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Volumn 93, Issue 1, 2006, Pages 159-168

Post-translational regulation of expression and conformation of an immunoglobulin domain in yeast surface display

Author keywords

CD47; Disulfide; Glycosylation; Immunoglobulin; Yeast display

Indexed keywords

ANTIBODIES; CELL MEMBRANES; CONFORMATIONS; GENES; IMMUNOLOGY; MUTAGENESIS; YEAST;

EID: 30944435410     PISSN: 00063592     EISSN: 10970290     Source Type: Journal    
DOI: 10.1002/bit.20684     Document Type: Article
Times cited : (24)

References (50)
  • 1
    • 0028946717 scopus 로고
    • Intracellular folding of tissue-type plasminogen activator. Effects of disulfide bond formation on N-linked glycosylation and secretion
    • Allen S, Naim HY, Bulleid NJ. 1995. Intracellular folding of tissue-type plasminogen activator. Effects of disulfide bond formation on N-linked glycosylation and secretion. J Biol Chem 270:4797-4804.
    • (1995) J Biol Chem , vol.270 , pp. 4797-4804
    • Allen, S.1    Naim, H.Y.2    Bulleid, N.J.3
  • 2
    • 0032486771 scopus 로고    scopus 로고
    • Leader peptide efficiency correlates with signal recognition particle dependence in Saccharomyces cerevisiae
    • Arnold CE, Parekh RN, Yang W, Wittrup KD. 1998. Leader peptide efficiency correlates with signal recognition particle dependence in Saccharomyces cerevisiae. Biotechnol Bioeng 59:286-293.
    • (1998) Biotechnol Bioeng , vol.59 , pp. 286-293
    • Arnold, C.E.1    Parekh, R.N.2    Yang, W.3    Wittrup, K.D.4
  • 3
    • 0030994634 scopus 로고    scopus 로고
    • Yeast surface display for screening combinatorial polypeptide libraries
    • Boder ET, Wittrup KD. 1997. Yeast surface display for screening combinatorial polypeptide libraries. Nature Biotechnol 15:553-557.
    • (1997) Nature Biotechnol , vol.15 , pp. 553-557
    • Boder, E.T.1    Wittrup, K.D.2
  • 4
    • 0033748716 scopus 로고    scopus 로고
    • Yeast surface display for directed evolution of protein expression, affinity, and stability
    • Boder ET, Wittrup KD. 2000. Yeast surface display for directed evolution of protein expression, affinity, and stability. Methods Enzymol 328:430-444.
    • (2000) Methods Enzymol , vol.328 , pp. 430-444
    • Boder, E.T.1    Wittrup, K.D.2
  • 6
    • 0025816663 scopus 로고
    • Folding of influenza hemagglutinin in the endoplasmic reticulum
    • Braakman I, Hoover-Litty H, Wagner KR, Helenius A. 1991. Folding of influenza hemagglutinin in the endoplasmic reticulum. J Cell Biol 114: 401-411.
    • (1991) J Cell Biol , vol.114 , pp. 401-411
    • Braakman, I.1    Hoover-Litty, H.2    Wagner, K.R.3    Helenius, A.4
  • 7
    • 0035280238 scopus 로고    scopus 로고
    • Integrin-associated protein (CD47) and its ligands
    • Brown EJ, Frazier WA. 2001. Integrin-associated protein (CD47) and its ligands. Trends Cell Biol 11:130-135.
    • (2001) Trends Cell Biol , vol.11 , pp. 130-135
    • Brown, E.J.1    Frazier, W.A.2
  • 8
    • 0141533196 scopus 로고    scopus 로고
    • Co-expression of molecular chaperones does not improve the heterologous expression of mammalian G-protein coupled receptor expression in yeast
    • Butz J, Niebauer RT, Robinson AS. 2003. Co-expression of molecular chaperones does not improve the heterologous expression of mammalian G-protein coupled receptor expression in yeast. Biotechnol Bioeng 84:292-304.
    • (2003) Biotechnol Bioeng , vol.84 , pp. 292-304
    • Butz, J.1    Niebauer, R.T.2    Robinson, A.S.3
  • 9
    • 0026669346 scopus 로고
    • An ovarian tumor marker with homology to vaccinia virus contains an IgV-like region and multiple transmembrane domains
    • Campbell IG, Freemont PS, Foulkes W, Trowsdale J. 1992. An ovarian tumor marker with homology to vaccinia virus contains an IgV-like region and multiple transmembrane domains. Cancer Res 52:5416-5420.
