Brett A. Feeney

Works (8)

Updated: July 5th, 2023 15:58

2007 journal article

Rapid folding and unfolding of Apaf-1 CARD

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

By: S. Milam n, N. Nicely n, B. Feeney n, C. Mattos n & A. Clark n

author keywords: caspase recruitment domain; protein folding; folding kinetics; parallel folding channels; sequential mixing stopped-flow
MeSH headings : Apoptotic Protease-Activating Factor 1 / chemistry; Apoptotic Protease-Activating Factor 1 / metabolism; Crystallography, X-Ray; Fluorescence; Kinetics; Models, Biological; Protein Denaturation; Protein Folding; Protein Structure, Secondary; Protein Structure, Tertiary; Thermodynamics
TL;DR: Examination of the equilibrium and kinetic folding of the CARD of Apaf-1 (apoptotic protease activating factor 1), which consists of 97 amino acid residues, at pH 6 and pH 8 showed that the native ensemble is formed rapidly upon refolding, in contrast to other CARDs in which folding appears to be dominated by formation of kinetic traps. (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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Added: August 6, 2018

2005 journal article

Novel protein purification system utilizing an N-terminal fusion protein and a caspase-3 cleavable linker

Protein Expression and Purification, 47(1), 311–318.

By: B. Feeney n, E. Soderblom n, M. Goshe n & A. Clark n

author keywords: caspase-3; fusion protein; protein expression; proteolysis
MeSH headings : Amino Acid Sequence; Caspase 3 / metabolism; Caspase 3 / physiology; Glutathione Transferase / genetics; Histidine / genetics; Hydrolysis; Molecular Sequence Data; Peptide Fragments / chemistry; Peptide Fragments / genetics; Peptide Fragments / metabolism; Protein Structure, Tertiary / genetics; Proteins / genetics; Proteins / isolation & purification; Proteins / metabolism; Recombinant Fusion Proteins / genetics; Recombinant Fusion Proteins / isolation & purification; Recombinant Fusion Proteins / metabolism
TL;DR: A glutathione S-transferase-fusion protein vector with a caspase-3 consensus cleavage sequence located between the N-terminal GST tag and a target protein is designed and it is shown that the enzyme efficiently cleaves the fusion protein without leaving excess amino acids on the target protein. (via Semantic Scholar)
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Added: August 6, 2018

2005 journal article

Reassembly of active caspase-3 is facilitated by the propeptide

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

By: B. Feeney n & A. Clark n

MeSH headings : Apoptosis; Binding Sites; Calcium / chemistry; Caspase 3; Caspase 6; Caspase 7; Caspases / chemistry; Caspases / metabolism; Cations; Dimerization; Dose-Response Relationship, Drug; Electrophoresis, Polyacrylamide Gel; Fluorescence Resonance Energy Transfer; Humans; Hydrogen-Ion Concentration; Ions; Magnesium / chemistry; Models, Chemical; Molecular Chaperones / chemistry; Mutagenesis; Mutation; Peptides / chemistry; Protein Binding; Protein Conformation; Protein Structure, Tertiary; Salts / chemistry; Salts / pharmacology; Temperature; Time Factors; Tryptophan / chemistry
TL;DR: The results show that caspase-3 is more sensitive to changes in pH and ion concentrations than is the zymogen and the prodomain acts as an intramolecular chaperone during assembly of the (pro)caspase subunits and increases the efficiency of formation of the native conformation. (via Semantic Scholar)
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2004 journal article

Evaluation of the DNA Binding Tendencies of the Transition State Regulator AbrB†

Biochemistry, 43(51), 16106–16118.

By: B. Bobay n, L. Benson n, S. Naylor  n, B. Feeney n, A. Clark n, M. Goshe n, M. Strauch n, R. Thompson n, J. Cavanagh n

MeSH headings : Bacillus subtilis / metabolism; Circular Dichroism; DNA / chemistry; DNA / metabolism; Kinetics; Protein Binding / physiology; Spectrometry, Mass, Electrospray Ionization; Transcription Factors / chemistry; Transcription Factors / metabolism
TL;DR: This comprehensive and corroborative spectroscopic study endorses the use of microESI-MS for rapidly ascertaining qualitative binding trends in noncovalent systems in a high-throughput manner. (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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