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Volumn 45, Issue 7, 2006, Pages 2129-2138

Role of arginine residues in the active site of the membrane-bound lytic transglycosylase B from Pseudomonas aeruginosa

Author keywords

[No Author keywords available]

Indexed keywords

ASSAYS; BACTERIA; CATALYSIS; CELLS; MUTAGENESIS; PERTURBATION TECHNIQUES; POLYMERS; PROTEINS; SUBSTRATES;

EID: 33144476665     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi052342t     Document Type: Article
Times cited : (14)

References (48)
  • 1
    • 0041664049 scopus 로고    scopus 로고
    • Bacterial shape
    • Young, K. D. (2003) Bacterial shape, Mol. Microbiol. 49, 571-580.
    • (2003) Mol. Microbiol. , vol.49 , pp. 571-580
    • Young, K.D.1
  • 3
    • 0037858060 scopus 로고    scopus 로고
    • Growth of the stress-bearing and shape-maintaining murein sacculus of Escherichia coli
    • Holtje, J. V. (1998) Growth of the stress-bearing and shape-maintaining murein sacculus of Escherichia coli, Microbiol. Mol. Biol. Rev. 62, 181-203.
    • (1998) Microbiol. Mol. Biol. Rev. , vol.62 , pp. 181-203
    • Holtje, J.V.1
  • 4
    • 0016726181 scopus 로고
    • Novel type of murein transglycosylase in Escherichia coli
    • Holtje, J. V., Mirelman, D., Sharon, N., and Schwarz, U. (1975) Novel type of murein transglycosylase in Escherichia coli, J. Bacteriol. 124, 1067-1076.
    • (1975) J. Bacteriol. , vol.124 , pp. 1067-1076
    • Holtje, J.V.1    Mirelman, D.2    Sharon, N.3    Schwarz, U.4
  • 5
    • 0021881891 scopus 로고
    • Recycling of murein by Escherichia coli
    • Goodell, E. W. (1985) Recycling of murein by Escherichia coli, J. Bacteriol. 163, 305-310.
    • (1985) J. Bacteriol. , vol.163 , pp. 305-310
    • Goodell, E.W.1
  • 6
    • 0026066957 scopus 로고
    • The murein hydrolases of Escherichia coli: Properties, functions and impact on the course of infections in vivo
    • Holtje, J. V., and Tuomanen, E. I. (1991) The murein hydrolases of Escherichia coli: properties, functions and impact on the course of infections in vivo, J. Gen. Microbiol. 137, 441-454.
    • (1991) J. Gen. Microbiol. , vol.137 , pp. 441-454
    • Holtje, J.V.1    Tuomanen, E.I.2
  • 7
    • 0344393521 scopus 로고    scopus 로고
    • Lytic transglycosylases in macromolecular transport systems of Gram-negative bacteria
    • Koraimann, G. (2003) Lytic transglycosylases in macromolecular transport systems of Gram-negative bacteria, Cell. Mol. Life Sci. 60, 2371-2388.
    • (2003) Cell. Mol. Life Sci. , vol.60 , pp. 2371-2388
    • Koraimann, G.1
  • 8
    • 0029842085 scopus 로고    scopus 로고
    • Peptidoglycan as a barrier to transenvelope transport
    • Dijkstra, A. J., and Keck, W. (1996) Peptidoglycan as a barrier to transenvelope transport, J. Bacteriol. 178, 5555-5562.
    • (1996) J. Bacteriol. , vol.178 , pp. 5555-5562
    • Dijkstra, A.J.1    Keck, W.2
  • 9
    • 0026605558 scopus 로고
    • O-Acetylated peptidoglycan: Its occurrence, pathobiological significance, and biosynthesis
    • Clarke, A. J., and Dupont, C. (1992) O-Acetylated peptidoglycan: its occurrence, pathobiological significance, and biosynthesis, Can. J. Microbiol. 38, 85-91.
