A. Clay Clark

Caspases from scleractinian coral show unique regulatory features

JOURNAL OF BIOLOGICAL CHEMISTRY, 295(43), 14578–14591.

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

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 113(41), E6080–E6088.

Modifying Caspase-3 Activity by Altering Allosteric Networks

BIOCHEMISTRY, 53(48), 7582–7595.

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

BIOCHEMISTRY, 52(36), 6219–6231.

Slow folding and assembly of a procaspase-3 interface variant

Biochemistry, 52(20), 3415–3427.

Allosteric modulation of caspase 3 through mutagenesis

BIOSCIENCE REPORTS, 32(4), 401–411.

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

ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, 508(1), 31–38.

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

BIOCHEMICAL JOURNAL, 424, 335–345.

Folding and assembly kinetics of procaspase-3

PROTEIN SCIENCE, 18(12), 2500–2517.

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

JOURNAL OF MOLECULAR BIOLOGY, 369(1), 290–304.

Role of loop bundle hydrogen bonds in the maturation and activity of (pro) caspase-3

BIOCHEMISTRY, 45(44), 13249–13263.

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

PROTEIN SCIENCE, 15(3), 395–409.

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

PROTEIN SCIENCE, 14(9), 2228–2235.

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

JOURNAL OF BIOLOGICAL CHEMISTRY, 280(48), 39772–39785.

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

PROTEIN SCIENCE, 13(8), 2196–2206.

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.

Equilibrium and kinetic folding of a alpha-helical Greek key protein domain: Caspase recruitment domain (CARD) of RICK

BIOCHEMISTRY, 42(20), 6310–6320.

Mutations in the procaspase-3 dimer interface affect the activity of the zymogen

BIOCHEMISTRY, 42(42), 12311–12320.

The C-terminal tail of Arabidopsis 14-3-3 omega functions as an autoinhibitor and may contain a tenth alpha-helix

PLANT JOURNAL, 34(4), 473–484.

Dimeric procaspase-3 unfolds via a four-state equilibrium process

BIOCHEMISTRY, 40(47), 14236–14242.

Removal of the pro-domain does not affect the conformation of the procaspase-3 dimer

BIOCHEMISTRY, 40(47), 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.