| Literature DB >> 15389864 |
Isabella Dalle-Donne1, Andrea Scaloni, Daniela Giustarini, Eleonora Cavarra, Gianluca Tell, Giuseppe Lungarella, Roberto Colombo, Ranieri Rossi, Aldo Milzani.
Abstract
Reactive oxygen species (ROS) and reactive nitrogen species (RNS) contribute to the pathogenesis and/or progression of several human diseases. Proteins are important molecular signposts of oxidative/nitrosative damage. However, it is generally unresolved whether the presence of oxidatively/nitrosatively modified proteins has a causal role or simply reflects secondary epiphenomena. Only direct identification and characterization of the modified protein(s) in a given pathophysiological condition can decipher the potential roles played by ROS/RNS-induced protein modifications. During the last few years, mass spectrometry (MS)-based technologies have contributed in a significant way to foster a better understanding of disease processes. The study of oxidative/nitrosative modifications, investigated by redox proteomics, is contributing to establish a relationship between pathological hallmarks of disease and protein structural and functional abnormalities. MS-based technologies promise a contribution in a new era of molecular medicine, especially in the discovery of diagnostic biomarkers of oxidative/nitrosative stress, enabling early detection of diseases. Indeed, identification and characterization of oxidatively/nitrosatively modified proteins in human diseases has just begun. 2004 Wiley Periodicals, Inc.Entities:
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Year: 2005 PMID: 15389864 DOI: 10.1002/mas.20006
Source DB: PubMed Journal: Mass Spectrom Rev ISSN: 0277-7037 Impact factor: 10.946