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Volumn 11, Issue 7, 2016, Pages 1852-1861

Stabilizing the CH2 Domain of an Antibody by Engineering in an Enhanced Aromatic Sequon

Author keywords

[No Author keywords available]

Indexed keywords

FC RECEPTOR; FC RECEPTOR IIA; FC RECEPTOR IIIA; FC RECEPTOR IIIB; IMMUNOGLOBULIN FC FRAGMENT; IMMUNOGLOBULIN G1; UNCLASSIFIED DRUG; MONOCLONAL ANTIBODY;

EID: 84978483848     PISSN: 15548929     EISSN: 15548937     Source Type: Journal    
DOI: 10.1021/acschembio.5b01035     Document Type: Article
Times cited : (43)

References (71)
  • 1
    • 61649087668 scopus 로고    scopus 로고
    • Glycosylation as a strategy to improve antibody-based therapeutics
    • Jefferis, R. (2009) Glycosylation as a strategy to improve antibody-based therapeutics Nat. Rev. Drug Discovery 8, 226-234 10.1038/nrd2804
    • (2009) Nat. Rev. Drug Discovery , vol.8 , pp. 226-234
    • Jefferis, R.1
  • 2
    • 84896086830 scopus 로고    scopus 로고
    • Competing aggregation pathways for monoclonal antibodies
    • Wu, H., Kroe-Barrett, R., Singh, S., Robinson, A. S., and Roberts, C. J. (2014) Competing aggregation pathways for monoclonal antibodies FEBS Lett. 588, 936-941 10.1016/j.febslet.2014.01.051
    • (2014) FEBS Lett. , vol.588 , pp. 936-941
    • Wu, H.1    Kroe-Barrett, R.2    Singh, S.3    Robinson, A.S.4    Roberts, C.J.5
  • 3
    • 0036598634 scopus 로고    scopus 로고
    • Bioequivalence and the immunogenicity of biopharmaceuticals
    • Schellekens, H. (2002) Bioequivalence and the immunogenicity of biopharmaceuticals Nat. Rev. Drug Discov 1, 457-462 10.1038/nrd818
    • (2002) Nat. Rev. Drug Discov , vol.1 , pp. 457-462
    • Schellekens, H.1
  • 5
    • 82755197856 scopus 로고    scopus 로고
    • Strategies for extended serum half-life of protein therapeutics
    • Kontermann, R. E. (2011) Strategies for extended serum half-life of protein therapeutics Curr. Opin. Biotechnol. 22, 868-876 10.1016/j.copbio.2011.06.012
    • (2011) Curr. Opin. Biotechnol. , vol.22 , pp. 868-876
    • Kontermann, R.E.1
  • 6
    • 71549161144 scopus 로고    scopus 로고
    • Physical instability of a therapeutic Fc fusion protein: Domain contributions to conformational and colloidal stability
    • Fast, J. L., Cordes, A. A., Carpenter, J. F., and Randolph, T. W. (2009) Physical instability of a therapeutic Fc fusion protein: domain contributions to conformational and colloidal stability Biochemistry 48, 11724-11736 10.1021/bi900853v
    • (2009) Biochemistry , vol.48 , pp. 11724-11736
    • Fast, J.L.1    Cordes, A.A.2    Carpenter, J.F.3    Randolph, T.W.4
  • 8
    • 67650683480 scopus 로고    scopus 로고
    • Aggregation-prone motifs in human immunoglobulin G
    • Chennamsetty, N., Helk, B., Voynov, V., Kayser, V., and Trout, B. L. (2009) Aggregation-prone motifs in human immunoglobulin G J. Mol. Biol. 391, 404-413 10.1016/j.jmb.2009.06.028
    • (2009) J. Mol. Biol. , vol.391 , pp. 404-413
    • Chennamsetty, N.1    Helk, B.2    Voynov, V.3    Kayser, V.4    Trout, B.L.5
  • 10
    • 79954494833 scopus 로고    scopus 로고
    • Nonnative aggregation of an IgG1 antibody in acidic conditions, part 2: Nucleation and growth kinetics with competing growth mechanisms
