메뉴 건너뛰기




Volumn 58, Issue , 2005, Pages 185-226

Engineering antibodies for biosensor technologies

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; CHAPERONE; HYBRID PROTEIN; IMMUNOGLOBULIN; IMMUNOGLOBULIN F(AB) FRAGMENT; IMMUNOGLOBULIN G; METALLOPROTEIN; MONOCLONAL ANTIBODY; PAPAIN; POLYCLONAL ANTIBODY; RECOMBINANT ANTIBODY; RECOMBINANT PROTEIN;

EID: 33644919974     PISSN: 00652164     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S0065-2164(05)58006-7     Document Type: Review
Times cited : (19)

References (206)
  • 1
  • 2
    • 0035207083 scopus 로고    scopus 로고
    • Mechanisms leading to an orientated immobilization of recombinant proteins derived from the p24 capsid of HIV-1 onto copolymers
    • Allard L., Cheynet V., Oriol L., Veron F., Merlier G., Scremin G., Mandrand B., Delair T., and Mallet F. Mechanisms leading to an orientated immobilization of recombinant proteins derived from the p24 capsid of HIV-1 onto copolymers Bioconjugate Chem. 12 2001 972 979
    • (2001) Bioconjugate Chem. , vol.12 , pp. 972-979
    • Allard, L.1    Cheynet, V.2    Oriol, L.3    Veron, F.4    Merlier, G.5    Scremin, G.6    Mandrand, B.7    Delair, T.8    Mallet, F.9
  • 3
    • 0037027405 scopus 로고    scopus 로고
    • Versatile method for production and controlled polymer-immobilisation of biologically active recombinant proteins
    • Allard L., Cheynet V., Oriol G., Mandrand B., Delair T., and Mallet F. Versatile method for production and controlled polymer-immobilisation of biologically active recombinant proteins Biotechnol. Bioeng. 80 2002 341 348
    • (2002) Biotechnol. Bioeng. , vol.80 , pp. 341-348
    • Allard, L.1    Cheynet, V.2    Oriol, G.3    Mandrand, B.4    Delair, T.5    Mallet, F.6
  • 4
    • 0035424963 scopus 로고    scopus 로고
    • In vitro display technologies: Novel developments and applications
    • Amstutz P., Forrer P., Zahnd C., and Plückthun A. In vitro display technologies: Novel developments and applications Curr. Opin. Biotech. 12 2001 400 405
    • (2001) Curr. Opin. Biotech. , vol.12 , pp. 400-405
    • Amstutz, P.1    Forrer, P.2    Zahnd, C.3    Plückthun, A.4
  • 6
    • 0034695427 scopus 로고    scopus 로고
    • A heterodimeric coiled-coil peptide pair selected in vivo from a designed library-versus-library ensemble
    • Arndt K., Pelletier J., Muller K., Alber T., Michnick S., and Pluckthun A. A heterodimeric coiled-coil peptide pair selected in vivo from a designed library-versus-library ensemble J. Mol. Biol. 295 2000 627 639
    • (2000) J. Mol. Biol. , vol.295 , pp. 627-639
    • Arndt, K.1    Pelletier, J.2    Muller, K.3    Alber, T.4    Michnick, S.5    Pluckthun, A.6
  • 7
    • 0036710244 scopus 로고    scopus 로고
    • Comparison of in vivo selection and rational design of heterodimeric coiled coils
    • Arndt K., Pelletier J., Muller K., Pluckthun A., and Alber T. Comparison of in vivo selection and rational design of heterodimeric coiled coils Structure 10 2002 1235 1248
    • (2002) Structure , vol.10 , pp. 1235-1248
    • Arndt, K.1    Pelletier, J.2    Muller, K.3    Pluckthun, A.4    Alber, T.5
  • 8
    • 0037440564 scopus 로고    scopus 로고
    • Shift of whispering gallery modes in microspheres by protein adsorption
    • Arnold S., Khoshsima M., Teraoka I., Holler S., and Vollmer F. Shift of whispering gallery modes in microspheres by protein adsorption Opt. Lett. 28 2003 272 274
    • (2003) Opt. Lett. , vol.28 , pp. 272-274
    • Arnold, S.1    Khoshsima, M.2    Teraoka, I.3    Holler, S.4    Vollmer, F.5
  • 9
    • 0035823143 scopus 로고    scopus 로고
    • Escherichia coli maltose-binding protein as a molecular chaperone for recombinant intracellular cytoplasmic single-chain antibodies
    • Bach H., Mazor Y., Shaky S., Shoham-Lev A., Berdichevsky Y., Gutnick D.L., and Benhar I. Escherichia coli maltose-binding protein as a molecular chaperone for recombinant intracellular cytoplasmic single-chain antibodies J. Mol. Biol. 312 2001 79 93
    • (2001) J. Mol. Biol. , vol.312 , pp. 79-93
    • Bach, H.1    Mazor, Y.2    Shaky, S.3    Shoham-lev, A.4    Berdichevsky, Y.5    Gutnick, D.L.6    Benhar, I.7
  • 10
    • 1242293716 scopus 로고    scopus 로고
    • A universal nucleic acid sequence biosensor with nanomolar detection limits
    • Baeumner A.J., Pretz J., and Fang S. A universal nucleic acid sequence biosensor with nanomolar detection limits Anal. Chem. 76 2004 888 894
    • (2004) Anal. Chem. , vol.76 , pp. 888-894
    • Baeumner, A.J.1    Pretz, J.2    Fang, S.3
  • 11
    • 0026563253 scopus 로고
    • Semisynthetic combinatorial antibody libraries: A chemical solution to the diversity problem
    • Barbas C.F., Bain J.D., Hoekstra D.M., and Lerner R.A. Semisynthetic combinatorial antibody libraries: A chemical solution to the diversity problem Proc. Natl. Acad. Sci. USA 89 1992 4457 4461
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 4457-4461
    • Barbas, C.F.1    Bain, J.D.2    Hoekstra, D.M.3    Lerner, R.A.4
  • 12
    • 0033598777 scopus 로고    scopus 로고
    • Efficient folding of proteins with multiple disulphide bonds in the Escherichia coli cytoplasm
    • Bessette P., Aslund F., Beckwith J., and Georgiou G. Efficient folding of proteins with multiple disulphide bonds in the Escherichia coli cytoplasm Proc. Natl. Acad. Sci. USA 96 1999 13703 13708
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 13703-13708
    • Bessette, P.1    Aslund, F.2    Beckwith, J.3    Georgiou, G.4
  • 13
    • 0029758834 scopus 로고    scopus 로고
    • Fused polycationic peptide mediates delivery of diptheria toxin a chain to the cytosol in the presence of anthrax protective antigen
    • Blanke S., Milne J., Benson E., and Collier R. Fused polycationic peptide mediates delivery of diptheria toxin A chain to the cytosol in the presence of anthrax protective antigen Proc. Natl. Acad. Sci. USA 93 1996 8437 8442
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 8437-8442
    • Blanke, S.1    Milne, J.2    Benson, E.3    Collier, R.4
  • 14
    • 0030994634 scopus 로고    scopus 로고
    • Yeast surface display for screening combinatorial polypeptide libraries
    • Boder E.T., and Wittrup K.D. Yeast surface display for screening combinatorial polypeptide libraries Nat. Biotechnol. 15 1997 553 557
    • (1997) Nat. Biotechnol. , vol.15 , pp. 553-557
    • Boder, E.T.1    Wittrup, K.D.2
  • 15
    • 0034718615 scopus 로고    scopus 로고
    • Directed evolution of antibody fragments with monovalent femtomolar antigen-binding affinity
    • Boder E.T., Midelfort K.S., and Wittrup K.D. Directed evolution of antibody fragments with monovalent femtomolar antigen-binding affinity Proc. Natl. Acad. Sci. USA 97 2000 10701 10705
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 10701-10705
    • Boder, E.T.1    Midelfort, K.S.2    Wittrup, K.D.3
  • 16
    • 0037457534 scopus 로고    scopus 로고
    • Surface functionalization for self-referencing surface plasmon resonance (SPR) biosensors by multi-step self-assembly
    • Boozer C., Yu Q.M., Chen S.F., Lee C.Y., Homola J., Yee S.S., and Jiang S.Y. Surface functionalization for self-referencing surface plasmon resonance (SPR) biosensors by multi-step self-assembly Sensor. Actuat. B-Chem. 90 2003 22 30
    • (2003) Sensor. Actuat. B-Chem. , vol.90 , pp. 22-30
    • Boozer, C.1    Yu, Q.M.2    Chen, S.F.3    Lee, C.Y.4    Homola, J.5    Yee, S.S.6    Jiang, S.Y.7
  • 17
    • 2642652226 scopus 로고    scopus 로고
    • Selection for a periplasmic factor improving phage display and functional periplasmic expression
    • Bothmann H., and Pluckthun A. Selection for a periplasmic factor improving phage display and functional periplasmic expression Nat. Biotechnol. 16 1998 376 380
    • (1998) Nat. Biotechnol. , vol.16 , pp. 376-380
    • Bothmann, H.1    Pluckthun, A.2
  • 18
    • 3142743794 scopus 로고    scopus 로고
    • Antibodies from phage antibody libraries
    • Bradbury A.R.M., and Marks J.D. Antibodies from phage antibody libraries J. Immunol. Methods 290 2004 29 49
    • (2004) J. Immunol. Methods , vol.290 , pp. 29-49
    • Bradbury, A.R.M.1    Marks, J.D.2
  • 19
    • 0028011935 scopus 로고
    • Bifunctional hybrids between the variable domains of an immunoglobulin and the maltose binding protein of Escherichia coli: Production, purification and antigen binding
    • Bregegere F., Schwartz J., and Bedouelle H. Bifunctional hybrids between the variable domains of an immunoglobulin and the maltose binding protein of Escherichia coli: Production, purification and antigen binding Protein Eng. 7 1994 271 280
    • (1994) Protein Eng. , vol.7 , pp. 271-280
    • Bregegere, F.1    Schwartz, J.2    Bedouelle, H.3
  • 20
    • 12944308809 scopus 로고    scopus 로고
    • Selecting for antibody scFv fragments with improved stability using phage display with denaturation under reducing conditions
    • Brockmann E-C., Cooper M., Strömsten N., Vehniäinen M., and Saviranta P. Selecting for antibody scFv fragments with improved stability using phage display with denaturation under reducing conditions J. Immunol. Methods 296 2005 159 170
    • (2005) J. Immunol. Methods , vol.296 , pp. 159-170
