ArticlePloS one2013
Plant coilin: structural characteristics and RNA-binding properties.
Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
22 citing papers in PubMed, 38 citations in OpenAlex.
- Dynamic interaction of spliceosomal snRNPs with coilin explains Cajal body characteristics.The Journal of cell biology · 2025Article
- Cajal body formation is regulated by coilin SUMOylation.Journal of cell science · 2024Article
- Biomolecular condensates in plant RNA silencing: insights into formation, function, and stress responses.The Plant cell · 2024Review
- Coilin and Cajal bodies.Nucleus (Austin, Tex.) · 2023Review
- A GFP splicing reporter in a coilin mutant background reveals links between alternative splicing, siRNAs, and coilin function in Arabidopsis thaliana.G3 (Bethesda, Md.) · 2023Article
- Cajal bodies: Evolutionarily conserved nuclear biomolecular condensates with properties unique to plants.The Plant cell · 2023Review
- The Cajal body marker protein coilin is SUMOylated and possesses SUMO E3 ligase-like activity.Frontiers in RNA research · 2023Article
- Analysis of the Arabidopsis coilin mutant reveals a positive role of AtCOILIN in plant immunity.Plant physiology · 2022Article
- Nuclear dynamics: Formation of bodies and trafficking in plant nuclei.Frontiers in plant science · 2022Review
- Emerging Roles for Phase Separation in Plants.Developmental cell · 2020Review
- Article
- Functional Analysis of Coilin in Virus Resistance and Stress Tolerance of Potato Solanum tuberosum using CRISPR-Cas9 Editing.Doklady. Biochemistry and biophysics · 2019Article
- Cajal bodies and snRNPs - friends with benefits.RNA biology · 2017Review
- Cajal bodies and their role in plant stress and disease responses.RNA biology · 2017Review
- Specific genomic cues regulate Cajal body assembly.RNA biology · 2017Review
- Article
- AIP1 is a novel Agenet/Tudor domain protein from Arabidopsis that interacts with regulators of DNA replication, transcription and chromatin remodeling.BMC plant biology · 2015Article
- Intrinsically disordered proteins in the nucleus of human cells.Biochemistry and biophysics reports · 2015Article
- Coilin: The first 25 years.RNA biology · 2015Review
- Coilin association with Box C/D scaRNA suggests a direct role for the Cajal body marker protein in scaRNP biogenesis.Biology open · 2014Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Cajal bodies (CBs) are dynamic subnuclear compartments involved in the biogenesis of ribonucleoproteins. Coilin is a major structural scaffolding protein necessary for CB formation, composition and activity. The predicted secondary structure of Arabidopsis thaliana coilin (Atcoilin) suggests that the protein is composed of three main domains. Analysis of the physical properties of deletion mutants indicates that Atcoilin might consist of an N-terminal globular domain, a central highly disordered domain and a C-terminal domain containing a presumable Tudor-like structure adjacent to a disordered C terminus. Despite the low homology in amino acid sequences, a similar type of domain organization is likely shared by human and animal coilin proteins and coilin-like proteins of various plant species. Atcoilin is able to bind RNA effectively and in a non-specific manner. This activity is provided by three RNA-binding sites: two sets of basic amino acids in the N-terminal domain and one set in the central domain. Interaction with RNA induces the multimerization of the Atcoilin molecule, a consequence of the structural alterations in the N-terminal domain. The interaction with RNA and subsequent multimerization may facilitate coilin's function as a scaffolding protein. A model of the N-terminal domain is also proposed.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.