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Volumn 48, Issue 21, 2009, Pages 4557-4566

The role of a second-shell residue in modifying substrate and inhibitor interactions in the SHV β-lactamase: A study of Ambler position Asn276

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID SUBSTITUTION; CARBAPENEM; CLASS A; CONFORMATIONAL FLEXIBILITY; ELECTROSPRAY IONIZATION MASS SPECTROMETRY; ELECTROSTATIC INTERACTIONS; ENERGY COST; INHIBITOR COMBINATION; LACTAMASE; LACTAMASES; MEROPENEM; SPATIAL POSITIONS; STEADY-STATE KINETICS; TEM;

EID: 66349089235     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi9003292     Document Type: Article
Times cited : (23)

References (50)
  • 1
    • 27144490073 scopus 로고    scopus 로고
    • Extended-spectrum β- lactamases: A clinical update
    • Paterson, D. L., and Bonomo, R. A. (2005) Extended-spectrum β- lactamases: a clinical update. Clin. Microbiol. Rev. 18, 657-686.
    • (2005) Clin. Microbiol. Rev. , vol.18 , pp. 657-686
    • Paterson, D.L.1    Bonomo, R.A.2
  • 3
    • 0023686284 scopus 로고
    • β-Lactamase inhibitors from laboratory to clinic
    • Bush, K. (1988) β-Lactamase inhibitors from laboratory to clinic. Clin. Microbiol. Rev. 1, 109-123.
    • (1988) Clin. Microbiol. Rev. , vol.1 , pp. 109-123
    • Bush, K.1
  • 4
    • 33644522058 scopus 로고    scopus 로고
    • Understanding the longevity of the β-lactam antibiotics and of antibiotic/β-lactamase inhibitor combinations
    • Buynak, J. D. (2006) Understanding the longevity of the β-lactam antibiotics and of antibiotic/β-lactamase inhibitor combinations. Biochem. Pharmacol. 71, 930-940.
    • (2006) Biochem. Pharmacol. , vol.71 , pp. 930-940
    • Buynak, J.D.1
  • 5
    • 35048865729 scopus 로고    scopus 로고
    • Overcoming resistance to β-lactamase inhibitors: Comparing sulbactam to novel inhibitors against clavulanate resistant SHV enzymes with substitutions at Ambler position 244
    • DOI 10.1021/bi700792a
    • Thomson, J. M., Distler, A. M., and Bonomo, R. A. (2007) Overcoming resistance to β-lactamase inhibitors: comparing sulbactam to novel inhibitors against clavulanate resistant SHV enzymes with substitutions at Ambler position 244. Biochemistry 46, 11361-11368. (Pubitemid 47556763)
    • (2007) Biochemistry , vol.46 , Issue.40 , pp. 11361-11368
    • Thomson, J.M.1    Distler, A.M.2    Bonomo, R.A.3
  • 7
    • 24344498687 scopus 로고    scopus 로고
    • Current challenges in antimicrobial chemotherapy: The impact of extended-spectrum β-lactamases and metallo-β-lactamases on the treatment of resistant Gram-negative pathogens
    • Helfand, M. S., and Bonomo, R. A. (2005) Current challenges in antimicrobial chemotherapy: the impact of extended-spectrum β-lactamases and metallo-β-lactamases on the treatment of resistant Gram-negative pathogens. Curr. Opin. Pharmacol. 5 452-458.
    • (2005) Curr. Opin. Pharmacol. , vol.5 , pp. 452-458
    • Helfand, M.S.1    Bonomo, R.A.2
  • 8
    • 3042617004 scopus 로고    scopus 로고
    • The discovery and development of modified penicillin- and cephalosporin-derived β-lactamase inhibitors
    • Buynak, J. D. (2004) The discovery and development of modified penicillin- and cephalosporin-derived β-lactamase inhibitors. Curr. Med. Chem. 11, 1951-1964.