    • Brockmann, E-C.1    Cooper, M.2    Strömsten, N.3    Vehniäinen, M.4    Saviranta, P.5
  • 21
  • 22
    • 0030969778 scopus 로고    scopus 로고
    • Metal-recognition by repeating polypeptides
    • Brown S. Metal-recognition by repeating polypeptides Nat. Biotechnol. 15 1997 269 272
    • (1997) Nat. Biotechnol. , vol.15 , pp. 269-272
    • Brown, S.1
  • 23
    • 0027280880 scopus 로고
    • A new cloning vector and expression strategy for genes encoding proteins toxic to Escherichia coli
    • Brown W.C., and Campbell J.L. A new cloning vector and expression strategy for genes encoding proteins toxic to Escherichia coli Gene 127 1993 99 103
    • (1993) Gene , vol.127 , pp. 99-103
    • Brown, W.C.1    Campbell, J.L.2
  • 25
    • 0029021085 scopus 로고
    • Anti-melanoma antibodies from melanoma patients immunised with genetically autologous tumour cells: Selection of specific antibodies from single-chain Fv fusion phage libraries
    • Cai X., and Garen A. Anti-melanoma antibodies from melanoma patients immunised with genetically autologous tumour cells: Selection of specific antibodies from single-chain Fv fusion phage libraries Proc. Natl. Acad. Sci. USA 92 1995 6537 6541
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 6537-6541
    • Cai, X.1    Garen, A.2
  • 26
    • 0037162583 scopus 로고    scopus 로고
    • Immobilization of metallothionein on gold/mica surfaces: Relationship between surface morphology and protein-substrate interaction
    • Casero E., Vazquez L., Martin-Benito J., Morcillo M., Lorenzo E., and Pariente F. Immobilization of metallothionein on gold/mica surfaces: Relationship between surface morphology and protein-substrate interaction Langmuir 18 2002 5909 5920
    • (2002) Langmuir , vol.18 , pp. 5909-5920
    • Casero, E.1    Vazquez, L.2    Martin-benito, J.3    Morcillo, M.4    Lorenzo, E.5    Pariente, F.6
  • 27
    • 0030738902 scopus 로고    scopus 로고
    • Kinetic analysis of the interaction between the monoclonal antibody A33 and its colonic epithelial antigen by the use of an optical biosensor - a comparison of immobilisation strategies
    • Catimel B., Nerrie M., Lee F.T., Scott A.M., Ritter G., Welt S., Old L.J., Burgess A.W., and Nice E.C. Kinetic analysis of the interaction between the monoclonal antibody A33 and its colonic epithelial antigen by the use of an optical biosensor - A comparison of immobilisation strategies J. Chromatogr. A 776 1997 15 30
    • (1997) J. Chromatogr. a , vol.776 , pp. 15-30
    • Catimel, B.1    Nerrie, M.2    Lee, F.T.3    Scott, A.M.4    Ritter, G.5    Welt, S.6    Old, L.J.7    Burgess, A.W.8    Nice, E.C.9
  • 28
    • 0032508511 scopus 로고    scopus 로고
    • Use of a heterodimeric coiled-coil system for biosensor application and affinity purification
    • Chao H., Bautista D., Litowski J., Irvin R., and Hodges R. Use of a heterodimeric coiled-coil system for biosensor application and affinity purification J. Chromatogr. B 715 1998 307 329
    • (1998) J. Chromatogr. B , vol.715 , pp. 307-329
    • Chao, H.1    Bautista, D.2    Litowski, J.3    Irvin, R.4    Hodges, R.5
  • 30
    • 0025835310 scopus 로고
    • Making antibody fragments using phage display libraries
    • Clackson T., Hoogenboom H.R., Griffiths A.D., and Winter G. Making antibody fragments using phage display libraries Nature 352 1991 624 628
    • (1991) Nature , vol.352 , pp. 624-628
    • Clackson, T.1    Hoogenboom, H.R.2    Griffiths, A.D.3    Winter, G.4
  • 31
    • 0011379580 scopus 로고    scopus 로고
    • Randomizing gene sequences with new PCR mutagenesis kit
    • Cline J., and Hogrefe H.H. Randomizing gene sequences with new PCR mutagenesis kit Strategies 13 2000 157 161
    • (2000) Strategies , vol.13 , pp. 157-161
    • Cline, J.1    Hogrefe, H.H.2
  • 32
    • 0030832921 scopus 로고    scopus 로고
    • Use of mutator cells as a means for increasing production levels of a recombinant antibody directed against Hepatitis B
    • Coia G., Ayres A., Lilley G.G., Hudson P.J., and Irving R.A. Use of mutator cells as a means for increasing production levels of a recombinant antibody directed against Hepatitis B Gene 201 1997 203 209
    • (1997) Gene , vol.201 , pp. 203-209
    • Coia, G.1    Ayres, A.2    Lilley, G.G.3    Hudson, P.J.4    Irving, R.A.5
  • 33
  • 34
    • 0034049316 scopus 로고    scopus 로고
    • Quantitative analysis of the effect of the mutation frequency on the affinity maturation of single chain Fv antibodies
    • Daugherty P.S., Chen G., Iverson B.L., and Georgiou G. Quantitative analysis of the effect of the mutation frequency on the affinity maturation of single chain Fv antibodies Proc. Natl. Acad. Sci. USA 97 2000 2029 2034
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 2029-2034
    • Daugherty, P.S.1    Chen, G.2    Iverson, B.L.3    Georgiou, G.4
  • 37
    • 0042709626 scopus 로고    scopus 로고
    • Development and use of antibodies in surface plasmon resonance-based immunosensors for environmental monitoring
    • Dillon P.P., Daly S.J., Killard A.J., and O'Kennedy R. Development and use of antibodies in surface plasmon resonance-based immunosensors for environmental monitoring Intern. J. Environ. Anal. Chem. 83 2003 525 543
    • (2003) Intern. J. Environ. Anal. Chem. , vol.83 , pp. 525-543
    • Dillon, P.P.1    Daly, S.J.2    Killard, A.J.3    O'Kennedy, R.4
  • 38
    • 0042195979 scopus 로고    scopus 로고
    • Selection and characterization of naturally occurring single-domain (IgNAR) antibody fragments from immunized sharks by phage display
    • Dooley H., Flajnik M.F., and Porter A.J. Selection and characterization of naturally occurring single-domain (IgNAR) antibody fragments from immunized sharks by phage display Mol. Immunol. 40 2003 25 33
    • (2003) Mol. Immunol. , vol.40 , pp. 25-33
    • Dooley, H.1    Flajnik, M.F.2    Porter, A.J.3
  • 40
    • 0037474477 scopus 로고    scopus 로고
    • Generation of affinity matured scFv antibodies against mouse neural cell adhesion molecule L1 by phage display
    • Dong L., Chen S., Bartsch U., and Schachner M. Generation of affinity matured scFv antibodies against mouse neural cell adhesion molecule L1 by phage display Bio. Biophys. Res. Comm. 301 2003 60 70
    • (2003) Bio. Biophys. Res. Comm. , vol.301 , pp. 60-70
    • Dong, L.1    Chen, S.2    Bartsch, U.3    Schachner, M.4
  • 41
    • 0028609602 scopus 로고
    • Elimination of endogenous aberrant kappa-chain transcripts from Sp2/0-derived hybridoma cells by specific ribozyme cleavage - utility in genetic therapy of Hiv-1 infections
    • Duan L.X., and Pomerantz R.J. Elimination of endogenous aberrant kappa-chain transcripts from Sp2/0-derived hybridoma cells by specific ribozyme cleavage - utility in genetic therapy of Hiv-1 infections Nucleic Acids Res. 22 1994 5433 5438
    • (1994) Nucleic Acids Res. , vol.22 , pp. 5433-5438
    • Duan, L.X.1    Pomerantz, R.J.2
  • 45
    • 0037133506 scopus 로고    scopus 로고
    • Biophysical properties of camelid VHH domains compared to those of human VH3 domains
    • Ewert S., Cambillau C., Conrath K., and Pluckthun A. Biophysical properties of camelid VHH domains compared to those of human VH3 domains Biochemistry 41 2002 3628 3636
    • (2002) Biochemistry , vol.41 , pp. 3628-3636
    • Ewert, S.1    Cambillau, C.2    Conrath, K.3    Pluckthun, A.4
  • 46
    • 4143110187 scopus 로고    scopus 로고
    • Stability improvement of antibodies for extracellular and intracellular applications: CDR grafting to stable frameworks and structure-based framework engineering
    • Ewert S., Honegger A., and Plückthun A. Stability improvement of antibodies for extracellular and intracellular applications: CDR grafting to stable frameworks and structure-based framework engineering Methods 34 2004 184 199
    • (2004) Methods , vol.34 , pp. 184-199
    • Ewert, S.1    Honegger, A.2    Plückthun, A.3
  • 47
    • 0026551323 scopus 로고
    • Biospecific interaction analysis using surface-plasmon resonance detection applied to kinetic, binding-site and concentration analysis
    • Fägerstam L.G., Frostellkarlsson A., Karlsson R., Persson B., and Ronnberg I. Biospecific interaction analysis using surface-plasmon resonance detection applied to kinetic, binding-site and concentration analysis J. Chromatogr. 597 1992 397 410
    • (1992) J. Chromatogr. , vol.597 , pp. 397-410
    • Fägerstam, L.G.1    Frostellkarlsson, A.2    Karlsson, R.3    Persson, B.4    Ronnberg, I.5
  • 48
    • 0035413239 scopus 로고    scopus 로고
    • P-chip and P-chip bienzyme electrodes based on recombinant forms of horseradish peroxidase immobilized on gold electrodes
    • Ferapontova E., Grigorenko V., and Egorov A. P-chip and P-chip bienzyme electrodes based on recombinant forms of horseradish peroxidase immobilized on gold electrodes Biochemistry (Moscow) 66 2001 832 839
    • (2001) Biochemistry (Moscow) , vol.66 , pp. 832-839
    • Ferapontova, E.1    Grigorenko, V.2    Egorov, A.3
  • 49
    • 3042634329 scopus 로고    scopus 로고
    • Specificity rescue and affinity maturation of a low-affinity IgM antibody against pro-gastrin-releasing peptide using phage display and DNA shuffling