    • Brummitt, R. K., Nesta, D. P., Chang, L., Kroetsch, A. M., and Roberts, C. J. (2011) Nonnative aggregation of an IgG1 antibody in acidic conditions, part 2: nucleation and growth kinetics with competing growth mechanisms J. Pharm. Sci. 100, 2104-2119 10.1002/jps.22447
    • (2011) J. Pharm. Sci. , vol.100 , pp. 2104-2119
    • Brummitt, R.K.1    Nesta, D.P.2    Chang, L.3    Kroetsch, A.M.4    Roberts, C.J.5
  • 12
    • 84929587129 scopus 로고    scopus 로고
    • A perspective on the structure and receptor binding properties of immunoglobulin G Fc
    • Hanson, Q. M. and Barb, A. W. (2015) A perspective on the structure and receptor binding properties of immunoglobulin G Fc Biochemistry 54, 2931-2942 10.1021/acs.biochem.5b00299
    • (2015) Biochemistry , vol.54 , pp. 2931-2942
    • Hanson, Q.M.1    Barb, A.W.2
  • 13
    • 81255197729 scopus 로고    scopus 로고
    • The impact of glycosylation on monoclonal antibody conformation and stability
    • Zheng, K., Bantog, C., and Bayer, R. (2011) The impact of glycosylation on monoclonal antibody conformation and stability MAbs 3, 568-576 10.4161/mabs.3.6.17922
    • (2011) MAbs , vol.3 , pp. 568-576
    • Zheng, K.1    Bantog, C.2    Bayer, R.3
  • 14
    • 84875998684 scopus 로고    scopus 로고
    • Impact of immune complex size and glycosylation on IgG binding to human FcγRs
    • Lux, A., Yu, X., Scanlan, C. N., and Nimmerjahn, F. (2013) Impact of immune complex size and glycosylation on IgG binding to human FcγRs J. Immunol. 190, 4315-4323 10.4049/jimmunol.1200501
    • (2013) J. Immunol. , vol.190 , pp. 4315-4323
    • Lux, A.1    Yu, X.2    Scanlan, C.N.3    Nimmerjahn, F.4
  • 15
    • 79951838374 scopus 로고    scopus 로고
    • NMR analysis demonstrates immunoglobulin G N-glycans are accessible and dynamic
    • Barb, A. W. and Prestegard, J. H. (2011) NMR analysis demonstrates immunoglobulin G N-glycans are accessible and dynamic Nat. Chem. Biol. 7, 147-153 10.1038/nchembio.511
    • (2011) Nat. Chem. Biol. , vol.7 , pp. 147-153
    • Barb, A.W.1    Prestegard, J.H.2
  • 16
    • 84947032537 scopus 로고    scopus 로고
    • The structural role of antibody N-glycosylation in receptor interactions
    • Subedi, G. P. and Barb, A. W. (2015) The structural role of antibody N-glycosylation in receptor interactions Structure 23, 1573-1583 10.1016/j.str.2015.06.015
    • (2015) Structure , vol.23 , pp. 1573-1583
    • Subedi, G.P.1    Barb, A.W.2
  • 17
    • 84908211671 scopus 로고    scopus 로고
    • Restricted motion of the conserved immunoglobulin G1 N-glycan is essential for efficient FcγRIIIa binding
    • Subedi, G. P., Hanson, Q. M., and Barb, A. W. (2014) Restricted motion of the conserved immunoglobulin G1 N-glycan is essential for efficient FcγRIIIa binding Structure 22, 1478-1488 10.1016/j.str.2014.08.002
    • (2014) Structure , vol.22 , pp. 1478-1488
    • Subedi, G.P.1    Hanson, Q.M.2    Barb, A.W.3
  • 18
    • 79551626904 scopus 로고    scopus 로고
    • Protein native-state stabilization by placing aromatic side chains in N-glycosylated reverse turns
    • Culyba, E. K., Price, J. L., Hanson, S. R., Dhar, A., Wong, C. H., Gruebele, M., Powers, E. T., and Kelly, J. W. (2011) Protein native-state stabilization by placing aromatic side chains in N-glycosylated reverse turns Science 331, 571-575 10.1126/science.1198461
    • (2011) Science , vol.331 , pp. 571-575
