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Volumn 1758, Issue 4, 2006, Pages 527-536

Use of a dialyzable short-chain phospholipid for efficient solubilization and reconstitution of influenza virus envelopes

Author keywords

Dialysis; Influenza virus; Reconstitution; Short chain lecithin; Virosome

Indexed keywords

1,2 DICAPROYL SN GLYCERO 3 PHOSPHOCHOLINE; DETERGENT; PHOSPHATIDYLCHOLINE; PHOSPHOLIPID; SOLUBILIZER; SUCROSE; UNCLASSIFIED DRUG; VIROSOME; VIRUS PROTEIN;

EID: 33646820050     PISSN: 00052736     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamem.2006.03.011     Document Type: Article
Times cited : (30)

References (56)
  • 1
    • 0016754576 scopus 로고
    • Formation of virosomes from influenza subunits and liposomes
    • Almeida J.D., Brand C.M., Edwards D.C., and Heath T.D. Formation of virosomes from influenza subunits and liposomes. Lancet 2 (1975) 899-901
    • (1975) Lancet , vol.2 , pp. 899-901
    • Almeida, J.D.1    Brand, C.M.2    Edwards, D.C.3    Heath, T.D.4
  • 2
    • 0027211806 scopus 로고
    • Hemagglutinin-neuraminidase enhances F protein-mediated membrane fusion of reconstituted Sendai virus envelopes with cells
    • Bagai S., Puri A., Blumenthal R., and Sarkar D.P. Hemagglutinin-neuraminidase enhances F protein-mediated membrane fusion of reconstituted Sendai virus envelopes with cells. J. Virol. 67 (1993) 3312-3318
    • (1993) J. Virol. , vol.67 , pp. 3312-3318
    • Bagai, S.1    Puri, A.2    Blumenthal, R.3    Sarkar, D.P.4
  • 3
    • 0018417571 scopus 로고
    • Reconstitution of lipid vesicles associated with HVJ (Sendai virus) spikes. Purification and some properties of vesicles containing nontoxic fragment A of diphtheria toxin
    • Uchida T., Kim J., Yamaizumi M., Miyake Y., and Okada Y. Reconstitution of lipid vesicles associated with HVJ (Sendai virus) spikes. Purification and some properties of vesicles containing nontoxic fragment A of diphtheria toxin. J. Cell Biol. 80 (1979) 10-20
    • (1979) J. Cell Biol. , vol.80 , pp. 10-20
    • Uchida, T.1    Kim, J.2    Yamaizumi, M.3    Miyake, Y.4    Okada, Y.5
  • 5
    • 0019726081 scopus 로고
    • Asymmetric and symmetric membrane reconstitution by detergent elimination. Studies with Semliki-Forest-virus spike glycoprotein and penicillinase from the membrane of Bacillus licheniformis
    • Helenius A., Sarvas M., and Simons K. Asymmetric and symmetric membrane reconstitution by detergent elimination. Studies with Semliki-Forest-virus spike glycoprotein and penicillinase from the membrane of Bacillus licheniformis. Eur. J. Biochem. 116 (1981) 27-35
    • (1981) Eur. J. Biochem. , vol.116 , pp. 27-35
    • Helenius, A.1    Sarvas, M.2    Simons, K.3
  • 6
    • 0017658904 scopus 로고
    • Reconstitution of Semliki Forest virus membrane
    • Helenius A., Fries E., and Kartenbeck J. Reconstitution of Semliki Forest virus membrane. J Cell Biol. 75 (1977) 866-880
    • (1977) J Cell Biol. , vol.75 , pp. 866-880
    • Helenius, A.1    Fries, E.2    Kartenbeck, J.3
  • 7
    • 0023054125 scopus 로고
    • Reconstitution of the fusogenic activity of vesicular stomatitis virus
    • Metsikkö K., van Meer G., and Simons K. Reconstitution of the fusogenic activity of vesicular stomatitis virus. EMBO J. 5 (1986) 3429-3435
    • (1986) EMBO J. , vol.5 , pp. 3429-3435
    • Metsikkö, K.1    van Meer, G.2    Simons, K.3
  • 8
    • 0018333291 scopus 로고
    • Reconstitution into liposomes of the glycoprotein of vesicular stomatitis virus by detergent dialysis
