메뉴 건너뛰기




Volumn 290, Issue 1-2, 2004, Pages 51-67

In-vitro protein evolution by ribosome display and mRNA display

Author keywords

mRNA display; PCR; Ribosome display

Indexed keywords

ANKYRIN; ANTIBODY; ENZYME; FIBRONECTIN; ISOPROTEIN; MESSENGER RNA; PEPTIDE; PROTEIN; PUROMYCIN;

EID: 3142685154     PISSN: 00221759     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jim.2004.04.008     Document Type: Review
Times cited : (299)

References (71)
  • 4
    • 0036839270 scopus 로고    scopus 로고
    • Sequence analysis of an artificial family of RNA-binding peptides
    • Barrick J.E., Roberts R.W. Sequence analysis of an artificial family of RNA-binding peptides. Protein Sci. 11:2002;2688
    • (2002) Protein Sci. , vol.11 , pp. 2688
    • Barrick, J.E.1    Roberts, R.W.2
  • 5
    • 0034854609 scopus 로고    scopus 로고
    • Selection of RNA-binding peptides using mRNA-peptide fusions
    • Barrick J.E., Takahashi T.T., Balakin A., Roberts R.W. Selection of RNA-binding peptides using mRNA-peptide fusions. Methods. 23:2001;287
    • (2001) Methods , vol.23 , pp. 287
    • Barrick, J.E.1    Takahashi, T.T.2    Balakin, A.3    Roberts, R.W.4
  • 8
    • 0042780350 scopus 로고    scopus 로고
    • Designing repeat proteins: Well-expressed, soluble and stable proteins from combinatorial libraries of consensus ankyrin repeat proteins
    • Binz H.K., Stumpp M.T., Forrer P., Amstutz P., Plückthun A. Designing repeat proteins: well-expressed, soluble and stable proteins from combinatorial libraries of consensus ankyrin repeat proteins. J. Mol. Biol. 332:2003;489
    • (2003) J. Mol. Biol. , vol.332 , pp. 489
    • Binz, H.K.1    Stumpp, M.T.2    Forrer, P.3    Amstutz, P.4    Plückthun, A.5
  • 13
    • 0034708337 scopus 로고    scopus 로고
    • Constructing high complexity synthetic libraries of long ORFs using in vitro selection
    • Cho G., Keefe A.D., Liu R., Wilson D.S., Szostak J.W. Constructing high complexity synthetic libraries of long ORFs using in vitro selection. J. Mol. Biol. 297:2000;309
    • (2000) J. Mol. Biol. , vol.297 , pp. 309
    • Cho, G.1    Keefe, A.D.2    Liu, R.3    Wilson, D.S.4    Szostak, J.W.5
  • 14
    • 0029838624 scopus 로고    scopus 로고
    • PCR fidelity of Pfu DNA polymerase and other thermostable DNA polymerases
    • Cline J., Braman J.C., Hogrefe H.H. PCR fidelity of Pfu DNA polymerase and other thermostable DNA polymerases. Nucleic Acids Res. 24:1996;3546
    • (1996) Nucleic Acids Res. , vol.24 , pp. 3546
    • Cline, J.1    Braman, J.C.2    Hogrefe, H.H.3
  • 16
    • 0036008852 scopus 로고    scopus 로고
    • Selection of v-abl tyrosine kinase substrate sequences from randomized peptide and cellular proteomic libraries using mRNA display
    • Cujec T.P., Medeiros P.F., Hammond P., Rise C., Kreider B.L. Selection of v-abl tyrosine kinase substrate sequences from randomized peptide and cellular proteomic libraries using mRNA display. Chem. Biol. 9:2002;253
    • (2002) Chem. Biol. , vol.9 , pp. 253
    • Cujec, T.P.1    Medeiros, P.F.2    Hammond, P.3    Rise, C.4    Kreider, B.L.5
  • 17
    • 0025004285 scopus 로고
    • Random peptide libraries: A source of specific protein binding molecules
    • Devlin J.J., Panganiban L.C., Devlin P.E. Random peptide libraries: a source of specific protein binding molecules. Science. 249:1990;404
    • (1990) Science , vol.249 , pp. 404
    • Devlin, J.J.1    Panganiban, L.C.2    Devlin, P.E.3
