메뉴 건너뛰기




Volumn 398, Issue 2, 2010, Pages 214-231

Human Framework Adaptation of a Mouse Anti-Human IL-13 Antibody

Author keywords

Affinity maturation; Antibody engineering; Humanization; Phage display; X ray crystallography

Indexed keywords

HYDROGEN; INTERLEUKIN 13 ANTIBODY; NEUTRALIZING ANTIBODY;

EID: 77951762065     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2010.03.004     Document Type: Article
Times cited : (36)

References (60)
  • 1
    • 38449104580 scopus 로고    scopus 로고
    • Humanization of antibodies
    • Almagro J.C., Fransson J. Humanization of antibodies. Front. Biosci. 2008, 13:1619-1633.
    • (2008) Front. Biosci. , vol.13 , pp. 1619-1633
    • Almagro, J.C.1    Fransson, J.2
  • 2
    • 0021716682 scopus 로고
    • Chimeric human antibody molecules: mouse antigen-binding domains with human constant region domains
    • Morrison S.L., Johnson M.J., Herzenberg L.A., Oi V.T. Chimeric human antibody molecules: mouse antigen-binding domains with human constant region domains. Proc. Natl Acad. Sci. USA 1984, 81:6851-6855.
    • (1984) Proc. Natl Acad. Sci. USA , vol.81 , pp. 6851-6855
    • Morrison, S.L.1    Johnson, M.J.2    Herzenberg, L.A.3    Oi, V.T.4
  • 3
    • 15944365883 scopus 로고    scopus 로고
    • A review of human anti-globulin antibody (HAGA, HAMA, HACA, HAHA) responses to monoclonal antibodies. Not four letter words
    • Mirick G.R., Bradt B.M., Denardo S.J., Denardo G.L. A review of human anti-globulin antibody (HAGA, HAMA, HACA, HAHA) responses to monoclonal antibodies. Not four letter words. Q. J. Nucl. Med. Mol. Imaging 2004, 48:251-257.
    • (2004) Q. J. Nucl. Med. Mol. Imaging , vol.48 , pp. 251-257
    • Mirick, G.R.1    Bradt, B.M.2    Denardo, S.J.3    Denardo, G.L.4
  • 4
    • 0042305160 scopus 로고    scopus 로고
    • Consequences of immunogenicity to the therapeutic monoclonal antibodies ReoPro and Remicade
    • Wagner C.L., Schantz A., Barnathan E., Olson A., Mascelli M.A., Ford J., et al. Consequences of immunogenicity to the therapeutic monoclonal antibodies ReoPro and Remicade. Dev. Biol. (Basel) 2003, 112:37-53.
    • (2003) Dev. Biol. (Basel) , vol.112 , pp. 37-53
    • Wagner, C.L.1    Schantz, A.2    Barnathan, E.3    Olson, A.4    Mascelli, M.A.5    Ford, J.6
  • 5
    • 0032791210 scopus 로고    scopus 로고
    • Extended rituximab (anti-CD20 monoclonal antibody) therapy for relapsed or refractory low-grade or follicular non-Hodgkin's lymphoma
    • Piro L.D., White C.A., Grillo-Lopez A.J., Janakiraman N., Saven A., Beck T.M., et al. Extended rituximab (anti-CD20 monoclonal antibody) therapy for relapsed or refractory low-grade or follicular non-Hodgkin's lymphoma. Ann. Oncol. 1999, 10:655-661.
    • (1999) Ann. Oncol. , vol.10 , pp. 655-661
    • Piro, L.D.1    White, C.A.2    Grillo-Lopez, A.J.3    Janakiraman, N.4    Saven, A.5    Beck, T.M.6
  • 7
    • 0022558297 scopus 로고
    • Replacing the complementarity-determining regions in a human antibody with those from a mouse
    • Jones P.T., Dear P.H., Foote J., Neuberger M.S., Winter G. Replacing the complementarity-determining regions in a human antibody with those from a mouse. Nature 1986, 321:522-525.