    • Petri Jr. W.A., and Wagner R.R. Reconstitution into liposomes of the glycoprotein of vesicular stomatitis virus by detergent dialysis. J. Biol. Chem. 254 (1979) 4313-4316
    • (1979) J. Biol. Chem. , vol.254 , pp. 4313-4316
    • Petri Jr., W.A.1    Wagner, R.R.2
  • 9
    • 0023058916 scopus 로고
    • Novel preparation of functional Sindbis virosomes
    • Scheule R.K. Novel preparation of functional Sindbis virosomes. Biochemistry 25 (1986) 4223-4232
    • (1986) Biochemistry , vol.25 , pp. 4223-4232
    • Scheule, R.K.1
  • 10
  • 11
    • 0037435832 scopus 로고    scopus 로고
    • Influenza virosomes: combining optimal presentation of hemagglutinin with immunopotentiating activity
    • Huckriede A., Bungener L., ter Veer W., Holtrop M., Daemen T., Palache A.M., and Wilschut J. Influenza virosomes: combining optimal presentation of hemagglutinin with immunopotentiating activity. Vaccine 21 (2003) 925-931
    • (2003) Vaccine , vol.21 , pp. 925-931
    • Huckriede, A.1    Bungener, L.2    ter Veer, W.3    Holtrop, M.4    Daemen, T.5    Palache, A.M.6    Wilschut, J.7
  • 14
    • 0034734990 scopus 로고    scopus 로고
    • Virosomes: evolution of the liposome as a targeted drug delivery system
    • Kaneda Y. Virosomes: evolution of the liposome as a targeted drug delivery system. Adv. Drug Delivery Rev. 43 (2000) 197-205
    • (2000) Adv. Drug Delivery Rev. , vol.43 , pp. 197-205
    • Kaneda, Y.1
  • 16
    • 9244234954 scopus 로고    scopus 로고
    • Liposomes and virosomes as delivery systems for antigens, nucleic acids and drugs
    • Felnerova D., Viret J.F., Glück R., and Moser C. Liposomes and virosomes as delivery systems for antigens, nucleic acids and drugs. Curr. Opin. Biotechnol. 15 (2004) 518-529
    • (2004) Curr. Opin. Biotechnol. , vol.15 , pp. 518-529
    • Felnerova, D.1    Viret, J.F.2    Glück, R.3    Moser, C.4
  • 17
    • 0037811025 scopus 로고    scopus 로고
    • Early steps of the conformational change of influenza virus hemagglutinin to a fusion active state-Stability and energetics of the hemagglutinin
    • Huang Q. Early steps of the conformational change of influenza virus hemagglutinin to a fusion active state-Stability and energetics of the hemagglutinin. Biochim. Biophys. Acta, Biomembr. 1614 (2003) 3-13
    • (2003) Biochim. Biophys. Acta, Biomembr. , vol.1614 , pp. 3-13
    • Huang, Q.1
  • 18
    • 0037381269 scopus 로고    scopus 로고
    • The structural biology of type I viral membrane fusion
    • Colman P.M., and Lawrence M.C. The structural biology of type I viral membrane fusion. Nat. Rev., Mol. Cell Biol. 4 (2003) 309-319
    • (2003) Nat. Rev., Mol. Cell Biol. , vol.4 , pp. 309-319
    • Colman, P.M.1    Lawrence, M.C.2
  • 20
    • 1642540252 scopus 로고    scopus 로고
    • Virology-A class act
    • Jardetzky T.S., and Lamb R.A. Virology-A class act. Nature 427 (2004) 307-308
    • (2004) Nature , vol.427 , pp. 307-308
    • Jardetzky, T.S.1    Lamb, R.A.2
  • 21
    • 1842534392 scopus 로고    scopus 로고
    • How viruses enter animal cells
    • Smith A.E., and Helenius A. How viruses enter animal cells. Science 304 (2004) 237-242
    • (2004) Science , vol.304 , pp. 237-242
    • Smith, A.E.1    Helenius, A.2
  • 23
    • 0027138269 scopus 로고
    • Delivery of foreign substances to cells mediated by fusion-active reconstituted influenza virus envelopes (virosomes)
    • Schoen P., Bron R., and Wilschut J. Delivery of foreign substances to cells mediated by fusion-active reconstituted influenza virus envelopes (virosomes). J. Liposome Res. 3 (1993) 767-792