    • Fermer C., Andersson I., Nilsson K., and Nilsson O. Specificity rescue and affinity maturation of a low-affinity IgM antibody against pro-gastrin-releasing peptide using phage display and DNA shuffling Tumor Biol. 25 2004 7 13
    • (2004) Tumor Biol. , vol.25 , pp. 7-13
    • Fermer, C.1    Andersson, I.2    Nilsson, K.3    Nilsson, O.4
  • 50
    • 0035040679 scopus 로고    scopus 로고
    • Formation of disulphide bonds during secretion of proteins through the periplasmic-independent type-1 pathway
    • Fernandez L., and de Lorenzo V. Formation of disulphide bonds during secretion of proteins through the periplasmic-independent type-1 pathway Mol. Microbiol. 40 2001 332 346
    • (2001) Mol. Microbiol. , vol.40 , pp. 332-346
    • Fernandez, L.1    De Lorenzo, V.2
  • 51
    • 3543069890 scopus 로고    scopus 로고
    • Prokaryotic expression of antibodies and affibodies
    • Fernandez L. Prokaryotic expression of antibodies and affibodies Curr. opin. Biotech. 15 2004 364 373
    • (2004) Curr. Opin. Biotech. , vol.15 , pp. 364-373
    • Fernandez, L.1
  • 52
    • 0031872669 scopus 로고    scopus 로고
    • Detection of Escherichia Coli O157:H7 using a surface plasmon resonance biosensor
    • Fratamico P.M., Strobaugh T.M., Medina M.B., and Gehring A.G. Detection of Escherichia Coli O157:H7 using a surface plasmon resonance biosensor Biotechnol. Tech. 12 1998 571 576
    • (1998) Biotechnol. Tech. , vol.12 , pp. 571-576
    • Fratamico, P.M.1    Strobaugh, T.M.2    Medina, M.B.3    Gehring, A.G.4
  • 53
    • 0029989229 scopus 로고    scopus 로고
    • Expression of correctly folded proteins in Escherichia coli
    • Georgiou G., and Valax P. Expression of correctly folded proteins in Escherichia coli Curr. Opin. Biotech. 7 1996 190 197
    • (1996) Curr. Opin. Biotech. , vol.7 , pp. 190-197
    • Georgiou, G.1    Valax, P.2
  • 54
    • 0029008438 scopus 로고
    • Stable chelating linkage for reversible immobilization of oligohistidine tagged proteins in the BIAcore surface plasmon resonance detector
    • Gershon P., and Khilko S. Stable chelating linkage for reversible immobilization of oligohistidine tagged proteins in the BIAcore surface plasmon resonance detector J. Immunol. Methods 183 1995 65 76
    • (1995) J. Immunol. Methods , vol.183 , pp. 65-76
    • Gershon, P.1    Khilko, S.2
  • 55
    • 0030767656 scopus 로고    scopus 로고
    • Selection and identification of single domain antibody fragments from camel heavy-chain antibodies
    • Ghahroudi M.A., Desmyter A., Wyns L., Hamers R., and Muyldermans S. Selection and identification of single domain antibody fragments from camel heavy-chain antibodies FEBS Lett. 414 1997 521 526
    • (1997) FEBS Lett. , vol.414 , pp. 521-526
    • Ghahroudi, M.A.1    Desmyter, A.2    Wyns, L.3    Hamers, R.4    Muyldermans, S.5
  • 56
    • 0027082901 scopus 로고
    • Antibody engineering by codon-based mutagenesis in a filamentous phage vector system
    • Glaser S.M., Yelton D.E., and Huse W.D. Antibody engineering by codon-based mutagenesis in a filamentous phage vector system J. Immunol. 15 1992 3903 3913
    • (1992) J. Immunol. , vol.15 , pp. 3903-3913
    • Glaser, S.M.1    Yelton, D.E.2    Huse, W.D.3
  • 57
    • 0025162270 scopus 로고
    • A comparison of strategies to stabilize immunoglobulin Fv-fragments
    • Glockshuber R., Malia M., Pfitzinger I., and Pluckthun A. A comparison of strategies to stabilize immunoglobulin Fv-fragments Biochemistry 29 1990 1362 1367
    • (1990) Biochemistry , vol.29 , pp. 1362-1367
    • Glockshuber, R.1    Malia, M.2    Pfitzinger, I.3    Pluckthun, A.4
  • 58
    • 0026572809 scopus 로고
    • The disulphide bonds in antibody variable domains: Effects on stability, folding in vitro and functional expression in Escherichia coli
    • Glockshuber R., Schmidt T., and Pluckthun A. The disulphide bonds in antibody variable domains: Effects on stability, folding in vitro and functional expression in Escherichia coli Biochemistry 31 1992 1270 1279
    • (1992) Biochemistry , vol.31 , pp. 1270-1279
    • Glockshuber, R.1    Schmidt, T.2    Pluckthun, A.3
  • 60
    • 0018721964 scopus 로고
    • The role of the intrachain disulphide bond in the conformation and stability of the constant fragment of the immunoglobulin light chain
    • Goto Y., and Hamaguchi K. The role of the intrachain disulphide bond in the conformation and stability of the constant fragment of the immunoglobulin light chain J. Biochem. 86 1979 1433 1441
    • (1979) J. Biochem. , vol.86 , pp. 1433-1441
    • Goto, Y.1    Hamaguchi, K.2
  • 61
    • 4143129879 scopus 로고    scopus 로고
    • Directed evolution of an anti-carcinoembryonic antigen scFv with a 4-day monovalent dissociation half-time at 37°C
    • Graff C.P., Chester K., Begent R., and Wittrup K.D. Directed evolution of an anti-carcinoembryonic antigen scFv with a 4-day monovalent dissociation half-time at 37°C Protein Engineering Design and Selection 17 2004 293 304
    • (2004) Protein Engineering Design and Selection , vol.17 , pp. 293-304
    • Graff, C.P.1    Chester, K.2    Begent, R.3    Wittrup, K.D.4
  • 63
    • 0028962371 scopus 로고
    • A new antigen receptor gene family that undergoes rearrangement and extensive somatic diversification in sharks
    • Greenberg A.S., Avila D., Hughes M., Hughes A., Churchill McKinney E., and Flajnik M.F. A new antigen receptor gene family that undergoes rearrangement and extensive somatic diversification in sharks Nature 374 1995 168 173
    • (1995) Nature , vol.374 , pp. 168-173
    • Greenberg, A.S.1    Avila, D.2    Hughes, M.3    Hughes, A.4    Churchill McKinney, E.5    Flajnik, M.F.6
  • 67
    • 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., and Pluckthun A. Ribosome display efficiently selects and evolves high-affinity antibodies in vitro from immune libraries Proc. Natl. Acad. Sci. USA 95 1998 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
  • 68
    • 0030974119 scopus 로고    scopus 로고
    • In vitro selection and evolution of functional proteins by using ribosome display
    • Hanes J., and Plückthun A. In vitro selection and evolution of functional proteins by using ribosome display Proc. Natl. Acad. Sci. USA 94 1997 4937 4942
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 4937-4942
    • Hanes, J.1    Plückthun, A.2
  • 69
    • 0033664270 scopus 로고    scopus 로고
    • Picomolar affinity antibodies from a fully synthetic naive library selected and evolved by ribosome display
    • Hanes J., Schaffitzel C., Knappik A., and Plückthun A. Picomolar affinity antibodies from a fully synthetic naive library selected and evolved by ribosome display Nature Biotechnol. 18 2000 1287 1292
    • (2000) Nature Biotechnol. , vol.18 , pp. 1287-1292
    • Hanes, J.1    Schaffitzel, C.2    Knappik, A.3    Plückthun, A.4
  • 70
    • 0026699293 scopus 로고
    • Selection of phage antibodies by binding affinity mimicking affinity maturation
    • Hawkins R.E., Russell S.J., and Winter G. Selection of phage antibodies by binding affinity mimicking affinity maturation J. Mol. Biol. 226 1992 889 896
    • (1992) J. Mol. Biol. , vol.226 , pp. 889-896
    • Hawkins, R.E.1    Russell, S.J.2    Winter, G.3
  • 71
    • 0033117352 scopus 로고    scopus 로고
    • Escherichia coli Skp chaperone coexpression improves solubility and phage display of single-chain antibody fragments
    • Hayhurst A., and Harris W. Escherichia coli Skp chaperone coexpression improves solubility and phage display of single-chain antibody fragments Protein Expres. Purif. 15 1999 336 343
    • (1999) Protein Expres. Purif. , vol.15 , pp. 336-343
    • Hayhurst, A.1    Harris, W.2
  • 72
    • 0034142296 scopus 로고    scopus 로고
    • Improved expression characteristics of single-chain Fv fragments when fused downstream of the Escherichia coli maltose-binding protein or upstream of a single immunoglobulin-constant domain
    • Hayhurst A. Improved expression characteristics of single-chain Fv fragments when fused downstream of the Escherichia coli maltose-binding protein or upstream of a single immunoglobulin-constant domain Protein Expres. Purif. 18 2000 1 10
    • (2000) Protein Expres. Purif. , vol.18 , pp. 1-10
    • Hayhurst, A.1
  • 73
    • 0037406621 scopus 로고    scopus 로고
    • Isolation and expression of recombinant antibody fragments to the biological warfare pathogen Brucella melitensis
    • Hayhurst A., Happe S., Mabry R., Koch Z., Iverson B., and Georgiou G. Isolation and expression of recombinant antibody fragments to the biological warfare pathogen Brucella melitensis J. Immunol. Methods 276 2003 185 196
    • (2003) J. Immunol. Methods , vol.276 , pp. 185-196
    • Hayhurst, A.1    Happe, S.2    Mabry, R.3    Koch, Z.4    Iverson, B.5    Georgiou, G.6
  • 74
    • 3242886171 scopus 로고    scopus 로고
    • Ribosome display: Cell free protein display technology
    • He M., and Taussig M.J. Ribosome display: Cell free protein display technology Brief. Funct. Genomic. Proteomic. 1 2002 204 212
    • (2002) Brief. Funct. Genomic. Proteomic. , vol.1 , pp. 204-212
    • He, M.1    Taussig, M.J.2
  • 75
    • 0035542874 scopus 로고    scopus 로고
