ArticleScientific reports2018
Crystal structure and mutation analysis revealed that DREP2 CIDE forms a filament-like structure with features differing from those of DREP4 CIDE.
Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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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
5 citing papers in PubMed, 6 citations in OpenAlex.
- Cinnamaldehyde affects lipid droplets metabolism after adipogenic differentiation of C2C12 cells.Molecular biology reports · 2023Article
- Molecular basis of apoptotic DNA fragmentation by DFF40.Cell death & disease · 2022Article
- Helical filament structure of the DREP3 CIDE domain reveals a unified mechanism of CIDE-domain assembly.Acta crystallographica. Section D, Structural biology · 2021Article
- The role of the DFF40/CAD endonuclease in genomic stability.Apoptosis : an international journal on programmed cell death · 2021Review
- Assembly of platforms for signal transduction in the new era: dimerization, helical filament assembly, and beyond.Experimental & molecular medicine · 2020Review
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Cell death-inducing DFF45-like effect (CIDE) domain-containing proteins, DFF40, DFF45, CIDE-A, CIDE-B, and FSP27, play important roles in apoptotic DNA fragmentation and lipid homeostasis. The function of DFF40/45 in apoptotic DNA fragmentation is mediated by CIDE domain filament formation. Although our recent structural study of DREP4 CIDE revealed the first filament-like structure of the CIDE domain and its functional importance, the filament structure of DREP2 CIDE is unclear because this structure was not helical in the asymmetric unit. In this study, we present the crystal structure and mutagenesis analysis of the DREP2 CIDE mutant, which confirmed that DREP2 CIDE also forms a filament-like structure with features differing from those of DREP4 CIDE.
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