    • (1992) Cancer Res , vol.52 , pp. 5416-5420
    • Campbell, I.G.1    Freemont, P.S.2    Foulkes, W.3    Trowsdale, J.4
  • 10
    • 0025996402 scopus 로고
    • Saccharomyces cerevisiae a- and α-agglutinin: Characterization of their molecular interaction
    • Capellaro C, Hauser K, Mrsa V, Watzele M, Watzele G, Gruber C, Tanner W. 1991. Saccharomyces cerevisiae a- and α-agglutinin: Characterization of their molecular interaction. EMBO J 10:4081-4088.
    • (1991) EMBO J , vol.10 , pp. 4081-4088
    • Capellaro, C.1    Hauser, K.2    Mrsa, V.3    Watzele, M.4    Watzele, G.5    Gruber, C.6    Tanner, W.7
  • 11
    • 1942520362 scopus 로고    scopus 로고
    • Domain-level antibody epitope mapping through yeast surface display of epidermal growth factor receptor fragments
    • Cochran JR, Kim YS, Olsen MJ, Bhandari R, Wittrup KD. 2004. Domain-level antibody epitope mapping through yeast surface display of epidermal growth factor receptor fragments. J Immunol Methods 287:147-158.
    • (2004) J Immunol Methods , vol.287 , pp. 147-158
    • Cochran, J.R.1    Kim, Y.S.2    Olsen, M.J.3    Bhandari, R.4    Wittrup, K.D.5
  • 12
    • 6344284868 scopus 로고    scopus 로고
    • Search for hyperglycosylation signals in yeast glycoproteins
    • Conde R, Cueva R, Pablo G, Polaina J, Larriba GA. 2004. Search for hyperglycosylation signals in yeast glycoproteins. J Biol Chem 279: 43789-43798.
    • (2004) J Biol Chem , vol.279 , pp. 43789-43798
    • Conde, R.1    Cueva, R.2    Pablo, G.3    Polaina, J.4    Larriba, G.A.5
  • 13
    • 0023597393 scopus 로고
    • The relationship of N-linked glycosylation and heavy chain-binding protein association with the secretion of glycoproteins
    • Dorner AJ, Bole DG, Kaufman RJ. 1987. The relationship of N-linked glycosylation and heavy chain-binding protein association with the secretion of glycoproteins. J Cell Biol 105:2665-2674.
    • (1987) J Cell Biol , vol.105 , pp. 2665-2674
    • Dorner, A.J.1    Bole, D.G.2    Kaufman, R.J.3
  • 14
    • 2942530683 scopus 로고    scopus 로고
    • Directed evolution of soluble single-chain human class II MHC molecules
    • Esteban O, Zhao H. 2004. Directed evolution of soluble single-chain human class II MHC molecules. J Mol Biol 340:81-95.
    • (2004) J Mol Biol , vol.340 , pp. 81-95
    • Esteban, O.1    Zhao, H.2
  • 15
    • 1842857805 scopus 로고    scopus 로고
    • Flow cytometric screening of yeast surface display libraries
    • Feldhaus M, Siegel R. 2004. Flow cytometric screening of yeast surface display libraries. Methods Mol Biol 263:311-332.
    • (2004) Methods Mol Biol , vol.263 , pp. 311-332
    • Feldhaus, M.1    Siegel, R.2
  • 16
    • 0029040839 scopus 로고
    • The asparagine-linked oligosaccharides of the human chorionic gonadotropin beta subunit facilitate correct disulfide bond pairing
    • Feng W, Matzuk MM, Mountjoy K, Bedows E, Ruddon RW, Boime I. 1995. The asparagine-linked oligosaccharides of the human chorionic gonadotropin beta subunit facilitate correct disulfide bond pairing. J Biol Chem 270:11851-11859.
    • (1995) J Biol Chem , vol.270 , pp. 11851-11859
    • Feng, W.1    Matzuk, M.M.2    Mountjoy, K.3    Bedows, E.4    Ruddon, R.W.5    Boime, I.6
  • 17
    • 0025367812 scopus 로고
    • Sequence differences between glycosylated and non-glycosylated Asn-X-Thr/Ser acceptor sites: Implications for protein engineering
    • Gavel Y, von Heijne G. 1990. Sequence differences between glycosylated and non-glycosylated Asn-X-Thr/Ser acceptor sites: Implications for protein engineering. Protein Eng 3:433-442.
