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Eduction in their synthesis remains to be determined. b) Strain differences at 24 hr after infection Extending the analysis to mice infected 24 hr earlier we gained some additional insight into the response pattern. Three gen-Ali et al. Proteome Science 2010, 8:34 http://www.proteomesci.com/content/8/1/Page 10 ofTable 2: Changes in protein expression between wild-type and SP-A-/- mice for control
Ice are shown for untreated (baseline) animals, 4 hours postinfection and 24 hours post-infection. Gel numbers (see Fig. 2), protein names, functional groups and percent change ( ) are listed. Abbreviations for functional groups: DEF, host defense; PMM, protein modification and metabolism; RED, redox regulation. Bolded numbers indicate changes that were significant (p
N of a -sheet using strands from the two monomers. As expected, CS-Rosetta calculations of the individual monomers failed to converge (Figure 5A); the native state cannot be energetically distinguished by considering only interactions within the monomer. If nevertheless the low energy, partially unfolded monomers are used as starting points in the symmetric docking protocol we obtain a converged
N of a -sheet using strands from the two monomers. As expected, CS-Rosetta calculations of the individual monomers failed to converge (Figure 5A); the native state cannot be energetically distinguished by considering only interactions within the monomer. If nevertheless the low energy, partially unfolded monomers are used as starting points in the symmetric docking protocol we obtain a converged
10.69 4.76 12.73 29.21 31.75 38.77 16.63 -12.1 2 3 4 5 6 714-3-3-Zeta Adipsin (Complement factor D) Albumin Aldehyde dehydrogenase AHD-M1 Aldehyde dehydrogenase II Aldehyde dehydrogenase, Dimeric NADP-preferring (EC 1.2.1.5) (ALDH class 3) Alpha-1-antitrypsin 1-1 precursor (Serine protease inhibitor 1-1) Alpha-1-antitrypsin 1-6 precursor (Serine protease inhibitor 1-6) (Alpha-1 protease inhibitor
Not yet known what causes these rapid changes. They may result from the presence of bacteria, the influx of immune cells to combat the bacteria, or the release of mediator(s) from immune cells or epithelium to deal with the insult. We speculate that the rapidity of the response (within 4 hr) is due to the release of stored mediators, such as chemokines, rather than due to the synthesis and secret
10.69 4.76 12.73 29.21 31.75 38.77 16.63 -12.1 2 3 4 5 6 714-3-3-Zeta Adipsin (Complement factor D) Albumin Aldehyde dehydrogenase AHD-M1 Aldehyde dehydrogenase II Aldehyde dehydrogenase, Dimeric NADP-preferring (EC 1.2.1.5) (ALDH class 3) Alpha-1-antitrypsin 1-1 precursor (Serine protease inhibitor 1-1) Alpha-1-antitrypsin 1-6 precursor (Serine protease inhibitor 1-6) (Alpha-1 protease inhibitor
Not yet known what causes these rapid changes. They may result from the presence of bacteria, the influx of immune cells to combat the bacteria, or the release of mediator(s) from immune cells or epithelium to deal with the insult. We speculate that the rapidity of the response (within 4 hr) is due to the release of stored mediators, such as chemokines, rather than due to the synthesis and secret
N of a -sheet using strands from the two monomers. As expected, CS-Rosetta calculations of the individual monomers failed to converge (Figure 5A); the native state cannot be energetically distinguished by considering only interactions within the monomer. If nevertheless the low energy, partially unfolded monomers are used as starting points in the symmetric docking protocol we obtain a converged
N of a -sheet using strands from the two monomers. As expected, CS-Rosetta calculations of the individual monomers failed to converge (Figure 5A); the native state cannot be energetically distinguished by considering only interactions within the monomer. If nevertheless the low energy, partially unfolded monomers are used as starting points in the symmetric docking protocol we obtain a converged
Ntrol, 4 hr post infection and 24 hr post infection: percent changes with significance for all identified proteins corresponding to reference gels in Fig. 2 (Continued)33 34 35 36 37 38 39 40 Glutathione S-transferase, alpha 3 Glutathione S-transferase, alpha 4 Glutathione S-transferase, mu 1 Glutathione S-transferase, omega 1 (Similar to) Glutathione S-transferase, Ya chain (GST class-alpha) (Ya
Ntrol, 4 hr post infection and 24 hr post infection: percent changes with significance for all identified proteins corresponding to reference gels in Fig. 2 (Continued)33 34 35 36 37 38 39 40 Glutathione S-transferase, alpha 3 Glutathione S-transferase, alpha 4 Glutathione S-transferase, mu 1 Glutathione S-transferase, omega 1 (Similar to) Glutathione S-transferase, Ya chain (GST class-alpha) (Ya
Ntrol, 4 hr post infection and 24 hr post infection: percent changes with significance for all identified proteins corresponding to reference gels in Fig. 2 (Continued)33 34 35 36 37 38 39 40 Glutathione S-transferase, alpha 3 Glutathione S-transferase, alpha 4 Glutathione S-transferase, mu 1 Glutathione S-transferase, omega 1 (Similar to) Glutathione S-transferase, Ya chain (GST class-alpha) (Ya
Ntrol, 4 hr post infection and 24 hr post infection: percent changes with significance for all identified proteins corresponding to reference gels in Fig. 2 (Continued)33 34 35 36 37 38 39 40 Glutathione S-transferase, alpha 3 Glutathione S-transferase, alpha 4 Glutathione S-transferase, mu 1 Glutathione S-transferase, omega 1 (Similar to) Glutathione S-transferase, Ya chain (GST class-alpha) (Ya