Sarah H. MacKenzie

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.

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

BIOPHYSICAL CHEMISTRY, 159(1), 100–109.

The potential for caspases in drug discovery

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

Targeting cell death in tumors by activating Caspases

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