    • (1992) Can. J. Microbiol. , vol.38 , pp. 85-91
    • Clarke, A.J.1    Dupont, C.2
  • 10
    • 0027499306 scopus 로고
    • Bordetella pertussis tracheal cytotoxin and other muramyl peptides: Distinct structure-activity relationships for respiratory epithelial cytopathology
    • Luker, K. E., Collier, J. L., Kolodziej, E. W., Marshall, G. R., and Goldman, W. E. (1993) Bordetella pertussis tracheal cytotoxin and other muramyl peptides: distinct structure-activity relationships for respiratory epithelial cytopathology, Proc. Natl. Acad. Sci. U.S.A. 90, 2365-2359.
    • (1993) Proc. Natl. Acad. Sci. U.S.A. , vol.90 , pp. 2365-12359
    • Luker, K.E.1    Collier, J.L.2    Kolodziej, E.W.3    Marshall, G.R.4    Goldman, W.E.5
  • 11
    • 0021326947 scopus 로고
    • Ability of monomeric peptidoglycan fragments from Neisseria gonorrhoeae to damage human fallopian-tube mucosa
    • Melly, M. A., McGee, Z. A., and Rosenthal, R. S. (1984) Ability of monomeric peptidoglycan fragments from Neisseria gonorrhoeae to damage human fallopian-tube mucosa, J. Infect. Dis. 149, 378-386.
    • (1984) J. Infect. Dis. , vol.149 , pp. 378-386
    • Melly, M.A.1    McGee, Z.A.2    Rosenthal, R.S.3
  • 12
    • 0035140936 scopus 로고    scopus 로고
    • Identification of four families of peptidoglycan lytic transglycosylases
    • Blackburn, N. T., and Clarke, A. J. (2001) Identification of four families of peptidoglycan lytic transglycosylases, J. Mol. Evol. 52, 78-84.
    • (2001) J. Mol. Evol. , vol.52 , pp. 78-84
    • Blackburn, N.T.1    Clarke, A.J.2
  • 13
    • 0029814366 scopus 로고    scopus 로고
    • Microbial pathogenesis in cystic fibrosis: Mucoid Pseudomonas aeruginosa and Burkholderia cepacia
    • Govan, J. R., and Deretic, V. (1996) Microbial pathogenesis in cystic fibrosis: mucoid Pseudomonas aeruginosa and Burkholderia cepacia, Microbiol. Rev. 60, 539-574.
    • (1996) Microbiol. Rev. , vol.60 , pp. 539-574
    • Govan, J.R.1    Deretic, V.2
  • 14
    • 0037154093 scopus 로고    scopus 로고
    • Characterization of soluble and membrane-bound family 3 lytic transglycosylases from Pseudomonas aeruginosa
    • Blackburn, N. T., and Clarke, A. J. (2002) Characterization of soluble and membrane-bound family 3 lytic transglycosylases from Pseudomonas aeruginosa, Biochemistry 41, 1001-1013.
    • (2002) Biochemistry , vol.41 , pp. 1001-1013
    • Blackburn, N.T.1    Clarke, A.J.2
  • 15
    • 4444306016 scopus 로고    scopus 로고
    • Substrate binding affinity of Pseudomonas aeruginosa membrane-bound lytic transglycosylase B by hydrogen-deuterium exchange MALDI MS
    • Reid, C. W., Brewer, D., and Clarke, A. J. (2004) Substrate binding affinity of Pseudomonas aeruginosa membrane-bound lytic transglycosylase B by hydrogen-deuterium exchange MALDI MS, Biochemistry 43, 11275-11282.
    • (2004) Biochemistry , vol.43 , pp. 11275-11282
    • Reid, C.W.1    Brewer, D.2    Clarke, A.J.3
  • 16
    • 0029947945 scopus 로고    scopus 로고
    • NAG-thiazoline, an N-acetyl-betahexosaminidase inhibitor that implicates acetamido participation
    • Knapp, S., Vocadlo, D. J., Gao, Z., Kirk, B., Lou, J., and Withers, S. G. (1996) NAG-thiazoline, an N-acetyl-betahexosaminidase inhibitor that implicates acetamido participation, J. Am. Chem. Soc. 118, 6804-6805.
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 6804-6805
    • Knapp, S.1    Vocadlo, D.J.2    Gao, Z.3    Kirk, B.4    Lou, J.5    Withers, S.G.6
  • 17
    • 2342542869 scopus 로고    scopus 로고
    • The effect of NAG-thiazoline on morphology and surface hydrophobicity of Escherichia coli
    • Reid, C. W., Blackburn, N. T., and Clarke, A. J. (2004) The effect of NAG-thiazoline on morphology and surface hydrophobicity of Escherichia coli, FEMS Microbiol. Lett. 234, 343-348.
