ReviewApoptosis : an international journal on programmed cell death2015
Activation and assembly of the inflammasomes through conserved protein domain families.
Review in Apoptosis : an international journal on programmed cell death, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
11 citing papers in PubMed.
- From gum inflammation to oral cancers: pyroptosis as the molecular torchbearer in periodontitis-driven carcinogenesis.Discover oncology · 2025Review
- Assessment of NLRP3 Inflammasome Activation and NLRP3-NEK7 Complex Assembly.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Homotypic CARD-CARD interaction is critical for the activation of NLRP1 inflammasome.Cell death & disease · 2021Article
- Activation and Immune Regulation Mechanisms of PYHIN Family During Microbial Infection.Frontiers in microbiology · 2021Review
- An Update on CARD Only Proteins (COPs) and PYD Only Proteins (POPs) as Inflammasome Regulators.International journal of molecular sciences · 2020Review
- Structure, interactions and self-assembly of ASC-dependent inflammasomes.Archives of biochemistry and biophysics · 2019Review
- Protein interactions of the inflammasome adapter ASC by solution NMR.Methods in enzymology · 2019Article
- Functional and structural characterization of zebrafish ASC.The FEBS journal · 2018Article
- Crystal structure of human NLRP12 PYD domain and implication in homotypic interaction.PloS one · 2018Article
- Innate Immune Recognition: Implications for the Interaction ofFrontiers in cellular and infection microbiology · 2017Review
- Inhibiting the inflammasome: one domain at a time.Immunological reviews · 2015Review
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.
Funding
Abstract
Inflammasomes are oligomeric protein complexes assembled through interactions among the death domain superfamily members, in particular the CARD and PYD domains. Recent progress has shed lights on how the ASC PYD can polymerize to form filaments using multiple domain:domain interfaces, and how the caspase4 CARD can recognize LPS to activate the non-classical inflammasome pathway. Comprehensive understanding of the molecular mechanisms of inflammasome activation and assembly require more extensive structural and biophysical dissection of the inflammasome components and complexes, in particular additional CARD or PYD filaments. Because of the variations in death domain structures and complexes observed so far, future work will undoubtedly shed lights on the mechanisms of inflammasome assembly as well as more surprises on the versatile structure and function of the death domain superfamily.
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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.