    • (1986) Nature , vol.321 , pp. 522-525
    • Jones, P.T.1    Dear, P.H.2    Foote, J.3    Neuberger, M.S.4    Winter, G.5
  • 9
    • 0036683449 scopus 로고    scopus 로고
    • Phase II trial of subcutaneous anti-CD52 monoclonal antibody alemtuzumab (Campath-1H) as first-line treatment for patients with B-cell chronic lymphocytic leukemia (B-CLL)
    • Lundin J., Kimby E., Bjorkholm M., Broliden P.A., Celsing F., Hjalmar V., et al. Phase II trial of subcutaneous anti-CD52 monoclonal antibody alemtuzumab (Campath-1H) as first-line treatment for patients with B-cell chronic lymphocytic leukemia (B-CLL). Blood 2002, 100:768-773.
    • (2002) Blood , vol.100 , pp. 768-773
    • Lundin, J.1    Kimby, E.2    Bjorkholm, M.3    Broliden, P.A.4    Celsing, F.5    Hjalmar, V.6
  • 12
    • 17644422139 scopus 로고    scopus 로고
    • Use of human germline genes in a CDR homology-based approach to antibody humanization
    • Hwang W.Y., Almagro J.C., Buss T.N., Tan P., Foote J. Use of human germline genes in a CDR homology-based approach to antibody humanization. Methods 2005, 36:35-42.
    • (2005) Methods , vol.36 , pp. 35-42
    • Hwang, W.Y.1    Almagro, J.C.2    Buss, T.N.3    Tan, P.4    Foote, J.5
  • 13
    • 0026559783 scopus 로고
    • Antibody framework residues affecting the conformation of the hypervariable loops
    • Foote J., Winter G. Antibody framework residues affecting the conformation of the hypervariable loops. J. Mol. Biol. 1992, 224:487-499.
    • (1992) J. Mol. Biol. , vol.224 , pp. 487-499
    • Foote, J.1    Winter, G.2
  • 14
    • 35349014634 scopus 로고    scopus 로고
    • Affinity maturation increases the stability and plasticity of the Fv domain of anti-protein antibodies
    • Acierno J.P., Braden B.C., Klinke S., Goldbaum F.A., Cauerhff A. Affinity maturation increases the stability and plasticity of the Fv domain of anti-protein antibodies. J. Mol. Biol. 2007, 374:130-146.
    • (2007) J. Mol. Biol. , vol.374 , pp. 130-146
    • Acierno, J.P.1    Braden, B.C.2    Klinke, S.3    Goldbaum, F.A.4    Cauerhff, A.5
  • 15
    • 0030821164 scopus 로고    scopus 로고
    • Structural insights into the evolution of an antibody combining site
    • Wedemayer G.J., Patten P.A., Wang L.H., Schultz P.G., Stevens R.C. Structural insights into the evolution of an antibody combining site. Science 1997, 276:1665-1669.
    • (1997) Science , vol.276 , pp. 1665-1669
    • Wedemayer, G.J.1    Patten, P.A.2    Wang, L.H.3    Schultz, P.G.4    Stevens, R.C.5
  • 16
    • 0038103565 scopus 로고    scopus 로고
    • X-ray snapshots of the maturation of an antibody response to a protein antigen
    • Li Y., Li H., Yang F., Smith-Gill S., Mariuzza R. X-ray snapshots of the maturation of an antibody response to a protein antigen. Nat. Struct. Biol. 2003, 482-488.
    • (2003) Nat. Struct. Biol. , pp. 482-488
    • Li, Y.1    Li, H.2    Yang, F.3    Smith-Gill, S.4    Mariuzza, R.5
  • 18
    • 0028348564 scopus 로고
    • In vitro evolution of a neutralizing human antibody to human immunodeficiency virus type 1 to enhance affinity and broaden strain cross-reactivity
    • Barbas C.F.R., Hu D., Dunlop N., Sawyer L., Cababa D., Hendry R.M., et al. In vitro evolution of a neutralizing human antibody to human immunodeficiency virus type 1 to enhance affinity and broaden strain cross-reactivity. Proc. Natl Acad. Sci. USA 1994, 91:3809-3813.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 3809-3813
    • Barbas, C.F.R.1    Hu, D.2    Dunlop, N.3    Sawyer, L.4    Cababa, D.5    Hendry, R.M.6
  • 19
    • 0032564346 scopus 로고    scopus 로고
    • Ribosome display efficiently selects and evolves high-affinity antibodies in vitro from immune libraries
    • Hanes J., Jermutus L., Weber-Bornhauser S., Bosshard H.R., Pluckthun A. Ribosome display efficiently selects and evolves high-affinity antibodies in vitro from immune libraries. Proc. Natl Acad. Sci. USA 1998, 95:14130-14135.
