고    scopus 로고
    • X-ray structure of cyclodextrin glucanotransferase from alkalophilic Bacillus sp. 1011. Comparison of two independent molecules at 1.8 Å resolution
    • Harata K., Haga K., Nakamura A., Aoyagi M., and Yamane K. X-ray structure of cyclodextrin glucanotransferase from alkalophilic Bacillus sp. 1011. Comparison of two independent molecules at 1.8 Å resolution. Acta Crystallogr. D 52 (1996) 1136-1145
    • (1996) Acta Crystallogr. D , vol.52 , pp. 1136-1145
    • Harata, K.1    Haga, K.2    Nakamura, A.3    Aoyagi, M.4    Yamane, K.5
  • 20
    • 33644877804 scopus 로고    scopus 로고
    • Dissociation/association properties of a dodecameric cyclomaltodextrinase
    • Lee H.S., Kim J.S., Shim K., Kim J.W., Inouye K., Oneda H., et al. Dissociation/association properties of a dodecameric cyclomaltodextrinase. FEBS J. 273 (2006) 109-121
    • (2006) FEBS J. , vol.273 , pp. 109-121
    • Lee, H.S.1    Kim, J.S.2    Shim, K.3    Kim, J.W.4    Inouye, K.5    Oneda, H.6
  • 21
    • 0035960637 scopus 로고    scopus 로고
    • Modulation of the multisubstrate specificity of Thermus maltogenic amylase by truncation of the N-terminal domain and by a salt-induced shift of the monomer/dimer equilibrium
    • Kim T.J., Nguyen V.D., Lee H.S., Kim M.J., Cho H.Y., Kim Y.W., et al. Modulation of the multisubstrate specificity of Thermus maltogenic amylase by truncation of the N-terminal domain and by a salt-induced shift of the monomer/dimer equilibrium. Biochemistry 40 (2001) 14182-14190
    • (2001) Biochemistry , vol.40 , pp. 14182-14190
    • Kim, T.J.1    Nguyen, V.D.2    Lee, H.S.3    Kim, M.J.4    Cho, H.Y.5    Kim, Y.W.6
  • 22
    • 0023890191 scopus 로고
    • Determination of the catalytic activity of cyclomaltodextrin glucanotransferase by maltotriose-methylorange assay
    • Mäkelä M.J., and Korpela T.K. Determination of the catalytic activity of cyclomaltodextrin glucanotransferase by maltotriose-methylorange assay. J. Biochem. Biophys. Methods 15 (1988) 307-318
    • (1988) J. Biochem. Biophys. Methods , vol.15 , pp. 307-318
    • Mäkelä, M.J.1    Korpela, T.K.2
  • 23
    • 0028763166 scopus 로고
    • Studies of the transglycosylation reaction catalysed by the decycling maltodextrinase of Flavobacterium sp. 92 with malto-oligosaccharides and cyclodextrins
    • Bender H. Studies of the transglycosylation reaction catalysed by the decycling maltodextrinase of Flavobacterium sp. 92 with malto-oligosaccharides and cyclodextrins. Carbohydr. Res. 263 (1994) 123-135
    • (1994) Carbohydr. Res. , vol.263 , pp. 123-135
    • Bender, H.1
  • 24
    • 0035823414 scopus 로고    scopus 로고
    • Role of Phe286 in the recognition mechanism of cyclomaltooligosaccharides (cyclodextrins) by Thermoactinomyces vulgaris R-47 α-amylase 2 (TVAII) X-ray structures of the mutant TVAIIs, F286A and F286Y, and kinetic analyses of the Phe286-replaced mutant TVAIIs
    • Ohtaki A., Kondo S., Shimura Y., Tonozuka T., Sakano Y., and Kamitori S. Role of Phe286 in the recognition mechanism of cyclomaltooligosaccharides (cyclodextrins) by Thermoactinomyces vulgaris R-47 α-amylase 2 (TVAII) X-ray structures of the mutant TVAIIs, F286A and F286Y, and kinetic analyses of the Phe286-replaced mutant TVAIIs. Carbohydr. Res. 334 (2001) 309-313
    • (2001) Carbohydr. Res. , vol.334 , pp. 309-313
    • Ohtaki, A.1    Kondo, S.2    Shimura, Y.3    Tonozuka, T.4    Sakano, Y.5    Kamitori, S.6
  • 25
    • 0027248441 scopus 로고
    • Purification and characterization of a cyclodextrin-degrading enzyme from Flavobacterium sp
    • Bender H. Purification and characterization of a cyclodextrin-degrading enzyme from Flavobacterium sp. Appl. Microbiol. Biotechnol. 39 (1993) 714-719
    • (1993) Appl. Microbiol. Biotechnol. , vol.39 , pp. 714-719
    • Bender, H.1
  • 26
    • 0034705064 scopus 로고    scopus 로고
    • Structure, specificity and function of cyclomaltodextrinase, a multispecific enzyme of the α-amylase family
