ArticleNucleic acids research2012
A comprehensive manually curated protein-protein interaction database for the Death Domain superfamily.
Article in Nucleic acids research, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed.
- High Throughput Characterization of Eukaryotic 2A-Like Peptides Identifies Novel Leucine-Associated Reduction in Protein Abundance.bioRxiv : the preprint server for biology · 2026Article
- An engineered construct of cFLIP provides insight into DED1 structure and interactions.Structure (London, England : 1993) · 2022Article
- TIAMMAt: Leveraging Biodiversity to Revise Protein Domain Models, Evidence from Innate Immunity.Molecular biology and evolution · 2021Article
- mPPI: a database extension to visualize structural interactome in a one-to-many manner.Database : the journal of biological databases and curation · 2021Article
- Article
- Assembly of platforms for signal transduction in the new era: dimerization, helical filament assembly, and beyond.Experimental & molecular medicine · 2020Review
- Structure, interactions and self-assembly of ASC-dependent inflammasomes.Archives of biochemistry and biophysics · 2019Review
- Multiple Sclerosis patients carry an increased burden of exceedingly rare genetic variants in the inflammasome regulatory genes.Scientific reports · 2019Article
- Caspase recruitment domains for protein interactions in cellular signaling (Review).International journal of molecular medicine · 2019Article
- The inflammasome adapter ASC assembles into filaments with integral participation of its two Death Domains, PYD and CARD.The Journal of biological chemistry · 2019Article
- Protein interactions of the inflammasome adapter ASC by solution NMR.Methods in enzymology · 2019Article
- ASC Pyrin Domain Self-associates and Binds NLRP3 Protein Using Equivalent Binding Interfaces.The Journal of biological chemistry · 2016Article
- Structure of the absent in melanoma 2 (AIM2) pyrin domain provides insights into the mechanisms of AIM2 autoinhibition and inflammasome assembly.The Journal of biological chemistry · 2013Article
- Crystallization and preliminary X-ray crystallographic studies of the CARD domain of human CARMA1.Acta crystallographica. Section F, Structural biology and crystallization communications · 2013Article
- Novel disulfide bond-mediated dimerization of the CARD domain was revealed by the crystal structure of CARMA1 CARD.PloS one · 2013Article
- Cataloging the biomedical world of pain through semi-automated curation of molecular interactions.Database : the journal of biological databases and curation · 2013Article
- Article
- Structural features of caspase-activating complexes.International journal of molecular sciences · 2012Review
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Authors and funding
8 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The Death Domain (DD) superfamily, which is one of the largest classes of protein interaction modules, plays a pivotal role in apoptosis, inflammation, necrosis and immune cell signaling pathways. Because aberrant or inappropriate DD superfamily-mediated signaling events are associated with various human diseases, such as cancers, neurodegenerative diseases and immunological disorders, the studies in these fields are of great biological and clinical importance. To facilitate the understanding of the molecular mechanisms by which the DD superfamily is associated with biological and disease processes, we have developed the DD database (http://www.deathdomain.org), a manually curated database that aims to offer comprehensive information on protein-protein interactions (PPIs) of the DD superfamily. The DD database was created by manually curating 295 peer-reviewed studies that were published in the literature; the current version documents 175 PPI pairs among the 99 DD superfamily proteins. The DD database provides a detailed summary of the DD superfamily proteins and their PPI data. Users can find in-depth information that is specified in the literature on relevant analytical methods, experimental resources and domain structures. Our database provides a definitive and valuable tool that assists researchers in understanding the signaling network that is mediated by the DD superfamily.
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