메뉴 건너뛰기




Volumn 6, Issue 4, 2011, Pages

High affinity antigen recognition of the dual specific variants of Herceptin is entropy-driven in spite of structural plasticity

Author keywords

[No Author keywords available]

Indexed keywords

ANTIBODY; BH1 44 ANTIBODY; BH1 ANTIBODY; EPIDERMAL GROWTH FACTOR RECEPTOR 2; TRASTUZUMAB; UNCLASSIFIED DRUG; VASCULOTROPIN; ANTIGEN; MONOCLONAL ANTIBODY; MUTANT PROTEIN; VASCULOTROPIN A;

EID: 79955545620     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0017887     Document Type: Article
Times cited : (66)

References (56)
  • 2
    • 1642315560 scopus 로고    scopus 로고
    • Polyreactivity of antibody molecules
    • Notkins AL, (2004) Polyreactivity of antibody molecules. Trends Immunol 25: 174-179.
    • (2004) Trends Immunol , vol.25 , pp. 174-179
    • Notkins, A.L.1
  • 3
    • 0037470415 scopus 로고    scopus 로고
    • Immunology. Isomeric antibodies
    • Foote J, (2003) Immunology. Isomeric antibodies. Science 299: 1327-1328.
    • (2003) Science , vol.299 , pp. 1327-1328
    • Foote, J.1
  • 4
    • 0037470496 scopus 로고    scopus 로고
    • Antibody multispecificity mediated by conformational diversity
    • James LC, Roversi P, Tawfik DS, (2003) Antibody multispecificity mediated by conformational diversity. Science 299: 1362-1367.
    • (2003) Science , vol.299 , pp. 1362-1367
    • James, L.C.1    Roversi, P.2    Tawfik, D.S.3
  • 5
    • 77957355961 scopus 로고    scopus 로고
    • Polyreactivity increases the apparent affinity of anti-HIV antibodies by heteroligation
    • Mouquet H, Scheid JF, Zoller MJ, Krogsgaard M, Ott RG, et al. (2010) Polyreactivity increases the apparent affinity of anti-HIV antibodies by heteroligation. Nature 467: 591-595.
    • (2010) Nature , vol.467 , pp. 591-595
    • Mouquet, H.1    Scheid, J.F.2    Zoller, M.J.3    Krogsgaard, M.4    Ott, R.G.5
  • 6
    • 33748992038 scopus 로고    scopus 로고
    • Receptor editing in lymphocyte development and central tolerance
    • Nemazee D, (2006) Receptor editing in lymphocyte development and central tolerance. Nat Rev Immunol 6: 728-740.
    • (2006) Nat Rev Immunol , vol.6 , pp. 728-740
    • Nemazee, D.1
  • 7
    • 0041689676 scopus 로고    scopus 로고
    • Predominant autoantibody production by early human B cell precursors
    • Wardemann H, Yurasov S, Schaefer A, Young JW, Meffre E, et al. (2003) Predominant autoantibody production by early human B cell precursors. Science 301: 1374-1377.
    • (2003) Science , vol.301 , pp. 1374-1377
    • Wardemann, H.1    Yurasov, S.2    Schaefer, A.3    Young, J.W.4    Meffre, E.5
  • 8
    • 0021745334 scopus 로고
    • Lymphocytes capable of making monoclonal autoantibodies that react with multiple organs are a common feature of the normal B cell repertoire
    • Prabhakar BS, Saegusa J, Onodera T, Notkins AL, (1984) Lymphocytes capable of making monoclonal autoantibodies that react with multiple organs are a common feature of the normal B cell repertoire. J Immunol 133: 2815-2817.
    • (1984) J Immunol , vol.133 , pp. 2815-2817
    • Prabhakar, B.S.1    Saegusa, J.2    Onodera, T.3    Notkins, A.L.4
  • 9
    • 0027943261 scopus 로고
    • Conformational isomerism and the diversity of antibodies
    • Foote J, Milstein C, (1994) Conformational isomerism and the diversity of antibodies. Proc Natl Acad Sci U S A 91: 10370-10374.