    • Park K.H., Kim T.J., Cheong T.K., Kim J.W., Oh B.H., and Svensson B. Structure, specificity and function of cyclomaltodextrinase, a multispecific enzyme of the α-amylase family. Biochim. Biophys. Acta 1478 (2000) 165-185
    • (2000) Biochim. Biophys. Acta , vol.1478 , pp. 165-185
    • Park, K.H.1    Kim, T.J.2    Cheong, T.K.3    Kim, J.W.4    Oh, B.H.5    Svensson, B.6
  • 27
    • 0027364214 scopus 로고
    • Refined 1.8-Å structure reveals the mode of binding of beta-cyclodextrin to the maltodextrin binding protein
    • Sharff A.J., Rodseth L.E., and Quiocho F.A. Refined 1.8-Å structure reveals the mode of binding of beta-cyclodextrin to the maltodextrin binding protein. Biochemistry 32 (1993) 10553-10559
    • (1993) Biochemistry , vol.32 , pp. 10553-10559
    • Sharff, A.J.1    Rodseth, L.E.2    Quiocho, F.A.3
  • 28
    • 0042011174 scopus 로고    scopus 로고
    • The binding of beta-and gamma-cyclodextrins to glycogen phosphorylase b: Kinetic and crystallographic studies
    • Pinotsis N., Leonidas D.D., Chrysina E.D., Oikonomakos N.G., and Mavridis I.M. The binding of beta-and gamma-cyclodextrins to glycogen phosphorylase b: Kinetic and crystallographic studies. Protein Sci. 12 (2003) 1914-1924
    • (2003) Protein Sci. , vol.12 , pp. 1914-1924
    • Pinotsis, N.1    Leonidas, D.D.2    Chrysina, E.D.3    Oikonomakos, N.G.4    Mavridis, I.M.5
  • 29
    • 46049115447 scopus 로고    scopus 로고
    • Starch catabolism by a prominent human gut symbiont is directed by the recognition of amylose helices
    • Koropatkin N.M., Martens E.C., Gordon J.I., and Smith T.J. Starch catabolism by a prominent human gut symbiont is directed by the recognition of amylose helices. Structure 16 (2008) 1105-1115
    • (2008) Structure , vol.16 , pp. 1105-1115
    • Koropatkin, N.M.1    Martens, E.C.2    Gordon, J.I.3    Smith, T.J.4
  • 30
    • 0032584737 scopus 로고    scopus 로고
    • Crystal structure of recombinant soybean beta-amylase complexed with beta-cyclodextrin
    • Adachi M., Mikami B., Katsube T., and Utsumi S. Crystal structure of recombinant soybean beta-amylase complexed with beta-cyclodextrin. J. Biol. Chem. 273 (1998) 19859-19865
    • (1998) J. Biol. Chem. , vol.273 , pp. 19859-19865
    • Adachi, M.1    Mikami, B.2    Katsube, T.3    Utsumi, S.4
  • 31
    • 41949118483 scopus 로고    scopus 로고
    • Crystal structure of the polyextremophilic α-amylase AmyB from Halothermothrix orenii: Details of a productive enzyme-substrate complex and an N domain with a role in binding raw starch
    • Tan T.C., Mijts B.N., Swaminathan K., Patel B.K.C., and Divne C. Crystal structure of the polyextremophilic α-amylase AmyB from Halothermothrix orenii: Details of a productive enzyme-substrate complex and an N domain with a role in binding raw starch. J. Mol. Biol. 378 (2008) 852-870
    • (2008) J. Mol. Biol. , vol.378 , pp. 852-870
    • Tan, T.C.1    Mijts, B.N.2    Swaminathan, K.3    Patel, B.K.C.4    Divne, C.5
  • 33
    • 0032574818 scopus 로고    scopus 로고
    • Structure of cyclodextrin glycosyltransferase complexed with a derivative of its main product β-cyclodextrin
    • Schmidt A.K., Cottaz S., Driguez H., and Schulz G.E. Structure of cyclodextrin glycosyltransferase complexed with a derivative of its main product β-cyclodextrin. Biochemistry 37 (1998) 5909-5915
    • (1998) Biochemistry , vol.37 , pp. 5909-5915
    • Schmidt, A.K.1    Cottaz, S.2    Driguez, H.3    Schulz, G.E.4
  • 34
    • 0032145538 scopus 로고    scopus 로고
    • Substrate binding to a cyclodextrin glycosyltransferase and mutations increasing the γ-cyclodextrin production
    • Parsiegla G., Schmidt A.K., and Schulz G.E. Substrate binding to a cyclodextrin glycosyltransferase and mutations increasing the γ-cyclodextrin production. Eur. J. Biochem. 255 (1998) 710-717
    • (1998) Eur. J. Biochem. , vol.255 , pp. 710-717
    • Parsiegla, G.1    Schmidt, A.K.2    Schulz, G.E.3
  • 36
    • 0032571332 scopus 로고    scopus 로고
    • Crystal structure of a catalytic-site mutant α-amylase from Bacillus subtilis complexed with maltopentaose
    • Fujimoto Z., Takase K., Doui N., Momma M., Matsumoto T., and Mizuno H. Crystal structure of a catalytic-site mutant α-amylase from Bacillus subtilis complexed with maltopentaose. J. Mol. Biol. 277 (1998) 393-407
    • (1998) J. Mol. Biol. , vol.277 , pp. 393-407
    • Fujimoto, Z.1    Takase, K.2    Doui, N.3    Momma, M.4    Matsumoto, T.5    Mizuno, H.6
  • 37
    • 3843112354 scopus 로고    scopus 로고
    • Complex structures of Thermoactinomyces vulgaris R-47 α-amylase 2 with acarbose and cyclodextrins demonstrate the multiple substrate recognition mechanism
    • Ohtaki A., Mizuno M., Tonozuka T., Sakano Y., and Kamitori S. Complex structures of Thermoactinomyces vulgaris R-47 α-amylase 2 with acarbose and cyclodextrins demonstrate the multiple substrate recognition mechanism. J. Biol. Chem. 279 (2004) 31033-31040
    • (2004) J. Biol. Chem. , vol.279 , pp. 31033-31040
    • Ohtaki, A.1    Mizuno, M.2    Tonozuka, T.3    Sakano, Y.4    Kamitori, S.5
  • 38
    • 0035045976 scopus 로고    scopus 로고
    • Studies on the hydrolyzing mechanism for cyclodextrins of Thermoactinomyces vulgaris R-47-amylase 2 (TVA II). X-ray structure of the mutant E354A complexed with β-cyclodextrin, and kinetic analyses on cyclodextrins
    • Kondo S., Ohtaki A., Tonozuka T., Sakano Y., and Kamitori S. Studies on the hydrolyzing mechanism for cyclodextrins of Thermoactinomyces vulgaris R-47-amylase 2 (TVA II). X-ray structure of the mutant E354A complexed with β-cyclodextrin, and kinetic analyses on cyclodextrins. J. Biochem. (Tokyo) 129 (2001) 423-428
    • (2001) J. Biochem. (Tokyo) , vol.129 , pp. 423-428
    • Kondo, S.1    Ohtaki, A.2    Tonozuka, T.3    Sakano, Y.4    Kamitori, S.5
  • 39
    • 0027879008 scopus 로고
    • Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants
    • Kabsch W. Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants. J. Appl. Crystallogr. 26 (1993) 795-800
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 795-800
    • Kabsch, W.1
  • 41
    • 13244281317 scopus 로고    scopus 로고
    • COOT: Model-building tools for molecular graphics
    • Emsley P., and Cowtan K. COOT: Model-building tools for molecular graphics. Acta Crystallogr. D 60 (2004) 2126-2132
    • (2004) Acta Crystallogr. D , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 42
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • Murshudov G.N., Vagin A.A., and Dodson E.J. Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr. D 53 (1997) 240-255
    • (1997) Acta Crystallogr. D , vol.53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 43
    • 0028103275 scopus 로고
    • The CCP4 suite: programs for protein crystallography
    • Collaborative Computational Project, Number 4
    • Collaborative Computational Project, Number 4. The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D 50 (1994) 760-763
    • (1994) Acta Crystallogr. D , vol.50 , pp. 760-763
  • 44
    • 34548232365 scopus 로고    scopus 로고
    • Inference of macromolecular assemblies from crystalline state
    • Krissinel E., and Henrick K. Inference of macromolecular assemblies from crystalline state. J. Mol. Biol. 372 (2007) 774-797
    • (2007) J. Mol. Biol. , vol.372 , pp. 774-797
    • Krissinel, E.1    Henrick, K.2
  • 46
    • 0027968068 scopus 로고
    • CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson J.D., Higgins D.G., and Gibson T.J. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22 (1994) 4673-4680
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 47
    • 0038243196 scopus 로고    scopus 로고
    • POVScript+: a program for model and data visualization using persistence of vision ray-tracing
    • Fenn T.D., Ringe D., and Petsko G.A. POVScript+: a program for model and data visualization using persistence of vision ray-tracing. J. Appl. Crystallogr. 36 (2003) 944-947
    • (2003) J. Appl. Crystallogr. , vol.36 , pp. 944-947
    • Fenn, T.D.1    Ringe, D.2    Petsko, G.A.3


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