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Background/purpose: Among the craniofacial structures, the mandible is the only bony structure with movable joints. Each part (including condyle process, coronoid process, and ramus) of mandible would interaction with the muscles and proceed different osteogenesis progress. The objective of this study was to evaluate the mandibles with symmetric and asymmetric skeletal Class III jaw relations by quantifying differences in the condyle process, coronoid process and ramus on CBCT (Cone-beam computer tomography) images. Our hypothesis was that CBCT would reveal no voluminal differences between deviated and non-deviated mandibular segments in asymmetric skeletal Class III. Materials and methods: CBCT imagines were collected from dental department, KMUH and then divided into symmetric Class III group (Menton deviation < 4mm) and asymmetric Class III group (Menton deviationâ§4mm). The mandibular structure would be segmented to ramus, condylar and coronoid process. Each volume was measured. Independent t test was used for comparison between groups, and paired t test was applied for comparison between both segmented parts within each group. Results: Significant differences between deviation and non-deviation sides in the asymmetric group were found in condylar and ramus segments for volumetric quantitative measurements. There has no significant difference in ramus parts between groups. Significant greater condylar volume was found in non-deviation side of asymmetric group. Conclusion: The results demonstrated that in the side with greater mandible growth potential, the condylar and the ramus volume would be greater as well. CBCT is a useful and accurate modality for quantification and evaluation of mandibular asymmetry.
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The purpose of this review is to provide updated information regarding bioinformatic software for the use in the characterization of glycosylated structures since 2013. A comprehensive review by Woodin et al.Analyst 138: 2793-2803, 2013 (ref. 1) described two main approaches that are introduced for starting researchers in this area; analysis of released glycans and the identification of glycopeptide in enzymatic digests, respectively. Complementary to that report, this review focuses on mass spectrometry related bioinformatics tools for the characterization of N-linked and O-linked glycopeptides. Specifically, it also provides information regarding automated tools that can be used for glycan profiling using mass spectrometry.
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The cytochrome P450 (P450, CYP) 2A6 inhibitor chalepensin was found to inhibit human CYP1A1, CYP1A2, CYP2A13, CYP2C9, CYP2D6, CYP2E1, and CYP3A4 to different extents. CYP1A1 and CYP3A4 underwent pronounced mechanism-based inactivation by chalepensin and had the smallest IC50 ratios of inhibition with NADPH-fortified pre-incubation (IC50(+)) to that without pre-incubation (IC50(-)). CYP2E1 had the least susceptibility to mechanism-based inactivation. This inactivation of CYP1A1 and CYP3A4 exhibited time-dependence, led to a loss of spectrophotometrically detected P450, and could not be fully recovered by dialysis. Pre-incubation with chalepensin did not affect NADPH-P450 reductase activity. Cytosol-supported glutathione conjugation protected CYP3A4 but not CYP1A1 against the inactivation by chalepensin. Cytosolic decomposition of chalepensin may contribute partially to the protection. The high epoxidation activities of CYP1A1, CYP2A6, and CYP3A4 were in agreement with their pronounced susceptibilities to mechanism-based inactivation by chalepensin. Considering both the IC50 values and inactivation kinetic parameters, the threshold concentrations of chalepensin for potential drug interactions through inhibition of CYP2A6 and CYP3A4 were estimated to be consistently low. These results demonstrate that chalepensin inhibits multiple P450s and that epoxidation activity is crucial for the potential drug interaction through mechanism-based inhibition.