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Monosodium glutamate (MSG) is widely used as food additive and flavor enhancer; however, consumption of high dose of MSG provokes oxidative stress in many organs and its safety and side effects on the body are still controversial. Therefore, it is crucial to investigate the long-lasting effects of MSG on cardiac muscle functions and structure. Forty male Wister albino rats were assigned into 3 groups. Control group was injected intraperitoneally with physiological saline for 7&nbsp;days. Second group was injected intraperitoneally with MSG at a dose of 4&nbsp;mg/g b.w/day for 7 consecutive days and then kept without any treatment till 45th day of the experiment. Third group was injected intraperitoneally with MSG at a dose of 6&nbsp;mg/g b.w/day for 7 consecutive days and then kept without any treatment till 45th day of the experiment. Monosodium glutamate significantly reduced body weight, force of cardiac muscle contractility, serum level of high-density lipoprotein, and superoxide dismutase activity in cardiac muscle, while it significantly elevated heart rate, serum levels of total cholesterol, low-density lipoprotein, triacylglycerides, atherogenic index and troponin T, activities of serum lactate dehydrogenase and creatine kinase-MB, malondialdehyde concentration, and P53 protein expression in cardiac muscle. In addition, it induced myocardial degeneration, cellular infiltration, deposition of collagen in cardiac muscle, and periodic acid-Schiff staining reaction. This study indicated that MSG exerted long-lasting functional and structural alterations in the heart of male albino rats through induction of oxidative stress, atherogenesis, and apoptosis.Inhibition of immune checkpoint receptor Programmed Death-1 (PD-1) via monoclonal antibodies is an established anticancer immunotherapeutic approach. This treatment has been largely successful; however, its high cost demands equally effective, more affordable alternatives. To date, the development of drugs targeting downstream players in the PD-1-dependent signaling pathway has been hampered by our poor understanding of the molecular details of the intermolecular interactions involved in the pathway. Activation of PD-1 leads to phosphorylation of two signaling motifs located in its cytoplasmic domain, the immune tyrosine inhibitory motif (ITIM) and immune tyrosine switch motif (ITSM), which recruit and activate protein tyrosine phosphatase SHP2. This interaction is mediated by the two Src homology 2 (SH2) domains of SHP2, termed N-SH2 and C-SH2, which recognize phosphotyrosines pY223 and pY248 of ITIM and ITSM, respectively. SHP2 then propagates the inhibitory signal, ultimately leading to suppression of T cell functionality. In order to facilitate mechanistic structural studies of this signaling pathway, we report the resonance assignments of the complexes formed by the signaling motifs of PD-1 and the SH2 domains of SHP2.Human neuron-specific PACSIN1 plays a key role in synaptic vesicle recycling and endocytosis, as well as reorganization of the microtubule dynamics to maintain axonal plasticity. PACSIN1 contains a highly conserved C-terminal SH3 domain and an F-bar domain at its N-terminus. Due to its remarkable interaction network, PACSIN1 plays a central role in key neuronal functions. Here, we present a robust backbone and side-chain assignment of PACSIN1 SH3 domain based on 2D [1H,15N] HSQC or HMQC, and 3D BEST-HNCO, -HNCACB, -HN(CO)CACB, -HN(CA)CO, and standard (H)CC(CO)NH, HN(CA)NNH, HN(COCA)NH, HBHANNH, HNHA, HBHA(CO)NH, H(CC)(CO)NH, HCCH-TOCSY, that covers 96% for all 13CO, 13Cα and 13Cβ, 28% of 13Cγδε, and 95% of 1HN and 15N chemical shifts. Modelling based on sequence homology with a known related structure, and chemical shift-based secondary structure predictions, identified the presence of five β-strands linked by flexible loops. Taken together, these results open up new avenues to investigate and develop new therapeutic strategies.In recent years, with the development of molecular imprinting technology, the imprinting sites, nature of imprinting, selection of functional monomers, cross-linking agents, solvents, and the optimization of the imprinting ratio are all the hot spots of researchers. In this work, the theoretical prediction of the self-assembly system of formaldehyde (HCHO) molecularly imprinted polymer was carried out by the B3LYP/6-31 G(d,p) method. The geometric configuration and active sites of the stable complex of HCHO and methacrylic acid (MAA) were analyzed. The selection of the imprinting ratios, cross-linking agents, and solvents was discussed. The topological properties of electron density of HCHO-MAA complex were considered by using the topological analysis method of chemical bond electron density based on valence bond theory. This study cannot only reveal the relationship between the imprinting mechanism of molecularly imprinted polymers and the molecular structure and properties of molecularly imprinted polymers but also provide valuable reference for the design and preparation of molecularly imprinted polymers.Over the past decade, global interest in the development of therapeutic monoclonal antibodies (mAbs) has risen rapidly. As therapeutic agents, antibodies have shown marked efficacy in combatting a range of cancers and immune diseases with high target specificity and low toxicity (Carla Lucia et al. in PLoS ONE 6e24071, 2011; Donaghy in MAbs 8659-671, 2016; Nasiri et al. in J Cell Physiol 96441-6457, 2018; Teo et al. in Cancer Immunol Immunother 612295-2309, 2012). Recent advances in cell culture technology, such as high-throughput clone screening, have facilitated antibody production at concentrations exceeding 10 g/L (Chen et al. [https://www.selleckchem.com/products/caspofungin-acetate.html L-743872] in BMC Immunol 1935, 2018; Huang et al. in Biotechnol Prog 261400-1410, 2010; Lu et al. in Biotechnol Bioeng 110191-205, 2013; Singh et al. in Biotechnol Bioeng 113698-716, 2016). As titers have improved, the industry has begun to focus on the adjustment of target antibody quality profiles to improve efficacy. Cell lines, culture media, and culture conditions impact protein quality nt loss of titer. This study provided supporting evidence for methods to improve charge variants arising during mAb production.