    • (1994) Proc Natl Acad Sci U S A , vol.91 , pp. 10370-10374
    • Foote, J.1    Milstein, C.2
  • 10
    • 47749123498 scopus 로고    scopus 로고
    • Autoreactive IgG memory antibodies in patients with systemic lupus erythematosus arise from nonreactive and polyreactive precursors
    • Mietzner B, Tsuiji M, Scheid J, Velinzon K, Tiller T, et al. (2008) Autoreactive IgG memory antibodies in patients with systemic lupus erythematosus arise from nonreactive and polyreactive precursors. Proc Natl Acad Sci U S A 105: 9727-9732.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 9727-9732
    • Mietzner, B.1    Tsuiji, M.2    Scheid, J.3    Velinzon, K.4    Tiller, T.5
  • 11
    • 0016756272 scopus 로고
    • Continuous cultures of fused cells secreting antibody of predefined specificity
    • Kohler G, Milstein C, (1975) Continuous cultures of fused cells secreting antibody of predefined specificity. Nature 256: 495-497.
    • (1975) Nature , vol.256 , pp. 495-497
    • Kohler, G.1    Milstein, C.2
  • 12
    • 33645990894 scopus 로고    scopus 로고
    • Differential epitope positioning within the germline antibody paratope enhances promiscuity in the primary immune response
    • Sethi DK, Agarwal A, Manivel V, Rao KV, Salunke DM, (2006) Differential epitope positioning within the germline antibody paratope enhances promiscuity in the primary immune response. Immunity 24: 429-438.
    • (2006) Immunity , vol.24 , pp. 429-438
    • Sethi, D.K.1    Agarwal, A.2    Manivel, V.3    Rao, K.V.4    Salunke, D.M.5
  • 13
    • 0031438526 scopus 로고    scopus 로고
    • Molecular basis for the binding promiscuity of an anti-p24 (HIV-1) monoclonal antibody
    • Kramer A, Keitel T, Winkler K, Stocklein W, Hohne W, et al. (1997) Molecular basis for the binding promiscuity of an anti-p24 (HIV-1) monoclonal antibody. Cell 91: 799-809.
    • (1997) Cell , vol.91 , pp. 799-809
    • Kramer, A.1    Keitel, T.2    Winkler, K.3    Stocklein, W.4    Hohne, W.5
  • 14
    • 0031571157 scopus 로고    scopus 로고
    • Antibody fragment Fv4155 bound to two closely related steroid hormones: the structural basis of fine specificity
    • Trinh CH, Hemmington SD, Verhoeyen ME, Phillips SE, (1997) Antibody fragment Fv4155 bound to two closely related steroid hormones: the structural basis of fine specificity. Structure 5: 937-948.
    • (1997) Structure , vol.5 , pp. 937-948
    • Trinh, C.H.1    Hemmington, S.D.2    Verhoeyen, M.E.3    Phillips, S.E.4
  • 15
    • 12044252333 scopus 로고
    • Molecular basis of crossreactivity and the limits of antibody-antigen complementarity
    • Arevalo JH, Taussig MJ, Wilson IA, (1993) Molecular basis of crossreactivity and the limits of antibody-antigen complementarity. Nature 365: 859-863.
    • (1993) Nature , vol.365 , pp. 859-863
    • Arevalo, J.H.1    Taussig, M.J.2    Wilson, I.A.3
  • 16
    • 14744300211 scopus 로고
    • Bypassing immunization: high affinity human antibodies by chain shuffling
    • Marks JD, Griffiths AD, Malmqvist M, Clackson T, Bye JM, et al. (1992) Bypassing immunization: high affinity human antibodies by chain shuffling. Bio/Tech 10: 779-783.
    • (1992) Bio/Tech , vol.10 , pp. 779-783
    • Marks, J.D.1    Griffiths, A.D.2    Malmqvist, M.3    Clackson, T.4    Bye, J.M.5
  • 17
    • 33751198274 scopus 로고    scopus 로고
    • Synthetic anti-BR3 antibodies that mimic BAFF binding and target both human and murine B cells
    • Lee CV, Hymowitz SG, Wallweber HJ, Gordon NC, Billeci KL, et al. (2006) Synthetic anti-BR3 antibodies that mimic BAFF binding and target both human and murine B cells. Blood 108: 3103-3111.
