NMDA Receptor Glycine Binding Site Modulators for Prevention and Treatment of Ketamine Use Disorder by Yu-Chin Hsiao, Mei-Yi Lee, Ming-Huan Chan, Hwei-Hsien Chen

Subjects: “…D-serine…”
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Phosphatidylethanolamine homeostasis under conditions of impaired CDP-ethanolamine pathway or phosphatidylserine decarboxylation by Michaela St Germain, Roya Iraji, Marica Bakovic

Subjects: “…serine…”
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Dipeptidyl peptidase IV and its implication in cancer by Yarini M Arrebola, Hansel Gómez, Pedro A Valiente, Maria de los A Chávez, Isel Pascual

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Crystal Structure of Bovine Alpha-Chymotrypsin in Space Group P6₅ by Andrew C. Marshall, Benjamin G. Keiller, Jordan L. Pederick, Andrew D. Abell, John B. Bruning

Subjects: “…trypsin-like serine protease…”
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EXTRACTION, PURIFICATION AND CHARACTERIZATION OF ELASTASE FROM THE DIGESTIVE DUCT OF CATFISH (SILURUS TRIOSTEGUS) by A. M. Kadhim, K. A. Shakir

Subjects: “…fish elastase . serine proteinase. size exclusion.…”
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Simultaneous suppression of PKM2 and PHGDH elicits synergistic anti-cancer effect in NSCLC by Kaixuan Wang, Hao Lu, Xinmiao Wang, Qingxia Liu, Jinxia Hu, Yao Liu, Yao Liu, Meihua Jin, Dexin Kong

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RECURRENT OF TMPRSS2 GENETIC POLYMORPHISM AND ITS ROLE IN IRAQI PATIENTS WITH PROSTATE CANCER by Ammar K. A., M. F. Altaee

Subjects: “…genotype, transmembrane protease serine 2, SNP.…”
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Structural and functional studies on human complement factor I by Tsiftsoglou, S, Stefanos Alex Tsiftsoglou

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Comparative Phenotypic, Proteomic, and Phosphoproteomic Analysis Reveals Different Roles of Serine/Threonine Phosphatase and Kinase in the Growth, Cell Division, and Pathogenicity of <i>Streptococcus suis</i> by Qiao Hu, Lun Yao, Xia Liao, Liang-Sheng Zhang, Hao-Tian Li, Ting-Ting Li, Qing-Gen Jiang, Mei-Fang Tan, Lu Li, Roger R. Draheim, Qi Huang, Rui Zhou

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Nattokinase (Bac s 1), a subtilisin family serine protease, is a novel allergen contained in the traditional Japanese fermented food natto by Kayoko Suzuki, Masashi Nakamura, Nayu Sato, Kyoko Futamura, Kayoko Matsunaga, Akiko Yagami

“…Conclusions: We identified a subtilisin family serine protease, nattokinase, as a novel allergen in natto allergy patients unsensitized to PGA.…”
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The accumulation of modular serine protease mediated by a novel circRNA sponging miRNA increases Aedes aegypti immunity to fungus by Tengfei Lu, Yannan Ji, Mengmeng Chang, Xiaoming Zhang, Yanhong Wang, Zhen Zou

“…Results We found a microRNA (miRNA) that can modulate the antifungal immunity of Aedes aegypti by inhibiting its cognate serine protease. Fungal infection can induce the expression of modular serine protease (ModSP), and ModSP knockdown mosquitoes were more sensitive to B. bassiana infection. …”
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The Serine Carboxypeptidase-Like Gene <i>SCPL41</i> Negatively Regulates Membrane Lipid Metabolism in <i>Arabidopsis thaliana</i> by Juan Chen, Wei-qi Li, Yan-xia Jia

Subjects: “…serine carboxypeptidase-like protein…”
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A Sub-Group of Kidney-Transplant Recipients with Highly Aggressive Squamous Cell Carcinoma Expressing Phosphorylated Serine392p53 by Diaddin Hamdan, Charlotte Gardair, Frédéric Pamoukdjian, Marie-Noëlle Peraldi Gardin, Inès Nakouri, Christophe Leboeuf, Anne Janin, Céleste Lebbé, Maxime Battistella, Guilhem Bousquet

