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Image Search Results
Journal: Viruses
Article Title: Cap Is the Protease of the Porcine Circovirus 2
doi: 10.3390/v14071550
Figure Lengend Snippet: The protein-protein interactions (PPIs) network analysis using STRING database. The linkers indicate associations of function and physical protein. The thickness of line indicates the strength of correlation (PPI enrichment p value < 0.05). Proteins represented have been named as NCBI gene names. JMJD6 and CCT5 were marked with Stars.
Article Snippet: The gene cap, JMJD6 and
Techniques: Protein-Protein interactions
Journal: Viruses
Article Title: Cap Is the Protease of the Porcine Circovirus 2
doi: 10.3390/v14071550
Figure Lengend Snippet: We validated the PCV2 Cap down-regulated host proteins by Western blotting (WB). ( A ) The expression of JMJD6 in PK-15 cells was determined by WB analysis. ( B ) The expression of CCT5 in PK-15 cells was determined by WB analysis.
Article Snippet: The gene cap, JMJD6 and
Techniques: Western Blot, Expressing
Journal: Viruses
Article Title: Cap Is the Protease of the Porcine Circovirus 2
doi: 10.3390/v14071550
Figure Lengend Snippet: Expression and purification of Cap, JMJD6 and CCT5. ( A ) SDS-PAGE analysis of the purified EDA-Cap. M, protein molecular mass standards; 1, the purified EDA-PCV2 Cap. ( B ) SDS-PAGE analysis of the purified JMJD6. M, protein molecular mass standards; 1, soluble fraction after cell sonication; 2, the purified JMJD6. ( C ) SDS-PAGE analysis of the purified CCT5. M, protein molecular mass standards; 1, soluble fraction after cell sonication; 2, the purified CCT5.
Article Snippet: The gene cap, JMJD6 and
Techniques: Expressing, Purification, SDS Page, Sonication
Journal: Viruses
Article Title: Cap Is the Protease of the Porcine Circovirus 2
doi: 10.3390/v14071550
Figure Lengend Snippet: The in vitro reaction assays and the PPI networks. ( A ) SDS-PAGE analysis the in vitro reaction that Cap digested JMJD6 and CCT5 at 37 °C 30 min, respectively. ( B ) Statistical analysis of the deduction of JMJD6 and CCT5 due to the digestion of Cap. All data were obtained from at least three independent experiments ( p < 0.05, p < 0.01, *** p < 0.001). ( C ) The PPI networks of the PCV2 Cap with JMJD6 and CCT5.
Article Snippet: The gene cap, JMJD6 and
Techniques: In Vitro, SDS Page
Journal: PLoS ONE
Article Title: Accurate Promoter and Enhancer Identification in 127 ENCODE and Roadmap Epigenomics Cell Types and Tissues by GenoSTAN
doi: 10.1371/journal.pone.0169249
Figure Lengend Snippet: GenoSTAN was learned on all 127 cell types and tissues (GenoSTAN-127) using the five core marks H3K4me1, H3K4me3, H3K36me3, H3K27me3, H3K9me3 and an input control (ChromHMM-15 was learned on the same data). To improve accuracy additional histone modifications H3K27ac, H3K9ac and DNase-Seq were used to learn another model (GenoSTAN-20) on a subset of 20 cell types and tissues, where the marks were available. (A) Performance of chromatin states in recovering FANTOM5 CAGE tags in 127 cell types. CAGE tags were verlapped with chromatin states wihout the use of cell type information. Cumulative FDR and recall are calculated by subsequently adding states (in order of increasing FDR). (B) Performance of chromatin states in recovering GRO-cap transcription start sites in two cell types where GRO-cap data was available. (C) The same as in (B) for ENCODE HOT regions for five cell types where annotation of HOT regions was available. (D) Recall of FANTOM5 promoters and enhancers by predicted promoters and enhancersis plotted to assess how well models distinguish promoters from enhancers. (E) The fraction of predicted enhancer segments bound by individual TFs is shown for different studies. GenoSTAN enhancers are more frequently bound by TFs than those from other studies.
Article Snippet: This approach leverages extensive genome-wide datasets of chromatin-immunoprecipitation followed by sequencing (ChIP-Seq) of transcription factors (TFs), histone modifications, or
Techniques: Control