    • (2006) Blood , vol.108 , pp. 3103-3111
    • Lee, C.V.1    Hymowitz, S.G.2    Wallweber, H.J.3    Gordon, N.C.4    Billeci, K.L.5
  • 18
    • 33646562554 scopus 로고    scopus 로고
    • Structure-function studies of two synthetic anti-vascular endothelial growth factor Fabs and comparison with the Avastin Fab
    • Fuh G, Wu P, Liang WC, Ultsch M, Lee CV, et al. (2006) Structure-function studies of two synthetic anti-vascular endothelial growth factor Fabs and comparison with the Avastin Fab. J Biol Chem 281: 6625-6631.
    • (2006) J Biol Chem , vol.281 , pp. 6625-6631
    • Fuh, G.1    Wu, P.2    Liang, W.C.3    Ultsch, M.4    Lee, C.V.5
  • 19
    • 0029764534 scopus 로고    scopus 로고
    • A mutational analysis of the binding of two different proteins to the same antibody
    • Dall'Acqua W, Goldman ER, Eisenstein E, Mariuzza RA, (1996) A mutational analysis of the binding of two different proteins to the same antibody. Biochemistry 35: 9667-9676.
    • (1996) Biochemistry , vol.35 , pp. 9667-9676
    • Dall'Acqua, W.1    Goldman, E.R.2    Eisenstein, E.3    Mariuzza, R.A.4
  • 21
    • 0031454829 scopus 로고    scopus 로고
    • Crystallographic analysis of anti-p24 (HIV-1) monoclonal antibody cross-reactivity and polyspecificity
    • Keitel T, Kramer A, Wessner H, Scholz C, Schneider-Mergener J, et al. (1997) Crystallographic analysis of anti-p24 (HIV-1) monoclonal antibody cross-reactivity and polyspecificity. Cell 91: 811-820.
    • (1997) Cell , vol.91 , pp. 811-820
    • Keitel, T.1    Kramer, A.2    Wessner, H.3    Scholz, C.4    Schneider-Mergener, J.5
  • 22
    • 62849095162 scopus 로고    scopus 로고
    • Variants of the antibody Herceptin that interact with HER2 and VEGF at the antigen binding site
    • Bostrom J, Yu SF, Kan D, Appleton BA, Lee CV, et al. (2009) Variants of the antibody Herceptin that interact with HER2 and VEGF at the antigen binding site. Science 323: 1610-1614.
    • (2009) Science , vol.323 , pp. 1610-1614
    • Bostrom, J.1    Yu, S.F.2    Kan, D.3    Appleton, B.A.4    Lee, C.V.5
  • 23
    • 0027467623 scopus 로고
    • X-ray structures of the antigen-binding domains from three variants of humanized anti-p185HER2 antibody 4D5 and comparison with molecular modeling
    • Eigenbrot C, Randal M, Presta L, Carter P, Kossiakoff AA, (1993) X-ray structures of the antigen-binding domains from three variants of humanized anti-p185HER2 antibody 4D5 and comparison with molecular modeling. J Mol Biol 229: 969-995.
    • (1993) J Mol Biol , vol.229 , pp. 969-995
    • Eigenbrot, C.1    Randal, M.2    Presta, L.3    Carter, P.4    Kossiakoff, A.A.5
  • 24
    • 0037434791 scopus 로고    scopus 로고
    • Structure of the extracellular region of HER2 alone and in complex with the Herceptin Fab
    • Cho HS, Mason K, Ramyar KX, Stanley AM, Gabelli SB, et al. (2003) Structure of the extracellular region of HER2 alone and in complex with the Herceptin Fab. Nature 421: 756-760.
    • (2003) Nature , vol.421 , pp. 756-760
    • Cho, H.S.1    Mason, K.2    Ramyar, K.X.3    Stanley, A.M.4    Gabelli, S.B.5
  • 25
    • 0027228495 scopus 로고
    • Thermodynamic analysis of an antibody functional epitope
    • Kelley RF, O'Connell MP, (1993) Thermodynamic analysis of an antibody functional epitope. Biochemistry 32: 6828-6835.
    • (1993) Biochemistry , vol.32 , pp. 6828-6835
    • Kelley, R.F.1    O'Connell, M.P.2
  • 26
    • 0026708489 scopus 로고
    • Antigen binding thermodynamics and antiproliferative effects of chimeric and humanized anti-p185HER2 antibody Fab fragments
    • Kelley RF, O'Connell MP, Carter P, Presta L, Eigenbrot C, et al. (1992) Antigen binding thermodynamics and antiproliferative effects of chimeric and humanized anti-p185HER2 antibody Fab fragments. Biochemistry 31: 5434-5441.
