A. Clay Clark

Caspases from scleractinian coral show unique regulatory features

Shrestha, S., Tung, J., Grinshpon, R. D., Swartz, P., Hamilton, P. T., Dimos, B., … Clark, A. C. (2020, August 12). Journal of Biological Chemistry, Vol. 295, pp. 14578–14591.

Tunable allosteric library of caspase-3 identifies coupling between conserved water molecules and conformational selection

Maciag, J. J., Mackenzie, S. H., Tucker, M. B., Schipper, J. L., Swartz, P., & Clark, A. C. (2016, September 28). Proceedings of the National Academy of Sciences.

Modifying Caspase-3 Activity by Altering Allosteric Networks

Cade, C., Swartz, P., MacKenzie, S. H., & Clark, A. C. (2014, October 24). Biochemistry.

Redesigning the procaspase-8 dimer interface for improved dimerization

Protein Science, 23(4), 442–453.

Lengthening the Intersubunit Linker of Procaspase 3 Leads to Constitutive Activation

MacKenzie, S. H., Schipper, J. L., England, E. J., Thomas, M. E., Blackburn, K., Swartz, P., & Clark, A. C. (2013, August 13). Biochemistry, Vol. 52, pp. 6219–6231.

Slow folding and assembly of a procaspase-3 interface variant

Biochemistry, 52(20), 3415–3427.

Allosteric modulation of caspase 3 through mutagenesis

Walters, J., Schipper, J. L., Swartz, P., Mattos, C., & Clark, A. C. (2012, May 21). Bioscience Reports.

A bifunctional allosteric site in the dimer interface of procaspase-3

Schipper, J. L., MacKenzie, S. H., Sharma, A., & Clark, A. C. (2011, May 26). Biophysical Chemistry.

A bifunctional allosteric site in the dimer interface of procaspase-3

Biophysical Chemistry, 159(1), 100–109.

Thermodynamic, enzymatic and structural effects of removing a salt bridge at the base of loop 4 in (pro)caspase-3

Walters, J., Swartz, P., Mattos, C., & Clark, A. C. (2011, January 24). Archives of Biochemistry and Biophysics.

The potential for caspases in drug discovery

[Review of ]. Current Opinion in Drug Discovery & Development, 13(5), 568–576.

A constitutively active and uninhibitable caspase-3 zymogen efficiently induces apoptosis

Walters, J., Pop, C., Scott, F. L., Drag, M., Swartz, P., Mattos, C., … Clark, A. C. (2009, October 1). Biochemical Journal.

Folding and assembly kinetics of procaspase‐3

Milam, S. L., & Clark, A. C. (2009, October 1). Protein Science.

Practical approaches to protein folding and assembly: Spectroscopic strategies in thermodynamics and kinetics

[Review of ]. Methods in enzymology: biothermodynamics,vol 455, part a, 455, 1–39.

Minimizing frustration by folding in an aqueous environment

[Review of ]. Archives of Biochemistry and Biophysics, 469(1), 118–131.

Protein folding: Are we there yet?

Archives of Biochemistry and Biophysics, 469(1), 1–3.

Targeting cell death in tumors by activating Caspases

[Review of ]. Current Cancer Drug Targets, 8(2), 98–109.

Rapid Folding and Unfolding of Apaf-1 CARD

Milam, S. L., Nicely, N. I., Feeney, B., Mattos, C., & Clark, A. C. (2007, March 16). Journal of Molecular Biology.

Role of Loop Bundle Hydrogen Bonds in the Maturation and Activity of (Pro)caspase-3

Feeney, B., Pop, C., Swartz, P., Mattos, C., & Clark, A. C. (2006, October 17). Biochemistry.

Substitutions of prolines examine their role in kinetic trap formation of the caspase recruitment domain (CARD) of RICK

Chen, Y. R., & Clark, A. C. (2006, February 24). Protein Science.

Characterization and enzymatic degradation of Sup35NM, a yeast prion‐like protein

Chen, C. Y., Rojanatavorn, K., Clark, A. C., & Shih, J. C. H. (2005, August 5). Protein Science.

Novel protein purification system utilizing an N-terminal fusion protein and a caspase-3 cleavable linker

Protein Expression and Purification, 47(1), 311–318.

Reassembly of Active Caspase-3 Is Facilitated by the Propeptide

Feeney, B., & Clark, A. C. (2005, October 4). Journal of Biological Chemistry.

pH effects on the stability and dimerization of procaspase-3

Protein Science, 14(1), 24–36.

Evaluation of the DNA Binding Tendencies of the Transition State Regulator AbrB†

Biochemistry, 43(51), 16106–16118.

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.

Kinetic traps in the folding/unfolding of procaspase‐1 CARD domain

Chen, Y. R., & Clark, A. C. (2004, July 23). Protein Science.

An Uncleavable Procaspase-3 Mutant Has a Lower Catalytic Efficiency but an Active Site Similar to That of Mature Caspase-3

Bose, K., Pop, C., Feeney, B., & Clark, A. C. (2003, October 1). Biochemistry.

Equilibrium and Kinetic Folding of a α-Helical Greek Key Protein Domain:  Caspase Recruitment Domain (CARD) of RICK

Chen, Y.-R., & Clark, A. C. (2003, May 1). Biochemistry, Vol. 42, pp. 6310–6320.

Mutations in the Procaspase-3 Dimer Interface Affect the Activity of the Zymogen

Pop, C., Feeney, B., Tripathy, A., & Clark, A. C. (2003, October 1). Biochemistry.

The C‐terminal tail of Arabidopsis 14‐3‐3ω functions as an autoinhibitor and may contain a tenth α‐helix

Shen, W., Clark, A. C., & Huber, S. C. (2003, May 1). The Plant Journal.

Dimeric Procaspase-3 Unfolds via a Four-State Equilibrium Process

Bose, K., & Clark, A. C. (2001, October 26). Biochemistry.

Removal of the Pro-Domain Does Not Affect the Conformation of the Procaspase-3 Dimer

Pop, C., Chen, Y.-R., Smith, B., Bose, K., Bobay, B., Tripathy, A., … Clark, A. C. (2001, October 30). Biochemistry, Vol. 40, pp. 14224–14235.

A rapid chromatographic method to separate the subunits of bacterial luciferase in urea-containing buffer

Bioluminescence and Chemiluminescence, Pt. C, 305, 157–164.