    • (2004) FEMS Microbiol. Lett. , vol.234 , pp. 343-348
    • Reid, C.W.1    Blackburn, N.T.2    Clarke, A.J.3
  • 18
    • 4444272536 scopus 로고    scopus 로고
    • Inhibition of membrane-bound lytic transglycosylase B by NAG-thiazoline
    • Reid, C. W., Blackburn, N. T., Legaree, B. A., Auzanneau, F. I., and Clarke, A. J. (2004) Inhibition of membrane-bound lytic transglycosylase B by NAG-thiazoline, FEBS Lett. 574, 73-79.
    • (2004) FEBS Lett. , vol.574 , pp. 73-79
    • Reid, C.W.1    Blackburn, N.T.2    Legaree, B.A.3    Auzanneau, F.I.4    Clarke, A.J.5
  • 19
    • 0027293346 scopus 로고
    • Compositional analysis of peptidoglycan by high-performance anion-exchange chromatography
    • Clarke, A. J. (1993) Compositional analysis of peptidoglycan by high-performance anion-exchange chromatography, Anal. Biochem. 212, 344-350.
    • (1993) Anal. Biochem. , vol.212 , pp. 344-350
    • Clarke, A.J.1
  • 20
    • 0023765918 scopus 로고
    • Separation and quantification of muropeptides with high-performance liquid chromatography
    • Glauner, B. (1988) Separation and quantification of muropeptides with high-performance liquid chromatography, Anal. Biochem. 172, 451-464.
    • (1988) Anal. Biochem. , vol.172 , pp. 451-464
    • Glauner, B.1
  • 21
    • 0028093382 scopus 로고
    • Analysis of the sodium dodecyl sulfate-stable peptidoglycan autolysins of select gram-negative pathogens by using renaturing polyacrylamide gel electrophoresis
    • Bernadsky, G., Beveridge, T. J., and Clarke, A. J. (1994) Analysis of the sodium dodecyl sulfate-stable peptidoglycan autolysins of select gram-negative pathogens by using renaturing polyacrylamide gel electrophoresis, J. Bacteriol. 176, 5225-5232.
    • (1994) J. Bacteriol. , vol.176 , pp. 5225-5232
    • Bernadsky, G.1    Beveridge, T.J.2    Clarke, A.J.3
  • 22
    • 0028132119 scopus 로고
    • Role of autolysins in the EDTA-induced lysis of Pseudomonas aeruginosa
    • Watt, S. R., and Clarke, A. J. (1994) Role of autolysins in the EDTA-induced lysis of Pseudomonas aeruginosa, FEMS Microbiol. Lett. 124, 113-119.
    • (1994) FEMS Microbiol. Lett. , vol.124 , pp. 113-119
    • Watt, S.R.1    Clarke, A.J.2
  • 23
    • 0031453760 scopus 로고    scopus 로고
    • Isolation, purification, and characterization of the major autolysin from Pseudomonas aeruginosa
    • Watt, S. R., and Clarke, A. J. (1997) Isolation, purification, and characterization of the major autolysin from Pseudomonas aeruginosa, Can. J. Microbiol. 43, 1054-1062.
    • (1997) Can. J. Microbiol. , vol.43 , pp. 1054-1062
    • Watt, S.R.1    Clarke, A.J.2
  • 24
    • 0034633271 scopus 로고    scopus 로고
    • Assay for lytic transglycosylases: A family of peptidoglycan lyases
    • Blackburn, N. T., and Clarke, A. J. (2000) Assay for lytic transglycosylases: a family of peptidoglycan lyases, Anal. Biochem. 284, 388-393.
    • (2000) Anal. Biochem. , vol.284 , pp. 388-393
    • Blackburn, N.T.1    Clarke, A.J.2
  • 25
    • 4944223117 scopus 로고    scopus 로고
    • Murein (peptidoglycan) binding property of the essential cell division protein FtsN from Escherichia coli
    • Ursinus, A., van den Ent, F., Brechtel, S., de Pedro, M., Holtje, J. V., Lowe, J., and Vollmer, W. (2004) Murein (peptidoglycan) binding property of the essential cell division protein FtsN from Escherichia coli, J. Bacteriol. 186, 6728-6737.