    • Applications of novel affinity cassette methods; Use of peptide fusion handles for the purification of recombinant proteins
    • Hearn M., and Acosta D. Applications of novel affinity cassette methods; use of peptide fusion handles for the purification of recombinant proteins J. Mol. Recognit. 14 2001 323 369
    • (2001) J. Mol. Recognit. , vol.14 , pp. 323-369
    • Hearn, M.1    Acosta, D.2
  • 76
    • 0032054156 scopus 로고    scopus 로고
    • Protein engineering and the development of generic biosensors
    • Hellinga H.W., and Marvin J.S. Protein engineering and the development of generic biosensors Trends Biotechnol. 16 1998 183 189
    • (1998) Trends Biotechnol. , vol.16 , pp. 183-189
    • Hellinga, H.W.1    Marvin, J.S.2
  • 77
    • 0036165438 scopus 로고    scopus 로고
    • Engineering receptors and antibodies for biosensors
    • Hock B., Seifert M., and Kramer K. Engineering receptors and antibodies for biosensors Biosens. Bioelectron. 17 2002 239 249
    • (2002) Biosens. Bioelectron. , vol.17 , pp. 239-249
    • Hock, B.1    Seifert, M.2    Kramer, K.3
  • 78
    • 0037117516 scopus 로고    scopus 로고
    • Selective immobilization of proteins to self-[assembelled?] monolayers presenting active site-directed capture ligands
    • Hodneland C., Lee Y., Min D., and Mrksich M. Selective immobilization of proteins to self-[assembelled?] monolayers presenting active site-directed capture ligands Proc. Natl. Acad. Sci. USA 99 2002 5048 5052
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 5048-5052
    • Hodneland, C.1    Lee, Y.2    Min, D.3    Mrksich, M.4
  • 79
    • 0032170796 scopus 로고    scopus 로고
    • Isolation of single chain antibody fragments with specificity for cell surface antigens by phage display utilising internal image anti-idiotypic antibodies
    • Hombach A., Pohl C., Heuser C., Sircar R., Diehl V., and Abken H. Isolation of single chain antibody fragments with specificity for cell surface antigens by phage display utilising internal image anti-idiotypic antibodies J. Immunol. Methods 218 1998 53 61
    • (1998) J. Immunol. Methods , vol.218 , pp. 53-61
    • Hombach, A.1    Pohl, C.2    Heuser, C.3    Sircar, R.4    Diehl, V.5    Abken, H.6
  • 80
    • 0042889500 scopus 로고    scopus 로고
    • Rapid, Quantitative colorimetric detection of a lectin using mannose-stabilized gold nanoparticles
    • Hone D.C., Haines A.H., and Russell D.A. Rapid, Quantitative colorimetric detection of a lectin using mannose-stabilized gold nanoparticles Langmuir 19 2003 7141 7144
    • (2003) Langmuir , vol.19 , pp. 7141-7144
    • Hone, D.C.1    Haines, A.H.2    Russell, D.A.3
  • 82
    • 0025740577 scopus 로고
    • Multisubunit proteins on the surface of filamentous phage - methodologies for displaying antibody (Fab) heavy and light-chains
    • Hoogenboom H.R., Griffiths A.D., Johnson K.S., Chiswell D.J., Hudson P., and Winter G. Multisubunit proteins on the surface of filamentous phage - methodologies for displaying antibody (Fab) heavy and light-chains Nucleic Acids Res. 19 1991 4133 4137
    • (1991) Nucleic Acids Res. , vol.19 , pp. 4133-4137
    • Hoogenboom, H.R.1    Griffiths, A.D.2    Johnson, K.S.3    Chiswell, D.J.4    Hudson, P.5    Winter, G.6
  • 84
    • 0032448966 scopus 로고    scopus 로고
    • High-density immobilisation of an antibody fragment to a carboxymethylated dextran-linked biosensor surface
    • Howell S., Kenmore M., Kirkland M., and Badley R.A. High-density immobilisation of an antibody fragment to a carboxymethylated dextran-linked biosensor surface J. Mol. Recognit. 11 1998 200 203
    • (1998) J. Mol. Recognit. , vol.11 , pp. 200-203
    • Howell, S.1    Kenmore, M.2    Kirkland, M.3    Badley, R.A.4
  • 85
    • 3142613002 scopus 로고    scopus 로고
    • Development of immunofiltration assay by light addressable potentiometric sensor with genetically biotinylated recombinant antibody for rapid identification of Venezuelan equine encephalitis virus
    • Hu W., Thompson H., Alvi A., Nagata L., Suresh M., and Fulton R. Development of immunofiltration assay by light addressable potentiometric sensor with genetically biotinylated recombinant antibody for rapid identification of Venezuelan equine encephalitis virus J. Immunol. Methods 289 2004 27 35
    • (2004) J. Immunol. Methods , vol.289 , pp. 27-35
    • Hu, W.1    Thompson, H.2    Alvi, A.3    Nagata, L.4    Suresh, M.5    Fulton, R.6
  • 86
    • 0346158535 scopus 로고    scopus 로고
    • Mating antibody phage display with proteomics
    • Hust M., and Dübel S. Mating antibody phage display with proteomics Trends Biotechnol. 22 2004 8 14
    • (2004) Trends Biotechnol. , vol.22 , pp. 8-14
    • Hust, M.1    Dübel, S.2
  • 88
    • 7544230375 scopus 로고    scopus 로고
    • Virus detection using nanoelectromechanical devices
    • Ilic B., Yang Y., and Craighead H.G. Virus detection using nanoelectromechanical devices App. Phys. Lett. 85 2004 2604 2606
    • (2004) App. Phys. Lett. , vol.85 , pp. 2604-2606
    • Ilic, B.1    Yang, Y.2    Craighead, H.G.3
  • 90
    • 0029931209 scopus 로고    scopus 로고
    • Affinity maturation of recombinant antibodies using E. coli mutator cells
    • Irving R.A., Kortt A.A., and Hudson P.J. Affinity maturation of recombinant antibodies using E. coli mutator cells Immunotechnology 2 1996 127 143
    • (1996) Immunotechnology , vol.2 , pp. 127-143
    • Irving, R.A.1    Kortt, A.A.2    Hudson, P.J.3
  • 91
    • 0033008183 scopus 로고    scopus 로고
    • Application of recombinant Fab fragment from a phage display library for sensitive detection of target antigen by an inhibitory ELISA system
    • Itoh K., Suzuki K., Ishiwata S., Tezuke T., Mizugaki M., and Suzuki T. Application of recombinant Fab fragment from a phage display library for sensitive detection of target antigen by an inhibitory ELISA system J. Immunol. Methods 203 1999 107 114
    • (1999) J. Immunol. Methods , vol.203 , pp. 107-114
    • Itoh, K.1    Suzuki, K.2    Ishiwata, S.3    Tezuke, T.4    Mizugaki, M.5    Suzuki, T.6
  • 95
    • 12444264902 scopus 로고    scopus 로고
    • Selection of optical biosensors from chemisynthetic antibody libraries
    • Jespers L., Bonnert T.P., and Winter G. Selection of optical biosensors from chemisynthetic antibody libraries Protein Eng. Des. Sel. 17 2004 709 713
    • (2004) Protein Eng. Des. Sel. , vol.17 , pp. 709-713
    • Jespers, L.1    Bonnert, T.P.2    Winter, G.3
  • 97
    • 0037376769 scopus 로고    scopus 로고
    • A protocol for "enhanced pepsin digestion": A step by step method for obtaining pure antibody fragments in high yield from serum
    • Jones R.G.A., and Landon J. A protocol for "enhanced pepsin digestion": A step by step method for obtaining pure antibody fragments in high yield from serum J. Immunol. Methods 275 2003 239 250
    • (2003) J. Immunol. Methods , vol.275 , pp. 239-250
    • Jones, R.G.A.1    Landon, J.2
  • 98
    • 0033885436 scopus 로고    scopus 로고
    • Electrochemical study of a metallothionein modified gold disk electrode and its action on Hg2+ cations
    • Ju H., and Leech D. Electrochemical study of a metallothionein modified gold disk electrode and its action on Hg2+ cations J. Electroanal. chem. 484 2000 150 156
    • (2000) J. Electroanal. Chem. , vol.484 , pp. 150-156
    • Ju, H.1    Leech, D.2
  • 99
    • 1842295679 scopus 로고    scopus 로고
    • Improving in vivo folding and stability of a single-chain Fv antibody fragment by loop grafting
    • Jung S., and Pluckthun A. Improving in vivo folding and stability of a single-chain Fv antibody fragment by loop grafting Protein Eng. 10 1997 959 966
    • (1997) Protein Eng. , vol.10 , pp. 959-966
    • Jung, S.1    Pluckthun, A.2
  • 100
    • 0036296338 scopus 로고    scopus 로고
    • Production of functional single-chain Fv antibodies in the cytoplasm of Escherichia coli
    • Jurado P., Ritz D., Beckwith J., de Lorenzo V., and Fernandez L. Production of functional single-chain Fv antibodies in the cytoplasm of Escherichia coli J. Mol. Biol. 320 2002 1 10
    • (2002) J. Mol. Biol. , vol.320 , pp. 1-10
    • Jurado, P.1    Ritz, D.2    Beckwith, J.3    De Lorenzo, V.4    Fernandez, L.5
  • 101
    • 0024511736 scopus 로고
    • Expression of the blue copper protein azurin from Pseudomonas aeruginosa in Escherichia coli
    • Karlsson B., Pascher T., Nordling M., Arvidsson R., and Lundberg L. Expression of the blue copper protein azurin from Pseudomonas aeruginosa in Escherichia coli FEBS Lett. 246 1989 211 217
    • (1989) FEBS Lett. , vol.246 , pp. 211-217
    • Karlsson, B.1    Pascher, T.2    Nordling, M.3    Arvidsson, R.4    Lundberg, L.5
  • 102
    • 0036462607 scopus 로고    scopus 로고
    • Recent Advances in the synthesis of sialic acid derivatives and sialylmimetics as biological probes
    • Kiefel M.J., and Itzstein M. Recent Advances in the synthesis of sialic acid derivatives and sialylmimetics as biological probes Chem. Rev. 102 2002 471 490
    • (2002) Chem. Rev. , vol.102 , pp. 471-490
    • Kiefel, M.J.1    Itzstein, M.2
  • 103
    • 14744271625 scopus 로고
    • Protein aggregation in vitro and in vivo: A quantitative model of the kinetic competition between folding and aggregation
