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Volumn 44, Issue 38, 2005, Pages 12728-12736

Shared promiscuous activities and evolutionary features in various members of the amidohydrolase superfamily

Author keywords

[No Author keywords available]

Indexed keywords

CHEMICAL REACTIONS; HYDROLYSIS; PROTEINS;

EID: 25444456889     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi051021e     Document Type: Article
Times cited : (107)

References (50)
  • 1
    • 0017272554 scopus 로고
    • Enzyme recruitment in evolution of new function
    • Jensen, R. A. (1976) Enzyme recruitment in evolution of new function, Annu. Rev. Microbiol. 30, 409-25.
    • (1976) Annu. Rev. Microbiol. , vol.30 , pp. 409-425
    • Jensen, R.A.1
  • 2
    • 0033117461 scopus 로고    scopus 로고
    • Catalytic promiscuity and the evolution of new enzymatic activities
    • O'Brien, P. J., and Herschlag, D. (1999) Catalytic promiscuity and the evolution of new enzymatic activities, Chem. Biol. 6, R91-105.
    • (1999) Chem. Biol. , vol.6
    • O'Brien, P.J.1    Herschlag, D.2
  • 3
    • 0035188466 scopus 로고    scopus 로고
    • Catalytic and binding poly-reactivities shared by two unrelated proteins: The potential role of promiscuity in enzyme evolution
    • James, L. C., and Tawfik, D. S. (2001 ) Catalytic and binding poly-reactivities shared by two unrelated proteins: The potential role of promiscuity in enzyme evolution, Protein Sci. 10, 2600-7.
    • (2001) Protein Sci. , vol.10 , pp. 2600-2607
    • James, L.C.1    Tawfik, D.S.2
  • 4
    • 0141957399 scopus 로고    scopus 로고
    • A despecialization step underlying evolution of a family of serine proteases
    • Wouters, M. A., Liu, K., Riek, P., and Husain, A. (2003) A despecialization step underlying evolution of a family of serine proteases, Mol. Cell 12, 343-54.
    • (2003) Mol. Cell , vol.12 , pp. 343-354
    • Wouters, M.A.1    Liu, K.2    Riek, P.3    Husain, A.4
  • 5
    • 10044221852 scopus 로고    scopus 로고
    • The hydratase activity of malonate semialdehyde decarboxylase: Mechanistic and evolutionary implications
    • Poelarends, G. J., Serrano, H., Johnson, W. H., Jr., Hoffman, D. W., and Whitman, C. P. (2004) The hydratase activity of malonate semialdehyde decarboxylase: mechanistic and evolutionary implications, J. Am. Chem. Soc. 126, 15658-9.
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 15658-15659
    • Poelarends, G.J.1    Serrano, H.2    Johnson Jr., W.H.3    Hoffman, D.W.4    Whitman, C.P.5
  • 6
    • 4644358158 scopus 로고    scopus 로고
    • Evolution of enzymatic activity in the tautomerase superfamily: Mechanistic and structural studies of the 1,3-dichloropropene catabolic enzymes
    • Poelarends, G. J., and Whitman, C. P. (2004) Evolution of enzymatic activity in the tautomerase superfamily: mechanistic and structural studies of the 1,3-dichloropropene catabolic enzymes, Bioorg. Chem. 32, 376-92.
    • (2004) Bioorg. Chem. , vol.32 , pp. 376-392
    • Poelarends, G.J.1    Whitman, C.P.2
  • 8
    • 13544277381 scopus 로고    scopus 로고
    • Evolution of enzymatic activities in the orotidine 5′-monophosphate decarboxylase suprafamily: Enhancing the promiscuous D-arabino-hex-3-ulose 6-phosphate synthase reaction catalyzed by 3-keto-L-gulonate 6-phosphate decarboxylase
    • Yew, W. S., Akana, J., Wise, E. L., Rayment, I., and Gerlt, J. A. (2005) Evolution of enzymatic activities in the orotidine 5′-monophosphate decarboxylase suprafamily: enhancing the promiscuous D-arabino-hex-3-ulose 6-phosphate synthase reaction catalyzed by 3-keto-L-gulonate 6-phosphate decarboxylase, Biochemistry 44, 1807-15.
