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Fig. 2 in Lichen-associated bacteria transform antibacterial usnic acid to products of lower antibiotic activity

Fig. 2. HPLC chromatograms of M. ruber cultures with or without UA. A) At the beginning of the stationary phase of bacterial growth; B) After 7 days of stationary phase. Compounds circled in red appear only in the culture with UA. (For interpretation of the references to colour in this figure legend, the reader is referred to the Web version of this article.)

Fig. 5 in Lichen-associated bacteria transform antibacterial usnic acid to products of lower antibiotic activity

Fig. 5. Comparison of HPLC chromatograms of B. weihenstephanensis extracts with UA at 0.01 mg/mL after 1 day of culture (blue), 9 days of culture (black) and without UA after 9 days of culture (red). (For interpretation of the references to colour in this figure legend, the reader is referred to the Web version of this article.)

Fig. 8 in Lichen-associated bacteria transform antibacterial usnic acid to products of lower antibiotic activity

Fig. 8. Fragmentation patterns in negative mode of A) compound H and B) UA; common fragments are highlighted in orange. (For interpretation of the references to colour in this figure legend, the reader is referred to the Web version of this article.)

Fig. 8 in Antibacterial kaneoheoic acids A-F from a Hawaiian fungus Fusarium sp. FM701

Fig. 8. Key COSY (bolds) and HMBC (red arrows) correlations of compounds 5 and 6. (For interpretation of the references to colour in this figure legend, the reader is referred to the Web version of this article.)

Fig. 4 in Antibacterial kaneoheoic acids A-F from a Hawaiian fungus Fusarium sp. FM701

Fig. 4. Key COSY (bolds) and HMBC (red arrows) correlations of compounds 3 and 4. (For interpretation of the references to colour in this figure legend, the reader is referred to the Web version of this article.)

Fig. 2 in Antibacterial kaneoheoic acids A-F from a Hawaiian fungus Fusarium sp. FM701

Fig. 2. Key COSY (bolds) and HMBC (red arrows) correlations of compounds 1 and 2. (For interpretation of the references to colour in this figure legend, the reader is referred to the Web version of this article.)

Fig. 1 in 1,3-Dioxepine and spiropyran derivatives of viomellein and other dimeric naphthopyranones from cultures of Aspergillus elegans KUFA0015 and their antibacterial activity

Fig. 1. Structures of specialised metabolites isolated from the cultures of the marine sponge-associated fungus Aspergillus elegans KUFA0015.

Fig. 7 in 1,3-Dioxepine and spiropyran derivatives of viomellein and other dimeric naphthopyranones from cultures of Aspergillus elegans KUFA0015 and their antibacterial activity

Fig. 7. Models of 6 representing the two lowest energy conformations of the central ring (groups G1, left, and G2, right) as well as the lowest energy transition state model TS for the conversion between G1 and G2. For correct 3D interpretation of these projections, consider the H-11 nuclei nearer to the observer and the methoxy groups farther from the observer.

Fig. 6 in 1,3-Dioxepine and spiropyran derivatives of viomellein and other dimeric naphthopyranones from cultures of Aspergillus elegans KUFA0015 and their antibacterial activity

Fig. 6. Expansion and assignments of 1H NMR spectra of H-11 geminal nuclei, Ha and Hb, at two different temperatures, in DMSO‑d6, at 500 MHz. The measured scalar coupling constant of 5 Hz is within the typical range for geminal protons. Assignments refer to labels used in Fig. 7.

Fig. 2 in Molecular characterization and evaluation of the antibacterial activity of a plant defensin peptide derived from a gene of oat (Avena sativa L.)

Fig. 2. Identification and characterization of AsDef1 (A) The identification steps of AsDef1. (B) Complete ORF of AsDef1. The exons and intron sequences have been shown in black and grey, respectively.

Fig. 3 in Molecular characterization and evaluation of the antibacterial activity of a plant defensin peptide derived from a gene of oat (Avena sativa L.)

Fig. 3. Multiple sequence alignment of AsDef1 and defensins from mono- and dicotyledon plants. Gaps () were introduced to improve the alignment. The numbers above the sequences show the position of amino acids and the numbering must take into account the gaps. Black and grey colors indicate identical and conservative amino acids, respectively. The red box shows the conserved γ-core motif. Disulfide bonds are indicated by bidirectional arrows. Knot1 functional domain and signal sequence have been shown by grey and black lines, respectively. (For interpretation of the references to color in this figure legend, the reader is referred to the Web version of this article.)

Fig. 5 in Molecular characterization and evaluation of the antibacterial activity of a plant defensin peptide derived from a gene of oat (Avena sativa L.)

Fig. 5. Maximum Likelihood phylogenetic tree of AsDef1 and defensins from mono- and di-cotyledon plants. Blue (monocot group) and red (dicot group) highlights are two groups of defensins. The AsDef1 has been indicated by blue triangle. Below each defensin name, their GenBank accession number is shown. (For interpretation of the references to color in this figure legend, the reader is referred to the Web version of this article.)

Fig. 7 in Molecular characterization and evaluation of the antibacterial activity of a plant defensin peptide derived from a gene of oat (Avena sativa L.)

Fig. 7. The results of primary evaluation of the growth rate of bacteria under the effect of AsDef1 at 0.078215 μM. All assays were done in three replications. The bars represent standard errors. The star indicates a significance at p <0.05 level. The values above the bars show inhibition percentage.

Fig. 1 in Molecular characterization and evaluation of the antibacterial activity of a plant defensin peptide derived from a gene of oat (Avena sativa L.)

Fig. 1. Agarose gel electrophoresis of PCR products of AsDef1. (A) PCR on cDNA template, M: 100 bp marker, C-: Negative control, D: AsDef1. (B) PCR on DNA template. M: 1 kb marker, C-: Negative control (double-distilled water), D: AsDef1.

Fig. 4 in Molecular characterization and evaluation of the antibacterial activity of a plant defensin peptide derived from a gene of oat (Avena sativa L.)

Fig. 4. Amino acid sequence, secondary and 3D structures of AsDef1 without signal sequence. The α-helix and β-strands has been indicated within the sequence by color shading. The N- and C-terminals of AsDef1 peptide have been indicated by black circles. (For interpretation of the references to color in this figure legend, the reader is referred to the Web version of this article.)

opencc-by-4.0Sep 2023View details →

Field Emission Scanning Electron Microscopy Figures from metallic glass antibacterial coatings

<p>Field Emission Scanning Electron Microscopy Figures from metallic glass (Zr-Cu-Ag) antibacterial coatings. Coatings have the name SP in their file name. The non-coated comparison is PBT. This is after the antibacterial test with <em>S.Aureus</em> after 24 hours. </p>

closedIPD-NOFeb 2026View details →

Antibacterial Effect and Clinical Performance of Chitosan Modified Glass Ionomer

ClinicalTrials.gov study NCT04365270. IPD Sharing: NO. Countries: 1. Publications: 5.

restrictedIPD-UNDECIDEDFeb 2026View details →

Clinical Study of Antibacterial Nanoparticles Incorporated in Composite Restorations

ClinicalTrials.gov study NCT00299598. IPD Sharing: Not stated. Countries: 1. Publications: 1.

controlledIPD-YESFeb 2026View details →

Antibacterial Effect of the Infusion of Green Tea Used as a Mouthwash on Saliva and Bacterial Plaque

ClinicalTrials.gov study NCT04410666. IPD Sharing: YES. Countries: 1. Publications: 5.