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oapen-20.500.12657-864752024-01-09T02:10:04Z Chapter 8 Research Strategies for Investigating Protein Ubiquitination in Lung Diseases Zhao, Yutong asthma; cystic fibrosis; gas exchange; homeostasis; inflammation; lung diseas; lung endothelium;stem cells bic Book Industry Communication::M Medicine::MJ Clinical & internal medicine::MJC Diseases & disorders::MJCM Immunology bic Book Industry Communication::M Medicine::MJ Clinical & internal medicine bic Book Industry Communication::P Mathematics & science::PS Biology, life sciences::PSD Molecular biology bic Book Industry Communication::P Mathematics & science::PS Biology, life sciences::PSF Cellular biology (cytology) bic Book Industry Communication::P Mathematics & science::PS Biology, life sciences ch. 8 Post-translational modification (PTMs) determines protein’s cellular functions including enzyme activity, localization, protein-protein interaction, and protein stability. Ubiquitin is a 7-kDa protein. Ubiquitination is one of PTMs and it is defined as protein covalently conjugation with a ubiquitin or poly-ubiquitin chains. A series of enzymatic reactions catalyze protein ubiquitination, which can be reversed by deubiquitinating enzymes (DUBs). The abnormal expression of ubiquitination-related enzymes and ubiquitination in lung cells have been demonstrated to alter cell functions, such as cell proliferation, death, and differentiation, ultimately contribute to the pathogenesis of lung diseases. In this chapter, we will introduce the methodology and research strategies for investigating protein ubiquitination in lung cells and experimental lung diseases. Common practice and edge-cutting laboratory technologies will be introduced in the chapter. Finally, we will discuss new drug development by targeting ubiquitination for therapies. 2024-01-08T12:38:07Z 2024-01-08T12:38:07Z 2024 chapter 9781032409023 9781032409061 https://library.oapen.org/handle/20.500.12657/86475 eng application/pdf Attribution-NonCommercial-NoDerivatives 4.0 International 9781003355243_10.1201_9781003355243-10.pdf Taylor & Francis Lung Biology and Pathophysiology CRC Press 10.1201/9781003355243-10 10.1201/9781003355243-10 7b3c7b10-5b1e-40b3-860e-c6dd5197f0bb f5c4fc45-bde3-45c9-82c5-5cd16b06ef43 4cc73c4d-ecdc-4788-a75c-f1eed7ff1852 9781032409023 9781032409061 CRC Press 13 Ohio State University Foundation open access
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ch. 8 Post-translational modification (PTMs) determines protein’s cellular functions including enzyme activity, localization, protein-protein interaction, and protein stability. Ubiquitin is a 7-kDa protein. Ubiquitination is one of PTMs and it is defined as protein covalently conjugation with a ubiquitin or poly-ubiquitin chains. A series of enzymatic reactions catalyze protein ubiquitination, which can be reversed by deubiquitinating enzymes (DUBs). The abnormal expression of ubiquitination-related enzymes and ubiquitination in lung cells have been demonstrated to alter cell functions, such as cell proliferation, death, and differentiation, ultimately contribute to the pathogenesis of lung diseases. In this chapter, we will introduce the methodology and research strategies for investigating protein ubiquitination in lung cells and experimental lung diseases. Common practice and edge-cutting laboratory technologies will be introduced in the chapter. Finally, we will discuss new drug development by targeting ubiquitination for therapies.
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Taylor & Francis
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2024
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1799945190230720512
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