    • Culyba, E.K.1    Price, J.L.2    Hanson, S.R.3    Dhar, A.4    Wong, C.H.5    Gruebele, M.6    Powers, E.T.7    Kelly, J.W.8
  • 19
    • 80052179739 scopus 로고    scopus 로고
    • Glycosylation of the enhanced aromatic sequon is similarly stabilizing in three distinct reverse turn contexts
    • Price, J. L., Powers, D. L., Powers, E. T., and Kelly, J. W. (2011) Glycosylation of the enhanced aromatic sequon is similarly stabilizing in three distinct reverse turn contexts Proc. Natl. Acad. Sci. U. S. A. 108, 14127-14132 10.1073/pnas.1105880108
    • (2011) Proc. Natl. Acad. Sci. U. S. A. , vol.108 , pp. 14127-14132
    • Price, J.L.1    Powers, D.L.2    Powers, E.T.3    Kelly, J.W.4
  • 20
  • 24
    • 62549107841 scopus 로고    scopus 로고
    • The core trisaccharide of an N-linked glycoprotein intrinsically accelerates folding and enhances stability
    • Hanson, S. R., Culyba, E. K., Hsu, T. L., Wong, C. H., Kelly, J. W., and Powers, E. T. (2009) The core trisaccharide of an N-linked glycoprotein intrinsically accelerates folding and enhances stability Proc. Natl. Acad. Sci. U. S. A. 106, 3131-3136 10.1073/pnas.0810318105
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 3131-3136
    • Hanson, S.R.1    Culyba, E.K.2    Hsu, T.L.3    Wong, C.H.4    Kelly, J.W.5    Powers, E.T.6
  • 25
    • 0035839050 scopus 로고    scopus 로고
    • The folding mechanism of a β-sheet: The WW domain
    • Jager, M., Nguyen, H., Crane, J. C., Kelly, J. W., and Gruebele, M. (2001) The folding mechanism of a β-sheet: the WW domain J. Mol. Biol. 311, 373-393 10.1006/jmbi.2001.4873
    • (2001) J. Mol. Biol. , vol.311 , pp. 373-393
    • Jager, M.1    Nguyen, H.2    Crane, J.C.3    Kelly, J.W.4    Gruebele, M.5
  • 27
    • 0032939806 scopus 로고    scopus 로고
    • WW: An isolated three-stranded antiparallel β-sheet domain that unfolds and refolds reversibly; Evidence for a structured hydrophobic cluster in urea and GdnHCl and a disordered thermal unfolded state
    • Koepf, E. K., Petrassi, H. M., Sudol, M., and Kelly, J. W. (1999) WW: An isolated three-stranded antiparallel β-sheet domain that unfolds and refolds reversibly; evidence for a structured hydrophobic cluster in urea and GdnHCl and a disordered thermal unfolded state Protein Sci. 8, 841-853 10.1110/ps.8.4.841
    • (1999) Protein Sci. , vol.8 , pp. 841-853
    • Koepf, E.K.1    Petrassi, H.M.2    Sudol, M.3    Kelly, J.W.4
  • 28
    • 84867644046 scopus 로고    scopus 로고
    • A fundamental protein property, thermodynamic stability, revealed solely from large-scale measurements of protein function
    • Araya, C. L., Fowler, D. M., Chen, W., Muniez, I., Kelly, J. W., and Fields, S. (2012) A fundamental protein property, thermodynamic stability, revealed solely from large-scale measurements of protein function Proc. Natl. Acad. Sci. U. S. A. 109, 16858-16863 10.1073/pnas.1209751109
    • (2012) Proc. Natl. Acad. Sci. U. S. A. , vol.109 , pp. 16858-16863
    • Araya, C.L.1    Fowler, D.M.2    Chen, W.3    Muniez, I.4    Kelly, J.W.5    Fields, S.6
  • 29
    • 84908501531 scopus 로고    scopus 로고
    • Structural basis for selective recognition of endogenous and microbial polysaccharides by macrophage receptor SIGN-R1
