Christina Pop

Works (5)

Updated: July 5th, 2023 15:58

2009 journal article

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

BIOCHEMICAL JOURNAL, 424, 335–345.

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)
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Source: Web Of Science
Added: August 6, 2018

2006 journal article

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

BIOCHEMISTRY, 45(44), 13249–13263.

By: B. Feeney n, C. Pop  n, P. Swartz n, C. Mattos n & A. Clark n

MeSH headings : Amino Acid Sequence; Base Sequence; Caspase 3 / chemistry; Caspase 3 / metabolism; Crystallography; DNA Primers; Hydrogen Bonding; Hydrogen-Ion Concentration; Hydrolysis; Models, Molecular; Molecular Sequence Data; Protein Conformation; Spectrometry, Fluorescence
TL;DR: It is shown that replacing the residues affects the activity of the procaspase as well as the mature caspase, with D169A and E167A replacements having the largest effects. (via Semantic Scholar)
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2004 journal article

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.

By: B. Feeney, C. Pop, A. Tripathy & A. Clark

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

2003 journal article

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.

By: K. Bose n, C. Pop n, B. Feeney n & A. Clark n

MeSH headings : Base Sequence; Binding Sites; Caspase 3; Caspases / genetics; Caspases / metabolism; Catalysis; DNA Primers; Enzyme Activation; Enzyme Precursors / genetics; Enzyme Precursors / metabolism; Fluorescence; Hydrolysis; Models, Molecular; Protein Conformation; Trypsin / metabolism
TL;DR: The data suggest that the major conformational change that occurs upon maturation results in formation of the loop bundle among loops L4, L2, and L2', and the pK(a) values of both catalytic groups decrease as a result of the loops movements. (via Semantic Scholar)
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2003 journal article

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

BIOCHEMISTRY, 42(42), 12311–12320.

By: C. Pop n, B. Feeney n, A. Tripathy  n & A. Clark n

MeSH headings : Base Sequence; Caspase 3; Caspases / chemistry; Caspases / genetics; Caspases / metabolism; DNA Primers; Dimerization; Enzyme Precursors / chemistry; Enzyme Precursors / genetics; Enzyme Precursors / metabolism; Models, Molecular; Mutagenesis, Site-Directed; Mutation; Protein Conformation; Spectrometry, Fluorescence
TL;DR: While the mutations do not affect the dimeric properties of the procaspase, it is shown that the V266E mutation may affect the formation of a loop bundle that is important for stabilizing the active site. (via Semantic Scholar)
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Added: August 6, 2018

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