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Volumn 335, Issue 4, 2004, Pages 1007-1018

Evolution of Aldolase Antibodies in Vitro: Correlation of Catalytic Activity and Reaction-based Selection

Author keywords

Aldolase antibody; Catalytic antibody; Enamine; In vitro evolution; Phage display

Indexed keywords

ALDOLASE ANTIBODY; ALDOLASE ANTIBODY 33F12; ALDOLASE ANTIBODY 38C2; AMINO ACID DERIVATIVE; CATALYTIC ANTIBODY; ENAMINE; IMMUNOGLOBULIN F(AB) FRAGMENT; KETONE DERIVATIVE; LYSINE DERIVATIVE; UNCLASSIFIED DRUG;

EID: 0345862284     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2003.11.014     Document Type: Article
Times cited : (34)

References (61)
  • 1
    • 0028817877 scopus 로고
    • From molecular diversity to catalysis: Lessons from the immune system
    • Schultz P.G., Lerner R.A. From molecular diversity to catalysis: lessons from the immune system. Science. 269:1995;1835-1842.
    • (1995) Science , vol.269 , pp. 1835-1842
    • Schultz, P.G.1    Lerner, R.A.2
  • 2
    • 0033791659 scopus 로고    scopus 로고
    • Critical analysis of antibody catalysis
    • Hilvert D. Critical analysis of antibody catalysis. Annu. Rev. Biochem. 69:2000;751-793.
    • (2000) Annu. Rev. Biochem. , vol.69 , pp. 751-793
    • Hilvert, D.1
  • 5
    • 0036882403 scopus 로고    scopus 로고
    • Catalytic antibodies as designer proteases and esterases
    • Tanaka F. Catalytic antibodies as designer proteases and esterases. Chem. Rev. 102:2002;4885-4906.
    • (2002) Chem. Rev. , vol.102 , pp. 4885-4906
    • Tanaka, F.1
  • 6
    • 0025941636 scopus 로고
    • V genes of oxazolone antibodies in 10 strains of mice
    • Kaartinen M., Solin M.-L., Makela O. V genes of oxazolone antibodies in 10 strains of mice. Eur. J. Immunol. 21:1991;2863-2869.
    • (1991) Eur. J. Immunol. , vol.21 , pp. 2863-2869
    • Kaartinen, M.1    Solin, M.-L.2    Makela, O.3
  • 7
    • 0026713943 scopus 로고
    • The same few V genes account for a majority of oxazolone antibodies in most mouse strains
    • Solin M.L., Kaartinen M., Makela O. The same few V genes account for a majority of oxazolone antibodies in most mouse strains. Mol. Immunol. 29:1992;1357-1362.
    • (1992) Mol. Immunol. , vol.29 , pp. 1357-1362
    • Solin, M.L.1    Kaartinen, M.2    Makela, O.3
  • 8
    • 0027496285 scopus 로고
    • Isoabzymes: Structurally and mechanistically similar catalytic antibodies from the same immunization
    • Angeles T.S., Smith R.G., Darsley M.J., Sugasawara R., Sanchez R.I., Kenten J., et al. Isoabzymes: structurally and mechanistically similar catalytic antibodies from the same immunization. Biochemistry. 32:1993;12128-12135.
    • (1993) Biochemistry , vol.32 , pp. 12128-12135
    • Angeles, T.S.1    Smith, R.G.2    Darsley, M.J.3    Sugasawara, R.4    Sanchez, R.I.5    Kenten, J.6
  • 9
    • 0028292036 scopus 로고
    • A common ancestry for multiple catalytic antibodies generated against a single transition-state analog
    • and see also 10757
    • Miyashita H., Hara T., Tanimura R., Tanaka F., Kikuchi M., Fujii I. A common ancestry for multiple catalytic antibodies generated against a single transition-state analog. Proc. Natl Acad. Sci. USA. 91:1994;6045-6049. and see also 10757.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 6045-6049
    • Miyashita, H.1    Hara, T.2    Tanimura, R.3    Tanaka, F.4    Kikuchi, M.5    Fujii, I.6
  • 10
    • 0028794728 scopus 로고
    • Correlation between antigen-combining-site structures and functions within a panel of catalytic antibodies generated against a single transition state analog
    • Fujii I., Tanaka F., Miyashita H., Tanimura R., Kinoshita K. Correlation between antigen-combining-site structures and functions within a panel of catalytic antibodies generated against a single transition state analog. J. Am. Chem. Soc. 117:1995;6199-6209.