    • (1992) Biochemistry , vol.31 , pp. 5434-5441
    • Kelley, R.F.1    O'Connell, M.P.2    Carter, P.3    Presta, L.4    Eigenbrot, C.5
  • 27
    • 33847416982 scopus 로고    scopus 로고
    • A broad range of Fab stabilities within a host of therapeutic IgGs
    • Garber E, Demarest SJ, (2007) A broad range of Fab stabilities within a host of therapeutic IgGs. Biochem Biophys Res Commun 355: 751-757.
    • (2007) Biochem Biophys Res Commun , vol.355 , pp. 751-757
    • Garber, E.1    Demarest, S.J.2
  • 28
    • 33644783935 scopus 로고    scopus 로고
    • Tyrosine plays a dominant functional role in the paratope of a synthetic antibody derived from a four amino acid code
    • Fellouse FA, Barthelemy PA, Kelley RF, Sidhu SS, (2006) Tyrosine plays a dominant functional role in the paratope of a synthetic antibody derived from a four amino acid code. J Mol Biol 357: 100-114.
    • (2006) J Mol Biol , vol.357 , pp. 100-114
    • Fellouse, F.A.1    Barthelemy, P.A.2    Kelley, R.F.3    Sidhu, S.S.4
  • 29
    • 0028809265 scopus 로고
    • Configurational effects in antibody-antigen interactions studied by microcalorimetry
    • Murphy KP, Freire E, Paterson Y, (1995) Configurational effects in antibody-antigen interactions studied by microcalorimetry. Proteins 21: 83-90.
    • (1995) Proteins , vol.21 , pp. 83-90
    • Murphy, K.P.1    Freire, E.2    Paterson, Y.3
  • 30
    • 0003920544 scopus 로고
    • Handbook of biochemistry and molecular biology, 3d edition
    • CRC Press, Cleveland
    • Fasman G, Sober H, Company CR, (1976) Handbook of biochemistry and molecular biology, 3d edition. CRC Press, Cleveland.
    • (1976)
    • Fasman, G.1    Sober, H.2    Company, C.R.3
  • 31
    • 0031670461 scopus 로고    scopus 로고
    • Enthalpy and heat capacity changes for the proton dissociation of various buffer components in 0.1 M potassium chloride
    • Fukada H, Takahashi K, (1998) Enthalpy and heat capacity changes for the proton dissociation of various buffer components in 0.1 M potassium chloride. Proteins 33: 159-166.
    • (1998) Proteins , vol.33 , pp. 159-166
    • Fukada, H.1    Takahashi, K.2
  • 32
    • 0025906146 scopus 로고
    • Contribution to the thermodynamics of protein folding from the reduction in water-accessible nonpolar surface area
    • Livingstone JR, Spolar RS, Record MT Jr, (1991) Contribution to the thermodynamics of protein folding from the reduction in water-accessible nonpolar surface area. Biochemistry 30: 4237-4244.
    • (1991) Biochemistry , vol.30 , pp. 4237-4244
    • Livingstone, J.R.1    Spolar, R.S.2    Record Jr., M.T.3
  • 33
    • 0348047600 scopus 로고    scopus 로고
    • Evidence that structural rearrangements and/or flexibility during TCR binding can contribute to T cell activation
    • Krogsgaard M, Prado N, Adams EJ, He XL, Chow DC, et al. (2003) Evidence that structural rearrangements and/or flexibility during TCR binding can contribute to T cell activation. Mol Cell 12: 1367-1378.
    • (2003) Mol Cell , vol.12 , pp. 1367-1378
    • Krogsgaard, M.1    Prado, N.2    Adams, E.J.3    He, X.L.4    Chow, D.C.5
  • 34
    • 0029080688 scopus 로고
    • Thermodynamic and kinetic characterization of the binding of the TATA binding protein to the adenovirus E4 promoter
    • Petri V, Hsieh M, Brenowitz M, (1995) Thermodynamic and kinetic characterization of the binding of the TATA binding protein to the adenovirus E4 promoter. Biochemistry 34: 9977-9984.
