ArticleBiochemistry2012
Structural and functional analysis of the NLRP4 pyrin domain.
Article in Biochemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 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
28 citing papers in PubMed, 50 citations in OpenAlex.
- ProbeST: a custom probe design pipeline for dual host-pathogen Spatial Transcriptomics.BMC genomics · 2026Article
- Role of inflammasomes in diabetes mellitus: mechanisms, complications, and therapeutic potential.Molecular biology reports · 2025Review
- Article
- The role of pyroptosis in cancer: key components and therapeutic potential.Cell communication and signaling : CCS · 2024Review
- The role of inflammasomes in human diseases and their potential as therapeutic targets.Signal transduction and targeted therapy · 2024Review
- The NLR gene family: from discovery to present day.Nature reviews. Immunology · 2023Review
- Role of Microgliosis and NLRP3 Inflammasome in Parkinson's Disease Pathogenesis and Therapy.Cellular and molecular neurobiology · 2022Review
- Directionality of PYD filament growth determined by the transition of NLRP3 nucleation seeds to ASC elongation.Science advances · 2022Article
- Role of NLRs in the Regulation of Type I Interferon Signaling, Host Defense and Tolerance to Inflammation.International journal of molecular sciences · 2021Review
- Structure, Activation and Regulation of NLRP3 and AIM2 Inflammasomes.International journal of molecular sciences · 2021Review
- Probing Intravascular Adhesion and Extravasation of Tumor Cells with Microfluidics.Methods in molecular biology (Clifton, N.J.) · 2021Article
- Epigenetic Mechanisms of Inflammasome Regulation.International journal of molecular sciences · 2020Review
- Structure, interactions and self-assembly of ASC-dependent inflammasomes.Archives of biochemistry and biophysics · 2019Review
- Assembly and regulation of ASC specks.Cellular and molecular life sciences : CMLS · 2017Review
- ASC Pyrin Domain Self-associates and Binds NLRP3 Protein Using Equivalent Binding Interfaces.The Journal of biological chemistry · 2016Article
- ATP binding by NLRP7 is required for inflammasome activation in response to bacterial lipopeptides.Molecular immunology · 2015Article
- Inhibiting the inflammasome: one domain at a time.Immunological reviews · 2015Review
- The hierarchical structural architecture of inflammasomes, supramolecular inflammatory machines.Current opinion in structural biology · 2015Review
- Activation and assembly of the inflammasomes through conserved protein domain families.Apoptosis : an international journal on programmed cell death · 2015Review
- An updated view on the structure and function of PYRIN domains.Apoptosis : an international journal on programmed cell death · 2015Article
Corrections and comments
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Authors and funding
12 authors at 5 institutions in 3 countries.
Funding
Abstract
NLRP4 is a member of the nucleotide-binding and leucine-rich repeat receptor (NLR) family of cytosolic receptors and a member of an inflammation signaling cascade. Here, we present the crystal structure of the NLRP4 pyrin domain (PYD) at 2.3 Å resolution. The NLRP4 PYD is a member of the death domain (DD) superfamily and adopts a DD fold consisting of six α-helices tightly packed around a hydrophobic core, with a highly charged surface that is typical of PYDs. Importantly, however, we identified several differences between the NLRP4 PYD crystal structure and other PYD structures that are significant enough to affect NLRP4 function and its interactions with binding partners. Notably, the length of helix α3 and the α2-α3 connecting loop in the NLRP4 PYD are unique among PYDs. The apoptosis-associated speck-like protein containing a CARD (ASC) is an adaptor protein whose interactions with a number of distinct PYDs are believed to be critical for activation of the inflammatory response. Here, we use co-immunoprecipitation, yeast two-hybrid, and nuclear magnetic resonance chemical shift perturbation analysis to demonstrate that, despite being important for activation of the inflammatory response and sharing several similarities with other known ASC-interacting PYDs (i.e., ASC2), NLRP4 does not interact with the adaptor protein ASC. Thus, we propose that the factors governing homotypic PYD interactions are more complex than the currently accepted model, which states that complementary charged surfaces are the main determinants of PYD-PYD interaction specificity.
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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.