    • (1993) J. Liposome Res. , vol.3 , pp. 767-792
    • Schoen, P.1    Bron, R.2    Wilschut, J.3
  • 24
    • 0028085720 scopus 로고
    • Cellular cytoplasmic delivery of a polypeptide toxin by reconstituted influenza-virus envelopes (virosomes)
    • Bron R., Ortiz A., and Wilschut J. Cellular cytoplasmic delivery of a polypeptide toxin by reconstituted influenza-virus envelopes (virosomes). Biochemistry 33 (1994) 9110-9117
    • (1994) Biochemistry , vol.33 , pp. 9110-9117
    • Bron, R.1    Ortiz, A.2    Wilschut, J.3
  • 26
    • 0033011921 scopus 로고    scopus 로고
    • Gene transfer mediated by fusion protein hemagglutinin reconstituted in cationic lipid vesicles
    • Schoen P., Chonn A., Cullis P.R., Wilschut J., and Scherrer P. Gene transfer mediated by fusion protein hemagglutinin reconstituted in cationic lipid vesicles. Gene Ther. 6 (1999) 823-832
    • (1999) Gene Ther. , vol.6 , pp. 823-832
    • Schoen, P.1    Chonn, A.2    Cullis, P.R.3    Wilschut, J.4    Scherrer, P.5
  • 27
    • 33645155231 scopus 로고    scopus 로고
    • Reconstituted influenza virus envelopes as an efficient carrier system for cellular delivery of small-interfering RNAs
    • de Jonge J., Holtrop M., Wilschut J., and Huckriede A. Reconstituted influenza virus envelopes as an efficient carrier system for cellular delivery of small-interfering RNAs. Gene Ther. 13 (2006) 400-411
    • (2006) Gene Ther. , vol.13 , pp. 400-411
    • de Jonge, J.1    Holtrop, M.2    Wilschut, J.3    Huckriede, A.4
  • 28
    • 0033959835 scopus 로고    scopus 로고
    • Induction of cytotoxic T lymphocyte activity by fusion-active peptide-containing virosomes
    • Arkema A., Huckriede A., Schoen P., Wilschut J., and Daemen T. Induction of cytotoxic T lymphocyte activity by fusion-active peptide-containing virosomes. Vaccine 18 (2000) 1327-1333
    • (2000) Vaccine , vol.18 , pp. 1327-1333
    • Arkema, A.1    Huckriede, A.2    Schoen, P.3    Wilschut, J.4    Daemen, T.5
  • 29
    • 12344265748 scopus 로고    scopus 로고
    • Virosome-mediated delivery of protein antigens in vivo: efficient induction of class I MHC-restricted cytotoxic T lymphocyte activity
    • Bungener L., Huckriede A., de Mare A., de Vries-Idema J., Wilschut J., and Daemen T. Virosome-mediated delivery of protein antigens in vivo: efficient induction of class I MHC-restricted cytotoxic T lymphocyte activity. Vaccine 23 (2005) 1232-1241
    • (2005) Vaccine , vol.23 , pp. 1232-1241
    • Bungener, L.1    Huckriede, A.2    de Mare, A.3    de Vries-Idema, J.4    Wilschut, J.5    Daemen, T.6
  • 30
    • 0015991171 scopus 로고
    • Physical chemical studies of short-chain lecithin homologues: I. Influence of the chain length of the fatty acid ester and of electrolytes on the critical micelle concentration
    • Tausk R.J., Karmiggelt J., Oudshoorn C., and Overbeek J.T. Physical chemical studies of short-chain lecithin homologues: I. Influence of the chain length of the fatty acid ester and of electrolytes on the critical micelle concentration. Biophys. Chem. 1 (1974) 175-183
    • (1974) Biophys. Chem. , vol.1 , pp. 175-183
    • Tausk, R.J.1    Karmiggelt, J.2    Oudshoorn, C.3    Overbeek, J.T.4
  • 31
    • 0034707098 scopus 로고    scopus 로고
    • Short-chain phospholipids as detergents
    • Hauser H. Short-chain phospholipids as detergents. Biochim. Biophys. Acta, Biomembr. 1508 (2000) 164-181
    • (2000) Biochim. Biophys. Acta, Biomembr. , vol.1508 , pp. 164-181
    • Hauser, H.1
  • 32
    • 0021772460 scopus 로고
