ArticleIUCrJ2019
Structures of three ependymin-related proteins suggest their function as a hydrophobic molecule binder.
Article in IUCrJ, 2019. 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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Who cites it
5 citing papers in PubMed, 5 citations in OpenAlex.
- Biophysical Characterization of a Carotenoprotein from Marine SpongeMarine drugs · 2026Article
- Ependymin-related protein 1 levels are elevated in children with obesity and correlated with metabolic disorders.Pediatric discovery · 2024Article
- Molecular evolution of the ependymin-related gene epdl2 in African weakly electric fish.G3 (Bethesda, Md.) · 2023Article
- Structure and proteomic analysis of the crown-of-thorns starfish (Acanthaster sp.) radial nerve cord.Scientific reports · 2023Article
- New players of the adipose secretome: Therapeutic opportunities and challenges.Current opinion in pharmacology · 2022Review
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Authors and funding
10 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Ependymin was first discovered as a predominant protein in brain extracellular fluid in fish and was suggested to be involved in functions mostly related to learning and memory. Orthologous proteins to ependymin called ependymin-related proteins (EPDRs) have been found to exist in various tissues from sea urchins to humans, yet their functional role remains to be revealed. In this study, the structures of EPDR1 from frog, mouse and human were determined and analyzed. All of the EPDR1s fold into a dimer using a monomeric subunit that is mostly made up of two stacking antiparallel β-sheets with a curvature on one side, resulting in the formation of a deep hydrophobic pocket. All six of the cysteine residues in the monomeric subunit participate in the formation of three intramolecular disulfide bonds. Other interesting features of EPDR1 include two asparagine residues with glycosylation and a Ca
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