    • Kiefhaber T., Rudolf R., Kohler H., and Buchner J. Protein aggregation in vitro and in vivo: A quantitative model of the kinetic competition between folding and aggregation Biotechnology 9 1991 825 829
    • (1991) Biotechnology , vol.9 , pp. 825-829
    • Kiefhaber, T.1    Rudolf, R.2    Kohler, H.3    Buchner, J.4
  • 104
    • 0028001154 scopus 로고
    • Recombinant single-chain Fv fragments carrying C-terminal cysteine residues: Production of bivalent and biotinylated antibodies
    • Kipriyanov S.M., Dubel S., Beitling F., Kontermann R., and Little M. Recombinant single-chain Fv fragments carrying C-terminal cysteine residues: Production of bivalent and biotinylated antibodies Mol. Immunol. 31 1994 1047 1058
    • (1994) Mol. Immunol. , vol.31 , pp. 1047-1058
    • Kipriyanov, S.M.1    Dubel, S.2    Beitling, F.3    Kontermann, R.4    Little, M.5
  • 105
    • 0842330081 scopus 로고    scopus 로고
    • Generation and production of engineered antibodies
    • Kipriyanov S., and Le Gall F. Generation and production of engineered antibodies Mol. Biotechnol. 26 2004 39 60
    • (2004) Mol. Biotechnol. , vol.26 , pp. 39-60
    • Kipriyanov, S.1    Le Gall, F.2
  • 107
    • 0033593238 scopus 로고    scopus 로고
    • Towards the design of an antibody that recognizes a given protein epitope
    • Kirkham P.M., Neri D., and Winter G. Towards the design of an antibody that recognizes a given protein epitope J. Mol. Biol. 285 1999 909 915
    • (1999) J. Mol. Biol. , vol.285 , pp. 909-915
    • Kirkham, P.M.1    Neri, D.2    Winter, G.3
  • 109
    • 0028966985 scopus 로고
    • Engineered turns of a recombinant antibody improve its in vivo folding
    • Knappik A., and Plückthun A. Engineered turns of a recombinant antibody improve its in vivo folding Protein Eng. 8 1995 81 89
    • (1995) Protein Eng. , vol.8 , pp. 81-89
    • Knappik, A.1    Plückthun, A.2
  • 111
    • 0031282109 scopus 로고    scopus 로고
    • Nonspecific amine immobilization of ligand can be a potential source of error in BIAcore binding experiments and may reduce binding affinities
    • Kortt A.A., Oddie G.W., Iliades P., Gruen L.C., and Hudson P.J. Nonspecific amine immobilization of ligand can be a potential source of error in BIAcore binding experiments and may reduce binding affinities Anal. Biochem. 253 1997 103 111
    • (1997) Anal. Biochem. , vol.253 , pp. 103-111
    • Kortt, A.A.1    Oddie, G.W.2    Iliades, P.3    Gruen, L.C.4    Hudson, P.J.5
  • 112
    • 0020490722 scopus 로고
    • Mechanisms of ligand-binding by monoclonal anti-fluorescyl antibodies
    • Kranz D.M., Herron J.N., and Voss E.W. Mechanisms of ligand-binding by monoclonal anti-fluorescyl antibodies J. Biol. Chem. 257 1982 6987 6995
    • (1982) J. Biol. Chem. , vol.257 , pp. 6987-6995
    • Kranz, D.M.1    Herron, J.N.2    Voss, E.W.3
  • 113
    • 0031032155 scopus 로고    scopus 로고
    • Reliable cloning of functional antibody variable domains from hybridomas and spleen cell repertoires employing a reengineered phage display system
    • Krebber A., Bornhauser S., Burmester J., Honegger A., Willuda J., Bosshard H.R., and Plückthun A. Reliable cloning of functional antibody variable domains from hybridomas and spleen cell repertoires employing a reengineered phage display system J. Immunol. Methods 201 1997 35 55
    • (1997) J. Immunol. Methods , vol.201 , pp. 35-55
    • Krebber, A.1    Bornhauser, S.2    Burmester, J.3    Honegger, A.4    Willuda, J.5    Bosshard, H.R.6    Plückthun, A.7
  • 114
    • 2442646664 scopus 로고    scopus 로고
    • Living bacterial cell array for genotoxin monitoring
    • Kuang Y., Biran I., and Watt D.R. Living bacterial cell array for genotoxin monitoring Anal. Chem. 76 2004 2902-2809.
    • (2004) Anal. Chem. , vol.76
    • Kuang, Y.1    Biran, I.2    Watt, D.R.3
  • 115
    • 0035424404 scopus 로고    scopus 로고
    • Advances in directed protein evolution by recursive genetic recombination: Applications to therapeutic proteins
    • Kurtzman A.L., Govindarajan S., Vahle K., Jones J.T., Heinrichs V., and Patten P.A. Advances in directed protein evolution by recursive genetic recombination: Applications to therapeutic proteins Curr. Opin. Biotech. 12 2001 361 370
    • (2001) Curr. Opin. Biotech. , vol.12 , pp. 361-370
    • Kurtzman, A.L.1    Govindarajan, S.2    Vahle, K.3    Jones, J.T.4    Heinrichs, V.5    Patten, P.A.6
  • 116
    • 4744345464 scopus 로고    scopus 로고
    • Antibody arrays prepared by cutinase-mediated immobilization on self-assembly monolayers
    • Kwon Y., Han Z., Karatan E., Mrksich M., and Kay B.K. Antibody arrays prepared by cutinase-mediated immobilization on self-assembly monolayers Anal. Chem. 76 2004 5713 5720
    • (2004) Anal. Chem. , vol.76 , pp. 5713-5720
    • Kwon, Y.1    Han, Z.2    Karatan, E.3    Mrksich, M.4    Kay, B.K.5
  • 117
    • 0002694056 scopus 로고
    • A method for random mutagenesis of a defined DNA segment using a modified polymerase chain reaction
    • Leung D.W., Chen E., and Goeddel D.V. A method for random mutagenesis of a defined DNA segment using a modified polymerase chain reaction J. Meth. Cell Mol. Biol. 1 1989 11 15
    • (1989) J. Meth. Cell Mol. Biol. , vol.1 , pp. 11-15
    • Leung, D.W.1    Chen, E.2    Goeddel, D.V.3
  • 118
    • 0034756555 scopus 로고    scopus 로고
    • Production of correctly folded Fab antibody fragment in the cytoplasm of Escherichia coli trxB gor mutants via the coexpression of molecular chaperones
    • Levy R., Weiss R., Chen G., Iverson B., and Georgiou G. Production of correctly folded Fab antibody fragment in the cytoplasm of Escherichia coli trxB gor mutants via the coexpression of molecular chaperones Protein Expres. Purif. 23 2001 338 347
    • (2001) Protein Expres. Purif. , vol.23 , pp. 338-347
    • Levy, R.1    Weiss, R.2    Chen, G.3    Iverson, B.4    Georgiou, G.5
  • 119
    • 3142685154 scopus 로고    scopus 로고
    • In vitro protein evolution by ribosome display and mRNA display
    • Lipovsek D., and Pluckthun A. In vitro protein evolution by ribosome display and mRNA display J. Immunol. Methods 290 2004 51 67
    • (2004) J. Immunol. Methods , vol.290 , pp. 51-67
    • Lipovsek, D.1    Pluckthun, A.2
  • 120
    • 0036883537 scopus 로고    scopus 로고
    • Copper proteins immobilized on gold electrodes for (bio)analytical studies
    • Lisdat F., and Karube I. Copper proteins immobilized on gold electrodes for (bio)analytical studies Biosens. Bioelectron. 17 2002 1051 1057
    • (2002) Biosens. Bioelectron. , vol.17 , pp. 1051-1057
    • Lisdat, F.1    Karube, I.2
  • 121
    • 0036712790 scopus 로고    scopus 로고
    • An aptamer-based quartz crystal protein biosensor
    • Liss M., Peterson B., and Prohaska E. An aptamer-based quartz crystal protein biosensor Anal. Chem. 74 2002 4488 4495
    • (2002) Anal. Chem. , vol.74 , pp. 4488-4495
    • Liss, M.1    Peterson, B.2    Prohaska, E.3
  • 122
    • 0005229135 scopus 로고    scopus 로고
    • Mimicking somatic hypermutation: Affinity maturation of antibodies displayed on bacteriophage using a bacterial mutator strain
    • Low N.M., Holliger P., and Winter Mimicking somatic hypermutation: Affinity maturation of antibodies displayed on bacteriophage using a bacterial mutator strain J. Mol. Biol. 260 1996 359 368
    • (1996) J. Mol. Biol. , vol.260 , pp. 359-368
    • Low, N.M.1    Holliger, P.2    Winter3
  • 123
    • 0033023649 scopus 로고    scopus 로고
    • Chemoselective biosensors
    • Lowe C.R. Chemoselective biosensors Curr. Opin. Chem. Biol. 3 1999 106 111
    • (1999) Curr. Opin. Chem. Biol. , vol.3 , pp. 106-111
    • Lowe, C.R.1
  • 124
    • 0029841258 scopus 로고    scopus 로고
    • Construction and expression of bi-functional proteins of single-chain Fv with effector domains
    • Luo D., Mah N., Wishart D., Zhang Y., Jacobs F., and Martin L. Construction and expression of bi-functional proteins of single-chain Fv with effector domains J. Biochem. 120 1996 229 232
    • (1996) J. Biochem. , vol.120 , pp. 229-232
    • Luo, D.1    Mah, N.2    Wishart, D.3    Zhang, Y.4    Jacobs, F.5    Martin, L.6
  • 126
    • 0035161282 scopus 로고    scopus 로고
    • Immunosensors - Principles and applications to clinical chemistry (Review)
    • Luppa P.B., Sokoll L.J., and Chan D.W. Immunosensors - principles and applications to clinical chemistry (Review) Clin. Chim. Acta 314 2001 1 26
    • (2001) Clin. Chim. Acta , vol.314 , pp. 1-26
    • Luppa, P.B.1    Sokoll, L.J.2    Chan, D.W.3
  • 129
    • 0030896261 scopus 로고    scopus 로고
    • The rational design of allosteric interactions in a monomeric protein and its applications to the construction of biosensors
    • Marvin J.S., Corcoran E.E., Hattangadi N.A., Zhang J.V., Gere S.A., and Hellinga H.W. The rational design of allosteric interactions in a monomeric protein and its applications to the construction of biosensors Proc. Natl. Acad. Sci. USA 94 1997 4366 4371
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 4366-4371
    • Marvin, J.S.1    Corcoran, E.E.2    Hattangadi, N.A.3    Zhang, J.V.4    Gere, S.A.5    Hellinga, H.W.6
  • 130
    • 0032515425 scopus 로고    scopus 로고