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 6199-6209
    • Fujii, I.1    Tanaka, F.2    Miyashita, H.3    Tanimura, R.4    Kinoshita, K.5
  • 11
    • 0030155251 scopus 로고    scopus 로고
    • Hydrolytic antibodies: Variations on a theme
    • MacBeath G., Hilvert D. Hydrolytic antibodies: variations on a theme. Chem. Biol. 3:1996;433-445.
    • (1996) Chem. Biol. , vol.3 , pp. 433-445
    • MacBeath, G.1    Hilvert, D.2
  • 12
    • 0032500701 scopus 로고    scopus 로고
    • A comparison of the crystallographic structures of two catalytic antibodies with esterase activity
    • Buchbinder J.L., Stephenson R.C., Scanlan T.S., Fletterick R.J. A comparison of the crystallographic structures of two catalytic antibodies with esterase activity. J. Mol. Biol. 282:1998;1033-1041.
    • (1998) J. Mol. Biol. , vol.282 , pp. 1033-1041
    • Buchbinder, J.L.1    Stephenson, R.C.2    Scanlan, T.S.3    Fletterick, R.J.4
  • 13
    • 0029610074 scopus 로고
    • Crystal structure of the complex of a catalytic antibody Fab fragment with a transition state analog: Structural similarities in esterase-like catalytic antibodies
    • Charbonnier J.B., Carpenter E., Gigant B., Golinelli-Pimpaneau B., Eshhar Z., Green B.S., Knossow M. Crystal structure of the complex of a catalytic antibody Fab fragment with a transition state analog: structural similarities in esterase-like catalytic antibodies. Proc. Natl Acad. Sci. USA. 92:1995;11721-11725.
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 11721-11725
    • Charbonnier, J.B.1    Carpenter, E.2    Gigant, B.3    Golinelli-Pimpaneau, B.4    Eshhar, Z.5    Green, B.S.6    Knossow, M.7
  • 15
    • 0034974933 scopus 로고    scopus 로고
    • Canonical binding arrays as molecular recognition elements in the immune system: Tetrahedral anions and the ester hydrolysis transition state
    • Tantillo D.J., Houk K.N. Canonical binding arrays as molecular recognition elements in the immune system: tetrahedral anions and the ester hydrolysis transition state. Chem. Biol. 8:2001;535-545.
    • (2001) Chem. Biol. , vol.8 , pp. 535-545
    • Tantillo, D.J.1    Houk, K.N.2
  • 16
    • 0003743858 scopus 로고    scopus 로고
    • C.F. III Barbas, D.R. Burton, J.K. Scott, & G.J. Silverman. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press
    • Barbas C.F. III, Burton D.R., Scott J.K., Silverman G.J. Phage Display of Proteins and Peptides: A Laboratory Manual. 2001;Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
    • (2001) Phage Display of Proteins and Peptides: A Laboratory Manual
  • 18
    • 0032568859 scopus 로고    scopus 로고
    • Detection of protein three-dimensional side-chain patterns: New examples of convergent evolution
    • Russell R.B. Detection of protein three-dimensional side-chain patterns: new examples of convergent evolution. J. Mol. Biol. 279:1998;1211-1227.
    • (1998) J. Mol. Biol. , vol.279 , pp. 1211-1227
    • Russell, R.B.1
  • 19
    • 0025815916 scopus 로고
    • Structural and evolutionary relationships between retroviral and eukaryotic aspartic proteinases
    • Rao J.K., Erickson J.W., Wlodawer A. Structural and evolutionary relationships between retroviral and eukaryotic aspartic proteinases. Biochemistry. 30:1991;4663-4671.
    • (1991) Biochemistry , vol.30 , pp. 4663-4671
    • Rao, J.K.1    Erickson, J.W.2    Wlodawer, A.3
  • 20
    • 0034679007 scopus 로고    scopus 로고
    • Reconstructing aldolase antibodies to alter their substrate specificity and turnover
    • Tanaka F., Lerner R.A., Barbas C.F. III. Reconstructing aldolase antibodies to alter their substrate specificity and turnover. J. Am. Chem. Soc. 122:2000;4835-4836.
