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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)
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Unteers' lung found significant decreases in levels of SP-A [28]. Unfortunately, there was little overlap in the sets of identified proteins between our studies and therefore little basis for comparison. When the DEF and RED proteins are individually examined as subgroups of the identified proteins, the changes are similar to those noted for all proteins. In both of these groups of proteins, more
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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 s
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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,
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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 secreti
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Cell 10K protein) (CC10) (CC16) Ceruloplasmin isoforms Chain A, Crystal structure of novel mammalian lectin Ym1-suggests a saccharide binding site Chain B, Chimeric human mouse carbonmonoxyhemoglobin (Human zeta, Mouse beta 2) Chia protein Coiled-coil domain containing 122 Complement component 3 Complement component C5 Contrapsin (Serine protease inhibitor A3K) Creatine kinase M-type (EC.2.7.3.2)
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Cell 10K protein) (CC10) (CC16) Ceruloplasmin isoforms Chain A, Crystal structure of novel mammalian lectin Ym1-suggests a saccharide binding site Chain B, Chimeric human mouse carbonmonoxyhemoglobin (Human zeta, Mouse beta 2) Chia protein Coiled-coil domain containing 122 Complement component 3 Complement component C5 Contrapsin (Serine protease inhibitor A3K) Creatine kinase M-type (EC.2.7.3.2)
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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) (Ya1

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