    • (1990) Protein Eng , vol.3 , pp. 433-442
    • Gavel, Y.1    Von Heijne, G.2
  • 18
    • 8344271025 scopus 로고    scopus 로고
    • Advances in the production of human therapeutic proteins in yeasts and filamentous fungi
    • Gerngross TU. 2004. Advances in the production of human therapeutic proteins in yeasts and filamentous fungi. Nat Biotechnol 22:1409-1414.
    • (2004) Nat Biotechnol , vol.22 , pp. 1409-1414
    • Gerngross, T.U.1
  • 19
    • 0036270543 scopus 로고    scopus 로고
    • Transformation of yeast by the LiAc/ss carrier DNA/PEG method
    • Gietz RD, Woods RA. 2002. Transformation of yeast by the LiAc/ss carrier DNA/PEG method. Meth Enzymol 350:87-96.
    • (2002) Meth Enzymol , vol.350 , pp. 87-96
    • Gietz, R.D.1    Woods, R.A.2
  • 21
    • 0029953675 scopus 로고    scopus 로고
    • Competition between folding and glycosylation in the endoplasmic reticulum
    • Holst B, Bruun AW, Kielland-Brandt MC, Winther JR. 1996. Competition between folding and glycosylation in the endoplasmic reticulum. EMBO J 15:3538-3546.
    • (1996) EMBO J , vol.15 , pp. 3538-3546
    • Holst, B.1    Bruun, A.W.2    Kielland-Brandt, M.C.3    Winther, J.R.4
  • 22
    • 16344379251 scopus 로고    scopus 로고
    • Secretion and surface display of green fluorescent protein using the yeats Saccharomyces cerevisiae
    • Huang D, Shusta EV. 2005. Secretion and surface display of green fluorescent protein using the yeats Saccharomyces cerevisiae. Biotechnol Prog 21:349-357.
    • (2005) Biotechnol Prog , vol.21 , pp. 349-357
    • Huang, D.1    Shusta, E.V.2
  • 23
    • 0028260121 scopus 로고
    • Selective retention of secretory proteins in the yeast endoplasmic reticulum by treatment of cells with a reducing agent
    • Jamsa E, Simonen M, Makarow M. 1994. Selective retention of secretory proteins in the yeast endoplasmic reticulum by treatment of cells with a reducing agent. Yeast 10:355-370.
    • (1994) Yeast , vol.10 , pp. 355-370
    • Jamsa, E.1    Simonen, M.2    Makarow, M.3
  • 24
    • 0029041308 scopus 로고
    • The hydroxy amino acid in an Asn-X-Ser/Thr sequon can influence N-linked core glycosylation efficiency and the level of expression of a cell surface glycoprotein
    • Kasturi L, Eshleman JR, Wunner WH, Shakin-Eshleman SH. 1995. The hydroxy amino acid in an Asn-X-Ser/Thr sequon can influence N-linked core glycosylation efficiency and the level of expression of a cell surface glycoprotein. J Biol Chem 270:14756-14761.
    • (1995) J Biol Chem , vol.270 , pp. 14756-14761
    • Kasturi, L.1    Eshleman, J.R.2    Wunner, W.H.3    Shakin-Eshleman, S.H.4
  • 26
    • 0032584722 scopus 로고    scopus 로고
    • Protein folding stability can determine the efficiency of escape from endoplasmic reticulum quality control
    • Kowalski JM, Parekh RN, Mao J, Wittrup KD. 1998. Protein folding stability can determine the efficiency of escape from endoplasmic reticulum quality control. J Biol Chem 273:19453-19458.
    • (1998) J Biol Chem , vol.273 , pp. 19453-19458
    • Kowalski, J.M.1    Parekh, R.N.2    Mao, J.3    Wittrup, K.D.4
  • 27
    • 0030996965 scopus 로고    scopus 로고
    • Designing out disulfide bonds: Thermodynamic properties of 30-51 cystine substitution mutants of bovine pancreatic trypsin inhibitor
    • Liu Y, Breslauer K, Anderson S. 1997. Designing out disulfide bonds: Thermodynamic properties of 30-51 cystine substitution mutants of bovine pancreatic trypsin inhibitor. Biochemistry 36:5323-5335.
