Search

Non-imaging radar can achieve the detection and localization of moving targets, but it faces difficulties in the classification of targets. Aiming for the application of moving target classification by low/medium resolution non-imaging radar, this paper proposes a novel feature extraction method, based on the statistical characteristics of echo amplitude with the L-band fully polarimetric radar. A feature plane, composed of the 3rd-order central moment (skewness) and 4th-order central moment (kurtosis) as the statistical characteristics of the echo envelope, is established. In addition, two types of moving targets, pedestrians and non-motorized vehicles, are able to be effectively distinguished according to whether the echo signals of different polarizations have overlapping areas in the feature plane. The L-band fully polarimetric radar has been developed and field experiments have been conducted. The experimental results verify that the kurtosis and skewness of the fully polarimetric echo amplitude of the pedestrians are very close, and there is an overlapping area in the feature plane, while the statistical characteristics of the fully polarimetric echo signal of non-motor vehicles are different, and there is no overlapping area in the feature plane. This proposed feature extraction method has the advantage of being simple and robust, compared to the traditional imaging approach. [ABSTRACT FROM AUTHOR]

N- linked glycosylation is a common posttranslational modification of proteins that results in macroheterogeneity of the modification site. However, unlike simpler modifications, N- glycosylation introduces an additional layer of complexity with tens of thousands of possible structures arising from various dimensions, including different monosaccharide compositions, sequence structures, linking structures, isomerism, and three-dimensional conformations. This results in additional microheterogeneity of the modification site of N- glycosylation, i.e., the same N- glycosylation site can be modified with different glycans with a certain stoichiometric ratio. N- glycosylation regulates the structure and function of N- glycoproteins in a site- and structure-specific manner, and differential expression of N- glycosylation under disease conditions needs to be characterized through site- and structure-specific quantitative analysis. Numerous advanced methods ranging from sample preparation to mass spectrum analysis have been developed to distinguish N-glycan structures. Chemical derivatization of monosaccharides, online liquid chromatography separation and ion mobility spectrometry enable the physical differentiation of samples. Tandem mass spectrometry further analyzes the macro/microheterogeneity of intact N- glycopeptides through the analysis of fragment ions. Moreover, the development of search engines and AI-based software has enhanced our understanding of the dissociation patterns of intact N- glycopeptides and the clinical significance of differentially expressed intact N- glycopeptides. With the help of these modern methods, structure-specific N- glycoproteomics has become an important tool with extensive applications in the biomedical field.

O-linked β-N-acetylglucosaminylation (O-GlcNAcylation) is a highly dynamic and widespread post-translational modification (PTM) that regulates the activity, subcellular localization, and stability of target proteins. O-GlcNAcylation is a reversible PTM controlled by two cycling enzymes: O-linked N-acetylglucosamine transferase and O-GlcNAcase. Emerging evidence indicates that O-GlcNAcylation plays critical roles in innate immunity, inflammatory signaling, and cancer development. O-GlcNAcylation usually occurs on serine/threonine residues, where it interacts with other PTMs, such as phosphorylation. Thus, it likely has a broad regulatory scope. This review discusses the recent research advances regarding the regulatory roles of O-GlcNAcylation in innate immunity and inflammation. A more comprehensive understanding of O-GlcNAcylation could help to optimize therapeutic strategies regarding inflammatory diseases and cancer., (© The Author(s) (2022). Published by Oxford University Press on behalf of Journal of Molecular Cell Biology, CEMCS, CAS.)