    • Engineering biosensors by introducing fluorescent allosteric signal transducers: Construction of a novel glucose sensor
    • Marvin J.S., and Hellinga H.W. Engineering biosensors by introducing fluorescent allosteric signal transducers: Construction of a novel glucose sensor J. Am. Chem. Soc. 120 1998 7 11
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 7-11
    • Marvin, J.S.1    Hellinga, H.W.2
  • 131
    • 0025226085 scopus 로고
    • Phage display antibodies: Filamentous phage displaying antibody variable domains
    • McCafferty J., Griffiths A.D., Winter G., and Chiswell D.J. Phage display antibodies: Filamentous phage displaying antibody variable domains Nature 348 1990 552 554
    • (1990) Nature , vol.348 , pp. 552-554
    • McCafferty, J.1    Griffiths, A.D.2    Winter, G.3    Chiswell, D.J.4
  • 132
    • 0035342475 scopus 로고    scopus 로고
    • Altering the fine specificity of an anti-Legionella single chain antibody by a single amino acid insertion
    • McCarthy B.J., and Hill A.S. Altering the fine specificity of an anti-Legionella single chain antibody by a single amino acid insertion J. Immunol. Methods 251 2001 137 147
    • (2001) J. Immunol. Methods , vol.251 , pp. 137-147
    • McCarthy, B.J.1    Hill, A.S.2
  • 134
    • 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., and Wittrup K.D. Substantial energetic improvement with minimal structural perturbation in a high affinity mutant antibody J. Mol. Biol. 343 2004 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
  • 135
    • 0031797448 scopus 로고    scopus 로고
    • Mutators in E. coli
    • Miller J.H. Mutators in E. coli Mutat. Res. 409 1998 99 106
    • (1998) Mutat. Res. , vol.409 , pp. 99-106
    • Miller, J.H.1
  • 136
    • 0033023075 scopus 로고    scopus 로고
    • Changes in the specificity of antibodies by site-specific mutagenesis followed by random mutagenesis
    • Miyazaki C., Iba Y., Yamada Y., Takahashi H., Sawada J., and Kurosawa Y. Changes in the specificity of antibodies by site-specific mutagenesis followed by random mutagenesis Protein Eng. 12 1999 407 415
    • (1999) Protein Eng. , vol.12 , pp. 407-415
    • Miyazaki, C.1    Iba, Y.2    Yamada, Y.3    Takahashi, H.4    Sawada, J.5    Kurosawa, Y.6
  • 137
    • 0141656689 scopus 로고    scopus 로고
    • Identification of scFv antibody fragments that specifically recognise the heroin metabolite 6-monoacetylmorphine but not morphine
    • Moghaddam A., Borgen T., Stacy J., Kausmally L., Simonsen B., Marvik O.L., Brekke O.L., and Braunagel M. Identification of scFv antibody fragments that specifically recognise the heroin metabolite 6-monoacetylmorphine but not morphine J. Immunol. Methods 280 2003 139 155
    • (2003) J. Immunol. Methods , vol.280 , pp. 139-155
    • Moghaddam, A.1    Borgen, T.2    Stacy, J.3    Kausmally, L.4    Simonsen, B.5    Marvik, O.L.6    Brekke, O.L.7    Braunagel, M.8
  • 138
    • 1642329356 scopus 로고    scopus 로고
    • Computational challenges in combinatorial library design for protein engineering
    • Moore G.L., and Maranas C.D. Computational challenges in combinatorial library design for protein engineering Am. Inst. Chem. Eng. 50 2004 262 272
    • (2004) Am. Inst. Chem. Eng. , vol.50 , pp. 262-272
    • Moore, G.L.1    Maranas, C.D.2
  • 139
    • 0002239134 scopus 로고    scopus 로고
    • Silica-precipitating peptides isolated from a combinatorial phage display peptide library
    • Naik R., Brott L., Clarson S., and Stone M. Silica-precipitating peptides isolated from a combinatorial phage display peptide library J. Nanosci. Nanotechnol. 2 2002 95 100
    • (2002) J. Nanosci. Nanotechnol. , vol.2 , pp. 95-100
    • Naik, R.1    Brott, L.2    Clarson, S.3    Stone, M.4
  • 140
    • 0029986466 scopus 로고    scopus 로고
    • Purification and characterization of intact and truncated forms of the Escherichia coli biotin carboxyl carrier subunit of acetyl-CoA carboxylase
    • Nenortas E., and Beckett D. Purification and characterization of intact and truncated forms of the Escherichia coli biotin carboxyl carrier subunit of acetyl-CoA carboxylase J. Biochem. 271 1996 7559 7567
    • (1996) J. Biochem. , vol.271 , pp. 7559-7567
    • Nenortas, E.1    Beckett, D.2
  • 141
    • 0030965970 scopus 로고    scopus 로고
    • Disrupting the hydrophobic patches at the antibody variable/constant domain interface: Improved in vivo folding and physical characterization of an engineered scFv fragment
    • Nieba L., Honegger A., Krebber C., and Pluckthun A. Disrupting the hydrophobic patches at the antibody variable/constant domain interface: Improved in vivo folding and physical characterization of an engineered scFv fragment Protein Eng. 10 1997 435 444
    • (1997) Protein Eng. , vol.10 , pp. 435-444
    • Nieba, L.1    Honegger, A.2    Krebber, C.3    Pluckthun, A.4
  • 143
    • 0035975883 scopus 로고    scopus 로고
    • The solid phase in affinity chromatography: Strategies for antibody attachment
    • Nisnevitch M., and Firer M.A. The solid phase in affinity chromatography: Strategies for antibody attachment J. Biochem. Bioph. Meth. 49 2001 467 480
    • (2001) J. Biochem. Bioph. Meth. , vol.49 , pp. 467-480
    • Nisnevitch, M.1    Firer, M.A.2
  • 145
    • 0021924914 scopus 로고
    • Immunosensors - antibody-based biosensors
    • North J.R. Immunosensors - antibody-based biosensors Trends Biotechnol. 3 1985 180 186
    • (1985) Trends Biotechnol. , vol.3 , pp. 180-186
    • North, J.R.1
  • 146
    • 0033894171 scopus 로고    scopus 로고
    • Characterization of self-assembled monolayers for biosensor applications
    • Nyquist R.M., Eberhardt A.S., Silks L.A., Li Z., Yang X., and Swanson B.I. Characterization of self-assembled monolayers for biosensor applications Langmuir 16 2000 1793 1800
    • (2000) Langmuir , vol.16 , pp. 1793-1800
    • Nyquist, R.M.1    Eberhardt, A.S.2    Silks, L.A.3    Li, Z.4    Yang, X.5    Swanson, B.I.6
  • 147
    • 0029950981 scopus 로고    scopus 로고
    • Improved cloning of antibody variable regions from hybridomas by an antisense-directed RNase H digestion of the P3-X63-Ag8.653 derived pseudogene mRNA
    • Ostermeier C., and Michel H. Improved cloning of antibody variable regions from hybridomas by an antisense-directed RNase H digestion of the P3-X63-Ag8.653 derived pseudogene mRNA Nucleic Acids Res. 24 1996 1979 1980
    • (1996) Nucleic Acids Res. , vol.24 , pp. 1979-1980
    • Ostermeier, C.1    Michel, H.2
  • 148
    • 0032977886 scopus 로고    scopus 로고
    • An in vivo library-versus-library selection of optimized protein-protein interactions
    • Pelletier J., Arndt K., Pluckthun A., and Michnick S. An in vivo library-versus-library selection of optimized protein-protein interactions Nature Biotechnol. 17 1999 683 690
    • (1999) Nature Biotechnol. , vol.17 , pp. 683-690
    • Pelletier, J.1    Arndt, K.2    Pluckthun, A.3    Michnick, S.4
  • 150
    • 0033959461 scopus 로고    scopus 로고
    • Development of instrumentation to allow the detection of microorganisms using light scattering in combination with surface plasmon resonance
    • Perkins E.A., and Squirrel D.J. Development of instrumentation to allow the detection of microorganisms using light scattering in combination with surface plasmon resonance Biosens. Bioelectron. 14 2000 853 859
    • (2000) Biosens. Bioelectron. , vol.14 , pp. 853-859
    • Perkins, E.A.1    Squirrel, D.J.2
  • 151
    • 0037401049 scopus 로고    scopus 로고
    • Phage display for detection of biological threat agents
    • Petrenko V.A., and Vodyanoy V.J. Phage display for detection of biological threat agents J. Microbiol. Meth. 53 2003 253 262
    • (2003) J. Microbiol. Meth. , vol.53 , pp. 253-262
    • Petrenko, V.A.1    Vodyanoy, V.J.2
  • 152
    • 0032029523 scopus 로고    scopus 로고
    • Genetic engineering of single-chain antibody fragment for surface immobilization in an optical biosensor
    • Piervincenzi R.T., Reichart W.M., and Hellinga H.W. Genetic engineering of single-chain antibody fragment for surface immobilization in an optical biosensor Biosens. Bioelectron. 13 1998 305 312
    • (1998) Biosens. Bioelectron. , vol.13 , pp. 305-312
    • Piervincenzi, R.T.1    Reichart, W.M.2    Hellinga, H.W.3
  • 153
    • 0016717761 scopus 로고
    • Metal chelate affinity chomatography, a new approach to protein fractionation
    • Porath J., Carlsson J., Olsson I., and Belfrage G. Metal chelate affinity chomatography, a new approach to protein fractionation Nature 258 1975 598 599
    • (1975) Nature , vol.258 , pp. 598-599
    • Porath, J.1    Carlsson, J.2    Olsson, I.3    Belfrage, G.4
  • 154
    • 0344813702 scopus 로고    scopus 로고
    • Antibody scFv fragments without disulfide bonds made by molecular evolution
    • Proba K., Worn A., Honegger A., and Plückthun A. Antibody scFv fragments without disulfide bonds made by molecular evolution J. Mol. Biol. 275 1998 245 253
    • (1998) J. Mol. Biol. , vol.275 , pp. 245-253
    • Proba, K.1    Worn, A.2    Honegger, A.3    Plückthun, A.4
  • 156
    • 1242318694 scopus 로고    scopus 로고
    • Identification of proteins in the exosporium of Bacillus anthracis.
