ArticleBiochemistry2003
Mutations in the procaspase-3 dimer interface affect the activity of the zymogen.
Article in Biochemistry, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 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.
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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
25 citing papers in PubMed, 42 citations in OpenAlex.
- Ectopic expression of a human cysteine aspartate-specific protease genePlant biotechnology (Tokyo, Japan) · 2026Article
- A novel interaction between aquaporin 1 and caspase-3 in pulmonary arterial smooth muscle cells.American journal of physiology. Lung cellular and molecular physiology · 2024Article
- Integrative X-ray Structure and Molecular Modeling for the Rationalization of Procaspase-8 Inhibitor Potency and Selectivity.ACS chemical biology · 2020Article
- Resurrection of ancestral effector caspases identifies novel networks for evolution of substrate specificity.The Biochemical journal · 2019Review
- In silico and in vivo analyses of the mutated human tissue plasminogen activator (mtPA) and the antithetical effects of P19 silencing suppressor on its expression in two Nicotiana species.Scientific reports · 2018Article
- Modifications to a common phosphorylation network provide individualized control in caspases.The Journal of biological chemistry · 2018Article
- Allosteric Tuning of Caspase-7: A Fragment-Based Drug Discovery Approach.Angewandte Chemie (International ed. in English) · 2017Article
- The Apaf-1 apoptosome induces formation of caspase-9 homo- and heterodimers with distinct activities.Nature communications · 2016Article
- 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 · 2016Article
- Genetic characterization of two gain-of-function alleles of the effector caspase DrICE in Drosophila.Cell death and differentiation · 2016Article
- Modifying caspase-3 activity by altering allosteric networks.Biochemistry · 2014Article
- Fibrils colocalize caspase-3 with procaspase-3 to foster maturation.The Journal of biological chemistry · 2012Article
- Allosteric modulation of caspase 3 through mutagenesis.Bioscience reports · 2012Article
- A bifunctional allosteric site in the dimer interface of procaspase-3.Biophysical chemistry · 2011Article
- 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 · 2011Article
- A constitutively active and uninhibitable caspase-3 zymogen efficiently induces apoptosis.The Biochemical journal · 2009Article
- Folding and assembly kinetics of procaspase-3.Protein science : a publication of the Protein Society · 2009Article
- Procaspase-3 activation as an anti-cancer strategy: structure-activity relationship of procaspase-activating compound 1 (PAC-1) and its cellular co-localization with caspase-3.Journal of medicinal chemistry · 2009Article
- Targeting cell death in tumors by activating caspases.Current cancer drug targets · 2008Review
- Role of loop bundle hydrogen bonds in the maturation and activity of (Pro)caspase-3.Biochemistry · 2006Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
The interface of the procaspase-3 dimer plays a critical role in zymogen maturation. We show that replacement of valine 266, the residue at the center of the procaspase-3 dimer interface, with glutamate resulted in an increase in enzyme activity of approximately 60-fold, representing a pseudoactivation of the procaspase. In contrast, substitution of V266 with histidine abolished the activity of the procaspase-3 as well as that of the mature caspase. While the mutations do not affect the dimeric properties of the procaspase, we show that the V266E mutation may affect the formation of a loop bundle that is important for stabilizing the active site. In contrast, the V266H mutation affects the positioning of loop L3, the loop that forms the bulk of the substrate binding pocket. In some cases, the amino acids affected by the mutations are >20 A from the interface. Overall, the results demonstrate that the integrity of the dimer interface is important for maintaining the proper active site 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.