ArticleThe protein journal2016
Structural Characterizations of the Fas Receptor and the Fas-Associated Protein with Death Domain Interactions.
Article in The protein journal, 2016. 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.
- Exploring apoptotic pathways: implications for cancer, inflammation, and neurodegeneration.Molecular biology reports · 2026Review
- Discovery of Loureirin analogues with colorectal cancer suppressive activity via regulating cell cycle and Fas death receptor.BMC pharmacology & toxicology · 2024Article
- Computational Investigation of Selected Spike Protein Mutations in SARS-CoV-2: Delta, Omicron, and Some Circulating Subvariants.Pathogens (Basel, Switzerland) · 2023Article
- Comparative structural analyses of selected spike protein-RBD mutations in SARS-CoV-2 lineages.Immunologic research · 2022Article
- Case report: Effectiveness of sirolimus in aFrontiers in pediatrics · 2022Article
- Insight into the structures of Interleukin-18 systems.Computational biology and chemistry · 2020Article
- Structural and molecular analyses of functional epitopes and escape mutants in Japanese encephalitis virus envelope protein domain III.Immunologic research · 2020Article
- Structure and Function of an Inflammatory Cytokine, Interleukin-2, Analyzed Using the Bioinformatic Approach.The protein journal · 2019Article
Corrections and comments
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Authors and funding
1 author.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The Fas receptor is a representative death receptor, and the Fas-associated protein with death domain (FADD) is a crucial adapter protein needed to support the Fas receptor's activity. The Fas-FADD interactions constitute an important signaling pathway that ultimately induces apoptosis or programmed cell death in biological systems. The interactions responsible for this cell-death process are governed by the binding process of the Fas ligand to the Fas, followed by the caspase cascade activation. Using a computational approach, the present communication explores certain essential structural aspects of the Fas-FADD death domains and their interfacial interactions.
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Registered trials
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