Journal: Nanomedicine

Article Title: Quantitative proteomic and phenotypic responses of urinary pathogens to CuO/Cu₂O nanoparticles

doi: 10.1080/17435889.2025.2579616

Figure Lengend Snippet: FESEM images of E. coli ATCC 700,928 (A, B), P. mirabilis ATCC 7002 (C, D), P. aeruginosa PA14 (E, F), and E. faecalis ATCC 29,212 (G, H). The scale bar in the images corresponds to 200 nm. A, C, E, and G are untreated (controls) and B, D, F, and H are CuO/Cu 2 O NP-treated for 10 min.

Article Snippet: Protein expression patterns and functional distribution in E. faecalis ATCC 29,212 after CuO/Cu2O NP treatment. cel, cellular processes and signaling; inf, Information storage and processing; met, metabolism.

Techniques:

Journal: Nanomedicine

Article Title: Quantitative proteomic and phenotypic responses of urinary pathogens to CuO/Cu₂O nanoparticles

doi: 10.1080/17435889.2025.2579616

Figure Lengend Snippet: Number of differentially expressed proteins in E. faecalis ATCC 29,212 following CuO/Cu₂O NP treatment.

Article Snippet: Protein expression patterns and functional distribution in E. faecalis ATCC 29,212 after CuO/Cu2O NP treatment. cel, cellular processes and signaling; inf, Information storage and processing; met, metabolism.

Techniques:

Journal: Nanomedicine

Article Title: Quantitative proteomic and phenotypic responses of urinary pathogens to CuO/Cu₂O nanoparticles

doi: 10.1080/17435889.2025.2579616

Figure Lengend Snippet: COG functional classification (major categories) of differentially expressed proteins in E. faecalis ATCC 29,212 after CuO/Cu₂O NP treatment. (A) Upregulated proteins. (B) Downregulated proteins.

Article Snippet: Protein expression patterns and functional distribution in E. faecalis ATCC 29,212 after CuO/Cu2O NP treatment. cel, cellular processes and signaling; inf, Information storage and processing; met, metabolism.

Techniques: Functional Assay

Journal: Nanomedicine

Article Title: Quantitative proteomic and phenotypic responses of urinary pathogens to CuO/Cu₂O nanoparticles

doi: 10.1080/17435889.2025.2579616

Figure Lengend Snippet: COG functional classification (detailed categories) of differentially expressed proteins in E. faecalis ATCC 29,212 after CuO/Cu₂O NP treatment. (A) Upregulated proteins. (B) Downregulated proteins. COG functional categories: J, translation, ribosomal structure, and biogenesis; K, transcription; L, replication, recombination, and repair; D, cell cycle control, cell division, chromosome partitioning; V, defense mechanisms; T, signal transduction mechanisms; M, cell wall/membrane/envelope biogenesis; N, cell motility; U, intracellular trafficking, secretion, and vesicular transport; O, post-translational modification, protein turnover, chaperones; C, energy production and conversion; G, carbohydrate transport and metabolism; E, amino acid transport and metabolism; F, nucleotide transport and metabolism; H, coenzyme transportand metabolism; I, lipid transport and metabolism; P, inorganic ion transport and metabolism; Q, secondary metabolite biosynthesis, transport, and catabolism. Poorly characterized (s) was excluded.

Article Snippet: Protein expression patterns and functional distribution in E. faecalis ATCC 29,212 after CuO/Cu2O NP treatment. cel, cellular processes and signaling; inf, Information storage and processing; met, metabolism.

Techniques: Functional Assay, Control, Transduction, Membrane, Modification

Journal: Nanomedicine

Article Title: Quantitative proteomic and phenotypic responses of urinary pathogens to CuO/Cu₂O nanoparticles

doi: 10.1080/17435889.2025.2579616

Figure Lengend Snippet: KEGG pathway classification (major groups) of differentially expressed proteins in E. faecalis ATCC 29,212 after CuO/Cu₂O NP treatment. (A) Upregulated proteins. (B) Downregulated proteins.

