Rate My Professor Lorena Beese

The Beese Lab utilizes X-ray crystallography and cryo-electron microscopy to determine high-resolution structures of proteins and complexes, combining these with biochemical, biophysical, genetic, and computational methods to investigate fundamental biological processes. Her research centers on the structural mechanisms of DNA replication and repair, including fidelity of DNA polymerases, human mismatch repair initiation and protein assemblies, and excision of DNA lesions. Additional foci include protein lipidation by farnesyl- and geranylgeranyltransferases, informing inhibitor design for anticancer and antifungal therapies, and implications for neurodegenerative diseases through DNA triplet repeat expansions. Key publications encompass "The Closing Mechanism of DNA Polymerase I at Atomic Resolution" (Structure, 2015), "Structural evidence for the rare tautomer hypothesis of spontaneous mutagenesis" (PNAS, 2011), "Structures of Cryptococcus neoformans protein farnesyltransferase reveal strategies for developing inhibitors that target fungal pathogens" (J Biol Chem, 2011), "Structure of mammalian protein geranylgeranyltransferase type-I" (EMBO J, 2003), and recent advances like "Structure-Guided Discovery of Potent Antifungals that Prevent Ras Signaling by Inhibiting Protein Farnesyltransferase" (J Med Chem, 2022). With over 12,000 citations on Google Scholar, her contributions have advanced understanding in structural biology and supported therapeutic development. Beese was elected to the National Academy of Sciences in 2009 and has secured major grants, including from the Burroughs Wellcome Fund for mismatch repair studies.