
Valentina Rossio
Articles
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Jan 8, 2025 |
mdpi.com | Valentina Rossio |João Paulo
1. IntroductionFirst synthesized in 1891, bisphenol A (BPA), or 4,40-dihydroxy-2,2-diphenylpropane, has become a central component of modern industrial chemistry. BPA is widely used, particularly in the production of plastics, and it is present in everyday items such as food packaging, baby bottles, toys, and electronics [,].
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Nov 5, 2024 |
mdpi.com | Valentina Rossio |Xinyue Liu |João Paulo
All articles published by MDPI are made immediately available worldwide under an open access license. No special permission is required to reuse all or part of the article published by MDPI, including figures and tables. For articles published under an open access Creative Common CC BY license, any part of the article may be reused without permission provided that the original article is clearly cited. For more information, please refer to https://www.mdpi.com/openaccess.
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Oct 30, 2024 |
mdpi.com | Valentina Rossio |João Paulo
All articles published by MDPI are made immediately available worldwide under an open access license. No special permission is required to reuse all or part of the article published by MDPI, including figures and tables. For articles published under an open access Creative Common CC BY license, any part of the article may be reused without permission provided that the original article is clearly cited. For more information, please refer to https://www.mdpi.com/openaccess.
Specificity profiling of deubiquitylases against endogenously generated ubiquitin-protein conjugates
May 28, 2024 |
cell.com | Valentina Rossio |João Paulo |Xinyue Liu |Steven Gygi
Deubiquitylating enzymes (DUBs) remove ubiquitin from proteins thereby regulating their stability or activity. Our understanding of DUB-substrate specificity is limited because DUBs are typically not compared to each other against many physiological substrates. By broadly inhibiting DUBs in Xenopus egg extract, we generated hundreds of ubiquitylated proteins and compared the ability of 30 DUBs to deubiquitylate them using quantitative proteomics.
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Dec 20, 2023 |
biorxiv.org | Valentina Rossio |João Paulo |Xinyue Liu |Steven Gygi
AbstractDeubiquitylating enzymes (DUBs) remove ubiquitin from proteins thereby regulating their stability or activity. Our understanding of DUB-substrate specificity is limited because DUBs are typically not compared to each other against many physiological substrates. By broadly inhibiting DUBs in Xenopus egg extract, we generated hundreds of ubiquitylated proteins and compared the ability of 30 DUBs to deubiquitylate them using quantitative proteomics.
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