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Claudia Fiorillo graduated in Biological Sciences in 1992. In 1996 she attained the School of Specialization in Biochemistry and Clinical Biochemistry. In march 2000 she get the PhD. In september 2000 she was appointed University Researcher in Clinical Biochemistry (BIO12) at the University of Florence, Faculty of Medicine. Since 2003 she is Confirmed University Researcher. She teaches Clinical Biochemistry in the graduate Medical School, in the Postgraduate School of Clinical Biochemistry, in the Nurses School, in the Biology and in the Biotechnology Schools at the University of Florence. Since her graduation she has been devoted to research on the biochemistry of the heart in particular to the regulatory mechanisms for calcium homeostasis and contraction efficiency in cardiac muscle and to the molecular mechanisms of myocardial damage induced by ischemia-reperfusion. She is actively involved in the study of the molecular pathways evoked by oxidative stress in several disorders, in particular dermatologic diseases (vitiligo and psoriasis). Moreover she is interested in the study of the molecular basis of the toxicity of protein aggregates in various cell types. The post-translational modifications responsible for alterations in fibrinogen function represent another important and recent topic of interest. She partecipated to several research programs in particular to the Projects of Relevant National Interest "Insufficienza cardiaca (heart failure)", "Molecular and metabolic myocardial damages induced by post ischemic reperfusion and mechanisms of protection" and "Mechanisms of injury and protection in the ischemic myocardium". She is a member of the Società Italiana di Biochimica clinica e Biologia molecolare clinica (SIBioC), of the Società Italiana di Biochimica (SIB) and of the Società Italiana per lo studio dell\emostasi e della trombosi (SISET).
Redox signaling in dermatologic diseases (vitiligo and psoriasis)
Antioxidant protection in ischemic-reperfused myocardium
Alterations in fibrinogen function elicited by its post-translational oxidative modification
Mechanisms of toxicity of protein aggregates.
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