ArticleCell death and differentiation2019
Molecular basis of dimerization of initiator caspase was revealed by crystal structure of caspase-8 pro-domain.
Article in Cell death and differentiation, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 18 citations in OpenAlex.
- Unlocking therapeutic potential in traumatic brain injury: exploring microenvironmental targets, signaling pathways and translational hurdles.Inflammopharmacology · 2025Review
- Deciphering DED assembly mechanisms in FADD-procaspase-8-cFLIP complexes regulating apoptosis.Nature communications · 2024Article
- Artificial Infestation ofInternational journal of molecular sciences · 2023Article
- Helical filament structure of the DREP3 CIDE domain reveals a unified mechanism of CIDE-domain assembly.Acta crystallographica. Section D, Structural biology · 2021Article
- Caspase-8 mutations associated with head and neck cancer differentially retain functional properties related to TRAIL-induced apoptosis and cytokine induction.Cell death & disease · 2021Article
- Assembly of platforms for signal transduction in the new era: dimerization, helical filament assembly, and beyond.Experimental & molecular medicine · 2020Review
- Receptor Oligomerization and Its Relevance for Signaling by Receptors of the Tumor Necrosis Factor Receptor Superfamily.Frontiers in cell and developmental biology · 2020Review
- Caspase recruitment domains for protein interactions in cellular signaling (Review).International journal of molecular medicine · 2019Article
Corrections and comments
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Authors and funding
1 author at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The assembly of death-inducing signaling complex (DISC) for activation of initiator caspase is a key step for the receptor-mediated apoptosis signaling. Many death effector domain (DED)-containing proteins are involved in DISC assembly and controlling. One of the main DISC component, caspase-8, contains DED and DED-mediated dimerization and oligomerization in the DISC is critical for the activation of this initiator caspase. There have been intensive studies to understand DED-mediated dimerization and oligomerization for the DISC assembly but no clear answer has been provided and there are many controversial arguments. Here, we suggested novel dimerization process of tandem DED of caspase-8 with crystallographic study.
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Registered trials
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