    • Spontaneous formation of stable unilamellar vesicles
    • Gabriel N.E., and Roberts M.F. Spontaneous formation of stable unilamellar vesicles. Biochemistry 23 (1984) 4011-4015
    • (1984) Biochemistry , vol.23 , pp. 4011-4015
    • Gabriel, N.E.1    Roberts, M.F.2
  • 33
    • 0028068353 scopus 로고
    • Short-chain phosphatidylcholines as superior detergents in solubilizing membrane proteins and preserving biological activity
    • Kessi J., Poiree J.C., Wehrli E., Bachofen R., Semenza G., and Hauser H. Short-chain phosphatidylcholines as superior detergents in solubilizing membrane proteins and preserving biological activity. Biochemistry 33 (1994) 10825-10836
    • (1994) Biochemistry , vol.33 , pp. 10825-10836
    • Kessi, J.1    Poiree, J.C.2    Wehrli, E.3    Bachofen, R.4    Semenza, G.5    Hauser, H.6
  • 34
    • 0030853496 scopus 로고    scopus 로고
    • Preservation of the native structure and function of Ca2+-ATPase from sarcoplasmic reticulum: solubilization and reconstitution by new short-chain phospholipid detergent 1,2-diheptanoyl-sn-phosphatidylcholine
    • Shivanna B.D., and Rowe E.S. Preservation of the native structure and function of Ca2+-ATPase from sarcoplasmic reticulum: solubilization and reconstitution by new short-chain phospholipid detergent 1,2-diheptanoyl-sn-phosphatidylcholine. Biochem. J. 325 (1997) 533-542
    • (1997) Biochem. J. , vol.325 , pp. 533-542
    • Shivanna, B.D.1    Rowe, E.S.2
  • 35
    • 0030868339 scopus 로고    scopus 로고
    • Reconstitution and further characterization of the cholesterol transport activity of the small-intestinal brush border membrane
    • Boffelli D., Weber F.E., Compassi S., Werder M., Schulthess G., and Hauser H. Reconstitution and further characterization of the cholesterol transport activity of the small-intestinal brush border membrane. Biochemistry 36 (1997) 10784-10792
    • (1997) Biochemistry , vol.36 , pp. 10784-10792
    • Boffelli, D.1    Weber, F.E.2    Compassi, S.3    Werder, M.4    Schulthess, G.5    Hauser, H.6
  • 36
    • 0023046596 scopus 로고
    • Spontaneous transmembrane insertion of membrane-proteins into lipid vesicles facilitated by short-chain lecithins
    • Dencher N.A. Spontaneous transmembrane insertion of membrane-proteins into lipid vesicles facilitated by short-chain lecithins. Biochemistry 25 (1986) 1195-1200
    • (1986) Biochemistry , vol.25 , pp. 1195-1200
    • Dencher, N.A.1
  • 37
    • 0017613512 scopus 로고
    • A simplification of the protein assay method of Lowry et al. which is more generally applicable
    • Peterson G.L. A simplification of the protein assay method of Lowry et al. which is more generally applicable. Anal. Biochem. 83 (1977) 346-356
    • (1977) Anal. Biochem. , vol.83 , pp. 346-356
    • Peterson, G.L.1
  • 38
    • 50549164858 scopus 로고
    • A rapid and sensitive sub-micro phosphorus determination
    • Böttcher C.J.F., van Gent C.M., and Pries C. A rapid and sensitive sub-micro phosphorus determination. Anal. Chim. Acta 24 (1961) 203-204
    • (1961) Anal. Chim. Acta , vol.24 , pp. 203-204
    • Böttcher, C.J.F.1    van Gent, C.M.2    Pries, C.3
  • 39
    • 33845261493 scopus 로고
    • A rapid method of total lipid extraction and purification
    • Bligh E.G., and Dyer W.J. A rapid method of total lipid extraction and purification. Can. J. Biochem. Physiol. 37 (1959) 911-917
    • (1959) Can. J. Biochem. Physiol. , vol.37 , pp. 911-917
    • Bligh, E.G.1    Dyer, W.J.2
  • 40
    • 51249189913 scopus 로고
