Russel, M., Lowman, H.B. & Clackson, T. Introduction to phage biology and phage display. in Phage Display: A Practical Approach (eds. Lowman, H.B. & Clackson, T.) 1–26, (Oxford University Press, New York, USA, 2004). Google Scholar
Sidhu, S.S., Lowman, H.B., Cunningham, B.C. & Wells, J.A. Phage display for selection of novel binding peptides. Methods Enzymol.328, 333–363 (2000). ArticleCASPubMed Google Scholar
Bradbury, A.R. & Marks, J.D. Antibodies from phage antibody libraries. J. Immunol. Methods290, 29–49 (2004). ArticleCASPubMed Google Scholar
Rakonjac, J., Feng, J. & Model, P. Filamentous phage are released from the bacterial membrane by a two-step mechanism involving a short C-terminal fragment of pIII. J. Mol. Biol.289, 1253–1265 (1999). ArticleCASPubMed Google Scholar
Wilson, D.R. & Finlay, B.B. Phage display: applications, innovations, and issues in phage and host biology. Can. J. Microbiol.44, 313–329 (1998). ArticleCASPubMed Google Scholar
Deng, S.J. et al. Selection of antibody single-chain variable fragments with improved carbohydrate binding by phage display. J. Biol. Chem.269, 9533–9538 (1994). CASPubMed Google Scholar
Jung, S. & Plückthun, A. Improving in vivo folding and stability of a single-chain Fv antibody fragment by loop grafting. Protein Eng.10, 959–966 (1997). ArticleCASPubMed Google Scholar
Krebber, A., Burmester, J. & Plückthun, A. Inclusion of an upstream transcriptional terminator in phage display vectors abolishes background expression of toxic fusions with coat protein g3p. Gene178, 71–74 (1996). ArticleCASPubMed Google Scholar
Brinkmann, U., Chowdhury, P.S., Roscoe, D.M. & Pastan, I. Phage display of disulfide-stabilized Fv fragments. J. Immunol. Methods182, 41–50 (1995). ArticleCASPubMed Google Scholar
Rodi, D.J., Soares, A.S. & Makowski, L. Quantitative assessment of peptide sequence diversity in M13 combinatorial peptide phage display libraries. J. Mol. Biol.322, 1039–1052 (2002). ArticleCASPubMed Google Scholar
Krebber, A. et al. Reliable cloning of functional antibody variable domains from hybridomas and spleen cell repertoires employing a reengineered phage display system. J. Immunol. Methods201, 35–55 (1997). ArticleCASPubMed Google Scholar
Bothmann, H. & Plückthun, A. Selection for a periplasmic factor improving phage display and functional periplasmic expression. Nat. Biotechnol.16, 376–380 (1998). ArticleCASPubMed Google Scholar
Bothmann, H. & Plückthun, A. The periplasmic Escherichia coli peptidylprolyl cis,trans-isomerase FkpA. I. Increased functional expression of antibody fragments with and without cis-prolines. J. Biol. Chem.275, 17100–17105 (2000). ArticleCASPubMed Google Scholar
Kramer, R.A. et al. A novel helper phage that improves phage display selection efficiency by preventing the amplification of phages without recombinant protein. Nucleic Acids Res.31, e59 (2003). ArticlePubMedPubMed Central Google Scholar
Baek, H., Suk, K.H., Kim, Y.H. & Cha, S. An improved helper phage system for efficient isolation of specific antibody molecules in phage display. Nucleic Acids Res.30, e18 (2002). ArticlePubMedPubMed Central Google Scholar
Rondot, S., Koch, J., Breitling, F. & Dübel, S. A helper phage to improve single-chain antibody presentation in phage display. Nat. Biotechnol.19, 75–78 (2001). ArticleCASPubMed Google Scholar
Jestin, J.L., Volioti, G. & Winter, G. Improving the display of proteins on filamentous phage. Res. Microbiol.152, 187–191 (2001). ArticleCASPubMed Google Scholar
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, 2–6 (2003). ArticleCASPubMed Google Scholar
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, 489–503 (2003). ArticleCASPubMed Google Scholar
Binz, H.K. et al. High-affinity binders selected from designed ankyrin repeat protein libraries. Nat. Biotechnol.22, 575–582 (2004). ArticleCASPubMed Google Scholar
Amstutz, P. et al. Intracellular kinase inhibitors selected from combinatorial libraries of designed ankyrin repeat proteins. J. Biol. Chem.280, 24715–24722 (2005). ArticleCASPubMed Google Scholar
Fekkes, P. & Driessen, A.J. Protein targeting to the bacterial cytoplasmic membrane. Microbiol. Mol. Biol. Rev.63, 161–173 (1999). CASPubMedPubMed Central Google Scholar
Koch, H.G., Moser, M. & Müller, M. Signal recognition particle-dependent protein targeting, universal to all kingdoms of life. Rev. Physiol. Biochem. Pharmacol.146, 55–94 (2003). ArticleCASPubMed Google Scholar
Valent, Q.A. Signal recognition particle mediated protein targeting in Escherichia coli . Antonie Van Leeuwenhoek79, 17–31 (2001). ArticleCASPubMed Google Scholar
Luirink, J. & Sinning, I. SRP-mediated protein targeting: structure and function revisited. Biochim. Biophys. Acta1694, 17–35 (2004). CASPubMed Google Scholar
Fisher, A.C. & DeLisa, M.P. A little help from my friends: quality control of presecretory proteins in bacteria. J. Bacteriol.186, 7467–7473 (2004). ArticleCASPubMedPubMed Central Google Scholar