    • (2004) Curr. Med. Chem. , vol.11 , pp. 1951-1964
    • Buynak, J.D.1
  • 10
    • 21644480798 scopus 로고    scopus 로고
    • Structural consequences of the inhibitor-resistant Ser130Gly substitution in TEM β-lactamase
    • DOI 10.1021/bi0502700
    • Thomas, V. L., Golemi-Kotra, D., Kim, C., Vakulenko, S. B., Mobashery, S., and Shoichet, B. K. (2005) Structural consequences of the inhibitor-resistant Ser130Gly substitution in TEM β-lactamase. Biochemistry 44, 9330-9338. (Pubitemid 40934383)
    • (2005) Biochemistry , vol.44 , Issue.26 , pp. 9330-9338
    • Thomas, V.L.1    Golemi-Kotra, D.2    Kim, C.3    Vakulenko, S.B.4    Mobashery, S.5    Shoichet, B.K.6
  • 11
    • 33749349243 scopus 로고    scopus 로고
    • Effect of the inhibitor-resistant M69V substitution on the structures and populations of trans-enamine β-lactamase intermediates
    • DOI 10.1021/bi060990m
    • Totir, M. A., Padayatti, P. S., Helfand, M. S., Carey, M. P., Bonomo, R. A., Carey, P. R., and van den Akker, F. (2006) Effect of the inhibitor-resistant M69V substitution on the structures and populations of trans-enamine β-lactamase intermediates. Biochemistry 45, 11895-11904. (Pubitemid 44497817)
    • (2006) Biochemistry , vol.45 , Issue.39 , pp. 11895-11904
    • Totir, M.A.1    Padayatti, P.S.2    Helfand, M.S.3    Carey, M.P.4    Bonomo, R.A.5    Carey, P.R.6    Van Den Akker, F.7
  • 12
    • 0026779284 scopus 로고
    • Sitedirected mutagenesis at the active site of Escherichia coli TEM-1 β- lactamase. Suicide inhibitor-resistant mutants reveal the role of arginine 244 and methionine 69 in catalysis
    • Delaire, M., Labia, R., Samama, J. P., and Masson, J. M. (1992) Sitedirected mutagenesis at the active site of Escherichia coli TEM-1 β- lactamase. Suicide inhibitor-resistant mutants reveal the role of arginine 244 and methionine 69 in catalysis. J. Biol. Chem. 267, 20600-20606.
    • (1992) J. Biol. Chem. , vol.267 , pp. 20600-20606
    • Delaire, M.1    Labia, R.2    Samama, J.P.3    Masson, J.M.4
  • 13
    • 33748742992 scopus 로고    scopus 로고
    • Probing active site chemistry in SHV β-lactamase variants at Ambler position 244. Understanding unique properties of inhibitor resistance
    • Thomson, J. M., Distler, A. M., Prati, F., and Bonomo, R. A. (2006) Probing active site chemistry in SHV β-lactamase variants at Ambler position 244. Understanding unique properties of inhibitor resistance. J. Biol. Chem. 281, 26734-26744.
    • (2006) J. Biol. Chem. , vol.281 , pp. 26734-26744
    • Thomson, J.M.1    Distler, A.M.2    Prati, F.3    Bonomo, R.A.4
  • 14
    • 0037200056 scopus 로고    scopus 로고
    • The structural bases of antibiotic resistance in the clinically derived mutant beta-lactamases TEM-30, TEM-32, and TEM-34
    • DOI 10.1074/jbc.M204212200
    • Wang, X., Minasov, G., and Shoichet, B. K. (2002) The structural bases of antibiotic resistance in the clinically derived mutant beta-lactamases TEM-30, TEM-32, and TEM-34. J. Biol. Chem. 277, 32149-32156. (Pubitemid 34969028)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.35 , pp. 32149-32156
    • Wang, X.1    Minasov, G.2    Shoichet, B.K.3
  • 16
    • 0033180477 scopus 로고    scopus 로고
    • Class A β- lactamases-enzyme-inhibitor interactions and resistance
    • Yang, Y., Rasmussen, B. A., and Shlaes, D. M. (1999) Class A β- lactamases-enzyme-inhibitor interactions and resistance. Pharmacol. Ther. 83, 141-151.