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 14130-14135
    • Hanes, J.1    Jermutus, L.2    Weber-Bornhauser, S.3    Bosshard, H.R.4    Pluckthun, A.5
  • 20
    • 4744369286 scopus 로고    scopus 로고
    • Substantial energetic improvement with minimal structural perturbation in a high affinity mutant antibody
    • Midelfort K.S., Hernandez H.H., Lippow S.M., Tidor B., Drennan C.L., Wittrup K.D. Substantial energetic improvement with minimal structural perturbation in a high affinity mutant antibody. J. Mol. Biol. 2004, 343:685-701.
    • (2004) J. Mol. Biol. , vol.343 , pp. 685-701
    • Midelfort, K.S.1    Hernandez, H.H.2    Lippow, S.M.3    Tidor, B.4    Drennan, C.L.5    Wittrup, K.D.6
  • 21
    • 0027768856 scopus 로고
    • The contribution of contact and non-contact residues of antibody in the affinity of binding to antigen. The interaction of mutant D1.3 antibodies with lysozyme
    • Hawkins R.E., Russell S.J., Baier M., Winter G. The contribution of contact and non-contact residues of antibody in the affinity of binding to antigen. The interaction of mutant D1.3 antibodies with lysozyme. J. Mol. Biol. 1993, 234:958-964.
    • (1993) J. Mol. Biol. , vol.234 , pp. 958-964
    • Hawkins, R.E.1    Russell, S.J.2    Baier, M.3    Winter, G.4
  • 22
    • 0026699293 scopus 로고
    • Selection of phage antibodies by binding affinity. Mimicking affinity maturation
    • Hawkins R.E., Russell S.J., Winter G. Selection of phage antibodies by binding affinity. Mimicking affinity maturation. J. Mol. Biol. 1992, 226:889-896.
    • (1992) J. Mol. Biol. , vol.226 , pp. 889-896
    • Hawkins, R.E.1    Russell, S.J.2    Winter, G.3
  • 23
    • 0026343486 scopus 로고
    • Selecting high-affinity binding proteins by monovalent phage display
    • Lowman H.B., Bass S.H., Simpson N., Wells J.A. Selecting high-affinity binding proteins by monovalent phage display. Biochemistry 1991, 30:10832-10838.
    • (1991) Biochemistry , vol.30 , pp. 10832-10838
    • Lowman, H.B.1    Bass, S.H.2    Simpson, N.3    Wells, J.A.4
  • 24
    • 64649099284 scopus 로고    scopus 로고
    • Affinity maturation of a humanized rat antibody for anti-RAGE therapy: comprehensive mutagenesis reveals a high level of mutational plasticity both inside and outside the complementarity-determining regions
    • Finlay W.J., Cunningham O., Lambert M.A., Darmanin-Sheehan A., Liu X., Fennell B.J., et al. Affinity maturation of a humanized rat antibody for anti-RAGE therapy: comprehensive mutagenesis reveals a high level of mutational plasticity both inside and outside the complementarity-determining regions. J. Mol. Biol. 2009, 388:541-558.
    • (2009) J. Mol. Biol. , vol.388 , pp. 541-558
    • Finlay, W.J.1    Cunningham, O.2    Lambert, M.A.3    Darmanin-Sheehan, A.4    Liu, X.5    Fennell, B.J.6
  • 26
    • 0035967886 scopus 로고    scopus 로고
    • Solution structure of human IL-13 and implication for receptor binding
    • Moy F.J., Diblasio E., Wilhelm J., Powers R. Solution structure of human IL-13 and implication for receptor binding. J. Mol. Biol. 2001, 310:219-230.
