Works (4)

Updated: July 7th, 2023 21:17

2012 journal article

Allosteric modulation of caspase 3 through mutagenesis

BIOSCIENCE REPORTS, 32(4), 401–411.

By: J. Walters n, J. Schipper n, P. Swartz n, C. Mattos n & A. Clark n

author keywords: allosteric site; apoptosis; caspase; inhibition; protein ensemble
MeSH headings : Allosteric Regulation / genetics; Allosteric Site / genetics; Amino Acid Substitution; Caspase 3 / chemistry; Caspase 3 / genetics; Catalytic Domain; Crystallography, X-Ray; Humans; Hydrogen Bonding; Molecular Dynamics Simulation; Mutagenesis, Site-Directed; Protein Interaction Domains and Motifs; Protein Structure, Secondary
TL;DR: The results demonstrate that considering allosteric inhibition of caspase 3 as a shift between discrete ‘off-state’ or ‘on- state’ conformations is insufficient and requires the representation of an ensemble of inactive states and shows that subtle structural changes lead to the population of the inactive ensemble. (via Semantic Scholar)
Source: Web Of Science
Added: August 6, 2018

2011 journal article

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


By: J. Walters n, P. Swartz n, C. Mattos n & A. Clark n

author keywords: Apoptosis; Caspase activation; Enzyme activity; Protein folding and assembly
MeSH headings : Caspase 3 / chemistry; Caspase 3 / genetics; Caspase 3 / metabolism; Catalytic Domain; Crystallography, X-Ray; Enzyme Stability; Hydrogen Bonding; Models, Molecular; Mutation; Protein Folding; Static Electricity; Structure-Activity Relationship; Thermodynamics
TL;DR: Results suggest E246 and K242 are important in procaspase-3 for their interaction with neighboring residues, not with one another, and formation of the K242-E246 salt bridge in caspases3 is needed for an accurate, stable conformation of loop L4 and proper active site formation in the mature enzyme. (via Semantic Scholar)
Source: Web Of Science
Added: August 6, 2018

2009 journal article

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


By: J. Walters n, C. Pop*, F. Scott*, M. Drag*, P. Swartz n, C. Mattos n, G. Salvesen*, A. Clark n

author keywords: apoptosis; cancer therapy; conformational switch; co-operative dimer interface; procaspase activation
MeSH headings : Amino Acid Substitution; Apoptosis; Binding Sites / genetics; Blotting, Western; Caspase 3 / chemistry; Caspase 3 / genetics; Caspase 3 / metabolism; Cell Line; Crystallography, X-Ray; Enzyme Activation; Enzyme Precursors / chemistry; Enzyme Precursors / genetics; Enzyme Precursors / metabolism; Humans; Models, Molecular; Mutation; Protein Conformation; Protein Multimerization; Protein Structure, Tertiary; Structure-Activity Relationship; Transfection; X-Linked Inhibitor of Apoptosis Protein / genetics; X-Linked Inhibitor of Apoptosis Protein / metabolism
TL;DR: It is shown that low concentrations of the pseudo-activated procaspase-3 kill mammalian cells rapidly and, importantly, this protein is not cleaved nor is it inhibited efficiently by the endogenous regulator XIAP (X-linked inhibitor of apoptosis). (via Semantic Scholar)
Source: Web Of Science
Added: August 6, 2018

2009 review

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.

By: J. Walters, S. Milam & A. Clark

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

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