    • Redmond C., Baillie L.W.J., Hibbs S., Moir A.J.G., and Moir A. Identification of proteins in the exosporium of Bacillus anthracis. Microbiology 150 2004 355 363
    • (2004) Microbiology , vol.150 , pp. 355-363
    • Redmond, C.1    Baillie, L.W.J.2    Hibbs, S.3    Moir, A.J.G.4    Moir, A.5
  • 158
    • 0036306954 scopus 로고    scopus 로고
    • Knowledge-based design of reagentless fluorescent biosensors from recombinant antibodies
    • Renard M., Belkadi L., Hugo N., England P., Altschuh D., and Bedouelle H. Knowledge-based design of reagentless fluorescent biosensors from recombinant antibodies J. Mol. Biol. 318 2002 429 442
    • (2002) J. Mol. Biol. , vol.318 , pp. 429-442
    • Renard, M.1    Belkadi, L.2    Hugo, N.3    England, P.4    Altschuh, D.5    Bedouelle, H.6
  • 159
    • 0037423703 scopus 로고    scopus 로고
    • Deriving topological constraints from functional data for the design of reagentless fluorescent immunosensors
    • Renard M., Belkadi L., and Bedouelle H. Deriving topological constraints from functional data for the design of reagentless fluorescent immunosensors J. Mol. Biol. 326 2003 167 175
    • (2003) J. Mol. Biol. , vol.326 , pp. 167-175
    • Renard, M.1    Belkadi, L.2    Bedouelle, H.3
  • 160
    • 0033955735 scopus 로고    scopus 로고
    • Advances in surface plasmon resonance biosensor analysis
    • Rich R., and Myska D. Advances in surface plasmon resonance biosensor analysis Curr. Opin. Biotech. 11 2000 54 61
    • (2000) Curr. Opin. Biotech. , vol.11 , pp. 54-61
    • Rich, R.1    Myska, D.2
  • 161
    • 11244313892 scopus 로고    scopus 로고
    • Survey of the year 2003 commercial optical biosensor literature
    • Rich R.L., and Myszka D.G. Survey of the year 2003 commercial optical biosensor literature J. Mol. Recognit. 18 2005 1 39
    • (2005) J. Mol. Recognit. , vol.18 , pp. 1-39
    • Rich, R.L.1    Myszka, D.G.2
  • 163
    • 1042269588 scopus 로고    scopus 로고
    • Electronic nanodevices based on self-assembled metalloproteins
    • Rinaldi R., and Cingolani R. Electronic nanodevices based on self-assembled metalloproteins Physica. E 21 2004 45 60
    • (2004) Physica. e , vol.21 , pp. 45-60
    • Rinaldi, R.1    Cingolani, R.2
  • 164
    • 0030817279 scopus 로고    scopus 로고
    • RNA-peptide fusion for the in vitro selection of peptides and proteins
    • Roberts R.W., and Szostak J.W. RNA-peptide fusion for the in vitro selection of peptides and proteins Proc. Natl. Acad. Sci. USA 94 1997 12297 12302
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 12297-12302
    • Roberts, R.W.1    Szostak, J.W.2
  • 165
    • 7944222460 scopus 로고    scopus 로고
    • Light-chain shuffling results in successful phage display selection of functional prokaryotic - expressed antibody fragments to N-glycolyl GM3 ganglioside
    • Rojas G., Talavera A., Munoz Y., Rengifo E., Krengel U., Angstrom J., Gavilondo J., and Moreno E. Light-chain shuffling results in successful phage display selection of functional prokaryotic - expressed antibody fragments to N-glycolyl GM3 ganglioside J. Immunol. Methods 293 2004 71 83
    • (2004) J. Immunol. Methods , vol.293 , pp. 71-83
    • Rojas, G.1    Talavera, A.2    Munoz, Y.3    Rengifo, E.4    Krengel, U.5    Angstrom, J.6    Gavilondo, J.7    Moreno, E.8
  • 166
    • 0032578554 scopus 로고    scopus 로고
    • Structural analysis of the nurse shark (new) antigen receptor (NAR): Molecular convergence of NAR and unusual mammalian immunoglobulins
    • Roux K.H., Greenberg A.S., Greene L., Strelets L., Avila D., Churchill Mikinney E., and Flajnik M.F. Structural analysis of the nurse shark (new) antigen receptor (NAR): Molecular convergence of NAR and unusual mammalian immunoglobulins Proc. Natl. Acad. Sci. USA 95 1998 11804 11809
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 11804-11809
    • Roux, K.H.1    Greenberg, A.S.2    Greene, L.3    Strelets, L.4    Avila, D.5    Churchill Mikinney, E.6    Flajnik, M.F.7
  • 167
    • 0027172622 scopus 로고
    • Retroviral vectors displaying functional antibody fragments
    • Russell S.J., Hawkins R.E., and Winter G. Retroviral vectors displaying functional antibody fragments Nucleic Acids Res. 21 1993 1081 1085
    • (1993) Nucleic Acids Res. , vol.21 , pp. 1081-1085
    • Russell, S.J.1    Hawkins, R.E.2    Winter, G.3
  • 168
    • 0347634531 scopus 로고    scopus 로고
    • Production of a biotinylated single-chain antibody fragment in the cytoplasm of Escherichia coli
    • Santala V., and Lamminmaki U. Production of a biotinylated single-chain antibody fragment in the cytoplasm of Escherichia coli J. Immunol. Methods 284 2004 165 175
    • (2004) J. Immunol. Methods , vol.284 , pp. 165-175
    • Santala, V.1    Lamminmaki, U.2
  • 169
    • 0039310043 scopus 로고
    • Use of peptide libraries to map the substrate specificity of a peptide-modifying enzyme: A 13-residue consensus peptide specifies biotinylation in Escherichia coli
    • Schatz P. Use of peptide libraries to map the substrate specificity of a peptide-modifying enzyme: A 13-residue consensus peptide specifies biotinylation in Escherichia coli Biotechnology 11 1993 1138 1143
    • (1993) Biotechnology , vol.11 , pp. 1138-1143
    • Schatz, P.1
  • 170
    • 0037071907 scopus 로고    scopus 로고
    • Prevention and reversion of protein aggregation by molecular chaperones in the E. coli cytosol: Implications for their applicability in biotechnology
    • Schlieker C., Bukau B., and Mogk A. Prevention and reversion of protein aggregation by molecular chaperones in the E. coli cytosol: Implications for
    • (2002) J. Biotechnol. , vol.96 , pp. 13-21
    • Schlieker, C.1    Bukau, B.2    Mogk, A.3
  • 171
    • 0034726412 scopus 로고    scopus 로고
    • Effects of unpaired cysteines on yield, solubility and activity of different recombinant antibody constructs expressed in E. coli
    • Schmiedl A., Breitling F., Winter C., Queitsch I., and Dubel S. Effects of unpaired cysteines on yield, solubility and activity of different recombinant antibody constructs expressed in E. coli J. Immunol. Methods 242 2000 101 114
    • (2000) J. Immunol. Methods , vol.242 , pp. 101-114
    • Schmiedl, A.1    Breitling, F.2    Winter, C.3    Queitsch, I.4    Dubel, S.5
  • 173
    • 0344352779 scopus 로고    scopus 로고
    • Silane-modified surfaces for biomaterial immobilization
    • T. Cass F.S. Ligler Oxford Univeristy Press New York
    • Schriver-Lake L.C. Silane-modified surfaces for biomaterial immobilization T. Cass F.S. Ligler "Immobilized Biomolecules in Analysis: A Practical Approach" 1998 Oxford Univeristy Press New York 1 14
    • (1998) "immobilized Biomolecules in Analysis: A Practical Approach" , pp. 1-14
    • Schriver-lake, L.C.1
  • 174
    • 0034541209 scopus 로고    scopus 로고
    • A tetravalent single-chain antibody-streptavidin fusion protein for pretargeted lymphoma therapy
    • Schultz J., Lin Y., Sanderson J., Zuo Y., Stone D., Mallett R., Wilbert S., and Axworthy D. A tetravalent single-chain antibody-streptavidin fusion protein for pretargeted lymphoma therapy Cancer res. 60 2000 6663 6669
    • (2000) Cancer Res. , vol.60 , pp. 6663-6669
    • Schultz, J.1    Lin, Y.2    Sanderson, J.3    Zuo, Y.4    Stone, D.5    Mallett, R.6    Wilbert, S.7    Axworthy, D.8
  • 175
    • 0033823060 scopus 로고    scopus 로고
    • The renaissance of fluorescence resonance energy transfer
    • Selvin P.R. The renaissance of fluorescence resonance energy transfer Nature Struct. Biol. 7 2000 730 734
    • (2000) Nature Struct. Biol. , vol.7 , pp. 730-734
    • Selvin, P.R.1
  • 177
    • 0033865190 scopus 로고    scopus 로고
    • Engineered protein scaffolds for molecular recognition
    • Skerra A. Engineered protein scaffolds for molecular recognition J. Mol. Recognit. 13 2000 167 187
    • (2000) J. Mol. Recognit. , vol.13 , pp. 167-187
    • Skerra, A.1
  • 178
    • 0024292736 scopus 로고
    • Assembly of a functional immunoglobulin-Fv fragment in Escherichia coli
    • Skerra A., and Pluckthun A. Assembly of a functional immunoglobulin-Fv fragment in Escherichia coli Science 240 1988 1038 1041
    • (1988) Science , vol.240 , pp. 1038-1041
    • Skerra, A.1    Pluckthun, A.2
  • 179
    • 0021818675 scopus 로고
    • Filamentous fusion phage - novel expression vectors that display cloned antigens on the virion surface
    • Smith G.P. Filamentous fusion phage - novel expression vectors that display cloned antigens on the virion surface Science 228 1985 1315 1317
    • (1985) Science , vol.228 , pp. 1315-1317
    • Smith, G.P.1
  • 181
    • 0028110130 scopus 로고
    • DNA shuffling by random fragmentation and reassembly in vitro recombination for molecular evolution
    • Stemmer W.P.C. DNA shuffling by random fragmentation and reassembly in vitro recombination for molecular evolution Proc. Natl. Acad. Sci. USA 91 1994 10747 10751
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 10747-10751
    • Stemmer, W.P.C.1
  • 183
    • 0030224828 scopus 로고    scopus 로고