    • (2005) Biochemistry , vol.44 , pp. 1807-1815
    • Yew, W.S.1    Akana, J.2    Wise, E.L.3    Rayment, I.4    Gerlt, J.A.5
  • 9
    • 2542531685 scopus 로고    scopus 로고
    • Evolution of enzymatic activities in the orotidine 5′-monophosphate decarboxylase suprafamily: Mechanistic evidence for a proton relay system in the active site of 3-keto-L-gulonate 6-phosphate decarboxylase
    • Yew, W. S., Wise, E. L., Rayment, I., and Gerlt, J. A. (2004) Evolution of enzymatic activities in the orotidine 5′-monophosphate decarboxylase suprafamily: mechanistic evidence for a proton relay system in the active site of 3-keto-L-gulonate 6-phosphate decarboxylase, Biochemistry 43, 6427-37.
    • (2004) Biochemistry , vol.43 , pp. 6427-6437
    • Yew, W.S.1    Wise, E.L.2    Rayment, I.3    Gerlt, J.A.4
  • 10
    • 2542594077 scopus 로고    scopus 로고
    • Identifying latent enzyme activities: Substrate ambiguity within modern bacterial sugar kinases
    • Miller, B. G., and Raines, R. T. (2004) Identifying latent enzyme activities: substrate ambiguity within modern bacterial sugar kinases, Biochemistry 43, 6387-92.
    • (2004) Biochemistry , vol.43 , pp. 6387-6392
    • Miller, B.G.1    Raines, R.T.2
  • 11
    • 0037780207 scopus 로고    scopus 로고
    • Evolutionary potential of (beta/alpha)8-barrels: Functional promiscuity produced by single substitutions in the enolase superfamily
    • Schmidt, D. M., Mundorff, E. C., Dojka, M., Bermudez, E., Ness, J. E., Govindarajan, S., Babbitt, P. C., Minshull, J., and Gerlt, J. A. (2003) Evolutionary potential of (beta/alpha)8-barrels: functional promiscuity produced by single substitutions in the enolase superfamily, Biochemistry 42, 8387-93.
    • (2003) Biochemistry , vol.42 , pp. 8387-8393
    • Schmidt, D.M.1    Mundorff, E.C.2    Dojka, M.3    Bermudez, E.4    Ness, J.E.5    Govindarajan, S.6    Babbitt, P.C.7    Minshull, J.8    Gerlt, J.A.9
  • 12
    • 0034923923 scopus 로고    scopus 로고
    • Divergent evolution of enzymatic function: Mechanistically diverse superfamilies and functionally distinct suprafamilies
    • Gerlt, J. A., and Babbitt, P. C. (2001) Divergent evolution of enzymatic function: mechanistically diverse superfamilies and functionally distinct suprafamilies, Annu. Rev. Biochem. 70, 209-46.
    • (2001) Annu. Rev. Biochem. , vol.70 , pp. 209-246
    • Gerlt, J.A.1    Babbitt, P.C.2
  • 13
    • 0025284257 scopus 로고
    • The evolution of alpha/beta barrel enzymes
    • Farber, G. K., and Petsko, G. A. (1990) The evolution of alpha/beta barrel enzymes, Trends Biochem. Sci. 15, 228-34.
    • (1990) Trends Biochem. Sci. , vol.15 , pp. 228-234
    • Farber, G.K.1    Petsko, G.A.2
  • 14
    • 0032835301 scopus 로고    scopus 로고
    • Barrel structures in proteins: Automatic identification and classification including a sequence analysis of TIM barrels
    • Nagano, N., Hutchinson, E. G., and Thornton, J. M. (1999) Barrel structures in proteins: automatic identification and classification including a sequence analysis of TIM barrels, Protein Sci. 8, 2072-84.
    • (1999) Protein Sci. , vol.8 , pp. 2072-2084
    • Nagano, N.1    Hutchinson, E.G.2    Thornton, J.M.3
  • 15
    • 0037396345 scopus 로고    scopus 로고
    • Evolution of function in (beta/alpha)8-barrel enzymes
    • Gerlt, J. A., and Raushel, F. M. (2003) Evolution of function in (beta/alpha)8-barrel enzymes, Curr. Opin. Chem. Biol. 7, 252-64.