    • (1999) Pharmacol. Ther. , vol.83 , pp. 141-151
    • Yang, Y.1    Rasmussen, B.A.2    Shlaes, D.M.3
  • 18
    • 0029120340 scopus 로고
    • The asparagine to aspartic acid substitution at position 276 of TEM-35 and TEM-36 is involved in the β-lactamase resistance to clavulanic acid
    • Saves, I., Burlet-Schiltz, O., Swaren, P., Lefevre, F., Masson, J. M., Prome, J. C., and Samama, J. P. (1995) The asparagine to aspartic acid substitution at position 276 of TEM-35 and TEM-36 is involved in the β-lactamase resistance to clavulanic acid. J. Biol. Chem. 270, 18240-18245.
    • (1995) J. Biol. Chem. , vol.270 , pp. 18240-18245
    • Saves, I.1    Burlet-Schiltz, O.2    Swaren, P.3    Lefevre, F.4    Masson, J.M.5    Prome, J.C.6    Samama, J.P.7
  • 19
    • 0033609444 scopus 로고    scopus 로고
    • X-ray structure of the Asn276Asp variant of the Escherichia coli TEM-1 β-lactamase: Direct observation of electrostatic modulation in resistance to inactivation by clavulanic acid
    • Swaren, P., Golemi, D., Cabantous, S., Bulychev, A., Maveyraud, L., Mobashery, S., and Samama, J. P. (1999) X-ray structure of the Asn276Asp variant of the Escherichia coli TEM-1 β-lactamase: direct observation of electrostatic modulation in resistance to inactivation by clavulanic acid. Biochemistry 38, 9570-9576. (Pubitemid 129515254)
    • (1999) Biochemistry , vol.38 , Issue.30 , pp. 9570-9576
    • Swaren, P.1    Golemi, D.2    Cabantous, S.3    Bulychev, A.4    Maveyraud, L.5    Mobashery, S.6    Samama, J.-P.7
  • 20
    • 0027316253 scopus 로고
    • Inactivation of class A β-lactamases by clavulanic acid: The role of Arginine 244 in a proposed noncerted sequence of events
    • Imtiaz, U., Billings, E. M., Knox, J. R., Manavathu, E. K., Lerner, S. A., and Mobashery, S. (1993) Inactivation of class A β-lactamases by clavulanic acid: the role of Arginine 244 in a proposed noncerted sequence of events. J. Am. Chem. Soc. 115, 4435-4442.
    • (1993) J. Am. Chem. Soc. , vol.115 , pp. 4435-4442
    • Imtiaz, U.1    Billings, E.M.2    Knox, J.R.3    Manavathu, E.K.4    Lerner, S.A.5    Mobashery, S.6
  • 21
    • 0026654218 scopus 로고
    • Elucidation of the role of Arginine-244 in the turnover processes of class A β-lactamases
    • Zafaralla, G., Manavathu, E. K., Lerner, S. A., and Mobashery, S. (1992) Elucidation of the role of Arginine-244 in the turnover processes of class A β-lactamases. Biochemistry 31, 3847-3852.
    • (1992) Biochemistry , vol.31 , pp. 3847-3852
    • Zafaralla, G.1    Manavathu, E.K.2    Lerner, S.A.3    Mobashery, S.4
  • 22
    • 0031805291 scopus 로고    scopus 로고
    • Phenotypic study of resistance of β-lactamase-inhibitor-resistant TEM enzymes which differ by naturally occurring variations and by site-directed substitution at Asp276
    • Canica, M. M., Caroff, N., Barthelemy, M., Labia, R., Krishnamoorthy, R., Paul, G., and Dupret, J. M. (1998) Phenotypic study of resistance of β-lactamase-inhibitor-resistant TEM enzymes which differ by naturally occurring variations and by site-directed substitution at Asp276. Antimicrob. Agents Chemother. 42, 1323-1328.
    • (1998) Antimicrob. Agents Chemother. , vol.42 , pp. 1323-1328
    • Canica, M.M.1    Caroff, N.2    Barthelemy, M.3    Labia, R.4    Krishnamoorthy, R.5    Paul, G.6    Dupret, J.M.7
  • 23
    • 0031834415 scopus 로고    scopus 로고
    • Selection and characterization of β-lactam-β-lactamase inactivator-resistant mutants following PCR mutagenesis of the TEM-1 β-lactamase gene
    • Vakulenko, S. B., Geryk, B., Kotra, L. P., Mobashery, S., and Lerner, S. A. (1998) Selection and characterization of β-lactam-β-lactamase inactivator-resistant mutants following PCR mutagenesis of the TEM-1 β-lactamase gene. Antimicrob. Agents Chemother. 42, 1542-1548.
