mers cov pseudovirus  (Sino Biological)

Journal: ACS Omega

Article Title: Structure-Based Drug Discovery of Triazine Derivatives as Potent and Orally Bioavailable AXL Inhibitors for Cancer Therapy

doi: 10.1021/acsomega.6c04179

Figure Lengend Snippet: Molecular docking results of three compounds with the kinase domains of MER and AXL. (A) Molecular docking of merestinib with MER kinase domain (PDB: 7AAY ). (B) Binding mode analysis of compound 1 to the AXL kinase domain (PDB: 5U6B ). (C) Molecular docking of merestinib with AXL DFG-out homologous modeling. (D) Molecular docking of compound w4 with AXL DFG-out homologous modeling.

Article Snippet: In 2017, researchers from Pfizer reported the X-ray cocrystal structures of AXL and MER kinase domains in complex with a type I AXL/MER inhibitor macrocyclic compound 1 , and elucidated the differences between the kinase ATP binding sites.

Techniques: Binding Assay

Journal: Vaccines

Article Title: Immunogenicity of Theileria parva p67C Antigen Delivered via Adjuvanted CoPoP Liposomes in Cattle and Mice

doi: 10.3390/vaccines14050459

Figure Lengend Snippet: p67C-CoPoP liposome nanoparticle characterisation. ( A ) Schematic representation of the generation of CoPoP liposomes with p67C antigen, including the schematic illustrations of the chemical structures of the key adjuvanting molecules. ( B ) Binding capacity of the p67C antigen to CoPoP liposomes after 3 h incubation in the dark, analysed using HisPur™ Ni-NTA Magnetic Beads and assessed by SDS-PAGE. Formulations included: CA (CoPoP only), CQ (CoPoP/QS-21), CP (CoPoP/PHAD), and CPQ (CoPoP/PHAD/QS-21), compared to soluble p67C (PBS). Non-liposome-bound antigen is shown in lanes “B”, while liposome-bound is shown in lanes “S”. The uncropped blots are shown in . ( C ) Binding capacity of fluorophore-labelled p67C-DY490 to CoPoP liposomes (CA, CQ, CP, and CPQ) was measured and compared with p67C bound to AS01, and ( D ) size and ( E ) zeta potential of p67C bound to CoPoP liposomes were measured by DLS.

Article Snippet: Peptide epitope specificity of the immunised bovine sera was evaluated using ten overlapping biotinylated 15-mer peptides to p67C (Mimotopes Pty, Victoria, Australia [ ]), as previously described [ ].

Techniques: Liposomes, Binding Assay, Incubation, Magnetic Beads, SDS Page, Zeta Potential Analyzer

Journal: Vaccines

Article Title: Immunogenicity of Theileria parva p67C Antigen Delivered via Adjuvanted CoPoP Liposomes in Cattle and Mice

doi: 10.3390/vaccines14050459

Figure Lengend Snippet: IgG responses in both cattle and mice immunised with p67C using different CoPoP liposomes. Serum samples from cattle immunised with ( A ) p67C-CA, ( B ) p67C-CP, ( C ) p67C-CQ and ( D ) p67C-CPQ were evaluated using a p67C quantitative ELISA. Kinetics of individual animals are presented in panels ( A – D ), and the mean and standard error of the groups are presented in panel ( E ). Antigen inoculation times are indicated with black arrows in the x-axis. ( F ) Semi-quantification of antibody titres at day 42 in mice immunised with p67C-CPQ or p67C-Alum is presented as the mean of the last positive dilution and standard error per group. Significance is represented by a “*” for p < 0.05.

Article Snippet: Peptide epitope specificity of the immunised bovine sera was evaluated using ten overlapping biotinylated 15-mer peptides to p67C (Mimotopes Pty, Victoria, Australia [ ]), as previously described [ ].

Techniques: Liposomes, Enzyme-linked Immunosorbent Assay

Journal: Vaccines

Article Title: Immunogenicity of Theileria parva p67C Antigen Delivered via Adjuvanted CoPoP Liposomes in Cattle and Mice

doi: 10.3390/vaccines14050459

Figure Lengend Snippet: Cellular response specific to p67C by means of the INFγ-ELISpot assay. ( A ) CD4 + T-cell, ( B ) CD8 + T-cell and ( C ) PBMC responses to 15-mer and 25-mer based on the p67C sequence and p67C protein used as stimuli. Irrelevant peptides and proteins based on the sequence of p67N (N-terminal portion of p67) were used as negative controls. Cells were stimulated for 20 h at 37 °C. Results are presented as the group mean ± standard deviation (SD) of the fold change in the number of spot-forming units compared to the cells stimulated with media only (background). Dotted red lines indicate the cut-off from which the response can be considered different from the background (fold change of 2).

Article Snippet: Peptide epitope specificity of the immunised bovine sera was evaluated using ten overlapping biotinylated 15-mer peptides to p67C (Mimotopes Pty, Victoria, Australia [ ]), as previously described [ ].

Techniques: Enzyme-linked Immunospot, Sequencing, Standard Deviation

Journal: Vaccines

Article Title: Immunogenicity of Theileria parva p67C Antigen Delivered via Adjuvanted CoPoP Liposomes in Cattle and Mice

doi: 10.3390/vaccines14050459

Figure Lengend Snippet: IgG reactivity to p67C 15-mer overlapping peptides. Day 42 sera from cattle immunised with p67C-CoPoP liposomes: Group 3 (p67C-CQ) and Group 4 (p67C-CPQ) were analysed by means of an ELISA assay. Results are presented as a heat map of the relative reactivity compared to the sum of responses against all peptides for each animal.

Article Snippet: Peptide epitope specificity of the immunised bovine sera was evaluated using ten overlapping biotinylated 15-mer peptides to p67C (Mimotopes Pty, Victoria, Australia [ ]), as previously described [ ].

Techniques: Liposomes, Enzyme-linked Immunosorbent Assay

Journal: Nucleic Acids Research

Article Title: A thumb-domain insertion balances processivity and fidelity in DNA polymerase ε

doi: 10.1093/nar/gkag282

Figure Lengend Snippet: Denaturing PAGE (8%) showing the impact of absence/presence of PCNA on processive leading strand synthesis by wild type Pol ε and its variants. Extension of a 5′-TET-labeled 35–mer oligo annealed to M13mp18ssDNA (NEB). Reactions were performed at 40-fold molar excess of DNA substrate over polymerase to meet single-hit criteria. Individual reactions were stopped at 0, 2, 5, and 15 min, respectively.

Article Snippet: The substrate for processivity assays was prepared by annealing M13mp18 single-stranded DNA (NEB) with a 5′-TET–labeled 35-mer oligonucleotide (TET-CCCAGTCACGACGTTGTAAAACGACGGCCAGTGCC) in equimolar amounts in 125 mM NaAc (pH 7.8).

Techniques: Labeling