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 4835-4836
    • Tanaka, F.1    Lerner, R.A.2    Barbas III, C.F.3
  • 21
    • 0029590066 scopus 로고
    • Efficient aldolase catalytic antibodies that use the enamine mechanism of natural enzymes
    • Wagner J., Lerner R.A., Barbas C.F. III. Efficient aldolase catalytic antibodies that use the enamine mechanism of natural enzymes. Science. 270:1995;1797-1800.
    • (1995) Science , vol.270 , pp. 1797-1800
    • Wagner, J.1    Lerner, R.A.2    Barbas III, C.F.3
  • 22
    • 0031457319 scopus 로고    scopus 로고
    • Immune versus natural selection: Antibody aldolases with enzymic rates but broader scope
    • Barbas C.F. III, Heine A., Zhong G., Hoffmann T., Gramatikova S., Bjornestedt R., et al. Immune versus natural selection: antibody aldolases with enzymic rates but broader scope. Science. 278:1997;2085-2092.
    • (1997) Science , vol.278 , pp. 2085-2092
    • Barbas III, C.F.1    Heine, A.2    Zhong, G.3    Hoffmann, T.4    Gramatikova, S.5    Bjornestedt, R.6
  • 25
    • 0031779141 scopus 로고    scopus 로고
    • Enantioselective total synthesis of some Brevicomins using aldolase antibody 38C2
    • List B., Shabat D., Barbas C.F. III, Lerner R.A. Enantioselective total synthesis of some Brevicomins using aldolase antibody 38C2. Chem. Eur. J. 4:1998;881-885.
    • (1998) Chem. Eur. J. , vol.4 , pp. 881-885
    • List, B.1    Shabat, D.2    Barbas III, C.F.3    Lerner, R.A.4
  • 26
    • 0032476093 scopus 로고    scopus 로고
    • Catalytic enantioselective retro-aldol reactions: Kinetic resolution of β-hydroxyketones with aldolase antibodies
    • Zhong G., Shabat D., List B., Anderson J., Sinha R.A., Barbas C.F. III. Catalytic enantioselective retro-aldol reactions: kinetic resolution of β-hydroxyketones with aldolase antibodies. Angew. Chem., Int. Ed. 37:1998;2481-2484.
    • (1998) Angew. Chem., Int. Ed. , vol.37 , pp. 2481-2484
    • Zhong, G.1    Shabat, D.2    List, B.3    Anderson, J.4    Sinha, R.A.5    Barbas III, C.F.6
  • 27
    • 0033581160 scopus 로고    scopus 로고
    • A catalytic enantioselective route to hydroxy-substituted quaternary carbon centers: Resolution of tertiary aldols with a catalytic antibody
    • List B., Shabat D., Zhong G., Turner J.M., Li A., Bui T., et al. A catalytic enantioselective route to hydroxy-substituted quaternary carbon centers: resolution of tertiary aldols with a catalytic antibody. J. Am. Chem. Soc. 121:1999;7283-7291.
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 7283-7291
    • List, B.1    Shabat, D.2    Zhong, G.3    Turner, J.M.4    Li, A.5    Bui, T.6
  • 29
    • 0033565014 scopus 로고    scopus 로고
    • Enantioselective aldol cyclodehydration catalyzed by antibody 38C2
    • List B., Lerner R.A., Barbas C.F. III. Enantioselective aldol cyclodehydration catalyzed by antibody 38C2. Org. Letters. 1:1999;59-61.
    • (1999) Org. Letters , vol.1 , pp. 59-61
    • List, B.1    Lerner, R.A.2    Barbas III, C.F.3
  • 30
    • 0033582687 scopus 로고    scopus 로고
    • A short enantioselective synthesis of 1-deoxy-L-xylulose by antibody catalysis
    • Shabat D., List B., Lerner R.A., Barbas C.F. III. A short enantioselective synthesis of 1-deoxy-L-xylulose by antibody catalysis. Tetrahedron Letters. 40:1999;1437-1440.