    • (1998) Antimicrob. Agents Chemother. , vol.42 , pp. 1542-1548
    • Vakulenko, S.B.1    Geryk, B.2    Kotra, L.P.3    Mobashery, S.4    Lerner, S.A.5
  • 25
    • 0036894095 scopus 로고    scopus 로고
    • Amino acid substitutions at Ambler position Gly238 in the SHV-1 β-lactamase: Exploring sequence requirements for resistance to penicillins and cephalosporins
    • Hujer, A. M., Hujer, K. M., Helfand, M. S., Anderson, V. E., and Bonomo, R. A. (2002) Amino acid substitutions at Ambler position Gly238 in the SHV-1 β-lactamase: exploring sequence requirements for resistance to penicillins and cephalosporins. Antimicrob. Agents Chemother. 46, 3971-3977.
    • (2002) Antimicrob. Agents Chemother. , vol.46 , pp. 3971-3977
    • Hujer, A.M.1    Hujer, K.M.2    Helfand, M.S.3    Anderson, V.E.4    Bonomo, R.A.5
  • 26
    • 4644252948 scopus 로고    scopus 로고
    • Antibody mapping of the linear epitopes of CMY-2 and SHV-1 β-lactamases
    • Hujer, A. M., Bethel, C. R., and Bonomo, R. A. (2004) Antibody mapping of the linear epitopes of CMY-2 and SHV-1 β-lactamases. Antimicrob. Agents Chemother. 48, 3980-3988.
    • (2004) Antimicrob. Agents Chemother. , vol.48 , pp. 3980-3988
    • Hujer, A.M.1    Bethel, C.R.2    Bonomo, R.A.3
  • 27
    • 0032528235 scopus 로고    scopus 로고
    • Kinetic analysis of an inhibitor-resistant variant of the OHIO-1 β-lactamase, an SHV-family class a enzyme
    • Lin, S., Thomas, M., Shlaes, D. M., Rudin, S. D., Knox, J. R., Anderson, V., and Bonomo, R. A. (1998) Kinetic analysis of an inhibitor-resistant variant of the OHIO-1 β-lactamase, an SHVfamily class A enzyme. Biochem. J. 333(2), 395-400. (Pubitemid 28379542)
    • (1998) Biochemical Journal , vol.333 , Issue.2 , pp. 395-400
    • Lin, S.1    Thomas, M.2    Shlaes, D.M.3    Rudin, S.D.4    Knox, J.R.5    Anderson, V.6    Bonomo, R.A.7
  • 31
    • 0027515959 scopus 로고
    • Kinetic interactions of tazobactam with β-lactamases from all major structural classes
    • Bush, K., Macalintal, C., Rasmussen, B. A., Lee, V. J., and Yang, Y. (1993) Kinetic interactions of tazobactam with β-lactamases from all major structural classes. Antimicrob. Agents Chemother. 37, 851-858.
    • (1993) Antimicrob. Agents Chemother. , vol.37 , pp. 851-858
    • Bush, K.1    Macalintal, C.2    Rasmussen, B.A.3    Lee, V.J.4    Yang, Y.5
  • 34
    • 52449111304 scopus 로고    scopus 로고
    • Inhibition of class A β-lactamases by carbapenems: Crystallographic observation of two conformations of Meropenem in SHV-1
    • Nukaga, M., Bethel, C. R., Thomson, J. M., Hujer, A. M., Distler, A., Anderson, V. E., Knox, J. R., and Bonomo, R. A. (2008) Inhibition of class A β-lactamases by carbapenems: crystallographic observation of two conformations of Meropenem in SHV-1. J. Am. Chem. Soc. 130, 12656-12662.