    • (2001) J. Mol. Biol. , vol.310 , pp. 219-230
    • Moy, F.J.1    Diblasio, E.2    Wilhelm, J.3    Powers, R.4
  • 28
    • 0034808223 scopus 로고    scopus 로고
    • Identification and association of polymorphisms in the interleukin-13 gene with asthma and atopy in a Dutch population
    • Howard T.D., Whittaker P.A., Zaiman A.L., Koppelman G.H., Xu J., Hanley M.T., et al. Identification and association of polymorphisms in the interleukin-13 gene with asthma and atopy in a Dutch population. Am. J. Respir. Cell. Mol. Biol. 2001, 25:377-384.
    • (2001) Am. J. Respir. Cell. Mol. Biol. , vol.25 , pp. 377-384
    • Howard, T.D.1    Whittaker, P.A.2    Zaiman, A.L.3    Koppelman, G.H.4    Xu, J.5    Hanley, M.T.6
  • 29
    • 9644276704 scopus 로고    scopus 로고
    • Anti-IL-13 monoclonal antibody inhibits airway hyperresponsiveness, inflammation and airway remodeling
    • Yang G., Volk A., Petley T., Emmell E., Giles-Komar J., Shang X., et al. Anti-IL-13 monoclonal antibody inhibits airway hyperresponsiveness, inflammation and airway remodeling. Cytokine 2004, 28:224-232.
    • (2004) Cytokine , vol.28 , pp. 224-232
    • Yang, G.1    Volk, A.2    Petley, T.3    Emmell, E.4    Giles-Komar, J.5    Shang, X.6
  • 31
    • 1642307201 scopus 로고    scopus 로고
    • Identification of differences in the specificity-determining residues of antibodies that recognize antigens of different size: implications for the rational design of antibody repertoires
    • Almagro J.C. Identification of differences in the specificity-determining residues of antibodies that recognize antigens of different size: implications for the rational design of antibody repertoires. J. Mol. Recognit. 2004, 17:132-143.
    • (2004) J. Mol. Recognit. , vol.17 , pp. 132-143
    • Almagro, J.C.1
  • 32
    • 0016756272 scopus 로고
    • Continuous cultures of fused cells secreting antibody of predefined specificity
    • Kohler G., Milstein C. Continuous cultures of fused cells secreting antibody of predefined specificity. Nature 1975, 256:495-497.
    • (1975) Nature , vol.256 , pp. 495-497
    • Kohler, G.1    Milstein, C.2
  • 33
    • 0034102759 scopus 로고    scopus 로고
    • A cluster of seven tightly linked polymorphisms in the IL-13 gene is associated with total serum IgE levels in three populations of white children
    • Graves P.E., Kabesch M., Halonen M., Holberg C.J., Baldini M., Fritzsch C., et al. A cluster of seven tightly linked polymorphisms in the IL-13 gene is associated with total serum IgE levels in three populations of white children. J. Allergy Clin. Immunol. 2000, 105:506-513.
    • (2000) J. Allergy Clin. Immunol. , vol.105 , pp. 506-513
    • Graves, P.E.1    Kabesch, M.2    Halonen, M.3    Holberg, C.J.4    Baldini, M.5    Fritzsch, C.6
  • 36
    • 0023278330 scopus 로고
    • Canonical structures for the hypervariable regions of immunoglobulins
    • Chothia C., Lesk A.M. Canonical structures for the hypervariable regions of immunoglobulins. J. Mol. Biol. 1987, 196:901-917.
    • (1987) J. Mol. Biol. , vol.196 , pp. 901-917
    • Chothia, C.1    Lesk, A.M.2
  • 39
    • 0031558798 scopus 로고    scopus 로고
    • Standard conformations for the canonical structures of immunoglobulins
    • Al-Lazikani B., Lesk A.M., Chothia C. Standard conformations for the canonical structures of immunoglobulins. J. Mol. Biol. 1997, 273:927-948.
    • (1997) J. Mol. Biol. , vol.273 , pp. 927-948
    • Al-Lazikani, B.1    Lesk, A.M.2    Chothia, C.3
  • 40
    • 0024403619 scopus 로고
    • High-resolution epitope mapping of hGH-receptor interactions by alanine-scanning mutagenesis
    • Cunningham B.C., Wells J.A. High-resolution epitope mapping of hGH-receptor interactions by alanine-scanning mutagenesis. Science 1989, 244:1081-1085.