    • Phospholipid reactivation of plasmalogen metabolism
    • Ellingson J.S., and Lands W.E.M. Phospholipid reactivation of plasmalogen metabolism. Lipids 3 (1968) 111-120
    • (1968) Lipids , vol.3 , pp. 111-120
    • Ellingson, J.S.1    Lands, W.E.M.2
  • 41
    • 0027434098 scopus 로고
    • Evaluation of viral membrane-fusion assays-Comparison of the octadecylrhodamine dequenching assay with the pyrene excimer assay
    • Stegmann T., Schoen P., Bron R., Wey J., Bartoldus I., Ortiz A., Nieva J.L., and Wilschut J. Evaluation of viral membrane-fusion assays-Comparison of the octadecylrhodamine dequenching assay with the pyrene excimer assay. Biochemistry 32 (1993) 11330-11337
    • (1993) Biochemistry , vol.32 , pp. 11330-11337
    • Stegmann, T.1    Schoen, P.2    Bron, R.3    Wey, J.4    Bartoldus, I.5    Ortiz, A.6    Nieva, J.L.7    Wilschut, J.8
  • 42
    • 0001178029 scopus 로고    scopus 로고
    • Orthomyxoviridae
    • Knipe D.M., and Howley P.N. (Eds), Lippincott Williams and Wilkins, Philadelphia
    • Lamb R.A., and Krug R.M. Orthomyxoviridae. In: Knipe D.M., and Howley P.N. (Eds). Fields Virology. 4th ed. (2001), Lippincott Williams and Wilkins, Philadelphia 1487-1531
    • (2001) Fields Virology. 4th ed. , pp. 1487-1531
    • Lamb, R.A.1    Krug, R.M.2
  • 44
    • 0027474746 scopus 로고
    • Principles of selective inactivation of viral genome: VIII. The influence of beta-propiolactone on immunogenic and protective activities of influenza virus
    • Budowsky E.I., Smirnov Y., and Shenderovich S.F. Principles of selective inactivation of viral genome: VIII. The influence of beta-propiolactone on immunogenic and protective activities of influenza virus. Vaccine 11 (1993) 343-348
    • (1993) Vaccine , vol.11 , pp. 343-348
    • Budowsky, E.I.1    Smirnov, Y.2    Shenderovich, S.F.3
  • 45
    • 0037224723 scopus 로고    scopus 로고
    • Virus inactivation in the 1990s-And into the 21st century. part 4, culture media, biotechnology products, and vaccines
    • Sofer G. Virus inactivation in the 1990s-And into the 21st century. part 4, culture media, biotechnology products, and vaccines. Biopharm Int. 16 (2003) 50-57
    • (2003) Biopharm Int. , vol.16 , pp. 50-57
    • Sofer, G.1
  • 46
    • 0030938886 scopus 로고    scopus 로고
    • Solubilization and reconstitution of vesicular stomatitis virus envelope using octylglucoside
    • Paternostre M., Viard M., Meyer O., Ghanam M., Ollivon M., and Blumenthal R. Solubilization and reconstitution of vesicular stomatitis virus envelope using octylglucoside. Biophys. J 72 (1997) 1683-1694
    • (1997) Biophys. J , vol.72 , pp. 1683-1694
    • Paternostre, M.1    Viard, M.2    Meyer, O.3    Ghanam, M.4    Ollivon, M.5    Blumenthal, R.6
  • 47
    • 0023029847 scopus 로고
    • Preparation of liposomes via detergent removal from mixed micelles by dilution. The effect of bilayer composition and process parameters on liposome characteristics
    • Jiskoot W., Teerlink T., Beuvery E.C., and Crommelin D.J. Preparation of liposomes via detergent removal from mixed micelles by dilution. The effect of bilayer composition and process parameters on liposome characteristics. Pharm. Weekbl. Sci. 8 (1986) 259-265
    • (1986) Pharm. Weekbl. Sci. , vol.8 , pp. 259-265
    • Jiskoot, W.1    Teerlink, T.2    Beuvery, E.C.3    Crommelin, D.J.4
  • 48
    • 0019875103 scopus 로고
    • Liposomes of controllable size in the range of 40 to 180 nm by defined dialysis of lipid/detergent mixed micelles
