ArticleThe Biochemical journal2014
N-terminus oligomerization is conserved in intracellular calcium release channels.
Article in The Biochemical journal, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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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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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
6 citing papers in PubMed.
- Editorial: The role of calcium and calcium binding proteins in cell physiology and disease.Frontiers in physiology · 2023Article
- Defective ryanodine receptor N-terminus inter-subunit interaction is a common mechanism in neuromuscular and cardiac disorders.Frontiers in physiology · 2022Article
- Identification of an amino-terminus determinant critical for ryanodine receptor/Ca2+ release channel function.Cardiovascular research · 2021Article
- Genetic and Biochemical Approaches for In Vivo and In Vitro Assessment of Protein Oligomerization: The Ryanodine Receptor Case Study.Journal of visualized experiments : JoVE · 2016Article
- Simple bioconjugate chemistry serves great clinical advances: albumin as a versatile platform for diagnosis and precision therapy.Chemical Society reviews · 2016Review
- Structural insights into the human RyR2 N-terminal region involved in cardiac arrhythmias.Acta crystallographica. Section D, Biological crystallography · 2014Article
Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
Oligomerization of all three mammalian ryanodine receptor isoforms, a structural requirement for normal intracellular Ca2+ release channel function, is displayed by the discrete N-terminal domain which assembles into homo- and hetero-tetramers. This is demonstrated in yeast, mammalian cells and native tissue by complementary yeast two-hybrid, chemical cross-linking and co-immunoprecipitation assays. The IP3 (inositol 1,4,5-trisphosphate) receptor N-terminus (residues 1-667) similarly exhibits tetrameric association as indicated by chemical cross-linking and co-immunoprecipitation assays. The presence of either a 15-residue splice insertion or of the cognate ligand IP3 did not affect tetramerization of the IP3 receptor N-terminus. Thus N-terminus tetramerization appears to be an essential intrinsic property that is conserved in both the ryanodine receptor and IP3 receptor families of mammalian intracellular Ca2+ release channels.
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