    • (1989) Science , vol.244 , pp. 1081-1085
    • Cunningham, B.C.1    Wells, J.A.2
  • 41
    • 0016374802 scopus 로고
    • Variable region sequences of five human immunoglobulin heavy chains of the VHTTI subgroup: definitive identification of four heavy chain hypervariable regions (myeloma proteins/amino acid sequences/antibody combining site)
    • Capra J.D., Kehoe M. Variable region sequences of five human immunoglobulin heavy chains of the VHTTI subgroup: definitive identification of four heavy chain hypervariable regions (myeloma proteins/amino acid sequences/antibody combining site). Proc. Natl Acad. Sci. USA 1974, 71:845-848.
    • (1974) Proc. Natl Acad. Sci. USA , vol.71 , pp. 845-848
    • Capra, J.D.1    Kehoe, M.2
  • 42
    • 17144404243 scopus 로고    scopus 로고
    • A structure-based database of antibody variable domain diversity
    • Bond C.J., Wiesmann C., Marsters J.C.J., Sidhu S.S. A structure-based database of antibody variable domain diversity. J. Mol. Biol. 2005, 348:699-709.
    • (2005) J. Mol. Biol. , vol.348 , pp. 699-709
    • Bond, C.J.1    Wiesmann, C.2    Marsters, J.C.J.3    Sidhu, S.S.4
  • 43
    • 0030993418 scopus 로고    scopus 로고
    • Antibody humanization using monovalent phage display
    • Baca M., Presta L.G., O'Connor J., Wells J.A. Antibody humanization using monovalent phage display. J. Biol. Chem. 1997, 272:10678-10684.
    • (1997) J. Biol. Chem. , vol.272 , pp. 10678-10684
    • Baca, M.1    Presta, L.G.2    O'Connor, J.3    Wells, J.A.4
  • 44
    • 0031091762 scopus 로고    scopus 로고
    • Structural consequences of humanizing an antibody
    • Holmes M.A., Foote J. Structural consequences of humanizing an antibody. J. Immunol. 1997, 158:2192-2201.
    • (1997) J. Immunol. , vol.158 , pp. 2192-2201
    • Holmes, M.A.1    Foote, J.2
  • 46
    • 0032568558 scopus 로고    scopus 로고
    • Stepwise in vitro affinity maturation of Vitaxin, an alphav beta3-specific humanized mAb
    • Wu H., Beuerlein G., Nie Y., Smith H., Lee B.A., Hensler M., et al. Stepwise in vitro affinity maturation of Vitaxin, an alphav beta3-specific humanized mAb. Proc. Natl Acad. Sci. USA 1998, 95:6037-6042.
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 6037-6042
    • Wu, H.1    Beuerlein, G.2    Nie, Y.3    Smith, H.4    Lee, B.A.5    Hensler, M.6
  • 47
    • 34047143155 scopus 로고    scopus 로고
    • Development of motavizumab, an ultra-potent antibody for the prevention of respiratory syncytial virus infection in the upper and lower respiratory tract
    • Wu H., Pfarr D.S., Johnson S., Brewah Y.A., Woods R.M., Patel N.K., et al. Development of motavizumab, an ultra-potent antibody for the prevention of respiratory syncytial virus infection in the upper and lower respiratory tract. J. Mol. Biol. 2007, 368:652-665.
    • (2007) J. Mol. Biol. , vol.368 , pp. 652-665
    • Wu, H.1    Pfarr, D.S.2    Johnson, S.3    Brewah, Y.A.4    Woods, R.M.5    Patel, N.K.6
  • 48
    • 45149093866 scopus 로고    scopus 로고
    • Affinity maturation of an anti-hepatitis B virus PreS1 humanized antibody by phage display
    • Yang G.H., Yoon S.O., Jang M.H., Hong H.J. Affinity maturation of an anti-hepatitis B virus PreS1 humanized antibody by phage display. J. Microbiol. 2007, 45:528-533.
