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Image Search Results
Journal: International Journal of Molecular Sciences
Article Title: Structural Characterization of Glycoprotein Glycans and Glycosaminoglycans of Brain Tissues in Slc35a3 -Knockout Mice
doi: 10.3390/ijms27041643
Figure Lengend Snippet: Brain N -glycome in wild-type, hetero, and Slc35a3 -KO mice. ( a ) Representative MALDI-TOF mass spectra of PNGase F-released N -glycans from whole brain for wild-type, hetero, and Slc35a3 -KO mice. Individual peak intensity was normalized to the internal standard (I.S.). Annotated peaks are shown as predicted glycan structures, illustrated with SNFG cartoons. ( b ) Classwise quantification of N -glycans (pmol per 100 µg protein): paucimannose type, high-mannose type, hybrid type, neutral complex type, and acidic complex type. ( c ) Branching distribution of N -glycans expressed as the number of HexNAc residues added beyond the chitobiose core (Core + HexNAc0–4). Bars: mean ± SD; colors denote genotype (wild type, white; hetero, blue; KO, red), (ns, not significant; *, p < 0.05; **, p < 0.01 and ***, p < 0.001; unpaired two-tailed Student’s t test). Individual data points are shown as black dots overlaid on the bar graph. Representative glycan structures for each class are illustrated as SNFG cartoons above the graph.
Article Snippet: To verify N -glycan dependence of lectin binding, lysates were treated with
Techniques: Glycoproteomics, Two Tailed Test
Journal: International Journal of Molecular Sciences
Article Title: Structural Characterization of Glycoprotein Glycans and Glycosaminoglycans of Brain Tissues in Slc35a3 -Knockout Mice
doi: 10.3390/ijms27041643
Figure Lengend Snippet: Lectin blotting analysis for brain tissues from wild-type (WT) and Slc35a3 -KO (KO) mice using ( a , b ) concanavalin A (ConA) and ( c , d ) peanut agglutinin (PNA). ( a ) Homogenized brain lysates from wild-type and Slc35a3 -KO mice were enzymatically digested with PNGase F or Endo H and subjected to lectin blotting using ConA, which recognizes high-mannose-type N -glycans. ( c ) Brain lysates prepared as in ( a ) were enzymatically digested with O -glycosidase and/or neuraminidase and analyzed by lectin blotting using PNA, which recognizes Galβ1–3GalNAc structures. β-Actin was used as a loading control to verify equal protein loading. ( b , d ) Quantification of ConA ( b ) and PNA ( d ) signals shown in the lectin blots in ( a , c ) and . The raw data are provided in . Lectin blot intensities above 48 kDa were quantified for the entire lane and normalized to β-actin. Signal intensities are expressed relative to the WT control. Data represent three independent experiments ( n = 3); bars indicate mean ± SD. Statistical significance was assessed as indicated (ns, not significant; **, p < 0.01 and ***, p < 0.001; two-way ANOVA). Individual data points are plotted as black dots on the bar graph.
Article Snippet: To verify N -glycan dependence of lectin binding, lysates were treated with
Techniques: Control
Journal: Microorganisms
Article Title: Unraveling the Diversity of Co-Colonization by CPE
doi: 10.3390/microorganisms10071292
Figure Lengend Snippet: Summary of results for patient in Case Study 1—CPE positive bacteria, isolated in the point prevalence study performed by the National Centre for Infection Control (NCIC).
Article Snippet: The presence of a carbapenemase was confirmed using a commercial
Techniques: Isolation, Infection
Journal: Microorganisms
Article Title: Unraveling the Diversity of Co-Colonization by CPE
doi: 10.3390/microorganisms10071292
Figure Lengend Snippet: Summary of results of CPE-positive bacteria isolated during routine CPE screening in Case Study 2.
Article Snippet: The presence of a carbapenemase was confirmed using a commercial
Techniques: Isolation, Plasmid Preparation
Journal: Microorganisms
Article Title: Unraveling the Diversity of Co-Colonization by CPE
doi: 10.3390/microorganisms10071292
Figure Lengend Snippet: Summary of results of CPE-positive bacteria isolated during CPE screening in Case Study 3.
Article Snippet: The presence of a carbapenemase was confirmed using a commercial
Techniques: Isolation, Variant Assay, Plasmid Preparation
Journal: Antimicrobial Agents and Chemotherapy
Article Title: False-Positive Carbapenem-Hydrolyzing Confirmatory Tests Due to ACT-28, a Chromosomally Encoded AmpC with Weak Carbapenemase Activity from Enterobacter kobei
doi: 10.1128/AAC.02388-18
Figure Lengend Snippet: Results of carbapenemase detection testsa
Article Snippet: Among 1,039 non-carbapenemase-producing ECC isolates with decreased susceptibility to carbapenems received in 2016-2017 at the French
Techniques:
Journal: Antimicrobial Agents and Chemotherapy
Article Title: False-Positive Carbapenem-Hydrolyzing Confirmatory Tests Due to ACT-28, a Chromosomally Encoded AmpC with Weak Carbapenemase Activity from Enterobacter kobei
doi: 10.1128/AAC.02388-18
Figure Lengend Snippet: Phylogenetic analysis of AmpC β-lactamases of ECC isolates addressed to the French National Reference Center for carbapenemase detection. This unrooted tree was constructed based on ampC genes using the maximum likelihood method with the Tamura-Nei model using the MEGA program (MEGA 7.0) The tree is drawn to scale, with branch lengths representing the evolutionary distances. ACT-28-producing ECC isolates from the NCBI database (1323, e1425, MGH25, MGH37, ICBEaBL-111-03-02, CRE54, CRE71, and GN02825) and ampC of ECC genomes of Chavda’s phylogenomic groups B, C, E, J, G, H, and Q were added to the analysis (23). NR, not realized.
Article Snippet: Among 1,039 non-carbapenemase-producing ECC isolates with decreased susceptibility to carbapenems received in 2016-2017 at the French
Techniques: Construct