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Image Search Results
Journal: Molecular plant
Article Title: DET1-mediated COP1 regulation avoids HY5 activity over second-site gene targets to tune plant photomorphogenesis.
doi: 10.1016/j.molp.2021.03.009
Figure Lengend Snippet: Figure 1. DET1- and COP1-associated proteins. (A) Schematic representation of proteins found to associate with DET1 and COP1 in TAP assays. Color code represents the maximum number of peptides for each represented protein found in a TAP assay as detailed in Supplemental Table 1. DET1 and COP1 proteins were expressed in Arabidopsis cell cultures. Five independent TAP experiments were performed for DET1 and two for COP1 (Supplemental Table 2). (B) MBP-COP1 and MBP-HY5 recombinant proteins expressed in E. coli pulled-down MYC-DET1 from 7-day-old Arabidopsis seedlings. MBP re- combinant protein was used as a control. Anti-MYC and anti-MBP antibodies were used for the immunoblots. (C and D) F€orster resonance energy transfer-fluorescence lifetime imaging microscopy (FRET–FLIM) analysis of the interaction between COP1 or HY5 fused to GFP and DET1 (C), and HY5 or COP1 fused to RFP (D). Box plots show the distribution of 5–9 measurements ±SD. (E) FRET–FLIM analysis of the interaction between GFP-COP1 and RFP-HY5 upon cluc-DET1 co-expression. Box plots show the distribution of 10 measurements ±SD. All FRET assays were performed following transient expression in N. benthamiana leaves. Free RFP was used as negative control. FE, FRET efficiency. Asterisks indicate statistically significant differences according to Student’s t-test (****p < 0.0001; ***p < 0.001; *p < 0.01). For all FRET experiments three independent biological replicates were performed, and results from one replicate are shown.
Article Snippet: Pull-down assays MBP recombinant protein fusions were expressed in the
Techniques: Recombinant, Control, Western Blot, Förster Resonance Energy Transfer, Imaging, Microscopy, Expressing, Negative Control
Journal: Cell reports
Article Title: Inhibition of FGF10-ERK signal activation suppresses intraductal papillary neoplasm of the bile duct and its associated carcinomas.
doi: 10.1016/j.celrep.2021.108772
Figure Lengend Snippet: Figure 5. Fgf10-induced IPNB shows stepwise carcinogenesis (A) Schematic representation of iFGF10: LSL-KrasG12D:Alb-Cre or Pdx1-Cre (iFGF10KA or iFGF10KP, respectively) mice. (B) H&E images of IPNB lesion in iFGF10KA (Kras+) and iFGF10A (Kras) mice following 0.002% Dox administration for 6 weeks (N = 5 each). Insets indicate high magnification of the rectangles.
Article Snippet: REAGENT or RESOURCE SOURCE IDENTIFIER Antibodies Mouse Monoclonal Anti-Human Cytokeratin (clones AE1/AE3) DAKO Cat# M3515 LOT: 10066159 Rabbit Polyclonal Phospho-p44/42 MAPK (Erk1/2) (Thr202/Tyr204) (D13.14.4E) Cell Signaling Technology Cat# 4370 RRID:AB_2315112 Rabbit polyclonal Anti-alpha smooth muscle Actin [1A4] Abcam Cat# ab7817 Rabbit polyclonal Anti-S100 antibody Abcam Cat# ab166649
Techniques:
Journal: Cell reports
Article Title: Inhibition of FGF10-ERK signal activation suppresses intraductal papillary neoplasm of the bile duct and its associated carcinomas.
doi: 10.1016/j.celrep.2021.108772
Figure Lengend Snippet: Figure 6. Fgf10 is required for maintaining papillary structure defined as IPNB (A) Experimental design of the withdrawal of Dox and/or TAA administration to iFGF10 mice: (1) Dox-only (Dox+) administration and (2) TAA+Dox+ administration followed by the withdrawal (OFF) (N = 5 each). ‘‘IPNB establishment time’’ and ‘‘endpoint time’’ are indicated.
Article Snippet: REAGENT or RESOURCE SOURCE IDENTIFIER Antibodies Mouse Monoclonal Anti-Human Cytokeratin (clones AE1/AE3) DAKO Cat# M3515 LOT: 10066159 Rabbit Polyclonal Phospho-p44/42 MAPK (Erk1/2) (Thr202/Tyr204) (D13.14.4E) Cell Signaling Technology Cat# 4370 RRID:AB_2315112 Rabbit polyclonal Anti-alpha smooth muscle Actin [1A4] Abcam Cat# ab7817 Rabbit polyclonal Anti-S100 antibody Abcam Cat# ab166649
Techniques:
Journal: Biomedicine & pharmacotherapy = Biomedecine & pharmacotherapie
Article Title: Signaling pathways involved in the expression of SZNF and the target genes binding with SZNF related to cyadox.
doi: 10.1016/j.biopha.2018.09.141
Figure Lengend Snippet: Fig. 2. Effect of cyadox on the expressions of STATs and Smads mRNA in swine hepatocyte. AG490 (Fig. 2A-C) or SB431542 (Fig. 2D-G) were applied in 2 μM cyadox- treated swine hepatocyte. The expression of STAT1, STAT3, STAT5B, Smad1, Smad2, Smad3 and Smad4 were detected by qRT-PCR. The results were presented as Mean ± SD. (n = 6). Significant differences were indicated by * p < 0.05, ** p < 0.01, versus control and # p < 0.05, ## p < 0.01, versus cyadox.
Article Snippet: Phospho-Akt (Ser473) Antibody, Phospho-p38 MAPK (Thr180/Tyr182) Antibody,
Techniques: Expressing, Quantitative RT-PCR, Control
Journal: Biomedicine & pharmacotherapy = Biomedecine & pharmacotherapie
Article Title: Signaling pathways involved in the expression of SZNF and the target genes binding with SZNF related to cyadox.
doi: 10.1016/j.biopha.2018.09.141
Figure Lengend Snippet: Fig. 3. Cyadox regulated the phosphorylation of signal factors in swine hepatocyte. A-D: The phosphorylation level of Smad3, STAT1, p38 and Akt in the presence of 2 μM cyadox and/or inhibitors of TGF-β, JAK/STAT, p38 MAPK and PI3K/Akt in swine hepatocyte were detected. E: The phosphorylation level of Smad3, STAT1, p38 and Akt after cyadox treatment at 0.5, 1, and 2 h. Significant difference was indicated by * p < 0.05, ** p < 0.01, versus control. # p < 0.05, ## p < 0.01, versus cyadox.
Article Snippet: Phospho-Akt (Ser473) Antibody, Phospho-p38 MAPK (Thr180/Tyr182) Antibody,
Techniques: Phospho-proteomics, Control