Article Snippet: Protein expression patterns and functional distribution in E. faecalis ATCC 29,212 after CuO/Cu2O NP treatment. cel, cellular processes and signaling; inf, Information storage and processing; met, metabolism.

Techniques:

Journal: Nanomedicine

Article Title: Quantitative proteomic and phenotypic responses of urinary pathogens to CuO/Cu₂O nanoparticles

doi: 10.1080/17435889.2025.2579616

Figure Lengend Snippet: KEGG pathway classification (detailed pathways) of differentially expressed proteins in E. faecalis ATCC 29,212 after CuO/Cu₂O NP treatment. (A) Upregulated proteins. (B) downregulated proteins.

Article Snippet: Protein expression patterns and functional distribution in E. faecalis ATCC 29,212 after CuO/Cu2O NP treatment. cel, cellular processes and signaling; inf, Information storage and processing; met, metabolism.

Techniques:

Journal: Nanomedicine

Article Title: Quantitative proteomic and phenotypic responses of urinary pathogens to CuO/Cu₂O nanoparticles

doi: 10.1080/17435889.2025.2579616

Figure Lengend Snippet: Protein expression patterns and functional distribution in E. faecalis ATCC 29,212 after CuO/Cu₂O NP treatment. cel, cellular processes and signaling; inf, Information storage and processing; met, metabolism. COG categories are as defined in .

Article Snippet: Protein expression patterns and functional distribution in E. faecalis ATCC 29,212 after CuO/Cu2O NP treatment. cel, cellular processes and signaling; inf, Information storage and processing; met, metabolism.

Techniques: Expressing, Functional Assay

Journal: Nanomedicine

Article Title: Quantitative proteomic and phenotypic responses of urinary pathogens to CuO/Cu₂O nanoparticles

doi: 10.1080/17435889.2025.2579616

Figure Lengend Snippet: Proposed antibacterial mechanisms of CuO/Cu₂O NPs in E. faecalis and P. mirabilis .

Article Snippet: Protein expression patterns and functional distribution in E. faecalis ATCC 29,212 after CuO/Cu2O NP treatment. cel, cellular processes and signaling; inf, Information storage and processing; met, metabolism.

Techniques:

Journal: Journal of biomechanics

Article Title: Tensile strain increases expression of CCN2 and COL2A1 by activating TGF-β-Smad2/3 pathway in chondrocytic cells.

doi: 10.1016/j.jbiomech.2013.03.028

Figure Lengend Snippet: Fig. 2. CTS increased the deposition of CCN2 (A, green) in the cytoplasm of chondrocytic SW1353 cells. In addition, CTS induced nuclear translocalization of Smad2/3 (A, green) and SOX9 (A, green) in SW1353 cells. Controls in the absence of primary antibodies showed no signals. Double-headed arrows represent the direction of stretching (Red, F-actin; Bars, 25 μm). In Western blot (WB) analysis, CTS treatment (2 h) did not influence total amounts of endogenous Smad2/3 and SOX9 in each whole cell lysate (B, 20 μg/lane). However, Smad2/3 detected in the nuclear fraction was increased by CTS (C, nucleus, 20 μg/lane). In IP analysis using an anti-SOX9 antibody, CTS increased the association between phosphorylated Smad2/3 and SOX9 in the nuclear fraction derived from stretched SW1353 cells (C, IP). Arrows indicate an expected size for each protein. (For interpretation of the references to color in this figure legend, the reader is referred to the web version of this article.)

Article Snippet: The distribution of CCN2 protein in SW1353 cells was assessed by immunohistochemical analyses using a goat anti-CCN2 antibody (R&D Systems, Minneapolis, MN, working dilution 1:100 for 1 h incubation) as described by Miyake et al. (2011).