    • (2003) Curr. Opin. Chem. Biol. , vol.7 , pp. 252-264
    • Gerlt, J.A.1    Raushel, F.M.2
  • 16
    • 17844384785 scopus 로고    scopus 로고
    • Structural and catalytic diversity within the amidohydrolase superfamily
    • Seibert, C. M., and Raushel, F. M. (2005) Structural and Catalytic Diversity within the Amidohydrolase Superfamily, Biochemistry 44, 6383-91.
    • (2005) Biochemistry , vol.44 , pp. 6383-6391
    • Seibert, C.M.1    Raushel, F.M.2
  • 17
    • 0031000649 scopus 로고    scopus 로고
    • An evolutionary treasure: Unification of a broad set of amidohydrolases related to urease
    • Holm, L., and Sander, C. (1997) An evolutionary treasure: unification of a broad set of amidohydrolases related to urease, Proteins 28, 72-82.
    • (1997) Proteins , vol.28 , pp. 72-82
    • Holm, L.1    Sander, C.2
  • 18
    • 0024340489 scopus 로고
    • Structure-activity relationships in the hydrolysis of substrates by the phosphotriesterase from Pseudomonas diminuta
    • Donarski, W. J., Dumas, D. P., Heitmeyer, D. P., Lewis, V. E., and Raushel, F. M. (1989) Structure-activity relationships in the hydrolysis of substrates by the phosphotriesterase from Pseudomonas diminuta, Biochemistry 28, 4650-5.
    • (1989) Biochemistry , vol.28 , pp. 4650-4655
    • Donarski, W.J.1    Dumas, D.P.2    Heitmeyer, D.P.3    Lewis, V.E.4    Raushel, F.M.5
  • 19
    • 0024316913 scopus 로고
    • Purification and properties of the phosphotriesterase from Pseudomonas diminuta
    • Dumas, D. P., Caldwell, S. R., Wild, J. R., and Raushel, F. M. (1989) Purification and properties of the phosphotriesterase from Pseudomonas diminuta, J. Biol. Chem. 264, 19659-65.
    • (1989) J. Biol. Chem. , vol.264 , pp. 19659-19665
    • Dumas, D.P.1    Caldwell, S.R.2    Wild, J.R.3    Raushel, F.M.4
  • 20
    • 0026748791 scopus 로고
    • Characterization of the zinc binding site of bacterial phosphotriesterase
    • Omburo, G. A., Kuo, J. M., Mullins, L. S., and Raushel, F. M. (1992) Characterization of the zinc binding site of bacterial phosphotriesterase, J. Biol. Chem. 267, 13278-83.
    • (1992) J. Biol. Chem. , vol.267 , pp. 13278-13283
    • Omburo, G.A.1    Kuo, J.M.2    Mullins, L.S.3    Raushel, F.M.4
  • 21
    • 0032504197 scopus 로고    scopus 로고
    • Hydrolysis of phosphodiesters through transformation of the bacterial phosphotriesterase
    • Shim, H., Hong, S. B., and Raushel, F. M. (1998) Hydrolysis of phosphodiesters through transformation of the bacterial phosphotriesterase, J. Biol. Chem. 273, 17445-50.
    • (1998) J. Biol. Chem. , vol.273 , pp. 17445-17450
    • Shim, H.1    Hong, S.B.2    Raushel, F.M.3
  • 22
    • 0033537687 scopus 로고    scopus 로고
    • Modification of near active site residues in organophosphorus hydrolase reduces metal stoichiometry and alters substrate specificity
    • diSioudi, B., Grimsley, J. K., Lai, K., and Wild, J. R. (1999) Modification of near active site residues in organophosphorus hydrolase reduces metal stoichiometry and alters substrate specificity, Biochemistry 38, 2866-72.
    • (1999) Biochemistry , vol.38 , pp. 2866-2872
    • Sioudi, B.1    Grimsley, J.K.2    Lai, K.3    Wild, J.R.4
  • 23
    • 17144364646 scopus 로고    scopus 로고
    • Directed evolution of phosphotriesterase from Pseudomonas diminuta for heterologous expression in Escherichia coli results in stabilization of the metal-free state
    • Roodveldt, C., and Tawfik, D. S. (2005) Directed evolution of phosphotriesterase from Pseudomonas diminuta for heterologous expression in Escherichia coli results in stabilization of the metal-free state, Protein Eng., Des. Sel. 18, 51-58.
    • (2005) Protein Eng., Des. Sel. , vol.18 , pp. 51-58
    • Roodveldt, C.1    Tawfik, D.S.2
  • 24
    • 0033658178 scopus 로고    scopus 로고
    • Phosphotriesterase: An enzyme in search of its natural substrate
    • Raushel, F. M., and Holden, H. M. (2000) Phosphotriesterase: an enzyme in search of its natural substrate, Adv. Enzymol. Relat. Areas Mol. Biol. 74, 51-93.
    • (2000) Adv. Enzymol. Relat. Areas Mol. Biol. , vol.74 , pp. 51-93
    • Raushel, F.M.1    Holden, H.M.2
  • 25
    • 0032515956 scopus 로고    scopus 로고
    • Biochemical characterization and crystallographic structure of an Escherichia coli protein from the phosphotriesterase gene family
    • Buchbinder, J. L., Stephenson, R. C., Dresser, M. J., Pitera, J. W., Scanlan, T. S., and Fletterick, R. J. (1998) Biochemical characterization and crystallographic structure of an Escherichia coli protein from the phosphotriesterase gene family, Biochemistry 37, 5096-106.
    • (1998) Biochemistry , vol.37 , pp. 5096-5106
    • Buchbinder, J.L.1    Stephenson, R.C.2    Dresser, M.J.3    Pitera, J.W.4    Scanlan, T.S.5    Fletterick, R.J.6
  • 26
  • 27
    • 11144301188 scopus 로고    scopus 로고
    • Mechanism of the dihydroorotase reaction
    • Porter, T. N., Li, Y., and Raushel, F. M. (2004) Mechanism of the dihydroorotase reaction, Biochemistry 43, 16285-92.
    • (2004) Biochemistry , vol.43 , pp. 16285-16292
    • Porter, T.N.1    Li, Y.2    Raushel, F.M.3
  • 28
    • 0035846958 scopus 로고    scopus 로고
    • In vitro evolution of beta-glucuronidase into a beta-galactosidase proceeds through non-specific intermediates
    • Matsumura, I., and Ellington, A. D. (2001) In vitro evolution of beta-glucuronidase into a beta-galactosidase proceeds through non-specific intermediates, J. Mol. Biol. 305, 331-9.
    • (2001) J. Mol. Biol. , vol.305 , pp. 331-339
    • Matsumura, I.1    Ellington, A.D.2
  • 30
    • 0021337801 scopus 로고
    • Dihydroorotase from Escherichia coli. Purification and characterization
    • Washabaugh, M. W., and Collins, K. D. (1984) Dihydroorotase from Escherichia coli. Purification and characterization, J. Biol. Chem. 259, 3293-8.
    • (1984) J. Biol. Chem. , vol.259 , pp. 3293-3298
    • Washabaugh, M.W.1    Collins, K.D.2
  • 31
    • 0029999325 scopus 로고    scopus 로고
    • Hyper-mutagenic PCR involving all four transitions and a sizeable proportion of transversions
    • Vartanian, J. P., Henry, M., and Wain-Hobson, S. (1996) Hyper-mutagenic PCR involving all four transitions and a sizeable proportion of transversions, Nucleic Acids Res. 24, 2627-31.
    • (1996) Nucleic Acids Res. , vol.24 , pp. 2627-2631
    • Vartanian, J.P.1    Henry, M.2    Wain-Hobson, S.3
  • 32
    • 0029869449 scopus 로고    scopus 로고
    • An approach to random mutagenesis of DNA using mixtures of triphosphate derivatives of nucleoside analogues
    • Zaccolo, M., Williams, D. M., Brown, D. M., and Gherardi, E. (1996) An approach to random mutagenesis of DNA using mixtures of triphosphate derivatives of nucleoside analogues, J. Mol. Biol. 255, 589-603.
    • (1996) J. Mol. Biol. , vol.255 , pp. 589-603
    • Zaccolo, M.1    Williams, D.M.2    Brown, D.M.3    Gherardi, E.4
  • 33
    • 0028110130 scopus 로고
    • DNA shuffling by random fragmentation and reassembly: In vitro recombination for molecular evolution
    • Stemmer, W. P. (1994) DNA shuffling by random fragmentation and reassembly: in vitro recombination for molecular evolution, Proc. Natl. Acad. Sci. U.S.A. 91, 10747-51.
    • (1994) Proc. Natl. Acad. Sci. U.S.A. , vol.91 , pp. 10747-10751
    • Stemmer, W.P.1
  • 34
    • 16844379112 scopus 로고    scopus 로고
    • Directed evolution of the promiscuous esterase activity of carbonic anhydrase II
    • Gould, S. M., and Tawfik, D. S. (2005) Directed evolution of the promiscuous esterase activity of carbonic anhydrase II, Biochemistry 44, 5444-52.
    • (2005) Biochemistry , vol.44 , pp. 5444-5452
    • Gould, S.M.1    Tawfik, D.S.2
  • 35
    • 0347635518 scopus 로고    scopus 로고
    • Directed evolution of mammalian paraoxonases PON1 and PON3 for bacterial expression and catalytic specialization
    • Aharoni, A., Gaidukov, L., Yagur, S., Toker, L., Silman, I., and Tawfik, D. S. (2004) Directed evolution of mammalian paraoxonases PON1 and PON3 for bacterial expression and catalytic specialization, Proc. Natl. Acad. Sci. U.S.A. 101, 482-7.
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 482-487
    • Aharoni, A.1    Gaidukov, L.2    Yagur, S.3    Toker, L.4    Silman, I.5    Tawfik, D.S.6
  • 36
    • 0033013283 scopus 로고    scopus 로고
    • Screening, nucleotide sequence, and biochemical characterization of an esterase from Pseudomonas fluorescens with high activity towards lactones
    • Khalameyzer, V., Fischer, L., Bornscheuer, U. T., and Altenbuchner, J. (1999) Screening, nucleotide sequence, and biochemical characterization of an esterase from Pseudomonas fluorescens with high activity towards lactones, Appl. Environ. Microbiol. 65, 477-82.
    • (1999) Appl. Environ. Microbiol. , vol.65 , pp. 477-482
    • Khalameyzer, V.1    Fischer, L.2    Bornscheuer, U.T.3    Altenbuchner, J.4
  • 38
    • 0029759529 scopus 로고    scopus 로고
    • Metal-substrate interactions facilitate the catalytic activity of the bacterial phosphotriesterase
    • Hong, S. B., and Raushel, F. M. (1996) Metal-substrate interactions facilitate the catalytic activity of the bacterial phosphotriesterase, Biochemistry 35, 10904-12.
    • (1996) Biochemistry , vol.35 , pp. 10904-10912
    • Hong, S.B.1    Raushel, F.M.2
  • 39
    • 0029137828 scopus 로고
    • The structure and evolution of alpha/beta barrel proteins
    • Reardon, D., and Farber, G. K. (1995) The structure and evolution of alpha/beta barrel proteins, FASEB J. 9, 497-503.
    • (1995) FASEB J. , vol.9 , pp. 497-503
    • Reardon, D.1    Farber, G.K.2
  • 40
    • 0035814923 scopus 로고    scopus 로고
    • High-resolution X-ray structures of different metal-substituted forms of phosphotriesterase from Pseudomonas diminuta
    • Benning, M. M., Shim, H., Raushel, F. M., and Holden, H. M. (2001) High-resolution X-ray structures of different metal-substituted forms of phosphotriesterase from Pseudomonas diminuta, Biochemistry 40, 2712-22.
    • (2001) Biochemistry , vol.40 , pp. 2712-2722
    • Benning, M.M.1    Shim, H.2    Raushel, F.M.3    Holden, H.M.4
  • 41
    • 2442496666 scopus 로고    scopus 로고
    • Mechanism for the hydrolysis of organophosphates by the bacterial phosphotriesterase
    • Aubert, S. D., Li, Y., and Raushel, F. M. (2004) Mechanism for the hydrolysis of organophosphates by the bacterial phosphotriesterase, Biochemistry 43, 5707-15.
