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个人简介
Dr. Maurizi conducted seminal studies uncovering the presence and importance of multi-component ATP-dependent proteases in bacterial cells. His biochemical and structural studies of Clp protease complexes helped generate current models of the mechanism by which these and other molecular machines recognize, unfold, and degrade intracellular proteins. Current research is focused on N-end rule degradation as a major pathway for cellular protein quality control. As Head of the Biochemistry of Proteins Section Dr. Maurizi directed a multi-disciplinary research program that combined genetics, biochemistry, and high-resolution structural analysis to study the regulatory pathways in which intracellular proteolysis plays a major role and the properties and behavior of the molecular machines that carry out ATP-dependent proteolysis.
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Journal of Biological Chemistryno. 40 (2013): 28913-28924
HANDBOOK OF PROTEOLYTIC ENZYMES, VOLS 1 AND 2, 3RD EDITIONpp.3600-3605, (2013)
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