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RESEARCH

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REFERENCE

  1. Bardwell, J. and E. Craig. 1984. Major heat shock gene of Drosophila and the Escherichia coli heat-inducible dnaK gene are homologous. Proc. Natl. Acad. Sci. USA. 81:848-852.
  2. Bassily, S. et al. 1972. Treatment of chronic urinary Salmonella carriers: 3-5 years follow-up. Gtrans. Roy. Soc. Trop. Med. Hygiene. 66:665-666.
  3. Bavoil, P., H. Nikaido and K. von Meyenburg. 1977. Mol. Gen. Genet. 158:23-33.
  4. Bragg, P.D. and C. Hou. 1972. Biochim. Biophys. Acta. 274:478-88.
  5. Cegielska, A. and C. Georgopoulos. 1989. Functional domains of the Escherichia coli dnaK heat shock protein as revealed by mutational analysis. J. Bio. Chem. 264:21122-21130.
  6. Chandrasekhar, G.N., K. Tilly, C. Woolford, R. Hendrix, and C. Georgopoulos. 1986. Purification and properties of the groES morphogenetic protein of Escherichia coli. J. Biol. Chem. 261:12414-12419.
  7. Chiang, H.L., S.R. Terlecky, C.P. Plant, and J.F. Dice. 1989. A role for a 70-kilodalton heat shock protein in lysosomal degradation of intracellular proteins. Science 246:382-385.
  8. Cohen, I.R. and D.B. Young. 1991. Autoimmunity, microbial immunity and the immunological homuniculus. Immunol. Today 12:105-110.
  9. Cooper, S. and T. Ruettinger. 1975. A temperature sensitive nonsense mutation affecting the synthesis of a major protein of Escherichia coli K12. Mol. Gen. Genet. 139:167-76.
  10. Craig, E.A. and C.A. Gross. 1991. Is hsp70 the cellular thermometer? TIBS 16:135-40.
  11. Dalie, B.I., D.A. Skaleris, K. Köhle, H. Weissbach, and N. Brot. 1990. Interaction of dnaK with ATP: binding, hydrolysis and Ca²⁺-stimulated autophosphorylation. Biochem. Biophys. Res. Commun. 166:1284-1292.
  12. Datta, D.B., C. Kramer and U. Henning. 1976. J. Bacterio. 131:821-29.
  13. DiDomenico, B.J., G.E. Bugaisky and S. Lindquist. 1982. The heat shock response is self-regulated at both the transcriptional and post-transcriptional levels. Cell 31:593-603.
  14. DiRienzo, J.M., K. Nakamura, and M. Inouye. 1978. The outer membrane proteins of gram-negative bacteria: biosynthesis, assembly and functions. Annu. Rev. Biochem. 47:481-532.
  15. DuPont, H.L., et al. 1971. Studies of immunity in typhoid fever. Protection induced by killed oral antigens or by primary infection. Bull. Wld. Hlth. Org. 44:667-672.
  16. Edelman, R. and M.M. Levine. 1986. Summary of an international workshop of typhoid fever. Rev. Infect. Dis. 8:329-349.
  17. Ellis, R. J. 1987. Proteins as molecular chaperones. Nature 328:378-379.
  18. Ellis, R. J., S.M. van der Vries, and S.M. Hemmingsen. 1989. The molecular chaperone concept. Biochem. Soc. Symp. 55:145-153.
  19. Ellis, R. J. and S.M. van der Vries. 1991. Molecular chaperones. Annu. Rev. Biochem. 60:321-47.
  20. Ensgraber, M. And M. Loos. 1992. A 66-kilodalton heat shock protein of Salmonella typhimurium is responsible for binding of the bacterium to intestinal mucus. Infec. Immun. 60(8):3072-3078.
  21. Fayet, O, J.M. Louran, and C. Georgopoulos. 1986. Suppression of the Escherichia coli dnaA46 mutation by amplification of the groES and groEL genes. Mol. Gen. Genet. 202:435-445.
  22. Foster, J.W. and M.P. Spector. 1995. How Salmonella survive against the odds. Annu. Rev. Microbiol. 49:156.
  23. Franco, A., C. Gonzales, and O.S. Levine. 1992. Further consideration of the clonal nature of Salmonella typhi: evaluation of molecular and clinical characteristics of strains from Indonesia and Peru. J. Clin. Microbiol. 30:2187-2190.