    • (1995) Biochemistry , vol.34 , pp. 9977-9984
    • Petri, V.1    Hsieh, M.2    Brenowitz, M.3
  • 35
    • 0347423200 scopus 로고    scopus 로고
    • Thermodynamic analysis of degenerate recognition by the NKG2D immunoreceptor: not induced fit but rigid adaptation
    • McFarland BJ, Strong RK, (2003) Thermodynamic analysis of degenerate recognition by the NKG2D immunoreceptor: not induced fit but rigid adaptation. Immunity 19: 803-812.
    • (2003) Immunity , vol.19 , pp. 803-812
    • McFarland, B.J.1    Strong, R.K.2
  • 36
    • 0028127923 scopus 로고
    • Entropy in biological binding processes: estimation of translational entropy loss
    • Murphy KP, Xie D, Thompson KS, Amzel LM, Freire E, (1994) Entropy in biological binding processes: estimation of translational entropy loss. Proteins 18: 63-67.
    • (1994) Proteins , vol.18 , pp. 63-67
    • Murphy, K.P.1    Xie, D.2    Thompson, K.S.3    Amzel, L.M.4    Freire, E.5
  • 37
    • 46849122649 scopus 로고    scopus 로고
    • Exploring the energy landscape of antibody-antigen complexes: protein dynamics, flexibility, and molecular recognition
    • Thielges MC, Zimmermann J, Yu W, Oda M, Romesberg FE, (2008) Exploring the energy landscape of antibody-antigen complexes: protein dynamics, flexibility, and molecular recognition. Biochemistry 47: 7237-7247.
    • (2008) Biochemistry , vol.47 , pp. 7237-7247
    • Thielges, M.C.1    Zimmermann, J.2    Yu, W.3    Oda, M.4    Romesberg, F.E.5
  • 38
    • 0030795733 scopus 로고    scopus 로고
    • Vascular endothelial growth factor: crystal structure and functional mapping of the kinase domain receptor binding site
    • Muller YA, Li B, Christinger HW, Wells JA, Cunningham BC, et al. (1997) Vascular endothelial growth factor: crystal structure and functional mapping of the kinase domain receptor binding site. Proc Natl Acad Sci U S A 94: 7192-7197.
    • (1997) Proc Natl Acad Sci U S A , vol.94 , pp. 7192-7197
    • Muller, Y.A.1    Li, B.2    Christinger, H.W.3    Wells, J.A.4    Cunningham, B.C.5
  • 39
    • 0029887430 scopus 로고    scopus 로고
    • Analysis of cell-adhesion molecule interactions using surface plasmon resonance
    • van der Merwe PA, Barclay AN, (1996) Analysis of cell-adhesion molecule interactions using surface plasmon resonance. Curr Opin Immunol 8: 257-261.
    • (1996) Curr Opin Immunol , vol.8 , pp. 257-261
    • van der Merwe, P.A.1    Barclay, A.N.2
  • 40
    • 0033103834 scopus 로고    scopus 로고
    • TCR binding to peptide-MHC stabilizes a flexible recognition interface
    • Willcox BE, Gao GF, Wyer JR, Ladbury JE, Bell JI, et al. (1999) TCR binding to peptide-MHC stabilizes a flexible recognition interface. Immunity 10: 357-365.
    • (1999) Immunity , vol.10 , pp. 357-365
    • Willcox, B.E.1    Gao, G.F.2    Wyer, J.R.3    Ladbury, J.E.4    Bell, J.I.5
  • 41
    • 0033613074 scopus 로고    scopus 로고
    • Thermodynamics of T cell receptor binding to peptide-MHC: evidence for a general mechanism of molecular scanning
    • Boniface JJ, Reich Z, Lyons DS, Davis MM, (1999) Thermodynamics of T cell receptor binding to peptide-MHC: evidence for a general mechanism of molecular scanning. Proc Natl Acad Sci U S A 96: 11446-11451.
    • (1999) Proc Natl Acad Sci U S A , vol.96 , pp. 11446-11451
    • Boniface, J.J.1    Reich, Z.2    Lyons, D.S.3    Davis, M.M.4
  • 42
    • 0141527338 scopus 로고    scopus 로고
    • Convergent mechanisms for recognition of divergent cytokines by the shared signaling receptor gp130
    • Boulanger MJ, Bankovich AJ, Kortemme T, Baker D, Garcia KC, (2003) Convergent mechanisms for recognition of divergent cytokines by the shared signaling receptor gp130. Mol Cell 12: 577-589.