    • (1999) Tetrahedron Letters , vol.40 , pp. 1437-1440
    • Shabat, D.1    List, B.2    Lerner, R.A.3    Barbas III, C.F.4
  • 31
    • 0032426662 scopus 로고    scopus 로고
    • The antibody catalysis route to the total synthesis of epothilones
    • Sinha S., Barbas C.F. III, Lerner R.A. The antibody catalysis route to the total synthesis of epothilones. Proc. Natl Acad. Sci. USA. 95:1998;14603-14608.
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 14603-14608
    • Sinha, S.1    Barbas III, C.F.2    Lerner, R.A.3
  • 32
    • 0033533131 scopus 로고    scopus 로고
    • Thiazolium-dependent catalytic antibodies produced using a covalent modification strategy
    • Tanaka F., Lerner R.A., Barbas C.F. III. Thiazolium-dependent catalytic antibodies produced using a covalent modification strategy. Chem. Commun. 1999;1383-1384.
    • (1999) Chem. Commun. , pp. 1383-1384
    • Tanaka, F.1    Lerner, R.A.2    Barbas III, C.F.3
  • 33
    • 0034604430 scopus 로고    scopus 로고
    • An efficient benchtop system for multigram-scale kinetic resolutions using aldolase antibodies
    • Turner J.M., Bui T., Lerner R.A., Barbas C.F. III, List B. An efficient benchtop system for multigram-scale kinetic resolutions using aldolase antibodies. Chem. Eur. J. 6:2000;2772-2774.
    • (2000) Chem. Eur. J. , vol.6 , pp. 2772-2774
    • Turner, J.M.1    Bui, T.2    Lerner, R.A.3    Barbas III, C.F.4    List, B.5
  • 34
    • 0035912801 scopus 로고    scopus 로고
    • In vitro activity in a catalytic antibody-prodrug system: Antibody catalyzed etoposide prodrug activation for selective chemotherapy
    • Shabat D., Lode H.N., Pertl U., Reisfeld R.A., Rader C., Lerner R.A., Barbas C.F. III. In vitro activity in a catalytic antibody-prodrug system: antibody catalyzed etoposide prodrug activation for selective chemotherapy. Proc. Natl Acad. Sci. USA. 98:2001;7528-7533.
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 7528-7533
    • Shabat, D.1    Lode, H.N.2    Pertl, U.3    Reisfeld, R.A.4    Rader, C.5    Lerner, R.A.6    Barbas III, C.F.7
  • 37
    • 0036837384 scopus 로고    scopus 로고
    • III Reactive immunization: A unique approach to catalytic antibodies
    • Tanaka F., Barbas C.F. III Reactive immunization: a unique approach to catalytic antibodies. J. Immunol. Methods. 269:2002;67-79.
    • (2002) J. Immunol. Methods , vol.269 , pp. 67-79
    • Tanaka, F.1    Barbas, C.F.2
  • 39
    • 0032416718 scopus 로고    scopus 로고
    • Aldol sensors for the rapid generation of tunable fluorescence by antibody catalysis
    • List B., Barbas C.F. III, Lerner R.A. Aldol sensors for the rapid generation of tunable fluorescence by antibody catalysis. Proc. Natl Acad. Sci. USA. 95:1998;15351-15355.
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 15351-15355
    • List, B.1    Barbas III, C.F.2    Lerner, R.A.3
  • 40
    • 0021964141 scopus 로고
    • Measurements of the true affinity constant in solution of antigen-antibody complexes by enzyme-linked immunosorbent assay
    • Friguet B., Chaffotte A.F., Djavadi-Ohaniance L., Goldberg M.E. Measurements of the true affinity constant in solution of antigen-antibody complexes by enzyme-linked immunosorbent assay. J. Immunol. Methods. 77:1985;305-319.
    • (1985) J. Immunol. Methods , vol.77 , pp. 305-319
    • Friguet, B.1    Chaffotte, A.F.2    Djavadi-Ohaniance, L.3    Goldberg, M.E.4
  • 41
    • 12944317155 scopus 로고    scopus 로고
    • Using antibody catalysis to study the outcome of multiple evolutionary trials of a chemical task
    • Karlstrom A., Zong G., Rader C., Larsen N.A., Heine A., Fuller R., et al. Using antibody catalysis to study the outcome of multiple evolutionary trials of a chemical task. Proc. Natl Acad. Sci. USA. 97:2000;3878-3883.