  24. Freeley, J.C. and M.D. Treger. 1969. Penetration of turtle eggs by Salmonella braenderup. Publ. Hlth. Rep. 84:156-158.
  25. Georgopoulos, C., D. Ang, K. Liberek and M. Zylicz. 1990. Properties of the Escherichia coli heat shock proteins and their role in bacteriophage λ growth. In Stress Proteins in Biology and Medicine. Cold Spring Harbor, NY: Cold Spring Harbor Lab. 191-221.
  26. Gladwin, M., and B. Trattler. 1997. Gram negative bacteria: the enterics. In Clinical microbiology made ridiculously simple. 58-59.
  27. Glauert, A.M and M.J. Thornley. 1969. The topography of the bacterial cell wall. Annu. Rev. Microbiol. 23:159-198.
  28. Goff, S.A. and A.L. Goldberg. 1985. Production of abnormal proteins in E. coli stimulates transcription of lon and other heat shock genes. Cell. 41:587-95.
  29. Grossman, A.D., J.W. Erickson and C.A. Gross. 1984. The htpR gene product of E. coli is a sigma factor for heat shock promoters. Cell. 38:383-90.
  30. Harlow, E. and D. Lane. 1988. Immunoblotting. In Antibodies laboratory manual. Cold Springs Harbor, NY: Cold Springs Harbor Lab. 473-480.
  31. Hemmingsen, S.M., C.Woolford, S.M. van der Vies, K. Tilly, D.T. Dennis, C.P. Georgopoulos, R.W. Hendrix, and R.J. Ellis. 1988. Homologous plant and bacterial proteins chaperone oligomeric protein assembly. Nature 333:330-334.
  32. Hendrix, R.W. 1979. Purification and properties of groE, a host protein in bacteriophate assembly. J. Mol. Bio. 129:375-392.
  33. Hoffman, J.P., C.A. Butler, and F.D. Quinn. 1990. Cloning and temperature-dependent expression in Escherichia coli of a Legionella pneumophila gene coding for a genus-common 60-kilodalton antigen. Infec. Immun. 57(6):1731-1739.
  34. Inouye, M. and M.L. Yee. 1973. J. Bacteriol. 113:304.
  35. Kaufmann, S.H.E., U. Vath, J.E.R. Thole, , J.D.A. van Embden, and F. Emmrich. 1987. Enumeration of T cells reactive with M. tuberculosis organisms and specific for the recombinant mycobacterial 64 kilodalton protein. Eur. J. Immunol. 17:351-357.
  36. Koga, T., A. Wand-Wurttenberger, J. de Bruyn, M.E. Munk, B. Schoel, and S.H.E. Kaufmann. 1989. T cells against a bacterial heat shock protein recognize stressed macrophages. Science 145:1112-1115.
  37. Kusukawa, N. and T. Yura. 1988. Heat-shock protein groE of Escherichia coli – key protective roles against thermal stress. Genes Dev. 2:874-882.
  38. Kuusi, N., M. Nurminen, H. Saxen, M. Valtonen and P.H. Mäkelä. 1979. Immunization with major outer membrane proteins in experimental salmonellosis in mice. Infect. Immun. 25:857-862.
  39. Lang, K., F.X. Schmidt, and G. Fischer. 1987. Catalysis of protein folding by prolyl isomerase. Nature 329:268-270.
  40. Langer, T. and W. Neupert. 1991. Heat shock proteins hsp 60 and hsp 70: Their roles in folding, assembly and membrane translocation of proteins. Current Topics in Microbiology and Immunology. 167:3-30.
  41. Laskey, R.A., B.M. Honda, A.D. Mills and J.T. Finch. 1978. Nucleosomes are assembled by an acidin protein which binds histones and transfers them to DNA. Nature 275:416-420.
  42. Lathigra, R.B., P.D. Butcher, T.R. Garbe, and D.B. Young. 1991. Heat shock proteins as virulence factors of pathogens. Current Topics in Microbiology and Immunology 167:125-131.
  43. Lemaux, P.G., S.L. Herendeen, P.L. Bloch and F.C. Neidhardt. 1978. Transient rates of synthesis of individual polypeptides in E. coli following temperature shifts. Cell 13:427-34.