  • 18
    • 0037468685 scopus 로고    scopus 로고
    • A novel strategy to design binding molecules harnessing the modular nature of repeat proteins
    • Forrer P., Stumpp M.T., Binz H.K., Plückthun A. A novel strategy to design binding molecules harnessing the modular nature of repeat proteins. FEBS Lett. 539:2003;2
    • (2003) FEBS Lett. , vol.539 , pp. 2
    • Forrer, P.1    Stumpp, M.T.2    Binz, H.K.3    Plückthun, A.4
  • 20
    • 0035171382 scopus 로고    scopus 로고
    • Emerging views on tmRNA-mediated protein tagging and ribosome rescue
    • Gillet R., Felden B. Emerging views on tmRNA-mediated protein tagging and ribosome rescue. Mol. Microbiol. 42:2001;879
    • (2001) Mol. Microbiol. , vol.42 , pp. 879
    • Gillet, R.1    Felden, B.2
  • 21
    • 0025162270 scopus 로고
    • A comparison of strategies to stabilize immunoglobulin Fv-fragments
    • Glockshuber R., Malia M., Pfitzinger I., Plückthun A. A comparison of strategies to stabilize immunoglobulin Fv-fragments. Biochemistry. 29:1990;1362
    • (1990) Biochemistry , vol.29 , pp. 1362
    • Glockshuber, R.1    Malia, M.2    Pfitzinger, I.3    Plückthun, A.4
  • 22
    • 0035877791 scopus 로고    scopus 로고
    • In vitro selection and characterization of Bcl-X(L)-binding proteins from a mix of tissue-specific mRNA display libraries
    • Hammond P.W., Alpin J., Rise C.E., Wright M., Kreider B.L. In vitro selection and characterization of Bcl-X(L)-binding proteins from a mix of tissue-specific mRNA display libraries. J. Biol. Chem. 276:2001;20898
    • (2001) J. Biol. Chem. , vol.276 , pp. 20898
    • Hammond, P.W.1    Alpin, J.2    Rise, C.E.3    Wright, M.4    Kreider, B.L.5
  • 23
    • 0030974119 scopus 로고    scopus 로고
    • In vitro selection and evolution of functional proteins by using ribosome display
    • Hanes J., Plückthun A. In vitro selection and evolution of functional proteins by using ribosome display. Proc. Natl. Acad. Sci. U. S. A. 94:1997;4937
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 4937
    • Hanes, J.1    Plückthun, A.2
  • 25
    • 0033006949 scopus 로고    scopus 로고
    • Comparison of Escherichia coli and rabbit reticulocyte ribosome display systems
    • Hanes J., Jermutus L., Schaffitzel C., Plückthun A. Comparison of Escherichia coli and rabbit reticulocyte ribosome display systems. FEBS Lett. 450:1999;105
    • (1999) FEBS Lett. , vol.450 , pp. 105
    • Hanes, J.1    Jermutus, L.2    Schaffitzel, C.3    Plückthun, A.4
  • 26
    • 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., Plückthun A. Picomolar affinity antibodies from a fully synthetic naive library selected and evolved by ribosome display. Nat. Biotechnol. 18:2000;1287
    • (2000) Nat. Biotechnol. , vol.18 , pp. 1287
    • Hanes, J.1    Schaffitzel, C.2    Knappik, A.3    Plückthun, A.4
  • 27
    • 0031574037 scopus 로고    scopus 로고
    • Antibody-ribosome-mRNA (ARM) complexes as efficient selection particles for in vitro display and evolution of antibody combining sites
    • He M., Taussig M.J. Antibody-ribosome-mRNA (ARM) complexes as efficient selection particles for in vitro display and evolution of antibody combining sites. Nucleic Acids Res. 25:1997;5132
    • (1997) Nucleic Acids Res. , vol.25 , pp. 5132
    • He, M.1    Taussig, M.J.2
  • 28
    • 0033505816 scopus 로고    scopus 로고
    • Selection of a human anti-progesterone antibody fragment from a transgenic mouse library by ARM ribosome display
