Works (33)
Updated: July 7th, 2023 21:17
2020 journal article
Caspases from scleractinian coral show unique regulatory features
JOURNAL OF BIOLOGICAL CHEMISTRY, 295(43), 14578–14591.
author keywords: caspase; cysteine protease; allosteric regulation; substrate specificity; coral apoptosis; coral immunity; functional divergence; substrate selection; CARD-caspase; apoptosis
MeSH headings : Amino Acid Sequence; Animals; Anthozoa / chemistry; Anthozoa / cytology; Anthozoa / enzymology; Anthozoa / metabolism; Apoptosis; Caspases / chemistry; Caspases / metabolism; Coral Reefs; Crystallography, X-Ray; Enzyme Activation; Humans; Models, Molecular; Protein Conformation; Protein Domains; Sequence Alignment; Substrate Specificity
open access via www.jbc.org (publisher PDF)
UN Sustainable Development Goal Categories
3. Good Health and Well-being
(Web of Science)
14. Life Below Water
(OpenAlex)
Sources: Web Of Science, ORCID, NC State University Libraries
Added: January 14, 2021
2016 journal article
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.
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
UN Sustainable Development Goal Categories
3. Good Health and Well-being
(Web of Science)
6. Clean Water and Sanitation
(OpenAlex)
Source: Web Of Science
Added: August 6, 2018
2014 journal article
Modifying Caspase-3 Activity by Altering Allosteric Networks
BIOCHEMISTRY, 53(48), 7582–7595.
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
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)
UN Sustainable Development Goal Categories
3. Good Health and Well-being
(Web of Science)
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.
Source: NC State University Libraries
Added: August 6, 2018
2013 journal article
Lengthening the Intersubunit Linker of Procaspase 3 Leads to Constitutive Activation
BIOCHEMISTRY, 52(36), 6219–6231.
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
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)
UN Sustainable Development Goal Categories
3. Good Health and Well-being
(Web of Science)
Source: Web Of Science
Added: August 6, 2018
2013 journal article
Slow folding and assembly of a procaspase-3 interface variant
Biochemistry, 52(20), 3415–3427.
Source: NC State University Libraries
Added: August 6, 2018
2012 journal article
Allosteric modulation of caspase 3 through mutagenesis
BIOSCIENCE REPORTS, 32(4), 401–411.
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)
UN Sustainable Development Goal Categories
3. Good Health and Well-being
(Web of Science)
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.
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
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 Goal Categories
3. Good Health and Well-being
(Web of Science; OpenAlex)
Sources: Web Of Science, NC State University Libraries
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
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, 508(1), 31–38.
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)
UN Sustainable Development Goal Categories
3. Good Health and Well-being
(Web of Science)
Source: Web Of Science
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.
Source: NC State University Libraries
Added: August 6, 2018
2009 journal article
A constitutively active and uninhibitable caspase-3 zymogen efficiently induces apoptosis
BIOCHEMICAL JOURNAL, 424, 335–345.
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)
UN Sustainable Development Goal Categories
3. Good Health and Well-being
(Web of Science)
Source: Web Of Science
Added: August 6, 2018
2009 journal article
Folding and assembly kinetics of procaspase-3
PROTEIN SCIENCE, 18(12), 2500–2517.
author keywords: apoptosis; dimer assembly; kinetic trap; burst-phase kinetics
MeSH headings : Caspase 3 / chemistry; Caspase 3 / metabolism; Circular Dichroism; Dimerization; Enzyme Activation; Models, Molecular; Protein Conformation; Protein Folding; Spectrometry, Fluorescence
TL;DR:
The folding and assembly of procaspase‐3 is examined by fluorescence emission, circular dichroism, differential quenching by acrylamide, anisotropy, and enzyme activity assays and suggest that slow dimerization results from the lack of stabilizing native contacts in the initial encounter complex.
(via Semantic Scholar)
UN Sustainable Development Goal Categories
3. Good Health and Well-being
(Web of Science)
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.
Source: NC State University Libraries
Added: August 6, 2018
2008 review
Minimizing frustration by folding in an aqueous environment
[Review of ]. Archives of Biochemistry and Biophysics, 469(1), 118–131.
Source: NC State University Libraries
Added: August 6, 2018
2008 journal article
Protein folding: Are we there yet?
Archives of Biochemistry and Biophysics, 469(1), 1–3.
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.
Source: NC State University Libraries
Added: August 6, 2018
2007 journal article
Rapid folding and unfolding of Apaf-1 CARD
JOURNAL OF MOLECULAR BIOLOGY, 369(1), 290–304.
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)
UN Sustainable Development Goal Categories
3. Good Health and Well-being
(Web of Science)
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.