    • (1997) Biochemistry , vol.36 , pp. 5323-5335
    • Liu, Y.1    Breslauer, K.2    Anderson, S.3
  • 28
    • 0033485642 scopus 로고    scopus 로고
    • Human signal-regulatory protein is expressed on normal, but not on subsets of leukemic myeloid cells and mediates cellular adhesion involving its counterreceptor CD47
    • Martina Seiffert, Charles Cant, Zhengjun Chen, Irene Rappold, Wolfram Brugger, Lothar Kanz, Eric J Brown, Axel Ullrich, Hans-Jörg Bühring. 1999. Human signal-regulatory protein is expressed on normal, but not on subsets of leukemic myeloid cells and mediates cellular adhesion involving its counterreceptor CD47. Blood 94:3633-3643.
    • (1999) Blood , vol.94 , pp. 3633-3643
    • Seiffert, M.1    Cant, C.2    Chen, Z.3    Rappold, I.4    Brugger, W.5    Kanz, L.6    Brown, E.J.7    Ullrich, A.8    Bühring, H.-J.9
  • 29
    • 0037108440 scopus 로고    scopus 로고
    • Mechanisms of CD47-induced caspase-independent cell death in normal and leukemic cells: Link between phosphatidylserine exposure and cytoskeleton organization
    • Mateo V, Brown EJ, Biron G, Rubio M, Fischer A, Deist FL, Sarfati M. 2002. Mechanisms of CD47-induced caspase-independent cell death in normal and leukemic cells: Link between phosphatidylserine exposure and cytoskeleton organization. Blood 100:2882-2890.
    • (2002) Blood , vol.100 , pp. 2882-2890
    • Mateo, V.1    Brown, E.J.2    Biron, G.3    Rubio, M.4    Fischer, A.5    Deist, F.L.6    Sarfati, M.7
  • 30
    • 0028063239 scopus 로고
    • Isolation and characterization of CD47 glycoprotein: A multispanning membrane protein which is the same as integrin-associated protein (IAP) and the ovarian tumour marker OA3
    • Mawby WJ, Holmes CH, Anstee DJ, Spring FA, Tanner MJ. 1994. Isolation and characterization of CD47 glycoprotein: A multispanning membrane protein which is the same as integrin-associated protein (IAP) and the ovarian tumour marker OA3. Biochem J 304:525-530.
    • (1994) Biochem J , vol.304 , pp. 525-530
    • Mawby, W.J.1    Holmes, C.H.2    Anstee, D.J.3    Spring, F.A.4    Tanner, M.J.5
  • 31
    • 0032510739 scopus 로고    scopus 로고
    • The amino acid following an asn-X-Ser/Thr sequon is an important determinant of N-linked core glycosylation efficiency
    • Mellquist JL, Kasturi L, Spitalnik SL, Shakin-Eshleman SH. 1998. The amino acid following an asn-X-Ser/Thr sequon is an important determinant of N-linked core glycosylation efficiency. Biochemistry 37:6833-6837.
    • (1998) Biochemistry , vol.37 , pp. 6833-6837
    • Mellquist, J.L.1    Kasturi, L.2    Spitalnik, S.L.3    Shakin-Eshleman, S.H.4
  • 32
    • 0141681120 scopus 로고    scopus 로고
    • Pegylated polyethylenimine-Fab' antibody fragment conjugates for targeted gene delivery to human ovarian carcinoma cells
    • Merdan T, Callahan J, Petersen H, Kunath K, Bakowsky U, Kopeckova P, Kissel T, Kopecek J. 2003. Pegylated polyethylenimine-Fab' antibody fragment conjugates for targeted gene delivery to human ovarian carcinoma cells. Bioconjug Chem 14:989-996.
    • (2003) Bioconjug Chem , vol.14 , pp. 989-996
    • Merdan, T.1    Callahan, J.2    Petersen, H.3    Kunath, K.4    Bakowsky, U.5    Kopeckova, P.6    Kissel, T.7    Kopecek, J.8
  • 33
    • 3543088051 scopus 로고    scopus 로고
    • Decreases in yeast expression yields of the himian adenosine A2a receptor are a result of translational or post-translational events
    • Niebauer RT, Wedekind A, Robinson AS. 2004. Decreases in yeast expression yields of the himian adenosine A2a receptor are a result of translational or post-translational events. Protein Expr Purif 37:134-143.
