ArticleThe Journal of biological chemistry2005
Reassembly of active caspase-3 is facilitated by the propeptide.
Article in The Journal of biological chemistry, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
19 citing papers in PubMed, 41 citations in OpenAlex.
- Molecular Characteristics of Cell Pyroptosis and Its Inhibitors: A Review of Activation, Regulation, and Inhibitors.International journal of molecular sciences · 2022Review
- Signal peptide stabilizes folding and inhibits misfolding of serum amyloid A.Protein science : a publication of the Protein Society · 2022Article
- The intricate biophysical puzzle of caspase-1 activation.Archives of biochemistry and biophysics · 2021Review
- Resurrection of ancestral effector caspases identifies novel networks for evolution of substrate specificity.The Biochemical journal · 2019Review
- Modifications to a common phosphorylation network provide individualized control in caspases.The Journal of biological chemistry · 2018Article
- Multiple proteolytic events in caspase-6 self-activation impact conformations of discrete structural regions.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Redesigning the procaspase-8 dimer interface for improved dimerization.Protein science : a publication of the Protein Society · 2014Article
- Death by caspase dimerization.Advances in experimental medicine and biology · 2012Review
- A bifunctional allosteric site in the dimer interface of procaspase-3.Biophysical chemistry · 2011Article
- Design and characterization of epitope-scaffold immunogens that present the motavizumab epitope from respiratory syncytial virus.Journal of molecular biology · 2011Article
- Substrate-induced conformational changes occur in all cleaved forms of caspase-6.Journal of molecular biology · 2011Article
- Ion channel inhibitors block caspase activation by mechanisms other than restoring intracellular potassium concentration.Cell death & disease · 2011Article
- Melody, an ENU mutation in Caspase 3, alters the catalytic cysteine residue and causes sensorineural hearing loss in mice.Mammalian genome : official journal of the International Mammalian Genome Society · 2010Article
- Folding and assembly kinetics of procaspase-3.Protein science : a publication of the Protein Society · 2009Article
- Intra-molecular chaperone: the role of the N-terminal in conformational selection and kinetic control.Physical biology · 2009Article
- Effect of unilateral ureteral obstruction and anti-angiotensin II treatment on renal tubule and interstitial cell apoptosis in rats.Croatian medical journal · 2008Article
- The pro-peptide of proNGF: structure formation and intramolecular association with NGF.Protein science : a publication of the Protein Society · 2007Article
- Role of loop bundle hydrogen bonds in the maturation and activity of (Pro)caspase-3.Biochemistry · 2006Article
- Novel protein purification system utilizing an N-terminal fusion protein and a caspase-3 cleavable linker.Protein expression and purification · 2006Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Changes in ionic homeostasis are early events leading up to the commitment to apoptosis. Although the direct effects of cations on caspase-3 activity have been examined, comparable studies on procaspase-3 are lacking. In addition, the effects of salts on caspase structure have not been examined. We have studied the effects of cations on the activities and conformations of caspase-3 and an uncleavable mutant of procaspase-3 that is enzymatically active. The results show that caspase-3 is more sensitive to changes in pH and ion concentrations than is the zymogen. This is due to the loss of both an intact intersubunit linker and the prodomain. The results show that, although the caspase-3 subunits reassemble to the heterotetramer, the activity return is low after the protein is incubated at or below pH 4.5 and then returned to pH 7.5. The data further show that the irreversible step in assembly results from heterotetramer rather than heterodimer dissociation and demonstrate that the active site does not form properly following reassembly. However, active-site formation is fully reversible when reassembly occurs in the presence of the prodomain, and this effect is specific for the propeptide of caspase-3. The data show that the prodomain facilitates both dimerization and active-site formation in addition to stabilizing the native structure. Overall, the results show that the prodomain acts as an intramolecular chaperone during assembly of the (pro)caspase subunits and increases the efficiency of formation of the native conformation.
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What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.