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)
UN Sustainable Development Goal Categories
3. Good Health and Well-being
(Web of Science)
Source: Web Of Science
Added: August 6, 2018
2006 journal article
Substitutions of prolines examine their role in kinetic trap formation of the caspase recruitment domain (CARD) of RICK
PROTEIN SCIENCE, 15(3), 395–409.
author keywords: caspase recruitment domain; RICK; Greek key; folding kinetics; equilibrium folding; folding intermediates; kinetic traps
MeSH headings : Amino Acid Substitution; Binding Sites; Caspase 1; Caspases / chemistry; Caspases / metabolism; Circular Dichroism; Enzyme Precursors / chemistry; Enzyme Precursors / metabolism; Kinetics; Models, Molecular; Proline / chemistry; Proline / genetics; Protein Folding; Protein Serine-Threonine Kinases / chemistry; Protein Serine-Threonine Kinases / genetics; Protein Serine-Threonine Kinases / metabolism; Protein Structure, Tertiary; Receptor-Interacting Protein Serine-Threonine Kinase 2; Tumor Necrosis Factor Receptor-Associated Peptides and Proteins / chemistry; Tumor Necrosis Factor Receptor-Associated Peptides and Proteins / genetics; Tumor Necrosis Factor Receptor-Associated Peptides and Proteins / metabolism
TL;DR:
The results show that P85 is critical for maintaining the function of the protein and that all mutations decrease the stability, and the complex folding pathway, especially formation of kinetically trapped species, is not due to prolyl isomerism.
(via Semantic Scholar)
UN Sustainable Development Goal Categories
3. Good Health and Well-being
(Web of Science)
15. Life on Land
(OpenAlex)
Source: Web Of Science
Added: August 6, 2018
2005 journal article
Characterization and enzymatic degradation of Sup35NM, a yeast prion-like protein
PROTEIN SCIENCE, 14(9), 2228–2235.
author keywords: BSE; prion; PrPSc; Sup35NM; yeast prion; prion surrogate protein; enzymatic degradation
MeSH headings : Amino Acid Sequence; Blotting, Western; Congo Red / metabolism; Endopeptidase K / metabolism; Escherichia coli / genetics; Fluorescence; Microscopy, Electron / methods; Molecular Sequence Data; Peptide Fragments / chemistry; Peptide Fragments / isolation & purification; Peptide Fragments / metabolism; Peptide Hydrolases / metabolism; Peptide Termination Factors; Prions / chemistry; Prions / isolation & purification; Prions / metabolism; Saccharomyces cerevisiae Proteins / chemistry; Saccharomyces cerevisiae Proteins / isolation & purification; Saccharomyces cerevisiae Proteins / metabolism; Temperature; Time Factors
TL;DR:
The degradation of Sup35NM aggregates by keratinase and proteinase K under various conditions was studied and compared and will be of value in understanding the mechanism and optimization of the degradation process.
(via Semantic Scholar)
UN Sustainable Development Goal Categories
3. Good Health and Well-being
(Web of Science)
Source: Web Of Science
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.
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)
UN Sustainable Development Goal Categories
3. Good Health and Well-being
(Web of Science)
Sources: Web Of Science, Crossref
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.
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)
UN Sustainable Development Goal Categories
3. Good Health and Well-being
(Web of Science)
Source: Web Of Science
Added: August 6, 2018
2005 journal article
pH effects on the stability and dimerization of procaspase-3
Protein Science, 14(1), 24–36.
Source: NC State University Libraries
Added: August 6, 2018
2004 journal article
Evaluation of the DNA Binding Tendencies of the Transition State Regulator AbrB†
Biochemistry, 43(51), 16106–16118.
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)
UN Sustainable Development Goal Categories
3. Good Health and Well-being
(Web of Science)
Sources: Web Of Science, Crossref
Added: August 6, 2018
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.
Source: NC State University Libraries
Added: August 6, 2018
2004 journal article
Kinetic traps in the folding/unfolding of procaspase-1 CARD domain
PROTEIN SCIENCE, 13(8), 2196–2206.
author keywords: caspase recruitment domain; alpha-helical Greek key; kinetic trap; double jump; interrupted refolding; equilibrium folding
MeSH headings : Amino Acid Sequence; Animals; Caspase 1; Caspases / chemistry; Caspases / genetics; Chromatography, Gel; Enzyme Precursors / chemistry; Enzyme Precursors / genetics; Humans; Kinetics; Molecular Sequence Data; Protein Denaturation / genetics; Protein Folding; Protein Structure, Secondary; Protein Structure, Tertiary / genetics
TL;DR:
The data show that both unfolding and refolding processes are slow, and the pathways contain kinetically trapped species.
(via Semantic Scholar)
UN Sustainable Development Goal Categories
3. Good Health and Well-being
(Web of Science)
Source: Web Of Science
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.
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)
UN Sustainable Development Goal Categories
3. Good Health and Well-being
(Web of Science)
Source: Web Of Science
Added: August 6, 2018
2003 journal article
Equilibrium and kinetic folding of a alpha-helical Greek key protein domain: Caspase recruitment domain (CARD) of RICK
BIOCHEMISTRY, 42(20), 6310–6320.