Robinson, C. & Bolhuis, A. Tat-dependent protein targeting in prokaryotes and chloroplasts. Biochim. Biophys. Acta1694, 135–147 (2004). ArticleCASPubMed Google Scholar
Rapoza, M.P. & Webster, R.E. The filamentous bacteriophage assembly proteins require the bacterial SecA protein for correct localization to the membrane. J. Bacteriol.175, 1856–1859 (1993). ArticleCASPubMedPubMed Central Google Scholar
Plückthun, A. et al. in Antibody Engineering, edn. 1 (eds. McCafferty, J., Hoogenboom, H.R. & Chiswell, D.J.) 203–252, (IRL Press, Oxford, 1996). Google Scholar
Debarbieux, L. & Beckwith, J. The reductive enzyme thioredoxin 1 acts as an oxidant when it is exported to the Escherichia coli periplasm. Proc. Natl. Acad. Sci. USA95, 10751–10756 (1998). ArticleCASPubMedPubMed Central Google Scholar
Jonda, S., Huber-Wunderlich, M., Glockshuber, R. & Mössner, E. Complementation of DsbA deficiency with secreted thioredoxin variants reveals the crucial role of an efficient dithiol oxidant for catalyzed protein folding in the bacterial periplasm. EMBO J.18, 3271–3281 (1999). ArticleCASPubMedPubMed Central Google Scholar
Schierle, C.F. et al. The DsbA signal sequence directs efficient, cotranslational export of passenger proteins to the Escherichia coli periplasm via the signal recognition particle pathway. J. Bacteriol.185, 5706–5713 (2003). ArticleCASPubMedPubMed Central Google Scholar
Yang, F. et al. Novel fold and capsid-binding properties of the lambda-phage display platform protein gpD. Nat. Struct. Biol.7, 230–237 (2000). ArticleCASPubMed Google Scholar
Huber, D. et al. Use of thioredoxin as a reporter to identify a subset of Escherichia coli signal sequences that promote signal recognition particle-dependent translocation. J. Bacteriol.187, 2983–2991 (2005). ArticleCASPubMedPubMed Central Google Scholar
Slootstra, J.W., Kuperus, D., Plückthun, A. & Meloen, R.H. Identification of new tag sequences with differential and selective recognition properties for the anti-FLAG monoclonal antibodies M1, M2 and M5. Mol. Divers.2, 156–164 (1997). ArticleCASPubMed Google Scholar
Georgescu, R.E., Li, J.H., Goldberg, M.E., Tasayco, M.L. & Chaffotte, A.F. Proline isomerization-independent accumulation of an early intermediate and heterogeneity of the folding pathways of a mixed alpha/beta protein, Escherichia coli thioredoxin. Biochemistry37, 10286–10297 (1998). ArticleCASPubMed Google Scholar
Huber, D. et al. A selection for mutants that interfere with folding of Escherichia coli thioredoxin-1 in vivo. Proc. Natl. Acad. Sci. USA102, 18872–18877 (2005). ArticleCASPubMedPubMed Central Google Scholar
Forrer, P., Chang, C., Ott, D., Wlodawer, A. & Plückthun, A. Kinetic stability and crystal structure of the viral capsid protein SHP. J. Mol. Biol.344, 179–193 (2004). ArticleCASPubMed Google Scholar
Ewert, S., Huber, T., Honegger, A. & Plückthun, A. Biophysical properties of human antibody variable domains. J. Mol. Biol.325, 531–553 (2003). ArticleCASPubMed Google Scholar
Jäger, M., Gehrig, P. & Plückthun, A. The scFv fragment of the antibody hu4D5–8: evidence for early premature domain interaction in refolding. J. Mol. Biol.305, 1111–1129 (2001). ArticlePubMed Google Scholar
Paschke, M. & Höhne, W. A twin-arginine translocation (Tat)-mediated phage display system. Gene350, 79–88 (2005). ArticleCASPubMed Google Scholar
DeLisa, M.P., Tullman, D. & Georgiou, G. Folding quality control in the export of proteins by the bacterial twin-arginine translocation pathway. Proc. Natl. Acad. Sci. USA100, 6115–6120 (2003). ArticleCASPubMedPubMed Central Google Scholar
Crameri, R., Hemmann, S. & Blaser, K. PJuFo: a phagemid for display of cDNA libraries on phage surface suitable for selective isolation of clones expressing allergens. Adv. Exp. Med. Biol.409, 103–110 (1996). ArticleCASPubMed Google Scholar
Löhning, C., Urban, M. & Knappik, A. Novel methods for displaying (poly) peptides/proteins on bacteriophage particles via disulfide bonds Patent WO0105950 (2001).
Sambrook, J. & Russell David, W. (eds.). Molecular Cloning: A Laboratory Manual, edn. 3. (Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY, 2001). Google Scholar
Clackson, T. & Lowman, H.B. . Phage Display: A Practical Approach (Oxford University Press, New York, 2004). Google Scholar
Barbas, C.F., III, Burton, D.R., Scott, J.K. & Silvermann, G.J. . Phage Display: A Laboratory Manual. (Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY 2001). Google Scholar
Nielsen, H., Engelbrecht, J., Brunak, S. & von Heijne, G. Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites. Protein Eng.10, 1–6 (1997). ArticleCASPubMed Google Scholar
Gailus, V. & Rasched, I. The adsorption protein of bacteriophage fd and its neighbour minor coat protein build a structural entity. Eur. J. Biochem.222, 927–931 (1994). ArticleCASPubMed Google Scholar