Sarah H. MacKenzie

Works (9)

Updated: July 5th, 2023 15:46

2016 article

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.

By: J. Maciag n, S. Mackenzie n, M. Tucker  n, J. Schipper n, P. Swartz n & A. Clark n

author keywords: allostery; conformational selection; saturation mutagenesis; protein solvation; protein structure
MeSH headings : Allosteric Regulation; Allosteric Site; Amino Acid Substitution; Caspase 3 / chemistry; Caspase 3 / genetics; Caspase 3 / metabolism; Catalytic Domain; Crystallography, X-Ray; Enzyme Activation; Models, Molecular; Molecular Conformation; Molecular Dynamics Simulation; Mutagenesis; Protein Binding; Protein Conformation; Protein Multimerization; Quantitative Structure-Activity Relationship; Solubility; Water / chemistry
topics (OpenAlex): CRISPR and Genetic Engineering; Cell death mechanisms and regulation; Autophagy in Disease and Therapy
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6. Clean Water and Sanitation (OpenAlex)
Source: Web Of Science
Added: August 6, 2018

2014 article

Modifying Caspase-3 Activity by Altering Allosteric Networks

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

By: C. Cade n, P. Swartz n, S. MacKenzie n & A. Clark n

MeSH headings : Allosteric Site / genetics; Amino Acid Substitution; Caspase 3 / chemistry; Caspase 3 / genetics; Caspase 3 / metabolism; Crystallography, X-Ray; Humans; Kinetics; Models, Molecular; Molecular Dynamics Simulation; Mutagenesis, Site-Directed; Protein Conformation; Protein Multimerization; Protein Structure, Quaternary; Recombinant Proteins / chemistry; Recombinant Proteins / genetics; Recombinant Proteins / metabolism
topics (OpenAlex): Cell death mechanisms and regulation; ATP Synthase and ATPases Research; Machine Learning in Bioinformatics
TL;DR: The data show that the caspase-3 native ensemble includes the canonical active state as well as an inactive conformation characterized by an intact substrate-binding pocket, but with an altered helix 3, which reflects the relative population of each species in the native ensemble. (via Semantic Scholar)
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Source: Web Of Science
Added: August 6, 2018

2014 journal article

Redesigning the procaspase-8 dimer interface for improved dimerization

Protein Science, 23(4), 442–453.

By: C. Ma, S. MacKenzie & A. Clark

Source: NC State University Libraries
Added: August 6, 2018

2013 article

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.

By: S. MacKenzie n, J. Schipper n, E. England n, M. Thomas n , K. Blackburn n, P. Swartz n, A. Clark n

MeSH headings : Apoptosis / physiology; Caspase 3 / chemistry; Caspase 3 / genetics; Caspase 3 / metabolism; Caspase Inhibitors / pharmacology; Catalytic Domain; Enzyme Activation; Enzyme Precursors / chemistry; Models, Chemical; Models, Molecular; Molecular Dynamics Simulation; Protein Conformation; Protein Multimerization
topics (OpenAlex): Cellular Mechanics and Interactions; Elasticity and Material Modeling
TL;DR: The data show that releasing the strain of the short IL is not sufficient to populate the active conformer of the native ensemble, and it is shown that increasing the length of the IL by introducing 3-5 alanines results in constitutively active procaspases. (via Semantic Scholar)
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Sources: Web Of Science, NC State University Libraries
Added: August 6, 2018

2013 journal article

Slow folding and assembly of a procaspase-3 interface variant

Biochemistry, 52(20), 3415–3427.

By: S. MacKenzie & A. Clark

Source: NC State University Libraries
Added: August 6, 2018

2011 article

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.

By: J. Schipper n, S. MacKenzie n, A. Sharma n & A. Clark n

author keywords: Caspase; Apoptosis; Allosteric activator; Drug design; Cancer therapy
MeSH headings : Allosteric Site; Caspase 3 / chemistry; Caspase 3 / metabolism; Enzyme Activation / drug effects; Humans; Models, Molecular; Protein Binding; Protein Multimerization; Small Molecule Libraries / chemistry; Small Molecule Libraries / pharmacology
topics (OpenAlex): Cell death mechanisms and regulation; Endoplasmic Reticulum Stress and Disease; Protein Structure and Dynamics
TL;DR: This work has utilized the allosteric site of caspase-3 to identify a small molecule activator of procaspase and to characterize its binding to the protease, and suggests that an efficient activator must stabilize the active conformer of the zymogen by expelling the intersubunit linker from the interface. (via Semantic Scholar)
UN Sustainable Development Goals Color Wheel
UN Sustainable Development Goal Categories
3. Good Health and Well-being (Web of Science; OpenAlex)
Source: Web Of Science
Added: August 6, 2018

2011 journal article

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

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

By: J. Schipper, S. MacKenzie, A. Sharma & A. Clark

Source: NC State University Libraries
Added: August 6, 2018

2010 review

The potential for caspases in drug discovery

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

By: S. MacKenzie, J. Schipper & A. Clark

Source: NC State University Libraries
Added: August 6, 2018

2008 review

Targeting cell death in tumors by activating Caspases

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

By: S. MacKenzie & A. Clark

Source: NC State University Libraries
Added: August 6, 2018

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