    • Silva-Martin, N., Bartual, S. G., Ramirez-Aportela, E., Chacon, P., Park, C. G., and Hermoso, J. A. (2014) Structural basis for selective recognition of endogenous and microbial polysaccharides by macrophage receptor SIGN-R1 Structure 22, 1595-1606 10.1016/j.str.2014.09.001
    • (2014) Structure , vol.22 , pp. 1595-1606
    • Silva-Martin, N.1    Bartual, S.G.2    Ramirez-Aportela, E.3    Chacon, P.4    Park, C.G.5    Hermoso, J.A.6
  • 33
    • 84897110175 scopus 로고    scopus 로고
    • Immunoglobulin G1 Fc domain motions: Implications for Fc engineering
    • Frank, M., Walker, R. C., Lanzilotta, W. N., Prestegard, J. H., and Barb, A. W. (2014) Immunoglobulin G1 Fc domain motions: implications for Fc engineering J. Mol. Biol. 426, 1799-1811 10.1016/j.jmb.2014.01.011
    • (2014) J. Mol. Biol. , vol.426 , pp. 1799-1811
    • Frank, M.1    Walker, R.C.2    Lanzilotta, W.N.3    Prestegard, J.H.4    Barb, A.W.5
  • 34
    • 84922360962 scopus 로고    scopus 로고
    • Structure of FcγRI in complex with Fc reveals the importance of glycan recognition for high-affinity IgG binding
    • Lu, J., Chu, J., Zou, Z., Hamacher, N. B., Rixon, M. W., and Sun, P. D. (2015) Structure of FcγRI in complex with Fc reveals the importance of glycan recognition for high-affinity IgG binding Proc. Natl. Acad. Sci. U. S. A. 112, 833-838 10.1073/pnas.1418812112
    • (2015) Proc. Natl. Acad. Sci. U. S. A. , vol.112 , pp. 833-838
    • Lu, J.1    Chu, J.2    Zou, Z.3    Hamacher, N.B.4    Rixon, M.W.5    Sun, P.D.6
  • 35
    • 63449138097 scopus 로고    scopus 로고
    • Carbohydrate and domain architecture of an immature antibody glycoform exhibiting enhanced effector functions
    • Crispin, M., Bowden, T. A., Coles, C. H., Harlos, K., Aricescu, A. R., Harvey, D. J., Stuart, D. I., and Jones, E. Y. (2009) Carbohydrate and domain architecture of an immature antibody glycoform exhibiting enhanced effector functions J. Mol. Biol. 387, 1061-1066 10.1016/j.jmb.2009.02.033
    • (2009) J. Mol. Biol. , vol.387 , pp. 1061-1066
    • Crispin, M.1    Bowden, T.A.2    Coles, C.H.3    Harlos, K.4    Aricescu, A.R.5    Harvey, D.J.6    Stuart, D.I.7    Jones, E.Y.8
  • 36
    • 0019522383 scopus 로고
    • Crystallographic refinement and atomic models of a human Fc fragment and its complex with fragment B of protein A from Staphylococcus aureus at 2.9- and 2.8-A resolution
    • Deisenhofer, J. (1981) Crystallographic refinement and atomic models of a human Fc fragment and its complex with fragment B of protein A from Staphylococcus aureus at 2.9- and 2.8-A resolution Biochemistry 20, 2361-2370 10.1021/bi00512a001
    • (1981) Biochemistry , vol.20 , pp. 2361-2370
    • Deisenhofer, J.1
  • 37
    • 0037474543 scopus 로고    scopus 로고
    • Structural analysis of human IgG-Fc glycoforms reveals a correlation between glycosylation and structural integrity
    • Krapp, S., Mimura, Y., Jefferis, R., Huber, R., and Sondermann, P. (2003) Structural analysis of human IgG-Fc glycoforms reveals a correlation between glycosylation and structural integrity J. Mol. Biol. 325, 979-989 10.1016/S0022-2836(02)01250-0
    • (2003) J. Mol. Biol. , vol.325 , pp. 979-989
    • Krapp, S.1    Mimura, Y.2    Jefferis, R.3    Huber, R.4    Sondermann, P.5
  • 38
    • 0034691322 scopus 로고    scopus 로고
    • The 3.2-Å crystal structure of the human IgG1 Fc fragment-FcγRIII complex