    • Effect of antibody orientation on immunosorbent performance
    • Subramanian A., and Velander A. Effect of antibody orientation on immunosorbent performance J. Mol. Recognit. 9 1996 528 535
    • (1996) J. Mol. Recognit. , vol.9 , pp. 528-535
    • Subramanian, A.1    Velander, A.2
  • 184
    • 13544264496 scopus 로고    scopus 로고
    • Improved secretory production of recombinant proteins by random mutagenesis of hlyB, an alpha-hemolysin transporter from Escherichia coli
    • Sugamata Y., and Shiba T. Improved secretory production of recombinant proteins by random mutagenesis of hlyB, an alpha-hemolysin transporter from Escherichia coli Appl. Environ. Microb. 71 2005 656 662
    • (2005) Appl. Environ. Microb. , vol.71 , pp. 656-662
    • Sugamata, Y.1    Shiba, T.2
  • 185
    • 0037127196 scopus 로고    scopus 로고
    • Structure of an anti-blood group a Fv and improvement of its binding affinity without loss of specificity
    • Thomas R., Patenaude S.I., MacKenzie C.R., To R., Hirama T., Young N.M., and Evans S.V. Structure of an anti-blood group A Fv and improvement of its binding affinity without loss of specificity J. Biol. Chem. 277 2002 2059 2064
    • (2002) J. Biol. Chem. , vol.277 , pp. 2059-2064
    • Thomas, R.1    Patenaude, S.I.2    MacKenzie, C.R.3    To, R.4    Hirama, T.5    Young, N.M.6    Evans, S.V.7
  • 186
    • 0038529792 scopus 로고    scopus 로고
    • Genes of Bacillus cereus and Bacillus anthracis encoding proteins of the exosporium
    • Todd S.J., Moir A.J., Johnson M.J., and Moir A. Genes of Bacillus cereus and Bacillus anthracis encoding proteins of the exosporium J. Bacteriol. 185 2003 3373 3378
    • (2003) J. Bacteriol. , vol.185 , pp. 3373-3378
    • Todd, S.J.1    Moir, A.J.2    Johnson, M.J.3    Moir, A.4
  • 187
    • 0029872080 scopus 로고    scopus 로고
    • A versatile plasmid expression vector for the production of biotinylated proteins by site-specific, enzymatic modification in Escherichia coli
    • Tsao K., DeBarbieri B., Michel H., and Waugh D. A versatile plasmid expression vector for the production of biotinylated proteins by site-specific, enzymatic modification in Escherichia coli Gene 169 1996 59 64
    • (1996) Gene , vol.169 , pp. 59-64
    • Tsao, K.1    Debarbieri, B.2    Michel, H.3    Waugh, D.4
  • 188
    • 0033979167 scopus 로고    scopus 로고
    • Rapid identification of biological warfare agents using an instrument employing a light addressable potentimetric sensor and a flow-through immunofiltration-enzyme assay system
    • Uithoven K.A., Schmidt J.C., and Ballman M.E. Rapid identification of biological warfare agents using an instrument employing a light addressable potentimetric sensor and a flow-through immunofiltration-enzyme assay system Biosens. Bioelectron. 14 2000 761 770
    • (2000) Biosens. Bioelectron. , vol.14 , pp. 761-770
    • Uithoven, K.A.1    Schmidt, J.C.2    Ballman, M.E.3
  • 190
    • 0037494981 scopus 로고    scopus 로고
    • Affinity maturation of Fab antibody fragment by fluorescent-activated cell sorting of yeast-displayed libraries. FEBS
    • van den Beucken T., Pieters H., Steukers M., van der Vaart M., Ladner R.C., Hoogenboom H.R., and Hufton S.E. Affinity maturation of Fab antibody fragment by fluorescent-activated cell sorting of yeast-displayed libraries. FEBS Lett. 546 2003 288 294
    • (2003) Lett. , vol.546 , pp. 288-294
    • Van Den Beucken, T.1    Pieters, H.2    Steukers, M.3    Van Der Vaart, M.4    Ladner, R.C.5    Hoogenboom, H.R.6    Hufton, S.E.7
  • 191
    • 0035253703 scopus 로고    scopus 로고
    • A quantitative assessment of heterogeneity for surface-immobilized proteins
    • Vijayendran R.A., and Leckband D.E. A quantitative assessment of heterogeneity for surface-immobilized proteins Anal. Chem. 73 2001 471 480
    • (2001) Anal. Chem. , vol.73 , pp. 471-480
    • Vijayendran, R.A.1    Leckband, D.E.2
  • 192
    • 0030848801 scopus 로고    scopus 로고
    • Electrochemical biosensor for detection DNA sequences from the pathogenic protozoan Cryptosporidium parvum
    • Wang J., Rivas G., Parrado C., Xiaohua C., and Flair M. Electrochemical biosensor for detection DNA sequences from the pathogenic protozoan Cryptosporidium parvum Talanta 44 1997 2003 2010
    • (1997) Talanta , vol.44 , pp. 2003-2010
    • Wang, J.1    Rivas, G.2    Parrado, C.3    Xiaohua, C.4    Flair, M.5
  • 193
    • 0024461313 scopus 로고
    • Binding activities of a repertoire of single immunoglobulin variable domains secreted from E. coli
    • Ward E.S., Gussow D., Griffiths A.D., Jones P.T., and Winter G. Binding activities of a repertoire of single immunoglobulin variable domains secreted from E. coli Nature 341 1989 544 546
    • (1989) Nature , vol.341 , pp. 544-546
    • Ward, E.S.1    Gussow, D.2    Griffiths, A.D.3    Jones, P.T.4    Winter, G.5
  • 194
    • 0034621827 scopus 로고    scopus 로고
    • Selection of peptides with semiconductor binding specificity for directed nanocrystal assembly
    • Whaley S., English D., Hu E., Barbara P., and Belcher A. Selection of peptides with semiconductor binding specificity for directed nanocrystal assembly Nature 405 2000 665 668
    • (2000) Nature , vol.405 , pp. 665-668
    • Whaley, S.1    English, D.2    Hu, E.3    Barbara, P.4    Belcher, A.5
  • 195
    • 0142072735 scopus 로고    scopus 로고
    • Species-specific peptide ligands for the detection of Bacillus anthracis spores
    • Williams D.D., Benedek O., and Turnbough C.L. Species-specific peptide ligands for the detection of Bacillus anthracis spores Appl. Environ. Microb. 69 2003 6288-6239.
    • (2003) Appl. Environ. Microb. , vol.69
    • Williams, D.D.1    Benedek, O.2    Turnbough, C.L.3
  • 196
    • 0032560552 scopus 로고    scopus 로고
    • Synthetic human antibodies and a strategy for protein engineering
    • Winter G. Synthetic human antibodies and a strategy for protein engineering FEBS Lett. 430 1998 92 94
    • (1998) FEBS Lett. , vol.430 , pp. 92-94
    • Winter, G.1
  • 199
    • 0032524034 scopus 로고    scopus 로고
    • An intrinsically stable antibody scFv fragment can tolerate the loss of both disulphide bonds and fold correctly
    • Wörn A., and Pluckthün A. An intrinsically stable antibody scFv fragment can tolerate the loss of both disulphide bonds and fold correctly FEBS Lett. 427 1998 357 361
    • (1998) FEBS Lett. , vol.427 , pp. 357-361
    • Wörn, A.1    Pluckthün, A.2
  • 200
    • 0025030263 scopus 로고
    • Gene probe coated piezoelectric biosensors for biochemical analysis
    • Wu T.Z., Wang H., and Au L.C. Gene probe coated piezoelectric biosensors for biochemical analysis Clin. J. Microbiol. Immunol. 23 1990 147 154
    • (1990) Clin. J. Microbiol. Immunol. , vol.23 , pp. 147-154
    • Wu, T.Z.1    Wang, H.2    Au, L.C.3
  • 201
    • 0028286019 scopus 로고
    • Protein folding in the periplasm of Escherichia coli
    • Wulfing C., and Pluckthun A. Protein folding in the periplasm of Escherichia coli Mol. Microbiol. 12 1994 685 692
    • (1994) Mol. Microbiol. , vol.12 , pp. 685-692
    • Wulfing, C.1    Pluckthun, A.2
  • 202
    • 0029869449 scopus 로고    scopus 로고
    • An approach to random mutagenesis of DNA using mixtures of triphosphate derivatives of nucleoside analogues
    • Zaccolo M., Williams D.M., Brown D.M., and Gherardi E. An approach to random mutagenesis of DNA using mixtures of triphosphate derivatives of nucleoside analogues J. Mol. Biol. 255 1996 589 603
    • (1996) J. Mol. Biol. , vol.255 , pp. 589-603
    • Zaccolo, M.1    Williams, D.M.2    Brown, D.M.3    Gherardi, E.4
  • 203
    • 0036417347 scopus 로고    scopus 로고
    • Overexpression of DsbC and DsbG markedly improves soluble and functional expression of single-chain Fv antibodies in Escherichia coli
    • Zhang Z., Li Z., Wang F., Fang M., Yin C., Zhou Z., Lin Q., and Huang H. Overexpression of DsbC and DsbG markedly improves soluble and functional expression of single-chain Fv antibodies in Escherichia coli Protein Expres. Purif. 26 2002 218 228
    • (2002) Protein Expres. Purif. , vol.26 , pp. 218-228
    • Zhang, Z.1    Li, Z.2    Wang, F.3    Fang, M.4    Yin, C.5    Zhou, Z.6    Lin, Q.7    Huang, H.8
  • 205
    • 0038308559 scopus 로고    scopus 로고
    • Production of a functional catalytic antibody ScFv-NusA fusion protein in bacterial cytoplasm
    • Zheng L., Baumann U., and Reymond J.L. Production of a functional catalytic antibody ScFv-NusA fusion protein in bacterial cytoplasm J. Biochem. 133 2003 577 581
    • (2003) J. Biochem. , vol.133 , pp. 577-581
    • Zheng, L.1    Baumann, U.2    Reymond, J.L.3
  • 206
    • 1642540197 scopus 로고    scopus 로고
    • Synthetic hosts via molecular imprinting - Are universal synthetic receptors realistically possible?
    • Zimmerman S.C., and Lemcoff N.G. Synthetic hosts via molecular imprinting - are universal synthetic receptors realistically possible? Chem. Commun. 1 2004 5 14
    • (2004) Chem. Commun. , vol.1 , pp. 5-14
    • Zimmerman, S.C.1    Lemcoff, N.G.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.