    • Zumbuehl O., and Weder H.G. Liposomes of controllable size in the range of 40 to 180 nm by defined dialysis of lipid/detergent mixed micelles. Biochim. Biophys. Acta 640 (1981) 252-262
    • (1981) Biochim. Biophys. Acta , vol.640 , pp. 252-262
    • Zumbuehl, O.1    Weder, H.G.2
  • 49
    • 0027769485 scopus 로고
    • Reconstitution of non-ionic monoalkyl amphiphile-cholesterol vesicles by dilution of lipids-octylglucoside mixed micelles
    • Seras M., Ollivon M., Edwards K., and Lesieur S. Reconstitution of non-ionic monoalkyl amphiphile-cholesterol vesicles by dilution of lipids-octylglucoside mixed micelles. Chem. Phys. Lipids 66 (1993) 93-109
    • (1993) Chem. Phys. Lipids , vol.66 , pp. 93-109
    • Seras, M.1    Ollivon, M.2    Edwards, K.3    Lesieur, S.4
  • 50
    • 0041859576 scopus 로고    scopus 로고
    • Kinetics of the micelle-to-vesicle transition: aqueous lecithin-bile salt mixtures
    • Leng J., Egelhaaf S.U., and Cates M.E. Kinetics of the micelle-to-vesicle transition: aqueous lecithin-bile salt mixtures. Biophys. J. 85 (2003) 1624-1646
    • (2003) Biophys. J. , vol.85 , pp. 1624-1646
    • Leng, J.1    Egelhaaf, S.U.2    Cates, M.E.3
  • 51
    • 0024281314 scopus 로고
    • Micelle vesicle transition of egg phosphatidylcholine and octyl glucoside
    • Ollivon M., Eidelman O., Blumenthal R., and Walter A. Micelle vesicle transition of egg phosphatidylcholine and octyl glucoside. Biochemistry 27 (1988) 1695-1703
    • (1988) Biochemistry , vol.27 , pp. 1695-1703
    • Ollivon, M.1    Eidelman, O.2    Blumenthal, R.3    Walter, A.4
  • 52
    • 0024289274 scopus 로고
    • The mechanism of vesicle formation
    • Lasic D.D. The mechanism of vesicle formation. Biochem. J. 256 (1988) 1-11
    • (1988) Biochem. J. , vol.256 , pp. 1-11
    • Lasic, D.D.1
  • 53
    • 0023656052 scopus 로고
    • Dynamics of proteoliposome formation. Intermediate states during detergent dialysis
    • Wrigglesworth J.M., Wooster M.S., Elsden J., and Danneel H.J. Dynamics of proteoliposome formation. Intermediate states during detergent dialysis. Biochem. J. 246 (1987) 737-744
    • (1987) Biochem. J. , vol.246 , pp. 737-744
    • Wrigglesworth, J.M.1    Wooster, M.S.2    Elsden, J.3    Danneel, H.J.4
  • 54
    • 0029101114 scopus 로고
    • Reconstitution of membrane proteins into liposomes: application to energy-transducing membrane proteins
    • Rigaud J.L., Pitard B., and Levy D. Reconstitution of membrane proteins into liposomes: application to energy-transducing membrane proteins. Biochim. Biophys. Acta 1231 (1995) 223-246
    • (1995) Biochim. Biophys. Acta , vol.1231 , pp. 223-246
    • Rigaud, J.L.1    Pitard, B.2    Levy, D.3
  • 55
    • 0018121353 scopus 로고
    • The preparation of large single bilayer liposomes by a fast and controlled dialysis
    • Milsmann M.H., Schwendener R.A., and Weder H.G. The preparation of large single bilayer liposomes by a fast and controlled dialysis. Biochim. Biophys. Acta 512 (1978) 147-155
    • (1978) Biochim. Biophys. Acta , vol.512 , pp. 147-155
    • Milsmann, M.H.1    Schwendener, R.A.2    Weder, H.G.3
  • 56
    • 0242355297 scopus 로고    scopus 로고
    • Cross-flow filtration-An improved detergent removal technique for the preparation of liposomes
    • Peschka R., Purmann T., and Schubert R. Cross-flow filtration-An improved detergent removal technique for the preparation of liposomes. Int. J. Pharm. 162 (1998) 177-183
    • (1998) Int. J. Pharm. , vol.162 , pp. 177-183
    • Peschka, R.1    Purmann, T.2    Schubert, R.3


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