Journal: Journal of Ovarian Research

Article Title: Trophoblast cell surface antigen 2 (TROP2) from ascitic extracellular vesicles drives peritoneal metastasis of ovarian cancer by mesothelial-to-mesenchymal transition

doi: 10.1186/s13048-025-01845-6

Figure Lengend Snippet: Mesothelial-mesenchymal transition of peritoneal mesothelial cells induced by ascites-derived EVs. A TEM analysis of EVs. B NTA analysis of EVs. C Western blot analysis of EVs markers. D Dil-labeled EVs were incubated with HMrSV5 cells for 24 h and then observed under a fluorescence microscope (Dil in red and DAPI in blue). HMrSV5 cells were incubated with EVs derived from Cancer EVs and Normal EVs, respectively. The PBS group and the TGF-β1 (0.5 ng/mL) + IL-1β (2.5 ng/mL) group served as negative and positive controls, respectively. E - H . The protein levels of E-Cadherin, N-Cadherin and Vimentin in HMrSV5 cells incubated with Cancer EVs and Normal EVs. I - J . The effect of HMrSV5 cells incubated with Cancer EVs and Normal EVs migration analyzed by Transwell assay. K - M . Representative images depicting the adhesion of CMTPX-labelled SKOV3 (red) and OVCAR3 (red) cells to HMrSV5 cells (blue) are shown and adhered cells were quantified. Data are representative of at least three independent experiments and are presented as mean ± SD. * P < 0.05, ** P < 0.01, *** P < 0.001

Article Snippet: D-Luciferin potassium salt was obtained from Yeasen (China), recombinant human TGF-β1 and human IL-1β were from R&D Systems (USA), and quinazoline (QNZ) was purchased from MCE (USA).

Techniques: Derivative Assay, Western Blot, Labeling, Incubation, Fluorescence, Microscopy, Migration, Transwell Assay

Journal: PLoS ONE

Article Title: Hydrophobin Fusion of an Influenza Virus Hemagglutinin Allows High Transient Expression in Nicotiana benthamiana , Easy Purification and Immune Response with Neutralizing Activity

doi: 10.1371/journal.pone.0115944

Figure Lengend Snippet: Wild-type cells (a), cells expressing H1 (b) and cells expressing H1-HFBI (c–e) at the exponential phase (3 days after dilution) were submitted to in situ immunolocalization as described in the using an FITC-conjugated anti-influenza H1N1. Bars = 25 µm (a, b, c) and 5 µm (d, e).

Article Snippet: To obtain a rough estimation of the expression level of recombinant H1 and H1-HFBI proteins, an immunoblotting technique was applied using the extracellular domain of a recombinant Influenza A/Texas/05/2009(H1N1) hemagglutinin produced in human cells (11085-V08H, Sino Biologicals, China) as a standard.

Techniques: Expressing, In Situ

Journal: PLoS ONE

Article Title: Hydrophobin Fusion of an Influenza Virus Hemagglutinin Allows High Transient Expression in Nicotiana benthamiana , Easy Purification and Immune Response with Neutralizing Activity

doi: 10.1371/journal.pone.0115944

Figure Lengend Snippet: (a) Hemagglutination assay was performed as indicated in Material and methods using serial two-fold diluted samples of duplicate (R1, R2) TSP fractions extracted from leaves expressing H1-HFBI or untagged H1. The two bottom rows contain inactivated A/Texas/05/2009(H1N1) virus as a positive control or a GFP-HFBI extract as a negative control. (b) Hemagglutination assay using serial two-fold diluted samples of ATPS-purified H1-HFBI (triplicates, R1–R3). The two bottom rows contain bovine serum albumin as a negative control or inactivated A/Texas/05/2009(H1N1) virus as a positive control. The hemagglutination titer (HT) or the amount of hemagglutination units (HAU) was calculated according to the well with the highest dilution giving a complete hemagglutination. This test was also used to quantify inactivated virus concentration in terms of HAU for inhibition assay.

Article Snippet: To obtain a rough estimation of the expression level of recombinant H1 and H1-HFBI proteins, an immunoblotting technique was applied using the extracellular domain of a recombinant Influenza A/Texas/05/2009(H1N1) hemagglutinin produced in human cells (11085-V08H, Sino Biologicals, China) as a standard.

