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.<Br>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.<Br>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.<Br>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.<Br>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.<Br>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.<Br>Crystal structure of FecA protein shows the location of conformational change upon binding to ferric citrate.