    • He M., Menges M., Groves M.A., Corps E., Liu H., Bruggemann M., Taussig M.J. Selection of a human anti-progesterone antibody fragment from a transgenic mouse library by ARM ribosome display. J. Immunol. Methods. 231:1999;105
    • (1999) J. Immunol. Methods , vol.231 , pp. 105
    • He, M.1    Menges, M.2    Groves, M.A.3    Corps, E.4    Liu, H.5    Bruggemann, M.6    Taussig, M.J.7
  • 30
    • 0035251462 scopus 로고    scopus 로고
    • Ribosome display and affinity maturation: From antibodies to single V-domains and steps towards cancer therapeutics
    • Irving R.A., Coia G., Roberts A., Nuttall S.D., Hudson P.J. Ribosome display and affinity maturation: from antibodies to single V-domains and steps towards cancer therapeutics. J. Immunol. Methods. 248:2001;31
    • (2001) J. Immunol. Methods , vol.248 , pp. 31
    • Irving, R.A.1    Coia, G.2    Roberts, A.3    Nuttall, S.D.4    Hudson, P.J.5
  • 32
    • 0032497314 scopus 로고    scopus 로고
    • Disassembly of the post-termination complex and reduction of translational error by ribosome recycling factor (RRF) - A possible new target for antibacterial agents
    • Kaji A., Teyssier E., Hirokawa G. Disassembly of the post-termination complex and reduction of translational error by ribosome recycling factor (RRF) - a possible new target for antibacterial agents. Biochem. Biophys. Res. Commun. 250:1998;1
    • (1998) Biochem. Biophys. Res. Commun. , vol.250 , pp. 1
    • Kaji, A.1    Teyssier, E.2    Hirokawa, G.3
  • 33
    • 0035810165 scopus 로고    scopus 로고
    • Functional proteins from a random-sequence library
    • Keefe A.D., Szostak J.W. Functional proteins from a random-sequence library. Nature. 410:2001;715
    • (2001) Nature , vol.410 , pp. 715
    • Keefe, A.D.1    Szostak, J.W.2
  • 34
    • 0035543198 scopus 로고    scopus 로고
    • One-step purification of recombinant proteins using a nanomolar-affinity streptavidin-binding peptide, the SBP-Tag
    • Keefe A.D., Wilson D.S., Seelig B., Szostak J.W. One-step purification of recombinant proteins using a nanomolar-affinity streptavidin-binding peptide, the SBP-Tag. Protein Expr. Purif. 23:2001;440
    • (2001) Protein Expr. Purif. , vol.23 , pp. 440
    • Keefe, A.D.1    Wilson, D.S.2    Seelig, B.3    Szostak, J.W.4
  • 36
    • 0034306119 scopus 로고    scopus 로고
    • When protein folding is simplified to protein coiling: The continuum of solenoid protein structures
    • Kobe B., Kajava A.V. When protein folding is simplified to protein coiling: the continuum of solenoid protein structures. Trends Biochem. Sci. 25:2000;509
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 509
    • Kobe, B.1    Kajava, A.V.2
  • 38
    • 0032509129 scopus 로고    scopus 로고
    • The fibronectin type III domain as a scaffold for novel binding proteins
    • Koide A., Bailey C.W., Huang X., Koide S. The fibronectin type III domain as a scaffold for novel binding proteins. J. Mol. Biol. 284:1998;1141
    • (1998) J. Mol. Biol. , vol.284 , pp. 1141
    • Koide, A.1    Bailey, C.W.2    Huang, X.3    Koide, S.4
  • 39
    • 0037723843 scopus 로고    scopus 로고
    • Searching sequence space for high-affinity binding peptides using ribosome display
    • Lamla T., Erdmann V.A. Searching sequence space for high-affinity binding peptides using ribosome display. J. Mol. Biol. 329:2003;381
    • (2003) J. Mol. Biol. , vol.329 , pp. 381
    • Lamla, T.1    Erdmann, V.A.2