    • (2004) Protein Expr Purif , vol.37 , pp. 134-143
    • Niebauer, R.T.1    Wedekind, A.2    Robinson, A.S.3
  • 34
    • 1842690705 scopus 로고    scopus 로고
    • Resistance of B16 melanoma cells to CD47-induced negative regulation of motility as a result of aberrant N-glycosylation of SHPS-1
    • Ogura T, Noguchi T, Murai-Takebe R, Hosooka T, Honma N, Kasuga M. 2004. Resistance of B16 melanoma cells to CD47-induced negative regulation of motility as a result of aberrant N-glycosylation of SHPS-1. J Biol Chem 279:13711-13720.
    • (2004) J Biol Chem , vol.279 , pp. 13711-13720
    • Ogura, T.1    Noguchi, T.2    Murai-Takebe, R.3    Hosooka, T.4    Honma, N.5    Kasuga, M.6
  • 36
    • 0037359054 scopus 로고    scopus 로고
    • Rapid method for measuring scFv thermal stability by yeast surface display
    • Orr BA, Carr LM, Wittrup KD, Roy EJ, Kranz DM. 2003. Rapid method for measuring scFv thermal stability by yeast surface display. Biotechnol Prog 19:631-638.
    • (2003) Biotechnol Prog , vol.19 , pp. 631-638
    • Orr, B.A.1    Carr, L.M.2    Wittrup, K.D.3    Roy, E.J.4    Kranz, D.M.5
  • 37
    • 0344813702 scopus 로고    scopus 로고
    • Antibody scFv fragments without disulfide bonds made by molecular evolution
    • Proba K, Worn A, Honegger A, Pluckthun A. 1998. Antibody scFv fragments without disulfide bonds made by molecular evolution. J Mol Biol 275:245-253.
    • (1998) J Mol Biol , vol.275 , pp. 245-253
    • Proba, K.1    Worn, A.2    Honegger, A.3    Pluckthun, A.4
  • 38
    • 0035860685 scopus 로고    scopus 로고
    • Normal ligand binding and signaling by CD47 (integrin-associated protein) requires a long range disulfide bond between the extracellular and membrane-spanning domains
    • Rebres RA, Vaz LE, Green JM, Brown EJ. 2001. Normal ligand binding and signaling by CD47 (integrin-associated protein) requires a long range disulfide bond between the extracellular and membrane-spanning domains. J Biol Chem 276:34607-34616.
    • (2001) J Biol Chem , vol.276 , pp. 34607-34616
    • Rebres, R.A.1    Vaz, L.E.2    Green, J.M.3    Brown, E.J.4
  • 39
    • 0026705149 scopus 로고
    • Expression of the 50-kDa integrin-associated protein on myeloid cells and erythrocytes
    • Rosales C, Gresham HD, Brown EJ. 1992. Expression of the 50-kDa integrin-associated protein on myeloid cells and erythrocytes. J Immunol 149:2759-2764.
    • (1992) J Immunol , vol.149 , pp. 2759-2764
    • Rosales, C.1    Gresham, H.D.2    Brown, E.J.3
  • 41
    • 4644299058 scopus 로고    scopus 로고
    • Sugar-mediated ligand-receptor interactions in the immune system
    • Rudd PM, Wormald MR, Dwek RA. 2004. Sugar-mediated ligand-receptor interactions in the immune system. Trends Biotechnol 22:524-530.
    • (2004) Trends Biotechnol , vol.22 , pp. 524-530
    • Rudd, P.M.1    Wormald, M.R.2    Dwek, R.A.3
  • 42
    • 0033485642 scopus 로고    scopus 로고
    • Human signal-regulatory protein is expressed on normal, but not on subsets of leukemic myeloid cells and mediates cellular adhesion involving its counterreceptor CD47
    • Seiffert M, Cant C, Chen Z, Rappold I, Brugger W, Kanz L, Brown EJ, Ullrich A, Buhring HL. 1999. Human signal-regulatory protein is expressed on normal, but not on subsets of leukemic myeloid cells and mediates cellular adhesion involving its counterreceptor CD47. Blood 94:3633-3643.
