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Cited by 14

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Production of a Soluble Disulfide Bond-Linked TCR in the Cytoplasm of Escherichia coli trxB gor Mutants

Liddy, Nathaniel, Molloy, Peter E., Bennett, Alan D., Boulter, Jonathan M., Jakobsen, Bent K., Li, Yi·2010·Molecular Biotechnology
DOI 10.1007/s12033-010-9250-0
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Research works printed but not linked: 39

  1. Davis, M. M., Boniface, J. J., Reich, Z., Lyons, D., Hampl, J., Arden, B., et al. (1998). Ligand recognition by alpha beta T cell receptors. Annual Review of Immunology, 16, 523–544. · DOI
  2. Fremont, D. H., Rees, W. A., & Kozono, H. (1996). Biophysical studies of T-cell receptors and their ligands. Current Opinion in Immunology, 8, 93–100. · DOI
  3. Boulter, J. M., Glick, M., Todorov, P. T., Baston, E., Sami, M., Rizkallah, P., et al. (2003). Stable, soluble T-cell receptor molecules for crystallization and therapeutics. Protein Engineering, 16, 707–711. · DOI
  4. Li, Y., Moysey, R., Molloy, P. E., Vuidepot, A. L., Mahon, T., Baston, E., et al. (2005). Directed evolution of human T-cell receptors with picomolar affinities by phage display. Nature Biotechnology, 23, 349–354. · DOI
  5. Maynard, J., Adams, E. J., Krogsgaard, M., Petersson, K., Liu, C. W., & Garcia, K. C. (2005). High-level bacterial secretion of single-chain alphabeta T-cell receptors. Journal of Immunological Methods, 306, 51–67. · DOI
  6. Wulfing, C., & Pluckthun, A. (1994). Correctly folded T-cell receptor fragments in the periplasm of Escherichia coli. Influence of folding catalysts. Journal of Molecular Biology, 242, 655–669. · DOI
  7. Golden, A., Khandekar, S. S., Osburne, M. S., Kawasaki, E., Reinherz, E. L., & Grossman, T. H. (1997). High-level production of a secreted, heterodimeric alpha beta murine T-cell receptor in Escherichia coli. Journal of Immunological Methods, 206, 163–169. · DOI
  8. Santala, V., & Lamminmaki, U. (2004). Production of a biotinylated single-chain antibody fragment in the cytoplasm of Escherichia coli. Journal of Immunological Methods, 284, 165–175. · DOI
  9. Proba, K., Ge, L., & Pluckthun, A. (1995). Functional antibody single-chain fragments from the cytoplasm of Escherichia coli: Influence of thioredoxin reductase (TrxB). Gene, 159, 203–207. · DOI
  10. Molloy, P. E., Harris, W. J., Strachan, G., Watts, C., & Cunningham, C. (1998). Production of soluble single-chain T-cell receptor fragments in Escherichia coli trxB mutants. Molecular Immunology, 35, 73–81. · DOI
  11. Bessette, P. H., Aslund, F., Beckwith, J., & Georgiou, G. (1999). Efficient folding of proteins with multiple disulfide bonds in the Escherichia coli cytoplasm. Proceedings of the National Academy of Sciences USA, 96, 13703–13708. · DOI
  12. Derman, A. I., & Beckwith, J. (1991). Escherichia coli alkaline phosphatase fails to acquire disulfide bonds when retained in the cytoplasm. Journal of Bacteriology, 173, 7719–7722. · DOI
  13. Prinz, W. A., Aslund, F., Holmgren, A., & Beckwith, J. (1997). The role of the thioredoxin and glutaredoxin pathways in reducing protein disulfide bonds in the Escherichia coli cytoplasm. Journal of Biological Chemistry, 272, 15661–15667. · DOI
  14. Berndt, C., Lillig, C. H., & Holmgren, A. (2008). Thioredoxins and glutaredoxins as facilitators of protein folding. Biochimica et Biophysica Acta, 1783, 641–650. · DOI
  15. Eser, M., Masip, L., Kadokura, H., Georgiou, G., & Beckwith, J. (2009). Disulfide bond formation by exported glutaredoxin indicates glutathione’s presence in the E. coli periplasm. Proceedings of the National Academy of Sciences USA, 106, 1572–1577. · DOI
  16. Derman, A. I., Prinz, W. A., Belin, D., & Beckwith, J. (1993). Mutations that allow disulfide bond formation in the cytoplasm of Escherichia coli. Science, 262, 1744–1747. · DOI
  17. Stewart, E. J., Aslund, F., & Beckwith, J. (1998). Disulfide bond formation in the Escherichia coli cytoplasm: An in vivo role reversal for the thioredoxins. EMBO Journal, 17, 5543–5550. · DOI · Paper page
  18. Petrov, K., Dion, M., Hoffmann, L., Dintinger, T., Defontaine, A., & Tellier, C. (2004). Bivalent Fv antibody fragments obtained by substituting the constant domains of a fab fragment with heterotetrameric molybdopterin synthase. Journal of Molecular Biology, 341, 1039–1048. · DOI
  19. Venturi, M., Seifert, C., & Hunte, C. (2002). High level production of functional antibody Fab fragments in an oxidizing bacterial cytoplasm. Journal of Molecular Biology, 315, 1–8. · DOI
  20. Baneyx, F., & Mujacic, M. (2004). Recombinant protein folding and misfolding in Escherichia coli. Nature Biotechnology, 22, 1399–1408. · DOI · Paper page