Techniques: Western Blot, Derivative Assay

Journal: Journal of biomechanics

Article Title: Tensile strain increases expression of CCN2 and COL2A1 by activating TGF-β-Smad2/3 pathway in chondrocytic cells.

doi: 10.1016/j.jbiomech.2013.03.028

Figure Lengend Snippet: Fig. 3. (A) CTS treatment (2 h) increased relative luciferase activity of pTS589, which contained the human CCN2 promoter, compared with a level of unstretched control in chondrocytic SW1353 cells. Smad2 transfection also stimulated pTS589 luciferase activity. No additional increase of the pTS589 activity was observed in Smad2-transfected cells under stretched condition. On the other hand, Smad3 and CTS synergistically enhanced the pTS589 activity up to a 2-fold level of control (*po0.05). (B) Chromatin IP analysis revealed that 2-h CTS treatment increased the association between Smad2/3 and the Smad-binding element located at the CCN2 promoter 2 in SW1353 cells. PCR fragment derived from the CCN2 promoter 2 was increased in the chromatin IP fraction using an anti-Smad2/3 antibody under a stretched condition (B, promoter 2), compared with that in unstretched condition (B, promoter 2). The CCN2 promoter 1 that did not contain the Smad-binding element was not amplified in chromatin IP analysis (B, promoter 1). CTS also induced the association between Smad2/3 and the COL2A1 enhancer in SW1353 cells (C, enhancer). The SOX9-binding site-free fragment was not detected in chromatin IP fraction (C, promoter). Mouse IgG was used as the control for chromatin IP (IgG). Schemes involving the promoters of human CCN2 and COL2A1 are shown (B and C). Gray box denotes the Smad-binding element on the CCN2 promoter (B). Filled box indicates the SOX9-binding site on the COL2A1 enhancer (C). Numbers indicate the distance from the transcription start site of the CCN2 gene (GenBank, AF316366) and the COL2A1 (GenBank, AC004801). Arrowheads and dotted lines denote the primer sets and expected PCR fragments in chromatin IP, respectively (B and C).

Article Snippet: The distribution of CCN2 protein in SW1353 cells was assessed by immunohistochemical analyses using a goat anti-CCN2 antibody (R&D Systems, Minneapolis, MN, working dilution 1:100 for 1 h incubation) as described by Miyake et al. (2011).

Techniques: Luciferase, Activity Assay, Control, Transfection, Chromatin Immunoprecipitation, Binding Assay, Derivative Assay

Journal: Journal of biomechanics

Article Title: Tensile strain increases expression of CCN2 and COL2A1 by activating TGF-β-Smad2/3 pathway in chondrocytic cells.

doi: 10.1016/j.jbiomech.2013.03.028

Figure Lengend Snippet: Fig. 6. Schematic illustration of mechanical stretch-mediated responses in chondrocytic cells. (A) In the absence of stretching force, sufficient amounts of SOX9, TGF-β1, and Smad2/3 are stored in the cytoplasm of chondrocytic cells. Gene expression of COL2A1 and CCN2 is maintained, but not excessively up-regulated, under unstretched condition. (B) Physiological stretching force induces TGF-β1 secretion from the cytoplasm of chondrocytic cells. Extracellular TGF-β1 would stimulate membrane-bound TGF- β receptors in an autocrine (or paracrine) fashion. Then, the nuclear translocalization of TGF-β receptor-regulated Smad2/3 is activated. In addition, mechanical stretch induces the nuclear translocalization of SOX9. Phosphorylated (P) Smad2/3 and SOX9 cooperatively enhance COL2A1 expression under stretched condition. CCN2 gene expression is also activated by nuclear translocated Smad2/3 in chondrocytic cells. Stretch-induced CCN2 would stimulate chondrocytic cell proliferation and COL2A1 expression.

Article Snippet: The distribution of CCN2 protein in SW1353 cells was assessed by immunohistochemical analyses using a goat anti-CCN2 antibody (R&D Systems, Minneapolis, MN, working dilution 1:100 for 1 h incubation) as described by Miyake et al. (2011).

Techniques: Gene Expression, Membrane, Expressing