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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: Scientific Reports
Article Title: A comparison of two MALDI-TOF MS based assays for the detection of carbapenemases in Enterobacterales
doi: 10.1038/s41598-024-77952-z
Figure Lengend Snippet: Isolates and test results. Incorrect results in bold.
Article Snippet: Isolates then were tested using the to
Techniques: