Faculty and Staff
Geoff Lippa
Visit Asst Professor Biology
Alfred University Contact Info
Office Location: Science Center 346
Department: Biology  
Office Hours: Mon: 9-10 am
Tue: 4-5 pm

Thu: 4-6 pm
Phone: 607.871.2850  
Post-doctoral studies: Structural Biology
Hauptman Woodward Medical Institute, 2015

PhD: Biochemistry
University of Rochester, 2013

B.S.: Chemistry (Biochemistry)
Hobart and William Smith Colleges, 2007

Areas of Concentration

Biology, Chemistry, Biochemistry, RNA Biology, X-ray crystallography, Biophysics, Computational Biology, Virology, Microbiology, Molecular Biology

Selected Publications

Zhu, J, Lippa, G.M., Gulick A.M., Tipton, P.A. "Examining Reaction Specificity in PvcB, a Source of Diversity in Isonitrile-containing Natural Products." Biochemistry. 2015, 54 (16) 2659-69.

Salter, J.S.*, Lippa, G.M.*, Belashov, I.A., Wedekind, J.E. "Core-binding factor ß (CBFß) increases the affinity between Cullin5 and HIV-1 Vif within an E3 Ligase Complex." Biochemistry. 2012, 51 (44) 8702-8704. (*Shared first authorship)

Lippa, G.M.*, Liberman, J.A.*, Jenkins, J.L.*, Krucinska, J., Salim, M., Wedekind, J.E. Crystallographic Analysis of Small Ribozymes and Riboswitches. In Ribozymes: Methods and Protocols; Hartig, Jorg S. Ed; Methods in Molecular Biology, Vol. 848,; Humana Press, 2012, p. 15984. (*Shared first authorship)


I am active in sports including soccer, tennis, swimming, and ultimate frisbee. I enjoy cooking and taking hikes with my wife and three rescued dogs.

Classes Taught

BIOL150 (Biological Foundations), BIOL207 (Anatomy and Physiology I), BIOL208 (Anatomy and Physiology II), CHEM105 (General Chemistry I), CHEM106 (General Chemistry II)

Current Research

Viruses, like the human immunodeficiency virus (HIV), have the ability to hijack host pathways to promote disease pathogenesis.  In 2004, the Nobel prize was given to three chemists who discovered a critical cellular process known as ubiquitination.  This process is used by the cell for protein signaling and degradation purposes.  The proteasome functions in the cell to break down or degrade unnecessary or damaged proteins.  Ubiquitination and the proteasome work together to degrade these target proteins.  Viruses have counteracted these natural processes by producing viral proteins capable of sequestering or enhancing host ubiquitination.   Substantial research efforts have been made in discovering both the host proteins targeted in this fashion and those viral proteins responsible for this aberrant activity.  Identifying these viral proteins and their mechanisms will provide appealing anti-viral therapeutic opportunities. 

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