Techniques: Hemagglutination Assay, Expressing, Positive Control, Negative Control, Purification, Concentration Assay, Inhibition

Journal: PLoS ONE

Article Title: Hydrophobin Fusion of an Influenza Virus Hemagglutinin Allows High Transient Expression in Nicotiana benthamiana , Easy Purification and Immune Response with Neutralizing Activity

doi: 10.1371/journal.pone.0115944

Figure Lengend Snippet: (a) ATPS-purified H1-HFBI (200 µg) was injected onto a Superdex G200 size exclusion column as described in the . Elution was fractionated in 1 ml aliquots. The logarithmic size of the standards (black square) is plotted according to their elution volume and peaks corresponding to H1-HFBI are indicated (red dot). (b) Fractions eluted at 14 ml to 18 ml and 27 ml to 31 ml were analyzed by Western blotting with an anti-influenza H1N1 and an anti-goat HRP-conjugated secondary antibody, and the signal was quantified using the Kodak image station 4000R (Arbitrary unit; <: below detection level).

Article Snippet: To obtain a rough estimation of the expression level of recombinant H1 and H1-HFBI proteins, an immunoblotting technique was applied using the extracellular domain of a recombinant Influenza A/Texas/05/2009(H1N1) hemagglutinin produced in human cells (11085-V08H, Sino Biologicals, China) as a standard.

Techniques: Purification, Injection, Western Blot

Journal: PLoS ONE

Article Title: Hydrophobin Fusion of an Influenza Virus Hemagglutinin Allows High Transient Expression in Nicotiana benthamiana , Easy Purification and Immune Response with Neutralizing Activity

doi: 10.1371/journal.pone.0115944

Figure Lengend Snippet: (a) Ten mice were immunized with H1-HFBI as indicated in the . Anti-HA antibodies were assayed by ELISA in the pre-immune sera (open circle) and the sera collected after the 4 th (blue triangle) and 6 th (red square) boost. Plates were coated with 5 µg/ml of recombinant Influenza A/Texas/05/2009(H1N1) ectodomain expressed in mammalian cells (Sino Biologicals, 11085-V08H). HRP-conjugated anti-mouse secondary antibody was used for detection. HA titer was calculated as the highest dilution giving a signal higher than three times the signal coming from the negative control. (b) Box and whisker analysis of antibody titers obtained after endpoint ELISA titer analysis of the test groups. Each dot represents the antibody titer from an individual mouse. (p-values = 0.18 (boost 4/boost 6), 1.8.10 −4 (boost 4/pre-immune), 3.8.10 −4 (boost 6/pre-immune))

Article Snippet: To obtain a rough estimation of the expression level of recombinant H1 and H1-HFBI proteins, an immunoblotting technique was applied using the extracellular domain of a recombinant Influenza A/Texas/05/2009(H1N1) hemagglutinin produced in human cells (11085-V08H, Sino Biologicals, China) as a standard.

Techniques: Enzyme-linked Immunosorbent Assay, Recombinant, Negative Control, Whisker Assay

Journal: Cells

Article Title: Phosphoproteomic Landscape of AML Cells Treated with the ATP-Competitive CK2 Inhibitor CX-4945

doi: 10.3390/cells10020338

Figure Lengend Snippet: Phosphoproteomic and proteomic analysis of human AML cells treated with the CK2 inhibitor CX-4945: ( A ) Workflow for the exploration of phosphorylation changes induced in HL-60 and OCI-AML3 cells after treatment with CX-4945. Three biological replicates of each group were evaluated; ( B ) Number of identified and significantly modulated phosphopeptides and proteins in each AML cell line. Phosphoproteomic results are showed before and after normalization with the proteome dataset. (*) MED-FASP: multienzyme digestion filter-aided sample preparation .

Article Snippet: Human AML cell lines HL-60 and OCI-AML3 were originally obtained from the American Type Culture Collection (ATCC, Manassas, VA, USA) and the German Collection of Microorganisms and Cell Cultures (DSMZ, Braunschweig, Germany), respectively.

Techniques: Phospho-proteomics, Sample Prep

Journal: Cells

Article Title: Phosphoproteomic Landscape of AML Cells Treated with the ATP-Competitive CK2 Inhibitor CX-4945

doi: 10.3390/cells10020338

Figure Lengend Snippet: Signaling pathways and biological processes deregulated in primary AML cells and modulated by the CK2 inhibitor CX-4945 in AML cell lines. Phosphoproteins up-regulated in primary AML cells and down-phosphorylated in CX-4945-treated AML cells are indicated.

Article Snippet: Human AML cell lines HL-60 and OCI-AML3 were originally obtained from the American Type Culture Collection (ATCC, Manassas, VA, USA) and the German Collection of Microorganisms and Cell Cultures (DSMZ, Braunschweig, Germany), respectively.

Techniques: Protein-Protein interactions