    • (2004) J. Bacteriol. , vol.186 , pp. 6728-6737
    • Ursinus, A.1    Van Den Ent, F.2    Brechtel, S.3    De Pedro, M.4    Holtje, J.V.5    Lowe, J.6    Vollmer, W.7
  • 26
    • 0037019523 scopus 로고    scopus 로고
    • A general mass spectrometry-based assay for the quantitation of protein-ligand binding interactions in solution
    • Powell, K. D., Ghaemmaghami, S., Wang, M. Z., Ma, L., Oas, T. G., and Fitzgerald, M. C. (2002) A general mass spectrometry-based assay for the quantitation of protein-ligand binding interactions in solution, J. Am. Chem. Soc. 124, 10256-10257.
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 10256-10257
    • Powell, K.D.1    Ghaemmaghami, S.2    Wang, M.Z.3    Ma, L.4    Oas, T.G.5    Fitzgerald, M.C.6
  • 27
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of bacteriophages T4
    • Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of bacteriophages T4, Nature 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 29
    • 0034595501 scopus 로고    scopus 로고
    • Enhanced genome annotation using structural profiles in the program 3D-PSSM
    • Kelly, L. A., MacCallum, R. M., and Sternberg, M. J. E. (2000) Enhanced genome annotation using structural profiles in the program 3D-PSSM, J. Mol. Biol. 299, 499-520.
    • (2000) J. Mol. Biol. , vol.299 , pp. 499-520
    • Kelly, L.A.1    MacCallum, R.M.2    Sternberg, M.J.E.3
  • 30
    • 0034728363 scopus 로고    scopus 로고
    • Crystallographic studies of the interactions of Escherichia coli lytic transglycosylase Slt35 with peptidoglycan
    • van Asselt, E. J., Kalk, K. H., and Dijkstra, B. W. (2000) Crystallographic studies of the interactions of Escherichia coli lytic transglycosylase Slt35 with peptidoglycan, Biochemistry 39, 1924-1934.
    • (2000) Biochemistry , vol.39 , pp. 1924-1934
    • Van Asselt, E.J.1    Kalk, K.H.2    Dijkstra, B.W.3
  • 31
    • 0342901668 scopus 로고    scopus 로고
    • Crystal structure of Escherichia coli lytic transglycosylase Slt35 reveals a lysozyme-like catalytic domain with an EF-hand
    • van Asselt, E.J., Dijkstra, A. J., Kalk, K. H., Takacs, B., Keck, W., and Dijkstra, B. W. (1999) Crystal structure of Escherichia coli lytic transglycosylase Slt35 reveals a lysozyme-like catalytic domain with an EF-hand, Structure 7, 1167-1180.
    • (1999) Structure , vol.7 , pp. 1167-1180
    • Van Asselt, E.J.1    Dijkstra, A.J.2    Kalk, K.H.3    Takacs, B.4    Keck, W.5    Dijkstra, B.W.6
  • 32
    • 0015462556 scopus 로고
    • Peptidoglycan types of bacterial cell walls and their taxonomic implications
    • Schleifer, K. H., and Kandler, O. (1972) Peptidoglycan types of bacterial cell walls and their taxonomic implications, Bacteriol. Rev. 36, 407-477.
    • (1972) Bacteriol. Rev. , vol.36 , pp. 407-477
    • Schleifer, K.H.1    Kandler, O.2
  • 33
    • 0029963621 scopus 로고    scopus 로고
    • Bacteriolytic effect of membrane vesicles from Pseudomonas aeruginosa on other bacteria including pathogens: Conceptually new antibiotics
    • Kadurugamuwa, J. L., and Beveridge, T. J. (1996) Bacteriolytic effect of membrane vesicles from Pseudomonas aeruginosa on other bacteria including pathogens: conceptually new antibiotics, J. Bacteriol. 178, 2767-2774.