“…Here, we investigated the phosphorylation status of p53 at Serine 392 in 25 cutaneous squamous cell carcinomas in kidney-transplant recipients, compared with 22 non-transplanted patients. …”
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<i>Campylobacter jejuni</i> Serine Protease HtrA Induces Paracellular Transmigration of Microbiota across Polarized Intestinal Epithelial Cells by Irshad Sharafutdinov, Nicole Tegtmeyer, Mathias Müsken, Steffen Backert

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Phosphoribosyl-linked serine ubiquitination of USP14 by the SidE family effectors of Legionella excludes p62 from the bacterial phagosome by Jinli Ge, Ying Wang, Xindi Chen, Kaiwen Yu, Zhao-Qing Luo, Xiaoyun Liu, Jiazhang Qiu

“…In the present study, we demonstrate that the host DUB USP14 is PR-ubiquitinated by SidEs at multiple serine residues, which impairs its DUB activity and its interactions with p62. …”
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Substrate specificity of branched chain amino acid aminotransferases: The substitution of glycine to serine in the active site determines the substrate specificity for α-ketoglutarate by Jan-Moritz Sutter, Daniel E. Mitchell, Marcel Schmidt, Michail N. Isupov, Jennifer A. Littlechild, Peter Schönheit

“…Examination of the active sites of the two related enzymes reveals a single amino acid substitution of a glycine residue to a serine residue which could be responsible for this difference. …”
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Proline/serine‐rich coiled‐coil protein 1 inhibits macrophage inflammation and delays atherosclerotic progression by binding to Annexin A2 by Hangyu Pan, Zhongzhou Guo, Ping Lv, Kexin Hu, Tongwei Wu, Zixiang Lin, Yazhi Xue, Yanan Zhang, Zhigang Guo

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Stabilization of the c-Myc Protein via the Modulation of Threonine 58 and Serine 62 Phosphorylation by the Disulfiram/Copper Complex in Oral Cancer Cells by Gunng-Shinng Chen, Ssu-Yu Chen, Shu-Ting Liu, Cheng-Chih Hsieh, Shiao-Pieng Lee, Shih-Ming Huang

“…Our previous study showed that the levels of c-Myc protein and the phosphorylation of threonine 58 (T58) and serine 62 (S62) increased in DSF-Cu-complex-treated oral epidermoid carcinoma Meng-1 (OECM-1) cells. …”
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Mapping of a N-terminal α-helix domain required for human PINK1 stabilization, Serine228 autophosphorylation and activation in cells by Poonam Kakade, Hina Ojha, Olawale G. Raimi, Andrew Shaw, Andrew D. Waddell, James R. Ault, Sophie Burel, Kathrin Brockmann, Atul Kumar, Mohd Syed Ahangar, Ewelina M. Krysztofinska, Thomas Macartney, Richard Bayliss, Julia C. Fitzgerald, Miratul M. K. Muqit

“…Q126P), located within the NTE : CTE interface, markedly inhibit stabilization of PINK1; autophosphorylation at Serine228 (Ser228) and Ubiquitin Serine65 (Ser65) phosphorylation. …”
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MECP2 Increases the Pro-Inflammatory Response of Microglial Cells and Phosphorylation at Serine 423 Regulates Neuronal Gene Expression upon Neuroinflammation by Rebekka Wittrahm, Mari Takalo, Mikael Marttinen, Teemu Kuulasmaa, Petra Mäkinen, Susanna Kemppainen, Henna Martiskainen, Tuomas Rauramaa, Ian Pike, Ville Leinonen, Teemu Natunen, Annakaisa Haapasalo, Mikko Hiltunen

“…The effects of wild type and phosphorylation-deficient MECP2 variants at serine 423 (S423) or S80 on microglial and neuronal function were assessed utilizing BV2 microglial monocultures and co-cultures with mouse cortical neurons under inflammatory stress conditions. …”
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