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 3878-3883
    • Karlstrom, A.1    Zong, G.2    Rader, C.3    Larsen, N.A.4    Heine, A.5    Fuller, R.6
  • 42
    • 0027285118 scopus 로고
    • A data-based reaction mechanism for type I fructose bisphosphate aldolase
    • Littlechild J.A., Watson H.C. A data-based reaction mechanism for type I fructose bisphosphate aldolase. Trends Biochem. Sci. 18:1993;36-39.
    • (1993) Trends Biochem. Sci. , vol.18 , pp. 36-39
    • Littlechild, J.A.1    Watson, H.C.2
  • 43
    • 0029970552 scopus 로고    scopus 로고
    • A lysine to arginine substitution at position 146 of rabbit aldolase a changes the rate-determining step to Schiff base formation
    • and references therein
    • Morris A.J., Davenport R.C., Tolan D.R. A lysine to arginine substitution at position 146 of rabbit aldolase A changes the rate-determining step to Schiff base formation. Protein Eng. 9:1996;61-67. and references therein.
    • (1996) Protein Eng. , vol.9 , pp. 61-67
    • Morris, A.J.1    Davenport, R.C.2    Tolan, D.R.3
  • 44
    • 0030924508 scopus 로고    scopus 로고
    • Phage display of catalytic antibody to optimize affinity for transition-state analog binding
    • Baca M., Scanlan T.S., Stephenson R.C., Wells J. Phage display of catalytic antibody to optimize affinity for transition-state analog binding. Proc. Natl Acad. Sci. USA. 94:1997;10063-10068.
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 10063-10068
    • Baca, M.1    Scanlan, T.S.2    Stephenson, R.C.3    Wells, J.4
  • 45
    • 0031945007 scopus 로고    scopus 로고
    • Evolving catalytic antibodies in a phage-displayed combinatorial library
    • Fujii I., Fukuyama S., Iwabuchi Y., Tanimura R. Evolving catalytic antibodies in a phage-displayed combinatorial library. Nature Biotechnol. 16:1998;463-467.
    • (1998) Nature Biotechnol. , vol.16 , pp. 463-467
    • Fujii, I.1    Fukuyama, S.2    Iwabuchi, Y.3    Tanimura, R.4
  • 46
    • 0032509131 scopus 로고    scopus 로고
    • Probing the importance of second sphere residues in an esterolytic antibody by phage display
    • Arkin M.R., Wells J.A. Probing the importance of second sphere residues in an esterolytic antibody by phage display. J. Mol. Biol. 284:1998;1083-1094.
    • (1998) J. Mol. Biol. , vol.284 , pp. 1083-1094
    • Arkin, M.R.1    Wells, J.A.2
  • 47
    • 0035011047 scopus 로고    scopus 로고
    • In vitro abzyme evolution to optimize antibody recognition for catalysis
    • Takahashi N., Kakinuma H., Liu L., Nishi Y., Fujii I. In vitro abzyme evolution to optimize antibody recognition for catalysis. Nature Biotechnol. 19:2001;563-567.
    • (2001) Nature Biotechnol. , vol.19 , pp. 563-567
    • Takahashi, N.1    Kakinuma, H.2    Liu, L.3    Nishi, Y.4    Fujii, I.5
  • 48
    • 0024722750 scopus 로고
    • Toward generating cytotoxic agents at cancer sites
    • Bagshawe K.D. Toward generating cytotoxic agents at cancer sites. Br. J. Cancer. 60:1989;275-281.
    • (1989) Br. J. Cancer , vol.60 , pp. 275-281
    • Bagshawe, K.D.1
  • 51
    • 0032542692 scopus 로고    scopus 로고
    • Direct selection for catalysis from combinatorial antibody libraries using boronic acid probe: Primary amide bond hyrolysis
    • Gao C., Lavey B.J., Lo C.-H.L., Datta A., Wentworth P., Janda K.D. Direct selection for catalysis from combinatorial antibody libraries using boronic acid probe: primary amide bond hyrolysis. J. Am. Chem. Soc. 120:1998;2211-2217.