    • (1996) J. Bacteriol. , vol.178 , pp. 2767-2774
    • Kadurugamuwa, J.L.1    Beveridge, T.J.2
  • 34
    • 0030844077 scopus 로고    scopus 로고
    • Natural release of virulence factors in membrane vesicles by Pseudomonas aeruginosa and the effect of aminoglycoside antibiotics on their release
    • Kadurugamuwa, J. L., and Beveridge, T. J. (1997) Natural release of virulence factors in membrane vesicles by Pseudomonas aeruginosa and the effect of aminoglycoside antibiotics on their release, J. Antimicrob. Chemother. 40, 615-621.
    • (1997) J. Antimicrob. Chemother. , vol.40 , pp. 615-621
    • Kadurugamuwa, J.L.1    Beveridge, T.J.2
  • 35
    • 0032820085 scopus 로고    scopus 로고
    • Membrane vesicles derived from Pseudomonas aeruginosa and Shigella flexneri can be integrated into the surfaces of other gram-negative bacteria
    • Kadurugamuwa, J. L., and Beveridge, T. J. (1999) Membrane vesicles derived from Pseudomonas aeruginosa and Shigella flexneri can be integrated into the surfaces of other gram-negative bacteria, Microbiology 145, 2051-2060.
    • (1999) Microbiology , vol.145 , pp. 2051-2060
    • Kadurugamuwa, J.L.1    Beveridge, T.J.2
  • 36
    • 0031663159 scopus 로고    scopus 로고
    • Gram-negative bacteria produce membrane vesicles which are capable of killing other bacteria
    • Li, Z., Clarke, A. J., and Beveridge, T. J. (1998) Gram-negative bacteria produce membrane vesicles which are capable of killing other bacteria, J. Bacteriol. 180, 5478-5483.
    • (1998) J. Bacteriol. , vol.180 , pp. 5478-5483
    • Li, Z.1    Clarke, A.J.2    Beveridge, T.J.3
  • 37
    • 0031956361 scopus 로고    scopus 로고
    • S-layered Aneurinibacillus and Bacillus spp. are susceptible to the lytic action of Pseudomonas aeruginosa membrane vesicles
    • Kadurugamuwa, J. L., Mayer, A., Messner, P., Sara, M., Sleytr, U. B., and Beveridge, T. J. (1998) S-layered Aneurinibacillus and Bacillus spp. are susceptible to the lytic action of Pseudomonas aeruginosa membrane vesicles, J. Bacteriol. 180, 2306-2311.
    • (1998) J. Bacteriol. , vol.180 , pp. 2306-2311
    • Kadurugamuwa, J.L.1    Mayer, A.2    Messner, P.3    Sara, M.4    Sleytr, U.B.5    Beveridge, T.J.6
  • 38
    • 0034704960 scopus 로고    scopus 로고
    • Role of beta Arg211 in the active site of human beta-hexosamindase B
    • Hou, Y., Vocadlo, D., Withers, S., and Mahuran, D. (2000) Role of beta Arg211 in the active site of human beta-hexosamindase B, Biochemistry 39, 6219-6227.
    • (2000) Biochemistry , vol.39 , pp. 6219-6227
    • Hou, Y.1    Vocadlo, D.2    Withers, S.3    Mahuran, D.4
  • 39
    • 43149095433 scopus 로고    scopus 로고
    • Mechanism of cellobiose inhibition in cellulose hydrolysis by cellobiohydrolase
    • Yue, Z., Bin, W., Baixu, Y., and Peiji, G. (2004) Mechanism of cellobiose inhibition in cellulose hydrolysis by cellobiohydrolase, Sci. China C. Life Sci. 47, 18-24.
    • (2004) Sci. China C. Life Sci. , vol.47 , pp. 18-24
    • Yue, Z.1    Bin, W.2    Baixu, Y.3    Peiji, G.4
  • 40
    • 0344043440 scopus 로고    scopus 로고
    • Quantitative studies of the non-productive binding of lysozyme to partially W-acetylated chitosans. Binding of large ligands to a one-dimensional binary lattice studied by a modified McGhee and von Hippel model
    • Kristiansen, A., Varum, K. M., and Grasdalen, H. (1998) Quantitative studies of the non-productive binding of lysozyme to partially W-acetylated chitosans. Binding of large ligands to a one-dimensional binary lattice studied by a modified McGhee and von Hippel model, Biochim. Biophys. Acta 1425, 137-150.
