BÁO CÁO Y HỌC: "META-ANALYSIS OF PRIMARY TARGET GENES OF PEROXISOME PROLIFERATOR-ACTIVATED RECEPTORS" PDF

a microarray are not definable on the basis of comparingtheir fold-changes alone. Soinov et al. [36] have proposedan alternative method to bypass the assumption of arbitr arydiscretization thresholds for the regulators. Their states of a“predicted gene” (i.e., a target gen[r]

proliferation [38].It is less obvious how other genes identified in Table 2are related to IFN-mediated activities, as none has beenpreviously characterized as an ISG. Nevertheless, thecase can be made for several of these genes to be linkedto different aspects of IFN biolo[r]

phoribosyl transferase. The nuclear receptor peroxisome proliferator-acti-vated receptor gamma (PPARc) exerts anti-inflammatory effects inmacrophages by inhibiting cytokine production and enhancing alternativedifferentiation. In this study, we investigated whether PPARc modulatesvisfati[r]

and GABAC receptors which are ionotropic receptors include the increased Cl- ion conductance, whereas for GABAB receptors (metabotropic receptors) which are coupled to G proteins and thereby altering indirectly membrane ion permeability and neuronal excitability. The info[r]

plant miRNA genes, we performed genome-wide analyses of Arabidopsisthaliana, Populus trichocarpa, Oryza sativa and Sorghum bicolor. Ourresults showed that miRNA pair distances were significantly higher thanwould have been expected to occur at random and that the number ofmiRNA gene pair[r]

asdescribedinthelegendsofFigs2and3.Fig. 5. Time course of 17b-HSD-11 and 17 b-HSD-4 mRNA inductionby Wy14 643 in hepatoma Fao cells. Wy14 643 was added to themedium of rat hepatoma Fao cells in the co nfluent stage at time 0 andthe cells were collected at the time indicated for total RN[r]

Boyd, D., and Beckwith, J. 1990. The role of charged amino acids in the localiza-tion of secreted and membrane proteins. Cell 62:1031–1033.Buell, G., Schulz, M. F., Selzer, G., Chollet,A., Movva, N. R., Semon, D., Escanez,S., and Kawashima, E. 1985. Optimizing the expression in E. coli[r]

complexes consisting at least in part ofoligomerized PPARb, and that these complexes arepolyubiquitinated and rapidly degraded. This possiblyserves as a safeguard mechanism protecting the cellfrom deregulated PPARb expression that could poten-tially occur under certain pathological conditions. Sucha[r]

500 Arcola Road, Collegeville, PA 19426, USAEmail: Elizabeth A DiBlasio-Smith - ldiblasio@wyeth.com; Maya Arai - mxarai@wyeth.com; Elaine M Quinet - quinete@wyeth.com; Mark J Evans - evansm@wyeth.com; Tad Kornaga - kornagt@wyeth.com; Michael D Basso - bassom1@wyeth.com; Liang Chen - chenl1@wyeth.com[r]

(Fig. 1B). In our screening, Clcn5 was listed as a poten-tial Six1-specific target and it is reasonable that eventhe genes naturally repressed by Six1 were activated byVP16–Six1 in our screening condition. Slc12a2 promo-ter was strongly activated by Six1, but weakly activa[r]

the gastrulation period (~7-9 hpf), irf6 expression is concentrated in the forerunner cells.From the bud stage to the 3-somite stage (~10–11 hpf), irf6 is highly expressed in theKupffer’s vesicle and at the 14-somite (16 hpf), expression is observed in the otic placode.From 2-5 day post fertilizatio[r]

inhibition of Y1 receptor internalization by these agents(Fig. 5B). With the gpY1-CHO receptor (which is inten-sively internalized and recycled, as different from the gpY2receptor expressed in the same cell type [12]), there was agradual relative increase (over eightfold) in labeled surfacesi[r]

genomic plasticity among diplomonads and significant lat-eral gene transfer in eukaryote genome evolution. BMCGenomics 2007, 8:51.29. Carlton JM, Hirt RP, Silva JC, Delcher AL, Schatz M, Zhao Q, Wort-man JR, Bidwell SL, Alsmark UCM, Besteiro S, Sicheritz-Ponten T,Noel CJ, Dacks JB, Foster PG, Simill[r]

detectable levels of desferrioxamines. The Adm proteinmay act as a positive regulator of desferrioxamineACBFig. 6. Immunodetection of DmdR1 and Adm proteins. (A,B) Western blot reactions of wild-type S. coelicolor A3(2) (lane 2) and the TAadm(lane 3), TAdmdR1 (lane 4) and[r]

appears that only adipocytes in the cephalic regionderive from the cranial neural crest [32] and that theother major depots have a separate developmentalorigin. It is very likely that the subcutaneous versusvisceral white depots have distinct origins because theyeach express a unique pattern of