IGEM:MIT/2005/IGEM2005: Front Page Summary

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  1. Koh, J. T. (2002). “Engineering selectivity and discrimination into ligand-receptor interfaces.” Chemistry & Biology, 9(1), 17-23.
    Analysis of receptor-ligand engineering emphasizes high selectivity and ability to discriminate ligand of reengineered receptor.
  2. Wittrup, K. D., Colby D., Yeung Y., Graff C., Swers J., and Kellogg, B. et al (2004). “Engineering antibody affinity by yeast surface display.” Methods in Enzymology, 388, 348-358.
    This article describes a new method to improve anti-flourescein scFv affinity by yeast surface display technology.
  3. Huston, J. S., Levinson D., Mudgett-Hunter M., and Tai, M. et al (1988). “Protein engineering of antibody binding sites: recovery of specific activity in an anti-digoxin single-chain fv analogue produced in escherichia coli.” Proc. Natl. Acad. Sci. USA, 85(16), 5879-5883.
    Experiment with anti-digoxin scFv in E.coli, the authors find a way to its improve specificity.
  4. Bedzyk, W. D., Weidner K. M., Denzin L. K., and Johnson, L. S. et al (1990). “Immunological and structural characterization of a high affinity anti-fluorescein single-chain antibody.” Journal of Biological Chemistry, 265(30), 18615-18620.
    Study on the general characteristics of high affinity anti-flourescein scFv provides insight into scFv affinity improvement.
  5. Mallender, W. D., Carrero J., Voss Jr. E. W. (1996). “Comparative properties of the single chain antibody and fv derivatives of mab 4-4-20. relationship between interdomain interactions and the high affinity for fluorescein ligand.” Journal of Biological Chemistry, 271(10), 5338-5346.
    Interactions between domains are examined and their affects on affinity of anti-flourescein scFv is observed.
  6. Denzin, L. K., Voss Jr. E. W. (1992). “Construction, characterization, and mutagenesis of an anti-fluorescein single chain antibody idiotype family.” Journal of Biological Chemistry, 267(13), 8925-8931.
    The authors provide various characteristics of anti-flourescein scFv through construction and mutation.
  7. Pantaliano, M. W., Bird R., Johnson S., and Asel, E. (1991). “Conformational stability, folding, and ligand-binding affinity of single-chain fv immunoglobulin fragments expressed in escherichia coli.” Biochemistry, 30(42), 10117-25.
    Stability and affinity of scFv are linked to the length of internal linker.
  8. Reiter, Y., Schuck P., Boyd L. F., and Plaksin, D. (1999). “An antibody single-domain phage display library of a native heavy chain variable region: isolation of functional single-domain vh molecules with a unique interface.” Journal of Molecular Biology, 290(3), 685-698.
    Phage display library is constructed to select for the best scFv.
  9. Shan, D., Press O. W., Tsu T. T., and Hayden, M. (1999). “Characterization of scfv-ig constructs generated from the anti-cd20 mab 1f5 using linker peptides of varying lengths.” Journal of Immunology, 162(11), 6589-6595.
    The authors examine the effect of linker lengths on affinity of scFv.
  10. Braun, V. (1997). “Surface signaling: novel transcription initiation mechanism starting from the cell surface.” Archives of Microbiology, 167(6), 325-331.
    This study of Fec pathway in E.coli identifies the major its major components, proteins, and genes involved.
  11. Yue, W. W., Grizot S., Buchanan S. K. (2003). “Structural evidence for iron-free citrate and ferric citrate binding to the tonb-dependent outer membrane transporter FecA.” Journal of Molecular Biology, 332(2), 353-368.
    Structural differences of bound and unbound FecA protein is explored.
  12. Harle, C., Kim I., Angerer A., and Braun, V. (1995). “Signal transfer through three compartments: transcription initiation of the escherichia coli ferric citrate transport system from the cell surface.” EMBO Journal, 14(7), 1430-1438.
    This paper demonstrates that ferric citrate uptake into the periplasm is not required for the induction of transcription of fec genes.
  13. Postle, K. (2002). Enhanced: close before opening. Science, 295(5560), 1658-1659.
    This short article provides summary and brief comparisons of iron transport pathways in E. coli.
  14. Braun, V., Mahren S., Ogierman M. (2003). “Regulation of the feci-type ecf sigma factor by transmembrane signaling.” Current Opinion in Microbiology, 6(2), 173-180.
    The authors identifie the components of Fec pathway that are required for signaling.
  15. Ferguson, A. D., Chakraborty R., Smith B. S., and Esser, L. et al (2002). “Structural basis of gating by the outer membrane transporter FecA.” Science, 295(5560), 1715-1719.
    Crystal structure of FecA protein shows the location of conformational change upon binding to ferric citrate.