    • (1999) Blood , vol.94 , pp. 3633-3643
    • Seiffert, M.1    Cant, C.2    Chen, Z.3    Rappold, I.4    Brugger, W.5    Kanz, L.6    Brown, E.J.7    Ullrich, A.8    Buhring, H.L.9
  • 43
    • 0029916898 scopus 로고    scopus 로고
    • The amino acid at the X position of an Asn-X-Ser sequon is an important determinant of N-linked core-glycosylation efficiency
    • Shakin-Eshleman SH, Spitalnik SL, Kasturi L. 1996. The amino acid at the X position of an Asn-X-Ser sequon is an important determinant of N-linked core-glycosylation efficiency. J Biol Chem 271:6363-6366.
    • (1996) J Biol Chem , vol.271 , pp. 6363-6366
    • Shakin-Eshleman, S.H.1    Spitalnik, S.L.2    Kasturi, L.3
  • 45
    • 1842839998 scopus 로고    scopus 로고
    • High efficiency recovery and epitope-specific sorting of an scFv yeast display library
    • Siegel RW, Coleman JR, Miller KD, Feldbaus MJ. 2004. High efficiency recovery and epitope-specific sorting of an scFv yeast display library. J Immunol Methods 286:141-153.
    • (2004) J Immunol Methods , vol.286 , pp. 141-153
    • Siegel, R.W.1    Coleman, J.R.2    Miller, K.D.3    Feldbaus, M.J.4
  • 46
    • 1642460190 scopus 로고    scopus 로고
    • Directed evolution of a single-chain class II MHC product by yeast display
    • Starwalt SE, Masteller EL, Bluestone JA, Kranz DM. 2003. Directed evolution of a single-chain class II MHC product by yeast display. Protein Eng 16:147-156.
    • (2003) Protein Eng , vol.16 , pp. 147-156
    • Starwalt, S.E.1    Masteller, E.L.2    Bluestone, J.A.3    Kranz, D.M.4
  • 47
    • 0031568080 scopus 로고    scopus 로고
    • Integrin-associated protein (CD47) is a comitogenic molecule on CD3-activated human T cells
    • Ticchioni M, Deckert M, Mary F, Bernard G, Brown EJ, Bernard A. 1997. Integrin-associated protein (CD47) is a comitogenic molecule on CD3-activated human T cells. J Immunol 158:677-684.
    • (1997) J Immunol , vol.158 , pp. 677-684
    • Ticchioni, M.1    Deckert, M.2    Mary, F.3    Bernard, G.4    Brown, E.J.5    Bernard, A.6
  • 48
    • 0035042939 scopus 로고    scopus 로고
    • Differential galactosylation of neuronal and haematopoietic signal regulatory protein-alpha determines its cellular binding-specificity
    • van den Nieuwenhof IM, Renardel de Lavalette C, Diaz N, van Die I, van den Berg TK. 2001. Differential galactosylation of neuronal and haematopoietic signal regulatory protein-alpha determines its cellular binding-specificity. J Cell Sci 114:1321-1329.
    • (2001) J Cell Sci , vol.114 , pp. 1321-1329
    • Van Den Nieuwenhof, I.M.1    De Renardel Lavalette, C.2    Diaz, N.3    Van Die, I.4    Van Den Berg, T.K.5
  • 49
    • 0024006651 scopus 로고
    • Purification and characterization of the inducible a agglutinin of Saccharomyces cerevisiae
    • Watzele M, Klis F, Tanner W. 1988. Purification and characterization of the inducible a agglutinin of Saccharomyces cerevisiae. The EMBO J 7:1483-1488.
    • (1988) The EMBO J , vol.7 , pp. 1483-1488
    • Watzele, M.1    Klis, F.2    Tanner, W.3
  • 50
    • 0036010267 scopus 로고    scopus 로고
    • Quantitative screening of yeast surface-displayed polypeptide libraries by magnetic bead capture
    • Yeung YA, Wittrup KD. 2002. Quantitative screening of yeast surface-displayed polypeptide libraries by magnetic bead capture. Biotechnol Prog 18:212-220.
    • (2002) Biotechnol Prog , vol.18 , pp. 212-220
    • Yeung, Y.A.1    Wittrup, K.D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.