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 12656-12662
    • Nukaga, M.1    Bethel, C.R.2    Thomson, J.M.3    Hujer, A.M.4    Distler, A.5    Anderson, V.E.6    Knox, J.R.7    Bonomo, R.A.8
  • 35
    • 0029842442 scopus 로고    scopus 로고
    • Inhibition of TEM-2 β-lactamase from Escherichia coli by clavulanic acid: Observation of intermediates by electrospray ionization mass spectrometry
    • DOI 10.1021/bi961044g
    • Brown, R. P., Aplin, R. T., and Schofield, C. J. (1996) Inhibition of TEM-2 β-lactamase from Escherichia coli by clavulanic acid: observation of intermediates by electrospray ionization mass spectrometry. Biochemistry 35, 12421-12432. (Pubitemid 26318037)
    • (1996) Biochemistry , vol.35 , Issue.38 , pp. 12421-12432
    • Brown, R.P.A.1    Aplin, R.T.2    Schofield, C.J.3
  • 37
    • 0027451306 scopus 로고
    • Structure of a phosphonate-inhibited β-lactamase. An analog of the tetrahedral transition state/intermediate of β-lactam hydrolysis
    • Chen, C. C., Rahil, J., Pratt, R. F., and Herzberg, O. (1993) Structure of a phosphonate-inhibited β-lactamase. An analog of the tetrahedral transition state/intermediate of β-lactam hydrolysis. J. Mol. Biol. 234, 165-178.
    • (1993) J. Mol. Biol. , vol.234 , pp. 165-178
    • Chen, C.C.1    Rahil, J.2    Pratt, R.F.3    Herzberg, O.4
  • 38
    • 0023892521 scopus 로고
    • β-Lactamase inhibitors. The inhibition of serine β-lactamases by specific boronic acids
    • Crompton, I. E., Cuthbert, B. K., Lowe, G., and Waley, S. G. (1988) β-Lactamase inhibitors. The inhibition of serine β-lactamases by specific boronic acids. Biochem. J. 251, 453-459.
    • (1988) Biochem. J. , vol.251 , pp. 453-459
    • Crompton, I.E.1    Cuthbert, B.K.2    Lowe, G.3    Waley, S.G.4
  • 39
    • 0035113737 scopus 로고    scopus 로고
    • Energetic, structural, and antimicrobial analyses of β-lactam side chain recognition by β-lactamases
    • DOI 10.1016/S1074-5521(00)00052-1, PII S1074552100000521
    • Caselli, E., Powers, R. A., Blasczcak, L. C., Wu, C. Y., Prati, F., and Shoichet, B. K. (2001) Energetic, structural, and antimicrobial analyses of β-lactam side chain recognition by β-lactamases. Chem Biol 8, 17-31. (Pubitemid 32165809)
    • (2001) Chemistry and Biology , vol.8 , Issue.1 , pp. 17-31
    • Caselli, E.1    Powers, R.A.2    Blasczcak, L.C.3    Wu, C.Y.E.4    Prati, F.5    Shoichet, B.K.6
  • 40
    • 34247135516 scopus 로고    scopus 로고
    • Use of novel boronic acid transition state inhibitors to probe substrate affinity in SHV-type extended-spectrum β-lactamases
    • Thomson, J. M., Prati, F., Bethel, C. R., and Bonomo, R. A. (2007) Use of novel boronic acid transition state inhibitors to probe substrate affinity in SHV-type extended-spectrum β-lactamases. Antimicrob. Agents Chemother. 51, 1577-1579.
    • (2007) Antimicrob. Agents Chemother. , vol.51 , pp. 1577-1579
    • Thomson, J.M.1    Prati, F.2    Bethel, C.R.3    Bonomo, R.A.4
  • 42
    • 0242569199 scopus 로고    scopus 로고
    • Inhibition of Class a and Class C β-Lactamases by Penems: Crystallographic Structures of a Novel 1,4-Thiazepine Intermediate
    • DOI 10.1021/bi034986b
    • Nukaga, M., Abe, T., Venkatesan, A. M., Mansour, T. S., Bonomo, R. A., and Knox, J. R. (2003) Inhibition of class A and class C β- lactamases by penems: crystallographic structures of a novel 1,4- thiazepine intermediate. Biochemistry 42, 13152-13159. (Pubitemid 37420667)
    • (2003) Biochemistry , vol.42 , Issue.45 , pp. 13152-13159
    • Nukaga, M.1    Abe, T.2    Venkatesan, A.M.3    Mansour, T.S.4    Bonomo, R.A.5    Knox, J.R.6
  • 44
    • 0032581949 scopus 로고    scopus 로고
    • Structural basis for clinical longevity of carbapenem antibiotics in the face of challenge by the common class A β-lactamases from the antibiotic-resistant bacteria
    • Maveyraud, L., Mourey, L., Kotra, L. P., Pedelacq, J.-D., Guillet, V., and Mobashery, S. (1998) Structural basis for clinical longevity of carbapenem antibiotics in the face of challenge by the common class A β-lactamases from the antibiotic-resistant bacteria. J. Am. Chem. Soc. 120, 9748-9752.
