Brett A. Feeney

Milam, S. L., Nicely, N. I., Feeney, B., Mattos, C., & Clark, A. C. (2007). Rapid folding and unfolding of Apaf-1 CARD. JOURNAL OF MOLECULAR BIOLOGY, 369(1), 290–304. https://doi.org/10.1016/j.jmb.2007.02.105

Feeney, B., Soderblom, E. J., Goshe, M. B., & Clark, A. C. (2006). Novel protein purification system utilizing an N-terminal fusion protein and a caspase-3 cleavable linker. Protein Expression and Purification, 47(1), 311–318. https://doi.org/10.1016/j.pep.2005.10.005

Feeney, B., Pop, C., Swartz, P., Mattos, C., & Clark, A. C. (2006). Role of loop bundle hydrogen bonds in the maturation and activity of (pro) caspase-3. BIOCHEMISTRY, 45(44), 13249–13263. https://doi.org/10.1021/bi0611964

Feeney, B., & Clark, A. C. (2005). Reassembly of active caspase-3 is facilitated by the propeptide. JOURNAL OF BIOLOGICAL CHEMISTRY, 280(48), 39772–39785. https://doi.org/10.1074/jbc.M505834200

Bobay, B. G., Benson, L., Naylor, S., Feeney, B., Clark, A. C., Goshe, M. B., … Cavanagh, J. (2004). Evaluation of the DNA Binding Tendencies of the Transition State Regulator AbrB†. Biochemistry, 43(51), 16106–16118. https://doi.org/10.1021/bi048399h

Feeney, B., Pop, C., Tripathy, A., & Clark, A. C. (2004). Ionic interactions near the loop L4 are important for maintaining the active-site environment and the dimer stability of (pro)caspase 3. Biochemical Journal (London, England : 1984), 384(Dec 15 2004), 515–525.

Bose, K., Pop, C., Feeney, B., & Clark, A. C. (2003). An uncleavable procaspase-3 mutant has a lower catalytic efficiency but an active site similar to that of mature caspase-3. BIOCHEMISTRY, 42(42), 12298–12310. https://doi.org/10.1021/bi034998x

Pop, C., Feeney, B., Tripathy, A., & Clark, A. C. (2003). Mutations in the procaspase-3 dimer interface affect the activity of the zymogen. BIOCHEMISTRY, 42(42), 12311–12320. https://doi.org/10.1021/bi034999p