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| http://dx.doi.org/10.1073/pnas.24.6.229 | DOI Listing |
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Protein prenylation in mechanotransduction: implications for disease and therapy.
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Department of Cardiology, The First Affiliated Hospital, Zhejiang University School of Medicine, Hangzhou 310003, China. Electronic address:
The process by which cells translate external mechanical cues into intracellular biochemical signals involves intricate mechanisms that remain unclear. In recent years, research into post-translational modifications (PTMs) has offered valuable insights into this field, spotlighting protein prenylation as a crucial mechanism in cellular mechanotransduction and various human diseases. Protein prenylation, which involves the covalent attachment of isoprenoid groups to specific substrate proteins, profoundly affects the functions of key mechanotransduction proteins such as Rho, Ras, and lamins.
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Department of Cardiology, The Second Affiliated Hospital, Jiangxi Medical College, Nanchang University, No. 1 Minde Road, Nanchang, Jiangxi Province 330006, China. Electronic address:
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In the past few years, three protein molecules-USP53, NPY2R, and DCTN1-AS1-have garnered significant attention in scientific research due to their potential implications in tumor development. Mass spectrometry and proteomics techniques were used to analyze the three-dimensional structure of these protein molecules and predict their active sites and functional domains. The effects of USP53, NPY2R and DCTN1-AS1 on biological behavior of tumor cells were studied by constructing gene knockout and overexpression cell models.
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Department of Urology, the Second Affiliated Hospital of Anhui Medical University, Hefei 230601, China; Department of Urology, Chaohu Hospital of Anhui Medical University, Chaohu 238000, China. Electronic address:
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