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ATCC
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Image Search Results
Journal: Frontiers in neurology
Article Title: Inside the Thrombus: Association of Hemostatic Parameters With Outcomes in Large Vessel Stroke Patients.
doi: 10.3389/fneur.2021.599498
Figure Lengend Snippet: FIGURE 3 | Matrix metalloproteinase-10 (MMP-10) and thrombin-activatable fibrinolysis inhibitor (TAFI) colocalize with inflammatory cells and platelets in thrombi. Double immunofluorescence for MMP-10 (top, red) and TAFI (bottom, red) and leukocytes (CD45, left), macrophages CD68 (middle), and platelets CD42b (right, green); cell nuclei are stained with 4′,6-diamidino-2-phenylindole (DAPI) (blue). Arrow heads point to double positive cells for MMP-10 (upper panels) and TAFI (lower panels) and the specified antigens (yellow). Scale = 20 µm.
Article Snippet: Finally, slides were mounted with
Techniques: Staining
Journal: Frontiers in neurology
Article Title: Inside the Thrombus: Association of Hemostatic Parameters With Outcomes in Large Vessel Stroke Patients.
doi: 10.3389/fneur.2021.599498
Figure Lengend Snippet: FIGURE 4 | Matrix metalloproteinase-10 (MMP-10) and thrombin-activatable fibrinolysis inhibitor (TAFI) colocalization in thrombi. Immunofluorescence for TAFI (red), MMP-10 (green), and 4′,6-diamidino-2-phenylindole (DAPI) (blue). Arrow heads point to double positive cells for MMP-10 and TAFI. Scale = 20 and 10 µm.
Article Snippet: Finally, slides were mounted with
Techniques:
Journal: Food Chemistry: Molecular Sciences
Article Title: Semi-rational engineering of an α-L-fucosidase for regioselective synthesis of fucosyl-N-acetylglucosamine disaccharides
doi: 10.1016/j.fochms.2025.100244
Figure Lengend Snippet: Fig. 4. Analysis of transglycosylation product by HPLC. Control, reaction containing pNPαFuc, GlcNAc, and inactivated BF3242. The retention times of standard Fuc-α-1,3-GlcNAc and Fuc-α-1,6-GlcNAc were 27 and 38 min, respectively.
Article Snippet: We purchased
Techniques: Control
Journal: Food Chemistry: Molecular Sciences
Article Title: Semi-rational engineering of an α-L-fucosidase for regioselective synthesis of fucosyl-N-acetylglucosamine disaccharides
doi: 10.1016/j.fochms.2025.100244
Figure Lengend Snippet: Fig. 2. Docking models of mutant L266H with Fuc-α-1,3-GlcNAc. Putative 3D structure of mutant L266H docking with Fuc-α-1,3-GlcNAc. Homology modeling of mutant L266H was performed using SWISS-MODEL (https://swiss model.expasy.org/interactive), and the 3D structure of fucosidase BtFuc2970 (PDB entry 4WSJ) from Bacteroides thetaiotaomicron ATCC 29148 served as the template. Catalytic nucleophile residue was shown in red. The distance between the catalytic nucleophile residue (D206) and the anomeric centre (C1) of Fuc was 4.8 Å. The aglycone subsites were around the GlcNAc segment. The highest efficiency site, M285, is shown in yellow. (For interpretation of the references to colour in this figure legend, the reader is referred to the web version of this article.)
Article Snippet: We purchased
Techniques: Mutagenesis, Residue
Journal: Food Chemistry: Molecular Sciences
Article Title: Semi-rational engineering of an α-L-fucosidase for regioselective synthesis of fucosyl-N-acetylglucosamine disaccharides
doi: 10.1016/j.fochms.2025.100244
Figure Lengend Snippet: Fig. 6. The distances between the nucleophile residue D206 and Fuc-α-1,3/1,6- GlcNAc in WT BF3242 (a) and mutant L266H/M285T (b) at 323 K. The mini mum distance between the nucleophilic catalytic residue D206 and the ligand was calculated using the gmx_mindist tool.
Article Snippet: We purchased
Techniques: Residue, Mutagenesis