    • Sondermann, P., Huber, R., Oosthuizen, V., and Jacob, U. (2000) The 3.2-Å crystal structure of the human IgG1 Fc fragment-FcγRIII complex Nature 406, 267-273 10.1038/35018508
    • (2000) Nature , vol.406 , pp. 267-273
    • Sondermann, P.1    Huber, R.2    Oosthuizen, V.3    Jacob, U.4
  • 41
    • 34548409568 scopus 로고    scopus 로고
    • Contrasting glycosylation profiles between Fab and Fc of a human IgG protein studied by electrospray ionization mass spectrometry
    • Mimura, Y., Ashton, P. R., Takahashi, N., Harvey, D. J., and Jefferis, R. (2007) Contrasting glycosylation profiles between Fab and Fc of a human IgG protein studied by electrospray ionization mass spectrometry J. Immunol. Methods 326, 116-126 10.1016/j.jim.2007.07.014
    • (2007) J. Immunol. Methods , vol.326 , pp. 116-126
    • Mimura, Y.1    Ashton, P.R.2    Takahashi, N.3    Harvey, D.J.4    Jefferis, R.5
  • 46
    • 80053474133 scopus 로고    scopus 로고
    • A broadly neutralizing human monoclonal antibody that recognizes a conserved, novel epitope on the globular head of the influenza H1N1 virus hemagglutinin
    • Krause, J. C., Tsibane, T., Tumpey, T. M., Huffman, C. J., Basler, C. F., and Crowe, J. E., Jr. (2011) A broadly neutralizing human monoclonal antibody that recognizes a conserved, novel epitope on the globular head of the influenza H1N1 virus hemagglutinin J. Virol 85, 10905-10908 10.1128/JVI.00700-11
    • (2011) J. Virol , vol.85 , pp. 10905-10908
    • Krause, J.C.1    Tsibane, T.2    Tumpey, T.M.3    Huffman, C.J.4    Basler, C.F.5    Crowe, Jr.J.E.6
  • 47
    • 79960128166 scopus 로고    scopus 로고
    • Classification and characterization of therapeutic antibody aggregates
    • Joubert, M. K., Luo, Q., Nashed-Samuel, Y., Wypych, J., and Narhi, L. O. (2011) Classification and characterization of therapeutic antibody aggregates J. Biol. Chem. 286, 25118-25133 10.1074/jbc.M110.160457
    • (2011) J. Biol. Chem. , vol.286 , pp. 25118-25133
    • Joubert, M.K.1    Luo, Q.2    Nashed-Samuel, Y.3    Wypych, J.4    Narhi, L.O.5
  • 48
    • 79956103081 scopus 로고    scopus 로고
    • Aggregates in monoclonal antibody manufacturing processes
    • Vazquez-Rey, M. and Lang, D. A. (2011) Aggregates in monoclonal antibody manufacturing processes Biotechnol. Bioeng. 108, 1494-1508 10.1002/bit.23155
    • (2011) Biotechnol. Bioeng. , vol.108 , pp. 1494-1508
    • Vazquez-Rey, M.1    Lang, D.A.2
  • 49
    • 32844462853 scopus 로고    scopus 로고
    • Thermodynamic stability and formation of aggregates of human immunoglobulin G characterised by differential scanning calorimetry and dynamic light scattering
    • Ahrer, K., Buchacher, A., Iberer, G., and Jungbauer, A. (2006) Thermodynamic stability and formation of aggregates of human immunoglobulin G characterised by differential scanning calorimetry and dynamic light scattering J. Biochem. Biophys. Methods 66, 73-86 10.1016/j.jbbm.2005.12.003
    • (2006) J. Biochem. Biophys. Methods , vol.66 , pp. 73-86
    • Ahrer, K.1    Buchacher, A.2    Iberer, G.3    Jungbauer, A.4
  • 51
    • 0029927482 scopus 로고    scopus 로고
    • Abnormally short serum half-lives of IgG in β 2-microglobulin-deficient mice
    • Ghetie, V., Hubbard, J. G., Kim, J. K., Tsen, M. F., Lee, Y., and Ward, E. S. (1996) Abnormally short serum half-lives of IgG in β 2-microglobulin-deficient mice Eur. J. Immunol. 26, 690-696 10.1002/eji.1830260327
    • (1996) Eur. J. Immunol. , vol.26 , pp. 690-696
    • Ghetie, V.1    Hubbard, J.G.2    Kim, J.K.3    Tsen, M.F.4    Lee, Y.5    Ward, E.S.6
  • 52
    • 0034042660 scopus 로고    scopus 로고
    • Multiple roles for the major histocompatibility complex class I- related receptor FcRn
    • Ghetie, V. and Ward, E. S. (2000) Multiple roles for the major histocompatibility complex class I- related receptor FcRn Annu. Rev. Immunol. 18, 739-766 10.1146/annurev.immunol.18.1.739
    • (2000) Annu. Rev. Immunol. , vol.18 , pp. 739-766
    • Ghetie, V.1    Ward, E.S.2
  • 54
    • 84867836578 scopus 로고    scopus 로고
    • Revisiting the role of glycosylation in the structure of human IgG Fc
    • Borrok, M. J., Jung, S. T., Kang, T. H., Monzingo, A. F., and Georgiou, G. (2012) Revisiting the role of glycosylation in the structure of human IgG Fc ACS Chem. Biol. 7, 1596-1602 10.1021/cb300130k
    • (2012) ACS Chem. Biol. , vol.7 , pp. 1596-1602
    • Borrok, M.J.1    Jung, S.T.2    Kang, T.H.3    Monzingo, A.F.4    Georgiou, G.5
  • 55
    • 0035794194 scopus 로고    scopus 로고
    • High resolution mapping of the binding site on human IgG1 for FcγRI, FcγRII, FcγRIII, and FcRn and design of IgG1 variants with improved binding to the FcγR
    • Shields, R. L., Namenuk, A. K., Hong, K., Meng, Y. G., Rae, J., Briggs, J., Xie, D., Lai, J., Stadlen, A., Li, B., Fox, J. A., and Presta, L. G. (2001) High resolution mapping of the binding site on human IgG1 for FcγRI, FcγRII, FcγRIII, and FcRn and design of IgG1 variants with improved binding to the FcγR J. Biol. Chem. 276, 6591-6604 10.1074/jbc.M009483200
    • (2001) J. Biol. Chem. , vol.276 , pp. 6591-6604
    • Shields, R.L.1    Namenuk, A.K.2    Hong, K.3    Meng, Y.G.4    Rae, J.5    Briggs, J.6    Xie, D.7    Lai, J.8    Stadlen, A.9    Li, B.10    Fox, J.A.11    Presta, L.G.12
  • 56
    • 84977126665 scopus 로고    scopus 로고
    • The role of Fcγ receptors in the activity of immunomodulatory antibodies for cancer
    • Stewart, R., Hammond, S. A., Oberst, M., and Wilkinson, R. W. (2014) The role of Fcγ receptors in the activity of immunomodulatory antibodies for cancer J. Immunother. Cancer 2, 29 10.1186/s40425-014-0029-x
    • (2014) J. Immunother. Cancer , vol.2 , pp. 29
    • Stewart, R.1    Hammond, S.A.2    Oberst, M.3    Wilkinson, R.W.4
  • 57
    • 78651360674 scopus 로고    scopus 로고
    • Optimizing therapeutic antibody function: Progress with Fc domain engineering
    • Kaneko, E. and Niwa, R. (2011) Optimizing therapeutic antibody function: progress with Fc domain engineering BioDrugs 25, 1-11 10.2165/11537830-000000000-00000
    • (2011) BioDrugs , vol.25 , pp. 1-11
    • Kaneko, E.1    Niwa, R.2
  • 58
    • 84874101229 scopus 로고    scopus 로고
    • Effective phagocytosis of low Her2 tumor cell lines with engineered, aglycosylated IgG displaying high FcγRIIa affinity and selectivity
    • Jung, S. T., Kelton, W., Kang, T. H., Ng, D. T., Andersen, J. T., Sandlie, I., Sarkar, C. A., and Georgiou, G. (2013) Effective phagocytosis of low Her2 tumor cell lines with engineered, aglycosylated IgG displaying high FcγRIIa affinity and selectivity ACS Chem. Biol. 8, 368-375 10.1021/cb300455f
    • (2013) ACS Chem. Biol. , vol.8 , pp. 368-375