    • (2004) Biochemistry , vol.43 , pp. 5707-5715
    • Aubert, S.D.1    Li, Y.2    Raushel, F.M.3
  • 44
    • 0028609492 scopus 로고
    • Three-dimensional structure of phosphotriesterase: An enzyme capable of detoxifying organophosphate nerve agents
    • Benning, M. M., Kuo, J. M., Raushel, F. M., and Holden, H. M. (1994) Three-dimensional structure of phosphotriesterase: an enzyme capable of detoxifying organophosphate nerve agents, Biochemistry 33, 15001-7.
    • (1994) Biochemistry , vol.33 , pp. 15001-15007
    • Benning, M.M.1    Kuo, J.M.2    Raushel, F.M.3    Holden, H.M.4
  • 45
    • 0034730534 scopus 로고    scopus 로고
    • The binding of substrate analogs to phosphotriesterase
    • Benning, M. M., Hong, S. B., Raushel, F. M., and Holden, H. M. (2000) The binding of substrate analogs to phosphotriesterase, J. Biol. Chem. 275, 30556-60.
    • (2000) J. Biol. Chem. , vol.275 , pp. 30556-30560
    • Benning, M.M.1    Hong, S.B.2    Raushel, F.M.3    Holden, H.M.4
  • 46
    • 0034730195 scopus 로고    scopus 로고
    • Directed evolution of a (beta alpha)8-barrel enzyme to catalyze related reactions in two different metabolic pathways
    • Jurgens, C., Strom, A., Wegener, D., Hettwer, S., Wilmanns, M., and Sterner, R. (2000) Directed evolution of a (beta alpha)8-barrel enzyme to catalyze related reactions in two different metabolic pathways, Proc. Natl. Acad. Sci. U.S.A. 97, 9925-30.
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 9925-9930
    • Jurgens, C.1    Strom, A.2    Wegener, D.3    Hettwer, S.4    Wilmanns, M.5    Sterner, R.6
  • 47
    • 0038625074 scopus 로고    scopus 로고
    • Mimicking natural evolution in vitro: An N-acetylneuraminate lyase mutant with an increased dihydrodipicolinate synthase activity
    • Joerger, A. C., Mayer, S., and Fersht, A. R. (2003) Mimicking natural evolution in vitro: an N-acetylneuraminate lyase mutant with an increased dihydrodipicolinate synthase activity, Proc. Natl. Acad. Sci. U.S.A. 100, 5694-9.
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 5694-5699
    • Joerger, A.C.1    Mayer, S.2    Fersht, A.R.3
  • 48
    • 0027245444 scopus 로고
    • Random mutagenesis of the substrate-binding site of a serine protease can generate enzymes with increased activities and altered primary specificities
    • Graham, L. D., Haggett, K. D., Jennings, P. A., Le Brocque, D. S., Whittaker, R. G., and Schober, P. A. (1993) Random mutagenesis of the substrate-binding site of a serine protease can generate enzymes with increased activities and altered primary specificities, Biochemistry 32, 6250-8.
    • (1993) Biochemistry , vol.32 , pp. 6250-6258
    • Graham, L.D.1    Haggett, K.D.2    Jennings, P.A.3    Le Brocque, D.S.4    Whittaker, R.G.5    Schober, P.A.6
  • 49
    • 0032510667 scopus 로고    scopus 로고
    • Directed evolution of an aspartate aminotransferase with new substrate specificities
    • Yano, T., Oue, S., and Kagamiyama, H. (1998) Directed evolution of an aspartate aminotransferase with new substrate specificities, Proc. Natl. Acad. Sci. U.S.A. 95, 5511-5.
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 5511-5515
    • Yano, T.1    Oue, S.2    Kagamiyama, H.3
  • 50
    • 0030989062 scopus 로고    scopus 로고
    • Directed evolution of a fucosidase from a galactosidase by DNA shuffling and screening
    • Zhang, J. H., Dawes, G., and Stemmer, W. P. (1997) Directed evolution of a fucosidase from a galactosidase by DNA shuffling and screening, Proc. Natl. Acad. Sci. U.S.A. 94, 4504-9.
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 4504-4509
    • Zhang, J.H.1    Dawes, G.2    Stemmer, W.P.3


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