  • 40
    • 0002694056 scopus 로고
    • A method for random mutagenesis of a defined DNA segment using a modified polymerase chain reaction
    • Leung D.W., Chen E., Goeddel D.V. A method for random mutagenesis of a defined DNA segment using a modified polymerase chain reaction. Technique. 1:1989;11
    • (1989) Technique , vol.1 , pp. 11
    • Leung, D.W.1    Chen, E.2    Goeddel, D.V.3
  • 41
    • 0037189891 scopus 로고    scopus 로고
    • In vitro selection of mRNA display libraries containing an unnatural amino acid
    • Li S., Millward S., Roberts R. In vitro selection of mRNA display libraries containing an unnatural amino acid. J. Am. Chem. Soc. 124:2002;9972
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 9972
    • Li, S.1    Millward, S.2    Roberts, R.3
  • 42
    • 1842577640 scopus 로고    scopus 로고
    • A novel ADP- and zinc-binding fold from function-directed in vitro evolution
    • Lo Surdo P., Walsh M.A., Sollazzo M. A novel ADP- and zinc-binding fold from function-directed in vitro evolution. Nat. Struct. Biol. 11:2004;382
    • (2004) Nat. Struct. Biol. , vol.11 , pp. 382
    • Lo Surdo, P.1    Walsh, M.A.2    Sollazzo, M.3
  • 43
    • 0026496886 scopus 로고
    • The three-dimensional structure of the tenth type III module of fibronectin: An insight into RGD-mediated interactions
    • Main A.L., Harvey T.S., Baron M., Boyd J., Campbell I.D. The three-dimensional structure of the tenth type III module of fibronectin: an insight into RGD-mediated interactions. Cell. 71:1992;671
    • (1992) Cell , vol.71 , pp. 671
    • Main, A.L.1    Harvey, T.S.2    Baron, M.3    Boyd, J.4    Campbell, I.D.5
  • 44
    • 0037468662 scopus 로고    scopus 로고
    • Selection based on the folding properties of proteins with ribosome display
    • Matsuura T., Plückthun A. Selection based on the folding properties of proteins with ribosome display. FEBS Lett. 539:2003;24
    • (2003) FEBS Lett. , vol.539 , pp. 24
    • Matsuura, T.1    Plückthun, A.2
  • 45
    • 0028592703 scopus 로고
    • An in vitro polysome display system for identifying ligands from very large peptide libraries
    • Mattheakis L.C., Bhatt R.R., Dower W.J. An in vitro polysome display system for identifying ligands from very large peptide libraries. Proc. Natl. Acad. Sci. U. S. A. 91:1994;9022
    • (1994) Proc. Natl. Acad. Sci. U. S. A. , vol.91 , pp. 9022
    • Mattheakis, L.C.1    Bhatt, R.R.2    Dower, W.J.3
  • 46
    • 0031559943 scopus 로고    scopus 로고
    • In vitro virus: Bonding of mRNA bearing puromycin at the 3′-terminal end to the C-terminal end of its encoded protein on the ribosome in vitro
    • Nemoto N., Miyamoto-Sato E., Husimi Y., Yanagawa H. In vitro virus: bonding of mRNA bearing puromycin at the 3′-terminal end to the C-terminal end of its encoded protein on the ribosome in vitro. FEBS Lett. 414:1997;405
    • (1997) FEBS Lett. , vol.414 , pp. 405
    • Nemoto, N.1    Miyamoto-Sato, E.2    Husimi, Y.3    Yanagawa, H.4
  • 47
    • 0030822252 scopus 로고    scopus 로고
    • Scaffolds for engineering novel binding sites in proteins
    • Nygren P.A., Uhlen M. Scaffolds for engineering novel binding sites in proteins. Curr. Opin. Struct. Biol. 7:1997;463
    • (1997) Curr. Opin. Struct. Biol. , vol.7 , pp. 463
    • Nygren, P.A.1    Uhlen, M.2
  • 48
    • 0034618493 scopus 로고    scopus 로고
    • Release factors and their role as decoding proteins: Specificity and fidelity for termination of protein synthesis