    • (2003) Mol Cell , vol.12 , pp. 577-589
    • Boulanger, M.J.1    Bankovich, A.J.2    Kortemme, T.3    Baker, D.4    Garcia, K.C.5
  • 44
    • 0036420965 scopus 로고    scopus 로고
    • Molecular recognition in antibody-antigen complexes
    • Sundberg EJ, Mariuzza RA, (2002) Molecular recognition in antibody-antigen complexes. Adv Protein Chem 61: 119-160.
    • (2002) Adv Protein Chem , vol.61 , pp. 119-160
    • Sundberg, E.J.1    Mariuzza, R.A.2
  • 46
    • 58649114309 scopus 로고    scopus 로고
    • The molecular basis of TCR germline bias for MHC is surprisingly simple
    • Garcia KC, Adams JJ, Feng D, Ely LK, (2009) The molecular basis of TCR germline bias for MHC is surprisingly simple. Nat Immunol 10: 143-147.
    • (2009) Nat Immunol , vol.10 , pp. 143-147
    • Garcia, K.C.1    Adams, J.J.2    Feng, D.3    Ely, L.K.4
  • 49
    • 49549102657 scopus 로고    scopus 로고
    • Understanding mechanisms governing protein-protein interactions from synthetic binding interfaces
    • Kossiakoff AA, Koide S, (2008) Understanding mechanisms governing protein-protein interactions from synthetic binding interfaces. Curr Opin Struct Biol 18: 499-506.
    • (2008) Curr Opin Struct Biol , vol.18 , pp. 499-506
    • Kossiakoff, A.A.1    Koide, S.2
  • 51
    • 0034681465 scopus 로고    scopus 로고
    • Convergent solutions to binding at a protein-protein interface
    • DeLano WL, Ultsch MH, de Vos AM, Wells JA, (2000) Convergent solutions to binding at a protein-protein interface. Science 287: 1279-1283.
    • (2000) Science , vol.287 , pp. 1279-1283
    • DeLano, W.L.1    Ultsch, M.H.2    de Vos, A.M.3    Wells, J.A.4
  • 53
    • 0032530717 scopus 로고    scopus 로고
    • VEGF and the Fab fragment of a humanized neutralizing antibody: crystal structure of the complex at 2.4 A resolution and mutational analysis of the interface
    • Muller YA, Chen Y, Christinger HW, Li B, Cunningham BC, et al. (1998) VEGF and the Fab fragment of a humanized neutralizing antibody: crystal structure of the complex at 2.4 A resolution and mutational analysis of the interface. Structure 6: 1153-1167.
    • (1998) Structure , vol.6 , pp. 1153-1167
    • Muller, Y.A.1    Chen, Y.2    Christinger, H.W.3    Li, B.4    Cunningham, B.C.5
  • 54
    • 1842605531 scopus 로고    scopus 로고
    • Insights into ErbB signaling from the structure of the ErbB2-pertuzumab complex
    • Franklin MC, Carey KD, Vajdos FF, Leahy DJ, de Vos AM, et al. (2004) Insights into ErbB signaling from the structure of the ErbB2-pertuzumab complex. Cancer Cell 5: 317-328.
    • (2004) Cancer Cell , vol.5 , pp. 317-328
    • Franklin, M.C.1    Carey, K.D.2    Vajdos, F.F.3    Leahy, D.J.4    de Vos, A.M.5
  • 55
    • 13244277757 scopus 로고    scopus 로고
    • Interpretation of the temperature dependence of rate constants in biosensor studies
    • Winzor DJ, Jackson CM, (2005) Interpretation of the temperature dependence of rate constants in biosensor studies. Anal Biochem 337: 289-293.
    • (2005) Anal Biochem , vol.337 , pp. 289-293
    • Winzor, D.J.1    Jackson, C.M.2
  • 56
    • 0023613953 scopus 로고
    • Rapid and efficient site-specific mutagenesis without phenotypic selection
    • Kunkel TA, Roberts JD, Zakour RA, (1987) Rapid and efficient site-specific mutagenesis without phenotypic selection. Methods Enzymol 154: 367-382.
    • (1987) Methods Enzymol , vol.154 , pp. 367-382
    • Kunkel, T.A.1    Roberts, J.D.2    Zakour, R.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.