ArticleMolecular biology of the cell2001
Association of human DEAD box protein DDX1 with a cleavage stimulation factor involved in 3'-end processing of pre-MRNA.
Article in Molecular biology of the cell, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 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.
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Who cites it
39 citing papers in PubMed, 84 citations in OpenAlex.
- Enzymology of the metazoan tRNA ligase complex: a lifetime in cycles.Cellular and molecular life sciences : CMLS · 2026Review
- Role of DEAD/DEAH-box helicases in immunity, infection and cancers.Cell communication and signaling : CCS · 2025Review
- Structural and biochemical characterization of the 3'-5' tRNA splicing ligases.The Journal of biological chemistry · 2025Article
- RNA biogenesis and RNA metabolism factors as R-loop suppressors: a hidden role in genome integrity.Genes & development · 2024Review
- Association between urinary arsenic concentration and genetic polymorphisms in Korean adults.Toxicological research · 2024Article
- Phosphorylation impacts GLE1 nuclear localization and association with DDX1.Advances in biological regulation · 2023Article
- DDX1 vesicles control calcium-dependent mitochondrial activity in mouse embryos.Nature communications · 2022Article
- DEAD-ly Affairs: The Roles of DEAD-Box Proteins on HIV-1 Viral RNA Metabolism.Frontiers in cell and developmental biology · 2022Review
- Identification ofFrontiers in cell and developmental biology · 2022Article
- The DEAD-box protein family of RNA helicases: sentinels for a myriad of cellular functions with emerging roles in tumorigenesis.International journal of clinical oncology · 2021Review
- Nucleocytoplasmic shuttling of Gle1 impacts DDX1 at transcription termination sites.Molecular biology of the cell · 2020Article
- RNA-binding protein DDX1 is responsible for fatty acid-mediated repression of insulin translation.Nucleic acids research · 2018Article
- Nuclear Factor I Represses the Notch Effector HEY1 in Glioblastoma.Neoplasia (New York, N.Y.) · 2018Article
- Intratumor heterogeneity ofOncotarget · 2018Article
- RNA Helicase DDX1 Converts RNA G-Quadruplex Structures into R-Loops to Promote IgH Class Switch Recombination.Molecular cell · 2018Article
- DEAD Box 1 Facilitates Removal of RNA and Homologous Recombination at DNA Double-Strand Breaks.Molecular and cellular biology · 2016Article
- Loss of the Drosophila melanogaster DEAD box protein Ddx1 leads to reduced size and aberrant gametogenesis.Developmental biology · 2015Article
- Ddx1 knockout results in transgenerational wild-type lethality in mice.Scientific reports · 2015Article
- Synergistic effects of ATP and RNA binding to human DEAD-box protein DDX1.Nucleic acids research · 2015Article
- Transcriptional response of chicken embryo cells to Newcastle disease virus (D58 strain) infection.Indian journal of virology : an official organ of Indian Virological Society · 2013Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
DEAD box proteins are putative RNA helicases that function in all aspects of RNA metabolism, including translation, ribosome biogenesis, and pre-mRNA splicing. Because many processes involving RNA metabolism are spatially organized within the cell, we examined the subcellular distribution of a human DEAD box protein, DDX1, to identify possible biological functions. Immunofluorescence labeling of DDX1 demonstrated that in addition to widespread punctate nucleoplasmic labeling, DDX1 is found in discrete nuclear foci approximately 0.5 microm in diameter. Costaining with anti-Sm and anti-promyelocytic leukemia (PML) antibodies indicates that DDX1 foci are frequently located next to Cajal (coiled) bodies and less frequently, to PML bodies. Most importantly, costaining with anti-CstF-64 antibody indicates that DDX1 foci colocalize with cleavage bodies. By microscopic fluorescence resonance energy transfer, we show that labeled DDX1 resides within a Förster distance of 10 nm of labeled CstF-64 protein in both the nucleoplasm and within cleavage bodies. Coimmunoprecipitation analysis indicates that a proportion of CstF-64 protein resides in the same complex as DDX1. These studies are the first to identify a DEAD box protein associating with factors involved in 3'-end cleavage and polyadenylation of pre-mRNAs.
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Registered trials
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