    • (1998) Biochim. Biophys. Acta , vol.1425 , pp. 137-150
    • Kristiansen, A.1    Varum, K.M.2    Grasdalen, H.3
  • 41
    • 0016836162 scopus 로고
    • Productive and unproductive lysozyme-chitosaccharide complexes. Kinetic investigations
    • Holler, E., Rupley, J. A., and Hess, G. P. (1975) Productive and unproductive lysozyme-chitosaccharide complexes. Kinetic investigations, Biochemistry 14, 2377-2385.
    • (1975) Biochemistry , vol.14 , pp. 2377-2385
    • Holler, E.1    Rupley, J.A.2    Hess, G.P.3
  • 44
    • 0035971079 scopus 로고    scopus 로고
    • Crystallographic evidence for substrate-assisted catalysis in a bacterial β-hexosaminidase
    • Mark, B. L., Vocadlo, D. J., Knapp, S., Triggs-Raine, B. L., Withers, S. G., and James, M. N. (2001) Crystallographic evidence for substrate-assisted catalysis in a bacterial β-hexosaminidase, J. Biol. Chem 276, 10330-10337.
    • (2001) J. Biol. Chem , vol.276 , pp. 10330-10337
    • Mark, B.L.1    Vocadlo, D.J.2    Knapp, S.3    Triggs-Raine, B.L.4    Withers, S.G.5    James, M.N.6
  • 45
    • 0037131312 scopus 로고    scopus 로고
    • Aspartate 313 in the Streptomyces plicatus hexosaminidase plays a critical role in substrate-assisted catalysis by orienting the 2-acetamido group and stabilizing the transition state
    • Williams, S. J., Mark, B. L., Vocadlo, D. J., James, M. N., and Withers, S. G. (2002) Aspartate 313 in the Streptomyces plicatus hexosaminidase plays a critical role in substrate-assisted catalysis by orienting the 2-acetamido group and stabilizing the transition state, J. Biol. Chem. 277, 40055-40065.
    • (2002) J. Biol. Chem. , vol.277 , pp. 40055-40065
    • Williams, S.J.1    Mark, B.L.2    Vocadlo, D.J.3    James, M.N.4    Withers, S.G.5
  • 46
    • 0033609769 scopus 로고    scopus 로고
    • High-resolution crystal structures of the Escherichia coli lytic transglycosylase Slt70 and its complex with a peptidoglycan fragment
    • van Asselt, E. J., Thunnissen, A. M., Dijkstra, B. W. (1999) High-resolution crystal structures of the Escherichia coli lytic transglycosylase Slt70 and its complex with a peptidoglycan fragment, J. Mol. Biol. 291, 877-898.
    • (1999) J. Mol. Biol. , vol.291 , pp. 877-898
    • Van Asselt, E.J.1    Thunnissen, A.M.2    Dijkstra, B.W.3
  • 47
    • 0037131312 scopus 로고    scopus 로고
    • Aspartate 313 in the Streptomyces plicatus beta-hexosaminidase plays a critical role in substrate-assisted catalysis by orienting the 2-acetamido group and stabilizing the transition state
    • Williams, S. J., Mark, B. L., Vocadlo, D. J., James, M. N. G., and Withers, S. G. (2002) Aspartate 313 in the Streptomyces plicatus beta-hexosaminidase plays a critical role in substrate-assisted catalysis by orienting the 2-acetamido group and stabilizing the transition state, J. Biol. Chem. 277, 40055-40065.
    • (2002) J. Biol. Chem. , vol.277 , pp. 40055-40065
    • Williams, S.J.1    Mark, B.L.2    Vocadlo, D.J.3    James, M.N.G.4    Withers, S.G.5
  • 48
    • 0027240681 scopus 로고
    • Characterization of three different lytic transglycosylases from Escherichia coli
    • Romeis, T., Vollmer, W., and Höltje, J.-V. (1993) Characterization of three different lytic transglycosylases from Escherichia coli, FEMS Microbiol. Lett. 111, 141-146.
    • (1993) FEMS Microbiol. Lett. , vol.111 , pp. 141-146
    • Romeis, T.1    Vollmer, W.2    Höltje, J.-V.3


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