ArticleProceedings of the National Academy of Sciences of the United States of America1999
Solution structure of Apaf-1 CARD and its interaction with caspase-9 CARD: a structural basis for specific adaptor/caspase interaction.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 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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Who cites it
50 citing papers in PubMed, 148 citations in OpenAlex.
- A histidine switch controls the pH-responsive self-assembly of a helical protein filament.bioRxiv : the preprint server for biology · 2026Article
- A histidine switch regulates pH-dependent filament formation by the caspase-9 CARD.bioRxiv : the preprint server for biology · 2025Article
- Caspases: structural and molecular mechanisms and functions in cell death, innate immunity, and disease.Cell discovery · 2025Review
- Computational Characterization of the Interaction of CARD Domains in the Apoptosome.Biochemistry · 2025Article
- Death domain fold proteins in immune signaling and transcriptional regulation.The FEBS journal · 2022Review
- Structure, Activation and Regulation of NLRP3 and AIM2 Inflammasomes.International journal of molecular sciences · 2021Review
- Structure, interactions and self-assembly of ASC-dependent inflammasomes.Archives of biochemistry and biophysics · 2019Review
- Caspase recruitment domains for protein interactions in cellular signaling (Review).International journal of molecular medicine · 2019Article
- Anemoside B4 exerts anti-cancer effect by inducing apoptosis and autophagy through inhibiton of PI3K/Akt/mTOR pathway in hepatocellular carcinoma.American journal of translational research · 2019Article
- Activation of innate antiviral immune response via double-stranded RNA-dependent RLR receptor-mediated necroptosis.Scientific reports · 2016Article
- Structural insights of homotypic interaction domains in the ligand-receptor signal transduction of tumor necrosis factor (TNF).BMB reports · 2016Review
- Rapid Eye Movement Sleep Deprivation Induces Neuronal Apoptosis by Noradrenaline Acting on Alpha1 Adrenoceptor and by Triggering Mitochondrial Intrinsic Pathway.Frontiers in neurology · 2016Article
- The tumor-modulatory effects of Caspase-2 and Pidd1 do not require the scaffold protein Raidd.Cell death and differentiation · 2015Article
- Inhibiting the inflammasome: one domain at a time.Immunological reviews · 2015Review
- Engineered solubility tag for solution NMR of proteins.Protein science : a publication of the Protein Society · 2013Article
- Pyrin- and CARD-only Proteins as Regulators of NLR Functions.Frontiers in immunology · 2013Review
- Novel disulfide bond-mediated dimerization of the CARD domain was revealed by the crystal structure of CARMA1 CARD.PloS one · 2013Article
- Structure and dynamics of the second CARD of human RIG-I provide mechanistic insights into regulation of RIG-I activation.Structure (London, England : 1993) · 2012Article
- Structural and functional analysis of the NLRP4 pyrin domain.Biochemistry · 2012Article
- Familial cortical myoclonus with a mutation in NOL3.Annals of neurology · 2012Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Direct recruitment and activation of caspase-9 by Apaf-1 through the homophilic CARD/CARD (Caspase Recruitment Domain) interaction is critical for the activation of caspases downstream of mitochondrial damage in apoptosis. Here we report the solution structure of the Apaf-1 CARD domain and its surface of interaction with caspase-9 CARD. Apaf-1 CARD consists of six tightly packed amphipathic alpha-helices and is topologically similar to the RAIDD CARD, with the exception of a kink observed in the middle of the N-terminal helix. By using chemical shift perturbation data, the homophilic interaction was mapped to the acidic surface of Apaf-1 CARD centered around helices 2 and 3. Interestingly, a significant portion of the chemically perturbed residues are hydrophobic, indicating that in addition to the electrostatic interactions predicted previously, hydrophobic interaction is also an important driving force underlying the CARD/CARD interaction. On the basis of the identified functional residues of Apaf-1 CARD and the surface charge complementarity, we propose a model of CARD/CARD interaction between Apaf-1 and caspase-9.
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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.