    • Jung, S.T.1    Kelton, W.2    Kang, T.H.3    Ng, D.T.4    Andersen, J.T.5    Sandlie, I.6    Sarkar, C.A.7    Georgiou, G.8
  • 59
    • 84892369713 scopus 로고    scopus 로고
    • Effects of subclass change on the structural stability of chimeric, humanized, and human antibodies under thermal stress
    • Ito, T. and Tsumoto, K. (2013) Effects of subclass change on the structural stability of chimeric, humanized, and human antibodies under thermal stress Protein Sci. 22, 1542-1551 10.1002/pro.2340
    • (2013) Protein Sci. , vol.22 , pp. 1542-1551
    • Ito, T.1    Tsumoto, K.2
  • 60
    • 36849001338 scopus 로고    scopus 로고
    • Isotype selection in antibody engineering
    • Salfeld, J. G. (2007) Isotype selection in antibody engineering Nat. Biotechnol. 25, 1369-1372 10.1038/nbt1207-1369
    • (2007) Nat. Biotechnol. , vol.25 , pp. 1369-1372
    • Salfeld, J.G.1
  • 61
    • 84865677743 scopus 로고    scopus 로고
    • Isotype and glycoform selection for antibody therapeutics
    • Jefferis, R. (2012) Isotype and glycoform selection for antibody therapeutics Arch. Biochem. Biophys. 526, 159-166 10.1016/j.abb.2012.03.021
    • (2012) Arch. Biochem. Biophys. , vol.526 , pp. 159-166
    • Jefferis, R.1
  • 62
    • 0030111265 scopus 로고    scopus 로고
    • Codon usage limitation in the expression of HIV-1 envelope glycoprotein
    • Haas, J., Park, E. C., and Seed, B. (1996) Codon usage limitation in the expression of HIV-1 envelope glycoprotein Curr. Biol. 6, 315-324 10.1016/S0960-9822(02)00482-7
    • (1996) Curr. Biol. , vol.6 , pp. 315-324
    • Haas, J.1    Park, E.C.2    Seed, B.3
  • 63
    • 77952575336 scopus 로고    scopus 로고
    • Expression, glycoform characterization, and antibody-binding of HIV-1 V3 glycopeptide domain fused with human IgG1-Fc
    • Yang, Q., Li, C., Wei, Y., Huang, W., and Wang, L. X. (2010) Expression, glycoform characterization, and antibody-binding of HIV-1 V3 glycopeptide domain fused with human IgG1-Fc Bioconjugate Chem. 21, 875-883 10.1021/bc9004238
    • (2010) Bioconjugate Chem. , vol.21 , pp. 875-883
    • Yang, Q.1    Li, C.2    Wei, Y.3    Huang, W.4    Wang, L.X.5
  • 64
    • 0023668218 scopus 로고
    • Differential scanning calorimetric study of the thermal unfolding of Taka-amylase A from Aspergillus oryzae
    • Fukada, H., Takahashi, K., and Sturtevant, J. M. (1987) Differential scanning calorimetric study of the thermal unfolding of Taka-amylase A from Aspergillus oryzae Biochemistry 26, 4063-4068 10.1021/bi00387a048
    • (1987) Biochemistry , vol.26 , pp. 4063-4068
    • Fukada, H.1    Takahashi, K.2    Sturtevant, J.M.3
  • 65
    • 0000826487 scopus 로고
    • Biochemical applications of differential scanning calorimetry
    • Sturtevant, J. M. (1987) Biochemical applications of differential scanning calorimetry Annu. Rev. Phys. Chem. 38, 463-488 10.1146/annurev.pc.38.100187.002335
    • (1987) Annu. Rev. Phys. Chem. , vol.38 , pp. 463-488
    • Sturtevant, J.M.1
  • 66
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski, Z. and Minor, W. (1997) Processing of X-ray diffraction data collected in oscillation mode Methods Enzymol. 276, 307-326 10.1016/S0076-6879(97)76066-X
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2


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