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 9748-9752
    • Maveyraud, L.1    Mourey, L.2    Kotra, L.P.3    Pedelacq, J.-D.4    Guillet, V.5    Mobashery, S.6
  • 45
    • 0036533471 scopus 로고    scopus 로고
    • Noncovalent interaction energies in covalent complexes: Tem-1 β-lactamase and β-lactams
    • DOI 10.1002/prot.10058
    • Wang, X., Minasov, G., and Shoichet, B. K. (2002) Noncovalent interaction energies in covalent complexes: TEM-1 β-lactamase and β-lactams. Proteins 47, 86-96. (Pubitemid 34195257)
    • (2002) Proteins: Structure, Function and Genetics , vol.47 , Issue.1 , pp. 86-96
    • Wang, X.1    Minasov, G.2    Shoichet, B.K.3
  • 46
    • 0037200056 scopus 로고    scopus 로고
    • The structural bases of antibiotic resistance in the clinically derived mutant β-lactamases TEM-30, TEM-32, and TEM-34
    • DOI 10.1074/jbc.M204212200
    • Wang, X., Minasov, G., and Shoichet, B. K. (2002) The structural bases of antibiotic resistance in the clinically derived mutant β-lactamases TEM-30, TEM-32, and TEM-34. J. Biol. Chem. 277, 32149-32156. (Pubitemid 34969028)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.35 , pp. 32149-32156
    • Wang, X.1    Minasov, G.2    Shoichet, B.K.3
  • 47
    • 0029916468 scopus 로고    scopus 로고
    • Problems encountered in the characterization of IRT β-lactamase- producing clinical Escherichia coli isolates intermediate-resistant to cephalothin
    • Chaibi, E. B., Farzaneh, S., Morand, A., Peduzzi, J., Barthelemy, M., Sirot, D., and Labia, R. (1996) Problems encountered in the characterization of IRT β-lactamase-producing clinical Escherichia coli isolates intermediate-resistant to cephalothin. J. Antimicrob. Chemother. 37, 190-191.
    • (1996) J. Antimicrob. Chemother. , vol.37 , pp. 190-191
    • Chaibi, E.B.1    Farzaneh, S.2    Morand, A.3    Peduzzi, J.4    Barthelemy, M.5    Sirot, D.6    Labia, R.7
  • 48
    • 47649094895 scopus 로고    scopus 로고
    • Zinc coordination geometry and ligand binding affinity: The structural and kinetic analysis of the second-shell serine 228 residue and the methionine 180 residue of the aminopeptidase from Vibrio proteolyticus
    • Ataie, N. J., Hoang, Q. Q., Zahniser, M. P., Tu, Y., Milne, A., Petsko, G. A., and Ringe, D. (2008) Zinc coordination geometry and ligand binding affinity: the structural and kinetic analysis of the second-shell serine 228 residue and the methionine 180 residue of the aminopeptidase from Vibrio proteolyticus. Biochemistry 47, 7673-7683.
    • (2008) Biochemistry , vol.47 , pp. 7673-7683
    • Ataie, N.J.1    Hoang, Q.Q.2    Zahniser, M.P.3    Tu, Y.4    Milne, A.5    Petsko, G.A.6    Ringe, D.7
  • 49
    • 25644459220 scopus 로고    scopus 로고
    • Mimicking natural evolution in metallo-β-lactamases through second-shell ligand mutations
    • Tomatis, P. E., Rasia, R. M., Segovia, L., and Vila, A. J. (2005) Mimicking natural evolution in metallo-β-lactamases through second-shell ligand mutations. Proc. Natl. Acad. Sci. U. S. A. 102, 13761-13766.
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 13761-13766
    • Tomatis, P.E.1    Rasia, R.M.2    Segovia, L.3    Vila, A.J.4


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