    • Poole E., Tate W. Release factors and their role as decoding proteins: specificity and fidelity for termination of protein synthesis. Biochim. Biophys. Acta. 1493:2000;1
    • (2000) Biochim. Biophys. Acta , vol.1493 , pp. 1
    • Poole, E.1    Tate, W.2
  • 49
    • 0344813702 scopus 로고    scopus 로고
    • Antibody scFv fragments without disulfide bonds made by molecular evolution
    • Proba K., Wörn A., Honegger A., Plückthun A. Antibody scFv fragments without disulfide bonds made by molecular evolution. J. Mol. Biol. 275:1998;245
    • (1998) J. Mol. Biol. , vol.275 , pp. 245
    • Proba, K.1    Wörn, A.2    Honegger, A.3    Plückthun, A.4
  • 50
    • 0033152942 scopus 로고    scopus 로고
    • Totally in vitro protein selection using mRNA-protein fusions and ribosome display
    • Roberts R.W. Totally in vitro protein selection using mRNA-protein fusions and ribosome display. Curr. Opin. Chem. Biol. 3:1999;268
    • (1999) Curr. Opin. Chem. Biol. , vol.3 , pp. 268
    • Roberts, R.W.1
  • 51
    • 0030817279 scopus 로고    scopus 로고
    • RNA-peptide fusions for the in vitro selection of peptides and proteins
    • Roberts R.W., Szostak J.W. RNA-peptide fusions for the in vitro selection of peptides and proteins. Proc. Natl. Acad. Sci. U. S. A. 94:1997;12297
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 12297
    • Roberts, R.W.1    Szostak, J.W.2
  • 52
    • 0031021109 scopus 로고    scopus 로고
    • Functional antibody production using cell-free translation: Effects of protein disulfide isomerase and chaperones
    • Ryabova L.A., Desplancq D., Spirin A.S., Plückthun A. Functional antibody production using cell-free translation: effects of protein disulfide isomerase and chaperones. Nat. Biotechnol. 15:1997;79
    • (1997) Nat. Biotechnol. , vol.15 , pp. 79
    • Ryabova, L.A.1    Desplancq, D.2    Spirin, A.S.3    Plückthun, A.4
  • 55
    • 0029865819 scopus 로고    scopus 로고
    • Molecular interaction between the Strep-tag affinity peptide and its cognate target, streptavidin
    • Schmidt T.G., Koepke J., Frank R., Skerra A. Molecular interaction between the Strep-tag affinity peptide and its cognate target, streptavidin. J. Mol. Biol. 255:1996;753
    • (1996) J. Mol. Biol. , vol.255 , pp. 753
    • Schmidt, T.G.1    Koepke, J.2    Frank, R.3    Skerra, A.4
  • 57
    • 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
    • (2000) J. Mol. Recognit. , vol.13 , pp. 167
    • Skerra, A.1
  • 58
    • 0028050350 scopus 로고
    • Rapid evolution of a protein in vitro by DNA shuffling
    • Stemmer W.P. Rapid evolution of a protein in vitro by DNA shuffling. Nature. 370:1994;389
    • (1994) Nature , vol.370 , pp. 389
    • Stemmer, W.P.1
  • 59
    • 0043281585 scopus 로고    scopus 로고
    • Designing repeat proteins: Modular leucine-rich repeat protein libraries based on the mammalian ribonuclease inhibitor family
    • Stumpp M.T., Forrer P., Binz H.K., Plückthun A. Designing repeat proteins: modular leucine-rich repeat protein libraries based on the mammalian ribonuclease inhibitor family. J. Mol. Biol. 332:2003;471
    • (2003) J. Mol. Biol. , vol.332 , pp. 471
    • Stumpp, M.T.1    Forrer, P.2    Binz, H.K.3    Plückthun, A.4
  • 60
    • 0037029135 scopus 로고    scopus 로고
    • Ribosome display for selection of active dihydrofolate reductase mutants using immobilized methotrexate on agarose beads