  21. Chen, J., Song, J. L., Zhang, S., Wang, Y., Cui, D. F., & Wang, C. C. (1999). Chaperone activity of DsbC. Journal of Biological Chemistry, 274, 19601–19605. · DOI
  22. Rietsch, A., Belin, D., Martin, N., & Beckwith, J. (1996). An in vivo pathway for disulfide bond isomerization in Escherichia coli. Proceedings of the National Academy of Sciences USA, 93, 13048–13053. · DOI
  23. Kadokura, H., Katzen, F., & Beckwith, J. (2003). Protein disulfide bond formation in prokaryotes. Annual Review of Biochemistry, 72, 111–135. · DOI · Paper page
  24. Holck, A., & Kleppe, K. (1988). Cloning and sequencing of the gene for the DNA-binding 17 K protein of Escherichia coli. Gene, 67, 117–124. · DOI
  25. Holck, A., Lossius, I., Aasland, R., & Kleppe, K. (1987). Purification and characterization of the 17 K protein, a DNA-binding protein from Escherichia coli. Biochimica et Biophysica Acta, 914, 49–54. · DOI
  26. Chen, R., & Henning, U. (1996). A periplasmic protein (Skp) of Escherichia coli selectively binds a class of outer membrane proteins. Molecular Microbiology, 19, 1287–1294. · DOI
  27. Wulfing, C., & Pluckthun, A. (1994). Protein folding in the periplasm of Escherichia coli. Molecular Microbiology, 12, 685–692. · DOI
  28. Walton, T. A., & Sousa, M. C. (2004). Crystal structure of Skp, a prefoldin-like chaperone that protects soluble and membrane proteins from aggregation. Molecular Cell, 15, 367–374. · DOI
  29. Schafer, U., Beck, K., & Muller, M. (1999). Skp, a molecular chaperone of gram-negative bacteria, is required for the formation of soluble periplasmic intermediates of outer membrane proteins. Journal of Biological Chemistry, 274, 24567–24574. · DOI · Paper page
  30. Heo, M. A., Kim, S. H., Kim, S. Y., Kim, Y. J., Chung, J., Oh, M. K., et al. (2006). Functional expression of single-chain variable fragment antibody against c-Met in the cytoplasm of Escherichia coli. Protein Expression and Purification, 47, 203–209. · DOI
  31. Jurado, P., de Lorenzo, V., & Fernandez, L. A. (2006). Thioredoxin fusions increase folding of single chain Fv antibodies in the cytoplasm of Escherichia coli: Evidence that chaperone activity is the prime effect of thioredoxin. Journal of Molecular Biology, 357, 49–61. · DOI
  32. Lefranc, M. P. (2001). IMGT, the international ImMunoGeneTics database. Nucleic Acids Research, 29, 207–209. · DOI
  33. Garboczi, D. N., Hung, D. T., & Wiley, D. C. (1992). HLA-A2-peptide complexes: Refolding and crystallization of molecules expressed in Escherichia coli and complexed with single antigenic peptides. Proceedings of the National Academy of Sciences USA, 89, 3429–3433. · DOI
  34. Willcox, B. E., Gao, G. F., Wyer, J. R., Ladbury, J. E., Bell, J. I., Jakobsen, B. K., et al. (1999). TCR binding to peptide-MHC stabilizes a flexible recognition interface. Immunity, 10, 357–365. · DOI
  35. Jurado, P., Ritz, D., Beckwith, J., de Lorenzo, V., & Fernandez, L. A. (2002). Production of functional single-chain Fv antibodies in the cytoplasm of Escherichia coli. Journal of Molecular Biology, 320, 1–10. · DOI
  36. Ward, E. S. (1992). Secretion of T cell receptor fragments from recombinant Escherichia coli cells. Journal of Molecular Biology, 224, 885–890. · DOI
  37. Hwang, C., Sinskey, A. J., & Lodish, H. F. (1992). Oxidized redox state of glutathione in the endoplasmic reticulum. Science, 257, 1496–1502. · DOI · Paper page
  38. Bothmann, H., & Pluckthun, A. (1998). Selection for a periplasmic factor improving phage display and functional periplasmic expression. Nature Biotechnology, 16, 376–380. · DOI
  39. Magnusdottir, A., Johansson, I., Dahlgren, L. G., Nordlund, P., & Berglund, H. (2009). Enabling IMAC purification of low abundance recombinant proteins from E. coli lysates. Nature Methods, 6, 477–478. · DOI

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Metadata

Authors
Liddy, N., Molloy, P. E., Bennett, A. D., Boulter, J. M., Jakobsen, B. K., & Li, Y.
Venue
Molecular Biotechnology
Publisher
Springer Science and Business Media LLC
Published
2010-02-09
Volume
45
Issue
2
Pages
140-149
ISSN
  • 1073-6085
  • 1559-0305
DOI
10.1007/s12033-010-9250-0
Cited by
14
References
1
Language
en
Licence
www.springer.com/tdm (tdm)

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CoChat. (2026). Citation check: Production of a Soluble Disulfide Bond-Linked TCR in the Cytoplasm of Escherichia coli trxB gor Mutants. https://app.cochat.ai/papers/10.1007/s12033-010-9250-0
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Liddy, N., Molloy, P. E., Bennett, A. D., Boulter, J. M., Jakobsen, B. K., & Li, Y. (2010). Production of a Soluble Disulfide Bond-Linked TCR in the Cytoplasm of Escherichia coli trxB gor Mutants. Molecular Biotechnology. https://doi.org/10.1007/s12033-010-9250-0

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