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Alessandra Rinna

Researcher at University of California, Merced

Publications -  11
Citations -  2871

Alessandra Rinna is an academic researcher from University of California, Merced. The author has contributed to research in topics: 4-Hydroxynonenal & Glutathione. The author has an hindex of 11, co-authored 11 publications receiving 2279 citations. Previous affiliations of Alessandra Rinna include University of Messina.

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Glutathione: overview of its protective roles, measurement, and biosynthesis.

TL;DR: The purpose here is to provide a brief overview of some of the important aspects of glutathione metabolism as part of this special issue that will provide a more comprehensive review of the state of knowledge regarding this essential molecule.
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ATP Activates a Reactive Oxygen Species-dependent Oxidative Stress Response and Secretion of Proinflammatory Cytokines in Macrophages

TL;DR: An increase in ROS levels in ATP-treated macrophages results in activation of a single pathway that promotes both adaptation to subsequent exposure to oxidants or inflammation, and processing and secretion of proinflammatory cytokines.
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The chemistry of cell signaling by reactive oxygen and nitrogen species and 4-hydroxynonenal

TL;DR: This article focuses on the chemistry of signaling by ROS, RNS, and HNE and will describe reactions with selected target proteins as representatives of the mechanisms rather attempt to comprehensively review the many signaling pathways in which the reactive species are involved.
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Stimulation of the alveolar macrophage respiratory burst by ADP causes selective glutathionylation of protein tyrosine phosphatase 1B

TL;DR: It is demonstrated that physiological stimulation of H(2)O(2), produced through the ADP-stimulated respiratory burst, results in PTP1B glutathionylation in intact cells, which may affect downstream signaling.
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Multidrug-resistant protein-3 gene regulation by the transcription factor Nrf2 in human bronchial epithelial and non-small-cell lung carcinoma.

TL;DR: The hypothesis that MRP3 induction by HNE involves Nrf2 activation is supported, as the presence of multiple putative electrophile-responsive elements suggests possible regulation of this gene by NRF2, the key transcription factor that binds to EpRE.