MeSH headings : Amino Acid Sequence; Caspases / metabolism; Drug Stability; Humans; In Vitro Techniques; Kinetics; Models, Molecular; Molecular Sequence Data; Protein Folding; Protein Kinases / chemistry; Protein Kinases / genetics; Protein Kinases / metabolism; Protein Structure, Secondary; Protein Structure, Tertiary; Receptor-Interacting Protein Serine-Threonine Kinase 2; Recombinant Proteins / chemistry; Recombinant Proteins / genetics; Recombinant Proteins / metabolism; Salts; Sequence Homology, Amino Acid; Thermodynamics
TL;DR:
The results suggest that electrostatic interactions are stabilizing in the native protein, and the favorable Coulombic interactions are reduced at low ionic strength.
(via Semantic Scholar)
UN Sustainable Development Goal Categories
3. Good Health and Well-being
(Web of Science)
Source: Web Of Science
Added: August 6, 2018
2003 journal article
Mutations in the procaspase-3 dimer interface affect the activity of the zymogen
BIOCHEMISTRY, 42(42), 12311–12320.
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)
UN Sustainable Development Goal Categories
3. Good Health and Well-being
(Web of Science)
Source: Web Of Science
Added: August 6, 2018
2003 journal article
The C-terminal tail of Arabidopsis 14-3-3 omega functions as an autoinhibitor and may contain a tenth alpha-helix
PLANT JOURNAL, 34(4), 473–484.
author keywords: 14-3-3 proteins; nitrate reductase; autoinhibition; protein structure; protein-protein interaction; protein phosphorylation
MeSH headings : 14-3-3 Proteins; Amino Acid Sequence; Antibodies / immunology; Arabidopsis / metabolism; Arabidopsis Proteins / antagonists & inhibitors; Arabidopsis Proteins / chemistry; Arabidopsis Proteins / metabolism; Arabidopsis Proteins / pharmacology; Cations / pharmacology; Molecular Sequence Data; Protein Binding / drug effects; Protein Isoforms / chemistry; Protein Isoforms / metabolism; Protein Structure, Secondary; Tyrosine 3-Monooxygenase / antagonists & inhibitors; Tyrosine 3-Monooxygenase / chemistry; Tyrosine 3-Monooxygenase / metabolism; Tyrosine 3-Monooxygenase / pharmacology
TL;DR:
It is proposed that in the absence of polycations, access of target proteins to their binding groove in the 14-3-3 protein is restricted by the C-terminus, which acts as part of a gate that opens with the binding of poly cations to loop 8.
(via Semantic Scholar)
UN Sustainable Development Goal Categories
3. Good Health and Well-being
(Web of Science)
Source: Web Of Science
Added: August 6, 2018
2001 journal article
Dimeric procaspase-3 unfolds via a four-state equilibrium process
BIOCHEMISTRY, 40(47), 14236–14242.
MeSH headings : Caspase 3; Caspases / drug effects; Caspases / genetics; Caspases / metabolism; Circular Dichroism; Dimerization; Enzyme Precursors / drug effects; Enzyme Precursors / genetics; Enzyme Precursors / metabolism; Models, Chemical; Mutation; Protein Denaturation; Spectrometry, Fluorescence; Thermodynamics; Urea / pharmacology
TL;DR:
First, dimerization of procaspase-3 occurs as a result of the association of two monomeric folding intermediates, demonstrating that procaspases-3Dimerization is a folding event and the stability of the dimer contributes significantly to the conformational free energy of the protein.
(via Semantic Scholar)
UN Sustainable Development Goal Categories
3. Good Health and Well-being
(Web of Science)
7. Affordable and Clean Energy
(OpenAlex)
Source: Web Of Science
Added: August 6, 2018
2001 journal article
Removal of the pro-domain does not affect the conformation of the procaspase-3 dimer
BIOCHEMISTRY, 40(47), 14224–14235.
MeSH headings : Caspase 3; Caspase Inhibitors; Caspases / chemistry; Caspases / genetics; Caspases / metabolism; Circular Dichroism; Dimerization; Enzyme Precursors / chemistry; Enzyme Precursors / genetics; Enzyme Precursors / metabolism; Protein Conformation; Protein Folding; Protein Processing, Post-Translational; Protein Structure, Secondary; Protein Structure, Tertiary; Sequence Deletion; Spectroscopy, Fourier Transform Infrared; Substrate Specificity
TL;DR:
A model for maturation of the procaspase-3 dimer is proposed based on results from circular dichroism, fluorescence anisotropy, and FTIR studies, which suggest that the pro-peptide adopts a beta-structure when in contact with the protein, but it is a random coil when free in solution.
(via Semantic Scholar)
UN Sustainable Development Goal Categories
3. Good Health and Well-being
(Web of Science)
14. Life Below Water
(OpenAlex)
Sources: Web Of Science, NC State University Libraries
Added: August 6, 2018
2000 journal article
A rapid chromatographic method to separate the subunits of bacterial luciferase in urea-containing buffer
Bioluminescence and Chemiluminescence, Pt. C, 305, 157–164.
Source: NC State University Libraries
Added: August 6, 2018
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