  44. Lindquist, S. 1986. The heat shock response. Annu. Rev. Biochem. 55:1151-1191.
  45. Lindquist, S. and E.A. Craig. 1988. The heat shock proteins. Annu. Rev. Genet. 22:631-677.
  46. Kauffman, S.H.E., U. Vath, J.E.R. Thole, J.D.A. Van Embden and F. Emmrich. 1987. Enumeration of T cells reactive with Mycobacterium tuberculosis organisms and specific for the 64-kDa protein. Eur. J. Immunol. 17:351-357.
  47. MacGregor, C.H., C.W Bishop and J.E. Blech.1979. Localization of proteolytic activity in the outer membrane of Escherichia coli. J. Bacteriol. 137: 574-583.
  48. Maizel, J.U. 1971. Polyacrylamide gel electrophoresis of viral proteins. Methods. Virol. 5: 179-246.
  49. Marshak, D.R., J.T. Kadonaga, R.R. Burges, M.W. Knuth, W.A. Brennan Jr., and S.H. Lin. 1996. Strategies for protein purification and characterization: A lab course manual. Cold Springs Harbor, NY: Cold Springs Harbor Lab Press.
  50. Matsuyama, S.I., K. Inokuchi, and S. Mizushima. 1984. Promoter exchange between OmpF and OmpC, genes for osmoregulated majour outer membrane proteins of Escherichia coli K-12. J. Bacterio. 158(3)1041-1047.
  51. Miller, J.F., J.J. Mekalanos, and S. Falkow. 1989. Coordinate regulation and sensory transduction in the control of bacterial virulence. Science 243:916-922.
  52. Morimoto, R., A. Tissiéres and C. Georgopoulos, eds. 1990. Stress Proteins in Biology and Medicine. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press.
  53. Morrison, R.P., R.J. Belland, K. Lyng, and HD. Caldwell. 1989. Clamydial disease pathogenesis. The 57-kD chlamydial hypersensitivity antigen is a stress response protein. J. Exp. Med. 170:1271-1283.
  54. Murray, P.J. and R.A. Young. 1992. Stress and immunological recognition in host-pathogen interactions. J. Bacteriol. 174:4193-4196.
  55. Neidhardt, F.C. and R.A. VanBogelen. 1981. Positive regulatory gene for temperature-controlled proteins in Escherichia coli. Biochem. Biophys. Res. Commun. 100:894-900.
  56. Neidhardt, F.C., R.A. VanBogelen, and Lau, E.T. 1982. The high temperature regulon of Escherichia coli. In Heat shock: From bacteria to man (ed M.J. Schlesinger, M. Ashburner and A. Tissieres). 139. New York: Cold Spring Harbor Laboratory Press.
  57. Neidhardt, F C., R.A. VanBogelen and V. Vaughn. 1984. The genetics and regulation of heat-shock proteins. Annu. Rev. Genet. 18:295.
  58. Ortiz, V., A. Isibasi, E. García-Ortigoza and J. Kumate. 1989. Immunoblot detection of class-specific humoral immune response to outer membrane proteins isolated from Salmonella typhi in humans with typhoid fever. J. Clin. Microbiol. 27(7):1640-1644.
  59. Osborn, M.J. and H.C.P. Wu. 1980. Proteins of the outer membrane of gram-negative bacteria. Annu. Rev. Microbiol. 34-369-422.
  60. Pelham, H.R.B. 1986. Speculations on the functions of the major heat shock and glucose-regulated proteins. Cell 46:959-61.
  61. Reading, D.S., R.L. Hallberg, and A.M. Myers. 1989. Characterization of the yeast hsp60 gene coding of a mitochondrial assembly facture. Nature 337:655-659.
  62. Ritossa, F. 1962. A new puffing pattern induced by temperature shock and DNP in Drosophila. Experentia 18:571-573.
  63. Rothman, J.E. 1989. Polypeptide chain binding proteins: catalysts of protein folding and related processes in cells. Cells 59:591-601.
  64. Salyers, A.A. and D.D. Whitt. 1994. Salmonella infections. In Bacterial Pathogenesis. Washington: ASM Press.
  65. Schnaitman, C.A. 1973. Outer membrane proteins of Escherichia coli. I. Effect of preparation conditions on the migration of protein in polyacrylamide gels. Arch. Biochem. Biophys. 157: 541-552.
  66. Shinnick, T.K., M.H. Vodkin, J.C. Williams. 1988. The Mycobacterium tuberculosis 65-kilodalton antigen is a heat-shock protein which corresponds to common antigen and to the Escherichia coli GroEL protein. Infect. Immun. 56:446-451.
