ArticleInternational journal of molecular sciences2008
TFIP11, CCNL1 and EWSR1 Protein-protein Interactions, and Their Nuclear Localization.
Article in International journal of molecular sciences, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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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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Who cites it
7 citing papers in PubMed, 14 citations in OpenAlex.
- Proteomic profiling of cerebrospinal fluid in pediatric myelin oligodendrocyte glycoprotein antibody-associated disease.World journal of pediatrics : WJP · 2024Article
- hnRNPDL Phase Separation Is Regulated by Alternative Splicing and Disease-Causing Mutations Accelerate Its Aggregation.Cell reports · 2020Article
- DNA Methylation Associated With Diabetic Kidney Disease in Blood-Derived DNA.Frontiers in cell and developmental biology · 2020Article
- Identification and characterization of the BmCyclin L1-BmCDK11A/B complex in relation to cell cycle regulation.Cell cycle (Georgetown, Tex.) · 2017Article
- NTR1 is required for transcription elongation checkpoints at alternative exons in Arabidopsis.The EMBO journal · 2015Article
- Molecular detection and targeting of EWSR1 fusion transcripts in soft tissue tumors.Medical oncology (Northwood, London, England) · 2013Review
- Identification of a novel nuclear localization signal and speckle-targeting sequence of tuftelin-interacting protein 11, a splicing factor involved in spliceosome disassembly.Biochemical and biophysical research communications · 2009Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Previous studies using the yeast two-hybrid assay (Y2H) have identified cyclin L1 (CCNL1) and Ewing sarcoma breakpoint region 1 protein (EWSR1) as being interacting partners of tuftelin-interacting protein 11 (TFIP11). All three proteins are functionally related to the spliceosome and involved in pre-mRNA splicing activities. The spliceosome is a dynamic ribonucleoprotein complex responsible for pre-mRNA splicing of intronic regions, and is composed of five small nuclear RNAs (snRNAs) and μ140 proteins. TFIP11 appears to play a role in spliceosome disassembly allowing for the release of the bound lariat-intron. The roles of CCNL1 and EWSR1 in the spliceosome are poorly understood. Using fluorescently-tagged proteins and confocal microscopy we show that TFIP11, CCNL1 and EWSR1 frequently co-localize to speckled nuclear domains. These data would suggest that all three proteins participate in a common cellular activity related to RNA splicing events.
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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.