    • Takahashi F., Ebihara T., Mie M., Yanagida Y., Endo Y., Kobatake E., Aizawa M. Ribosome display for selection of active dihydrofolate reductase mutants using immobilized methotrexate on agarose beads. FEBS Lett. 514:2002;106
    • (2002) FEBS Lett. , vol.514 , pp. 106
    • Takahashi, F.1    Ebihara, T.2    Mie, M.3    Yanagida, Y.4    Endo, Y.5    Kobatake, E.6    Aizawa, M.7
  • 61
    • 0037333841 scopus 로고    scopus 로고
    • MRNA display: Ligand discovery, interaction analysis and beyond
    • Takahashi T.T., Austin R.J., Roberts R.W. mRNA display: ligand discovery, interaction analysis and beyond. Trends Biochem. Sci. 28:2003;159
    • (2003) Trends Biochem. Sci. , vol.28 , pp. 159
    • Takahashi, T.T.1    Austin, R.J.2    Roberts, R.W.3
  • 62
    • 0024282746 scopus 로고
    • Fidelity of DNA synthesis by the Thermus aquaticus DNA polymerase
    • Tindall K.R., Kunkel T.A. Fidelity of DNA synthesis by the Thermus aquaticus DNA polymerase. Biochemistry. 27:1988;6008
    • (1988) Biochemistry , vol.27 , pp. 6008
    • Tindall, K.R.1    Kunkel, T.A.2
  • 63
    • 0030780364 scopus 로고    scopus 로고
    • Mutagenesis of a flexible loop in streptavidin leads to higher affinity for the Strep-tag II peptide and improved performance in recombinant protein purification
    • Voss S., Skerra A. Mutagenesis of a flexible loop in streptavidin leads to higher affinity for the Strep-tag II peptide and improved performance in recombinant protein purification. Protein Eng. 10:1997;975
    • (1997) Protein Eng. , vol.10 , pp. 975
    • Voss, S.1    Skerra, A.2
  • 65
  • 66
    • 0032524034 scopus 로고    scopus 로고
    • An intrinsically stable antibody scFv fragment can tolerate the loss of both disulfide bonds and fold correctly
    • Wörn A., Plückthun A. An intrinsically stable antibody scFv fragment can tolerate the loss of both disulfide bonds and fold correctly. FEBS Lett. 427:1998;357
    • (1998) FEBS Lett. , vol.427 , pp. 357
    • Wörn, A.1    Plückthun, A.2
  • 69
    • 0033555718 scopus 로고    scopus 로고
    • The effect of high-frequency random mutagenesis on in vitro protein evolution: A study on TEM-1 beta-lactamase
    • Zaccolo M., Gherardi E. The effect of high-frequency random mutagenesis on in vitro protein evolution: a study on TEM-1 beta-lactamase. J. Mol. Biol. 285:1999;775
    • (1999) J. Mol. Biol. , vol.285 , pp. 775
    • Zaccolo, M.1    Gherardi, E.2
  • 70
    • 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., Gherardi E. An approach to random mutagenesis of DNA using mixtures of triphosphate derivatives of nucleoside analogues. J. Mol. Biol. 255:1996;589
    • (1996) J. Mol. Biol. , vol.255 , pp. 589
    • Zaccolo, M.1    Williams, D.M.2    Brown, D.M.3    Gherardi, E.4
  • 71
    • 2442442119 scopus 로고    scopus 로고
    • Directed in vitro evolution and crystallographic analysis of a peptide binding scFv antibody with low picomolar affinity. J. Biol. Chem. 279, 18870
    • Zahnd C., Spinelli S., Luginbühl B., Amstutz P., Cambillau C., Plückthun A. Directed in vitro evolution and crystallographic analysis of a peptide binding scFv antibody with low picomolar affinity. J. Biol. Chem. 279, 18870. J. Biol. Chem. 279:2004;18870
    • (2004) J. Biol. Chem. , vol.279 , pp. 18870
    • Zahnd, C.1    Spinelli, S.2    Luginbühl, B.3    Amstutz, P.4    Cambillau, C.5    Plückthun, A.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.