  67. Shinnick, T.M. 1991. Heat shock proteins as antigens of bacterial and parasitic pathogens. Current topics in microbiology and immunology 167:153-155.
  68. Stevenson, M.A. and S.K. Calderwood. 1990. Members of the 70-kilodalton heat shock protein family contain a highly conserved almodulin-binding domain. Mol. Cell. Bio. 10:1234-1238.
  69. Taglicht, D., E. Padan, A.B. Oppenheim and S. Schuldiner. 1987. An alkaline shift induces the heat shock response in Escherichia coli. J. Bacteriol. 169:885-887.
  70. Tan, V.Y.M. 1991. Methods for rapid diagnosis of typhoid fever. Thesis submitted in partial fulfillment of the requirements for the degree of Bachelor of Science with Honours in Microbiology at the University of Malaya.
  71. Tang, S.W., S. Abubakar, S. Devi, S. Puthucheary, and T. Pang. 1997. Induction and characterization of heat shock proteins of Salmonella typhi and their reactivity with sera from patients with typhoid fever. Infec. Immun. 65(7):2-3 (notes).
  72. Tang, S.W. 1998. Identification of heat shock proteins (hsps) in Salmonella typhi. Dissertation presented to the Faculty of Medicine, Universiti Malaya, in partial fulfillment of the requirements for the degree of Master of Medical Science.
  73. Tortora, G.J., B.R. Funke and C.L. Case. 1998. Bacterial groups: Facultatively Anaerobic Gram-Negative Rods. In Microbiology: An Introduction. California: Benjamin/Cummings Publishing Company.
  74. Towbin, H., T. Staehelin and J. Gordon. 1979. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl. Acad. Sci. U.S.A. 76:4350-4354.
  75. Towner, K.J., and A. Cockayne. 1993. Analysis of protein and lipopolysaccharide profiles. In Molecular methods for microbial identification and typing. London: Chapman and Hall. 133-138.
  76. Udhayakumar, V. and Muthukkaruppan. 1987. Protective immunity induced by outer membrane proteins of Salmonella typhimurium in mice. Infect. Immun. 55:816-821.
  77. Welch, N.J. 1993. Heat shock proteins functioning as molecular chaperones: their roles in normal and stressed cells. In Molecular Chaperones (ed. R.J. Ellis, R.A. Laskey, and G.H. Lorimer). London: Chapman & Hall.
  78. Yamamori, T., K. Ito, Y. Nakamura, T. Yura. 1978. Transient regulation of protein synthesis in Escherichia coli upon shift-up of growth temperature. J. Bacteriol. 134:1133-40.
  79. Yamamori, T., T. Osawa, T. Tobe, K. Ito and T. Yura. 1982. Escherichia coli gene (hin) controls transcription of heat-shock operons and cell growth at high temperatures. In Heat Shock from Bacteria to Man. Cold Spring Harbor, NY: Cold Spring Harbor Lab pp 131-37.
  80. Yamamori, T. and T. Yura. 1980. Temperature-induced synthesis of specific proteins in Escherichia coli: evidence for transcriptional control. J. Bacteriol. 142:843-51.
  81. Yamamori, T. and T. Yura. 1982. Genetic control of heat-shock protein synthesis and its bearing on growth and thermal resistance in Escherichia coli K-12. Proc. Natl. Acad. Sci. USA 79:860-64.
  82. Young, D.B., E. Roman, C. Moreno, R. O’Brien, and W. Born. 1993. Molecular chaperones and the immune response. In Molecular Chaperones (ed. R.J. Ellis, R.A. Laskey, and G.H. Lorimer). London: Chapman and Hall. 107.
  83. Yura, T., H. Nagai and H. Mori. 1993. Regulation of the heat-shock response in bacteria. Annu. Rev. Microbiol. 47:321-50.
  84. Zylicz, M. and C. Georgopoulos. 1984. Purification and properties of the Escherichia coli dnaK replication protein. J. Bio. Chem. 259:8820-8825.
  85. Zylicz, M., LeBowitz, R. McMacken and C. Georgopoulos. 1983. The dnaK protein of Escherichia coli possesses an ATPase and autophosphorylating activity and is essential to an in vitro DNA replication system. Proc. Natl. Acad. Sci. USA 80:6431-6435.

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