ArticleRNA (New York, N.Y.)2003
Association of polyadenylation cleavage factor I with U1 snRNP.
Article in RNA (New York, N.Y.), 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 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.
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.
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Who cites it
36 citing papers in PubMed, 65 citations in OpenAlex.
- The Arabidopsis U1 snRNP regulates mRNA 3'-end processing.Nature plants · 2024Article
- Comparative genomics and interactomics of polyadenylation factors for the prediction of new parasite targets: Entamoeba histolytica as a working model.Bioscience reports · 2023Article
- U1 snRNP proteins promote proximal alternative polyadenylation sites by directly interacting with 3' end processing core factors.Journal of molecular cell biology · 2022Article
- Deregulated expression and subcellular localization of CPSF6, a circRNA-binding protein, promote malignant development of esophageal squamous cell carcinoma.Chinese journal of cancer research = Chung-kuo yen cheng yen chiu · 2022Article
- U1 snRNP telescripting: molecular mechanisms and beyond.RNA biology · 2021Review
- Proximity to the Promoter and Terminator Regions Regulates the Transcription Enhancement Potential of an Intron.Frontiers in molecular biosciences · 2021Article
- A Complex of U1 snRNP with Cleavage and Polyadenylation Factors Controls Telescripting, Regulating mRNA Transcription in Human Cells.Molecular cell · 2019Article
- Suboptimal RNA-RNA interaction limits U1 snRNP inhibition of canonical mRNA 3' processing.RNA biology · 2019Article
- U1 snRNP Telescripting: Suppression of Premature Transcription Termination in Introns as a New Layer of Gene Regulation.Cold Spring Harbor perspectives in biology · 2019Review
- Alternative Polyadenylation: Methods, Findings, and Impacts.Genomics, proteomics & bioinformatics · 2017Review
- Silencing the cleavage factor CFIm25 as a new strategy to control Entamoeba histolytica parasite.Journal of microbiology (Seoul, Korea) · 2017Article
- Exploring the Impact of Cleavage and Polyadenylation Factors on Pre-mRNA Splicing Across Eukaryotes.G3 (Bethesda, Md.) · 2017Article
- Molecular association of herpes simplex virus type 1 glycoprotein E with membrane protein Us9.Archives of virology · 2016Article
- The reciprocal regulation between splicing and 3'-end processing.Wiley interdisciplinary reviews. RNA · 2016Review
- Mutant allele of rna14 in fission yeast affects pre-mRNA splicing.Journal of genetics · 2016Article
- Processing and transcriptome expansion at the mRNA 3' end in health and disease: finding the right end.Pflugers Archiv : European journal of physiology · 2016Review
- A critical role for alternative polyadenylation factor CPSF6 in targeting HIV-1 integration to transcriptionally active chromatin.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Multilayer regulatory mechanisms control cleavage factor I proteins in filamentous fungi.Nucleic acids research · 2015Article
- New links between mRNA polyadenylation and diverse nuclear pathways.Molecules and cells · 2014Review
- Delineating the structural blueprint of the pre-mRNA 3'-end processing machinery.Molecular and cellular biology · 2014Review
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Splicing and polyadenylation factors interact for the control of polyadenylation and the coupling of splicing and polyadenylation. We document an interaction between the U1 snRNP and mammalian polyadenylation cleavage factor I (CF Im), one of several polyadenylation factors needed for the cleavage of the pre-mRNA at the polyadenylation site. Sucrose density gradient centrifugation demonstrated that CF Im separated into two fractions, a light fraction which contained the known CF Im subunits (72, 68, 59, and 25 kD), and a heavy fraction, rich in snRNPs, which contained predominately the 68- and 25-kD CF Im subunits. Using specific antibodies we found that the heavy fraction contains U1 snRNP/CF Im coprecipitable complexes. These complexes were insensitive to RNase treatment, suggesting that the coprecipitation is not due to RNA tethering. In vitro binding experiments show that both the 68- and 25-kD subunits bind to and comigrate with U1 snRNP. In addition, the 25-kD CF Im subunit binds specifically to the 70K protein of U1 snRNP (U1 70K). This binding may account for the CF Im/U1 snRNP interaction. During these studies we found that mAb 2.73 (mAb 2.73), an established U1 70K antibody, efficiently precipitates the bulk of the CF Im from cellular extracts. Because mAb 2.73 has been used in a number of previous studies related to the U1 snRNP and the U1 70K protein, the precipitation of CF Im must be considered in evaluating past and future data based on the use of mAb 2.73.
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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.