Lorena S Beese

Conversion of protein farnesyltransferase to a geranylgeranyltransferase.

P. Casey, L. Beese, K. L. Terry, 2006, Biochemistry.

3-Aminopyrrolidinone farnesyltransferase inhibitors: design of macrocyclic compounds with improved pharmacokinetics and excellent cell potency.

A. D. Rodrigues, J Christopher Culberson, Ronald Robinson, 2002, Journal of medicinal chemistry.

The mechanism of the translocation step in DNA replication by DNA polymerase I: a computer simulation analysis.

Martin Karplus, M. Karplus, L. Beese, 2010, Structure.

Crystal structures of the anticancer clinical candidates R115777 (Tipifarnib) and BMS-214662 complexed with protein farnesyltransferase suggest a mechanism of FTI selectivity.

L. Beese, T. Reid, Lorena S Beese, 2004, Biochemistry.

Ligand-induced conformational changes in a thermophilic ribose-binding protein

Homme W Hellinga, H. Hellinga, L. Beese, 2008, BMC Structural Biology.

Structural adaptations that modulate monosaccharide, disaccharide, and trisaccharide specificities in periplasmic maltose-binding proteins.

Homme W Hellinga, H. Hellinga, L. Beese, 2009, Journal of molecular biology.

Thematic review series: Lipid Posttranslational Modifications. Structural biology of protein farnesyltransferase and geranylgeranyltransferase type I Published, JLR Papers in Press, February 13, 2006.

L. Beese, Lorena S Beese, Kimberly T. Lane, 2006, Journal of Lipid Research.

Structural basis for binding and selectivity of antimalarial and anticancer ethylenediamine inhibitors to protein farnesyltransferase.

Steven Fletcher, M. Gelb, L. Beese, 2009, Chemistry & biology.

Crystallographic analysis of CaaX prenyltransferases complexed with substrates defines rules of protein substrate selectivity.

P. Casey, L. Beese, T. Reid, 2004, Journal of molecular biology.