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 2211-2217
    • Gao, C.1    Lavey, B.J.2    Lo, C.-H.L.3    Datta, A.4    Wentworth, P.5    Janda, K.D.6
  • 52
    • 0033550282 scopus 로고    scopus 로고
    • Catalytic single-chain antibodies possessing β-lactamase activity selected from a phage displayed combinatorial library using a mechanism-based inhibitor
    • Tanaka F., Almer H., Lerner R.A., Barbas C.F. III. Catalytic single-chain antibodies possessing β-lactamase activity selected from a phage displayed combinatorial library using a mechanism-based inhibitor. Tetrahedron Letters. 40:1999;8063-8066.
    • (1999) Tetrahedron Letters , vol.40 , pp. 8063-8066
    • Tanaka, F.1    Almer, H.2    Lerner, R.A.3    Barbas III, C.F.4
  • 54
    • 0035926124 scopus 로고    scopus 로고
    • Phage display selection of peptides possessing aldolase activity
    • Tanaka F., Barbas C.F. III. Phage display selection of peptides possessing aldolase activity. Chem. Commun. 2001;769-770.
    • (2001) Chem. Commun. , pp. 769-770
    • Tanaka, F.1    Barbas III, C.F.2
  • 55
    • 0037051643 scopus 로고    scopus 로고
    • A modular assembly strategy for improving the substrate specificity of small catalytic peptides
    • Tanaka F., Barbas C.F. III. A modular assembly strategy for improving the substrate specificity of small catalytic peptides. J. Am. Chem. Soc. 124:2002;3510-3511.
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 3510-3511
    • Tanaka, F.1    Barbas III, C.F.2
  • 56
    • 0014259004 scopus 로고
    • Acetoacetate decarboxylase. Reaction with acetopyruvate
    • Tagaki W., Guthrie J.P., Westheimer F.H. Acetoacetate decarboxylase. Reaction with acetopyruvate. Biochemistry. 7:1968;905-913.
    • (1968) Biochemistry , vol.7 , pp. 905-913
    • Tagaki, W.1    Guthrie, J.P.2    Westheimer, F.H.3
  • 57
    • 0016765041 scopus 로고
    • Modification of arginine and lysine in proteins
    • Gilbert H.F. III, O'Leary M.H. Modification of arginine and lysine in proteins. Biochemistry. 14:1975;5194-5199.
    • (1975) Biochemistry , vol.14 , pp. 5194-5199
    • Gilbert III, H.F.1    O'Leary, M.H.2
  • 58
    • 0017394582 scopus 로고
    • Reversible modification of amino groups in aspartate aminotransferase
    • Gilbert H.F. III, O'Leary M.H. Reversible modification of amino groups in aspartate aminotransferase. Biochim. Biophys. Acta. 483:1977;79-89.
    • (1977) Biochim. Biophys. Acta , vol.483 , pp. 79-89
    • Gilbert III, H.F.1    O'Leary, M.H.2
  • 59
    • 0018783090 scopus 로고
    • Modification of lysyl residues of dihydrofolate reductase with 2,4-pentanedione
    • Otwell H.B., Cipollo K.L., Dunlap R.B. Modification of lysyl residues of dihydrofolate reductase with 2,4-pentanedione. Biochim. Biophys. Acta. 568:1979;297-306.
    • (1979) Biochim. Biophys. Acta , vol.568 , pp. 297-306
    • Otwell, H.B.1    Cipollo, K.L.2    Dunlap, R.B.3
  • 60
    • 0025720729 scopus 로고
    • An active-site lysine in liver phosphoenolpyruvate carboxykinase
    • Guidinger P.F., Nowak T. An active-site lysine in liver phosphoenolpyruvate carboxykinase. Biochemistry. 30:1991;8851-8861.
    • (1991) Biochemistry , vol.30 , pp. 8851-8861
    • Guidinger, P.F.1    Nowak, T.2
  • 61
    • 0025838021 scopus 로고
    • Assembly of combinatorial antibody libraries on phage surfaces: The gene III site
    • Barbas C.F. III, Kang A.S., Lerner R.A., Benkovic S.J. Assembly of combinatorial antibody libraries on phage surfaces: the gene III site. Proc. Natl Acad. Sci. USA. 88:1991;7978-7982.
    • (1991) Proc. Natl Acad. Sci. USA , vol.88 , pp. 7978-7982
    • Barbas III, C.F.1    Kang, A.S.2    Lerner, R.A.3    Benkovic, S.J.4


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