Publications by authors named "Takanori Tabata"
Article Synopsis
- Certain influenza viruses require the cleavage of their hemagglutinin (HA) by host cell proteases to trigger infection, with different proteases acting on distinct HA motifs.
- The study focuses on the human protease MSPL, revealing its crystal structure in complex with a substrate-analog inhibitor, highlighting key interactions that facilitate its enzymatic function.
- Insights from MSPL's structure led to a model for another protease, TMPRSS2, which is crucial for activating the spike protein of SARS-CoV-2, potentially guiding the development of new COVID-19 treatments.
A series of indazole derivatives were identified as Sirt 1 activators though high-throughput screening. Optimization of each substituent on the indazole ring led to the identification of compound 13. Compound 13 appeared to give the best Sirt 1 activity of the compounds tested and also showed osteogenesis activity in a cell assay.
View Article and Find Full Text PDFThe products encoded by ski and its related gene, sno, (Ski and Sno) act as transcriptional co-repressors and interact with other co-repressors such as N-CoR/SMRT and mSin3A. Ski and Sno mediate transcriptional repression by various repressors, including Mad, Rb and Gli3. Ski/Sno also suppress transcription induced by multiple activators, such as Smads and c-Myb.
View Article and Find Full Text PDFWe have identified a novel nucleolar protein, PAP-1-associated protein-1 (PAPA-1), after screening the interacting proteins with Pim-1-associated protein-1 (PAP-1), a protein that is a phosphorylation target of Pim-1 kinase. PAPA-1 comprises 345 amino acids with a basic amino-acid cluster. PAPA-1 was found to be localized in the nucleolus in transfected HeLa cells, and the lysine/histidine cluster was essential for nucleolar localization of PAPA-1.
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