Hyperuricaemia, Xanthine Oxidoreductase and Ribosome-Inactivating Proteins from Plants: The Contributions of Fiorenzo Stirpe to Frontline Research

The enzymes called ribosome-inactivating proteins (RIPs) that are able to depurinate nucleic acids and arrest vital cellular functions, including protein synthesis, are still a frontline research field, mostly because of their promising medical applications. The contributions of Stirpe to the develo...

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Autores principales: Bolognesi, Andrea, Bortolotti, Massimo, Battelli, Maria Giulia, Polito, Letizia
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2017
Materias:
Review
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6155646/
https://www.ncbi.nlm.nih.gov/pubmed/28134797
http://dx.doi.org/10.3390/molecules22020206
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author Bolognesi, Andrea
Bortolotti, Massimo
Battelli, Maria Giulia
Polito, Letizia
author_facet Bolognesi, Andrea
Bortolotti, Massimo
Battelli, Maria Giulia
Polito, Letizia
author_sort Bolognesi, Andrea
collection PubMed
description The enzymes called ribosome-inactivating proteins (RIPs) that are able to depurinate nucleic acids and arrest vital cellular functions, including protein synthesis, are still a frontline research field, mostly because of their promising medical applications. The contributions of Stirpe to the development of these studies has been one of the most relevant. After a short biographical introduction, an overview is offered of the main results obtained by his investigations during last 55 years on his main research lines: hyperuricaemia, xanthine oxidoreductase and RIPs.
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spelling pubmed-61556462018-11-13 Hyperuricaemia, Xanthine Oxidoreductase and Ribosome-Inactivating Proteins from Plants: The Contributions of Fiorenzo Stirpe to Frontline Research Bolognesi, Andrea Bortolotti, Massimo Battelli, Maria Giulia Polito, Letizia Molecules Review The enzymes called ribosome-inactivating proteins (RIPs) that are able to depurinate nucleic acids and arrest vital cellular functions, including protein synthesis, are still a frontline research field, mostly because of their promising medical applications. The contributions of Stirpe to the development of these studies has been one of the most relevant. After a short biographical introduction, an overview is offered of the main results obtained by his investigations during last 55 years on his main research lines: hyperuricaemia, xanthine oxidoreductase and RIPs. MDPI 2017-01-27 /pmc/articles/PMC6155646/ /pubmed/28134797 http://dx.doi.org/10.3390/molecules22020206 Text en © 2017 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Review
Bolognesi, Andrea
Bortolotti, Massimo
Battelli, Maria Giulia
Polito, Letizia
Hyperuricaemia, Xanthine Oxidoreductase and Ribosome-Inactivating Proteins from Plants: The Contributions of Fiorenzo Stirpe to Frontline Research
title Hyperuricaemia, Xanthine Oxidoreductase and Ribosome-Inactivating Proteins from Plants: The Contributions of Fiorenzo Stirpe to Frontline Research
title_full Hyperuricaemia, Xanthine Oxidoreductase and Ribosome-Inactivating Proteins from Plants: The Contributions of Fiorenzo Stirpe to Frontline Research
title_fullStr Hyperuricaemia, Xanthine Oxidoreductase and Ribosome-Inactivating Proteins from Plants: The Contributions of Fiorenzo Stirpe to Frontline Research
title_full_unstemmed Hyperuricaemia, Xanthine Oxidoreductase and Ribosome-Inactivating Proteins from Plants: The Contributions of Fiorenzo Stirpe to Frontline Research
title_short Hyperuricaemia, Xanthine Oxidoreductase and Ribosome-Inactivating Proteins from Plants: The Contributions of Fiorenzo Stirpe to Frontline Research
title_sort hyperuricaemia, xanthine oxidoreductase and ribosome-inactivating proteins from plants: the contributions of fiorenzo stirpe to frontline research
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6155646/
https://www.ncbi.nlm.nih.gov/pubmed/28134797
http://dx.doi.org/10.3390/molecules22020206
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