ArticleCurrent proteomics2008
Insight into the Protein Components of the Box H/ACA RNP.
Article in Current proteomics, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 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
5 citing papers in PubMed, 6 citations in OpenAlex.
- Structure-function relationships of archaeal Cbf5 during in vivo RNA-guided pseudouridylation.RNA (New York, N.Y.) · 2016Article
- Purification and Functional Reconstitution of Box H/ACA Ribonucleoprotein Particles.Methods in molecular biology (Clifton, N.J.) · 2016Article
- Pseudouridine in mRNA: Incorporation, Detection, and Recoding.Methods in enzymology · 2015Article
- Inducing nonsense suppression by targeted pseudouridylation.Nature protocols · 2012Article
- Pseudouridine formation in archaeal RNAs: The case of Haloferax volcanii.RNA (New York, N.Y.) · 2011Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Among eukaryotic organisms a vast majority of Box H/ACA ribonucleoproteins (RNPs) are responsible for the post-transcriptional introduction of pseudouridine (Psi) into ribosomal RNAs (rRNA) and spliceosomal small nuclear RNAs (snRNA), thus influencing protein translation and pre-mRNA splicing, respectively. Additionally, a few distinct Box H/ACA RNPs are involved in the processing of rRNA, and the stabilization of vertebrate telomerase RNA. Thus, whether directly or indirectly, Box H/ACA RNPs impact major steps of gene expression, as well as play a role in maintaining genome integrity. Box H/ACA RNPs each consist of a unique Box H/ACA RNA and a set of four common core proteins. While the RNA component is responsible for dictating site-specificity, the four core proteins impact numerous aspects of RNP function including both stability and catalytic potential. Interestingly, mutations have been identified in the core proteins of the Box H/ACA RNP, resulting in a rare inherited bone marrow failure syndrome referred to as dyskeratosis congenita. This review discusses our current understanding of the roles of the protein components of the Box H/ACA RNP, and provides a framework to understand how mutations in the Box H/ACA RNP contribute to disease pathology.
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.