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Image Search Results
Journal: Insect Science
Article Title: lncR26319/miR‐2834/ EndophilinA axis regulates oogenesis of the silkworm, Bombyx mori
doi: 10.1111/1744-7917.13082
Figure Lengend Snippet: List of primers
Article Snippet: The lncR26319 ASO was transfected into the
Techniques: Negative Control, Sequencing, Control, Mutagenesis, In Situ Hybridization
Journal: Insect Science
Article Title: lncR26319/miR‐2834/ EndophilinA axis regulates oogenesis of the silkworm, Bombyx mori
doi: 10.1111/1744-7917.13082
Figure Lengend Snippet: lncR26319 regulates Endophilin A ( EndoA ) by binding to miR‐2834. The expression level of lncR26319 (A) and miR‐2834 (B) after knockdown of lncR26319 with antisense oligonucleotide (ASO) (lncR26319i). (C) Expression change of EndoA after lncR26319 knockdown (lncR26319i). (D) Messenger RNA (mRNA) level of lncR26319 after overexpression of lncR26319 (pIE‐EGFP‐lncR26319). (E) Expression change of EndoA after lncR26319 and miR‐2834 overexpress in BmN4 cells. Three independent experiments were performed, and each sample was repeated 3 times (values are means ± SEM of 3 experiments. * P < 0.05, *** P < 0.001). Significance analysis was conducted with ANOVA and Student's t ‐test. ANOVA, analysis of variance; SEM, standard error of the mean.
Article Snippet: The lncR26319 ASO was transfected into the
Techniques: Binding Assay, Expressing, Knockdown, Over Expression
Journal: Insect Science
Article Title: lncR26319/miR‐2834/ EndophilinA axis regulates oogenesis of the silkworm, Bombyx mori
doi: 10.1111/1744-7917.13082
Figure Lengend Snippet: Expression changes of yolk family genes after knockdown of miR‐2834 in BmN4 cells. Expression changes of miR‐2834 (A), lncR26319 (B), and Endophilin A ( EndoA ) (C) after knockdown of miR‐2834. Expression level of yolk protein (Yp) genes were normalized to actinA3 . (D) Expression changes of yolk family genes after repression of miR‐2834. The expression level of yolk family genes was normalized to RP49 . Three independent experiments were performed, and each sample was repeated 3 times (values are means ± SEM of 3 experiments. n.s. P > 0.05, * P < 0.05, *** P < 0.001). Significance analysis was conducted with ANOVA and Student's t ‐test. ANOVA, analysis of variance; SEM, standard error of the mean.
Article Snippet: The lncR26319 ASO was transfected into the
Techniques: Expressing, Knockdown
Journal: PLOS ONE
Article Title: Human BST2 inhibits rabies virus release independently of cysteine-linked dimerization and asparagine-linked glycosylation
doi: 10.1371/journal.pone.0292833
Figure Lengend Snippet: (A) HEK293T cells were transfected with plasmids expressing flag-hBST2. Cell lysates were prepared and incubated in the presence or absence of PNGase F and subjected to western blot analysis of hBST2. HEK293T cells were transfected with (B) 1 μg of flag-hBST2 plasmid and an increasing amount (0.5, 1 and 2 μg) of plasmids encoding RABV G-myc, M-myc, N-myc and P-myc or (C) 1 μg of plasmids encoding individual myc-tagged RABV proteins with an increasing amount of flaghBST2 plasmid (0.5, 1 and 2 μg). At 48 hpt, cell lysates were collected and analyzed by western blotting for RABV protein and hBST2 expression using rabbit α-myc and α-human BST2 antibodies, respectively. Arrow heads indicate glycosylated monomeric hBST2 of approximately 30 kDa. Arrows indicate a low molecular weight, glycosylated dimeric hBST2 of approximately 55 kDa. Asterisks indicate high molecular weight glycosylated dimeric hBST2 of approximately 65 kDa.
Article Snippet: HEK293T cells seeded in 10-cm 2 dishes were transfected with 6 μg of plasmid expressing RABV Gmyc and
Techniques: Transfection, Expressing, Incubation, Western Blot, Plasmid Preparation, Molecular Weight, High Molecular Weight
Journal: PLOS ONE
Article Title: Human BST2 inhibits rabies virus release independently of cysteine-linked dimerization and asparagine-linked glycosylation
doi: 10.1371/journal.pone.0292833
Figure Lengend Snippet: HEK293T cells were transfected with plasmids expressing RABV Gmyc and flaghBST2. At 24 hpt, cells were fixed and probed with mouse α-myc and rabbit α-human BST2 primary antibodies to detect RABV G and hBST2, respectively followed by Alexa Fluor ® 488-conjugated goat α-rabbit IgG H&L and Alexa Fluor ® 647-conjugated goat α-mouse IgG H&L secondary antibodies. Localization of the proteins were visualized by confocal microscopy.
Article Snippet: HEK293T cells seeded in 10-cm 2 dishes were transfected with 6 μg of plasmid expressing RABV Gmyc and
Techniques: Transfection, Expressing, Confocal Microscopy