Saint Louis University

Education

Ph.D., 1995, University of Padua, Italy

Research Interests

Aberrant DNA replication is one of the leading causes of mutations and chromosome rearrangements associated with several cancer related pathologies, and several chemotherapeutic strategies employ agents that induce replication stress in the attempt to selectively target highly proliferating cancer cells. Our group studies the mechanisms that operate in eukaryotic cells to maintain replication fork integrity. In particular, we use a combination of cellular, biochemical and structural approaches to define the role of RecQ helicases in this process. Our recent studies provided new mechanistic insight into the role of RecQ helicases in replication stress response, offering new molecular perspectives to potentiate chemotherapeutic regimens based on replication inhibitor treatment.

Recent Publications

• Bioinformatic analysis of RecQ4 helicases reveals the presence of a RQC domain and a Zn knuckle.
  Marino F, Vindigni A, et al. Biophys Chem. (2013) 177-178:34-9.
  
• Human RECQ1 promotes restart of replication forks reversed by DNA topoisomerase 1 inhibition.
  Berti M, Chaudhuri AR, et al. Nat Struct Mol Biol. (2013) Feb 10 [Epub ahead of print].
  
• In vitro enzyme comparative kinetics: Unwinding of surface-bound DNA nanostructures by RecQ and RecQ1.
  Parisse P, Vindigni A, et al. J Phys Chem Lett. (2012) 3(23):3532-7.
  
• The alpha2 helix in the DNA ligase IV BRCT-1 domain is required for targeted degradation of ligase IV during adenovirus infection.
  Gilson T, Greer AE, et al. Virology. (2012) 428(2):128-35.
  
• Proteomic analysis of gastric cancer and immunoblot validation of potential biomarkers.
  Kocevar N, Odreman F, et al. World J Gastroenterol. (2012) 18(11):128-35.
  
• The human RECQ1 helicase is highly expressed in glioblastoma and plays an important role in tumor cell proliferation.
  Mendoza-Maldonado R, Faoro V, et al. Mol Cancer. (2011) 10:83-100.
  
• A prominent {beta}-hairpin structure in the winged-helix domain of RECQ1 is required for DNA unwinding and oligomer formation.
  Lucic B, Zhang Y, et al. Nucleic Acids Res. (2011) 39(5):1703-17.