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More susceptible to UTIs than are healthy patients because of the greater adherence of type 1 fimbriated E. coli to bladder cells (57). The LGI network of Candida Als and Epa adhesins N-Als1p has been shown to interact with fucose-containing glycans that are present in blood group antigens and preferentially with antigen Htype 2 (22). Therefore, we performed glycan array screening to also determin
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Ell, T., and R. G. E. Murray. 1986. Polar lipid profiles of the genus Deinococcus. Int. J. Syst. Bacteriol. 36:202?06. 40. Craig, E. A. 1993. Chaperones: helpers along the pathways to protein folding. Science 260:1902?903. 41. Craig, E. A., B. D. Gambill, and R. J. Nelson. 1993. Heat shock proteins: molecular chaperones of protein biogenesis. Microbiol. Rev. 57:402?14. 42. Creti, R., E. Ceccarelli
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Ell, T., and R. G. E. Murray. 1986. Polar lipid profiles of the genus Deinococcus. Int. J. Syst. Bacteriol. 36:202?06. 40. Craig, E. A. 1993. Chaperones: helpers along the pathways to protein folding. Science 260:1902?903. 41. Craig, E. A., B. D. Gambill, and R. J. Nelson. 1993. Heat shock proteins: molecular chaperones of protein biogenesis. Microbiol. Rev. 57:402?14. 42. Creti, R., E. Ceccarelli
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Ell, T., and R. G. E. Murray. 1986. Polar lipid profiles of the genus Deinococcus. Int. J. Syst. Bacteriol. 36:202?06. 40. Craig, E. A. 1993. Chaperones: helpers along the pathways to protein folding. Science 260:1902?903. 41. Craig, E. A., B. D. Gambill, and R. J. Nelson. 1993. Heat shock proteins: molecular chaperones of protein biogenesis. Microbiol. Rev. 57:402?14. 42. Creti, R., E. Ceccarelli
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Of a protein altered in mutants resistant to microtubule inhibitors as a member of the major heat shock protein (hsp70) family. Mol. Cell. Biol. 10:5160?5165. 3. Alberts, B., D. Bray, J. Lewis, M. Raff, K. Roberts, and J. D. Watson. 1994. Molecular biology of the cell. Garland Publishing, Inc., New York, N.Y. 4. Allsopp, A. 1969. Phylogenetic relationships of the procaryota and the origin of the e
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Of a protein altered in mutants resistant to microtubule inhibitors as a member of the major heat shock protein (hsp70) family. Mol. Cell. Biol. 10:5160?5165. 3. Alberts, B., D. Bray, J. Lewis, M. Raff, K. Roberts, and J. D. Watson. 1994. Molecular biology of the cell. Garland Publishing, Inc., New York, N.Y. 4. Allsopp, A. 1969. Phylogenetic relationships of the procaryota and the origin of the e
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Of a protein altered in mutants resistant to microtubule inhibitors as a member of the major heat shock protein (hsp70) family. Mol. Cell. Biol. 10:5160?5165. 3. Alberts, B., D. Bray, J. Lewis, M. Raff, K. Roberts, and J. D. Watson. 1994. Molecular biology of the cell. Garland Publishing, Inc., New York, N.Y. 4. Allsopp, A. 1969. Phylogenetic relationships of the procaryota and the origin of the e
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Ell, T., and R. G. E. Murray. 1986. Polar lipid profiles of the genus Deinococcus. Int. J. Syst. Bacteriol. 36:202?06. 40. Craig, E. A. 1993. Chaperones: helpers along the pathways to protein folding. Science 260:1902?903. 41. Craig, E. A., B. D. Gambill, and R. J. Nelson. 1993. Heat shock proteins: molecular chaperones of protein biogenesis. Microbiol. Rev. 57:402?14. 42. Creti, R., E. Ceccarelli
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Ell, T., and R. G. E. Murray. 1986. Polar lipid profiles of the genus Deinococcus. Int. J. Syst. Bacteriol. 36:202?06. 40. Craig, E. A. 1993. Chaperones: helpers along the pathways to protein folding. Science 260:1902?903. 41. Craig, E. A., B. D. Gambill, and R. J. Nelson. 1993. Heat shock proteins: molecular chaperones of protein biogenesis. Microbiol. Rev. 57:402?14. 42. Creti, R., E. Ceccarelli
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Archaebacteria but instead was a chimera formed by fusion and integration of the genomes of an archaebacterium and a gram-negative bacterium. The available data indicate that the primary fusion event that gave rise to the ancestral eukaryotic cell was unique and that it was very probably distinct from (and preceded) the one that gave rise to mitochondria and hydrogenosomes. These results provide e