Dr. Bazzaro is a Tenured Associate Professor in the Department of Department of Obstetrics, Gynecology and Women's Health and Masonic Cancer Center at the University of Minnesota. She earned a Ph.D. in Medicinal Chemistry from the Department of Pharmaceutical Science of the University of Ferrara, Italy.
Dr. Bazzaro served as guest researcher at the "Institut de Biochemie" in Lausanne, Switzerland and at the Karolinska Institute in Stockholm, Sweden.
She competed her postdoctoral training at the Department of Pathology of the Johns Hopkins Hospital.Dr. Bazzaro is an Italian citizen, U.S.A permanent resident and speaks English, French, Spanish, and Italian.
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Dr. Bazzaro has a lifelong research interest in cervical and ovarian cancer. She combines her expertise in both the biology of ovarian cancer and pharmaceutical chemistry for the discovery of personalized medicine for women affected by cervical and ovarian cancer for which conventional chemotherapy is not a satisfactory option.
Dr. Bazzaro's has ongoing research collaboration with several institutions and hospitals, nationally and internationally.
Mayo Clinic in Rochester, MN
Johns Hopkins Hospital in Baltimore, MD
University of Alabama in Birmingham, AL
University of Ferrara, Italy
University of Linkoping, Sweden
Microtubule dynamics in the context of cancer and neurodegeneration
Personalized therapies for ovarian cancer resistant to conventional chemotherapy treatment
Combinatorial chemotherapic treatment for ovarian cancer
Targeting of metabolic pathways for ovarian and cancer treatment
Role of Natural Killer (NK) cell in ovarian cancer
Study of the mechanisms underlying breast and ovarian cancer development and progression
Dr. Bazzaro's laboratory is interested in studying abnormalities of protein degradation pathways in breast and ovarian cancer. The Ubiquitin-Proteasome-System (UPS) is responsible for degradation of over 90% of short-lived intracellular proteins. Protein degradation through Ubiquitin-Proteasome-System is a multistep process that begins with de-ubiquitination of ubiquitin-tagged target molecules by de-ubiquitinating enzymes following their entrance in the 20S catalytic chamber of the proteasomes were the actual degradation occurs. The polypeptide targets of the proteasome include proteins involved in cell cycle progression, survival and inflammation and while the ubiquitin-dependent proteasomal degradation is crucial for both normal and malignant cells the higher demand for metabolic/catabolic activity associated with the malignant phenotype renders the ubiquitin-proteasome pathway a suitable tool for cancer treatment. The laboratory is particularly interested in studying the role played by proteasomal- and lysosomal-assisted protein degradation pathways during the development and the progression of breast and ovarian cancer and in the development of new small-molecules inhibitors of ubiquitin-proteasome-system for targeting breast and ovarian cancer cells.