    • (2007) J. Microbiol. , vol.45 , pp. 528-533
    • Yang, G.H.1    Yoon, S.O.2    Jang, M.H.3    Hong, H.J.4
  • 49
    • 33646382846 scopus 로고    scopus 로고
    • Construction, affinity maturation, and biological characterization of an anti-tumor-associated glycoprotein-72 humanized antibody
    • Yoon S.O., Lee T.S., Kim S.J., Jang M.H., Kang Y.J., Park J.H., et al. Construction, affinity maturation, and biological characterization of an anti-tumor-associated glycoprotein-72 humanized antibody. J. Biol. Chem. 2006, 281:6985-6992.
    • (2006) J. Biol. Chem. , vol.281 , pp. 6985-6992
    • Yoon, S.O.1    Lee, T.S.2    Kim, S.J.3    Jang, M.H.4    Kang, Y.J.5    Park, J.H.6
  • 50
    • 0028798104 scopus 로고
    • Identification of specificity-determining residues in antibodies
    • Padlan E.A., Abergel C., Tipper J.P. Identification of specificity-determining residues in antibodies. FASEB J. 1995, 9:133-139.
    • (1995) FASEB J. , vol.9 , pp. 133-139
    • Padlan, E.A.1    Abergel, C.2    Tipper, J.P.3
  • 51
    • 0033527584 scopus 로고    scopus 로고
    • Selection and analysis of an optimized anti-VEGF antibody: crystal structure of an affinity-matured Fab in complex with antigen
    • Chen Y., Wiesmann C., Fuh G., Li B., Christinger H.W., McKay P., et al. Selection and analysis of an optimized anti-VEGF antibody: crystal structure of an affinity-matured Fab in complex with antigen. J. Mol. Biol. 1999, 293:865-881.
    • (1999) J. Mol. Biol. , vol.293 , pp. 865-881
    • Chen, Y.1    Wiesmann, C.2    Fuh, G.3    Li, B.4    Christinger, H.W.5    McKay, P.6
  • 52
    • 0026458378 scopus 로고
    • Amino acid substitution matrices from protein blocks
    • Henikoff S., Henikoff J.G. Amino acid substitution matrices from protein blocks. Proc. Natl Acad. Sci. USA 1992, 89:10915-10919.
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , pp. 10915-10919
    • Henikoff, S.1    Henikoff, J.G.2
  • 54
    • 1642397503 scopus 로고    scopus 로고
    • Selection of human antibodies from phage display libraries
    • Marks J.D., Bradbury A. Selection of human antibodies from phage display libraries. Methods Mol. Biol. 2004, 248:161-176.
    • (2004) Methods Mol. Biol. , vol.248 , pp. 161-176
    • Marks, J.D.1    Bradbury, A.2
  • 55
    • 7444264009 scopus 로고    scopus 로고
    • Microseed matrix screening to improve crystals of yeast cytosine deaminase
    • Ireton G.C., Stoddard B.L. Microseed matrix screening to improve crystals of yeast cytosine deaminase. Acta Crystallogr. Sect. D 2004, 60:601-605.
    • (2004) Acta Crystallogr. Sect. D , vol.60 , pp. 601-605
    • Ireton, G.C.1    Stoddard, B.L.2
  • 56
    • 0035788107 scopus 로고    scopus 로고
    • Pushing the boundaries of molecular replacement with maximum likelihood
    • Read R.J. Pushing the boundaries of molecular replacement with maximum likelihood. Acta Crystallogr. Sect. D 2001, 57:1373-1382.
    • (2001) Acta Crystallogr. Sect. D , vol.57 , pp. 1373-1382
    • Read, R.J.1
  • 58
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • Murshudov G.N., Vagin A.A., Dodson E.J. Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr. Sect. D 1997, 53:240-255.
    • (1997) Acta Crystallogr. Sect. D , vol.53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 59
    • 0028103275 scopus 로고
    • The CCP4 suite: programs for protein crystallography
    • CCP4
    • The CCP4 suite: programs for protein crystallography. Acta Crystallogr. Sect. D 1994, 50:760-763. CCP4.
    • (1994) Acta Crystallogr. Sect. D , vol.50 , pp. 760-763
  • 60
    • 13244281317 scopus 로고    scopus 로고
    • Coot: model-building tools for molecular graphics
    • Emsley P., Cowtan K. Coot: model-building tools for molecular graphics. Acta Crystallogr. Sect. D 2004, 60:2126-2132.
    • (2004) Acta Crystallogr. Sect. D , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.