ArticleProceedings of the National Academy of Sciences of the United States of America2007
Functional redundancy of worm spliceosomal proteins U1A and U2B''.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 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
16 citing papers in PubMed, 28 citations in OpenAlex.
- The Arabidopsis U1 snRNP regulates mRNA 3'-end processing.Nature plants · 2024Article
- Phylogenetic analysis and stress response of the plant U2 small nuclear ribonucleoprotein B″ gene family.BMC genomics · 2022Article
- Phylogeny and conservation of plant U2A/U2A', a core splicing component in U2 spliceosomal complex.Planta · 2021Article
- Multiomic analysis of Schistosoma mansoni reveals unique expression profiles in cercarial heads and tails.Communications biology · 2021Article
- Effects of U1 Small Nuclear Ribonucleoprotein Inhibition on the Expression of Genes Involved in Alzheimer's Disease.ACS omega · 2020Article
- TDP-43 knockdown causes innate immune activation via protein kinase R in astrocytes.Neurobiology of disease · 2019Article
- Structural and functional modularity of the U2 snRNP in pre-mRNA splicing.Critical reviews in biochemistry and molecular biology · 2019Review
- The surveillance of pre-mRNA splicing is an early step inGenes & development · 2018Article
- Spliceosomal protein U1A is involved in alternative splicing and salt stress tolerance in Arabidopsis thaliana.Nucleic acids research · 2018Article
- Co-evolution of SNF spliceosomal proteins with their RNA targets in trans-splicing nematodes.Genetica · 2016Article
- TDP-1, the Caenorhabditis elegans ortholog of TDP-43, limits the accumulation of double-stranded RNA.The EMBO journal · 2014Article
- Climbing the vertebrate branch of U1A/U2B″ protein evolution.RNA (New York, N.Y.) · 2014Article
- Resurrection of an Urbilaterian U1A/U2B″/SNF protein.Journal of molecular biology · 2013Article
- Human U2B″ protein binding to snRNA stemloops.Biophysical chemistry · 2011Article
- Special Sm core complex functions in assembly of the U2 small nuclear ribonucleoprotein of Trypanosoma brucei.Eukaryotic cell · 2009Article
- Identification and analysis of internal promoters in Caenorhabditis elegans operons.Genome research · 2007Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
In Caenorhabditis elegans, the small nuclear ribonucleoprotein (snRNP)-associated proteins U1A and U2B'' are approximately 50% identical to each other, and neither bears signature characteristics of mammalian U1A or U2B'' or the single Drosophila homolog, SNF. We show here that the genes that encode these proteins (rnp-2 and rnp-3) are cotranscribed in an operon, and that ribonucleoprotein RNP-2 is U1 snRNP-associated (U1A) whereas RNP-3 is U2 snRNP-associated (U2B''). U2B'' interacts with U2 even in the absence of another U2 snRNP protein, U2A'. Like U1A and U2B'' from yeast, plants, and vertebrates, worm U1A and U2B'' are more similar to each other than they are to other U1A or U2B'' proteins, respectively. Even though U1A and U2B'' interact with different snRNPs, they are functionally redundant; knockout of both is required for a lethal phenotype. Interestingly, U1A associates with U2 RNA when U2B'' is deleted. Thus, the two members of this gene family normally function as components of different snRNPs but apparently remain capable of performing the function of the other. Redundancy results from the fact that one protein can substitute for the other, even though it normally does not.
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.